Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
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A9JTS5 | STPAP_XENTR | MEAEESSSSVVPLPQDVQSVVRGGFRCLLCGVNIPNRPSLTDHLSGRRHVRLHEERDKRNQQQERSVYVSNFPRETSEEQLRDVFQKISPVRNIVMDKDRGLYAIVEFESKDGMCAALEEPQIKLSGKRLRVKPREKKEFQRKKGGSPRTLQPPDPEALSKELLNCADVEQQIKKLVSLCSPSHHESHLRELLLSLLQETFTEFFPGCQLLPFGSSVNGFEISGCDLDLYLDLGDDEAENVEGKAEKEIQNREESSTDMEVSMEDPETERKEEEMEIGNSKNDEDEDVTPGLSLKGLSSEEILEVVGKVLRHCVPGVHGVQSVPTARRPVIHFQHKTSGLRGDVTLNNRLALRNSSFLRLCSDLDARVPQLVYTVRYWARVNQLAGNPFGGGPLLNNYALTLLVFFFLQTRNPPVLPTLVHLREETANEVPQVIDGWDCSFPSDPAQVKESGNQQSLSSLLSEFFSFYASLDLHLLILCPCNGLTIPLPFSSPPPAWSEGFRLGPLNIQDPFELSHNVCGNVSSRAARRFISHCAAAARICRTPNYNLHSTSHPWGITPILLPPPTERECVGRGGTEISIPLGGVSPEKTYAAVSKVFVDVLLCTLEEGREDSCQEGKALELSTKHAKAQCKVEKNEVGGELGEQEVPCKAEQNNTKEASKQKSIFKTEEGMTESARRKREMTEPCMSDMTNGKKRRLEFTRGIWDHHLATSAMEEEMCGEAHKDSKTKIDYSNNGTAQWELLVWHRVWEGRRKERRRKQKGEADGVELEIAVSQALALEKEDKCDGPLMKLILTAQLTVKESLQLYLTPKFDPQGLSSTFFHFLESYLPRMVAQIQGCGDPV | 2.7.7.19; 2.7.7.52 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9H6E5}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9NVV4}; Note=Binds 1 divalent cation per subunit. {ECO:0000250|UniProtKB:Q9H6E5}; | co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway [GO:0180010]; mRNA polyadenylation [GO:0006378]; snRNA processing [GO:0016180] | mitochondrion [GO:0005739]; mRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; nuclear speck [GO:0016607]; nucleolus [GO:0005730] | ATP binding [GO:0005524]; enzyme-substrate adaptor activity [GO:0140767]; metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730]; poly(A) RNA polymerase activity [GO:1990817]; RNA binding [GO:0003723]; RNA uridylyltransferase activity [GO:0050265] | PF03828;PF00076; | 1.10.1410.10;3.30.70.330;3.30.460.10; | DNA polymerase type-B-like family | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H6E5}. Nucleus speckle {ECO:0000250|UniProtKB:Q9H6E5}. | CATALYTIC ACTIVITY: Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395, ChEBI:CHEBI:173116; EC=2.7.7.52; Evidence={ECO:0000250|UniProtKB:Q9H6E5}; CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000250|UniProtKB:Q9H6E5}; | null | null | null | null | FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. {ECO:0000250|UniProtKB:Q9H6E5}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A9LLI7 | RP6L2_ARATH | MSDGNMDVDESPVSWKVKSLEKLIDGSSFSSTLSRLSSSSRLIPTSRDFHFYYNFDEFKRPIDEITGTSQSTLATIGDSEQVWGKSMKFPGDVDDVYAEDWLCNVNDELIERFDVSVDEFQRIRKKEKEIGRSVVADDGDDGFQMVYGKKKKPVGNVVTGSAAVNGGGSVIDVKMAERDKNSSGKAKVPFHVPTIKKPQEEYNILVNNANLPFEHVWLERSEDDLRAMHPLEKFSVLDFVDKDVNEMEPVKPLPLEQTPFKFVQEVKDLKELVAKLRSVEEFAVDLEHNQYRSFQGLTCLMQISTRTEDYIVDTFKLRIHIGPYLREIFKDPKKKKVMHGADRDIIWLQRDFGIYVCNLFDTGQASRVLNLERNSLEFLLQHFCGVTANKEYQNADWRIRPLPEEMTRYAREDTHYLLYIYDLIKLELQRMAKDDAHTDSPLLEVYKRSYDVCTQLYEKELLTENSYLHVYGLQAAGFNAAQLAIVAGLCEWRDFIARAEDESTGYVLPNKVLLEIAKEMPDSVGKLRRMLKSKHPYIERNVDSVVSVIRQSMQHYAAFESAALSLKDVSPGNVMDKNIEPISEKKDLHTGDVASPSLKENSSQLESTRDLIMGAANTNEGRGLGSGLFGSAKVSAAVRISKKPSSGLGALLGNAASKKKSRTDEKVKEDVKLEQIRSSVNLSFHSFTEKVPDSKSTSETSPKVYGKPEEMSSTMPASVSKEDGVKELKDDSEEASEIVGTSGRVSESKVSSSEMGDIILLENGDEKKVDAEDEPMSLSELSTNFQKCFKSMNKSKKAQKQTEFLNIEPFDYEAARKEVKFGEGHKGRQGKREAAAGQKKGSTQEQSEFGQGKRRQAFPASGNRSMSFKN | null | null | exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000467]; gene silencing by RNA-directed DNA methylation [GO:0080188]; histone mRNA catabolic process [GO:0071044]; nuclear polyadenylation-dependent antisense transcript catabolic process [GO:0071040]; nuclear polyadenylation-dependent CUT catabolic process [GO:0071039]; nuclear polyadenylation-dependent rRNA catabolic process [GO:0071035]; nuclear polyadenylation-dependent snoRNA catabolic process [GO:0071036]; nuclear polyadenylation-dependent snRNA catabolic process [GO:0071037]; nuclear polyadenylation-dependent tRNA catabolic process [GO:0071038]; polyadenylation-dependent RNA catabolic process [GO:0043633]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; rRNA processing [GO:0006364] | cytoplasm [GO:0005737]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]; nucleus [GO:0005634] | 3'-5'-RNA exonuclease activity [GO:0000175]; nucleotide binding [GO:0000166]; single-stranded RNA binding [GO:0003727] | PF01612;PF00570; | 1.10.150.80;3.30.420.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18285452}. Nucleus, nucleolus {ECO:0000269|PubMed:18285452}. Cytoplasm {ECO:0000269|PubMed:18285452}. Note=Localizes predominantly in the nucleus. {ECO:0000269|PubMed:18285452}. | null | null | null | null | null | FUNCTION: Acts as an important epigenetic regulator through multiple silencing mechanisms (PubMed:23555312, PubMed:25211139). Involved in association with RRP6L1 in the silencing of the solo LTR locus. Controls levels of non-coding RNAs (ncRNAs) from the solo LTR locus. Seems to function independently of the RNA-mediated gene silencing (RdDM) pathway (PubMed:23555312). Functions redundantly with RRP6L1 in the regulation of FLC locus. Participates in the maintenance of trimethylated 'Lys-27' (H3K27me3) at FLC locus via the regulation of antisense long non-coding RNAs (lncRNAs) and the regulation of diverse antisense RNAs derived from the FLC locus. Seems not involved in the exosomal RNA degradation (PubMed:25211139). May be involved in poly(A)-mediated RNA degradation (PubMed:18285452). {ECO:0000269|PubMed:18285452, ECO:0000269|PubMed:23555312, ECO:0000269|PubMed:25211139}. | Arabidopsis thaliana (Mouse-ear cress) |
A9LNK9 | CPSF_ARATH | MEDADGLSFDFEGGLDSGPVQNTASVPVAPPENSSSAAVNVAPTYDHSSATVAGAGRGRSFRQTVCRHWLRGLCMKGDACGFLHQFDKARMPICRFFRLYGECREQDCVYKHTNEDIKECNMYKLGFCPNGPDCRYRHAKLPGPPPPVEEVLQKIQQLTTYNYGTNRLYQARNVAPQLQDRPQGQVPMQGQPQESGNLQQQQQQQPQQSQHQVSQTLIPNPADQTNRTSHPLPQGVNRYFVVKSNNRENFELSVQQGVWATQRSNEAKLNEAFDSVENVILIFSVNRTRHFQGCAKMTSRIGGYIGGGNWKHEHGTAQYGRNFSVKWLKLCELSFHKTRNLRNPYNENLPVKISRDCQELEPSVGEQLASLLYLEPDSELMAISIAAEAKREEEKAKGVNPESRAENPDIVPFEDNEEEEEEEDESEEEEESMAGGPQGRGRGRGIMWPPQMPLGRGIRPMPGMGGFPLGVMGPGDAFPYGPGGYNGMPDPFGMGPRPFGPYGPRFGGDFRGPVPGMMFPGRPPQQFPHGGYGMMGGGRGPHMGGMGNAPRGGRPMYYPPATSSARPGPSNRKTPERSDERGVSGDQQNQDASHDMEQFEVGNSLRNEESESEDEDEAPRRSRHGEGKKRR | 3.1.21.- | null | mRNA 3'-end processing [GO:0031124]; mRNA polyadenylation [GO:0006378]; mRNA splicing, via spliceosome [GO:0000398]; plant-type hypersensitive response [GO:0009626]; positive regulation of plant-type hypersensitive response [GO:0034052]; positive regulation of programmed cell death [GO:0043068]; regulation of mRNA splicing, via spliceosome [GO:0048024]; regulation of salicylic acid mediated signaling pathway [GO:2000031]; response to oxidative stress [GO:0006979]; RNA processing [GO:0006396] | cytoplasm [GO:0005737]; mRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | calmodulin binding [GO:0005516]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521] | PF04146; | 3.10.590.10;4.10.1000.10; | CPSF4/YTH1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16500995, ECO:0000269|PubMed:19573236}. Cytoplasm {ECO:0000269|PubMed:19573236}. Note=Localized in the cytoplasm when not in complex or when associated with CPSF100, but move to the nucleus when associated with the cleavage and polyadenylation specificity factor (CPSF) subunits CPSF160 or CPSF73s. {ECO:0000269|PubMed:19573236}. | null | null | null | null | null | FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation. May interact with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition (By similarity). Mediates poly(A) site selection (PubMed:23136375). Binds RNA in a calcium-dependent manner (PubMed:16500995, PubMed:17576667, PubMed:20214900). Exhibits endonuclease activity with an ability to nick and degrade linear as well as circular single-stranded RNA that leaves RNA 3' ends with hydroxyl groups, thus mediating processing of the pre-mRNA as a prelude to the polyadenylation (PubMed:17576667). Involved in the post-transcriptional control, probably via poly(A) addition, of the responses of plants to stress, especially genes mediating tolerance to oxidative stress (PubMed:18545667). Plays a role in the regulation of salicylic acid (SA) production via the control of messenger RNA 3' end processing, thus being a key component of programmed cell death and plant immune responses required for resistance to virulent Pseudomonas syringae pv tomato DC3000 (Pst) (PubMed:24706550). {ECO:0000250|UniProtKB:O95639, ECO:0000269|PubMed:16500995, ECO:0000269|PubMed:17576667, ECO:0000269|PubMed:18545667, ECO:0000269|PubMed:20214900, ECO:0000269|PubMed:23136375, ECO:0000269|PubMed:24706550}. | Arabidopsis thaliana (Mouse-ear cress) |
A9NJG2 | 13S_FAGTA | MSTKLILSFSLCLMVLSCSAQAAQLWPWRKGQDSRPHHGHQQFQQQCDIQRLTASEPSRRVRSEAGVTEIWDHNTPEFRCTGFVAVRYVIQPGGLLLPSYSNAPYITFVEQGRGVQGVVIPGCPETFQSDSEYPQSQRGQHSRESESQESSRGDQHQKIFRVREGDVIPSPAGVVQWTHNDGDQDLISVTLLDANSFHNQLDENVRSFFLAGQSQQGREERRSQQQTREEGGDRQSRESDDVEALIGANILSGFQDEILHELFRDVDRETISKLRGENDQRGFIVQAQDLKLRVPEDSEEGYERQRGDRKRDERGSGRSNGLEQAFCNLKFRQNVNRPSHADVFNPRAGRINTVNSNNLPILEFLQLSAQHVVLYKNAIIGPRWNLNAHSALYVTRGEGRVQVVGDEGKSVFDDNVQRGQILVVPQGFAVVVKAGRQGLEWVELKNNDNAITSPIAGRTSVLRAIPVEVLANSYDISTEEAYKLKNGRQEVEVFRPFQSRYEKEEEKERERFSIV | null | null | null | null | IgE binding [GO:0019863]; IgG binding [GO:0019864]; nutrient reservoir activity [GO:0045735] | PF00190; | 2.60.120.10; | 11S seed storage protein (globulins) family | PTM: Proteolytically processed from a single precursor to produce an acidic and a basic chain that are linked by a disulfide bond. {ECO:0000250|UniProtKB:A0A1L6K371}. | null | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Highly thermostable. Loss of stability only after incubation for 1 hour at 100 degrees Celsius. {ECO:0000269|PubMed:15277744}; | FUNCTION: Seed storage protein. {ECO:0000305}. | Fagopyrum tataricum (Tartarian buckwheat) (Polygonum tataricum) |
A9PCL4 | PRX2_POPTR | MAPIAVGDVLPDGKLAYFDEQDQLQEVSVHSLVAGKKVILFGVPGAFTPTCSLKHVPGFIEKAGELKSKGVTEILCISVNDPFVMKAWAKSYPENKHVKFLADGSATYTHALGLELNLQEKGLGTRSRRFALLVDDLKVKAANIEGGGEFTVSSADDILKDL | 1.11.1.25 | null | cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; hydrogen peroxide catabolic process [GO:0042744] | cytoplasm [GO:0005737] | thioredoxin peroxidase activity [GO:0008379] | PF08534; | 3.40.30.10; | Peroxiredoxin family, Prx5 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=[glutaredoxin]-dithiol + a hydroperoxide = [glutaredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62624, Rhea:RHEA-COMP:10729, Rhea:RHEA-COMP:10730, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.25; Evidence={ECO:0000269|PubMed:11706208, ECO:0000269|PubMed:15032877}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 uM for phosphatidylcholine hydroperoxide {ECO:0000269|PubMed:15032877}; | null | null | null | FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. Plays a role in cell protection against oxidative stress by detoxifying peroxides. {ECO:0000269|PubMed:15032877, ECO:0000269|PubMed:18230180}. | Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa) |
A9Q751 | PCDP1_MOUSE | MEVVKSPMQELQQAKEPFDTMSPLLLKSLVEEPKKRTEVPNHLLESRVYAKLLNNKVIQARPGIVHFGGYEIESKHQQILNIANISDEDTHLHILPPQTKYFQINFEKKEHRLIPGLSLTVTITFSPDEWRYYYDCIRIHCKGDDTLLVPIHAYPVLNNLDFPTFINLSDVFLGESKSYVIPLQCSCPVDFEFHITLLRSHQAFTIEPKSGIIPANGKAKVTVKFTPIQYGMAQIKIQLWISQFNSQPYECVFTGTCYPNMALPLEEFKRLNTRSKKVNVPLEKTTYVQFYPAPAKAKPQKLKEIDYQDLRFPADLSNPFAVATVLNQEPGKLKIKELKQVLDQGDEISKTRQMKEAIFEQKVRQDILTEIENHLKWQVHLGKEHTTYRFKRELTEEWKKARAKYKQNRGDPVEGEELQRLQTEQSQKRIVRDLKGKRQEFHPNFDPLVNNVWLTRHRAQRRFQQAARKIMLERRLLSMLGAIRGMDKESILRKIIQVNGKLIQGENPSRGRRAHLKQEDNIWRYSLESEEVLHFAFPTDSESYNELALDGLGLVPIKSPEIQIKHSYPYFTLKVPQLYKIKGYHPFSVNKSSTNYRLQKLARPLKHGAEDEVTTIITIPKKDTTPLSAKPSILSMKPPEGLAMSVEYDPLYIFNPSPGLFAVKHPLTYAETLIDYHLCSHPKYKYTQESHMGSSIPLTQRQFLHHTDIIPGIMNWKKFQPLVFSSMSDPSMVEATQRSDWYSSVMLPIDVPAPLEDLPEEDRLETTERDLCDQGIEVMLTPEMVQVEFPMLIHRDSKKEKDFKDSTQLPEKVGERVQEEMKNLRSKALNTYLILD | null | null | cerebrospinal fluid circulation [GO:0090660]; establishment of localization in cell [GO:0051649]; motile cilium assembly [GO:0044458]; mucociliary clearance [GO:0120197]; sperm flagellum assembly [GO:0120316] | 9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; manchette [GO:0002177]; sperm flagellum [GO:0036126] | calmodulin binding [GO:0005516] | null | 2.60.40.10; | PCDP1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:18039845}. Cytoplasm {ECO:0000269|PubMed:18039845, ECO:0000269|PubMed:29690537}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:29690537}. Note=Localizes to the manchette in elongating spermatids in a SPAG17-dependent manner. {ECO:0000269|PubMed:29690537}. | null | null | null | null | null | FUNCTION: May play a role in cilium morphogenesis. {ECO:0000305|PubMed:18039845}. | Mus musculus (Mouse) |
A9QA56 | ABC3H_FELCA | MNPLQEVIFCRQFGNQHRVPKPYYRRKTYLCYQLKLPEGTLIHKDCLRNKKKRHAEMCFIDKIKALTRDTSQRFEIICYITWSPCPFCAEELVAFVKDNPHLSLRIFASRLYVHWRWKYQQGLRHLHASGIPVAVMSLPEFEDCWRNFVDHQDRSFQPWPNLDQYSKSIKRRLGKILTPLNDLRNDFRNLKLE | 3.5.4.38 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9GZX7}; | cytidine to uridine editing [GO:0016554]; defense response to virus [GO:0051607]; DNA cytosine deamination [GO:0070383]; DNA demethylation [GO:0080111]; negative regulation of single stranded viral RNA replication via double stranded DNA intermediate [GO:0045869] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; P-body [GO:0000932] | cytidine deaminase activity [GO:0004126]; deoxycytidine deaminase activity [GO:0047844]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270] | PF18772; | 3.40.140.10; | Cytidine and deoxycytidylate deaminase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q19Q52}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'-deoxyuridine in single-stranded DNA + NH4(+); Xref=Rhea:RHEA:50948, Rhea:RHEA-COMP:12846, Rhea:RHEA-COMP:12847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:85452, ChEBI:CHEBI:133902; EC=3.5.4.38; Evidence={ECO:0000269|PubMed:26491161}; | null | null | null | null | FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA (By similarity). Exhibits single-stranded DNA deaminase activity (in vitro) (PubMed:26491161). Incorporates into the released virions of the virion infectivity factor (vif)-deficient feline immunodeficiency virus (FIV) and suppresses FIV infectivity, probably in a deaminase-dependent manner (in vitro) (PubMed:26491161). Induces G-to-A hypermutations in vif-deficient FIV (in vitro) (PubMed:26491161). The APOBEC3H/APOBEC3Z3 haplotype 5 exhibits antiviral activity against vif-proficient FIV, strains Petaluma, C36 and Shizuoka (in vitro) (PubMed:26491161). Does not exhibit inhibitory activity against feline leukemia virus (FeLV), feline endogenous retrovirus (RD-114 virus) or a long interspersed nuclear element-1 (LINE-1) retrotransposon (in vitro) (PubMed:26491161). {ECO:0000250|UniProtKB:P60705, ECO:0000269|PubMed:26491161}. | Felis catus (Cat) (Felis silvestris catus) |
A9QM73 | SMG7_ARATH | MMTLQMDKTTASSSWERAKSIYDEIAELANKRQKAGNPPDPNLLQLLREKYEAIILESHTFSEQHNIEIPLWQLHYKRIEYFRLHINRVLASSTSTAAQNVKGPSKAEQIAQLKLQFRTFLSEATGFYHDMILKIRSKYGLPLGSFSEDQQSQNLSDKDGKELAEVQKALKSCHRCLIYLGDLARYKGMYAEGDSRSRQYASASSYYLQAASLWPASGNPHHQLAIVASYSRDEFVTTYRYFRSLAVEYPFPTARDNLIVAFDKNRQSYEKLFVPSKDSSKRLTGKGRGKGADISLKDATLVAGPEKDKVTIANEMLKAFSIRFVHLNGILFTRTSLETFFDVLASTSSSLREVISLGSAKELTLGIDTSDSALFIVRVVTMLIFSVHNSKKETEGQSYAEIVQRVEPARNSLTASFELLGLVIEKCVQLGDPSSSYFLPGVLVFVEWLACCPDIALGSDPDDRQTAVRNSFWNQFVVFFNQVLSLGPTFIDDVEDETCFSNMSLYDERETENRLALWEDYELRGFLPLLPAQTILNFSRKHSFGTEGPKEKKARIKRIFAAGKALTSVIKVDQNHVYFDSKKKKFLVGVKPADDFLDSHSSPPKACNALQDNQVMIDHNSPIMQLDQQIYMGEEDDDDEVIVFKPLVTEKRKEASDQIYVPSGGFRKSDQVTTMGDFKALSGSDVAFHENQILQARGNASIQVPASVGANLLGPLQPSTQSQAMHMQQVQTQVQVPASVGANLLGLLLTSTQSQAMHMQQVQTQAVNPQPAQSLAASRLQPIQSQVAQPLPSRVVHFQQTQAQVSHVSPAHSQSTSFGGGSKWSPEEAASLASSLSGFAQLGNGHVMRNEMQGNHGVSYYPAHSLPVHQSYNGNGMGGMPYSQSRTPEAVFPPKIDPVLSSGVVADGLGVQSSLAKKNPISRAFRHLGPPPGFNSVPAKLQKEPAPGSELSGNNHLPVDDYSWLDGYQAQSSRGVGLNSSLNYATSGKPEHLGSTGNGLNGPANFPFPGKQVPTSQVQADFPYFQNPQKDNFVDKNHQSTQLPEQYQGQSTWSSRHFV | null | null | defense response [GO:0006952]; meiotic cell cycle [GO:0051321]; meiotic spindle assembly [GO:0090306]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; programmed cell death [GO:0012501]; regulation of defense response [GO:0031347] | nucleus [GO:0005634]; P-body [GO:0000932]; telomerase holoenzyme complex [GO:0005697] | telomerase RNA binding [GO:0070034]; telomeric DNA binding [GO:0042162] | PF10374;PF10373; | 1.25.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:22974464, ECO:0000269|PubMed:29073135}. | null | null | null | null | null | FUNCTION: Plays multiple roles in growth and development. Involved in nonsense-mediated mRNA decay (NMD). May provide a link to the mRNA degradation machinery to initiate NMD and serve as an adapter for UPF proteins function. Required for meiotic progression through anaphase II of pollen mother cells. May counteract cyclin-dependent kinase (CDK) activity at the end of meiosis. May play a role in plant defense through its involvement in NMD. Together with EXA1, helps to restrict cell death induction during pathogen infection in a salicylic acid- (SA) and reactive oxygen species- (ROS) independent manner (PubMed:29073135). {ECO:0000269|PubMed:18544632, ECO:0000269|PubMed:21119056, ECO:0000269|PubMed:22379136, ECO:0000269|PubMed:22974464, ECO:0000269|PubMed:29073135}. | Arabidopsis thaliana (Mouse-ear cress) |
A9QM74 | IMA8_HUMAN | MPTLDAPEERRRKFKYRGKDVSLRRQQRMAVSLELRKAKKDEQTLKRRNITSFCPDTPSEKTAKGVAVSLTLGEIIKGVNSSDPVLCFQATQTARKMLSQEKNPPLKLVIEAGLIPRMVEFLKSSLYPCLQFEAAWALTNIASGTSEQTRAVVEGGAIQPLIELLSSSNVAVCEQAVWALGNIAGDGPEFRDNVITSNAIPHLLALISPTLPITFLRNITWTLSNLCRNKNPYPCDTAVKQILPALLHLLQHQDSEVLSDACWALSYLTDGSNKRIGQVVNTGVLPRLVVLMTSSELNVLTPSLRTVGNIVTGTDEQTQMAIDAGMLNVLPQLLQHNKPSIQKEAAWALSNVAAGPCHHIQQLLAYDVLPPLVALLKNGEFKVQKEAVWMVANFATGATMDQLIQLVHSGVLEPLVNLLTAPDVKIVLIILDVISCILQAAEKRSEKENLCLLIEELGGIDRIEALQLHENRQIGQSALNIIEKHFGEEEDESQTLLSQVIDQDYEFIDYECLAKK | null | null | blastocyst development [GO:0001824]; epigenetic regulation of gene expression [GO:0040029]; negative regulation of gene expression [GO:0010629]; NLS-bearing protein import into nucleus [GO:0006607]; positive regulation of gene expression [GO:0010628]; protein import into nucleus [GO:0006606] | cytosol [GO:0005829]; female germ cell nucleus [GO:0001674]; NLS-dependent protein nuclear import complex [GO:0042564]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819] | nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139] | PF00514;PF16186;PF01749; | 1.20.5.690;1.25.10.10; | Importin alpha family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20701745, ECO:0000269|PubMed:36647821}. | null | null | null | null | null | FUNCTION: Functions in nuclear protein import. {ECO:0000269|PubMed:36647821}. | Homo sapiens (Human) |
A9QT41 | NEMO_PIG | MSRTPWKSQPCEMVQPSGGPAGDQDVLGEESSLGKPTMLHLPSEQGAPETFQRCLEENQELRDAIRQSNQMLRERCEELQRFQGSQREEKEFLMQKFCEARRLVERLSLEKLELRRQREQALQEVELLKTCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQALESRVRATSEQVRQLENEREALQQQHSVQVDQLRLQSQSMEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVVSSERNRGLQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREQLAERKELLQEQLEQLQREYSRLKTSCQESARIEDMRKRHVEVSQPTLPPAPAHHSFHPALPSQRRSPPEEPPNFCCPKCQYQAPDMDTLQIHVMECIE | null | null | DNA damage response [GO:0006974]; phosphorylation [GO:0016310]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of T cell receptor signaling pathway [GO:0050862] | cytoplasm [GO:0005737]; IkappaB kinase complex [GO:0008385]; nucleus [GO:0005634] | K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; kinase activity [GO:0016301]; linear polyubiquitin binding [GO:1990450]; metal ion binding [GO:0046872] | PF16516;PF11577;PF18414; | 1.20.5.390;1.20.5.990; | null | PTM: Phosphorylation at Ser-68 attenuates aminoterminal homodimerization. {ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: Polyubiquitinated on Lys-285 via 'Lys-63'-linked ubiquitin; the ubiquitination is mediated downstream of NOD2 and RIPK2 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway. Polyubiquitinated on Lys-285 and Lys-399 through 'Lys-63'-linked ubiquitin; the ubiquitination is mediated by BCL10, MALT1 and TRAF6 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway. Monoubiquitinated on Lys-277 and Lys-309; promotes nuclear export. Polyubiquitinated through 'Lys-27' by TRIM23; involved in antiviral innate and inflammatory responses. Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-264, Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation. Deubiquitinated by USP10 in a TANK-dependent and -independent manner, leading to the negative regulation of NF-kappa-B signaling upon DNA damage. Ubiquitinated at Lys-326 by MARCHF2 following bacterial and viral infection which leads to its degradation. {ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: Sumoylated on Lys-277 and Lys-309 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues. {ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: Neddylated by TRIM40, resulting in stabilization of NFKBIA and down-regulation of NF-kappa-B activity. {ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: (Microbial infection) Cleaved by porcine reproductive and respiratory syndrome virus serine protease nsp4 after Glu-349. The cleavage inhibits NEMO proper function. {ECO:0000269|PubMed:25008936}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6K9}. Nucleus {ECO:0000250|UniProtKB:Q9Y6K9}. Note=Sumoylated NEMO accumulates in the nucleus in response to genotoxic stress. {ECO:0000250|UniProtKB:Q9Y6K9}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling receptor pathways. Can recognize and bind both 'Lys-63'-linked and linear polyubiquitin upon cell stimulation, with a much highr affinity for linear polyubiquitin. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination. {ECO:0000250|UniProtKB:Q9Y6K9}. | Sus scrofa (Pig) |
A9RA84 | HMGB1_PAPAN | MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEDEEEDDDDE | null | null | adaptive immune response [GO:0002250]; autophagy [GO:0006914]; chemotaxis [GO:0006935]; DNA geometric change [GO:0032392]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; positive regulation of response to external stimulus [GO:0032103]; regulation of transcription by RNA polymerase II [GO:0006357] | chromosome [GO:0005694]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endosome [GO:0005768]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | bubble DNA binding [GO:0000405]; DNA binding, bending [GO:0008301]; four-way junction DNA binding [GO:0000400]; supercoiled DNA binding [GO:0097100] | PF00505;PF09011; | 1.10.30.10; | HMGB family | PTM: Phosphorylated at serine residues. Phosphorylation in both NLS regions is required for cytoplasmic translocation followed by secretion. {ECO:0000250|UniProtKB:P09429}.; PTM: Acetylated on multiple sites upon stimulation with LPS (By similarity). Acetylation on lysine residues in the nuclear localization signals (NLS 1 and NLS 2) leads to cytoplasmic localization and subsequent secretion. Acetylation on Lys-3 results in preferential binding to DNA ends and impairs DNA bending activity (By similarity). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}.; PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-106 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB1 (HMGB1C23hC45hC106h), 2- disulfide HMGB1 (HMGB1C23-C45C106h) and 3- sulfonyl HMGB1 (HMGB1C23soC45soC106so). {ECO:0000250|UniProtKB:P09429}.; PTM: Poly-ADP-ribosylated by PARP1 when secreted following stimulation with LPS (By similarity). {ECO:0000250|UniProtKB:P63158}.; PTM: In vitro cleavage by CASP1 is liberating a HMG box 1-containing peptide which may mediate immunogenic activity; the peptide antagonizes apoptosis-induced immune tolerance. Can be proteolytically cleaved by a thrombin:thrombomodulin complex; reduces binding to heparin and pro-inflammatory activities (By similarity). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103}.; PTM: Forms covalent cross-links mediated by transglutaminase TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers. {ECO:0000250|UniProtKB:P09429}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09429}. Chromosome {ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}. Cytoplasm {ECO:0000250|UniProtKB:P09429}. Secreted {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}. Cell membrane {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}; Peripheral membrane protein {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}; Extracellular side {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}. Endosome {ECO:0000250|UniProtKB:P63158}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P63158}. Note=In basal state predominantly nuclear. Shuttles between the cytoplasm and the nucleus. Translocates from the nucleus to the cytoplasm upon autophagy stimulation. Release from macrophages in the extracellular milieu requires the activation of NLRC4 or NLRP3 inflammasomes (By similarity). Passively released to the extracellular milieu from necrotic cells by diffusion, involving the fully reduced HGMB1 which subsequently gets oxidized. Also released from apoptotic cells. Active secretion from a variety of immune and non-immune cells such as macrophages, monocytes, neutrophils, dendritic cells, natural killer cells and plasma cells in response to various stimuli such as LPS and cytokines involves a nonconventional secretory process via secretory lysosomes. Found on the surface of activated platelets. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}. | null | null | null | null | null | FUNCTION: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as a sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as a danger-associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. Has proangiogenic activity. May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}.; FUNCTION: Nuclear functions are attributed to fully reduced HGMB1. Associates with chromatin and binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA, DNA-containing cruciforms or bent structures, supercoiled DNA and ZDNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity. May be involved in nucleotide excision repair (NER), mismatch repair (MMR) and base excision repair (BER) pathways, and double strand break repair such as non-homologous end joining (NHEJ). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). In vitro can displace histone H1 from highly bent DNA. Can restructure the canonical nucleosome leading to relaxation of structural constraints for transcription factor-binding. Enhances binding of sterol regulatory element-binding proteins (SREBPs) such as SREBF1 to their cognate DNA sequences and increases their transcriptional activities. Facilitates binding of TP53 to DNA. May be involved in mitochondrial quality control and autophagy in a transcription-dependent fashion implicating HSPB1. Can modulate the activity of the telomerase complex and may be involved in telomere maintenance. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}.; FUNCTION: In the cytoplasm proposed to dissociate the BECN1:BCL2 complex via competitive interaction with BECN1 leading to autophagy activation. Can protect BECN1 and ATG5 from calpain-mediated cleavage and thus proposed to control their proautophagic and proapoptotic functions and to regulate the extent and severity of inflammation-associated cellular injury. In myeloid cells has a protective role against endotoxemia and bacterial infection by promoting autophagy. Involved in endosomal translocation and activation of TLR9 in response to CpG-DNA in macrophages. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}.; FUNCTION: In the extracellular compartment (following either active secretion or passive release) involved in regulation of the inflammatory response. Fully reduced HGMB1 (which subsequently gets oxidized after release) in association with CXCL12 mediates the recruitment of inflammatory cells during the initial phase of tissue injury; the CXCL12:HMGB1 complex triggers CXCR4 homodimerization. Induces the migration of monocyte-derived immature dendritic cells and seems to regulate adhesive and migratory functions of neutrophils implicating AGER/RAGE and ITGAM. Can bind to various types of DNA and RNA including microbial unmethylated CpG-DNA to enhance the innate immune response to nucleic acids. Proposed to act in promiscuous DNA/RNA sensing which cooperates with subsequent discriminative sensing by specific pattern recognition receptors. Promotes extracellular DNA-induced AIM2 inflammasome activation implicating AGER/RAGE. Disulfide HMGB1 binds to transmembrane receptors, such as AGER/RAGE, TLR2, TLR4 and probably TREM1, thus activating their signal transduction pathways. Mediates the release of cytokines/chemokines such as TNF, IL-1, IL-6, IL-8, CCL2, CCL3, CCL4 and CXCL10. Promotes secretion of interferon-gamma by macrophage-stimulated natural killer (NK) cells in concert with other cytokines like IL-2 or IL-12. TLR4 is proposed to be the primary receptor promoting macrophage activation and signaling through TLR4 seems to implicate LY96/MD-2. In bacterial LPS- or LTA-mediated inflammatory responses binds to the endotoxins and transfers them to CD14 for signaling to the respective TLR4:LY96 and TLR2 complexes. Contributes to tumor proliferation by association with ACER/RAGE. Can bind to IL1-beta and signals through the IL1R1:IL1RAP receptor complex. Binding to class A CpG activates cytokine production in plasmacytoid dendritic cells implicating TLR9, MYD88 and AGER/RAGE and can activate autoreactive B cells. Via HMGB1-containing chromatin immune complexes may also promote B cell responses to endogenous TLR9 ligands through a B-cell receptor (BCR)-dependent and ACER/RAGE-independent mechanism. Inhibits phagocytosis of apoptotic cells by macrophages; the function is dependent on poly-ADP-ribosylation and involves binding to phosphatidylserine on the cell surface of apoptotic cells. In adaptive immunity may be involved in enhancing immunity through activation of effector T-cells and suppression of regulatory T (TReg) cells. In contrast, without implicating effector or regulatory T-cells, required for tumor infiltration and activation of T-cells expressing the lymphotoxin LTA:LTB heterotrimer thus promoting tumor malignant progression. Also reported to limit proliferation of T-cells. Released HMGB1:nucleosome complexes formed during apoptosis can signal through TLR2 to induce cytokine production. Involved in induction of immunological tolerance by apoptotic cells; its pro-inflammatory activities when released by apoptotic cells are neutralized by reactive oxygen species (ROS)-dependent oxidation specifically on Cys-106. During macrophage activation by activated lymphocyte-derived self apoptotic DNA (ALD-DNA) promotes recruitment of ALD-DNA to endosomes. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}. | Papio anubis (Olive baboon) |
A9RVK2 | M3K1B_PHYPA | MVEERGSSRSSRGGSWGSGEDGGSSHGGKGVPKLSRTVAKKIHKYDVSADHSDYEDDGSVHSTSSSGSRRNPLSKSIIQQQSFRVGANFEEDLKTLYELIGVSKPADLAISASDWQSRGKSIAYSQPLSSPSLSQEHGEASHSNDLKPSIIDFRSEAPAASPRELPVAPVKLDAHERMTYRSDYVNSQPQNHYGRKNSPSQRSPPPESFPAFDSSPSRLGREGYGLHRMQSDPVMPTLGALSPLGTGNAHPESAGSTATRRWSFDLVPGNHEGDYANMSQVVRDNLPSAAVAMPKNGLVRRSPIIRDPNRSNSSVSNPYAQRQYPNLAEEAESSAKPESSAIPDSSAMPELPAKLESTAVPELSAKPESNAKPESEPEQDSSVEARTEHYGSVRKSKIPSALIIDKFEEPSIVSTGRSPGVVSKRPPWDTWFKGDFIGSGTFGSVYEGIDNNGMFFAVKEVSLKDQGKVGQEAIKQLEHEIALLSDIQHPNIVQYLGTERDDEKLYIFLELVSKGSLASLYKKYYFVYDQVRAYTKQILSGLKYLHDRKIIHRDIKCANILVDTNGVVKLADFGMAKQVDKLGLLKSFMGSAHWMAPEVVNPKRQYNFLADIWSLGCTVLEMATGDAPFGELECHSVLWKVGNGEGPLIPDDLEDEMKDFISKCLEVTVGNRPTCDMLLTHPFITGEPMTGPVKLVPMPELSTISEERSIDVSESPSIATSSQSGSSPSVAGDAVSPASVAVRPRSMRTLRSEFSMSSPESIAS | 2.7.11.25 | null | defense response [GO:0006952]; MAPK cascade [GO:0000165]; phosphorylation [GO:0016310]; response to chitin [GO:0010200] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q39008}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000250|UniProtKB:Q39008}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000250|UniProtKB:Q39008}; | null | null | null | null | FUNCTION: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for responses to chitin and acts redundantly with MEKK1a. {ECO:0000269|PubMed:27268428}. | Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens) |
A9S9Q8 | MPK4B_PHYPA | MDVAGAGGGGAADGNIQGVPTHNGEYTQYNIFGNLFEVSRKYVPPIRPIGRGAYGIVCSAVNSETGEEVAIKKIGNAFDNRIDAKRTLREIKLLRHMDHENIVAIRDIIRPPTRENFNDVYIVYELMDTDLHQIIRSNQPLTEDHCQYFLYQLLRGLKYIHSAKVLHRDLKPSNLLLNANCDLKICDFGLARTTSETDFMTEYVVTRWYRAPELLLNCSEYTAAIDVWSVGCIFMELLNREPLFPGRDYVQQLRLITELIGSPEDHDLGFLRSDNARRYIRQLPRFARQPLDRKFPNMGPAAIDLVEHMLRFDPARRITVEEALAHPYLATLHDINDEPICHSPFEFDFEQPSFTEEHIKELIMMEAIAFNPGNVGDMMS | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|RuleBase:RU361165}; | innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; pattern recognition receptor signaling pathway [GO:0002221]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Dually phosphorylated on Thr-201 and Tyr-203, which activates the enzyme. Phosphorylated in response to pathogen-associated molecular pattern (PAMP) chitin and to a lot lesser extent in response to necrotrophic fungus B.cinerea spores. Not phosphorylated in response to osmotic stress. {ECO:0000269|PubMed:27268428}. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000255|RuleBase:RU361165, ECO:0000269|PubMed:27268428}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000255|RuleBase:RU361165, ECO:0000269|PubMed:27268428}; | null | null | null | null | FUNCTION: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein may act redundantly with MPK4a in innate immunity triggered by pathogen-associated molecular patterns (PAMPs). May also be involved in resistance to necrotrophic fungi B.cinerea. {ECO:0000305|PubMed:27268428}. | Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens) |
A9SIZ6 | D5FAD_PHYPA | MAPHSADTAGLVPSDELRLRTSNSKGPEQEQTLKKYTLEDVSRHNTPADCWLVIWGKVYDVTSWIPNHPGGSLIHVKAGQDSTQLFDSYHPLYVRKMLAKYCIGELVPSAGDDKFKKATLEYADAENEDFYLVVKQRVESYFKSNKINPQIHPHMILKSLFILGGYFASYYLAFFWSSSVLVSLFFALWMGFFAAEVGVSIQHDGNHGSYTKWRGFGYIMGASLDLVGASSFMWRQQHVVGHHSFTNVDNYDPDIRVKDPDVRRVATTQPRQWYHAYQHIYLAVLYGTLALKSIFLDDFLAYFTGSIGPVKVAKMTPLEFNIFFQGKLLYAFYMFVLPSVYGVHSGGTFLALYVASQLITGWMLAFLFQVAHVVDDVAFPTPEGGKVKGGWAAMQVATTTDFSPRSWFWGHVSGGLNNQIEHHLFPGVCHVHYPAIQPIVEKTCKEFDVPYVAYPTFWTALRAHFAHLKKVGLTEFRLDG | 1.14.19.30 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:O00767}; | lipid metabolic process [GO:0006629]; long-chain fatty acid biosynthetic process [GO:0042759]; unsaturated fatty acid biosynthetic process [GO:0006636] | membrane [GO:0016020] | di-homo-gamma-linolenate delta5 desaturase activity [GO:0102866]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water [GO:0016717] | PF00173;PF00487; | 3.10.120.10; | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=an (8Z,11Z,14Z)-icosatrienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46260, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:90076, ChEBI:CHEBI:90077; EC=1.14.19.30; Evidence={ECO:0000305|PubMed:16728405}; CATALYTIC ACTIVITY: Reaction=an (8Z,11Z,14Z,17Z)-eicosatetraenoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46264, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:90082, ChEBI:CHEBI:90083; EC=1.14.19.30; Evidence={ECO:0000305|PubMed:16728405}; | null | null | null | null | FUNCTION: Fatty acid desaturase that introduces a cis double bond at the 5-position in 20-carbon polyunsaturated fatty acids incorporated in a glycerolipid that contain a Delta(8) double bond. {ECO:0000269|PubMed:16728405}. | Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens) |
A9SR33 | M2K1B_PHYPA | MSRRHRTGGLRVAVPKQENSIHRFLTANGVFHDDDIQLDHMGLRVVSSESTAYANPPDAQLSLADLEAVRVLGKGAGGSVQLVRHKWTNDIYALKGIQMNINETVRKQIVQELKINQLTLHQCPYIVKCYHSFYHNGIISIVLEYMDRGSLADIIKQTKQIPEPYLAVISNQVLKGLNYLHQVRHIIHRDIKPSNLLINQKGEVKISDFGVSAVLISSMAQRDTFVGTYTYMSPERLGGQSYAYDSDIWSLGLTILECALGYFPYRPPGQEEGWNNFFMLMELVINQPPVAAPPDKFSPEFCSFIAACIQKRPGDRLSTADLLKHPFLQKYSEEEYHLSNLR | 2.7.12.2 | null | defense response [GO:0006952]; phosphorylation [GO:0016310]; response to chitin [GO:0010200] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2; Evidence={ECO:0000250|UniProtKB:Q9S7U9}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.2; Evidence={ECO:0000250|UniProtKB:Q9S7U9}; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2; Evidence={ECO:0000250|UniProtKB:Q9S7U9}; | null | null | null | null | FUNCTION: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for full defense response to fungal pathogen chitin. {ECO:0000269|PubMed:27268428}. | Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens) |
A9SY39 | M3K1A_PHYPA | MIEERGSSRGSREDRGSSRGSSRGSFEDKGSSHDWKGMGGSTPRPRLTRLVAKKDRNYDAKVDSDFDDDSSVHSTSSPRLSPASSDNLSKITIGQQSFRVGGDVDNLKALYEALGATSPAALGIEASDWESRRKSAVYSRPTSPPRVSHDTGQSSYSHDFQFPASRVDSSLESPPLSPRGLAPMSPVRPIEVEWRKHRNNYAKPTISNRPGRENNPLKPSQPPPTMFPQSSGLRTPDPLPPIDTSTSRLGRESLELQNRHTTLGAYSPPGLRKVHSELTGLVSARSDGAGWASDIESAKRNEDLAVASPVFRDNLPSAAVAMPNGSLVRASFTPRDSNRMNSVRSNSHGLRWNSCHAQEAEAIAKTALEETSNGLRIEDPERIRDLEKPSPLIIEKVDEPLSEVSSSVSTESSPSVIPKRPPWDTWAKGEFLGSGTFGSVYEGVARNGTFFAVKEVNLADEGKLGRQAVKQLEREIALLSDIQHPNIVQYLGTERTEDKLYIFLELLNKGSLANLYRKYGLFYEQIKAYTEQILTGLKYLHDRKIIHRDIKCANILVDTNGVVKLADFGMAKQVEKFGFAKSFVGSAHWMAPEVVDPKQQYNFAADIWSLGCTVLEMATEGPPFGELEFIAVFWKIGRGEAPLIPDDLEDELKDFIAQCLQVDASKRPTCDMLLAHPFITGEEMTGPVTQMGTPGLSTISEERSVDMSVTSSIAVSSNSGTSPRVIENLVNHLSIERRPKSMRTLRSELSMSSAESIAS | 2.7.11.25 | null | defense response [GO:0006952]; MAPK cascade [GO:0000165]; phosphorylation [GO:0016310]; response to chitin [GO:0010200] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q39008}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000250|UniProtKB:Q39008}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000250|UniProtKB:Q39008}; | null | null | null | null | FUNCTION: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for responses to chitin and acts redundantly with MEKK1b. {ECO:0000269|PubMed:27268428}. | Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens) |
A9T142 | MPK4A_PHYPA | METSSGTPELKVISTPTYGGHYVKYVVAGTDFEVTARYKPPLRPIGRGAYGIVCSLFDTVTGEEVAVKKIGNAFDNRIDAKRTLREIKLLRHMDHENVVAITDIIRPPTRENFNDVYIVYELMDTDLHQIIRSNQALTEDHCQYFLYQILRGLKYIHSANVLHRDLKPTNLLVNANCDLKIADFGLARTLSETDFMTEYVVTRWYRAPELLLNCSAYTAAIDIWSVGCIFMELLNRSALFPGRDYVHQLRLITELIGTPEDRDLGFLRSDNARRYIKHLPRQSPIPLTQKFRGINRSALDLVEKMLVFDPAKRITVEAALAHPYLASLHDINDEPASVSPFEFDFEEPSISEEHIKDLIWREALDCSLGPDDMVQ | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|RuleBase:RU361165}; | innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; pattern recognition receptor signaling pathway [GO:0002221]; phosphorylation [GO:0016310]; regulation of gene expression [GO:0010468] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Dually phosphorylated on Thr-197 and Tyr-199, which activates the enzyme. Phosphorylated in response to pathogen-associated molecular pattern (PAMP) chitin and in response to necrotrophic fungus B.cinerea spores. Not phosphorylated in response to osmotic stress. {ECO:0000269|PubMed:27268428}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27268428}. Nucleus {ECO:0000269|PubMed:27268428}. Note=Localization to the cytoplasm and nucleus does not change significantly following chitin treatment. {ECO:0000269|PubMed:27268428}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000255|RuleBase:RU361165, ECO:0000269|PubMed:27268428}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000255|RuleBase:RU361165, ECO:0000269|PubMed:27268428}; | null | null | null | null | FUNCTION: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for innate immunity triggered by pathogen-associated molecular patterns (PAMPs). Involved in resistance to necrotrophic fungi B.cinerea and A.brassicicola. Involved in the transduction of signals from chitosan perception to the activation of defense genes. {ECO:0000269|PubMed:27268428}. | Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens) |
A9TXT1 | CERK1_PHYPA | MKFQMKMKSELCRTYKYWLILLVLWLSGVTQRETGVLIVDADCIPPNGCKALAYYRLKQGDDLEKLQGRFQTNNSEVLAYNPQLVDANSIQAGTNIYLPFDCLCLNGELVHRFSYTVTTNDTAEKVVDVTYQKLTTVGAVRSASNSGDLSSIYSGQSLTIPVRCYCGDPNVDPKYGLFSTYVVQADDQLTSLSTNFSVDADVISKFNSDTRNLSPDSIIFIPSKAANGSFPPFSGYVLGTVHWRSNVGIIVGVVVGGIVLAVLLLFALIFGFKHFRRRKLAKEPTMQQSGLLSSSSMAGSKPSRSGSTMLPVPKSVEFTYEELAAATDNFSLAKKIGQGGFASVYYGVIRDQKLAIKKMTLQCTKEFLAELQVLTNVHHTNLVQLIGYCTTNSLFLVYEYIENGTLDHHLRRRKSDDKPPLSWLQRVQICLDSARGLEYIHEHTKPTYIHRDIKSANILLDDNFRAKVADFGLAKLAEEGTGTGIVGTFGYMPPEYALYGEVSPKLDVYAFGVVLFEIISGRVAISSALPSENDQQSPAQNRESRTLTSFFEPVLNDPDGKTLLPKCIDPALNGEYSLDAVWKMAQLARRCTHQSPDMRPTMRFAVVQLMTLASVTQEWDVGYFSRASSQSQPPSGNDQL | 2.7.11.1 | null | innate immune response [GO:0045087]; phosphorylation [GO:0016310] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; chitin binding [GO:0008061]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; transmembrane receptor protein kinase activity [GO:0019199] | PF01476;PF07714; | 3.10.350.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A8R7E6}; Single-pass membrane protein {ECO:0000250|UniProtKB:A8R7E6}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:A8R7E6}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:A8R7E6}; | null | null | null | null | FUNCTION: Lysin motif (LysM) receptor kinase required as a cell surface receptor for chitin elicitor (chitooligosaccharides) signaling leading to innate immunity in response to biotic stresses (By similarity). The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for response to chitin. Is able to complement the A.thaliana cerk1 mutant (PubMed:27268428). {ECO:0000250|UniProtKB:A0A0P0XII1, ECO:0000269|PubMed:27268428}. | Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens) |
A9UHW6 | MI4GD_HUMAN | MGEPSREEYKIQSFDAETQQLLKTALKDPGAVDLEKVANVIVDHSLQDCVFSKEAGRMCYAIIQAESKQAGQSVFRRGLLNRLQQEYQAREQLRARSLQGWVCYVTFICNIFDYLRVNNMPMMALVNPVYDCLFRLAQPDSLSKEEEVDCLVLQLHRVGEQLEKMNGQRMDELFVLIRDGFLLPTGLSSLAQLLLLEIIEFRAAGWKTTPAAHKYYYSEVSD | null | null | cap-dependent translational initiation [GO:0002191]; regulation of translational initiation [GO:0006446] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; histone mRNA stem-loop binding complex [GO:0062073]; nucleolus [GO:0005730] | identical protein binding [GO:0042802]; RNA binding [GO:0003723]; translation activator activity [GO:0008494] | PF02854; | 1.25.40.180; | MIF4GD family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18025107}. Nucleus {ECO:0000269|PubMed:18025107}. | null | null | null | null | null | FUNCTION: Functions in replication-dependent translation of histone mRNAs which differ from other eukaryotic mRNAs in that they do not end with a poly-A tail but a stem-loop. May participate in circularizing those mRNAs specifically enhancing their translation. {ECO:0000269|PubMed:18025107}. | Homo sapiens (Human) |
A9ULC7 | OSTA_XENTR | MDPEQNDTKPPFNPICATRQAPYSHEILENLDITGILLFAILTFMTLVSLLVFLEEAYYMYRKIPNPKNSIIIWINAGAMMIATTSCFGMWIPRSTMFTDFTASVFLAVLIHKFQLMLVNECGGRREFLSTFGDTKLKISTGPFCCCCLCLPHKDINRKTLFILKLGTFQFAFLRPVLMFLAVVLWTNGTYMIGNSSAEKATIWINIGVGITTITALWAVGIMFNLVKDNLKEKNIIGKFAVYQFTVILSQLQTSIINILGTTGVISCVPPLPGPSRASYMNQQLLIMEMFLVTVICRVLYRRRYDDKNLLENQETNDNLRNSMMHLNGKALEDGPQSV | null | null | bile acid and bile salt transport [GO:0015721] | endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF03619; | null | OST-alpha family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703, ChEBI:CHEBI:36257; Evidence={ECO:0000250|UniProtKB:Q90YM5}; CATALYTIC ACTIVITY: Reaction=prostaglandin E2(out) = prostaglandin E2(in); Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:Q90YM5}; CATALYTIC ACTIVITY: Reaction=estrone 3-sulfate(out) = estrone 3-sulfate(in); Xref=Rhea:RHEA:71835, ChEBI:CHEBI:60050; Evidence={ECO:0000250|UniProtKB:Q86UW1}; CATALYTIC ACTIVITY: Reaction=dehydroepiandrosterone 3-sulfate(out) = dehydroepiandrosterone 3-sulfate(in); Xref=Rhea:RHEA:71839, ChEBI:CHEBI:57905; Evidence={ECO:0000250|UniProtKB:Q86UW1}; CATALYTIC ACTIVITY: Reaction=tauroursodeoxycholate(out) = tauroursodeoxycholate(in); Xref=Rhea:RHEA:71843, ChEBI:CHEBI:132028; Evidence={ECO:0000250|UniProtKB:Q8R000}; CATALYTIC ACTIVITY: Reaction=glycoursodeoxycholate(out) = glycoursodeoxycholate(in); Xref=Rhea:RHEA:71847, ChEBI:CHEBI:132030; Evidence={ECO:0000250|UniProtKB:Q8R000}; CATALYTIC ACTIVITY: Reaction=glycocholate(out) = glycocholate(in); Xref=Rhea:RHEA:71851, ChEBI:CHEBI:29746; Evidence={ECO:0000250|UniProtKB:Q8R000}; CATALYTIC ACTIVITY: Reaction=taurochenodeoxycholate(out) = taurochenodeoxycholate(in); Xref=Rhea:RHEA:71855, ChEBI:CHEBI:9407; Evidence={ECO:0000250|UniProtKB:Q8R000}; CATALYTIC ACTIVITY: Reaction=glycochenodeoxycholate(out) = glycochenodeoxycholate(in); Xref=Rhea:RHEA:71859, ChEBI:CHEBI:36252; Evidence={ECO:0000250|UniProtKB:Q8R000}; CATALYTIC ACTIVITY: Reaction=taurodeoxycholate(out) = taurodeoxycholate(in); Xref=Rhea:RHEA:71863, ChEBI:CHEBI:36261; Evidence={ECO:0000250|UniProtKB:Q8R000}; CATALYTIC ACTIVITY: Reaction=glycodeoxycholate(out) = glycodeoxycholate(in); Xref=Rhea:RHEA:71867, ChEBI:CHEBI:82982; Evidence={ECO:0000250|UniProtKB:Q8R000}; | null | null | null | null | FUNCTION: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for the translocation of bile acids (such as taurocholate), steroids (such as estrone sulfate), and eicosanoids (such as prostaglandin E2). {ECO:0000250|UniProtKB:Q90YM5}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A9ULR9 | BACD1_DANRE | MSAEASGSSGGHAVTVSGSSPSSSSHVGEEKPGRSLVSSKYVKLNVGGTLHYTTVQTLSKEDSLLRSICDGSTEVSIDSEGWVVLDRCGRHFSLVLNFLRDGTVPLPDSTRELEEVLKEAQYYRLQGLVQHCLSTLQKRRDVCRGCHIPMITSAKEEQRMIATCRKPVVKLQNNRGNNKYSYTSNSDDNLLKNIELFDKLGLRFNGRVLFIKDVLGDEICCWSFYGEGRKIAEVCCTSIVYATEKKQTKVEFPEARIFEETLNILIYENGRGSGGMALLESGGVSSSGAGQSEEEGAGAGGGDRRVRRIHVRRHIMHDERGHGQQTVYKD | null | null | brain development [GO:0007420]; central nervous system projection neuron axonogenesis [GO:0021952]; head development [GO:0060322]; negative regulation of Rho protein signal transduction [GO:0035024]; neural precursor cell proliferation [GO:0061351]; positive regulation of apoptotic process [GO:0043065]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein homooligomerization [GO:0051260]; protein ubiquitination [GO:0016567] | Cul3-RING ubiquitin ligase complex [GO:0031463]; nucleus [GO:0005634] | ubiquitin-protein transferase activity [GO:0004842] | PF02214; | null | BACURD family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WZ19}. | null | null | null | null | null | FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for synaptic transmission (By similarity). The BCR(KCTD13) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and promoting synaptic transmission (PubMed:29088697). {ECO:0000250|UniProtKB:Q8BGV7, ECO:0000305|PubMed:29088697}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A9WCM4 | ENO_CHLAA | MSTLIEAIVAREVLDSRGNPTIEVDVRLESGDVGRAIVPSGASTGAHEALELRDGDKSRYNGKGVLKAVQAVNEDIAEALIGFDAADQIALDQELIALDGTPNKSKLGANAILGVSLAAAKAAAAAFGLPLYRYLGGVYAHVLPVPMMNIMNGGQHATNSTDFQEFMIMPVGAESFREGLRWGAEIYHMLKKVIHDRGFSTTVGDEGGFAPSLPTNDAPLQLIMEAIEKAGYRPGEQIVIALDPATTEIFEDGKYHLKREGRSLSSAEMVDYWVDLVNRYPIISLEDGLAEDDWEGWALLRAKLGDRVQLVGDDFLVTNVQRLQRAIEAKAANSILIKLNQIGSLTETLSAIQLAQRSGWTAVVSHRSGESEDVTIADLVVATNAGQIKTGAPARTDRIAKYNQLLRIEEELGSAARYAGRSAFKV | 4.2.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26082925}; Note=Binds a second Mg(2+) ion via substrate during catalysis (PubMed:26082925). {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26082925}; | glycolytic process [GO:0006096] | cell surface [GO:0009986]; extracellular region [GO:0005576]; phosphopyruvate hydratase complex [GO:0000015] | magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634] | PF00113;PF03952; | 3.20.20.120;3.30.390.10; | Enolase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000305|PubMed:26082925}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. {ECO:0000255|HAMAP-Rule:MF_00318}. | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26082925}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165; Evidence={ECO:0000269|PubMed:26082925}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10166; Evidence={ECO:0000305|PubMed:26082925}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=35 uM for 2-phosphoglycerate (2-PG) at 80 degrees Celsius {ECO:0000269|PubMed:26082925}; KM=158 uM for 2-PG at 25 degrees Celsius {ECO:0000269|PubMed:26082925}; Vmax=50 umol/min/mg enzyme for 2-PG at 80 degrees Celsius {ECO:0000269|PubMed:26082925}; Vmax=9 umol/min/mg enzyme for 2-PG at 25 degrees Celsius {ECO:0000269|PubMed:26082925}; | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00318}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5, thermostable up to 85 degrees Celsius, at 90 degrees it loses about 50% activity (PubMed:26082925). {ECO:0000269|PubMed:26082925}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius. {ECO:0000269|PubMed:26082925}; | FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP) (PubMed:26082925). It is essential for the degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26082925}. | Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl) |
A9WGE2 | CCL_CHLAA | MEAVTIVDVAPRDGLQNEPDVLEPATRVELIERLLAAGVPRIEIGSFVNPRQVPQMAGIDQIARMLIERGHNLAARTTNDLFRFTALVPNQRGYELAAAAGLRHVRLVLAASDGLNRANFKRTTAESLIEFSRFALNIRRDGLTFGVAIGAAFGCPFDGYVSPERVRAIAEHAVDIGAGEIILADTTGMAVPTQVAALCRTILDRIPDVTVTLHLHNTRNTGYANAFAAWQVGIRSFDAALGGIGGCPFAPRAVGNIASEDLVHLFNGLGVPTGIDLSALIAASDWLSATLGRPLPALVGKAGPVYPQVVSMAPYLS | 4.1.3.46 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17259315}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:17259315}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:17259315}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17259315}; Note=Divalent cations such as manganese, cobalt, nickel and magnesium. {ECO:0000269|PubMed:17259315}; | carbon fixation by 3-hydroxypropionate cycle [GO:0043427]; glyoxylate catabolic process [GO:0009436]; ketone body biosynthetic process [GO:0046951]; leucine catabolic process [GO:0006552] | null | (3R)-citramalyl-CoA lyase activity [GO:0044101]; hydroxymethylglutaryl-CoA lyase activity [GO:0004419]; metal ion binding [GO:0046872]; oxo-acid-lyase activity [GO:0016833]; transferase activity [GO:0016740] | PF00682; | 3.20.20.70; | HMG-CoA lyase family | null | null | CATALYTIC ACTIVITY: Reaction=(3R)-citramalyl-CoA = acetyl-CoA + pyruvate; Xref=Rhea:RHEA:38275, ChEBI:CHEBI:15361, ChEBI:CHEBI:57288, ChEBI:CHEBI:75637; EC=4.1.3.46; Evidence={ECO:0000269|PubMed:17259315}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=70 uM for (R)-citramalyl-CoA {ECO:0000269|PubMed:17259315}; Note=kcat is 1.7 sec(-1) for lyase activity with (R)-citramalyl-CoA as substrate.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7 (at 55 degrees Celsius). {ECO:0000269|PubMed:17259315}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:17259315}; | FUNCTION: Involved in the glyoxylate assimilation cycle used to regenerate acetyl-CoA and produce pyruvate as universal precursor for biosynthesis. Catalyzes the cleavage of (R)-citramalyl-CoA to yield acetyl-CoA and pyruvate. {ECO:0000269|PubMed:17259315}. | Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl) |
A9X1A0 | PI4KB_PAPAN | MGDTVVEPAPLKPTSEPTSGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLRGGVAVSSRGTPLELVNGDGVDSEIRCLDDPPAQIREEEDEMGATVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPVRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTSVPARIPENRIRSTRSVENLPECGITHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEVHTNSCDNISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFKRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM | 2.7.1.67 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; | inner ear development [GO:0048839]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310] | Golgi membrane [GO:0000139]; mitochondrial outer membrane [GO:0005741]; rough endoplasmic reticulum membrane [GO:0030867] | 1-phosphatidylinositol 4-kinase activity [GO:0004430]; 14-3-3 protein binding [GO:0071889]; ATP binding [GO:0005524] | PF00454;PF21245; | 1.10.1070.11; | PI3/PI4-kinase family, Type III PI4K subfamily | null | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Rough endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UBF8}. Note=Found in the outer membrane of mitochondria and membranes of the rough endoplasmic reticulum. Recruited to the Golgi complex by the small GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5-bisphosphate (PIP2) on the Golgi complex. Recruited to the Golgi apparatus membrane by ACBD3, GGA2 is also involved in the recruitment. {ECO:0000250|UniProtKB:Q9UBF8}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.67; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; | null | null | null | null | FUNCTION: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation (By similarity). Involved in Golgi-to-plasma membrane trafficking (By similarity). May play an important role in the inner ear development. {ECO:0000250|UniProtKB:O08561, ECO:0000250|UniProtKB:Q9UBF8}. | Papio anubis (Olive baboon) |
A9XMT3 | CCLOP_LOTJA | MEGRGFSGLYRNSSEELFLKTVMESPIGMPVPSMEMLGFKNVSQGFRADSEELFKRWLTNGEGYNSSSIGFSSRLSKRISTELVNGSNQLQVGVASDGRNNDKPFIQNNLLANDVSGDFNFPIRDPVDRELQPSNLFLAKAWFLSDQRMTRSRSSELRRRYSEMQNGLATQGIESICMDPQHGAEATKQEVANFNGYNYLSMCELPSQKGSFMSPSNSCSSNFNTPQFGDMDKVSSCVSMLKGTLQRRRLSSQLEKEAAEDDLNGIFYPQEPLFQTGFDQGQENWSNQTPVNVQVDSIGEVKDHGVLQTLEGSTNPVVDGFANQINQIYVGTASGEPSQSESSNAAPVISSGLDTCEGPINSNQTLCESSWKQVGVSKSSENTQNRVKGFREQIMDNLKDDKKRKSLERYGSITSAVSDDKGDTTKKRRVERSRKMAEAKERNSTPSVPSDMQAVLKRCENLEKEVRSLKLNLSFMNRKDSEQTKQIEDLQKQNEELADEKERLLEEIERILSETEKM | null | null | arbuscular mycorrhizal association [GO:0036377]; nodulation [GO:0009877]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; protein homodimerization activity [GO:0042803]; sequence-specific DNA binding [GO:0043565] | null | null | CYCLOPS family | PTM: Phosphorylated at the N-terminus by CCAMK. {ECO:0000269|PubMed:19074278}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19074278}. | null | null | null | null | null | FUNCTION: Involved in symbiotic signaling. Required for root infection by symbiotic rhizobia, infection thread (IT) formation, and nodule development (PubMed:19074278). Probably not involved in nodule organogenesis (PubMed:19074278). Involved in arbuscular mycorrhizal (AM) symbiosis (PubMed:19074278). Required for fungal infection of the outer cortical cell layers, and for arbuscule development during the AM symbiosis, by binding, as a complex comprising CCaMK, CYCLOPS, and DELLA, to RAM1 promoter cis element thus promoting its expression (PubMed:19074278, PubMed:27020747). Acts downstream of CCAMK (PubMed:19074278). Binds to the promoter of ERN1 and strongly transactivates ERN1, a transcriptional regulator required for nodulation (PubMed:28503742). {ECO:0000269|PubMed:19074278, ECO:0000269|PubMed:27020747, ECO:0000269|PubMed:28503742}. | Lotus japonicus (Lotus corniculatus var. japonicus) |
A9YTQ3 | AHRR_HUMAN | MPRTMIPPGECTYAGRKRRRPLQKQRPAVGAEKSNPSKRHRDRLNAELDHLASLLPFPPDIISKLDKLSVLRLSVSYLRVKSFFQVVQEQSSRQPAAGAPSPGDSCPLAGSAVLEGRLLLESLNGFALVVSAEGTIFYASATIVDYLGFHQTDVMHQNIYDYIHVDDRQDFCRQLHWAMDPPQVVFGQPPPLETGDDAILGRLLRAQEWGTGTPTEYSAFLTRCFICRVRCLLDSTSGFLTMQFQGKLKFLFGQKKKAPSGAMLPPRLSLFCIAAPVLLPSAAEMKMRSALLRAKPRADTAATADAKVKATTSLCESELHGKPNYSAGRSSRESGVLVLREQTDAGRWAQVPARAPCLCLRGGPDLVLDPKGGSGDREEEQHRMLSRASGVTGRRETPGPTKPLPWTAGKHSEDGARPRLQPSKNDPPSLRPMPRGSCLPCPCVQGTFRNSPISHPPSPSPSAYSSRTSRPMRDVGEDQVHPPLCHFPQRSLQHQLPQPGAQRFATRGYPMEDMKLQGVPMPPGDLCGPTLLLDVSIKMEKDSGCEGAADGCVPSQVWLGASDRSHPATFPTRMHLKTEPDSRQQVYISHLGHGVRGAQPHGRATAGRSRELTPFHPAHCACLEPTDGLPQSEPPHQLCARGRGEQSCTCRAAEAAPVVKREPLDSPQWATHSQGMVPGMLPKSALATLVPPQASGCTFLP | null | null | xenobiotic metabolic process [GO:0006805] | aryl hydrocarbon receptor complex [GO:0034751]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; nuclear receptor activity [GO:0004879]; protein dimerization activity [GO:0046983]; transcription cis-regulatory region binding [GO:0000976] | PF00010;PF00989; | 4.10.280.10;3.30.450.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17980155}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:17980155}. Note=Predominantly in the nuclear compartment. First cytoplasmic, translocates into the nuclear compartment upon interaction with ARNT in the cytoplasmic compartment. | null | null | null | null | null | FUNCTION: Mediates dioxin toxicity and is involved in regulation of cell growth and differentiation. Represses the transcription activity of AHR by competing with this transcription factor for heterodimer formation with the ARNT and subsequently binding to the xenobiotic response element (XRE) sequence present in the promoter regulatory region of variety of genes. Represses CYP1A1 by binding the XRE sequence and recruiting ANKRA2, HDAC4 and/or HDAC5. Autoregulates its expression by associating with its own XRE site. {ECO:0000269|PubMed:17890447, ECO:0000269|PubMed:18172554}. | Homo sapiens (Human) |
A9YWR6 | STR2_MEDTR | MKTQGLELETVIDIKHKPVSFTGGLEFESLTYTVTKKKKVDGKWSNEDVDLLHDITGYAPKGCITAVMGPSGAGKSTLLDGLAGRIASGSLKGKVSLDGNSVNASLIKRTSAYIMQEDRLFPMLTVYETLMFAADFRLGPLSAVDKRQRVEKLIEQLGLSSSRNTYIGDEGTRGVSGGERRRVSIGVDIIHGPSLLFLDEPTSGLDSTSALSVIEKLHDIARNGSTVILTIHQPSSRIQLLLDHLIILARGQLMFQGSLKDVGHHLNRMGRKIPKGENPIENLIDVIQEYDQCDFVGVEVLAEFARTGMKPPLLSDMEEIISYTNSIAPSPSPLHRGSKYEEKSQDFSYSSQISRRSLNDEFDHSIRSPYNNTPMSWSASNSAAFLKFTPSRLKNENKVQKPPSHASPGIYTYSSEILPATPTPHSSDYVVDENDYLTPTNSSQEHLGPKFANSYIGETWILMRRNFTNIRRTPELFLSRLMVLTFMGVMMATMFHNPKNTLQGITNRLSFFIFTVCLFFFSSNDAVPAFIQERFIFIRETSHNAYRASCYTIASLITHMPFLALQALAYAAIVWFALELRGPFIYFFLVLFISLLSTNSFVVFVSSIVPNYILGYAAVIAFTALFFLFCGYFLSSEDIPLYWRWMNKVSTMTYPYEGLLMNEYQTNETFGSNDGVSITGFDILKSLHIGTEEIKKRNNVLIMLGWAVLYRILFYIILRFASKNQRS | 7.6.2.- | null | arbuscular mycorrhizal association [GO:0036377]; response to symbiotic fungus [GO:0009610]; transmembrane transport [GO:0055085] | membrane [GO:0016020]; periarbuscular membrane [GO:0085042]; plasma membrane [GO:0005886] | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626] | PF01061;PF19055;PF00005; | 3.40.50.300; | ABC transporter superfamily, ABCG family, Stunted arbuscule (STR) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20453115}; Multi-pass membrane protein {ECO:0000255}. Note=Located in the peri-arbuscular membrane of arbuscular mycorrhiza (AM). {ECO:0000269|PubMed:20453115}. | null | null | null | null | null | FUNCTION: Together with STR, required for arbuscule development in arbuscular mycorrhizal symbiosis. {ECO:0000269|PubMed:20453115}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
A9ZLX4 | RIPR2_COTJA | MSIGSHSFSPGGPNGIIRSQSFAGFSGLQERRSRCNSFIENTSALKKPQAKVKKMHNLGHKNSTTPKEPQPKRVEEVYRALKNGLDEYLEVHQTELDKLTAQLKDMRRNSRLGVLYDLDKQIKAVERYMRRLEFHISKVDELYEAYCIQRRLCDGASKMKQAFAMSPTSKAARESLTEINRSYKEYTENMCTIEAELENLLGEFCIKMKGLAGFARLCPGDQYEIFMRYGRQRWKLKGKIEVNGKQSWDGEEMVFLPLIVGLISIKVTEVKGLATHILVGSVTCETKDLFAARPQVVAVDINDLGTIKLNLEITWYPFDVEDLTPSTGNVSKASALQRRMSMYSQGTPETPTFKDHSFFRWLHPLQDRPRLAILDALQDTFFDKLRRSRSFSDLPSLRLSPKAGLELYSNLPDDVFENGTATTEKRPLSFTFGDLPYEDRVPPANSAEPSSAHVTSSPDIATTATQHRARAQTAAAVTPAEGKACPGVRCEPRGHGDSCQEYPPGFQKPSDTGSDRVFIEANVPVSLLQDTDEGSELKPVELDTYEGNITKQLVKRLTSAEVPGTPERLPCEGSISGESEGYKSYLDGSIEEALQGLLLALEPHKEQYKEFQDLDQEVMHLDDILKCKPAVSRSRSSSLSLTVESALESFDFLNTSDFDDEDGGGEEVCNGGGGADSVFSDTEVEKNSYRTEHPEARGHLQRSLTEDTGVGTSVAGSPLPLTTGSDSLDITIVKHLQYCTQLIQQIVFSRKTPFVTRDLLDKLSRQTLVMENIAEISTENLGSITSLTDAIPEFHKKLSLLAFWMKCTGPSGVYHTSADKMMKQLDINFAATVNEECPGLAETVFRILVSQILDRTEPVLYSTMSSEIITVFQYYNYFASHSVNDLGSYLLQLAKEASVVQMLQSVKDGKLQQNVSKINSNNLPPQQEVLRALALLLNENKNEVSETVASLLTATAENKHFREKALIYYCEALTQPNLQLQKAACLALRYLKATESIKMLVMLCQSDNEEIRKVASETLLSLGEDGRLAYEQLDNSPGNLSELEVAGELNLPQLSRRTCLSVTATEEGWSCH | null | null | cell adhesion [GO:0007155]; cell differentiation [GO:0030154]; cellular response to chemokine [GO:1990869]; chemotaxis [GO:0006935]; muscle organ development [GO:0007517]; negative regulation of cell adhesion [GO:0007162]; negative regulation of establishment of T cell polarity [GO:1903904]; negative regulation of protein localization to cell leading edge [GO:1905872]; negative regulation of Rho guanyl-nucleotide exchange factor activity [GO:2001107]; negative regulation of Rho protein signal transduction [GO:0035024]; negative regulation of T cell migration [GO:2000405]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of myoblast fusion [GO:1901741]; positive regulation of neutrophil chemotaxis [GO:0090023]; positive regulation of neutrophil extravasation [GO:2000391]; regulation of establishment of cell polarity [GO:2000114]; sensory perception of sound [GO:0007605] | apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; filopodium [GO:0030175]; stereocilium [GO:0032420]; stereocilium membrane [GO:0060171] | 14-3-3 protein binding [GO:0071889] | PF15903; | 1.25.10.10; | RIPOR family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17825087}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9Y4F9}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9Y4F9}. Apical cell membrane {ECO:0000250|UniProtKB:Q7TP54}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q80U16}. Cell projection, stereocilium membrane {ECO:0000250|UniProtKB:Q7TP54}. | null | null | null | null | null | FUNCTION: Acts as an inhibitor of the small GTPase RHOA and plays several roles in the regulation of myoblast and hair cell differentiation, lymphocyte T proliferation and neutrophil polarization. Plays a role in fetal mononuclear myoblast differentiation by promoting filopodia and myotube formation (PubMed:17825087). Maintains naive T lymphocytes in a quiescent state and prevents chemokine-induced T lymphocyte responses, such as cell adhesion, polarization and migration. Involved also in the regulation of neutrophil polarization, chemotaxis and adhesion. Required for normal development of inner and outer hair cell stereocilia within the cochlea of the inner ear. Plays a role for maintaining the structural organization of the basal domain of stereocilia. Involved in mechanosensory hair cell function. Required for normal hearing (By similarity). {ECO:0000250|UniProtKB:Q80U16, ECO:0000250|UniProtKB:Q9Y4F9, ECO:0000269|PubMed:17825087}. | Coturnix japonica (Japanese quail) (Coturnix coturnix japonica) |
A9ZPH9 | GMAS_METMY | MKSLEEAQKFLEDHHVKYVLAQFVDIHGVAKVKSVPASHLNDILTTGAGFAGGAIWGTGIAPNGPDYMAIGELSTLSLIPWQPGYARLVCDGHVNGKPYEFDTRVVLKQQIARLAEKGWTLYTGLEPEFSLLKKDEHGAVHPFDDSDTLQKPCYDYKGITRHSPFLEKLTESLVEVGLDIYQIDHEDANGQFEINYTYADCLKSADDYIMFKMAASEIANELGIICSFMPKPFSNRPGNGMHMHMSIGDGKKSLFQDDSDPSGLGLSKLAYHFLGGILAHAPALAAVCAPTVNSYKRLVVGRSLSGATWAPAYIAYGNNNRSTLVRIPYGRLELRLPDGSCNPYLATAAVIAAGLDGVARELDPGTGRDDNLYDYSLEQLAEFGIGILPQNLGEALDALEADQVIMDAMGPGLSKEFVELKRMEWVDYMRHVSDWEINRYVQFY | 6.3.1.6; 6.3.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17284842}; | glutamine biosynthetic process [GO:0006542]; polyamine catabolic process [GO:0006598] | null | ATP binding [GO:0005524]; glutamate-ethylamine ligase activity [GO:0047942]; glutamate-methylamine ligase activity [GO:0047943]; glutamine synthetase activity [GO:0004356] | PF00120; | 3.10.20.70;3.30.590.10; | Glutamine synthetase family, Type 3 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + methylamine = ADP + H(+) + N(5)-methyl-L-glutamine + phosphate; Xref=Rhea:RHEA:17117, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58200, ChEBI:CHEBI:59338, ChEBI:CHEBI:456216; EC=6.3.4.12; Evidence={ECO:0000269|PubMed:17284842, ECO:0000269|PubMed:18175924}; CATALYTIC ACTIVITY: Reaction=ATP + ethylamine + L-glutamate = ADP + H(+) + N(5)-ethyl-L-glutamine + phosphate; Xref=Rhea:RHEA:20525, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58128, ChEBI:CHEBI:456216, ChEBI:CHEBI:566789; EC=6.3.1.6; Evidence={ECO:0000269|PubMed:17284842, ECO:0000269|PubMed:18175924}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.18 mM for methylamine {ECO:0000269|PubMed:17284842}; KM=0.57 mM for ethylamine {ECO:0000269|PubMed:17284842}; KM=3.9 mM for hydroxylamine {ECO:0000269|PubMed:17284842}; KM=84 mM for ammonia {ECO:0000269|PubMed:17284842}; KM=1.4 mM for glutamic acid (with methylamine as substrate) {ECO:0000269|PubMed:17284842}; KM=1.3 mM for glutamic acid (with ethylamine as substrate) {ECO:0000269|PubMed:17284842}; KM=1.3 mM for ATP (with methylamine as substrate) {ECO:0000269|PubMed:17284842}; KM=0.63 mM for ATP (with ethylamine as substrate) {ECO:0000269|PubMed:17284842}; | null | null | null | FUNCTION: Catalyzes the formation of N(5)-methyl-L-glutamine from glutamate and methylamine. In vitro, can also use ethylamine, hydroxylamine and ammonia, with 75%, 40% and 1% activity compared to methylamine, respectively. {ECO:0000269|PubMed:17284842, ECO:0000269|PubMed:18175924}. | Methylovorus mays |
A9ZSZ2 | AGO3_BOMMO | MADPGKGRGRSLALLQALKKSQMMDSPSQSESQSPESTPEQSTAPSTIASATPSTSGVSIGGRGRAAALMLAKMQQKPGSTTPAIFVPPSSTSAPTAGTGRGFKLLQNLQASQKASSQIASSQVTSSAQSDIKDLTEKMSETSVSAQASSVAKNKYFREVKDTPPVVKKGETGVPIEVTCNYIYLNFKENIVFEYEVKFEPDQDYKHLRFKLLNEHIEHFKEKTFDGTTLYVPHELPDAVRNLVSTNPYDQSKVNVSIIFRRTRRLSEMIHIYNVMFKCIMKDLKLIRFGRQHYNEHAAIQIPQHKLEVWPGYVTAVDEYEGGLMLTLDSTHRVLRTQTVLSLIKEVVQTEGANWKRKMTDILIGASVMTTYNKKLFRVDTIDDKMSPRSTFEKTEKGETVQISFIDYYKKNYGIEIMDWDQPLLISRDTKRMPGSDTPTDFMICLIPELCQLTGLTDDQRSNFRLMKDVATYTRITPNQRHAAFKKYIESVMKNETAKSRLAGWGLSIAPETVNLTARTLPPETLYFGDNVRVPGKPNAEWNSEVTKHSVMQAVDIMRWVLLFTQRDKQVAMDFLSTLKRNCRPMGIMVSDAELVPLANDRTDTYVLALKKCITSSVQLVVAICSTKRDDRYAAIKKVCCADNPVPSQVINARTLMNTNKIRSITQKILLQLNCKLGGTLWSISIPFKSAMIVGIDSYHDPSRRNRSVCSFVASYNQSMTLWYSKVIFQEKGQEIVDGLKCCLVDALTHYLRSNGQLPDRIIIYRDGVGDGQLKLLQQYEIPQMKICFTILGSNYQPTLTYVVVQKRINTRIFLKSRDGYDNPNPGTVVDHCITRRDWYDFLIVSQKVTQGTVTPTHYVVVYDDSGITPDQCQRLTYKMCHLYYNWPGTVRVPAPCQYAHKLSYLVGQCVHAQPSDVLVDKLFFL | 3.1.26.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A8D8P8}; | cell differentiation [GO:0030154]; meiotic cell cycle [GO:0051321]; regulatory ncRNA-mediated gene silencing [GO:0031047]; spermatogenesis [GO:0007283] | P granule [GO:0043186] | metal ion binding [GO:0046872]; piRNA binding [GO:0034584]; RNA endonuclease activity [GO:0004521] | PF02170;PF02171; | 3.40.50.2300;2.170.260.10;3.30.420.10; | Argonaute family, Piwi subfamily | PTM: Arginine methylation is required for the interaction with Tudor domain-containing protein Papi/TDRKH. {ECO:0000269|PubMed:23970546}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25558067}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. {ECO:0000269|PubMed:25558067}. | null | null | null | null | null | FUNCTION: Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity (PubMed:19460866). Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiation and in self-renewal of spermatogonial stem cells (PubMed:19460866, PubMed:25558067). Its presence in oocytes suggests that it may participate in similar functions during oogenesis in females (PubMed:18191035). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons (PubMed:19460866, PubMed:25558067). Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements (PubMed:19460866, PubMed:25558067). Strongly prefers a have adenine at position 10 of their guide (g10A preference) (PubMed:24757166, PubMed:25558067). Plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle: antisense piRNA-bound Siwi and sense piRNA-bound Ago3 reciprocally cleave complementary transcripts, to couple the amplification of piRNAs with the repression of transposable elements (PubMed:25558067). {ECO:0000269|PubMed:18191035, ECO:0000269|PubMed:19460866, ECO:0000269|PubMed:24757166, ECO:0000269|PubMed:25558067}. | Bombyx mori (Silk moth) |
B0B9A0 | CDUB1_CHLT2 | MLSPTNSTSKTAPVPPRDSSKPVLISEEPRNQLLQKVARTALAVLLVVVTLGLILLFYSFSDLQSFPWCCQTHPSTKEQPTISIPVPLPSPPLAVPRPSTPPPPVISRPSTPSAPKPSTPPPLLPKAPKPVKTQEDLLPLVPEQVFVEMYEDMARRQTIEALVPAWDSDIIFKCLCYFHTLYPGLIPLETFPPATIFNFKQKIISILEDKKAVLRGEPIKGPLPICCSKENYRRHLQRTTLLPVFMWYHPTPKTLSDTMQTMKQLAIKGSVGASHWLLVIVDIQARRLVYFDSLYNYVMPPENMKKELQSFAQQLDQVYPAYDSKKFSVKIAAKEVIQRGSGSSCGAWCCQFLHWYLKDPLTDALNDLPVDSVERHENLASFVQACEAAVQDLPELSWPEA | 3.4.22.- | null | protein deneddylation [GO:0000338]; protein desumoylation [GO:0016926]; protein deubiquitination [GO:0016579]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; host cell [GO:0043657]; membrane [GO:0016020] | cysteine-type deubiquitinase activity [GO:0004843]; deNEDDylase activity [GO:0019784]; deSUMOylase activity [GO:0016929] | PF02902; | null | Peptidase C48 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18503636}. Host cell {ECO:0000269|PubMed:18503636}. Membrane {ECO:0000269|PubMed:18503636}; Single-pass membrane protein {ECO:0000269|PubMed:18503636}. Note=Secreted, and delivered into the host cell. Located predominantly on the plasma membrane and to a lesser extent on intracellular membranes, especially the host cell nuclear envelope. | null | null | null | null | null | FUNCTION: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protease possesses deubiquitinating and deneddylating activities (By similarity). Impairs ubiquitination and degradation of NF-kappa-B inhibitor alpha (NFKBIA), thereby preventing NF-kappa-B activation. {ECO:0000250, ECO:0000269|PubMed:18503636}. | Chlamydia trachomatis serovar L2 (strain ATCC VR-902B / DSM 19102 / 434/Bu) |
B0BF33 | PKP2_DANRE | MLKPHPEHKEQPQDSFTPSGDSTPDASMAEERDFMRSVLPVYDSFHPEDSSLALPLANKLTLADAHRLNRLQQQVQLTLSRKKRKPKPADSSLAESQSSCQISSSSSLGSLHLKRTFSVNHEATRSLRMVDRSQWPSMEPPLFHRGYGSFRYTPKRAGLCLGSNSLTLPSAPTTSHFQMNKLPLRYAHSEVLRNPRFAGLSAATQIPSSPVYENPHTDDTDDVFLPSTSVERGRMESEKHTLQQTLCKQREGGFVALEQSENVSWQSRVRKPSLEFVAGRRPSQTGSLISMEEQSGSLGRIEKLEVKQHAVTTLTKKGKPGELSAEMTLKEAVNLLTQDNNMETQIAAANFIQNQCFNSPDAKRKILHLQGIPKLLKLMQNDSEELQWAAVSSLRNIVFENNENKMEVKDCEGLPVILRLLKINRDIETRRQLTGLLWNLSSHDLLKEHLSREAVKPLTDSVLVPCSGISEGEDPKLELLADPDIFYNATGCLRNLSSAGPDGRKVMRDCEGLIECVIYYIRGTIADYKPDDKATENCVCILHNLSYRFDCEVPRVDSPVAQKPKQTHTETSNPGCFIIKTPKNSAENLEADEDYPALEENGSPHGVEWLWSAITVRMYLSLIAVSTNQHTKQASIGTLQNLTACSGEISQAIAHFIVQKEGGLSQVKKLLQEAEKEELRISVSLLKNISRYRELHADIVKQVLPELVAILPNSDRNVEQPIEITVTICHILINLSQASASNTCAIINQGALPKIISISSKDNGFGPTRAGQAACVLLHTLWRHSELHSSFKKAGYRKTDFINNRTVKAVNSARE | null | null | cell-cell adhesion [GO:0098609]; cell-cell junction assembly [GO:0007043]; cell-cell signaling involved in cardiac conduction [GO:0086019]; desmosome organization [GO:0002934]; heart development [GO:0007507]; heart looping [GO:0001947]; intermediate filament bundle assembly [GO:0045110]; protein localization to plasma membrane [GO:0072659] | adherens junction [GO:0005912]; cytoplasm [GO:0005737]; desmosome [GO:0030057]; intercalated disc [GO:0014704]; intermediate filament [GO:0005882]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | alpha-catenin binding [GO:0045294]; cadherin binding [GO:0045296]; intermediate filament binding [GO:0019215]; molecular adaptor activity [GO:0060090]; protein kinase C binding [GO:0005080] | PF00514; | 1.25.10.10; | Beta-catenin family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99959}. Cell junction, desmosome {ECO:0000250|UniProtKB:Q99959}. Cell junction {ECO:0000250|UniProtKB:Q99959}. Cytoplasm {ECO:0000250|UniProtKB:Q99959}. | null | null | null | null | null | FUNCTION: Required for development of the heart, potentially via cell-cell adhesion and modulation of expression of cardiac precursor genes (PubMed:23124967). Plays a role in desmosome cell-cell junctions and their intracellular connectivity (PubMed:23124967). {ECO:0000269|PubMed:23124967}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B0BK71 | MSP1_MYCSO | MKLFSASVFAAIIASHYASATAHIRAPNVKPRRTNSLLTAPPQQPPLPSAQQAASASSSAGLNLTDIQGDILIGMKKNKELFFFFSITDAATFKAKLGSDILELITSTNQLLAVATQPITAVNVAFSSTGLKALGITDDLKDPVFEAGMLSNAVSDLSDPGTGNWVPGFVGTSVHGVFLLASDTIDNVNTELANIQTILNGSITEIHRLQGEARPGDQQGHEHFGFMDGISNPAVDGFTPPAEIRPGQALIPPGIMLLGEANDTFQNDRPPWAKDGSFLVFRQMQQRAPEFNKFLQDHALNMPNMTSEQGADLLGARIVGRWKSDAPIDLTPLVDDPVLAADNQRNNNFDFSDATNQTRCPFSAHIRKANPRGDLGGINKFPNQHIIRAGIPYGPEVTDAEKASNSSSTDPSLERGLAFVAYQSNIQNGFVFLQKNWVDNTNFFRPGTGVDPLIGTNSRNSGTDAPNTPRVVSGLDPNNATSTIEIGIDFVVSRGGEYFFSPSLSAIRTVLSV | 1.11.1.19; 1.11.1.7 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P31545, ECO:0000269|PubMed:18038130}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently per monomer. {ECO:0000250|UniProtKB:P31545, ECO:0000269|PubMed:18038130}; | carotene catabolic process [GO:0016121] | cytosol [GO:0005829]; extracellular region [GO:0005576] | heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF21105;PF20628; | null | DyP-type peroxidase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18038130}. | CATALYTIC ACTIVITY: Reaction=2 H2O2 + Reactive Blue 5 = 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H(+) + 2 H2O + phthalate; Xref=Rhea:RHEA:28086, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:17563, ChEBI:CHEBI:63950, ChEBI:CHEBI:63955, ChEBI:CHEBI:64278; EC=1.11.1.19; Evidence={ECO:0000269|PubMed:23111597}; CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; Evidence={ECO:0000269|PubMed:23111597}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 uM for H(2)O(2) {ECO:0000269|PubMed:23111597}; | null | null | null | FUNCTION: Manganese-independent peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known (PubMed:23111597). In addition to classic peroxidase substrates (e.g. 2,6-dimethoxyphenol), oxidizes dyes such as Reactive Blue 5 (PubMed:23111597). Also degrades beta-carotene (PubMed:18038130). {ECO:0000269|PubMed:18038130, ECO:0000269|PubMed:23111597}. | Mycetinis scorodonius (Garlic mushroom) (Marasmius scorodonius) |
B0BK72 | MSP2_MYCSO | MRLTYLPLFAGIAIQSASALPDFFKSSVLKPRRTNSLLINPDAQPDLPTAQQASTAAASVGLNLTDIQGDILIGMKKNKEMFFFFSIADATAFKSHLDSAILPLITSTQQLLTVATQPTTAVNLAFSQTGLNALGLASQGLGDSLFASGQFSGAESLGDPGTSNWVQAFAGTGIHGVFLLASDTIDNVNAELSQIQSILGTSITEAYRLQGEARPDDQQGHEHFGFMDGISNPAIDGFSTALPGQAVLSPGLFLLAEDGDGSSSSRPSWAKDGSLLAFRQLQQRVPEFNKFLADNAALTQGNADLLGARMMGRWKSGAPVDLAPTADDVDLANDPQRNNNFNFTHPDFTETTDQTHCPFSAHIRKTNPRSDFNPLNTANHIIRAGIPYGPEVTDAEASSNTSSTDASLERGLAFVAYQSNIGNGFAFIQQNWVDNANFFFGKTTPPGIDPIIGSNAAQNNFAPNSPRPVSGLDPTDSTTIVTLNTDFVVSRGGEYFFSPSLSAIQNTLSV | 1.11.1.- | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255, ECO:0000269|PubMed:18038130}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently per monomer. {ECO:0000255, ECO:0000269|PubMed:18038130}; | carotene catabolic process [GO:0016121] | cytosol [GO:0005829] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF21105;PF20628; | null | DyP-type peroxidase family | null | null | null | null | null | null | null | FUNCTION: Peroxidase capable of degrading beta-carotene. {ECO:0000269|PubMed:18038130}. | Mycetinis scorodonius (Garlic mushroom) (Marasmius scorodonius) |
B0BLU1 | RN168_XENTR | MAKVQKLPLPWSECICPICQEILLEPVTLPCKHTLCNPCFQMTVEKASLCCPFCRKRVSTWARQHSRTRTLVNKELWEVIQKQYPKQCQRRASGQESDDLSDELTSCPVPVLCKPGEIRQEYEAEVSKIEAERTAQEEAERKASEDYIQKLLAEEEAEENLHAEASQREIEEQLKRDEELARLLSGDMDLSNASCTSVSPVTSKKVVSKSSKIVKSKQRVSGDIERFLSPKPRRALAAFGINESRNSDTSGSCILLDEDEDEIPDLSPQCPSTSLIQERDVELPMPYLPNCYKLESDAASQQDSCSERNDICNGTYSCSDSIDVEVSKTMEQQRATADSQEYRMETNAMSYSTPKRKCEECYLDIEEKAGSCQSVKKKKLSLSEDSPVLSVHAGKFIELEENLYERRKQEEHDRLFALQLQRELDKELKQVNRGKGSPDEYQLRPKRGLKLQECNDSPLPHNEQTPVQDKGGNTQSGYSPDENKKPSRKKSITSSQVRQSRAVTNTERSSEGMNVLKPSNKQPTILDLFQRSAGK | 2.3.2.27 | null | DNA damage response [GO:0006974]; DNA repair-dependent chromatin remodeling [GO:0140861]; double-strand break repair [GO:0006302]; isotype switching [GO:0045190]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; positive regulation of DNA repair [GO:0045739]; protein K63-linked ubiquitination [GO:0070534]; protein ubiquitination [GO:0016567]; response to ionizing radiation [GO:0010212]; ubiquitin-dependent protein catabolic process [GO:0006511] | nucleus [GO:0005634]; site of double-strand break [GO:0035861]; ubiquitin ligase complex [GO:0000151] | chromatin binding [GO:0003682]; histone binding [GO:0042393]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872]; nucleosome binding [GO:0031491]; ubiquitin binding [GO:0043130]; ubiquitin-protein transferase activity [GO:0004842] | PF00097; | 3.30.40.10; | RNF168 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03066}. Note=Localizes to double-strand breaks (DSBs) sites of DNA damage. {ECO:0000255|HAMAP-Rule:MF_03066}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000255|HAMAP-Rule:MF_03066}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|HAMAP-Rule:MF_03066}. | null | null | FUNCTION: E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with ube2n/ubc13 to amplify the rnf8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and ubiquitinates histone H2A and H2AX, leading to amplify the rnf8-dependent H2A ubiquitination and promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of tp53bp1 and brca1. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively). {ECO:0000255|HAMAP-Rule:MF_03066}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B0BLW3 | LGR4_XENTR | MGCPGWPLALFALLLASCSGGPSGVSSPAPCPAPCACDLDGGADCSGKGLVTVPDGLSVFTHSLDLSMNNITKLPEGAFKGFPYLEELRLAGNDLSIIHPMALSGLKELKVLTLQNNQLKTVPSESLKGLVSLQSLRLDANHIVTVPEDSFEGLVQLRHLWLDDNSLTEVPIRPLSNLPSLQALTLALNKISHIPDYAFSNLSSLVVLHLHNNKIRTLGPHCFHGLDNLEALDLNYNNLIDFPDSIRSLPNLKELGFHSNSITIIPDGAFVKNPLLRTIHLYDNPLSFVGNSAFQNLSDLHFLIIRGASNVQWFPNLTGTNNLESLTLTGTKIRSIPIKFCQEQKMLRTLDLSYNEISALVGFEGCSSLEEVYLQNNQIQEVQNETFQGLAALRMLDLSRNRIHTIHKEAFVTLKALTNLDLSFNDLTAFPTAGLHGLNQLKLTGNPNFKETLTAKDLIKLSSVSVPYAYQCCAFSACNSYMTTTVEEDRLRAQRLLLDHDRAAMDPDYMGTEDDKEHVQALIQCNPATGPFKPCEYLLGSWMIRLTVWFIFLLALIFNVIVIVTMFASCSQLTSSKLFIGLIAVSNLFMGVYTGTLTVLDTISWGQFAEFGIWWETGNGCKVAGFLAIFSSESAIFFLMLAAIERSLSAKDIIKKEKHQHLRKFQVASLLAVLLAAAAGCLPLFHIGEFSSSPLCLPFPTGETPSLGFTVTLVLLNSLAFLIMVITYTKLYCTIEKEDLSENAESSMIKHVAWLIFTNCIFFCPVAFFSFAPLITAIYISPEIMKSVTLIFLPLPACLNPVLYVFFNPKFKEDWKLLRWRLTKRSGSVAVATNSQRGCVTQDFYYDFGMYSHLQGGNFAVCDYCESVLLKNPPPCKHLIKSHSCPTLAVVPCQRPDNYWSEFGTQSAHSDCADEEDSFVSDSSDQVQVCGRACFYQSRGLPLVRYAYNIPRMKD | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; bone mineralization [GO:0030282]; bone remodeling [GO:0046849]; hormone-mediated signaling pathway [GO:0009755]; negative regulation of cytokine production [GO:0001818]; negative regulation of toll-like receptor signaling pathway [GO:0034122]; osteoblast differentiation [GO:0001649]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; rhythmic process [GO:0048511]; spermatogenesis [GO:0007283]; Wnt signaling pathway [GO:0016055] | plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; protein-hormone receptor activity [GO:0016500]; transmembrane signaling receptor activity [GO:0004888] | PF00001;PF13855; | 1.20.1070.10;3.80.10.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BXB1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BXB1}. | null | null | null | null | null | FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Its function as activator of the Wnt signaling pathway is required for the development of various organs, including liver, kidney, intestine, bone, reproductive tract and eye. May play a role in regulating the circadian rhythms of plasma lipids (By similarity). Required for proper development of GnRH neurons (gonadotropin-releasing hormone expressing neurons) that control the release of reproductive hormones from the pituitary gland (By similarity). {ECO:0000250|UniProtKB:A2ARI4, ECO:0000250|UniProtKB:E7FE13, ECO:0000269|PubMed:21909076}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B0BMY1 | LAAT1_RAT | MVWRTLVASNFSTCPNGSIQWIWDVFGECAQDGWDEASVALGLVSIFCFAASTFPQYIKACKTGNMDQALSLWFLLGWIGGDSCNLIGSFLADQLPLQTYTAVYYVLADLLMLTLYFHYKFKKQPSLLSAPINSVLLFILGTVCITPLLSSTDPVAVPREGFRGRTLLSVEPGNKPFTKKEVVGFVIGSASSVLYLLSRLPQIRTNFVRQSTQGISYSLFALVMLGNTLYGLSVLLKNPEVGQSEGSYLLHHLPWLVGSLGVLLLDTIISIQFLVYRSHDADAASEREPLLPS | null | null | intracellular amino acid homeostasis [GO:0080144]; L-arginine transmembrane transport [GO:1903826]; lysine transport [GO:0015819] | lysosomal membrane [GO:0005765]; organelle membrane [GO:0031090] | basic amino acid transmembrane transporter activity [GO:0015174]; L-arginine transmembrane transporter activity [GO:0061459]; L-lysine transmembrane transporter activity [GO:0015189] | PF04193; | 1.20.1280.290; | Laat-1 family | null | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:23169667}; Multi-pass membrane protein {ECO:0000269|PubMed:23169667}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.36 mM for arginine {ECO:0000269|PubMed:23169667}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is acidic with no activity detected at a pH higher that 7.0. {ECO:0000269|PubMed:23169667}; | null | FUNCTION: Amino acid transporter that specifically mediates the pH-dependent export of the cationic amino acids arginine, histidine and lysine from lysosomes. {ECO:0000269|PubMed:23169667}. | Rattus norvegicus (Rat) |
B0BND0 | ENPP6_RAT | MAGKLWTFLLLFGFSWVWPASAHRKLLVLLLDGFRSDYISEDALASLPGFREIVNRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPRTNKSFDIGVNRDSLMPLWWNGSEPLWITLMKARRKVYMYYWPGCEVEILGVRPTYCLEYKNVPTDINFANAVSDALDSLKSGRADLAAIYHERIDVEGHHYGPSSPQRKDALKAVDTVLKYMTQWIQERGLQNDLNVILFSDHGMTDIFWMDKVIELSKYISLDDLQQVKDQGPVVSLWPVPEKHSEIYHKLRTVEHMTVYEKEAIPNRFYYKKGKFVSPLTLVADEGWFIAESREALPFWMNSTGKREGWQHGWHGYDNELMDMRGIFLAFGPDFKSNFRAAPIRSVDVYNIMCNVVGITPLPNNGSWSRVVCMLKSQTSSSPSIPPNSCALVLILLLYFV | 3.1.4.-; 3.1.4.38 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q8BGN3}; | choline metabolic process [GO:0019695]; lipid catabolic process [GO:0016042]; lipid metabolic process [GO:0006629] | extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | glycerophosphocholine cholinephosphodiesterase activity [GO:0047390]; glycerophosphodiester phosphodiesterase activity [GO:0008889]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081] | PF01663; | 3.30.1360.180;3.40.720.10; | Nucleotide pyrophosphatase/phosphodiesterase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=H2O + sn-glycerol 3-phosphocholine = glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:19545, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:17754, ChEBI:CHEBI:295975; EC=3.1.4.38; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19546; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:44720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58168, ChEBI:CHEBI:64683, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44721; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=1-O-alkyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:36083, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15850, ChEBI:CHEBI:30909, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36084; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=1-dodecanoyl-sn-glycero-3-phosphocholine + H2O = 1-dodecanoyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41127, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74966, ChEBI:CHEBI:75529, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41128; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:75542, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41120; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41003, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:34071, ChEBI:CHEBI:74344, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41004; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=1-tetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-tetradecanoyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:40999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64489, ChEBI:CHEBI:75536, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41000; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=H2O + sphing-4-enine-phosphocholine = H(+) + phosphocholine + sphing-4-enine; Xref=Rhea:RHEA:41095, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57756, ChEBI:CHEBI:58906, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41096; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41091, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:75757, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41092; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine + H2O = 1-(9Z,12Z-octadecadienoyl)-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28733, ChEBI:CHEBI:75561, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41116; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; CATALYTIC ACTIVITY: Reaction=glycero-2-phosphocholine + H2O = glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:61684, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:144950, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61685; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; | null | null | null | null | FUNCTION: Choline-specific glycerophosphodiesterase that hydrolyzes glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and contributes to supplying choline to the cells. Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty acids. In vitro, hydrolyzes only choline-containing lysophospholipids, such as sphingosylphosphorylcholine (SPC), platelet-activating factor (PAF) and lysoPAF, but not other lysophospholipids. {ECO:0000250|UniProtKB:Q8BGN3}. | Rattus norvegicus (Rat) |
B0BNF1 | SEPT8_RAT | MAATDLERISNAEPEPRSLSLGGHVGFDSLPDQLVSKSVTQGFSFNILCVGETGIGKSTLMNTFFNTTFETEEASHHEECVRLRPQTYDLQESNVHLKLTIVDAVGFGDQINKDDSYRPIVDYIDTQFENYLQEELKIRRSLFDYHDTRIHVCLYFITPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTISKSELHKFKIKIMGELVSNGVQIYQFPTDDEAVAEINAVMNAHLPFAVVGSTEEVKVGNKLVRARQYPWGVVQVENENHCDFVKLREMLIRVNMEDLREQTHSRHYELYRRCKLEEMGFQDSDGDSQPFSLQETYEAKRKEFLSELQRKEEEMRQMFVNKVKETELELKEKERELHEKFEHLKRIHQEEKRKVEEKRRELEEETNAFNCRKAAMEALQSQALHATSQQPLRKDKDKKKVGGWSSIYSVTIP | null | null | cytoskeleton-dependent cytokinesis [GO:0061640]; regulation of intracellular protein transport [GO:0033157]; regulation of protein stability [GO:0031647]; regulation of SNARE complex assembly [GO:0035542] | axon [GO:0030424]; cell division site [GO:0032153]; microtubule cytoskeleton [GO:0015630]; myelin sheath [GO:0043209]; presynapse [GO:0098793]; septin complex [GO:0031105]; septin ring [GO:0005940]; synaptic vesicle membrane [GO:0030672] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; molecular adaptor activity [GO:0060090]; SNARE binding [GO:0000149] | PF00735; | 3.40.50.300; | TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19196426}. Cytoplasm, cytoskeleton {ECO:0000250}. Synapse {ECO:0000269|PubMed:19196426}. Cell projection, axon {ECO:0000269|PubMed:19196426}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000305|PubMed:19196426}. Presynapse {ECO:0000269|PubMed:19196426}. Note=Expressed in axons of immature neurons, localizes to synapses in mature neurons. {ECO:0000269|PubMed:19196426}. | null | null | null | null | null | FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in platelet secretion (By similarity). Seems to participate in the process of SNARE complex formation in synaptic vesicles (PubMed:19196426). {ECO:0000250|UniProtKB:Q92599, ECO:0000269|PubMed:19196426}. | Rattus norvegicus (Rat) |
B0BNF9 | HAOX1_RAT | MLPRLVCISDYEQHARTVLQKSVYDYYKSGANDQETLADNIRAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALRWMQLYIYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPPQLRMKNFETNDLAFSPKGNFGDNSGLAEYVAQAIDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKNPLAVSKI | 1.1.3.15; 1.2.3.5 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q9UJM8}; | fatty acid alpha-oxidation [GO:0001561]; glycine biosynthetic process [GO:0006545]; glycolate catabolic process [GO:0046296]; response to oxidative stress [GO:0006979] | peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | (S)-2-hydroxy-acid oxidase activity [GO:0003973]; FMN binding [GO:0010181]; glyoxylate oxidase activity [GO:0047969] | PF01070; | 3.20.20.70; | FMN-dependent alpha-hydroxy acid dehydrogenase family | null | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000305|PubMed:10777549}. | CATALYTIC ACTIVITY: Reaction=a (2S)-2-hydroxycarboxylate + O2 = a 2-oxocarboxylate + H2O2; Xref=Rhea:RHEA:16789, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:35179, ChEBI:CHEBI:58123; EC=1.1.3.15; Evidence={ECO:0000250|UniProtKB:Q9UJM8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16790; Evidence={ECO:0000250|UniProtKB:Q9UJM8}; CATALYTIC ACTIVITY: Reaction=glycolate + O2 = glyoxylate + H2O2; Xref=Rhea:RHEA:25311, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29805, ChEBI:CHEBI:36655; EC=1.1.3.15; Evidence={ECO:0000250|UniProtKB:Q9UJM8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312; Evidence={ECO:0000250|UniProtKB:Q9UJM8}; CATALYTIC ACTIVITY: Reaction=glyoxylate + H2O + O2 = H(+) + H2O2 + oxalate; Xref=Rhea:RHEA:14837, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:30623, ChEBI:CHEBI:36655; EC=1.2.3.5; Evidence={ECO:0000250|UniProtKB:Q9UJM8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14838; Evidence={ECO:0000250|UniProtKB:Q9UJM8}; CATALYTIC ACTIVITY: Reaction=2-hydroxyhexadecanoate + O2 = 2-oxohexadecanoate + H2O2; Xref=Rhea:RHEA:67944, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:65097, ChEBI:CHEBI:176593; Evidence={ECO:0000250|UniProtKB:Q9UJM8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67945; Evidence={ECO:0000250|UniProtKB:Q9UJM8}; CATALYTIC ACTIVITY: Reaction=2-hydroxyoctanoate + O2 = 2-oxooctanoate + H2O2; Xref=Rhea:RHEA:67940, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:133514, ChEBI:CHEBI:176689; Evidence={ECO:0000250|UniProtKB:Q9UJM8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67941; Evidence={ECO:0000250|UniProtKB:Q9UJM8}; | null | PATHWAY: Amino-acid biosynthesis; glycine biosynthesis. {ECO:0000250|UniProtKB:Q9UJM8}. | null | null | FUNCTION: Broad substrate specificity (S)-2-hydroxy-acid oxidase that preferentially oxidizes glycolate. The glyoxylate produced by the oxidation of glycolate can then be utilized by alanine-glyoxylate aminotransferase for the peroxisomal synthesis of glycine; this pathway appears to be an important step for the detoxification of glyoxylate which, if allowed to accumulate, may be metabolized to oxalate with formation of kidney stones. Can also catalyze the oxidation of glyoxylate, and long chain hydroxyacids such as 2-hydroxyhexadecanoate and 2-hydroxyoctanoate. Active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCIP), but O2 is believed to be the physiological electron acceptor, leading to the production of H2O2. {ECO:0000250|UniProtKB:Q9UJM8}. | Rattus norvegicus (Rat) |
B0BNK7 | LRFN3_RAT | MAVLPLLLCLLPLAPASSPPQPATSSPCPRRCRCQTQSLPLSVLCPGAGLLFVPPSLDRRAAELRLADNFIAAVRRRDLANMTGLLHLSLSRNTIRHVAAGAFADLRALRALHLDGNRLTSLGEGQLRGLVNLRHLILSNNQLAALAAGALDDCAETLEDLDLSYNNLEQLPWEALGRLGNVNTLGLDHNLLASVPAGAFSRLHKLARLDMTSNRLTTIPPDPLFSRLPLLARPRGSPASALVLAFGGNPLHCNCELVWLRRLAREDDLEACASPPALGGRYFWAVGEEEFVCEPPVVTHRSPPLAVPAGRPAALRCRAVGDPEPRVRWVSPQGRLLGNSSRARAFPNGTLELLVTEPEDGGTFTCIAANAAGEATAAVELTVGPPPPPQLANSTSCDPPRDGEPDALTPPSAASASAKVADTVAPTDRGVQVTEHGATAALVQWPDQRPVPGIRMYQIQYNSSADDILVYRMIPADSRSFLLTDLASGRTYDLCVLAVYEDSATGLTATRPVGCARFSTEPALRPCAAPHAPFLGGTMIIALGGVIVASVLVFIFVLLLRYKVHGVQPPGKAKATAPVSSVCSQTNGALGPVPSAPAPEPAAPRAHTVVQLDCEPWGPSHEPAGP | null | null | regulation of presynapse assembly [GO:1905606]; regulation of synaptic membrane adhesion [GO:0099179]; synaptic membrane adhesion [GO:0099560] | axon [GO:0030424]; cell surface [GO:0009986]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; postsynaptic density membrane [GO:0098839]; postsynaptic specialization membrane [GO:0099634]; presynaptic active zone membrane [GO:0048787] | null | PF00041;PF07679;PF13855; | 2.60.40.10;3.80.10.10; | LRFN family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BLY3}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18227064}; Single-pass type I membrane protein {ECO:0000269|PubMed:18227064}. Cell projection, axon {ECO:0000269|PubMed:18227064}. Cell projection, dendrite {ECO:0000269|PubMed:18227064}. Synapse {ECO:0000269|PubMed:18227064}. Presynaptic cell membrane {ECO:0000269|PubMed:18227064}. Postsynaptic cell membrane {ECO:0000269|PubMed:18227064}. Note=Detected also in intracellular vesicular and tubovesicular structures and in membranes of cell soma. On overexpression, detected throughout hippocampal neurons in soma, axons, dendrites and growth cones. {ECO:0000255, ECO:0000269|PubMed:18227064}. | null | null | null | null | null | FUNCTION: Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
B0BNM1 | NNRE_RAT | MSGLRTLLGLGLLVAGSRLPRIASRQSVCRAGPIWWGTQHRSSETMASAAVKYLSQEEAQAVDEELFNEYQFSVDQLMELAGLSCATAIAKAYPPTSMSKSPPTVLVICGPGNNGGDGLVCARHLKLFGYQPTIYYPKRPNKPLFTGLVTQCQKMDIPFLGEMPPEPMMVDELYELVVDAIFGFSFKGDVREPFHSILSVLSGLTVPIASIDIPSGWDVEKGNPSGIQPDLLISLTAPKKSATQFTGRYHYLGGRFVPPALEKKYQLNLPAYPDTECVYRLQ | 5.1.99.6 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_03159}; Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03159}; | lipid transport [GO:0006869]; membrane raft distribution [GO:0031580]; negative regulation of angiogenesis [GO:0016525]; nicotinamide nucleotide metabolic process [GO:0046496]; regulation of cholesterol efflux [GO:0010874]; sprouting angiogenesis [GO:0002040] | cell body [GO:0044297]; cilium [GO:0005929]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; mitochondrion [GO:0005739] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; NADHX epimerase activity [GO:0052856]; NADPHX epimerase activity [GO:0052857]; nucleotide binding [GO:0000166] | PF03853; | 3.40.50.10260; | NnrE/AIBP family | PTM: Undergoes physiological phosphorylation during sperm capacitation, downstream to PKA activation. {ECO:0000255|HAMAP-Rule:MF_03159}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03159}. Secreted {ECO:0000255|HAMAP-Rule:MF_03159}. Note=In sperm, secretion gradually increases during capacitation. {ECO:0000255|HAMAP-Rule:MF_03159}. | CATALYTIC ACTIVITY: Reaction=(6R)-NADHX = (6S)-NADHX; Xref=Rhea:RHEA:32215, ChEBI:CHEBI:64074, ChEBI:CHEBI:64075; EC=5.1.99.6; Evidence={ECO:0000250|UniProtKB:Q8NCW5}; CATALYTIC ACTIVITY: Reaction=(6R)-NADPHX = (6S)-NADPHX; Xref=Rhea:RHEA:32227, ChEBI:CHEBI:64076, ChEBI:CHEBI:64077; EC=5.1.99.6; Evidence={ECO:0000250|UniProtKB:Q8NCW5}; | null | null | null | null | FUNCTION: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. Accelerates cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis (By similarity). {ECO:0000250|UniProtKB:Q8NCW5, ECO:0000255|HAMAP-Rule:MF_03159}. | Rattus norvegicus (Rat) |
B0CM99 | HMGB1_CALJA | MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEDEEEDDDDE | null | null | adaptive immune response [GO:0002250]; autophagy [GO:0006914]; chemotaxis [GO:0006935]; DNA geometric change [GO:0032392]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; positive regulation of response to external stimulus [GO:0032103]; regulation of transcription by RNA polymerase II [GO:0006357] | chromosome [GO:0005694]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endosome [GO:0005768]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | bubble DNA binding [GO:0000405]; DNA binding, bending [GO:0008301]; four-way junction DNA binding [GO:0000400]; non-sequence-specific DNA binding, bending [GO:0044378]; supercoiled DNA binding [GO:0097100] | PF00505;PF09011; | 1.10.30.10; | HMGB family | PTM: Phosphorylated at serine residues. Phosphorylation in both NLS regions is required for cytoplasmic translocation followed by secretion. {ECO:0000250|UniProtKB:P09429}.; PTM: Acetylated on multiple sites upon stimulation with LPS (By similarity). Acetylation on lysine residues in the nuclear localization signals (NLS 1 and NLS 2) leads to cytoplasmic localization and subsequent secretion. Acetylation on Lys-3 results in preferential binding to DNA ends and impairs DNA bending activity (By similarity). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}.; PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-106 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB1 (HMGB1C23hC45hC106h), 2- disulfide HMGB1 (HMGB1C23-C45C106h) and 3- sulfonyl HMGB1 (HMGB1C23soC45soC106so). {ECO:0000250|UniProtKB:P09429}.; PTM: Poly-ADP-ribosylated by PARP1 when secreted following stimulation with LPS. {ECO:0000250|UniProtKB:P63158}.; PTM: In vitro cleavage by CASP1 is liberating a HMG box 1-containing peptide which may mediate immunogenic activity; the peptide antagonizes apoptosis-induced immune tolerance. Can be proteolytically cleaved by a thrombin:thrombomodulin complex; reduces binding to heparin and pro-inflammatory activities (By similarity). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103}.; PTM: Forms covalent cross-links mediated by transglutaminase TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers. {ECO:0000250|UniProtKB:P09429}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09429}. Chromosome {ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}. Cytoplasm {ECO:0000250|UniProtKB:P09429}. Secreted {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}. Cell membrane {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}; Peripheral membrane protein {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}; Extracellular side {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}. Endosome {ECO:0000250|UniProtKB:P63158}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P63158}. Note=In basal state predominantly nuclear. Shuttles between the cytoplasm and the nucleus. Translocates from the nucleus to the cytoplasm upon autophagy stimulation. Release from macrophages in the extracellular milieu requires the activation of NLRC4 or NLRP3 inflammasomes (By similarity). Passively released to the extracellular milieu from necrotic cells by diffusion, involving the fully reduced HGMB1 which subsequently gets oxidized. Also released from apoptotic cells. Active secretion from a variety of immune and non-immune cells such as macrophages, monocytes, neutrophils, dendritic cells, natural killer cells and plasma cells in response to various stimuli such as LPS and cytokines involves a nonconventional secretory process via secretory lysosomes. Found on the surface of activated platelets. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}. | null | null | null | null | null | FUNCTION: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as a sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as a danger-associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. Has proangiogenic activity. May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}.; FUNCTION: Nuclear functions are attributed to fully reduced HGMB1. Associates with chromatin and binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA, DNA-containing cruciforms or bent structures, supercoiled DNA and ZDNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity. May be involved in nucleotide excision repair (NER), mismatch repair (MMR) and base excision repair (BER) pathways, and double strand break repair such as non-homologous end joining (NHEJ). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). In vitro can displace histone H1 from highly bent DNA. Can restructure the canonical nucleosome leading to relaxation of structural constraints for transcription factor-binding. Enhances binding of sterol regulatory element-binding proteins (SREBPs) such as SREBF1 to their cognate DNA sequences and increases their transcriptional activities. Facilitates binding of TP53 to DNA. May be involved in mitochondrial quality control and autophagy in a transcription-dependent fashion implicating HSPB1. Can modulate the activity of the telomerase complex and may be involved in telomere maintenance. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}.; FUNCTION: In the cytoplasm proposed to dissociate the BECN1:BCL2 complex via competitive interaction with BECN1 leading to autophagy activation. Can protect BECN1 and ATG5 from calpain-mediated cleavage and thus proposed to control their proautophagic and proapoptotic functions and to regulate the extent and severity of inflammation-associated cellular injury. In myeloid cells has a protective role against endotoxemia and bacterial infection by promoting autophagy. Involved in endosomal translocation and activation of TLR9 in response to CpG-DNA in macrophages. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}.; FUNCTION: In the extracellular compartment (following either active secretion or passive release) involved in regulation of the inflammatory response. Fully reduced HGMB1 (which subsequently gets oxidized after release) in association with CXCL12 mediates the recruitment of inflammatory cells during the initial phase of tissue injury; the CXCL12:HMGB1 complex triggers CXCR4 homodimerization. Induces the migration of monocyte-derived immature dendritic cells and seems to regulate adhesive and migratory functions of neutrophils implicating AGER/RAGE and ITGAM. Can bind to various types of DNA and RNA including microbial unmethylated CpG-DNA to enhance the innate immune response to nucleic acids. Proposed to act in promiscuous DNA/RNA sensing which cooperates with subsequent discriminative sensing by specific pattern recognition receptors. Promotes extracellular DNA-induced AIM2 inflammasome activation implicating AGER/RAGE. Disulfide HMGB1 binds to transmembrane receptors, such as AGER/RAGE, TLR2, TLR4 and probably TREM1, thus activating their signal transduction pathways. Mediates the release of cytokines/chemokines such as TNF, IL-1, IL-6, IL-8, CCL2, CCL3, CCL4 and CXCL10. Promotes secretion of interferon-gamma by macrophage-stimulated natural killer (NK) cells in concert with other cytokines like IL-2 or IL-12. TLR4 is proposed to be the primary receptor promoting macrophage activation and signaling through TLR4 seems to implicate LY96/MD-2. In bacterial LPS- or LTA-mediated inflammatory responses binds to the endotoxins and transfers them to CD14 for signaling to the respective TLR4:LY96 and TLR2 complexes. Contributes to tumor proliferation by association with ACER/RAGE. Can bind to IL1-beta and signals through the IL1R1:IL1RAP receptor complex. Binding to class A CpG activates cytokine production in plasmacytoid dendritic cells implicating TLR9, MYD88 and AGER/RAGE and can activate autoreactive B cells. Via HMGB1-containing chromatin immune complexes may also promote B cell responses to endogenous TLR9 ligands through a B-cell receptor (BCR)-dependent and ACER/RAGE-independent mechanism. Inhibits phagocytosis of apoptotic cells by macrophages; the function is dependent on poly-ADP-ribosylation and involves binding to phosphatidylserine on the cell surface of apoptotic cells. In adaptive immunity may be involved in enhancing immunity through activation of effector T-cells and suppression of regulatory T (TReg) cells. In contrast, without implicating effector or regulatory T-cells, required for tumor infiltration and activation of T-cells expressing the lymphotoxin LTA:LTB heterotrimer thus promoting tumor malignant progression. Also reported to limit proliferation of T-cells. Released HMGB1:nucleosome complexes formed during apoptosis can signal through TLR2 to induce cytokine production. Involved in induction of immunological tolerance by apoptotic cells; its pro-inflammatory activities when released by apoptotic cells are neutralized by reactive oxygen species (ROS)-dependent oxidation specifically on Cys-106. During macrophage activation by activated lymphocyte-derived self apoptotic DNA (ALD-DNA) promotes recruitment of ALD-DNA to endosomes. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}. | Callithrix jacchus (White-tufted-ear marmoset) |
B0D6H2 | ARO1_LACBS | MANADVLKVSILGKESIHCGFHLIPYIAQTVLSNLPSSTYVLVTDTNVANFHLTAFEKEFEQRISSLPTSSTKPRFLSLVIPPGETSKSREGKANIEDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYIFIDAAFLETLPSREFSNGMAEVVKTAAIWNEAEFISLESRSADIFAAIQTPSADYAGRSKQTRSIAQELLLSVIVGSISVKAHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPTILHGECVSVGMILEGEISRQMGILSQVGVGRLNRCLKAYNLPVTLADPRIASLPAAKLLTVERLLDIMRIDKKNSGPEKKIVILSRIGATYEPKATVVPDSIIAKTLSEAAKVIPGVPRHHPVKMATPGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELKGASFAWEDAGETLVVKGGEGSLSVPPKGKELYLGNAGTAARFLTTVCTLVQSSPQDNAEYTVITGNARMKQRPIGPLVTALQANGSKIDFLESEGCLPLAIAPQGLKGSQLQLAASVSSQYVSSILLCAPYAEEPITLELIGGQVISQPYIDMTVAMMKTFGVDVVRRKDPVTGKFLDVYEIPKAVYTNPPEYNIESDASSATYPLAIAAVTGTSCTIQNIGSASLQGDAKFAKEVLEKMGCQVSQTATETTVQGPPIGQLKAIEEVDMEVMTDAFLTATALAAVANGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIIGKPISDLKRGVSVHCYDDHRVAMAFSVLSTVVEGTIIEEKRCVEKTWPNWWDDLENKIGLTVQGVDLASVASEASASGTINHDSAASIILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELIAEKSQGHVISLGGGIVETPAARELLKEYAATKGPVVHIVRPIDEVIRYLNSEASRPAYDEAIVDVFRRREPWFGECCSHDFFNRFGDLPYSSPKATSREIARFFNHITGQRPNLAQNLTSGRRSYFLCLTYPDVTQSFPVIHELTQGVDAIELRVDLLRASKDYDSIEYSIPTLAYVSSQVAALRRVTSLPIVFTVRTQSQGGSFPDAAEKEAVELLKLALRLGVEYVDVEISLSEKKIKELVSLKGSSHMIASWHDWSGNMIWDGPVVKEKYDAAARFGDIIKIVGKANSIQDNFTLYNFVSKVNSTAGSKPFIAINMGLEGQMSRVLNSTLSPVSHPLLPSKAAPGQLSFKQIQNALHLLGLLPAQRFYLFGTPIAHSMSPTLHNTGFEILGLPHHYELLETKEVAEEIKIAIGDSAFGGASVTIPYKLDVIPLLDKLSPAAEAIGAVNTIIPRTTGSGRMLVGDNTDWLGIKACITEQLSSKPIHAALVIGAGGTARAAIYALSALNVGDIYLYNRTTSKAYELAHAFPHAPVHVLEQLGQWPNGAVPPCVIVSTVPASATTTEEETSGILLPSKLFDYRDGPAVVIDMAYKPAETPLLRLAKTAGDNWATVPGLEVLLEQGYVQFEMWTGRRCPKELVAKWLGRLTTDHKQFVFEEECES | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver) (Laccaria laccata var. bicolor) |
B0EXJ8 | HTOMT_CATRO | MDVQSEEFRGAQAQIWSQSCSFITSASLKCAVKLGIPDTIDNHGKPITLSELTNALVPPVHPSKAPFIYRLMRVLAKNGFCSEEQLDGETEPLYSLTPSSRILLKKEPLNLRGIVLTMADPVQLKAWESLSDWYQNEDDSSTAFETAHGKNFWGYSSEHMEHAEFFNEAMASDSQLISKLLIGEYKFLFEGLASLVDIGGGTGTIAKAIAKNFPQLKCTVFDLPHVVANLESKENVEFVAGDMFEKIPSANAIFLKWILHDWNDEDCVKILKSCKKAIPAKGGKVIIIDMVMYSDKKDDHLVKTQTSMDMAMLVNFAAKERCEKEWAFLFKEAGFSDYKIYPKLDFTRSLIEVYP | 2.1.1.94 | null | alkaloid biosynthetic process [GO:0009821]; aromatic compound biosynthetic process [GO:0019438]; methylation [GO:0032259] | cytoplasm [GO:0005737] | 11-O-demethyl-17-O-deacetylvindoline O-methyltransferase activity [GO:0030766]; O-methyltransferase activity [GO:0008171]; protein homodimerization activity [GO:0042803] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family, COMT subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21047699}. | CATALYTIC ACTIVITY: Reaction=16-hydroxytabersonine + S-adenosyl-L-methionine = 16-methoxytabersonine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:20992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58239, ChEBI:CHEBI:58930, ChEBI:CHEBI:59789; EC=2.1.1.94; Evidence={ECO:0000269|PubMed:18053006}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 uM for 16-hydroxytabersonine {ECO:0000269|PubMed:18053006}; KM=21.7 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18053006}; Vmax=0.58 mmol/sec/mg enzyme toward 16-hydroxytabersonine {ECO:0000269|PubMed:18053006}; Vmax=0.79 mmol/sec/mg enzyme toward S-adenosyl-L-methionine {ECO:0000269|PubMed:18053006}; | PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:18053006}; | null | FUNCTION: 16-O-methyltransferase involved in the biosynthesis of vindoline. Highly specific for 16-hydroxytabersonine. No activity with tabersonine, 3-hydroxytyramine, 4-hydroxytyramine, 5-hydroxytryptamine (5HT), 2,3-dihydro-3-hydroxytabersonine, lochnericine, hoerhammericine, 16-hydroxy-2,3-dihydro-3-hydroxytabersonine, 16-hydroxylochnericine, 16-hydroxyhoerhammericine, quercetin, kaempferol and caffeic acid as substrates. {ECO:0000269|PubMed:18053006}. | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) |
B0F0H3 | MKRN2_XENLA | MSPKQVTCRYFLHGVCREGSRCLFSHDLATSKPSTVCRFFLRGQCAYGTRCRYDHVKPCNGTVFIPPQEMSPVLSPPPLFPAQEAAVPPTIPAPQRREKKTLVLRDRDLCGASVDPALQPGCITESQGSEGEAKPHSYLEAICTGLDESQDPASYPGAPQQLCPFAQAGECHCGDSCPYLHGDACEICGLQVLHPHDQEQRRDHEKLCMENFELDMERAFAVQASEGRVCSICMERVYEKQSPAQRRFRILSDCNHTYCLTCIRQWRCARQFDNPVIKSCPECRVISEFVIPSAYWVEDQSKKDELIEAFKQGMGKKLCKYFDQGRGTCPFGGKCLYLHSYPDGTRAQPEKPRKQLGSEGSVRFLNSLRLWDFIEDREQRGVPNAEVGKLGELFMHLSGADEELPAPFN | 2.3.2.27 | null | axis specification [GO:0009798]; cell differentiation [GO:0030154]; DNA-templated transcription [GO:0006351]; embryo development ending in birth or egg hatching [GO:0009792]; negative regulation of inflammatory response to antigenic stimulus [GO:0002862]; negative regulation of neurogenesis [GO:0050768]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; nervous system development [GO:0007399]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein polyubiquitination [GO:0000209]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630] | PF00642;PF14608;PF18044;PF13445; | 4.10.1000.10;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ERV1}. Nucleus {ECO:0000250|UniProtKB:Q9ERV1}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9ERV1}; | null | null | null | null | FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (By similarity). Inhibits neurogenesis and axis formation during embryonic development by modulating the phosphatidylinositol 3-kinase (PI3K) pathway (PubMed:18198183). Acts downstream of PI3K and akt1 to up-regulate gsk3b mRNA expression (PubMed:18198183). {ECO:0000250|UniProtKB:Q9ERV1, ECO:0000269|PubMed:18198183}. | Xenopus laevis (African clawed frog) |
B0F2B4 | NLGN4_MOUSE | MPAPVPALLCLALALASAQPSPPPPPPFPVVATNYGKLRGVRAALPGDVLGPVTQFLGVPYAAPPTGERRFQPPEPPSSWAGVRDATRFAPVCPQHLDERALLRDCLPAWFAANLDAIAAYVQDQSEDCLYLNLYVPGGANGKKMADDVTGNDHGDDQDSRDPGVGGAAAAAARKPVMVYIHGGSYMEGTANIVDGSVLASYGDVIVVTVNYRLGVLGFLSTGDQAAKGNYGLLDQIQALRWVEENAGAFGGDPDRVTVFGSGAGASCVSLLTLSHYSEGLFQKAIIQSGTALSSWAVNYQPARYARALGERVGCATPDPGSPPGSPPGWDSASLVSCLRGKAAGELARARVTPATYHVAFGPTVDGDVIPDDPQILMEQGEFLNYDIMLGVNQGEGARFVDGLGGGHDGGYGGYGGGYGGGVEDDEVQDGGPDGAAGGVSAGEFDLAVSGFINDLYGRPEGRGDALRETVKFMYTDWADRDSPEARRKTLVALFTDHQWVAPAVATADLHARYGSPTYFYAFYHRCHGGGGGGGGVDGVAGGVAGGVGGEEARPAWADAAHGDEVPYVFGVHMAGPGDVFGCNFSRNDVMLSAVVMTYWTNFAKTGDPNQPVAQDTRFVHTRPNRFEEVAWAKYDPRGQLYLHIGLRPRVRDHYRAAKVAFWLELVPHLHGLAADPGAYLSAAATRAAPSGDPDRDPGGGGGGRRRPRPATRRPAVMTSSSMASGSGMTSSSGSGMTSSSGSSASAVLIETRRDYSTELSVTIAVGASLLFLNVLAFAALYYKKDKRRHETHRRPPPPRPPQAPPSAAAADRNPRPDPGPAGRRGGECGAVVTAMAAEASAGGLGHDGVGGVGVGGVIGGVAGLRLACPPDYALTLRRSPDDVPRAGAGPGTMTLIPGALGGGGGGAVHGFNTFGSGVGVAGVAGVATSQAGPGLPHGHSTTRV | null | null | brainstem development [GO:0003360]; cerebellum development [GO:0021549]; chemical synaptic transmission [GO:0007268]; male courtship behavior [GO:0008049]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of excitatory postsynaptic potential [GO:0090394]; neuron cell-cell adhesion [GO:0007158]; organ growth [GO:0035265]; postsynaptic membrane assembly [GO:0097104]; presynaptic membrane assembly [GO:0097105]; social behavior [GO:0035176]; synaptic vesicle endocytosis [GO:0048488]; territorial aggressive behavior [GO:0002124]; vocalization behavior [GO:0071625] | cell surface [GO:0009986]; dendrite [GO:0030425]; excitatory synapse [GO:0060076]; glycinergic synapse [GO:0098690]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; postsynaptic specialization membrane [GO:0099634]; presynapse [GO:0098793]; synapse [GO:0045202] | neurexin family protein binding [GO:0042043]; signaling receptor activity [GO:0038023] | PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Postsynaptic cell membrane. Note=Detected at glycinergic postsynapses in retina. Detected on dendritic spines on cultured neurons. | null | null | null | null | null | FUNCTION: Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in the formation or maintenance of synaptic junctions via its interactions (via the extracellular domains) with neurexin family members. Plays a role in synaptic signal transmission. {ECO:0000269|PubMed:18434543, ECO:0000269|PubMed:21282647, ECO:0000269|PubMed:30100184}. | Mus musculus (Mouse) |
B0F481 | BIODA_ARATH | MIPVTATLIRHRLRHLRHRIRFKSTSVSPFHLPLNHPTYLIWSANTSLGKTLVSTGIAASFLLQQPSSSATKLLYLKPIQTGFPSDSDSRFVFSKLDSLSLRRQIPISISNSVLHSSLPAAKSLGLNVEVSESGMCSLNFRDEKTVTGAPELLCKTLYAWEAAISPHLAAERENATVEDSVVLQMIEKCLKEEMECGVKSEKSDLLCLVETAGGVASPGPSGTLQCDLYRPFRLPGILVGDGRLGGISGTIAAYESLKLRGYDIAAVVFEDHGLVNEVPLTSYLRNKVPVLVLPPVPKDPSDDLIEWFVESDGVFKALKETMVLANLERLERLNGMAKLAGEVFWWPFTQHKLVHQETVTVIDSRCGENFSIYKASDNSSLSQQFDACASWWTQGPDPTFQAELAREMGYTAARFGHVMFPENVYEPALKCAELLLDGVGKGWASRVYFSDNGSTAIEIALKMAFRKFCVDHNFCEATEEEKHIVVKVIALRGSYHGDTLGAMEAQAPSPYTGFLQQPWYTGRGLFLDPPTVFLSNGSWNISLPESFSEIAPEYGTFTSRDEIFDKSRDASTLARIYSAYLSKHLQEHSGVRQSAHVGALIIEPVIHGAGGMHMVDPLFQRVLVNECRNRKIPVIFDEVFTGFWRLGVETTTELLGCKPDIACFAKLLTGGMVPLAVTLATDAVFDSFSGDSKLKALLHGHSYSAHAMGCATAAKAIQWFKDPETNHNITSQGKTLRELWDEELVQQISSHSAVQRVVVIGTLFALELKADASNSGYASLYAKSLLIMLREDGIFTRPLGNVIYLMCGPCTSPEICRRLLTKLYKRLGEFNRT | 2.6.1.62; 6.3.3.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22547782}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:22547782}; | biotin biosynthetic process [GO:0009102] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | adenosylmethionine-8-amino-7-oxononanoate transaminase activity [GO:0004015]; ATP binding [GO:0005524]; dethiobiotin synthase activity [GO:0004141]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170] | PF13500;PF00202; | 3.90.1150.10;3.40.50.300;3.40.640.10; | Dethiobiotin synthetase family; Class-III pyridoxal-phosphate-dependent aminotransferase family, BioA subfamily | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:22547782}. | CATALYTIC ACTIVITY: Reaction=(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate; Xref=Rhea:RHEA:15805, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:149469, ChEBI:CHEBI:149473, ChEBI:CHEBI:456216; EC=6.3.3.3; Evidence={ECO:0000269|PubMed:22547782}; CATALYTIC ACTIVITY: Reaction=(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = (7R,8S)-7,8-diammoniononanoate + S-adenosyl-4-methylsulfanyl-2-oxobutanoate; Xref=Rhea:RHEA:16861, ChEBI:CHEBI:16490, ChEBI:CHEBI:59789, ChEBI:CHEBI:149468, ChEBI:CHEBI:149469; EC=2.6.1.62; Evidence={ECO:0000269|PubMed:22547782}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 0.072 min(-1) for 7,8-diamino-pelargonic acid aminotransferase + dethiobiotin synthetase activities, and 1.85 min(-1) for 7,8-diamino-pelargonic acid aminotransferase activity only (at pH 7.5 and 30 degrees Celsius). {ECO:0000269|PubMed:22547782}; | PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2. {ECO:0000269|PubMed:22547782}.; PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1. {ECO:0000269|PubMed:22547782}. | null | null | FUNCTION: Bifunctional enzyme that catalyzes two different reactions involved in the biotin biosynthesis. {ECO:0000269|PubMed:12644697, ECO:0000269|PubMed:17993549, ECO:0000269|PubMed:22547782, ECO:0000269|PubMed:23031218}.; FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring. {ECO:0000250, ECO:0000269|PubMed:16667573, ECO:0000269|PubMed:17993549, ECO:0000269|PubMed:22547782, ECO:0000269|PubMed:2909401, ECO:0000269|PubMed:8676868}.; FUNCTION: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor. {ECO:0000269|PubMed:22547782}. | Arabidopsis thaliana (Mouse-ear cress) |
B0F9L4 | GOGC6_ARATH | MDLASRYKGVVGMVFGDNQSSNEDSYIQRLLDRISNGTLPDDRRTAIVELQSVVAESNAAQLAFGAAGFPVIVGILKDQRDDLEMVRGALETLLGALTPIDHARAQKTEVQAALMNSDLLSREAENITLLLSLLEEEDFYVRYYTLQILTALLMNSQNRLQEAILTTPRGITRLMDMLMDREVIRNEALLLLTHLTREAEEIQKIVVFEGAFEKIFSIIKEEGGSDGDVVVQDCLELLNNLLRSSSSNQILLRETMGFEPIISILKLRGITYKFTQQKTVNLLSALETINMLIMGRADTEPGKDSNKLANRTVLVQKKLLDYLLMLGVESQWAPVAVRCMTFKCIGDLIDGHPKNRDILASKVLGEDRQVEPALNSILRIILQTSSIQEFVAADYVFKTFCEKNTEGQTMLASTLIPQPHPTSRDHLEDDVHMSFGSMLLRGLCSGEADGDLETCCRAASILSHVVKDNLRCKEKALKIVLESPMPSMGTPEPLFQRIVRYLAVASSMKSKEKSSTLGKSYIQQIILKLLVTWTVDCPTAVQCFLDSRHHLTFLLELVTDPAATVCIRGLASILLGECVIYNKSIENGKDAFSVVDAVGQKMGLTSYFSKFEEMQNSFIFSPSKKPPQGYKPLTRTPTPSEAEINEVDEVDEMVKGNEDHPMLLSLFDASFIGLVKSLEGNIRERIVDVYSRPKSEVAVVPADLEQKSGENEKDYINRLKAFIEKQCSEIQNLLARNAALAEDVASSGRNEQSQGSEQRASTVMDKVQMESIRRELQETSQRLETVKAEKAKIESEASSNKNMAAKLEFDLKSLSDAYNSLEQANYHLEQEVKSLKGGESPMQFPDIEAIKEEVRKEAQKESEDELNDLLVCLGQEESKVEKLSAKLIELGVDVDKLLEDIGDESEAQAESEED | null | null | endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; Golgi vesicle docking [GO:0048211]; post-embryonic development [GO:0009791]; protein exit from endoplasmic reticulum [GO:0032527]; transcytosis [GO:0045056]; vesicle fusion with Golgi apparatus [GO:0048280] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795] | null | PF04871;PF04869; | 1.25.10.10; | null | null | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:18182439}. Golgi apparatus, Golgi stack {ECO:0000269|PubMed:20837504}. Note=Concentrates only on one side of the Golgi bodies. {ECO:0000269|PubMed:18182439}. | null | null | null | null | null | FUNCTION: Golgi matrix protein playing a role in tethering of vesicles to Golgi membranes and in maintaining the overall structure of the Golgi apparatus. Functions in the anterograde transport of storage protein precursors from the endoplasmic reticulum (ER) to the Golgi complex. {ECO:0000269|PubMed:20837504}. | Arabidopsis thaliana (Mouse-ear cress) |
B0F9W3 | GPER1_MICUN | MEEQTTSLVWIYVNSTEQLNTSYEYNTTYLIEDSDKYQSYVIGLFLSCLYTILLFPIGFIGNILILVVNLNHRGKMAIPDLYFVNLAVADLILVADSLIEVFNLNEKYYDYAVLCTFMSLFLQVNMYSSIFFLTWMSFDRYIALANSMSSSPLRTMQHAKLSCGLIWMASILATLLPFTIVQTQHRGEVHFCFANVFEIQWLEVTIGFLVPFSIIGLCYSLIGRILMRSQKHRGLWPRRQKALRMIVVVVLVFFICWLPENVFISIQLLQGTADPSQRTATTLRHDYPLTGHIVNLAAFSNSCLNPIIYSFLGETFRDKLRLFIKQKASWSVVNRFCHHGLDLHLPVRSEVSEV | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to estradiol stimulus [GO:0071392]; cellular response to gonadotropin stimulus [GO:0071371]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; negative regulation of meiotic cell cycle [GO:0051447]; negative regulation of oocyte maturation [GO:1900194]; nervous system development [GO:0007399]; steroid hormone mediated signaling pathway [GO:0043401] | axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; cytoplasmic vesicle membrane [GO:0030659]; cytoskeleton [GO:0005856]; dendritic spine membrane [GO:0032591]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; recycling endosome [GO:0055037] | G protein-coupled receptor activity [GO:0004930]; nuclear estrogen receptor activity [GO:0030284]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:18420744}; Multi-pass membrane protein {ECO:0000269|PubMed:18420744}. Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, axon {ECO:0000250}. Postsynaptic density {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Colocalized with cadherin at the plasma membrane. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=Binds 17-beta-estradiol (E2) in plasma membranes with high affinity and displays rapid kinetics of association and dissociation. {ECO:0000269|PubMed:18420744, ECO:0000269|PubMed:19931550}; | null | null | null | FUNCTION: Membrane G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Plays a role in the embryonic development of sensory and motor neurons. May induce apoptosis and reduce proliferation of brain cells. Involved in maintenance of meiotic arrest in oocytes. {ECO:0000269|PubMed:18420744, ECO:0000269|PubMed:19931550}. | Micropogonias undulatus (Atlantic croaker) |
B0FPE9 | NLRP3_MACMU | MKMASTRCKLARYLEDLEDVDLKKFKMHLEDYPPQKGCISLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEKAKRDEPKWGSDNARVSNPTVICQEDSIEEEWMGLLEYLSRISICKKKKDYCKKYRKYVRSRFQCIEDRNARLGESVSLNKRYTRLRLIKEHRSQQEREHELLAIGKTKTWESPVSPIKMELLFDPDDEHSEPVHTVVFQGAAGIGKTILARKIMLDWASGTLYQDRFDYLFYIHCREVSLVTQRSLGDLIMSCCPDPNPPIRKIVSKPSRILFLMDGFDELQGAFDEHIGPLCTDWQKAERGDILLSSLIRKKLLPEASLLITTRPVALEKLQHLLDHPRHVEILGFSEAKRKEYFFKYFSDEAQARAAFSLIQENEVLFTMCFIPLVCWIVCTGLKQQMESGKSLAQTSKTTTAVYTFFLSSLLQPRGGSQEHRLCAHLWGLCSLAADGIWNQKILFEESDLRNHGLQKADVSAFLRMNLFQKEVDCEKFYSFIHMTFQEFFAAMYYLLEEEKEGRTNVPGSCLKLPSRDVTVLLENYGKFEKGYLIFVVRFLFGLVNQERTCYLEKKLSCKISQQIRLELLKWIEVKAKAKKLQIQPSQLELFYCLYEMQEEDFVQRAMDYFPKIEINLSTRMDHVVSSFCIENCHRVESLSLGFLHNMPKEEEEEEKEGRHLDMVQCVLPGSHAACSHRLVNSHLTSSFCRGLFSVLSTSQSLTELDLSDNSLGDPGMRVLCETLQHPDCNIRRLWLGRCGLSHECCFDISLVLSSNQKLVELDLSDNALGDFGIRLLCVGLKHLLCNLKKLWLVSCCLTSACCQDLASVLSTSRSLTRLYVGENALGDAGVAILCEKAKNPQCNLQKLGLVNSGLTSACCSALSSVLSTNQNLTHLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNCNLTSHCCWDLSTLLTSSQSLRKLSLGNNDLGDLGVMMFCEVLKQQSCLLQNLGLSEMYFNYETKSALETLQEEKPELTIVFEPSW | 3.6.4.- | null | detection of biotic stimulus [GO:0009595]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; negative regulation of acute inflammatory response [GO:0002674]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; NLRP3 inflammasome complex assembly [GO:0044546]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-4 production [GO:0032753]; positive regulation of T-helper 2 cell cytokine production [GO:2000553]; positive regulation of T-helper 2 cell differentiation [GO:0045630]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of type 2 immune response [GO:0002830]; protein homooligomerization [GO:0051260] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; Golgi membrane [GO:0000139]; interphase microtubule organizing center [GO:0031021]; membrane [GO:0016020]; mitochondrion [GO:0005739]; NLRP3 inflammasome complex [GO:0072559]; nucleus [GO:0005634] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA-binding transcription factor binding [GO:0140297]; phosphatidylinositol phosphate binding [GO:1901981]; phosphatidylinositol-4-phosphate binding [GO:0070273]; sequence-specific DNA binding [GO:0043565]; signaling adaptor activity [GO:0035591]; small molecule sensor activity [GO:0140299] | PF14484;PF13516;PF05729;PF17776;PF17779;PF02758; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: The disulfide bond in the pyrin domain might play a role in reactive oxygen species-mediated activation. {ECO:0000250|UniProtKB:Q96P20}.; PTM: Phosphorylation at Ser-198 by MAPK8/JNK1 increases inflammasome activation by promoting deubiquitination by BRCC3 and NLRP3 homooligomerization. Phosphorylation at Ser-805 by CSNK1A1 prevents inflammasome activation by preventing NEK7 recruitment. Phosphorylation at Ser-5 in the pyrin domain inhibits homomultimerization of NLRP3 and activation of the NLRP3 inflammasome: dephosphorylation by protein phosphatase 2A (PP2A) promotes assembly of the NLRP3 inflammasome (By similarity). Phosphorylation at Ser-295 by PKD/PRKD1 promotes NLRP3 inflammasome assembly (By similarity). Phosphorylation by ERK1/MAPK3 promotes NLRP3 inflammasome assembly. Phosphorylation by BTK (at Tyr-136, Tyr-140, Tyr-143 and Tyr-168) in the region that mediates binding to phosphatidylinositol phosphate, promotes relocalization of NLRP3 and assembly of the NLRP3 inflammasome. Phosphorylation at Tyr-860 inhibits NLRP3 inflammasome assembly: dephosphorylation by PTPN22 promotes inflammasome activation (By similarity). {ECO:0000250|UniProtKB:Q8R4B8, ECO:0000250|UniProtKB:Q96P20}.; PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination (By similarity). Ubiquitination does not lead to degradation, but inhibits inflammasome activation. Deubiquitination is catalyzed by BRCC3 and associated with NLRP3 activation and inflammasome assembly. This process can be induced by the activation of Toll-like receptors (by LPS), through a non-transcriptional pathway dependent on the mitochondrial production of reactive oxygen species, and by ATP (By similarity). Ubiquitinated by TRIM31 via 'Lys-48'-linked ubiquitination, leading to its degradation by the proteasome. Ubiquitinated at Lys-689 by the SCF(FBXL2) complex, leading to its degradation by the proteasome (By similarity). Ubiquitinated by TRIM35 via 'lys-48' and 'Lys-63'-linked ubiquitination leading to inhibition of NLRP3 inflammasome activation (By similarity). {ECO:0000250|UniProtKB:Q8R4B8, ECO:0000250|UniProtKB:Q96P20}.; PTM: Palmitoylation by ZDHHC12 inhibits the NLRP3 inflammasome by promoting NLRP3 degradation by the chaperone-mediated autophagy pathway. Following palmitoylation, HSPA8/HSC70 recognizes and binds the KFERQ-like motifs on NLRP3 and promotes NLRP3 recruitment to lysosomes, where it is degraded via the chaperone-mediated autophagy pathway in a LAMP2-dependent process. Palmitoylation by ZDHHC5 enhances its binding to NEK7 leading to inflammasome assembly and activation. Depalmitoylated by ABHD17A. {ECO:0000250|UniProtKB:Q96P20}.; PTM: Degraded via selective autophagy following interaction with IRGM. IRGM promotes NLRP3 recruitment to autophagosome membranes, promoting its SQSTM1/p62-dependent autophagy-dependent degradation. {ECO:0000250|UniProtKB:Q96P20}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8R4B8}. Inflammasome {ECO:0000250|UniProtKB:Q8R4B8}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q8R4B8}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8R4B8}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8R4B8}. Mitochondrion {ECO:0000250|UniProtKB:Q8R4B8}. Secreted {ECO:0000250|UniProtKB:Q8R4B8}. Nucleus {ECO:0000250|UniProtKB:Q8R4B8}. Note=In macrophages, under resting conditions, mainly located in the cytosol and on membranes of various organelles, such as endoplasmic reticulum, mitochondria and Golgi: forms an inactive double-ring cage that is primarily localized on membranes. Upon activation, NLRP3 is transported to microtubule organizing center (MTOC), where it is unlocked by NEK7, leading to its relocalization to dispersed trans-Golgi network (dTGN) vesicle membranes for the formation of an active inflammasome complex. Recruited to dTGN vesicle membranes by binding to phosphatidylinositol 4-phosphate (PtdIns4P). After the induction of pyroptosis, inflammasome specks are released into the extracellular space where they can further promote IL1B processing and where they can be engulfed by macrophages. Phagocytosis induces lysosomal damage and inflammasome activation in the recipient cells. In the Th2 subset of CD4(+) helper T-cells, mainly located in the nucleus. Nuclear localization depends upon KPNA2. In the Th1 subset of CD4(+) helper T-cells, mainly cytoplasmic. {ECO:0000250|UniProtKB:Q8R4B8}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q8R4B8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q8R4B8}; | null | null | null | null | FUNCTION: Sensor component of the NLRP3 inflammasome, which mediates inflammasome activation in response to defects in membrane integrity, leading to secretion of inflammatory cytokines IL1B and IL18 and pyroptosis. In response to pathogens and other damage-associated signals that affect the integrity of membranes, initiates the formation of the inflammasome polymeric complex composed of NLRP3, CASP1 and PYCARD/ASC. Recruitment of pro-caspase-1 (proCASP1) to the NLRP3 inflammasome promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), promoting cytokine secretion and pyroptosis. Activation of NLRP3 inflammasome is also required for HMGB1 secretion; stimulating inflammatory responses (By similarity). Under resting conditions, ADP-bound NLRP3 is autoinhibited (By similarity). NLRP3 activation stimuli include extracellular ATP, nigericin, reactive oxygen species, crystals of monosodium urate or cholesterol, amyloid-beta fibers, environmental or industrial particles and nanoparticles, such as asbestos, silica, aluminum salts, cytosolic dsRNA, etc. Almost all stimuli trigger intracellular K(+) efflux (By similarity). These stimuli lead to membrane perturbation and activation of NLRP3 (By similarity). Upon activation, NLRP3 is transported to microtubule organizing center (MTOC), where it is unlocked by NEK7, leading to its relocalization to dispersed trans-Golgi network (dTGN) vesicle membranes and formation of an active inflammasome complex. Associates with dTGN vesicle membranes by binding to phosphatidylinositol 4-phosphate (PtdIns4P). Shows ATPase activity (By similarity). {ECO:0000250|UniProtKB:Q8R4B8, ECO:0000250|UniProtKB:Q96P20}.; FUNCTION: Independently of inflammasome activation, regulates the differentiation of T helper 2 (Th2) cells and has a role in Th2 cell-dependent asthma and tumor growth. During Th2 differentiation, required for optimal IRF4 binding to IL4 promoter and for IRF4-dependent IL4 transcription. Binds to the consensus DNA sequence 5'-GRRGGNRGAG-3'. May also participate in the transcription of IL5, IL13, GATA3, CCR3, CCR4 and MAF. {ECO:0000250|UniProtKB:Q8R4B8}. | Macaca mulatta (Rhesus macaque) |
B0FYY4 | ITB1_SHEEP | MNLQLIFWIGLISSVCCVFGQADENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCHPNDIENPRGSKDIKKNKNVTNRSKGTAEKLQPEDITQIQPQQLVLQLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTNEQNCTSPFSYKNVLSLTDKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENDMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSGNVIQLIIDAYNSLSSEVILENSKLPEGVTINYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITANKCPNKNSETIKIKPLGFTEEVEIILQFICECECQSEGIPGSPKCHDGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTTSCMAVNGQICNGRGVCECGACKCTDPKFQGPTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCAQECSHFNITKVENRDKLPQPGQVDPLSHCKEKDVDDCWFYFTYSVNGNNEATVHVVETPECPTGPDIIPIVAGVVAGIVLIGPALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGK | null | null | cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; integrin-mediated signaling pathway [GO:0007229]; muscle organ development [GO:0007517]; myoblast differentiation [GO:0045445]; myoblast fusion [GO:0007520]; negative regulation of vasoconstriction [GO:0045906]; positive regulation of cell migration [GO:0030335]; positive regulation of protein localization to plasma membrane [GO:1903078]; receptor internalization [GO:0031623]; regulation of collagen catabolic process [GO:0010710] | cell surface [GO:0009986]; focal adhesion [GO:0005925]; integrin alpha9-beta1 complex [GO:0034679]; lamellipodium [GO:0030027]; melanosome [GO:0042470]; membrane [GO:0016020]; recycling endosome [GO:0055037]; ruffle membrane [GO:0032587] | C-X3-C chemokine binding [GO:0019960]; collagen binding involved in cell-matrix adhesion [GO:0098639]; fibronectin binding [GO:0001968]; integrin binding involved in cell-matrix adhesion [GO:0098640]; laminin binding [GO:0043236]; metal ion binding [GO:0046872]; protein heterodimerization activity [GO:0046982] | PF07974;PF18372;PF08725;PF07965;PF00362;PF17205; | 4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Recycling endosome {ECO:0000250|UniProtKB:P05556}. Melanosome {ECO:0000250|UniProtKB:P05556}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P05556}. Cell projection, ruffle {ECO:0000250|UniProtKB:P05556}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P05556}. Note=Enriched preferentially at invadopodia, cell membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. Colocalizes with ITGB1BP1 and metastatic suppressor protein NME2 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen. Translocates from peripheral focal adhesions to fibrillar adhesions in an ITGB1BP1-dependent manner. {ECO:0000250|UniProtKB:P05556}. | null | null | null | null | null | FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion. Integrin alpha-4/beta-1 is a receptor for VCAM1 and recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis (By similarity). ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 acts as a receptor for fibronectin FN1 and mediates R-G-D-dependent cell adhesion to FN1 (By similarity). ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (By similarity). ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling (By similarity). Plays an important role in myoblast differentiation and fusion during skeletal myogenesis (By similarity). ITGA9:ITGB1 may play a crucial role in SVEP1/polydom-mediated myoblast cell adhesion (By similarity). Integrins ITGA9:ITGB1 and ITGA4:ITGB1 repress PRKCA-mediated L-type voltage-gated channel Ca(2+) influx and ROCK-mediated calcium sensitivity in vascular smooth muscle cells via their interaction with SVEP1, thereby inhibit vasocontraction (By similarity). {ECO:0000250|UniProtKB:P05556, ECO:0000250|UniProtKB:P07228, ECO:0000250|UniProtKB:P09055}. | Ovis aries (Sheep) |
B0G0Y8 | PDE3_DICDI | MAPQQNIMKQLQQMQSSPYPSSSPSSTTVSQNNDNLNHNVHSLNNSSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSINEKNKINDNNNRGNSDDGNNNNSNNNSNNNNSNNNNRDDEEEEGDDEDNNNNNNSNNNKIRGYNDNNDINDIFSINFSSWSKSKDNLIENGVLIFEESGLYKELNLSKSSILNFLSIVASSYRNNPFHSFNHAIAVTQTIFLILLKTNLFNILSPIEKLSIIIASICHDLDHPALSNRFQINMKSSIAVLYNNKSVLENHHLSICLGILESKIGNELLSTLTVEEKKQFFRRVKILILATDMENHFTYKKQFDDIISTFSWDNSEHRDLLLIMFLKSADISNELRSFDISNKWANALMEEFFNQSDLEKLNNLPLTPFMEREKVVLHLTQVSFIEKFLLPSYQSLQNLLPSLEDFVQRIIENKEIWSNNGSSSSTTSSSPN | 3.1.4.35 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. {ECO:0000250}; | cAMP-mediated signaling [GO:0019933]; cGMP-mediated signaling [GO:0019934] | cytosol [GO:0005829] | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; cGMP binding [GO:0030553]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145] | PF00233; | 1.10.1300.10; | Cyclic nucleotide phosphodiesterase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12429832, ECO:0000269|PubMed:17040207}. | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; EC=3.1.4.35; Evidence={ECO:0000269|PubMed:11171061}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958; Evidence={ECO:0000269|PubMed:11171061}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.22 uM for cGMP {ECO:0000269|PubMed:11171061}; Vmax=2 pmol/min/mg enzyme with cGMP as substrate {ECO:0000269|PubMed:11171061}; Note=cAMP/cGMP selectivity of 0.0015. {ECO:0000269|PubMed:11171061}; | null | null | null | FUNCTION: Phosphodiesterase specific for cGMP, which is not activated by cGMP. Involved in the degradation of intracellular cGMP. {ECO:0000269|PubMed:11171061, ECO:0000269|PubMed:12429832}. | Dictyostelium discoideum (Social amoeba) |
B0G126 | FYV1_DICDI | MAESFQQLGVGSKSNERSFFSKFFGTDDSQKDFGPLPEIEYSDEQRFNPYPAIYEKKNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSNGNGNRSNSSLNNSNNNNQVRRTHSPSVSNKSDESNTTNTNTNITTNTNITTNTNTNTNTNSTNNDTSSNVTQQQLLTNLGQSKIISALKTKFQRPLPPVDDKKFWMPDHSSAVCYECSEEFTTFKRRHHCRLCGQIFCWKCSQKTLTDGKGERVRVCNFCYRRYMAPDDLDMEGYHYDPITGTVISLITNNDDGTNLNNGNGLIKLDGSTHNMNVSLGNSGDNSSFVQSPNNNFSQSPTFSQQQQQQQQQQQQQQQQQQQQQQQQTTGVMSGLNPFSNSTLLFGRNNNNNNQQQQQPIIEEDKQYYGDINTSYNNSYFNNNGFNNFNNEHYNNTNFNATSLNLNSQLHSNLLANTNGELFYDNSQHSISNYGNLDHHQQQQQSNSHGSLSATPSNTPSGLISPIVGAPSILDPNKMIFYSDQEGNYDNLDDYETSSSDGSDNDNEDNHLKSSHSSANDLGTSNTVSTGESNSESKLSSSSNDISIHHHHYHHHHHHSHGNLLKSNSLTPLNLNNNNIIINNNNINNNNNNDNGNDDNNNNNNDNNNNTTIEVDPRHSMPSKTSNTSFSMASLPSIFKLPTIGRNNNNNNNSGSGNSQYLSANSNASNSISPPNSARGSSSNPNSMTPTPTLSSSFSNLPNAETSPPSLVKAKQQQQQQQQQQQQPQPVLQPTIHHPLKTSLPMFSTQSPPPPTNQLAQSTSMAPPPSIFSPLGKLQALSHPSSSSNNQQQQQPQIVKPIIIAPNSLFFSDPSIVSLKSHPKTTNKTKFLEKYPLPKKYYESTENIIDTFGFKRTPSTEGNLLSQMLATSKQKEFDEKERLKISNNPQMSVYIQHINNLVSEQLEKNNIDLSWRSIIIDLTKKATDNVKIFVRKGDKMSTNEYIKIKKIPGGNKSECNYVDGVVMTKILTHKKMKDKFINPKILLLSCSVEFQRVENKFLYFDQLLQQEKEYLRILVSKIAERKPDLVLVEKTVSRHAQDFLLDAGISLALNVKPKLLERLGRCLGGEVLPTLDIIYNNNSNNNNSNSIQLQQQQNSNSPASLQNSTTTTNNNNNNNNNSTTLGSCGQFKVITYSEIGLKEKEILGKKTLMYFEKCPVELGATIIIRGEDLAVLKIIKKILKLSIFSMHNAYLELKYLNDQSSTSNLLFVNNNGQNLSCSPQIKFPLPKTYPTIPWKYQFTSQHIPVKKALLTSFYKPHSDFGQQQSVIQWTSDDEVLGIGTSDAFKHCDMKFPIENESIYDHQSIVFSHSIFCNSNQCIPFEIHAIDYYTDNDLTLGEFLSKFCFSLHICNIKECNRPLIEHERTFMNSTTRINICVQKTQTIQDRPTNSSPAQQRNQPVQRAGINVINLCKICNKFSPESPMSEEAWEMSFGKFLELCFFGFLPIKTGISPECSHNNAKDHISYFYYQDLAAIFSYEPLPSLELSLPPKNLKATYTEKQRQSVRAKELEIMNQCANQVYSAIHERLYEIGQENQGDRVQELIPSLVQEKQLICSKIESLLLLPESAHKSNDQIINLTKLLYANFMTWNSQLTGLIDSTSYQRSKRNVQQQQQQQQHQQSQQPQPQILIGGDVYSDSHLHTDSVKKINSKQHSHNTILLQSIQSNQEQQLEQQEEFEINVNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNTIDNKSENENENKNENKNENENENENKNENKNENENENKKENENQLEIKNENNDSGEEITNNNNNNNNNNNNNNNNNNNNNNNIDNNNNKDENISSTPLLSPSSVLGVSNSGINQAFLNAPNNTYNSVEQDLTLPLNHQSLNFAVGGLVSPGSSSGGLPVGSVPNSSSMPSIHNGGSGNIPSNLVGSASGLSTNYSPNALKDPKKLKIIDTIAGIVSSISQTRILGPTMPYLLLESTDNVALFENEPSTTIAYTLSSSDFKIALNSLLDEEWKRISEIEKQYELQQQQQQDSQDLESSSQQQQQQQQQQQEQQEQPSLPTPSHPLSQSMNFSPSSLLKISSSSLPKDNNNSSENKPNSETNDIVRSRGSVKLSGSPISISPLSNAFEKRKSTSLSSSANNSPISSILEKEKKLKQQSPSLSNSLSGQTIINNNQQQQQQQQPSPIIIDEKDDRNTEKSSIIETDSIIEDLNINQDESNITNEDGGKIGDYESELLYDHHQQGDSENNNNNNNNNNNNNNNNNNNNNNNNNNNTNNNNEQQINNSDTEGDSDSIKSSNSNIYSEKNIKLSKLMVSTQRKEIRSRFKFEKNGYELNIFCSSYYPVQFHALREYMCGDQEFIQSLTRSKIWNAKGGKSGSSWNKTLDDRFILKQVSRIELESFLDFAPLYFEYICKSFLNQIPTALCKILGVFTVRWKDSNGKALKKDLIVMENLFHSKCISKTYDLKGSLRGRLVKNESEVLLDENLLQASFASPICLGEYDKTRVALAVWNDTAFLSSLNVMDYSLLSGIDNQSNQLVVGIIDYMRKFTWDKALEMKVKQSGIMGGGGKVPTVISPKQYKLRFRDAMWLYFTLSPDKFTKVKHLMPYEKKKNNNNNYNYNNFNNNNFNNNNNISNNGNGNINQRQVQQINK | 2.7.1.150; 2.7.11.1 | null | defense response to Gram-negative bacterium [GO:0050829]; phagosome acidification [GO:0090383]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phospholipid metabolic process [GO:0006644]; phosphorylation [GO:0016310]; protein localization to phagocytic vesicle [GO:1905161]; sorocarp spore cell differentiation [GO:0044671] | early endosome membrane [GO:0031901]; endosome membrane [GO:0010008]; late endosome membrane [GO:0031902]; macropinosome [GO:0044354]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670] | 1-phosphatidylinositol-3-phosphate 5-kinase activity [GO:0000285]; 1-phosphatidylinositol-5-kinase activity [GO:0052810]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310] | PF00118;PF01363;PF01504; | 3.30.810.10;3.50.7.10;3.30.800.10;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q9Y2I7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z1T6}. Early endosome membrane {ECO:0000250|UniProtKB:Q9Y2I7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y2I7}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9Y2I7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y2I7}. Late endosome membrane {ECO:0000250|UniProtKB:Q9Y2I7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z1T6}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:13609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57923, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.150; Evidence={ECO:0000250|UniProtKB:Q9Y2I7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13610; Evidence={ECO:0000250|UniProtKB:Q9Y2I7}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + ADP + H(+); Xref=Rhea:RHEA:44680, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57795, ChEBI:CHEBI:57880, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9Y2I7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44681; Evidence={ECO:0000250|UniProtKB:Q9Y2I7}; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9Y2I7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:Q9Y2I7}; | null | null | null | null | FUNCTION: Dual specificity kinase part of the PI(3,5)P2 regulatory complex which regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate. {ECO:0000250|UniProtKB:Q9Y2I7}. | Dictyostelium discoideum (Social amoeba) |
B0G168 | SRSA_DICDI | MIAKVFKSITPESYILLVNAGLISAYGVRIIFQSVKNDEGKVDEKAHIGIGHFFKKRGAQLVDGKNLTDILKEKKKKKKKKKKINISNKLIIFKISRQLYSKLKLK | null | null | aggregation involved in sorocarp development [GO:0031152]; cell aggregation [GO:0098743]; regulation of DNA-templated transcription [GO:0006355]; response to imidacloprid [GO:1902351]; response to starvation [GO:0042594]; socially cooperative development [GO:0099120]; sorocarp morphogenesis [GO:0031288]; sporulation resulting in formation of a cellular spore [GO:0030435] | plasma membrane [GO:0005886] | null | null | null | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Involved in starvation response and aggregation stage of the life cycle. May be involved in fruiting body morphogenesis and spore formation. {ECO:0000269|PubMed:18673382}. | Dictyostelium discoideum (Social amoeba) |
B0I1T2 | MYO1G_HUMAN | MEDEEGPEYGKPDFVLLDQVTMEDFMRNLQLRFEKGRIYTYIGEVLVSVNPYQELPLYGPEAIARYQGRELYERPPHLYAVANAAYKAMKHRSRDTCIVISGESGAGKTEASKHIMQYIAAVTNPSQRAEVERVKDVLLKSTCVLEAFGNARTNRNHNSSRFGKYMDINFDFKGDPIGGHIHSYLLEKSRVLKQHVGERNFHAFYQLLRGSEDKQLHELHLERNPAVYNFTHQGAGLNMTVHSALDSDEQSHQAVTEAMRVIGFSPEEVESVHRILAAILHLGNIEFVETEEGGLQKEGLAVAEEALVDHVAELTATPRDLVLRSLLARTVASGGRELIEKGHTAAEASYARDACAKAVYQRLFEWVVNRINSVMEPRGRDPRRDGKDTVIGVLDIYGFEVFPVNSFEQFCINYCNEKLQQLFIQLILKQEQEEYEREGITWQSVEYFNNATIVDLVERPHRGILAVLDEACSSAGTITDRIFLQTLDMHHRHHLHYTSRQLCPTDKTMEFGRDFRIKHYAGDVTYSVEGFIDKNRDFLFQDFKRLLYNSTDPTLRAMWPDGQQDITEVTKRPLTAGTLFKNSMVALVENLASKEPFYVRCIKPNEDKVAGKLDENHCRHQVAYLGLLENVRVRRAGFASRQPYSRFLLRYKMTCEYTWPNHLLGSDKAAVSALLEQHGLQGDVAFGHSKLFIRSPRTLVTLEQSRARLIPIIVLLLQKAWRGTLARWRCRRLRAIYTIMRWFRRHKVRAHLAELQRRFQAARQPPLYGRDLVWPLPPAVLQPFQDTCHALFCRWRARQLVKNIPPSDMPQIKAKVAAMGALQGLRQDWGCRRAWARDYLSSATDNPTASSLFAQRLKTLQDKDGFGAVLFSSHVRKVNRFHKIRNRALLLTDQHLYKLDPDRQYRVMRAVPLEAVTGLSVTSGGDQLVVLHARGQDDLVVCLHRSRPPLDNRVGELVGVLAAHCQGEGRTLEVRVSDCIPLSHRGVRRLISVEPRPEQPEPDFRCARGSFTLLWPSR | null | null | actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; cell gliding [GO:0071976]; cell-substrate adhesion [GO:0031589]; endocytosis [GO:0006897]; exocytosis [GO:0006887]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; T cell meandering migration [GO:0120117]; T cell mediated immunity [GO:0002456]; T cell migration [GO:0072678]; vesicle transport along actin filament [GO:0030050] | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; leading edge membrane [GO:0031256]; membrane [GO:0016020]; microvillus [GO:0005902]; myosin complex [GO:0016459]; nucleoplasm [GO:0005654]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546] | PF00063;PF06017; | 1.10.10.820;1.20.5.4820;1.20.58.530;3.40.850.10;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19968988, ECO:0000269|PubMed:20071333}; Peripheral membrane protein {ECO:0000269|PubMed:19968988, ECO:0000269|PubMed:20071333}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q5SUA5}. Note=Recruited to Fc-gamma receptor (Fc-gamma-R) phagocytic cup. In T-cells, transiently accumulates in discrete areas at the plasma membrane of migrating cells or when membranes are deformed (By similarity). Localization at the membrane is not highly dependent on phosphatidylinositol 4,5-bisphosphate levels. Released from the membrane in the presence of ATP. May be enriched in peripheral processes, such as microvilli or ruffles. {ECO:0000250|UniProtKB:Q5SUA5, ECO:0000269|PubMed:20071333}. | null | null | null | null | null | FUNCTION: Unconventional myosin required during immune response for detection of rare antigen-presenting cells by regulating T-cell migration. Unconventional myosins are actin-based motor molecules with ATPase activity and serve in intracellular movements. Acts as a regulator of T-cell migration by generating membrane tension, enforcing cell-intrinsic meandering search, thereby enhancing detection of rare antigens during lymph-node surveillance, enabling pathogen eradication. Also required in B-cells, where it regulates different membrane/cytoskeleton-dependent processes. Involved in Fc-gamma receptor (Fc-gamma-R) phagocytosis. {ECO:0000250|UniProtKB:Q5SUA5}.; FUNCTION: [Minor histocompatibility antigen HA-2]: Constitutes the minor histocompatibility antigen HA-2. More generally, minor histocompatibility antigens (mHags) refer to immunogenic peptide which, when complexed with MHC, can generate an immune response after recognition by specific T-cells. The peptides are derived from polymorphic intracellular proteins, which are cleaved by normal pathways of antigen processing. The binding of these peptides to MHC class I or class II molecules and their expression on the cell surface can stimulate T-cell responses and thereby trigger graft rejection or graft-versus-host disease (GVHD) after hematopoietic stem cell transplantation from HLA-identical sibling donor. GVHD is a frequent complication after bone marrow transplantation (BMT), due to mismatch of minor histocompatibility antigen in HLA-matched sibling marrow transplants. HA-2 is restricted to MHC class I HLA-A*0201. {ECO:0000269|PubMed:11544309, ECO:0000305}. | Homo sapiens (Human) |
B0JJ82 | GLMU_MICAN | MVAVAILAAGKGTRMKSSLPKVLHPLGSRSLVERVLNVSESLHPQRKLVIIGYQGQQVRNTLQHLDDIEFVEQKEQLGTGHAIQQLIPHLEDFQGDLLVLNGDVPLLRPETLQNLLQIHQDHGNAATLLTANLPNPKGYGRVFCDGNNLVKQIVEERDCTDAQRQNHRINGGIYCFNWSKLAAILPNLTPNNDQGEYYLTDVVNFLDPVMAVDVEDFLEITGINDRKQLAAAYDILQTRVKDDWMAAGVTIIDPDSVTIEDTVTLSADVIIEPQTHLRGETIIASGCRIGPGSLIENSRIGSDVTVLFSVISDSQVDSGCRIGPYAHLRGEAKIGANCRVGNFVEIKKSSIGNKTNIAHLSYLGDATLGEKVNVGAGTITANYDGVKKHQTMIGSGTKTGANSVLVAPLKLGKNVTVAAGSTITKNVPDNALVIARESQRVIENWADQFQ | 2.3.1.157; 2.7.7.23 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01631}; | cell morphogenesis [GO:0000902]; cell wall organization [GO:0071555]; lipid A biosynthetic process [GO:0009245]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048] | carboxysome [GO:0031470]; cytoplasm [GO:0005737] | glucosamine-1-phosphate N-acetyltransferase activity [GO:0019134]; magnesium ion binding [GO:0000287]; structural constituent of carboxysome shell [GO:0043886]; UDP-N-acetylglucosamine diphosphorylase activity [GO:0003977] | PF00132;PF12804; | 2.160.10.10; | N-acetylglucosamine-1-phosphate uridyltransferase family; Transferase hexapeptide repeat family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; | null | PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. {ECO:0000255|HAMAP-Rule:MF_01631}.; PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01631}.; PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01631}. | null | null | FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}. | Microcystis aeruginosa (strain NIES-843 / IAM M-2473) |
B0JZV4 | CBPC5_XENTR | MEVRCGGLLFSSKFDSGNLARVEKVEKPGAEGDAFSGSVSGGSVPTPDYEFNIWTKPDCAETEYENGNRSWFYFSVRFGAPGKLIKINIMNMNKQSKLYSQGMAPFVRTVPIRSRWERIRDRPTFEMVENQFILSFVHRFLDCRGSTTYFAFCFPFSYEESQELMAGLDDRFSDCKNITPGSFPDSIYYHRELLCHSLDGLRVDLLTISSCHGMTEEREPRLDKLFPDRSTPRPYRFTGKRVYFLSSRVHPGETPSSFVFNGFLEFILRQDDPRAQMLRRMFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLNPDFELHPSVYAAKTVLLYHHVYNSVGPNDPDWRTSVSLQTSNISLCPKTSNHSLKDLPLEDSLSELEKANNLLNSMEKEECYITCPQAVTQGAPPENDPNFLSDSRDFIRQRDVFILESDTEPKDIYSHSGSSQPTIFTKSIPPQESGIAFYVDLHGHASKRGCFMYGNYFTEENDQVENMLYPKLISLNSANFDFLACNFSEKNMYAKDKRDGQSKEGSGRVAIHKATGIIHSYTLECNYNTGRCVNSIPAACHDCGRASPPPPPAFPPKYTTQVFEQIGRAVATAALDMAECNPWPRLIMSEYNNLTNLRAWMLKHLRNTKGVLPGTLKKKSTKSPVKASSLTSGSLSENSLIRTRSYSNSTASTNSQQNSPQIKPSINFTFLCSSSNHSPPKVSQRVLGPVRETKAQEKRRQQSLLRSSVRSPTACQQRLSTQAPSLSSGYPKTSSHAKTSCPLSLSLSMSGSGFSGLSQAAKVKNGTKKNNLEGDSTRQHIHQGHGIALLQNMQKRGSSHNNAEYSKSLESLGVRPSRIPVRRNGLLTNEKESPILRVWKYTTDTSLKHCSLADLAAVTSSLTVCSVPLLKSKAEEPVFICEATKETADQHFPAVSQDAAHLSAYQSVLSFCSEA | 3.4.17.-; 3.4.17.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730}; | C-terminal protein deglutamylation [GO:0035609]; defense response to virus [GO:0051607]; protein branching point deglutamylation [GO:0035611]; protein deglutamylation [GO:0035608]; protein side chain deglutamylation [GO:0035610]; proteolysis [GO:0006508] | cytosol [GO:0005829]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nucleus [GO:0005634] | metallocarboxypeptidase activity [GO:0004181]; tubulin binding [GO:0015631]; zinc ion binding [GO:0008270] | PF18027;PF00246; | 2.60.40.3120;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09M02}. Nucleus {ECO:0000250|UniProtKB:Q09M02}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NDL9}. Midbody {ECO:0000250|UniProtKB:Q8NDL9}. | CATALYTIC ACTIVITY: Reaction=gamma-L-glutamyl-L-glutamyl-[protein] + H2O = L-glutamate + L-glutamyl-[protein]; Xref=Rhea:RHEA:60152, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15377, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:143622; Evidence={ECO:0000250|UniProtKB:Q09M02}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60153; Evidence={ECO:0000250|UniProtKB:Q09M02}; CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-glutamate; Xref=Rhea:RHEA:60004, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:143623; Evidence={ECO:0000250|UniProtKB:Q09M02}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000250|UniProtKB:Q09M02}; CATALYTIC ACTIVITY: Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-[tubulin] + L-glutamate; Xref=Rhea:RHEA:63796, Rhea:RHEA-COMP:16436, Rhea:RHEA-COMP:16437, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90782, ChEBI:CHEBI:149556; EC=3.4.17.24; Evidence={ECO:0000250|UniProtKB:Q09M02}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63797; Evidence={ECO:0000250|UniProtKB:Q09M02}; CATALYTIC ACTIVITY: Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-glutamate; Xref=Rhea:RHEA:63792, Rhea:RHEA-COMP:16435, Rhea:RHEA-COMP:16436, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:149555, ChEBI:CHEBI:149556; EC=3.4.17.24; Evidence={ECO:0000250|UniProtKB:Q09M02}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793; Evidence={ECO:0000250|UniProtKB:Q09M02}; | null | null | null | null | FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Cleaves alpha- and gamma-linked polyglutamate tubulin side-chain, as well as the branching point glutamate. Also catalyzes the removal of alpha-linked glutamate residues from the carboxy-terminus of alpha-tubulin. {ECO:0000250|UniProtKB:Q09M02}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B0K011 | OSR1_RAT | MGSKTLPAPVPIHPSLQLTNYSFLQAVNGLPTVPSDHLPNLYGFSALHAVHLHQWTLGYPAMHLPRSSFSKVPGAVSSLMDARFQLPAFPWFPHVIHPKPEITAGGSGAALKTKPRFDFANLALAATQEDPTKLGRGEGPGSPAGGLGALLDVTKLSPEKKPTRGRLPSKTKKEFVCKFCGRHFTKSYNLLIHERTHTDERPYTCDICHKAFRRQDHLRDHRYIHSKEKPFKCQECGKGFCQSRTLAVHKTLHSQVKELKTSKIKC | null | null | cell differentiation [GO:0030154]; cell proliferation involved in kidney development [GO:0072111]; cellular response to retinoic acid [GO:0071300]; chondrocyte differentiation [GO:0002062]; embryonic digit morphogenesis [GO:0042733]; embryonic forelimb morphogenesis [GO:0035115]; embryonic hindlimb morphogenesis [GO:0035116]; embryonic skeletal joint development [GO:0072498]; embryonic skeletal joint morphogenesis [GO:0060272]; embryonic skeletal limb joint morphogenesis [GO:0036023]; gonad development [GO:0008406]; heart development [GO:0007507]; intermediate mesoderm development [GO:0048389]; mesangial cell development [GO:0072143]; mesonephric duct morphogenesis [GO:0072180]; mesonephros development [GO:0001823]; metanephric cap mesenchymal cell proliferation involved in metanephros development [GO:0090094]; metanephric epithelium development [GO:0072207]; metanephric glomerulus vasculature development [GO:0072239]; metanephric interstitial fibroblast development [GO:0072259]; metanephric mesenchymal cell differentiation [GO:0072162]; metanephric mesenchyme development [GO:0072075]; metanephric mesenchyme morphogenesis [GO:0072133]; metanephric nephron tubule development [GO:0072234]; metanephric smooth muscle tissue development [GO:0072208]; metanephros development [GO:0001656]; middle ear morphogenesis [GO:0042474]; negative regulation of apoptotic process [GO:0043066]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of nephron tubule epithelial cell differentiation [GO:0072183]; negative regulation of transcription by RNA polymerase II [GO:0000122]; odontogenesis [GO:0042476]; pattern specification involved in metanephros development [GO:0072268]; positive regulation of bone mineralization [GO:0030501]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of gastrulation [GO:2000543]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; posterior mesonephric tubule development [GO:0072166]; pronephros development [GO:0048793]; regulation of transcription by RNA polymerase II [GO:0006357]; renal vesicle progenitor cell differentiation [GO:0072184]; roof of mouth development [GO:0060021]; sodium ion transmembrane transport [GO:0035725]; specification of anterior mesonephric tubule identity [GO:0072168]; specification of posterior mesonephric tubule identity [GO:0072169]; stem cell differentiation [GO:0048863]; ureter urothelium development [GO:0072190]; ureteric bud development [GO:0001657]; urogenital system development [GO:0001655] | cell cortex [GO:0005938]; cytosol [GO:0005829]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00096; | 3.30.160.60; | Odd C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcription factor that plays a role in the regulation of embryonic heart and urogenital development. {ECO:0000250}. | Rattus norvegicus (Rat) |
B0K019 | BAG1_RAT | MADRGGARRPRGDQEPLGPRLRAPRSARETRQSESRAERGLPPSQRSSVRSAASGHDRSTRGAASGACKPRVKKKVRPRSSQSEKVAHSKELTRSKKLTRSKKVTGTQEATQVEEVTTIEEATQTEEITVAEEVTQTENMAQTEEMVQTEEMEPPTLSVVVTHSNERYDLLVTPQQGNSEPIVQDLAQLVEEATGVPLPFQKLIFKGKSLKEMETPLSALGMQNGCRVMLIGEKSNPEEEAELKKLKDLEVSVEKTANHLEELNKELSDIQQGFLAKELQAEALCRLDRKIKATIEQFMKILEEIDTMVLPENFKDSRLKRKNLVKKVQVFLAECDTVEQYICQETERLQSTNLALPE | null | null | apoptotic process [GO:0006915]; chaperone cofactor-dependent protein refolding [GO:0051085]; negative regulation of apoptotic process [GO:0043066]; negative regulation of motor neuron apoptotic process [GO:2000672]; negative regulation of protein phosphorylation [GO:0001933]; neuron differentiation [GO:0030182]; positive regulation of Schwann cell differentiation [GO:0014040]; positive regulation of smooth muscle cell apoptotic process [GO:0034393]; protein localization to mitochondrion [GO:0070585]; protein stabilization [GO:0050821]; response to benzene [GO:1901423]; response to nicotine [GO:0035094]; response to organic cyclic compound [GO:0014070]; response to xenobiotic stimulus [GO:0009410] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | adenyl-nucleotide exchange factor activity [GO:0000774]; protein-folding chaperone binding [GO:0051087]; ubiquitin protein ligase binding [GO:0031625] | PF02179;PF00240; | 1.20.58.120; | null | PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli. Involved in the STUB1-mediated proteasomal degradation of ESR1 in response to age-related circulating estradiol (17-beta-estradiol/E2) decline, thereby promotes neuronal apoptosis in response to ischemic reperfusion injury (PubMed:21808025). {ECO:0000250|UniProtKB:Q99933, ECO:0000269|PubMed:21808025}. | Rattus norvegicus (Rat) |
B0K020 | CISD1_RAT | MGLSSDSPVRVEWIAAVTFAAGTAALGYLAYKKFYAKESRTKAMVNLQIQKDNPKVVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHIKHNEETGDNVGPLIIKKKET | 2.6.1.3 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:Q9NZ45}; Note=Binds 1 [2Fe-2S] cluster per subunit. The [2Fe-2S] cluster is redox-active and pH labile and is significantly less stable at pH 4.5 as compared with pH 7.0. {ECO:0000250|UniProtKB:Q9NZ45}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:Q9NZ45}; | protein maturation by [2Fe-2S] cluster transfer [GO:0106034]; regulation of autophagy [GO:0010506]; regulation of cellular respiration [GO:0043457] | cytoplasmic side of mitochondrial outer membrane [GO:0032473]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739] | 2 iron, 2 sulfur cluster binding [GO:0051537]; identical protein binding [GO:0042802]; L-cysteine transaminase activity [GO:0047801]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170] | PF10660;PF09360; | 3.40.5.90; | CISD protein family | PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:Q9NZ45}. | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9NZ45}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:Q9NZ45}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-cysteine = 2-oxo-3-sulfanylpropanoate + L-glutamate; Xref=Rhea:RHEA:17441, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35235, ChEBI:CHEBI:57678; EC=2.6.1.3; Evidence={ECO:0000250|UniProtKB:Q9NZ45}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17442; Evidence={ECO:0000250|UniProtKB:Q9NZ45}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17443; Evidence={ECO:0000250|UniProtKB:Q9NZ45}; | null | null | null | null | FUNCTION: L-cysteine transaminase that catalyzes the reversible transfer of the amino group from L-cysteine to the alpha-keto acid 2-oxoglutarate to respectively form 2-oxo-3-sulfanylpropanoate and L-glutamate (By similarity). The catalytic cycle occurs in the presence of pyridoxal 5'-phosphate (PLP) cofactor that facilitates transamination by initially forming an internal aldimine with the epsilon-amino group of active site Lys-55 residue on the enzyme (PLP-enzyme aldimine), subsequently displaced by formation of an external aldimine with the substrate amino group (PLP-L-cysteine aldimine). The external aldimine is further deprotonated to form a carbanion intermediate, which in the presence of 2-oxoglutarate regenerates PLP yielding final products 2-oxo-3-sulfanylpropanoate and L-glutamate. The proton transfer in carbanion intermediate is suggested to be controlled by the active site lysine residue, whereas PLP stabilizes carbanion structure through electron delocalization, also known as the electron sink effect (By similarity). Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation (By similarity). May be involved in iron-sulfur cluster shuttling and/or in redox reactions. Can transfer the [2Fe-2S] cluster to an apo-acceptor protein only when in the oxidation state, likely serving as a redox sensor that regulates mitochondrial iron-sulfur cluster assembly and iron trafficking upon oxidative stress (By similarity). {ECO:0000250|UniProtKB:Q91WS0, ECO:0000250|UniProtKB:Q9NZ45}. | Rattus norvegicus (Rat) |
B0KW95 | CADH2_CALJA | MCRIAGAPRTLLPLLAALLQASVEASGEIALCKTGFPEDVYSAVLSKDVHEGQPLLNVKFSNCNGKRKVQYESSEPADFKVDEDGMVYAVRSFPLSSEHAKFLIYAQDKETQEKWQVAVKLSLKPTLPEESVKESTEVEEIVFPRQLGKHSGHLQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDREQIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGTVPEGSKPGTYVMTVTAIDADDPNALNGMLRYRILSQAPSTPSPNMFTINNETGDIITVAAGLDREKVQQYTLIIQATDMEGNPTYGLSNTATAIITVTDVNDNPPEFTAMTFYGEVPENRVDVIVANLTVTDKDQPHTPAWNAVYRISGGDPTGRFAIQTDPNSNDGLVTVVKPIDFETNRMFVLTVAAENQVPLAKGIQHPPQSTATVSVTVIDVNENPYFAPNPKIIRQEEGLHAGTMLTTFTAQDPDRYMQQNIRYTKLSDPANWLKIDPVNGQITTIAILDRESPNVKNNIYNATFLASDNGIPPMSGTGTLQIYLLDINDNAPQVLPQEAETCETPDPNSINITALDYDIDPNAGPFAFDLPLSPVNIKRNWTITRLNGDFAQLNLKIKFLEAGIYEVPIIITDSGNPPKSNISILRVKVCQCDSNGDCTDVDRIVGAGLGTGAIIAILLCIIILLILVLMFVVWMKRRDKERQAKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPDTVEPDAIKPVGIRRMDERPIHAEPQYPVRSAAPHPGDIGDFINEGLKAADNDPTAPPYDSLLVFDYEGSGSTAGSLSSLNSSSSGGEQDYDYLNDWGPRFKKLADMYGGGDD | null | null | adherens junction organization [GO:0034332]; blood vessel morphogenesis [GO:0048514]; brain development [GO:0007420]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell morphogenesis [GO:0000902]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction assembly [GO:0007043]; glial cell differentiation [GO:0010001]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; neural crest cell development [GO:0014032]; neuronal stem cell population maintenance [GO:0097150]; regulation of axonogenesis [GO:0050770]; regulation of synaptic transmission, glutamatergic [GO:0051966]; synapse assembly [GO:0007416]; synaptic vesicle clustering [GO:0097091]; type B pancreatic cell development [GO:0003323] | adherens junction [GO:0005912]; apical part of cell [GO:0045177]; catenin complex [GO:0016342]; cell junction [GO:0030054]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; desmosome [GO:0030057]; intercalated disc [GO:0014704]; lamellipodium [GO:0030027]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; sarcolemma [GO:0042383] | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509] | PF01049;PF00028;PF08758; | 2.60.40.60;4.10.900.10; | null | PTM: Cleaved by MMP24. Ectodomain cleavage leads to the generation of a soluble 90 kDa N-terminal soluble fragment and a 45 kDa membrane-bound C-terminal fragment 1 (CTF1), which is further cleaved by gamma-secretase into a 35 kDa (By similarity). Cleavage in neural stem cells by MMP24 affects CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate neural stem cell quiescence (By similarity). {ECO:0000250|UniProtKB:P15116}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15116}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P15116}. Cell junction {ECO:0000250|UniProtKB:P19022}. Cell surface {ECO:0000250|UniProtKB:P15116}. Cell junction, desmosome {ECO:0000250|UniProtKB:P15116}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P15116}. Note=Colocalizes with TMEM65 at the intercalated disk in cardiomyocytes (By similarity). Colocalizes with OBSCN at the intercalated disk and sarcolemma in cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:P15116}. | null | null | null | null | null | FUNCTION: Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell. Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. Plays a role in cell-to-cell junction formation between pancreatic beta cells and neural crest stem (NCS) cells, promoting the formation of processes by NCS cells (By similarity). Required for proper neurite branching. Required for pre- and postsynaptic organization (By similarity). CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density. {ECO:0000250|UniProtKB:P10288, ECO:0000250|UniProtKB:P15116}. | Callithrix jacchus (White-tufted-ear marmoset) |
B0KWU8 | BRCC3_CALJA | MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDTRSDSKFAYTGTEMRTVAEKVDAVRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQKSSESLHGPRDFWSSSKHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHLRELQQEKEELMQELSSLE | 3.4.19.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:E2AXC7, ECO:0000250|UniProtKB:P46736}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:E2AXC7}; | cell division [GO:0051301]; chromatin remodeling [GO:0006338]; DNA repair-dependent chromatin remodeling [GO:0140861]; double-strand break repair [GO:0006302]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; positive regulation of DNA repair [GO:0045739]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; protein K63-linked deubiquitination [GO:0070536]; proteolysis [GO:0006508]; response to ionizing radiation [GO:0010212] | BRCA1-A complex [GO:0070531]; BRISC complex [GO:0070552]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; spindle pole [GO:0000922] | cysteine-type deubiquitinase activity [GO:0004843]; metal ion binding [GO:0046872]; metal-dependent deubiquitinase activity [GO:0140492]; metallopeptidase activity [GO:0008237]; polyubiquitin modification-dependent protein binding [GO:0031593] | PF18110;PF01398; | 3.40.140.10; | Peptidase M67A family, BRCC36 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46736}. Cytoplasm {ECO:0000250|UniProtKB:P46736}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P46736}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with ABRAXAS2 retains BRCC3 in the cytoplasm. {ECO:0000250|UniProtKB:P46736}. | null | null | null | null | null | FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (By similarity). Acts as a regulator of the NLRP3 inflammasome by mediating deubiquitination of NLRP3, leading to NLRP3 inflammasome assembly (By similarity). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (By similarity). Deubiquitinates HDAC1 and PWWP2B leading to their stabilization (By similarity). {ECO:0000250|UniProtKB:P46736, ECO:0000250|UniProtKB:P46737}. | Callithrix jacchus (White-tufted-ear marmoset) |
B0KYV5 | LIMA1_PIG | MESTPFNRQQWTSLSLRVTAKELSLVNKNKSSAIVEIFSKYQKAAEEANMEKRRSNTENLPQHFRRGNLTVLKKKWENPAPGVESLPESTRNSSAEVRHRGDPPPAEVASSSASGVEADQGVCPRPRFSSPPEVPYPNPRIKDTEHLKDHSAESKKMENCLAESRHEVGKPETSENAEASNKIEKYNVPLNRLKMMFERGEPAQTKILRAQSRSTGGRKISENSYSLDDLEIGPGQLSSSAFNTEKSESRRNLEFPRLSDTSIKDRMAKYQAAVSKQSSSTNYTNELKANGGEIKTHKLEQKENVPPGPEVCISHQDGEKVSASENSLAACSTPPEDDSCKSQVKSDVQQPVHPKPLSPVARASSLSESSPPKAVKKFQAPARETCVECQKTVYPMERLLANQQVFHISCFRCSYCNNKLSLGTYASLHGRIYCKPHFNQLFKSKGNYDEGFGHRPHKDLWASKLENEETLERPAQLPNAAEIPQSPGVEDAPIAKVGVLTASMEAKASSQLEKEDKPAETKKLRIAWPPPTELSSSGSALEEGIKVSKPKWPPEDEVSKPEAPEDVDLDLKKLRRSSSLKERSRPFTVAASFRTASVKSPKPLSPPMRKGWSLSEQSEEFGGGVAAERKQMEKASASEKNGSVGKTTWPSKESRGGEAAGRSKEVQDFEIGSENLIENGASLDEGDRDLLQQQSPLEPKSKNWSSFADNTSAKEFTTQKQKSQDVEFWEGEVVEELSVEEQIKRNRYYDEEEDEE | null | null | actin filament bundle assembly [GO:0051017]; cell migration [GO:0016477]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; intestinal cholesterol absorption [GO:0030299]; ruffle organization [GO:0031529] | actin cytoskeleton [GO:0015629]; brush border membrane [GO:0031526]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; ruffle [GO:0001726] | actin filament binding [GO:0051015]; metal ion binding [GO:0046872] | PF00412; | 2.10.110.10; | null | PTM: Phosphorylation of the C-terminal region by MAPK1/MAPK3 reduces its association with F-actin and contributes to actin filament reorganization and enhances cell motility. {ECO:0000250|UniProtKB:Q9ERG0}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UHB6}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9UHB6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UHB6}. Cell membrane {ECO:0000250|UniProtKB:Q9ERG0}. Note=This cytoskeletal protein colocalizes with actin stress fibers and focal adhesion plaques. Expressed mainly in the brush border membrane of the small intestine and colocalizes with NPC1L1 and MYO5B (By similarity). Colocalizes with PXN at focal adhesions in mesangial cells (By similarity). Colocalizes with actin stress fibers in quiescent cells. PDGF stimulation induced disassembly of stress fibers and formation of peripheral and dorsal ruffles, where LIMA1 is relocalized (By similarity). {ECO:0000250|UniProtKB:Q9ERG0, ECO:0000250|UniProtKB:Q9UHB6}. | null | null | null | null | null | FUNCTION: Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (By similarity). Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By similarity). {ECO:0000250|UniProtKB:Q9ERG0, ECO:0000250|UniProtKB:Q9UHB6}. | Sus scrofa (Pig) |
B0L3A2 | DESPR_HUMAN | MTMFKGSNEMKSRWNWGSITCIICFTCVGSQLSMSSSKASNFSGPLQLYQRELEIFIVLTDVPNYRLIKENSHLHTTIVDQGRTV | null | null | endothelin receptor signaling pathway [GO:0086100]; vascular endothelial growth factor signaling pathway [GO:0038084] | plasma membrane [GO:0005886] | endothelin receptor activity [GO:0004962]; vascular endothelial growth factor binding [GO:0038085] | null | null | null | PTM: N-glycosylated. {ECO:0000269|PubMed:27301377}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24465725, ECO:0000269|PubMed:27301377, ECO:0000269|PubMed:33853558}; Single-pass membrane protein {ECO:0000305|PubMed:27301377}. | null | null | null | null | null | FUNCTION: Dual receptor for both endothelin-1 and the signal sequence of vascular endothelial growth factor A (PubMed:17446437, PubMed:24465725). Does not act as a receptor for angiotensin-2 (PubMed:17446437). Does not bind the VEGFA mature protein (By similarity). May play a role in angiogenesis with a significant role in cardiovascular and neural development (By similarity). {ECO:0000250|UniProtKB:Q2QKR2, ECO:0000269|PubMed:17446437, ECO:0000269|PubMed:24465725}. | Homo sapiens (Human) |
B0LDU5 | PKS4_RUBID | MVTVEEVRKAQRAEGPATVLAIGTATPPNCVGQSTYPDYYFRITNSEHKIELKQKFQRMCDKSMIKKRYMYLTEEILKENPSMCEYMAPSLDARQDMVIVEIPKLGKEAATKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLIKLFGLRPSVKRLMMYQQGCFAGGTVLRLAKDLAENNRGARVLVVCSEITVVTFRGPSDTHLDCLVGQALFGDGVASIIVGADPLPEIEKPLFELVSAAQTILPDSEGAIEGHLREVGLTFHLLENVPALISKNIEKSLNETFKPLDIMDWNSLFWIAHPGGPAILDQVEAKLGLKPEKLEATGHILSEYGNMSSACVLFILDVVRRKSAANGVTTRILSIGQISKSLLILAWFLFSLV | 2.3.1.212; 2.3.1.74 | null | flavonoid biosynthetic process [GO:0009813]; polyketide biosynthetic process [GO:0030639] | null | chalcone synthase activity [GO:0102128]; naringenin-chalcone synthase activity [GO:0016210]; protein homodimerization activity [GO:0042803] | PF02797;PF00195; | 3.40.47.10; | Thiolase-like superfamily, Chalcone/stilbene synthases family | null | null | CATALYTIC ACTIVITY: Reaction=4-coumaroyl-CoA + H(+) + H2O + malonyl-CoA = 4-hydroxybenzalacetone + 2 CO2 + 2 CoA; Xref=Rhea:RHEA:34483, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57355, ChEBI:CHEBI:57384, ChEBI:CHEBI:68636; EC=2.3.1.212; Evidence={ECO:0000269|PubMed:12226219, ECO:0000269|PubMed:18068110}; CATALYTIC ACTIVITY: Reaction=4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'-tetrahydroxychalcone + 3 CO2 + 4 CoA; Xref=Rhea:RHEA:11128, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57355, ChEBI:CHEBI:57384, ChEBI:CHEBI:77645; EC=2.3.1.74; Evidence={ECO:0000255|PROSITE-ProRule:PRU10023, ECO:0000269|PubMed:12226219, ECO:0000269|PubMed:18068110}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 uM for malonyl-CoA {ECO:0000269|PubMed:12226219}; KM=3 uM for p-coumaryl CoA {ECO:0000269|PubMed:12226219}; | PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is approximately 8.0. {ECO:0000269|PubMed:12226219}; | null | FUNCTION: Bifunctional polyketide synthase producing both 4-hydroxybenzalacetone and naringenin chalcone. Can use p-coumaryl-CoA and ferulyl-CoA as substrates. Catalyzes the initial key reaction step in the biosynthesis of phenylbutanoids. {ECO:0000269|PubMed:18068110}. | Rubus idaeus (Raspberry) |
B0LL23 | PLR_SINHE | MAKSRVLIVGGTGYLGRRMVKACLDQGHTTYVLHRQEVGVDIDKIQMLLSFKEQGAHLVEGSFNDHRSLVEAVKLVDVVICTISGVHIRSHQILLQLKLVEAIEEAGNVKRFLPSEFGMDPARMAHAMEPGRATFDEKMVVRKAIEDAKIPHTYASANCFAGYFLGGLCQFGKIIPSKESVILSGDGNVKGIYVDEYDIATYTIKTMDDPRTLNKTIYIRPPANILSQREVVEIWEKLIGKVLDKSSLSEEDFLALMKGLSHGHQAGLTHYYHVSYEGCLTNFEVEDGVDASKLYPQVNYTTVSEYLKRYL | 1.23.1.1; 1.23.1.2 | null | (+)-pinoresinol catabolic process [GO:1902125]; (-)-secoisolariciresinol biosynthetic process [GO:1902138]; aromatic compound biosynthetic process [GO:0019438]; phenylpropanoid biosynthetic process [GO:0009699]; response to jasmonic acid [GO:0009753]; response to UV [GO:0009411]; response to wounding [GO:0009611] | null | lariciresinol reductase activity [GO:0010284]; pinoresinol reductase activity [GO:0010283] | PF05368; | 3.40.50.720;3.90.25.10; | NmrA-type oxidoreductase family, Isoflavone reductase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(-)-secoisolariciresinol + NADP(+) = (+)-lariciresinol + H(+) + NADPH; Xref=Rhea:RHEA:34423, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65004, ChEBI:CHEBI:67246; EC=1.23.1.2; Evidence={ECO:0000269|PubMed:26359402}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34424; Evidence={ECO:0000269|PubMed:26359402}; CATALYTIC ACTIVITY: Reaction=(+)-lariciresinol + NADP(+) = (+)-pinoresinol + H(+) + NADPH; Xref=Rhea:RHEA:34419, ChEBI:CHEBI:40, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67246; EC=1.23.1.1; Evidence={ECO:0000269|PubMed:26359402}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34420; Evidence={ECO:0000269|PubMed:26359402}; | null | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:26359402}. | null | null | FUNCTION: Reductase involved in lignan biosynthesis (PubMed:26359402). Also involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family (PubMed:26359402). Catalyzes the enantioselective sequential conversion of (+)-pinoresinol into (+)-lariciresinol and of (+)-lariciresinol into (-)-secoisolariciresinol (PubMed:26359402). Abstracts the 4R-hydride from the NADPH cofactor during catalysis (PubMed:26359402). {ECO:0000269|PubMed:26359402}. | Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum) |
B0LPN4 | RYR2_RAT | MADAGEGEDEIQFLRTDDEVVLQCTATIHKEQQKLCLAAEGFGNRLCFLESTSNSKNVPPDLSICTFVLEQSLSVRALQEMLANTVEKSEGKFMMKTAQGGGHRTLLYGHAILLRHSYSGMYLCCLSTSRSSTDKLAFDVGLQEDTTGEACWWTIHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSYGNSSWRVDAAFQQTLWSVAPISSGSEAAQGYLIGGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLMEDKNLLLMDKEKADVKSTAFAFRSSKEKLDAGVRKEVDGMGTSEIKYGDSICYIQHVDTGLWLTYQAVDVKSARMGSIQRKAIMHHEGHMDDGLNLSRSQHEESRTARVIRSTVFLFNRFIRGLDALSKRAKLPTVDLPIESVSLSLQDLIGYFHPPDEHLEHEDKQNRLRALKNRQNLFQEEGMINLVLECIDRLHVYSSAAHFADVAGREAGESWKSILNSLYELLAALIRGNRKNCAQFSGSLDWLISRLERLEASSGILEVLHCVLVESPEALNIIKEGHIKSIISLLDKHGRNHKVLDVLCSLCVCHGVAVRSNQHLICDNLLPGRDLLLQTRLVNHVSSMRPNIFLGVSEGSAQYKKWYYELMVDHTEPFVTAEATHLRVGWASTEGYSPYPGGGEEWGGNGVGDDLFSYGFDGLHLWSGCIARTVSSPNQHLLRTDDVISCCLDLSAPSISFRINGQPVQGMFENFNIDGLFFPVVSFSAGIKVRFLLGGRHGEFKFLPPPGYAACYEAVLPKEKLKVEHSREYKQERTYTRDLLGPTVSLTQAAFTPVPVDTSQIVLPPHLERIRERLAENIHELWVMNKIELGWQYGPVRDDNKRQHPCLVEFCKLPEQERNYNLQMSLETLKTLLALGCHVGIADEHAEEKVKKMKLPKNYQLTSGYKPAPMDLSFIKLTPSQEAMVDKLAENAHNVWARDRIRQGWTYGIQQDVKNRRNPRLVPYTLLDDRTKKSNKDSLREAVRTLLGYGYHLEAPDQDHASRAEVCSGTGERFRIFRAEKTYAVKAGRWYFEFEAVTAGDMRVGWSRPGCQPDLELGSDERAFAFDGFKAQRWHQGNEHYGRSWQAGDVVGCMVDMNEHTMMFTLNGEILLDDSGSELAFKDFDVGDGFIPVCSLGVAQVGRMNFGKDVSTLKYFTICGLQEGYEPFAVNTNRDITMWLSKRLPQFLQVPSNHEHIEVTRIDGTIDSSPCLKVTQKSFGSQNSNTDIMFYRLSMPIECAEVFSKSVAGGIPGAGFYGPKNDLEDFDVDSDFEVLMKTAHGHLVPDRMDKDKETPKPEFNNHKDYAQEKPSRLKQRFLLRRTKPDYSTSHSARLTEDVLADDRDDYEYLMQTSTYYYSVRIFPGQEPANVWVGWITSDFHQYDTGFDLDRVRTVTVTLGDEKGKVHESIKRSNCYMVCAGESMSPGQGRNNSNGLEIGCVVDAASGLLTFIANGKELSTYYQVEPSTKLFPAVFAQATSPNVFQFELGRIKNVMPLSAGLFKSEHKNPVPQCPPRLHVQFLSHVLWSRMPNQFLKVDVSRISERQGWLVQCLDPLQFMSLHIPEENRSVDILELTEQEELLQFHYHTLRLYSAVCALGNHRVAHALCSHVDEPQLLYAIENKYMPGLLRAGYYDLLIDIHLSSYATARLMMNNEFIVPMTEETKSITLFPDENKKHGLPGIGLSTSLRPRMCFSSPSFVSISNECYQYSPEFPLDILKAKTIQMLTEAVKEGSLHARDPVGGTTEFLFVPLIKLFYTLLIMGIFHNEDLKHILQLIEPSVFKEAATPEEEGGAPEKEISIDDSKLEVKEEAKAGKRPKEGLLQMKLPEPVKLQMCLLLQYLCDCQVRHRIEAIVAFSDDFVAKLQDNQRFRYNEVMQALNMSAALTARKEFRSPPQEQINMLLNFKDDKSECPCPEEIRDQLLDFHEDLMTHCGIELDEDGSLDGSNDLTIRGRLLSLVEKVTYLKKKQAEKPVASDSRKSSSLQQLISETMVRWAQESVIEDPELVRAMFVLLHRQYDGIGGLVRALPKTYTINGVSVEDTINLLASLGQIRSLLSVRMGKEEEKLMIRGLGDIMNNKVFYQHPNLMRALGMHETVMEVMVNVLGGGESKEITFPKMVANCCRFLCYFCRISRQNQKAMFDHLSYLLENSSVGLASPAMRGSTPLDVAAASVMDNNELALALREPDLEKVVRYLAGCGLQSCQMLVSKGYPDIGWNPVEGERYLDFLRFAVFCNGESVEENANVVVRLLIRRPECFGPALRGEGGNGLLAAMEEAIKIAEDPSRDGPSPTSGSSKTLDAEEEEDDTIHMGNAIMTFYAALIDLLGRCAPEMHLIHAGKGEAIRIRSILRSLIPLGDLVGVISIAFQMPTIAKDGKVVEPDMSAGFCPDHKAAMVLFLDRVYGIEVQDFLLHLLEVGFLPDLRAAASLDTAALSATDMALALNRYLCTAVLPLLTRCAPLFAGTEHHASLIDSLLHTVYRLSKGCSLTKAQRDSIEVCLLSICGQLRPSMMQHLLRRLVFDVPLLNEHAKMPLKLLTNHYERCWKYYCLPGGWSNFGAASEEELHLSRKLFWGIFDALSQKKYEQELFKLALPCLSAVAGALPPDYMESNYVSMMEKQSSMDSEGNFNPQPVDTSNITIPEKLEYFINKYAEHSHDKWSMDKLANGWIYGEIYSDSSKIQPLMKPYKLLSEKEKEIYRWPIKESLKTMLAWGWRIERTREGDSMALYNRTRRISQTSQVSIDAAHGYSPRAIDMSNVTLSRDLHAMAEMMAENYHNIWAKKKKMELESKGGGNHPLLVPYDTLTAKEKAKDREKAQDIFKFLQISGYAVSRGFKDLDLDTPSIEKRFAYSFLQQLIRYVDEAHQYILEFDGGSRSKGEHFPYEQEIKFFAKVVLPLIDQYFKNHRLYFLSAASRPLCTGGHASNKEKEMVTSLFCKLGVLVRHRISLFGNDATSIVNCLHILGQTLDARTVMKTGLDSVKSALRAFLDNAAEDLEKTMENLKQGQFTHTRSQPKGVTQIINYTTVALLPMLSSLFEHIGQHQFGEDLILEDVQVSCYRILTSLYALGTSKSIYVERQRSALGECLAAFAGAFPIAFLETHLDKHNVYSIYNTRSSRERAALSLPANVEDVCPNIPSLEKLMTEIIELAESGIRYTQMPHMMEVVLPMLCSYMSRWWEHGPENHPERAEMCCTALNSEHMNTLLGNILKIIYNNLGIDEGAWMKRLAVFSQPIINKVKPQLLKTHFLPLMEKLKKKAAMVVSEEDHLKAEARGDMSEAELLILDEFTTLARDLYAFYPLLIRFVDYNRAKWLKEPNPEAEELFRMVAEVFIYWSKSHNFKREEQNFVVQNEINNMSFLITDTKSKMSKAAISDQERKKMKRKGDRYSMQTSLIVAALKRLLPIGLNICAPGDQELIALAKNRFSLKDTEEEVRDVIRSNIHLQGKLEDPAIRWQMALYKDLPNRAEDTSDPERTVERVLDIANVLFHLEQVEHPQRSKKAVWHKLLSKQRKRAVVACFRMAPLYNLPRHRAVNLFLQGYEKSWIETEEHYFEDKLIEDLAKPGSELPEEDEAMKRVDPLHQLILLFSRTALTEKCKLEEDFLYMAYADIMAKSCHDEEDDDGEEEVKSFEVTGSQRSKEKEMEKQKLLYQQARLHDRGAAEMVLQTFSASKGETGPMVAATLKLGIAILNGGNSTVQQKMLDYLKEKKDVGFFQSLAGLMQSCSVLDLNAFERQNKAEGLGMVTEEGSGEKVLQDDEFTCDLFRFLQLLCEGHNSDFQNYLRTQTGNNTTVNIIISTVDYLLRVQESISDFYWYYSGKDIIDEQGQRNFSKAIQVAKQVFNTLTEYIQGPCTGNQQSLAHSRLWDAVVGFLHVFAHMQMKLSQDSSQIELLKELMDLQKDMVVMLLSMLEGNVVNGTIGKQMVDMLVESSNNVEMILKFFDMFLKLKDLTSSDTFKEYDPDGKGVISKRDFHKAMESHKHYTQSETEFLLSCAETDENETLDYEEFVKRFHEPAKDIGFNVAVLLTNLSEHMPNDTRLQTFLELAESVLNYFQPFLGRIEIMGSAKRIERVYFEISESSRTQWEKPQVKESKRQFIFDVVNEGGEKEKMELFVNFCEDTIFEMQLAAQISESDLNERSANKEESEKERPEEQAPRMGFFSLLTVQSALFALRYNVLTLVRMLSLKSLKKQMKRMKKMTVKDMVSAFFSSYWSVFVTLLHFVASVCRGFFRIVSSLLLGGSLVEGAKKIKVAELLANMPDPTQDEVRGDEEEGERKPLESALPSEDLTDLKELTEESDLLSDIFGLDLKREGGQYKLIPHNPNAGLSDLMTNPIPVPEVQEKFQEQKVKEEKEGKEETKSEPEKAEGEDGEKEEKAKDDKGKQKLRQLHTHRYGEPEVPESAFWKKIIAYQQKLLNYFARNFYNMRMLALFVAFAINFILLFYKVSTSSVVEGKELPTRTSSDAAKVTTSLDSSPHRIIAVHYVLEESSGYMEPTLRILAILHTIISFFCIIGYYCLKVPLVIFKREKEVARKLEFDGLYITEQPSEDDIKGQWDRLVINTQSFPNNYWDKFVKRKVMDKYGEFYGRDRISELLGMDKAALDFSDAREKKKPKKDSSLSAVLNSIDVKYQMWKLGVVFTDNSFLYLAWYMTMSVLGHYNNFFFAAHLLDIAMGFKTLRTILSSVTHNGKQLVLTVGLLAVVVYLYTVVAFNFFRKFYNKSEDGDTPDMKCDDMLTCYMFHMYVGVRAGGGIGDEIEDPAGDEYEIYRIIFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVKEDMETKCFICGIGNDYFDTVPHGFETHTLQEHNLANYLFFLMYLINKDETEHTGQESYVWKMYQERCWEFFPAGDCFRKQYEDQLN | null | null | calcium ion transmembrane import into cytosol [GO:0097553]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; calcium ion transport into cytosol [GO:0060402]; calcium-mediated signaling [GO:0019722]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cardiac muscle contraction [GO:0060048]; cardiac muscle hypertrophy [GO:0003300]; cellular response to caffeine [GO:0071313]; cellular response to epinephrine stimulus [GO:0071872]; detection of calcium ion [GO:0005513]; embryonic heart tube morphogenesis [GO:0003143]; establishment of localization in cell [GO:0051649]; establishment of protein localization to endoplasmic reticulum [GO:0072599]; intracellular calcium ion homeostasis [GO:0006874]; left ventricular cardiac muscle tissue morphogenesis [GO:0003220]; manganese ion transmembrane transport [GO:0071421]; monoatomic ion transmembrane transport [GO:0034220]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; positive regulation of heart rate [GO:0010460]; positive regulation of sequestering of calcium ion [GO:0051284]; positive regulation of the force of heart contraction [GO:0098735]; Purkinje myocyte to ventricular cardiac muscle cell signaling [GO:0086029]; regulation of atrial cardiac muscle cell action potential [GO:0098910]; regulation of AV node cell action potential [GO:0098904]; regulation of cardiac muscle contraction [GO:0055117]; regulation of cardiac muscle contraction by calcium ion signaling [GO:0010882]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]; regulation of cytosolic calcium ion concentration [GO:0051480]; regulation of heart rate [GO:0002027]; regulation of SA node cell action potential [GO:0098907]; regulation of ventricular cardiac muscle cell action potential [GO:0098911]; release of sequestered calcium ion into cytosol [GO:0051209]; release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0014808]; response to caffeine [GO:0031000]; response to calcium ion [GO:0051592]; response to hypoxia [GO:0001666]; response to magnesium ion [GO:0032026]; response to muscle activity [GO:0014850]; response to muscle stretch [GO:0035994]; response to nutrient [GO:0007584]; response to redox state [GO:0051775]; response to xenobiotic stimulus [GO:0009410]; sarcoplasmic reticulum calcium ion transport [GO:0070296]; striated muscle contraction [GO:0006941]; type B pancreatic cell apoptotic process [GO:0097050]; ventricular cardiac muscle cell action potential [GO:0086005] | A band [GO:0031672]; calcium channel complex [GO:0034704]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; protein-containing complex [GO:0032991]; sarcolemma [GO:0042383]; sarcomere [GO:0030017]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017]; smooth endoplasmic reticulum [GO:0005790]; Z disc [GO:0030018] | calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-induced calcium release activity [GO:0048763]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; intracellularly gated calcium channel activity [GO:0015278]; organic cyclic compound binding [GO:0097159]; protein kinase A catalytic subunit binding [GO:0034236]; protein kinase A regulatory subunit binding [GO:0034237]; protein kinase binding [GO:0019901]; protein self-association [GO:0043621]; ryanodine-sensitive calcium-release channel activity [GO:0005219]; scaffold protein binding [GO:0097110]; suramin binding [GO:0043924] | PF13499;PF08709;PF00520;PF02815;PF08454;PF06459;PF01365;PF21119;PF02026;PF00622; | 1.10.287.70;1.10.490.160;2.60.120.920;2.80.10.50;1.10.238.10;1.25.10.30; | Ryanodine receptor (TC 1.A.3.1) family, RYR2 subfamily | PTM: Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2798 and Ser-2804 increases the open probability of the calcium channel. Phosphorylation is increased in failing heart, leading to calcium leaks and increased cytoplasmic Ca(2+) levels (By similarity). {ECO:0000250}.; PTM: Phosphorylation at Ser-2021 by PKA enhances the response to lumenal calcium. {ECO:0000250}. | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92736}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q92736}; | null | null | null | null | FUNCTION: Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytosol and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca(2+) cytosolic levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity is modulated by formation of heterotetramers with RYR3. Required for cellular calcium ion homeostasis. Required for embryonic heart development. {ECO:0000250|UniProtKB:Q92736, ECO:0000269|PubMed:20431056, ECO:0000269|PubMed:20471962}. | Rattus norvegicus (Rat) |
B0LSW3 | LIS1_FELCA | MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR | null | null | acrosome assembly [GO:0001675]; actin cytoskeleton organization [GO:0030036]; adult locomotory behavior [GO:0008344]; ameboidal-type cell migration [GO:0001667]; auditory receptor cell development [GO:0060117]; brain morphogenesis [GO:0048854]; cell division [GO:0051301]; chemical synaptic transmission [GO:0007268]; cochlea development [GO:0090102]; corpus callosum morphogenesis [GO:0021540]; cortical microtubule organization [GO:0043622]; establishment of mitotic spindle orientation [GO:0000132]; establishment of planar polarity of embryonic epithelium [GO:0042249]; germ cell development [GO:0007281]; hippocampus development [GO:0021766]; interneuron migration [GO:1904936]; JNK cascade [GO:0007254]; layer formation in cerebral cortex [GO:0021819]; learning or memory [GO:0007611]; lipid catabolic process [GO:0016042]; maintenance of centrosome location [GO:0051661]; microtubule cytoskeleton organization involved in establishment of planar polarity [GO:0090176]; microtubule organizing center organization [GO:0031023]; microtubule sliding [GO:0051012]; modulation of chemical synaptic transmission [GO:0050804]; myeloid leukocyte migration [GO:0097529]; negative regulation of JNK cascade [GO:0046329]; neuroblast proliferation [GO:0007405]; neuromuscular process controlling balance [GO:0050885]; nuclear membrane disassembly [GO:0051081]; nuclear migration [GO:0007097]; osteoclast development [GO:0036035]; positive regulation of cytokine-mediated signaling pathway [GO:0001961]; positive regulation of dendritic spine morphogenesis [GO:0061003]; positive regulation of embryonic development [GO:0040019]; protein secretion [GO:0009306]; radial glia-guided pyramidal neuron migration [GO:0140650]; reelin-mediated signaling pathway [GO:0038026]; regulation of microtubule cytoskeleton organization [GO:0070507]; retrograde axonal transport [GO:0008090]; transmission of nerve impulse [GO:0019226]; vesicle transport along microtubule [GO:0047496] | 1-alkyl-2-acetylglycerophosphocholine esterase complex [GO:0008247]; astral microtubule [GO:0000235]; axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cell leading edge [GO:0031252]; centrosome [GO:0005813]; cytoplasmic microtubule [GO:0005881]; glutamatergic synapse [GO:0098978]; kinetochore [GO:0000776]; microtubule associated complex [GO:0005875]; motile cilium [GO:0031514]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; perinuclear region of cytoplasm [GO:0048471]; Schaffer collateral - CA1 synapse [GO:0098685]; stereocilium [GO:0032420] | dynein complex binding [GO:0070840]; identical protein binding [GO:0042802]; microtubule plus-end binding [GO:0051010]; phosphoprotein binding [GO:0051219]; protein heterodimerization activity [GO:0046982] | PF08513;PF00400; | 1.20.960.30;2.130.10.10; | WD repeat LIS1/nudF family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03141}. Nucleus membrane {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane. Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes. {ECO:0000255|HAMAP-Rule:MF_03141}. | null | null | null | null | null | FUNCTION: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition-dependent manner (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos. May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity). {ECO:0000250|UniProtKB:P43033, ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P63005, ECO:0000255|HAMAP-Rule:MF_03141}. | Felis catus (Cat) (Felis silvestris catus) |
B0LT89 | STK24_RAT | MAHSPVQSGLPGMQTLKADPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLDEIQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELAKGEPPHSELHPMKVLFLIPKNNPPTLEGSYSRPLKEFVEACLNKEPSFRPTAKELLKHKFIIRNAKKTSYLTELIDRYKRWKAEQSHEDSSSEDSDVETDSQASGGSDSGDWIFTIREKDPKNLENGTLQPSDLERNKMKDFPKRPFSQCLSTIISPLFAELKEKSQACGGNLGSIEELRGAIYLAEEACPGISDTMVAQLVQRLQRYSLSGGGASAH | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; | cellular response to oxidative stress [GO:0034599]; cellular response to starvation [GO:0009267]; execution phase of apoptosis [GO:0097194]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; negative regulation of cell migration [GO:0030336]; positive regulation of axon regeneration [GO:0048680]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of axon regeneration [GO:0048679]; response to hydrogen peroxide [GO:0042542] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleolus [GO:0005730]; nucleus [GO:0005634] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF20929;PF00069; | 1.10.12.70;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Proteolytically processed by caspases during apoptosis. Proteolytic cleavage results in kinase activation, nuclear translocation of the truncated form (MST3/N) and the induction of apoptosis (By similarity). {ECO:0000250}.; PTM: Oxidative stress induces phosphorylation. Activated by autophosphorylation at Thr-178 and phosphorylation at this site is essential for its function. Manganese, magnesium and cobalt-dependent autophosphorylation is mainly on threonine residues while zinc-dependent autophosphorylation is on both serine and threonine residues (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000250}. Note=The truncated form (MST3/N) translocates to the nucleus. Colocalizes with STK38L in the membrane (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that acts on both serine and threonine residues and promotes apoptosis in response to stress stimuli and caspase activation. Mediates oxidative-stress-induced cell death by modulating phosphorylation of JNK1-JNK2 (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during oxidative stress. Plays a role in a staurosporine-induced caspase-independent apoptotic pathway by regulating the nuclear translocation of AIFM1 and ENDOG and the DNase activity associated with ENDOG. Phosphorylates STK38L on 'Thr-442' and stimulates its kinase activity. In association with STK26 negatively regulates Golgi reorientation in polarized cell migration upon RHO activation. Regulates also cellular migration with alteration of PTPN12 activity and PXN phosphorylation: phosphorylates PTPN12 and inhibits its activity and may regulate PXN phosphorylation through PTPN12 (By similarity). May act as a key regulator of axon regeneration in the optic nerve and radial nerve (PubMed:19855390). Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (By similarity). {ECO:0000250|UniProtKB:Q9Y6E0, ECO:0000269|PubMed:19855390}. | Rattus norvegicus (Rat) |
B0M3E8 | UGE1_PEA | MVASSQKILVTGGAGFIGTHTVVQLLNNGFNVSIIDNFDNSVMEAVERVREVVGSNLSQNLEFTLGDLRNKDDLEKLFSKSKFDAVIHFAGLKAVGESVENPRRYFDNNLVGTINLYEVMAKHNCKKMVFSSSATVYGQPEKIPCVEDFKLQAMNPYGRTKLFLEEIARDIQKAEPEWRIVLLRYFNPVGAHESGKLGEDPRGIPNNLMPYIQQVAVGRLPELNVYGHDYPTRDGSAIRDYIHVMDLADGHIAALRKLFTSENIGCTAYNLGTGRGSSVLEMVAAFEKASGKKIALKLCPRRPGDATEVYASTAKAEKELGWKAKYGVEEMCRDQWNWAKNNPWGYSGKP | 5.1.3.2; 5.1.3.5 | COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250|UniProtKB:Q14376}; | capsule polysaccharide biosynthetic process [GO:0045227]; cell wall organization [GO:0071555]; galactose catabolic process via UDP-galactose [GO:0033499]; UDP-L-arabinose biosynthetic process [GO:0033358] | cytosol [GO:0005829] | UDP-arabinose 4-epimerase activity [GO:0050373]; UDP-glucose 4-epimerase activity [GO:0003978] | PF16363; | 3.40.50.720;3.90.25.10; | NAD(P)-dependent epimerase/dehydratase family | null | null | CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose; Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914; EC=5.1.3.2; Evidence={ECO:0000269|PubMed:19754426}; CATALYTIC ACTIVITY: Reaction=UDP-beta-L-arabinopyranose = UDP-alpha-D-xylose; Xref=Rhea:RHEA:11320, ChEBI:CHEBI:57632, ChEBI:CHEBI:61457; EC=5.1.3.5; Evidence={ECO:0000269|PubMed:19754426}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.29 mM for UDP-galactose {ECO:0000269|PubMed:19754426}; KM=0.31 mM for UDP-glucose {ECO:0000269|PubMed:19754426}; KM=0.15 mM for UDP-xylose {ECO:0000269|PubMed:19754426}; KM=0.16 mM for UDP-arabinose {ECO:0000269|PubMed:19754426}; | PATHWAY: Carbohydrate metabolism; galactose metabolism. {ECO:0000305}.; PATHWAY: Nucleotide-sugar biosynthesis; UDP-L-arabinose biosynthesis; UDP-L-arabinose from UDP-alpha-D-xylose: step 1/1. {ECO:0000305}.; PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9.0. {ECO:0000269|PubMed:19754426}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:19754426}; | FUNCTION: Catalyzes the interconversion between UDP-glucose and UDP-galactose and the interconversion between UDP-arabinose and UDP-xylose. {ECO:0000269|PubMed:19754426}. | Pisum sativum (Garden pea) (Lathyrus oleraceus) |
B0R0I6 | CHD8_DANRE | MADPIMDLFDDTPLFNLDSLPEDAFSQGSSDPVEEALKLALGQVDPPTDPIPDPGVPILSDVVTDPALIPTPVSVPLQNLQTQQLSQIPHEVSVASAPISIQPSLSVASNSSGAATVLLSSSLGVPVSGAQVTPQQQTQQITAVTQQAAGQHAPKIVILKGPQGQTQVLQGVTGATGSPGKVTLARVLTGTPLRPGMAVVSGGTVLNATSPAQGQVKVGTGVQRLVQTANGPMKQVLLTSVPQTQSQVQTQPVQVQIPVQTQLQSPSQPQQLQAQIQAQTQVALQTQAQTQTPTSPAAAGIRPQSVTLSAVPQQVRFVLGSLPGKLVLQGDQLAALAQAKAGQTGAQAKVLTIQLQVQQQPNQQGAKFQLVSGAANAGGSPQVVQISQGQGGQRLAVPLKLLLQPQSNTVSSAGGAVSVVKVINTSAAGSTSGTTTTAASSGVRLAKIQEPVRRVETLCKQEKANRIVAEAIARAKARGERNIPRVLNQDELPAGQTSADLEGAGGATGAKKKGGGGVGGGGGGSKKKSPSAGGAKMVVGGDKKSKAKTPVIPGGGSKSKSKTKLNTITLVGKKRKRNPSSDHSDVDLSPPVSPRTLEEEMSQKRRSNRQVKRKKYTEDLDIKITDDEDELDADVDVTTTPMPAVGHVQPLGAELPPELDGDGLPSMQFFVENPSEEDAAIVDKILSMRVTKKEARQYTNVEEFFVKYKNYSYMHCEWASLEQLERDKRIHQKLKRFKTKQAQMRNLFQEDEEPFNPDYVEVDRILDESHSVDKDNGEPVVYYLVKWCSLPYEDATWELKEDVDEGKVEEFRKIESRQPRLKRTPRPAASAWKKLDESTEYKNGNQLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIALLSEMFSAGVQSPFMIIAPLSTITNWEREFSNWTDMNAIVYHGSLASRQMIQQYEMYCKDDKGHLIPGAYKFDALITTFEMILSDCPELREISWRCVVIDEAHRLKNRNCKLLDSLKMLEIEHKVLLTGTPLQNTVEELFSLLHFLEPAQFPSEIEFLREFGDLKTEEQVQKLQSILKPMMLRRLKEDVEKNLAPKQETIIEVELTDVQKKYYRAILERNFSFLSMGATQNSNVPNLLNTMMELRKCCNHPYLITGAEEKIVSELREVYDPLAPDFHLQALVRSAGKLVLLDKLLPRLKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDRFVFLLCTRAGGLGINLTAADTCVIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMLDKASLKLGLDRAVLQSMSGNKESSIQQFSKKEIEDLLRKGAYAAIMDENDEGSRFCEEDIDQILQRRATTITIESEGKGSTFSKASFVASENRTDIALDDPEFWQKWAKKADIDMDSLNRKNTLVIDTPRVRKQTRQFSSLRGEGGDLSDLDSDDDYPPHNSRQSRASRRSDRHSGGGYGRTDCFRVEKHLLVYGWGRWRDILSHARCKRRLSERDVETICRVILVFCLIHYRGDENIKSFIWELITPPENGREPQALLNHSGLSIPVPRGRKGKRVKAQSSFDVQKVEWIRKYNPDSLLLDDSYRKHLKHQCNKVLLRVRMLYYLKQEVIGEHADSVLSGADARDIDIWLPEMEQQDVPSGWWDAEADRCLLIGVYKHGYEMYTTMRADPCLCFVERCGRPNEQDINAEQQAADPELGEGGDYDKYSEDPEFKPATRHAKEMYEEGDSVNADGEICVEDRSAPMQVEGPSSGSSDLCYWPTSSSLTARLRRLITAYQRSYRREQLKIEAAEKGDRRRRRCEQATKLKEIARQERQQRWTRREECDFYRVVSTFGVERIKKETDAPEGDEHHMDWNRFRSFARLDKKTDESLTRYFKCFMSMCRKVCHIRPGRGDESQDMSQSLAPITEERASRTLYRVTLLCRLRERVLPHPSLEERLSLAPQTSDLPSWWSIPKHDHELLLAAARHGVSRTELSIFSDPLYSFSQSRLDYLQNQQAQAAAQIHAFSQSQDPAGIKEEGLEDESRLLGVEALCPSDSPAMLLSHSDSKVGIQAGWVWKKSKNNGPSERKLGGGGGGASDSDSDSDSGSSSSSRHSGSSDDSGDSDVEREQAALKMCDGDEENSILSLTPSQEGAPPESLTDPLRVDWPKDRILINRIENLCSLVITGHWPSGRRYISDIQLNTVSDEHELGDDLGYSRVARKINSTLSAEALEGQESEFTVKLLKEEGLKLTFSKQALMPNGEGSARKKRKDHELEDAEGVLHAPRRRDLPNWLKENPDYEVEGDMLELLVNRTKRKRRRKRVEKGAALTGSERVKVIDIRTGKKFAGVFGPALQDLREHLEENPDHAVAPEWSETVRHSGFLPEILFHRLLSPHASIPKKSRHYLHTPSLQTDDPLLGGGEGEMLVSDGAYMMDDEDLEDGGHLTSSHHFLTPAYDVKMEPSALDMDGGDSLSQGGYDSSDREAILDDVIMAPKHSDTSSSSED | 3.6.4.12 | null | brain development [GO:0007420]; chromatin remodeling [GO:0006338]; digestive tract development [GO:0048565]; enteric nervous system development [GO:0048484]; forebrain development [GO:0030900]; head development [GO:0060322]; midbrain development [GO:0030901]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of neural precursor cell proliferation [GO:2000178]; positive regulation of DNA-templated transcription [GO:0045893]; Wnt signaling pathway [GO:0016055] | chromatin [GO:0000785]; MLL1 complex [GO:0071339]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; beta-catenin binding [GO:0008013]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; histone binding [GO:0042393]; p53 binding [GO:0002039] | PF07533;PF00385;PF00271;PF00176; | 2.40.50.40;3.40.5.120;1.10.10.60;3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family, CHD8 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03071}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_03071}; | null | null | null | null | FUNCTION: DNA helicase that acts as a chromatin remodeling factor and regulates transcription. Acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. Suppresses p53/tp53-mediated apoptosis by recruiting histone H1 and preventing p53/tp53 transactivation activity. Acts as a negative regulator of Wnt signaling pathway by regulating beta-catenin (ctnnb1) activity. Negatively regulates ctnnb1-targeted gene expression by being recruited specifically to the promoter regions of several ctnnb1 responsive genes. May also act as a transcription activator by participating in efficient U6 RNA polymerase III transcription. {ECO:0000255|HAMAP-Rule:MF_03071}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B0R367 | MPCT_HALS3 | MNITQAYKRSLWWSMDMVGATGSVERKMLTAVGLQFLAAGGMAFLTVFTAGTVQLIGVGGMLALSVVAFYNTYLIAEADFVEPLVALEDAADDIAAGEFERADIPSSKRDDEIASLVASFDGMQSNLEVASRQADALARQAFDDPALDESVPGAFGESITEMADSLEAYTAELEDKTAELEHQQAELERQSEQLRALVDALSEATDAARAGDLTATVDAAALDVTDDHRAAVEDFNQLLETLADTISDIQSFSDAVLAVSRTTDERVDAVADRSAAVSESVTEIADGANQQTNQLNNIAAEMDTVSATVEEIAASANDVAKTAQAAADRGEDGRGEVEETIEALRALREQSQAVAETVESLAAEVERIDGITALIEDIAEETNMLALNASIEAARTGSDGDGFAVVADEVKDLAEETREQAADISEIVDAVTEKAEDASIAIGEVDAEVERKITKAEGVLRDFEAIVDEVANVNHAVQEISDATDQGAQSVTDVVGMVEEVASVSEETAAESDTVADNAAEQTDATDEVADQMDELAEQTAALAGMLDDFTVPADAGTADQSVADDSPTAQPPAADDEPAAAVVDQPQPASDAEDEEGVPDSGGESVAVSDGGWADDRSSFTWADSQ | null | null | chemotaxis [GO:0006935]; signal transduction [GO:0007165] | plasma membrane [GO:0005886] | lysozyme activity [GO:0003796]; transmembrane signaling receptor activity [GO:0004888] | PF00672;PF00015; | 1.10.8.500;1.10.287.950; | Methyl-accepting chemotaxis (MCP) protein family | PTM: Methylated by CheR. {ECO:0000269|PubMed:15752193, ECO:0000269|PubMed:18514223}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15752193}; Multi-pass membrane protein {ECO:0000305|PubMed:15752193}. | null | null | null | null | null | FUNCTION: Mediates bacteriorhodopsin- and halorhodopsin-dependent photoresponses by detecting membrane potential changes. Probably transduces the signal to the histidine kinase CheA. {ECO:0000269|PubMed:15752193}. | Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) |
B0R6I4 | BAST_HALS3 | MSDIDRGLFERVLPARIRGSYAAKFNVLLLVVVIIVAAAGGYIHLQTQSTVGENTERRVSGIAEQQAATLHDWLTQKESTTTFLASNIGGDAVRTSDVKPQLERQLATLQQDVRAIHVVSTSQDTVVASTDDARSGTTLQAGDAPWLSTIEDGTTDVSVSDPYEVDDSPVVAMTAPTDKPGWVLVMTMSLAQHSQSFNSPIATGDVKVVNGDGVITLDNRNRALLEQYTDTAGNVPAAVATARSGQTVYNTEPERTGMDDGRYATAYTPVAGTDWVLTYHVPRGQAYALQSEVTQNLAGLVVVALVGLLLVGLTVGRRTSSALDELAGVAAAIADGDLDTTIPDTDRTDELGQLVGAFGEMQTYLTTAASQADALADQNFDADVLDEDLPGAFGASLSQMHTRLEALITDLDEAREDAEQTRKDAEEARAASERLNERLERRAAEYSDEMAAAAAGDLTRRLDEDVDSEPMQDIAEAFNDMMGDVEATLAQVRSIADAVDAASTDVSTSAAEIRSASDQVSESVQDISADADQQRDRLGTVGDEVTSLSATVEEIAASADDVAETVNQAATESERGQELGEDAVAELERIEATADSAVERVTALEEAVDAIGDVTGVITDIAEQTNMLALNANIEAARADKSGDGFAVVADEVKDLADEVKESATEIETLVDDVQADVADTVADMSELGDRVDAGSETIEAALAALDDIGDQVEAANGSVQSISDATDEQAASTEEVVTMIDEVTDLSDRTATESQQVSAAAEEQAASVSEVAGRADDLDDQVSTLNDLLDQFDARAASADTDEN | null | null | chemotaxis [GO:0006935]; signal transduction [GO:0007165] | plasma membrane [GO:0005886] | lysozyme activity [GO:0003796]; transmembrane signaling receptor activity [GO:0004888] | PF00672;PF00015; | 6.10.340.10;1.10.287.950;3.30.450.20; | Methyl-accepting chemotaxis (MCP) protein family | PTM: Methylated by CheR. {ECO:0000269|PubMed:10672186, ECO:0000269|PubMed:18514223}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10672186}; Multi-pass membrane protein {ECO:0000269|PubMed:10672186}. | null | null | null | null | null | FUNCTION: Mediates chemotaxis towards five attractant amino acids (leucine, isoleucine, valine, methionine and cysteine). Probably transduces the signal from the substrate-binding protein BasB to the histidine kinase CheA. {ECO:0000269|PubMed:10672186, ECO:0000269|PubMed:12006484}. | Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) |
B0R8E4 | CSG_HALS3 | MTDTTGKLRAVLLTALMVGSVIGAGVAFTGGAAAANASDLNDYQRFNENTNYTYSTASEDGKTEGSVASGATIFQGEEDVTFRKLDNEKEVSPATLSRTGGSDEGVPLQMPIPEDQSTGSYDSNGPDNDEADFGVTVQSPSVTMLEVRNNADNDVTGGVLNTQQDESSIAVDYNYYAAEDLELTVEDEDGLDVTDEILAADQSGGAYEDGTGNNGPNTLRFDIDPNNVDAGDYTVSVEGVEDLDFGDATESASVTISSSNKASLNLAEDEVVQGANLKYTIENSPEGNYHAVTIDSSDFRDSSSGADAAKVMRSVGDTVDTGLVVDNDSTTEIVDDYENTSISDVDYAYAIVEIDDGNGVGSIETQYLDDSSADIDLYPASDTEDAPDYVNSNEELTNGSALDGVSTDDDTDFDVTQGDITLDNPTGAYVVGSEVDINGTANEGTDDVVLYARDNNDFELVTVDGEKSIEVDSDDTFEEEDITLSDGDKGGDDILGLPGTYRLGIIAKSDAVNSSGGVKDNIDTSDFNQGVSSTSSIRVTDTELTASFETYNGQVADDDNQIDVEGTAPGKDNVAAIIIGSRGKVKFQSISVDSDDTFDEEDIDISELRQGSASAHILSSGRDGKFGEDTANSISDLEDEVGNYTSGSPTGDQIRDRILSNTVDDTASDDLIVTQQFRLVDGLTTIEATEGGEAGGSLTVMGTTNRKADDNTITVELLQGDASIEINSTDEWNSDGQWSVDVPLSNVEPGNYTVEADDGDNTDRQNVEIVEELEEPDQTTVDQPENNQTMTTTMTETTTETTTEMTTTQENTTENGSEGTSDGESGGSIPGFGVGVALVAVLGAALLALRQN | null | null | cell wall organization [GO:0071555] | extracellular region [GO:0005576]; plasma membrane [GO:0005886]; S-layer [GO:0030115] | null | PF18204; | null | Halobacterial S-layer protein family | PTM: N-linked glycan at Asn-36 consists of a glycosaminoglycan chain, constructed by a repeating sulfated pentasaccharide block composed of GlcNAc, GalNAc, Gal, GalA, 3-O-methyl-GalA, and sulfate in the molar ratio of 1:1:1:1:1:2; the other N-linked glycans contain Glc, GlcA and IdoA. {ECO:0000269|PubMed:3036870}.; PTM: O-linked glycans consist of Glc-Gal disaccharides. {ECO:0000269|PubMed:3036870}.; PTM: The C-terminus (residues 770-778) is lipidated with diphytanylglyceryl phosphate. {ECO:0000269|PubMed:10364251}.; PTM: Cleaved by the archaeosortase ArtA at the C-terminus, with removal of a short hydrophobic segment. {ECO:0000250|UniProtKB:P25062}. | SUBCELLULAR LOCATION: Secreted, cell wall, S-layer {ECO:0000250|UniProtKB:P25062}. Cell membrane {ECO:0000250|UniProtKB:P25062}. | null | null | null | null | null | FUNCTION: S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell. {ECO:0000250|UniProtKB:P25062}. | Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) |
B0RP51 | PFP_XANCB | MTNGNLLYAQSGGVTAVINATAAGVIGEARARKIKVLAARNGILGALREELIDTSKESAAAIAALAQTPGGAFGSCRYKLKSLEQDRAKYERLLEVLRAHDVRWFLYNGGNDSADTALKVSQLAKAFGYPLHCIGVPKTIDNDLAVTDTCPGFGSAAKYTAVSVREAALDVAAMADTSTKVFIYEAMGRHAGWLAAAAGLAGQGPDDAPQIILLPERAFDQAAFLAKVRQMVERVGWCVVVASEGIQDAQGKFVADAGGATDSFGHAQLGGVASFLAAQVKQELGYKVHWTLPDYLQRSARHLASKTDWEQAQAVGKAAVQYALKGMNAVIPVIERVSDAPYRWKIVPAPLHKVANHEKKMPPSFLRKDGFGITERARRYFAPLIKGEAPLAYGSDGLPKYVSLKNVAVAKKLPAWEG | 2.7.1.90 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01978}; | fructose 6-phosphate metabolic process [GO:0006002] | cytoplasm [GO:0005737] | 6-phosphofructokinase activity [GO:0003872]; diphosphate-fructose-6-phosphate 1-phosphotransferase activity [GO:0047334]; metal ion binding [GO:0046872] | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, PPi-dependent PFK group II subfamily, Clade 'B2' sub-subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01978}. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; Evidence={ECO:0000255|HAMAP-Rule:MF_01978, ECO:0000269|PubMed:24508689}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.5 mM for phosphate {ECO:0000269|PubMed:24508689}; KM=41 uM for diphosphate {ECO:0000269|PubMed:24508689}; KM=202 uM for fructose 6-phosphate {ECO:0000269|PubMed:24508689}; KM=24 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:24508689}; Vmax=58 umol/min/mg enzyme for the forward reaction {ECO:0000269|PubMed:24508689}; Vmax=59 umol/min/mg enzyme for the reverse reaction {ECO:0000269|PubMed:24508689}; | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_01978}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8. {ECO:0000269|PubMed:24508689}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:24508689}; | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. {ECO:0000255|HAMAP-Rule:MF_01978, ECO:0000269|PubMed:24508689}. | Xanthomonas campestris pv. campestris (strain B100) |
B0S5G3 | CSTN2_DANRE | MKMRAITAMLLLVLSGQCGILAGKVNKHKPWIETSYHGVITENMDTVMLDPPLVALDKDAPVPYAGEICAFKIHGQEAPFEAEVLNRTSGEGVLRARGPIDCEQQKEYTFIIQAYDCGASPNGADWKKSHKAVVHIQVDDVNEFSPVFREPLYRATVTEGKIYDSILQVEAWDQDCSPQYSQICNYEIVTQDTPFAIDRNGNIRNTERLSFDKQQHYKIMVTAYDCGQKRAMESVPVHIDVKPVCKPGWQGWNKRVDYEPGTGSKQLFPKMHLETCDGPLSSVRAMVELQTSHIGKGCDRETYSEKSLQKLCGAASGSTDLLPAPSTSTNWTASLLTDSGRDSDLIFRFDGRQAANIPDWVVPQNLTDQFTIATWMKHGPSPGLRAEKETLLCNSDKTEMNRHHYSLYVHNCRLVFLLRRDFIQLDSFRPAEFHWRLEQICDKEWHYYVINVEFPSVTLFVDGVTYEPYLVTDDWPIHPSEIDVQLTVGACWQGGEVTTPRFTQYFRGSLSGLTIRPGKIATQKVISCLQACKEGLDISSLESLGKGIKFHFNPAQSVLVMEADDLESINTAMTKVSYINSRQFPTPGLRKLHITTTVQCFGEDTCISIPEIKAMVMVLPPSEPRITIAGVERLVWPSAQLRAPVGVALFKDIHIISTVTKTDATLSIARRPGVLELMHNLDYCDVLVIGEELDPERESLEIHHSSLLGKHLDATNSTSGISIYGVDSMAHYEQAIRQVRYRNWKPGSLSERRFRLSCSELNGRYTSNEFNLEIGVVHSSEAVEHVNHMAVQSQFMRPVHHPLVVHTVNSDHISGTPPAATVVIVMCIAALVVIVVLGIYRIHTTHQDSSKEDEEERKDPEMDWDNSNLNSIEGTQIAEEVREEEPEEDEDEDEEDDDLAGDLSSAESEDSDEDEETNIQKGKVKGKLEWDPSTLPY | null | null | homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; positive regulation of synapse assembly [GO:0051965]; positive regulation of synaptic transmission [GO:0050806] | cell surface [GO:0009986]; dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; postsynaptic membrane [GO:0045211] | amyloid-beta binding [GO:0001540]; calcium ion binding [GO:0005509]; kinesin binding [GO:0019894]; X11-like protein binding [GO:0042988] | PF00028;PF19699; | 2.60.120.200;2.60.40.60; | Calsyntenin family | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9ER65}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9ER65}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9ER65}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9ER65}. Note=Most prominent in the postsynaptic specializations of asymmetric (type I) synapses with both axodendritic and axospinous localization. {ECO:0000250|UniProtKB:Q9ER65}. | null | null | null | null | null | FUNCTION: Postsynaptic adhesion molecule (PubMed:25463516). Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with presynaptic neurexins (By similarity). {ECO:0000250|UniProtKB:Q99JH7, ECO:0000269|PubMed:25463516}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B0S5N4 | PLXA3_DANRE | MRSLWLLVFSFSVLTGTNMAFPMILSERPEVTGSFKVKDTSLTHLTVHRKTGEVFVGAINRVYKLSANLTETRSHQTGPVEDNAKCYPPPSVRACTQKLESTDNVNKLLLVDYAGNRLVACGSIWQGVCQFLRLEDLFKLGEPHHRKEHYLSGAKESDGMAGVVVGDDDGDLKKKKKGGSRLFIGAAIDGKSEYFPTLSSRKLVADEESVNMFSLVYQDEFVSSQIKIPSDTLSQYPAFDIYYVYGFSSRTYIYFLTLQLDTQLTQVDVTGEKFFTSKIVRMCSNDTEFYSYVEFPLGCTKDGVEYRLVQAAYKHRPGKILAQALGLSEDEDVLFVIFSQGQKNRANPPRETVLCLFTLHQINLAMRERIKSCYRGEGKLSLPWLLNKELPCINTPKQIGDDFCGLVLNQPLGGLMVIEGIPLFDDRTDGMASVAAYTYGDHSVVFVGTRSGHLKKIRVNGVPPPSENALLYETVTVVEGSPILRDMVFSPDYQYIYLLSDKQVSRLPVESCSQYSSCKTCLGSGDPHCGWCVLHNKCSRKEACEKWAEPLHFSTELKQCVDITVTPDNMSVTSVSTQLSVKVANVPNLSAGVTCVFEELTESPGEVLAEGQILCMSPSLRDVPSVTQGYGDKRVVKLSLKSKETGLKFITTDFVFYNCSVLQSCSSCVSSPFPCNWCKYRHICTNNVAECSFQEGRVSSAEGCPQILPSSDILVPAGIVRPITLRARNLPQPQSGQKNYECVFNIQGKVQRIPAVRFNSSCIQCQNTSYWYEGNEMGDLPVDFSIVWDGDFPIDKPSSMRALLYKCEAQRDSCGLCLKADSTFECGWCLADKKCLLKQHCPSAEHNWMHQGRRNIRCSHPRITKIRPLTGPKEGGTRVTIEGENLGLQVREITHVRVAGVRCNPAAAEYISAERIVCDMEESLMSSPPGGPVELCIGDCSAEYRTQSTQTYSFVMPSFSRVRPEKGPVSGGTRLTISGRHLDAGSAVTVFLAQEECLFVRRTVREIVCVTPPSASGSGPSSVKLFIDKAEITSDTRYIYTEDPNISTIEPNWSIINGSTSLTVTGTNLLTIQEPKVRAKYGGVETTNICSLVNDSVMTCLAPGIIYTKREAPESGVHPDEFGFILDHVSALLILNGTPFTYYPNPTFEPLGNAGILEVKPGSPIILKGKNLIPPAPGNIRLNYSVTIGETPCLLTVSESQLLCDSPDLTGEQRVMILVGGLEYSPGMLHIYSDSTLTLPAIIGIGAGGGVLLIAIIAVLIAYKRKTRDADRTLKRLQLQMDNLESRVALECKEAFAELQTDIQELTNDMDGVKIPFLEYRTYTMRVMFPGIEEHPVLKELDSPANVEKALRLFSQLLHNKMFLLTFIHTLEAQRSFSMRDRGNVASLLMAALQGRMEYATVVLKQLLADLIEKNLENRNHPKLLLRRTESVAEKMLTNWFTFLLHRFLKECAGEPLFMLYCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIDYKQLTLMCIPPEGEAGTEIPVKVLNCDTITQVKDKLLDAVYKGIPYSQRPQADDMDLEWRQGRLTRIILQDEDVTTKIESDWKRLNTLAHYQVTDGSLVALVQKQVSAYNIANSFTFTRSLSRYESLLRTSSSPDSLRSRAPMITPDQETGTKLWHLVKNHEHADQREGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETVFSTAHRGSALPLAIKYMFDFLDEQADKRQITDPDVRHTWKSNCLPLRFWVNVIKNPQFVFDIHKNSITDACLSVVAQTFMDSCSTSEHRLGKDSPSNKLLYAKDIPNYKSWVERYYRDISKMPSISDQDMDAYLVEQSRLHGNEFNTLSALSELYFYINKYKEEILTALDRDGYCRKHKLRHKLEQAINLMSGSS | null | null | axon extension [GO:0048675]; branching morphogenesis of a nerve [GO:0048755]; cardiac chamber development [GO:0003205]; embryonic skeletal joint morphogenesis [GO:0060272]; motor neuron axon guidance [GO:0008045]; negative regulation of cell adhesion [GO:0007162]; positive regulation of axonogenesis [GO:0050772]; regulation of cell migration [GO:0030334]; regulation of cell shape [GO:0008360]; regulation of collateral sprouting in absence of injury [GO:0048696]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287] | membrane [GO:0016020]; plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116] | identical protein binding [GO:0042802]; semaphorin receptor activity [GO:0017154] | PF08337;PF20170;PF01437;PF01403;PF01833;PF18020;PF17960; | 2.60.40.10;2.130.10.10; | Plexin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Coreceptor for class 3 semaphorins. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm. {ECO:0000269|PubMed:17475806, ECO:0000269|PubMed:17699603}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B0S6J3 | SRGP2_DANRE | MTSPAKFRKDKEIIAEYETQVKEIRAQLVEQLKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRYTKDPQFKKEQNILSPVNCWNLLLAQVKRESRDHATLSDLYLNNIIPRFAQISEDSGRLFKKSKEVGLQLQEDLMKVLNELYTVMKTYHMYNMDSINAESKLKEAEKQEEKQMSRSVRHEEKQTPRSPDSLTNIKIEDKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNSCVFKYYIHDLSDLIDCCDLGYHASLNRALRTYLSAEFNVETSKHGGLETIENAAENLEANSDKQRLMETYNNVFCPPMRFDFQSHMGDMVGHLCAQQPVQGELIQRCQQLQSRLSTLNIENEEVKKTMEATLQTIQDMVTIEDFDVTDCFHHSNSMESVKSTVSESFMSKPSLAKRRANQQETEQFYFTKLKEFLEGRNLITKLQAKHDLIQKTLGESQKTDYCLASGRRDSTVRKQEAIQIIPLMVESCIRFISRHGLHHEGIFRVSGSQVEVNDIKNAFERGEDPLAGDQNDHDMDSIAGVLKLYFRGLENALFPKEVFHDLMSCVSIESLQERAVHIRKVLLSLPSNILVIMRYLFAFLNHLSQYSDDNMMDPYNLAICFGPTLMSVPEGHDQVSCQAHVNELIKTIIIHHESIFPGPRELEGPVYDRGGAPEEYCDSPHIEPPLVDEPAPDTVSVIHNSDDVKSGPLTVSESDPIEAIARFDYSGRTNRELSFKKGASLLLYSRASDDWWEGRHNGTEGLVPHQYIVVQDMPDGYAGRGSPKADLEGSHDSVEEKVSTRASASSPTGGHVADIYLANLNKLRKRPEATSIRRTIRPVEEGSSGAAGGLKTSSMPAGGLAKDSSDKRPVSAHSVLNSITRHSSLKTKVEGPQVRKSTPTGRSKSFSNHRPLDPEVIAQVEHSSQDIEATMNTALSELRELERQSNVKHAPDVVLDTLEQLKSGGTSEPSSPLHSRLLREAESSQHPLQRSASSASDMPSTFRPSKTTGPKSPLSSMTTASGSTFRDNKPPATRPKPVVFPKSSSAGGSPAMGSPTTTIPPTPPPPPPPTDKSCPV | null | null | actin filament severing [GO:0051014]; dendritic spine development [GO:0060996]; filopodium assembly [GO:0046847]; negative regulation of cell migration [GO:0030336]; negative regulation of neuron migration [GO:2001223]; neuron projection morphogenesis [GO:0048812]; podocyte development [GO:0072015]; positive regulation of GTPase activity [GO:0043547]; regulation of cell migration [GO:0030334]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine head [GO:0044327]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211] | GTPase activator activity [GO:0005096]; protein homodimerization activity [GO:0042803]; small GTPase binding [GO:0031267] | PF00611;PF00620;PF00018; | 1.20.1270.60;1.10.555.10;2.30.30.40; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q91Z67}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q91Z67}. Postsynaptic density {ECO:0000250|UniProtKB:Q91Z67}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q91Z67}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O75044}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q91Z67}. Nucleus {ECO:0000250|UniProtKB:D4A208}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q91Z67}. | null | null | null | null | null | FUNCTION: Postsynaptic RAC1 GTPase activating protein (GAP) that plays a key role in neuronal morphogenesis and migration mainly during development of the cerebral cortex. Regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons. Mechanistically, acts by binding and deforming membranes, thereby regulating actin dynamics to regulate cell migration and differentiation. {ECO:0000250|UniProtKB:Q91Z67}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B0S6T2 | S15A2_DANRE | MGKMKDKDVDAEKYEKAQRSPKLCGTNYPVSIAFIVVNEFCERFSYYGMKAVLTLYFMNYLHWDKNLSTAIYHAFSGLCYFTPLLGALIADSWLGKFKTIIYLSIVYVIGHVVKSVGAIPDVGDSTVHIALSMVGLGLIALGTGGIKPCVAAFGGDQFDEDNIDERRKFFSIFYMSINAGSVLSTIITPILRGDVQCFGGDCYALAFGVPAALMVIALVVFISGSGLYKKSPPEGNVLVRVCKCIGFAISNRWTNSKKSPKRSHWLDWAEEKYSKRLIQEIKMVCRVLVLYIPLPMFWALFDQQGSRWTLQATRMNMDFGGGFIIKPDQMQMLNALLILVFIPIFDMGIYPLVGLCRIKLTPLKKMATGMILAALAFCAATAVEVYVIKTVVEPPPAKESLVQVYNLMDSDVTVQFPAHNVFSEPLKPYEEPSGYSSLPLTGESQLQNVVVSHNGMNYQCRLTFTERMAYSLLLHPTAQHNGSVCNLVKDHITKSETGAAYIRFINTHTENINVTVGTEEVHASANYGISRNISVPRGEYNKAVCVTDTKEYEINLGLLDFGAFYTVILSEAGNNLAVKKMEDIQANNIHIGWQIPQYVFLTAGEVMFSITGLEFSYSQAPASMKSVLQAGWLMTVAFGNVIVLIVAEGAGMEQWVEFLLFAALLVAVSIIFSIMAYFYTYVDPDQLDKLFKEDGDGGKVESSKKDELSLGDMPKQTKM | null | null | dipeptide import across plasma membrane [GO:0140206]; innate immune response [GO:0045087]; peptidoglycan transport [GO:0015835]; protein transport [GO:0015031]; regulation of nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0070424]; response to yeast [GO:0001878]; tripeptide import across plasma membrane [GO:0140207] | apical plasma membrane [GO:0016324]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886] | dipeptide transmembrane transporter activity [GO:0071916]; peptide:proton symporter activity [GO:0015333]; tripeptide transmembrane transporter activity [GO:0042937] | PF00854; | 1.20.1250.20; | Major facilitator superfamily, Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q63424}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q16348}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000305|PubMed:16317081}; Multi-pass membrane protein {ECO:0000255}. Note=Associated with the cell membrane in resting macrophages and enriched in phagocytic cups and phagosomes after particle internalization. {ECO:0000250|UniProtKB:Q16348}. | CATALYTIC ACTIVITY: Reaction=a dipeptide(out) + 2 H(+)(out) = a dipeptide(in) + 2 H(+)(in); Xref=Rhea:RHEA:76179, ChEBI:CHEBI:15378, ChEBI:CHEBI:90799; Evidence={ECO:0000269|PubMed:16317081}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76180; Evidence={ECO:0000269|PubMed:16317081}; CATALYTIC ACTIVITY: Reaction=3 H(+)(out) + N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine(out) = 3 H(+)(in) + N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine(in); Xref=Rhea:RHEA:76375, ChEBI:CHEBI:15378, ChEBI:CHEBI:155830; Evidence={ECO:0000250|UniProtKB:Q16348}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76376; Evidence={ECO:0000250|UniProtKB:Q16348}; CATALYTIC ACTIVITY: Reaction=glycyl-L-leucine(out) + 2 H(+)(out) = glycyl-L-leucine + 2 H(+)(in); Xref=Rhea:RHEA:76167, ChEBI:CHEBI:15378, ChEBI:CHEBI:143163; Evidence={ECO:0000250|UniProtKB:Q63424}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76168; Evidence={ECO:0000250|UniProtKB:Q63424}; CATALYTIC ACTIVITY: Reaction=glycyl-L-lysine(out) + 2 H(+)(out) = glycyl-L-lysine(in) + 2 H(+)(in); Xref=Rhea:RHEA:76171, ChEBI:CHEBI:15378, ChEBI:CHEBI:194323; Evidence={ECO:0000250|UniProtKB:Q63424}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76172; Evidence={ECO:0000250|UniProtKB:Q63424}; CATALYTIC ACTIVITY: Reaction=glycyl-L-glutamate(out) + 3 H(+)(out) = glycyl-L-glutamate(in) + 3 H(+)(in); Xref=Rhea:RHEA:76175, ChEBI:CHEBI:15378, ChEBI:CHEBI:73784; Evidence={ECO:0000250|UniProtKB:Q63424}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76176; Evidence={ECO:0000250|UniProtKB:Q63424}; CATALYTIC ACTIVITY: Reaction=2 H(+)(out) + L-alanyl-L-alanine(out) = 2 H(+)(in) + L-alanyl-L-alanine(in); Xref=Rhea:RHEA:76183, ChEBI:CHEBI:15378, ChEBI:CHEBI:195181; Evidence={ECO:0000250|UniProtKB:Q63424}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76184; Evidence={ECO:0000250|UniProtKB:Q63424}; CATALYTIC ACTIVITY: Reaction=an L-amino acid tripeptide(out) + 2 H(+)(out) = an L-amino acid tripeptide(in) + 2 H(+)(in); Xref=Rhea:RHEA:76187, ChEBI:CHEBI:15378, ChEBI:CHEBI:155837; Evidence={ECO:0000250|UniProtKB:Q63424}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76188; Evidence={ECO:0000250|UniProtKB:Q63424}; CATALYTIC ACTIVITY: Reaction=carnosine(out) + 2 H(+)(out) = carnosine(in) + 2 H(+)(in); Xref=Rhea:RHEA:76191, ChEBI:CHEBI:15378, ChEBI:CHEBI:57485; Evidence={ECO:0000250|UniProtKB:Q16348}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76192; Evidence={ECO:0000250|UniProtKB:Q16348}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=97 uM for Gly-L-Gln (at pH 5.5 and -160 mV) {ECO:0000269|PubMed:16317081}; KM=79 uM for Gly-L-Gln (at pH 6.5 and -160 mV) {ECO:0000269|PubMed:16317081}; KM=48 uM for Gly-L-Gln (at pH 7.5 and -160 mV) {ECO:0000269|PubMed:16317081}; KM=163 uM for Gly-L-Gln (at pH 8.5 and -160 mV) {ECO:0000269|PubMed:16317081}; KM=82 uM for Gly-L-Gln (at pH 5.5 and -120 mV) {ECO:0000269|PubMed:16317081}; KM=38 uM for Gly-L-Gln (at pH 6.5 and -120 mV) {ECO:0000269|PubMed:16317081}; KM=18 uM for Gly-L-Gln (at pH 7.5 and -120 mV) {ECO:0000269|PubMed:16317081}; KM=118 uM for Gly-L-Gln (at pH 8.5 and -120 mV) {ECO:0000269|PubMed:16317081}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:16317081}; | null | FUNCTION: Proton-coupled amino-acid transporter that transports oligopeptides of 2 to 4 amino acids with a preference for dipeptides (PubMed:16317081). Transports neutral and anionic dipeptides with a proton to peptide stoichiometry of 2:1 or 3:1 (By similarity). {ECO:0000250|UniProtKB:Q63424, ECO:0000269|PubMed:16317081}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B0TLB9 | FADB_SHEHH | MIYQSPTIEVELLEDNIAHLCFKAQGSVNKFDRETIDSLNAALDSIKQDTSIKALMLSSAKDAFIVGADITEFLGLFAEEDAVLQSWLEQANVVFNKLEDLPFPTLSAINGFALGAGCETILATDFRIADTTARIGLPETKLGIIPGFGGTVRLPRVIGADNALEWITSGKDQRPDAALKVGAIDAVVAPEQLRPAALRMLKDAMAEKLDWQTRRAKKLAPLTLPKLEAMMSFATAKGMVFKIAGKHYPAPMAVISVIEQAAQCGRAEALQIEHQAFIKLAKTEVAQALIGIFLNDQLVKGKAKKAGKLAKKVNSAAVLGAGIMGGGIAYQSASKGTPIVMKDIAQPALDLGLGEAAKLLTAQVKRGRSTPAKMATVLNNITPALDYAPVKDTDIIVEAVVEHPKVKSMVLAEVEEHVSEDAIITSNTSTISINLLAKSLKKPERFCGMHFFNPVHKMPLVEVIRGENSSDETVASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSGLLADGADFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMAEGFPDRMGKSGKDAIDVMFEAERFGQKNNKGFYQYSVDHRGKPKKDLDPTSYELLQAEFGEQKAFESDEIIARTMIPMIIETVRCLEEGIIASPAEADMGLVYGLGFPPFRGGVFRYLDTIGVANFVALADKYAHLGGLYQVTDTMRELAANNGSYYQQA | 1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | fatty acid beta-oxidation multienzyme complex [GO:0036125] | 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF00378; | 1.10.1040.50;3.40.50.720; | Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318, ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521, ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA; Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316; EC=5.1.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}. | null | null | FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. | Shewanella halifaxensis (strain HAW-EB4) |
B0V1P1 | MC4R_DANRE | MNTSHHHGLHHSFRNHSQGALPVGKPSHGDRGSASGCYEQLLISTEIFLTLGLVSLLENILVIAAIVKNKNLHSPMYFFICSLAVADLLVSVSNASETVVMALITGGNLTNRESIIKNMDNVFDSMICSSLLASIWSLLAIAVDRYITIFYALRYHNIMTQRRAGTIITCIWTFCTVSGVLFIVYSESTTVLICLISMFFTMLALMASLYVHMFLLARLHMKRIAALPGNGPIWQAANMKGAITITILLGVFVVCWAPFFLHLILMISCPRNPYCVCFMSHFNMYLILIMCNSVIDPLIYAFRSQEMRKTFKEICCCWYGLASLCV | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; energy homeostasis [GO:0097009]; energy reserve metabolic process [GO:0006112]; negative regulation of feeding behavior [GO:2000252]; regulation of growth [GO:0040008]; regulation of metabolic process [GO:0019222] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | melanocortin receptor activity [GO:0004977]; melanocyte-stimulating hormone receptor activity [GO:0004980] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Receptor specific to the heptapeptide core common to adrenocorticotropic hormone and alpha-, beta-, and gamma-MSH. Plays a central role in energy homeostasis and somatic growth. This receptor is mediated by G proteins that stimulate adenylate cyclase (cAMP). {ECO:0000269|PubMed:23869017}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B0V2N1 | PTPRS_MOUSE | MAPTWSPSVVSVVGPVGLFLVLLARGCLAEEPPRFIREPKDQIGVSGGVASFVCQATGDPKPRVTWNKKGKKVNSQRFETIDFDESSGAVLRIQPLRTPRDENVYECVAQNSVGEITIHAKLTVLREDQLPPGFPNIDMGPQLKVVERTRTATMLCAASGNPDPEITWFKDFLPVDPSASNGRIKQLRSGALQIESSEETDQGKYECVATNSAGVRYSSPANLYVRVRRVAPRFSILPMSHEIMPGGNVNITCVAVGSPMPYVKWMQGAEDLTPEDDMPVGRNVLELTDVKDSANYTCVAMSSLGVIEAVAQITVKSLPKAPGTPVVTENTATSITVTWDSGNPDPVSYYVIEYKSKSQDGPYQIKEDITTTRYSIGGLSPNSEYEIWVSAVNSIGQGPPSESVVTRTGEQAPASAPRNVQARMLSATTMIVQWEEPVEPNGLIRGYRVYYTMEPEHPVGNWQKHNVDDSLLTTVGSLLEDETYTVRVLAFTSVGDGPLSDPIQVKTQQGVPGQPMNLRAEAKSETSIGLSWSAPRQESVIKYELLFREGDRGREVGRTFDPTTAFVVEDLKPNTEYAFRLAARSPQGLGAFTAVVRQRTLQAKPSAPPQDVKCTSLRSTAILVSWRPPPPETHNGALVGYSVRYRPLGSEDPDPKEVNNIPPTTTQILLEALEKWTEYRVTAVAYTEVGPGPESSPVVVRTDEDVPSAPPRKVEAEALNATAIRVLWRSPTPGRQHGQIRGYQVHYVRMEGAEARGPPRIKDIMLADAQEMVITNLQPETAYSITVAAYTMKGDGARSKPKVVVTKGAVLGRPTLSVQQTPEGSLLARWEPPADAAEDPVLGYRLQFGREDAAPATLELAAWERRFAAPAHKGATYVFRLAARGRAGLGEEAAAALSIPEDAPRGFPQILGAAGNVSAGSVLLRWLPPVPAERNGAIIKYTVSVREAGAPGPATETELAAAAQPGAETALTLRGLRPETAYELRVRAHTRRGPGPFSPPLRYRLARDPVSPKNFKVKMIMKTSVLLSWEFPDNYNSPTPYKIQYNGLTLDVDGRTTKKLITHLKPHTFYNFVLTNRGSSLGGLQQTVTARTAFNMLSGKPSVAPKPDNDGFIVVYLPDGQSPVTVQNYFIVMVPLRKSRGGQFPVLLGSPEDMDLEELIQDISRLQRRSLRHSRQLEVPRPYIAARFSILPAVFHPGNQKQYGGFDNRGLEPGHRYVLFVLAVLQKNEPTFAASPFSDPFQLDNPDPQPIVDGEEGLIWVIGPVLAVVFIICIVIAILLYKNKPDSKRKDSEPRTKCLLNNADLAPHHPKDPVEMRRINFQTPGMLSHPPIPITDMAEHMERLKANDSLKLSQEYESIDPGQQFTWEHSNLEANKPKNRYANVIAYDHSRVILQPLEGIMGSDYINANYVDGYRRQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTRLEEKSRIKCDQYWPNRGTETYGFIQVTLLDTMELATFCVRTFSLHKNGSSEKREVRHFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKTEKTVDVYGHVTLMRSQRNYMVQTEDQYGFIHEALLEAVGCGNTEVPARSLYTYIQKLAQVEPGEHVTGMELEFKRLASSKAHTSRFITASLPCNKFKNRLVNILPYESSRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRALWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGAPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKVLRTQRPAMVQTEDEYQFCFQAALEYLGSFDHYAT | 3.1.3.48 | null | cerebellum development [GO:0021549]; cerebral cortex development [GO:0021987]; corpus callosum development [GO:0022038]; establishment of endothelial intestinal barrier [GO:0090557]; hippocampus development [GO:0021766]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of axon extension [GO:0030517]; negative regulation of axon regeneration [GO:0048681]; negative regulation of collateral sprouting [GO:0048671]; negative regulation of dendritic spine development [GO:0061000]; negative regulation of interferon-alpha production [GO:0032687]; negative regulation of interferon-beta production [GO:0032688]; negative regulation of neuron projection development [GO:0010977]; negative regulation of toll-like receptor 9 signaling pathway [GO:0034164]; peptidyl-tyrosine dephosphorylation [GO:0035335]; presynapse assembly [GO:0099054]; regulation of postsynaptic density assembly [GO:0099151]; spinal cord development [GO:0021510]; synapse organization [GO:0050808]; synaptic membrane adhesion [GO:0099560]; trans-synaptic signaling [GO:0099537] | axon [GO:0030424]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734]; receptor complex [GO:0043235]; Schaffer collateral - CA1 synapse [GO:0098685]; synaptic vesicle membrane [GO:0030672] | chondroitin sulfate binding [GO:0035374]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; protein tyrosine phosphatase activity [GO:0004725] | PF00041;PF07679;PF13927;PF00102; | 2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 2A subfamily | PTM: A cleavage occurs, separating the extracellular domain from the transmembrane segment. This process called 'ectodomain shedding' is thought to be involved in receptor desensitization, signal transduction and/or membrane localization (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26231120}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:21454754}. Perikaryon {ECO:0000269|PubMed:21454754}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q64605}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q64605}. Postsynaptic density {ECO:0000250|UniProtKB:Q64605}. Cell projection, neuron projection {ECO:0000269|PubMed:21454754}. Cell projection, growth cone {ECO:0000269|PubMed:21454754}. Note=Is rapidly internalized when dendritic cells are stimulated with the TLR9 ligand cytidine-phosphate-guanosine (CpG) (PubMed:26231120). Detected in a punctate pattern along neurites and axon growth cones (PubMed:21454754). {ECO:0000269|PubMed:21454754, ECO:0000269|PubMed:26231120}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:7529177, ECO:0000305|PubMed:22027896}; | null | null | null | null | FUNCTION: Cell surface receptor that binds to glycosaminoglycans, including chondroitin sulfate proteoglycans and heparan sulfate proteoglycans (PubMed:19833921, PubMed:21454754, PubMed:22406547). Binding to chondroitin sulfate and heparan sulfate proteoglycans has opposite effects on PTPRS oligomerization and regulation of neurite outgrowth (PubMed:21454754). Contributes to the inhibition of neurite and axonal outgrowth by chondroitin sulfate proteoglycans, also after nerve transection (PubMed:15797710, PubMed:19780196, PubMed:19833921, PubMed:21454754, PubMed:22406547, PubMed:22519304). Plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2 (PubMed:21454754). Required for normal brain development, especially for normal development of the pituitary gland and the olfactory bulb (PubMed:10080191). Functions as a tyrosine phosphatase (PubMed:7529177). Mediates dephosphorylation of NTRK1, NTRK2 and NTRK3 (By similarity). Plays a role in down-regulation of signaling cascades that lead to the activation of Akt and MAP kinases (PubMed:15797710). Down-regulates TLR9-mediated activation of NF-kappa-B, as well as production of TNF, interferon alpha and interferon beta (PubMed:26231120). {ECO:0000250|UniProtKB:F1NWE3, ECO:0000269|PubMed:10080191, ECO:0000269|PubMed:15797710, ECO:0000269|PubMed:19780196, ECO:0000269|PubMed:19833921, ECO:0000269|PubMed:21454754, ECO:0000269|PubMed:22406547, ECO:0000269|PubMed:26231120, ECO:0000269|PubMed:7529177}. | Mus musculus (Mouse) |
B0VXE8 | CDK14_CALJA | MSTRNCQGMDSVIKPLDTIPEDKKVRVQRTQSTFDPFEKPTNQVKRVHSENNACINFKTSSTGKESPKVRRHSSPSSPTSPKFGKADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHTDLCQYMDKHPGGLHPDNVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLERIFLVLGTPNEDTWPGVHSLPHFKPERFTLYSSKNLRQAWNKLSYVNHAEDLASKLLQCSPKNRLSAQAALSHEYFSDLPPRLWELTDMSSIFTVPNVRLQPEAGESMRAFGKNNSYGKSLSNSKH | 2.7.11.22 | null | cell division [GO:0051301]; G2/M transition of mitotic cell cycle [GO:0000086]; phosphorylation [GO:0016310]; regulation of canonical Wnt signaling pathway [GO:0060828]; Wnt signaling pathway [GO:0016055] | cytoplasmic cyclin-dependent protein kinase holoenzyme complex [GO:0000308]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Recruited to the cell membrane by CCNY. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase involved in the control of the eukaryotic cell cycle, whose activity is controlled by an associated cyclin. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by mediating the phosphorylation of LRP6 at 'Ser-1490', leading to the activation of the Wnt signaling pathway. Acts as a regulator of cell cycle progression and cell proliferation via its interaction with CCDN3. Phosphorylates RB1 in vitro, however the relevance of such result remains to be confirmed in vivo. May also play a role in meiosis, neuron differentiation and may indirectly act as a negative regulator of insulin-responsive glucose transport (By similarity). {ECO:0000250}. | Callithrix jacchus (White-tufted-ear marmoset) |
B0XMC1 | ER10A_ASPFC | MAIQTTTGLAARLVAKRATFPASRRNFSASRSALKEIQEAYILSGARTPTAKFNGSFVSVSAPELGAVAIKSAVSKSGVPVEKITDVYMGNVLQGAVGQAPARQASMFAGLSPTVESMTVNKVCASGLKAVALAAQNIQLGLAEAQVAGGMENMSRVPYYLPRSTQLPPFGEIKLQDGLIQDGLWDVYNQFHMGICAEKTAKKYEISREEQDQYAIQSYQRAQAAWKENKFAEEIAPVTVKGKKGETVVERDEGYENLRIDKMATLKPAFLRDGTGTVTAGNASTMNDGASALVLGSKAIAREFAQGNRALARIVSTADAAIDPVDFPVAPAKAVPIALERAGITKDQVAVWEFNEAFAAVIKANEKILGLQNARVNPLGGAISLGHALGSSGSRILVTLLHQLQPGEYGVAAICNGGGAATAMVVQKLDRVD | 2.3.1.9 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:Q4WCL5}; | fatty acid beta-oxidation [GO:0006635] | mitochondrion [GO:0005739] | acetyl-CoA C-acetyltransferase activity [GO:0003985]; metal ion binding [GO:0046872] | PF02803;PF00108; | 3.40.47.10; | Thiolase-like superfamily, Thiolase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:32005728}. | CATALYTIC ACTIVITY: Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9; Evidence={ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000269|PubMed:32005728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21037; Evidence={ECO:0000269|PubMed:32005728}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=26 uM for CoA {ECO:0000269|PubMed:32005728}; KM=43 uM for acetoacetyl-CoA {ECO:0000269|PubMed:32005728}; KM=232 uM for acetyl-CoA {ECO:0000269|PubMed:32005728}; | PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3. {ECO:0000269|PubMed:32005728}. | null | null | FUNCTION: Mitochondrial acetyl-CoA acetyltransferase that catalyzes both the formation and degradation of acetoacetyl-CoA (PubMed:32005728). Has no overlapping function with erg10B and seems not to be involved in ergosterol biosynthesis (PubMed:32005728). Plays an important role in growth, morphogenesis and maintaining mitochondrial function including the response to oxidative stresses (PubMed:32005728). {ECO:0000269|PubMed:32005728}. | Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) |
B0XRM8 | ARO1_ASPFC | MTGPTKISILGQESIVADFGLWRNYVAKDLISGCPSTTYVLITDTNIGSIYTPGFQKSFEEAAASVSPSPRLLIYNAPPGEVSKSRQTKADIEDWMLSQSPPCGRDTVVIALGGGVIGDLTGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPSRIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALEDNAETILSAVRREVKPGQRRFEGIEEILKARILASARHKAFVVSADEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLGILKGVAVARIVKCIAAYGLPTSLKDSRIRKLTAGKHCSVDQILFNMALDKKNDGPKKKIVLLSAIGRTYEPRASVVPNEDIGVVLAPSIEVHPGVSTTSEVVCAPPGSKSISNRALVLAALGSGTVRIKNLLHSDDTEVMLNALERLGAATFSWEEEGEVLVVNGKGGALQAHPSPLYLGNAGTASRFLTTVATLATASSVDSSVLTGNNRMKQRPIGDLVDALTANGAQIEYVENKGSLPLKIAASGGFTGGQINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGKPISQPYIDMTTAMMRSFGIDVKKSTTEEHTYHIPQGRYINPAEYVVESDASSATYPLAIAAVTGTTCTIPNIGSKSLQGDARFAVDVLRPMGCTVEQTDTSTTVTGPADGVLRPLPNVDMEPMTDAFLGASVLAAIARGKDSNHTTRIYGIANQRVKECNRIKAMHDELAKFGVVCREHDDGLEIDGIDRSTLRQPAGGVFCYDDHRVAFSFSVLSLIAPKPTLILEKECVGKTWPGWWDTLRQKFAVKLEGKELKEAESPVLTRAEKASASVFIIGMRGAGKTTSGHWVASTLKRPFIDLDDELERIEGMTIPDIIKQRGWQGFRDAELNLLQRTMKERPTGHVFACGGGVVEIPEARKLLIDWHKTKGNVLLIMRDIKQVMAFLNIDKTRPAYVEDMLGVWLRRKPWFQECSNIQYYSQHASAGLPRASEDFARFIKFVTGLEDSLGTIKKKQHSFFVSLTLPDVRGADQILEQACVGSDAVELRVDLLEDPDSSNGIPTVDFVADQISYLRSRITLPVIFTIRTKGQGGRFPDDAHAEAMQLYRLAVRSGCEFVDLEIAFPDEMLRAVTEMKGYSKIIASHHDPNGELSWANMSWMKYYNRALEYGDVIKLVGVARNLDDNTALRKFKNWAEEAHDVPLIAINMGGNGQLSRILNGFMTPVSHPALPFRAAPGQLSATDIRKGLSLMGEIKKKRFALFGSPISESRSPALHNTLFAEMGLPHEYTRLETANVEDVKDFIRAPDFGGASVTIPLKLDIMPLLDEITAEAEIIGAVNTVVPVSDGEGKPQRLVGHNTDWQGMVQCLRNAGAYGADGSASALVVGGGGTSRAAIYALHQMGFSPIYIVGRNPAKLESMVSTFPTSYNIQIVEGNEKLEHVPHVAIGTIPADRPIDPGMREILCHMFERAQEADADASRTIEGSPRVLLEMAYKPRVTALMQLAVDAGWTTIPGLEALIGQGVHQVGLIDLLQMDITDGVQFQHWTGIRPLYERARVCCDILLSGRTMLTCS | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) |
B0XT72 | GEL1_ASPFC | MKASAVTAALAVGASTVLAAPSIKARDDVTPITVKGNAFFKGDERFYIRGVDYQPGGSSDLADPIADADGCKRDIAKFKELGLNTIRVYSVDNSKNHDECMNALADAGIYLVLDVNTPKYSINRAKPKESYNDVYLQYIFATVDAFAGYKNTLAFFSGNEVINDGPSSSAAPYVKAVTRDLRQYIRSRKYREIPVGYSAADIDTNRLQMAQYMNCGSDDERSDFFAFNDYSWCDPSSFKTSGWDQKVKNFTGYGLPLFLSEYGCNTNKRQFQEVSSLYSTDMTGVYSGGLVYEYSQEASNYGLVEISGNNVKELPDFDALKTAFEKTSNPSGDGNYNKTGGANPCPAKDAPNWDVDNDALPAIPEPAKKYMTEGAGKGPGFAGPGSQDRGTQSTATAEPGSGSATGSSSSGTSTSSKGAAAGLTVPSLTMAPVVVGAVTLLSTVFGAGLVLL | 2.4.1.- | null | fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process [GO:0071970]; fungal-type cell wall organization [GO:0031505] | plasma membrane [GO:0005886]; side of membrane [GO:0098552] | 1,3-beta-glucanosyltransferase activity [GO:0042124] | PF03198; | 3.20.20.80; | Glycosyl hydrolase 72 family | PTM: The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined. | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. Active from pH 2.5 to 6.0. {ECO:0000269|PubMed:8900166}; | null | FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall morphogenesis. {ECO:0000269|PubMed:10769178, ECO:0000269|PubMed:10809732, ECO:0000269|PubMed:8900166}. | Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) |
B0Y0P7 | UBA4_ASPFC | MENLEQTCASLRAQIAATEAQLAGLKRELEIAEQAAEVKAQSTTRTITAEDGKTNETREWPLLSEEYKRYGRQMIVPQLGLQGQLKLRAARVLIVGAGGLGCPAALYLAGAGVGTLGLVDGDTVENSNLHRQVLHSSKNVGTFKVDSAIEYLRELNPHPTYVPYRAHLTPQEAPGIFKDYDIVLDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLMVLNYPPRPVGDKSGGPCYRCVFPKPPPANSVVSCADGGILGPVVGTMGVLQALEAIKVITSPAVNPSASPPSLLIFSAYSTPLFRTIRLRARRANCAVCSADASVTLETLKNGSTDYVFFCGVAGLEATLSPEERISPLEFKKRHPKEVPQDGGRINKEPTIIDVREKVQFDICSLENSINIPISTILSSASSPTNVDANAQPSLPFWLPRELASADSTDPIYVVCRHGNDSQIAVRRLKELGLDRGGQRYVGDIQGGLRAWREQIDPDWPEY | 2.7.7.80; 2.8.1.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049}; | cell budding [GO:0007114]; cellular response to oxidative stress [GO:0034599]; invasive growth in response to glucose limitation [GO:0001403]; Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein urmylation [GO:0032447]; regulation of pseudohyphal growth [GO:2000220]; tRNA wobble position uridine thiolation [GO:0002143] | cytosol [GO:0005829] | AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; sulfotransferase activity [GO:0008146]; thiosulfate sulfurtransferase activity [GO:0004792]; URM1 activating enzyme activity [GO:0042292] | PF00581;PF00899; | 3.40.50.720;3.40.250.10; | HesA/MoeB/ThiF family, UBA4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}. | CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618, ChEBI:CHEBI:90778; EC=2.7.7.80; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:48612, Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12160, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619, ChEBI:CHEBI:456215; EC=2.8.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.; PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}. | null | null | FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions (By similarity). {ECO:0000250}. | Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) |
B0Y3B5 | SKP1_ASPFC | MTTVTLTSSDGVDITVDRDVAERSILIKNMLEDLGESDEAIPIPNVNEVVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE | null | null | exit from mitosis [GO:0010458]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; kinetochore assembly [GO:0051382]; mitotic nuclear membrane biogenesis [GO:0101026]; negative regulation of cytoplasmic translation [GO:2000766]; negative regulation of mitotic metaphase/anaphase transition [GO:0045841]; positive regulation of glucose transmembrane transport [GO:0010828]; protein neddylation [GO:0045116]; protein ubiquitination [GO:0016567]; regulation of DNA recombination [GO:0000018]; regulation of exit from mitosis [GO:0007096]; regulation of protein-containing complex assembly [GO:0043254]; resolution of meiotic recombination intermediates [GO:0000712]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; septin ring assembly [GO:0000921]; silent mating-type cassette heterochromatin formation [GO:0030466]; vacuolar acidification [GO:0007035]; vacuolar proton-transporting V-type ATPase complex assembly [GO:0070072] | CBF3 complex [GO:0031518]; kinetochore [GO:0000776]; nuclear SCF ubiquitin ligase complex [GO:0043224]; RAVE complex [GO:0043291]; single-stranded DNA-dependent ATP-dependent DNA helicase complex [GO:0017117] | cullin family protein binding [GO:0097602]; DNA replication origin binding [GO:0003688]; ubiquitin protein ligase activity [GO:0061630] | PF01466;PF03931; | null | SKP1 family | null | null | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor (By similarity). {ECO:0000250}. | Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) |
B0Y4X4 | MPKA_ASPFC | MSDLQGRKVFKVFNQDFIVDERYNVTKELGQGAYGIVCAATNVHTGEGVAIKKVTNVFSKKILAKRALREIKLLQHFRGHRNITCLYDMDIPRPDNFNETYLYEELMECDLAAIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSIDPEENAGYMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGGRPFFKGRDYVDQLNQILHYLGTPNEETLSRIGSPRAQEYVRNLPFMPKIPFQRLFPNANPDALDLLDRMLAFDPASRISVEEALEHPYLHIWHDASDEPTCPTTFDFHFEVVDDVQEMRKMIYDEVVRFRNLVRQQSQAQAAAAAQQQQQQIAQQTNVPIPDHQQGGWKQEEPKPQEVHAAGGHVNDLESSLQRGMDVQ | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:17981060}; | negative regulation of glucose mediated signaling pathway [GO:1902660]; negative regulation of mitotic cytokinesis [GO:1902413]; phosphorylation [GO:0016310]; positive regulation of calcium ion import across plasma membrane [GO:1905665]; positive regulation of calcium-mediated signaling [GO:0050850] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Phosphorylated during cell wall stress by the upstream MAPKK mkk2 (PubMed:17981060). Iron starvation triggers phosphorylation and thus activation of mpkA (PubMed:21883519). Phosphorylation increases upon osmotic stress and cell wall damage and depends on mpkC and sakA (PubMed:26878695). {ECO:0000269|PubMed:17981060, ECO:0000269|PubMed:21883519, ECO:0000269|PubMed:26878695}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21883519}. Note=Accumulates in the nucleus under iron depletion conditions. {ECO:0000269|PubMed:21883519}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000305|PubMed:17981060}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000305|PubMed:17981060}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000305|PubMed:17981060}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000255|RuleBase:RU361165}; | null | null | null | null | FUNCTION: Mitogen-activated kinase (MAPK), part of the cell wall integrity (CWI) signaling pathway composed by three protein kinases bck1, mkk2 and mpkA and responsible for the maintaining of cell-wall integrity balance (PubMed:17981060, PubMed:19715768). The CWI pathway regulates also the oxidative stress response, as well as the production of some secondary metabolites including gliotoxin, pyomelanin, pseurotin A, fumiquinazoline C or dihydroxynaphthalene (DHN)-melanin (PubMed:19715768, PubMed:21883519, PubMed:30914505, PubMed:33705521). MpkA directly phosphorylates the fumiquinazoline C biosynthesis cluster nonribosomal peptide synthetase fmqC during conidiation (PubMed:33705521). Mpka is also required for adaptation to iron starvation and regulates the expression of genes involved in siderophore biosynthesis in a hapX/sreA-independent manner (PubMed:21883519). {ECO:0000269|PubMed:17981060, ECO:0000269|PubMed:19715768, ECO:0000269|PubMed:21883519, ECO:0000269|PubMed:30914505, ECO:0000269|PubMed:33705521}. | Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) |
B0YA65 | ER10B_ASPFC | MSSLPAVYIVSSARTPVGSFLGSLSSLTAPQLGAHAIKAALAKVDGLKPSDVQEVFFGNVISANVGQNPARQCALGAGLEESTICTTVNKVCASGLKAIILGAQTIMTGNADVVVAGGTESMSNAPHYLPNLRTGAKYGHQSLVDGIMKDGLTDAGKQELMGLQAEECAQDHGFSREQQDEYAIRTYEKAQAAQKAGLFDEEIAPIQLPGFRGKPDVTVTQDEEPKNLNPEKLRAIKPAFIPGSGTVTAPNSSPLNDGAAAVVLVSEAKLKELNLKPVAKILGWGDAAQQPSKFTTAPALAIPKALKHAGVGQDAIDAFEINEAFSVVALANMKLLGIPEEKVNLHGGAVAIGHPIGASGARILTTLLGVLKAKKGKLGCAGICNGGGGASALVVELL | 2.3.1.9 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000269|Ref.5}; | ergosterol biosynthetic process [GO:0006696]; fatty acid beta-oxidation [GO:0006635] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | acetyl-CoA C-acetyltransferase activity [GO:0003985]; metal ion binding [GO:0046872] | PF02803;PF00108; | 3.40.47.10; | Thiolase-like superfamily, Thiolase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:32005728}. | CATALYTIC ACTIVITY: Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9; Evidence={ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000269|Ref.5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21037; Evidence={ECO:0000269|Ref.5}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=42 uM for acetoacetyl-CoA (in law salt conditions) {ECO:0000269|Ref.5}; KM=8 uM for acetoacetyl-CoA (in the presence of 100 mM NaCl) {ECO:0000269|Ref.5}; KM=8 uM for acetoacetyl-CoA (in the presence of 100 mM KCl) {ECO:0000269|Ref.5}; | PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3. {ECO:0000269|Ref.5}. | null | null | FUNCTION: Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (Probable) (PubMed:32005728). In this module, the cytosolic acetyl-CoA acetyltransferase erg10B catalyzes the formation of acetoacetyl-CoA (PubMed:32005728). The hydroxymethylglutaryl-CoA synthases AFUA_8G07210 and AFUA_3G10660 then condense acetyl-CoA with acetoacetyl-CoA to form HMG-CoA (Probable). The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hmg1 and hmg2 (PubMed:22106303, PubMed:30940706). Mevalonate is also a precursor for the extracellular siderophore triacetylfusarinine C (TAFC) (PubMed:22106303). {ECO:0000269|PubMed:22106303, ECO:0000269|PubMed:30940706, ECO:0000269|PubMed:32005728, ECO:0000305|PubMed:16110826}. | Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) |
B0YJ81 | HACD1_HUMAN | MGRLTEAAAAGSGSRAAGWAGSPPTLLPLSPTSPRCAATMASSDEDGTNGGASEAGEDREAPGERRRLGVLATAWLTFYDIAMTAGWLVLAIAMVRFYMEKGTHRGLYKSIQKTLKFFQTFALLEIVHCLIGIVPTSVIVTGVQVSSRIFMVWLITHSIKPIQNEESVVLFLVAWTVTEITRYSFYTFSLLDHLPYFIKWARYNFFIILYPVGVAGELLTIYAALPHVKKTGMFSIRLPNKYNVSFDYYYFLLITMASYIPLFPQLYFHMLRQRRKVLHGEVIVEKDD | 4.2.1.134 | null | cementum mineralization [GO:0071529]; fatty acid elongation [GO:0030497]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; positive regulation of cell-substrate adhesion [GO:0010811]; protein-containing complex assembly [GO:0065003]; sphingolipid biosynthetic process [GO:0030148]; very long-chain fatty acid biosynthetic process [GO:0042761] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | 3-hydroxyacyl-CoA dehydratase activity [GO:0018812]; enzyme binding [GO:0019899]; hydroxyapatite binding [GO:0046848]; very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase activity [GO:0102158] | PF04387; | null | Very long-chain fatty acids dehydratase HACD family | PTM: N-glycosylated. {ECO:0000269|PubMed:23933735}. | SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18554506}; Multi-pass membrane protein {ECO:0000269|PubMed:18554506}. | CATALYTIC ACTIVITY: Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:45812, ChEBI:CHEBI:15377, ChEBI:CHEBI:83728, ChEBI:CHEBI:85440; EC=4.2.1.134; Evidence={ECO:0000269|PubMed:18554506, ECO:0000269|PubMed:23933735}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45813; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexadecanoyl-CoA = (2E)-hexadecenoyl-CoA + H2O; Xref=Rhea:RHEA:39159, ChEBI:CHEBI:15377, ChEBI:CHEBI:61526, ChEBI:CHEBI:74278; Evidence={ECO:0000269|PubMed:18554506}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39160; Evidence={ECO:0000305|PubMed:18554506}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyoctadecanoyl-CoA = (2E)-octadecenoyl-CoA + H2O; Xref=Rhea:RHEA:39155, ChEBI:CHEBI:15377, ChEBI:CHEBI:71412, ChEBI:CHEBI:76374; Evidence={ECO:0000269|PubMed:18554506}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39156; Evidence={ECO:0000305|PubMed:18554506}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyeicosanoyl-CoA = (2E)-eicosenoyl-CoA + H2O; Xref=Rhea:RHEA:39175, ChEBI:CHEBI:15377, ChEBI:CHEBI:74691, ChEBI:CHEBI:76373; Evidence={ECO:0000269|PubMed:18554506}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39176; Evidence={ECO:0000305|PubMed:18554506}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydocosanoyl-CoA = (2E)-docosenoyl-CoA + H2O; Xref=Rhea:RHEA:39187, ChEBI:CHEBI:15377, ChEBI:CHEBI:74692, ChEBI:CHEBI:76375; Evidence={ECO:0000269|PubMed:18554506}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39188; Evidence={ECO:0000305|PubMed:18554506}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + H2O; Xref=Rhea:RHEA:39199, ChEBI:CHEBI:15377, ChEBI:CHEBI:74693, ChEBI:CHEBI:76377; Evidence={ECO:0000269|PubMed:18554506}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39200; Evidence={ECO:0000305|PubMed:18554506}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexacosanoyl-CoA = (2E)-hexacosenoyl-CoA + H2O; Xref=Rhea:RHEA:39211, ChEBI:CHEBI:15377, ChEBI:CHEBI:74281, ChEBI:CHEBI:76378; Evidence={ECO:0000269|PubMed:18554506}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39212; Evidence={ECO:0000305|PubMed:18554506}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=33.6 uM for 3-hydroxypalmitoyl-CoA (at 37 degrees Celsius) {ECO:0000269|PubMed:18554506}; | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000269|PubMed:18554506}. | null | null | FUNCTION: [Isoform 1]: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000269|PubMed:18554506}.; FUNCTION: [Isoform 2]: In tooth development, may play a role in the recruitment and the differentiation of cells that contribute to cementum formation. May also bind hydroxyapatite and regulate its crystal nucleation to form cementum. {ECO:0000269|PubMed:22067203}. | Homo sapiens (Human) |
B0ZB55 | OMT1_HUMLU | MESLRGQEQIWQLMFSFVDSMALKCAIELRIADIIHSHGKPITLSQIASGIRSNSNSSISPNIPYLSRIMRFLVRKNIFTEHQEDNDEVISLYGLSDSSRWLLRDFKSSLAPMVLMQTHPLSMAVWHFLEDYVRNSSNTFEKAHGCNIWEFSSANPDFNKIFNNAMASIVPIYMGAVLSSYKDGLGCIKGTVVDVGGGTGGSISELMKYYPNIKGINFDLPHVIATAPALDGVTHISGDIFESIPSADAVLMKGVLHCFSDEKCVKVLRNCRKAITDKKNGKIIILEIVLDPTSNQIFDETRMVYDLLIPLFSGGKERTELEWKRLLNEAGFTSIKITKIPIIPAIIEAFLV | 2.1.1.338 | null | melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259] | cytoplasm [GO:0005737] | acetylserotonin O-methyltransferase activity [GO:0017096]; protein dimerization activity [GO:0046983] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29760092}. | CATALYTIC ACTIVITY: Reaction=desmethylxanthohumol + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + xanthohumol; Xref=Rhea:RHEA:51696, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134289, ChEBI:CHEBI:134302; EC=2.1.1.338; Evidence={ECO:0000269|PubMed:18223037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51697; Evidence={ECO:0000269|PubMed:18223037}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + xanthogalenol = 4'-O-methylxanthohumol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51700, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134308, ChEBI:CHEBI:134309; EC=2.1.1.338; Evidence={ECO:0000269|PubMed:18223037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51701; Evidence={ECO:0000269|PubMed:18223037}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 uM for desmethylxanthohumol {ECO:0000269|PubMed:18223037}; KM=286 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18223037}; Vmax=55 pmol/sec/mg enzyme toward desmethylxanthohumol {ECO:0000269|PubMed:18223037}; Vmax=56 pmol/sec/mg enzyme toward S-adenosyl-L-methionine {ECO:0000269|PubMed:18223037}; | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:30468448}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:18223037}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-37 degrees Celsius.; | FUNCTION: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the biosynthesis of xanthohumol (PubMed:18223037). Methylates desmethylxanthohumol and xanthogalenol, but not caffeic acid, prenylflavanones, simple phenols or phenylpropanoids (PubMed:18223037). {ECO:0000269|PubMed:18223037, ECO:0000305|PubMed:30468448}. | Humulus lupulus (European hop) |
B0ZB56 | OMT2_HUMLU | MELARNDQTEAALRGEANVWKSINGIADFMVMKCALELRIPDIVHSHSAPITLAQIASSVPDSPSLNLSYLSRIMRLLVRRKIFSQHKSLDGEEVLYGPTHSSRLLLSKTTLPDQVTLAPFVAFMTHPYLSAPWSCLARCVKEGGNGFEMVHGGRQLWDLSPGNPEFNKVFNDGMASTARITTMAILSEYRDVFCGICSLVDVGGEFGGSISAIVKSHPHIKGINYDLPHVVATAPTYTGLVSHVGGNMFEWIPTAVAVFMKWILHDWADEDCVKILKNCRRAMPEKGGKIIIVDIVLEPEGNGLFDDAAVMLDIALMALTRGKERTEKEWKRVLEEGGFPRYQILKIPALTSVIEAYPQ | 2.1.1.154; 2.1.1.338; 2.1.1.339 | null | melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259] | cytoplasm [GO:0005737] | acetylserotonin O-methyltransferase activity [GO:0017096]; isoliquiritigenin 2'-O-methyltransferase activity [GO:0033802]; protein dimerization activity [GO:0046983] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0ZB55}. | CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + xanthohumol = 4-O-methylxanthohumol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51704, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134289, ChEBI:CHEBI:139273; EC=2.1.1.339; Evidence={ECO:0000269|PubMed:18223037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51705; Evidence={ECO:0000269|PubMed:18223037}; CATALYTIC ACTIVITY: Reaction=desmethylxanthohumol + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + xanthohumol; Xref=Rhea:RHEA:51696, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134289, ChEBI:CHEBI:134302; EC=2.1.1.338; Evidence={ECO:0000269|PubMed:18223037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51697; Evidence={ECO:0000269|PubMed:18223037}; CATALYTIC ACTIVITY: Reaction=isoliquiritigenin + S-adenosyl-L-methionine = 2'-O-methylisoliquiritigenin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:21608, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77948, ChEBI:CHEBI:519567; EC=2.1.1.154; Evidence={ECO:0000269|PubMed:18223037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21609; Evidence={ECO:0000269|PubMed:18223037}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + trans-resveratrol = 3-methoxy-4',5-dihydroxy-trans-stilbene + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32111, ChEBI:CHEBI:15378, ChEBI:CHEBI:45713, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:63672; Evidence={ECO:0000269|PubMed:18223037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32112; Evidence={ECO:0000269|PubMed:18223037}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=237 uM for chalconaringenin {ECO:0000269|PubMed:18223037}; KM=23 uM for desmethylxanthohumol {ECO:0000269|PubMed:18223037}; KM=31 uM for xanthohumol {ECO:0000269|PubMed:18223037}; KM=19 uM for resveratrol {ECO:0000269|PubMed:18223037}; KM=34 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18223037}; Vmax=914 pmol/sec/mg enzyme with chalconaringenin as substrate {ECO:0000269|PubMed:18223037}; Vmax=468 pmol/sec/mg enzyme with desmethylxanthohumol as substrate {ECO:0000269|PubMed:18223037}; Vmax=451 pmol/sec/mg enzyme with xanthohumol as substrate {ECO:0000269|PubMed:18223037}; Vmax=908 pmol/sec/mg enzyme with resveratrol as substrate {ECO:0000269|PubMed:18223037}; Vmax=402 pmol/sec/mg enzyme toward S-adenosyl-L-methionine {ECO:0000269|PubMed:18223037}; | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:30468448}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:18223037}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 39 degrees Celsius. {ECO:0000269|PubMed:18223037}; | FUNCTION: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). O-methyltransferase with a low substrate selectivity (PubMed:18223037). Methylates chalconaringenin, desmethylxanthohumol, xanthohumol, isoliquiritigenin, butein, 2',4-dihydroxychalcone, resveratrol, genistein and guaiacol (PubMed:18223037). Catalyzes the biosynthesis of 2',4'-dihydroxy-4,6'-dimethoxy-3'-prenylchalcone (4-O-methylxanthohumol) (PubMed:18223037). {ECO:0000269|PubMed:18223037, ECO:0000305|PubMed:30468448}. | Humulus lupulus (European hop) |
B1A612 | MENC_GEOKU | MAINIEYVILRHLQMELKAPFTTSFGTFQTKEFILVEVVDCDGVSGWGESVAFSVPWYSEETVKTNWHMLEEFLVPLLFSKPLRHPAELPERFAAIRQNNMAKAALEGAVWDLYAKRLGVPLCQALGGTKKEIEVGVSIGIQPTVDDLLQVIERYVAQGYRRIKVKIKPGWDVDVIRDVRRAFPDVPLMADANSAYTLADAKRLQALDEFGLMMIEQPLAADDLVDHARLQPLLKTPICLDESIRSYDDARKALDLGSCRIINIKIGRVGGLWEAKRIHDLCAERGVPVWCGGMLEAGVGRAHNIAITTLENFALPGDTAASSHYWERDIITPEVEVHNGLIRVPNAPGIGYDVDRRQVERYTQFAKLFHRTATA | 4.2.1.113; 5.1.1.- | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000269|Ref.1}; Note=Shows highest activity in vitro with Co(2+), Mn(2+) and Ni(2+). {ECO:0000269|Ref.1}; | menaquinone biosynthetic process [GO:0009234] | null | isomerase activity [GO:0016853]; magnesium ion binding [GO:0000287]; O-succinylbenzoate synthase activity [GO:0043748] | PF13378;PF02746; | 3.20.20.120;3.30.390.10; | Mandelate racemase/muconate lactonizing enzyme family, MenC type 2 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H2O; Xref=Rhea:RHEA:10196, ChEBI:CHEBI:15377, ChEBI:CHEBI:18325, ChEBI:CHEBI:58689; EC=4.2.1.113; Evidence={ECO:0000255|HAMAP-Rule:MF_01933}; CATALYTIC ACTIVITY: Reaction=N(alpha)-acetyl-D-methionine = N(alpha)-acetyl-L-methionine; Xref=Rhea:RHEA:59960, ChEBI:CHEBI:71670, ChEBI:CHEBI:85220; Evidence={ECO:0000269|PubMed:25875730, ECO:0000269|Ref.1}; CATALYTIC ACTIVITY: Reaction=N-acetyl-D-phenylalanine = N-acetyl-L-phenylalanine; Xref=Rhea:RHEA:62772, ChEBI:CHEBI:57702, ChEBI:CHEBI:143878; Evidence={ECO:0000269|Ref.1}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.12 mM for N-succinyl-L-alanine {ECO:0000269|Ref.1}; KM=0.13 mM for N-succinyl-D-alanine {ECO:0000269|Ref.1}; KM=0.13 mM for N-succinyl-L-phenylalanine {ECO:0000269|Ref.1}; KM=0.04 mM for N-succinyl-D-phenylalanine {ECO:0000269|Ref.1}; KM=8 mM for N-acetyl-L-methionine {ECO:0000269|Ref.1}; KM=7 mM for N-acetyl-D-methionine {ECO:0000269|Ref.1}; KM=43 mM for N-acetyl-L-phenylalanine {ECO:0000269|Ref.1}; KM=23 mM for N-acetyl-D-phenylalanine {ECO:0000269|Ref.1}; KM=5 mM for N-carbamoyl-L-methionine {ECO:0000269|Ref.1}; KM=2 mM for N-carbamoyl-D-methionine {ECO:0000269|Ref.1}; Note=kcat is 43 sec(-1) with N-succinyl-L-alanine as substrate. kcat is 15 sec(-1) with N-succinyl-D-alanine as substrate. kcat is 5 sec(-1) with N-succinyl-L-phenylalanine as substrate. kcat is 2 sec(-1) with N-succinyl-D-phenylalanine as substrate. kcat is 22 sec(-1) with N-acetyl-L-methionine as substrate. kcat is 20 sec(-1) with N-acetyl-D-methionine as substrate. kcat is 16 sec(-1) with N-acetyl-L-phenylalanine as substrate. kcat is 10 sec(-1) with N-acetyl-D-phenylalanine as substrate. kcat is 2 sec(-1) with N-carbamoyl-L-methionine as substrate. kcat is 2 sec(-1) with N-carbamoyl-D-methionine as substrate. {ECO:0000269|Ref.1}; | PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_01933}.; PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01933}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|Ref.1}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|Ref.1}; | FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (By similarity). Also acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of various N-succinylamino acids, including N-succinyl-alanine and N-succinyl-phenylalanine (Ref.1). Can catalyze the racemization of a broad range of N-acylamino acids, including N-acetyl-methionine, N-acetyl-phenylalanine, N-carbamoyl-methionine, N-formyl-D-methionine, N-formyl-D-norleucine and N-carbamoyl-D-norleucine (PubMed:25875730, Ref.1). May be a bifunctional enzyme involved in menaquinone biosynthesis and in an irreversible pathway for the conversion of D- to L-amino acids, thereby facilitating the survival and/or growth of the organism (By similarity). {ECO:0000250|UniProtKB:Q5L1G9, ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000269|PubMed:25875730, ECO:0000269|Ref.1}. | Geobacillus kaustophilus |
B1A8Z2 | CIB1_SHEEP | MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPQEHRSVEESLQARVSLEQILSLPELKANPFKERICKVFSTSPSRDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLNREDLSQLVNCLTGESEDTRLSASEMKQLIDNILEESDIDRDGTINLSEFQHVISRSPDFASSFKIVL | null | null | angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cell division [GO:0051301]; cellular response to growth factor stimulus [GO:0071363]; integrin-mediated signaling pathway [GO:0007229]; positive regulation of calcineurin-NFAT signaling cascade [GO:0070886]; positive regulation of protein localization to plasma membrane [GO:1903078]; spermatogenesis [GO:0007283] | apical plasma membrane [GO:0016324]; centrosome [GO:0005813]; filopodium tip [GO:0032433]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; ruffle membrane [GO:0032587]; sarcolemma [GO:0042383] | calcium ion binding [GO:0005509]; magnesium ion binding [GO:0000287]; protein-membrane adaptor activity [GO:0043495] | PF13499; | 1.10.238.10; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q99828}; Lipid-anchor {ECO:0000250|UniProtKB:Q99828}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q99828}. Cell membrane {ECO:0000250|UniProtKB:Q99828}. Apical cell membrane {ECO:0000250|UniProtKB:Q99828}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q99828}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:Q99828}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99828}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q99828}. Cytoplasm {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q99828}. Nucleus {ECO:0000250|UniProtKB:Q99828}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q99828}. Perikaryon {ECO:0000250|UniProtKB:Q99828}. Note=Colocalized with PPP3R1 at the cell membrane of cardiomyocytes in the hypertrophic heart (By similarity). Colocalized with NBR1 to the perinuclear region. Colocalizes with TAS1R2 in apical regions of taste receptor cells. Colocalized with RAC3 in the perinuclear area and at the cell periphery. Colocalized with PAK1 within membrane ruffles during cell spreading upon readhesion to fibronectin. Redistributed to the cytoskeleton upon platelet aggregation. Translocates from the cytosol to the plasma membrane in a calcium-dependent manner. Colocalized with PLK3 at centrosomes in ductal breast carcinoma cells. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Calcium-binding protein that plays a role in the regulation of numerous cellular processes, such as cell differentiation, cell division, cell proliferation, cell migration, thrombosis, angiogenesis, cardiac hypertrophy and apoptosis. Involved in bone marrow megakaryocyte differentiation by negatively regulating thrombopoietin-mediated signaling pathway. Participates in the endomitotic cell cycle of megakaryocyte, a form of mitosis in which both karyokinesis and cytokinesis are interrupted. Plays a role in integrin signaling by negatively regulating alpha-IIb/beta3 activation in thrombin-stimulated megakaryocytes preventing platelet aggregation. Up-regulates PTK2/FAK1 activity, and is also needed for the recruitment of PTK2/FAK1 to focal adhesions; it thus appears to play an important role in focal adhesion formation. Positively regulates cell migration on fibronectin in a CDC42-dependent manner, the effect being negatively regulated by PAK1. Functions as a negative regulator of stress activated MAP kinase (MAPK) signaling pathways. Down-regulates inositol 1,4,5-trisphosphate receptor-dependent calcium signaling. Involved in sphingosine kinase SPHK1 translocation to the plasma membrane in a N-myristoylation-dependent manner preventing TNF-alpha-induced apoptosis. Regulates serine/threonine-protein kinase PLK3 activity for proper completion of cell division progression. Plays a role in microtubule (MT) dynamics during neuronal development; disrupts the MT depolymerization activity of STMN2 attenuating NGF-induced neurite outgrowth and the MT reorganization at the edge of lamellipodia. Promotes cardiomyocyte hypertrophy via activation of the calcineurin/NFAT signaling pathway. Stimulates calcineurin PPP3R1 activity by mediating its anchoring to the sarcolemma. In ischemia-induced (pathological or adaptive) angiogenesis, stimulates endothelial cell proliferation, migration and microvessel formation by activating the PAK1 and ERK1/ERK2 signaling pathway. Promotes also cancer cell survival and proliferation. May regulate cell cycle and differentiation of spermatogenic germ cells, and/or differentiation of supporting Sertoli cells (By similarity). {ECO:0000250}. | Ovis aries (Sheep) |
B1AK53 | ESPN_HUMAN | MALEQALQAARQGELDVLRSLHAAGLLGPSLRDPLDALPVHHAARAGKLHCLRFLVEEAALPAAARARNGATPAHDASATGHLACLQWLLSQGGCRVQDKDNSGATVLHLAARFGHPEVVNWLLHHGGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEHYPEGVNAQTKNGATPLYLACQEGHLEVTQYLVQECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVSCTDVSLSEQDKDGATAMHFAASRGHTKVLSWLLLHGGEISADLWGGTPLHDAAENGELECCQILVVNGAELDVRDRDGYTAADLSDFNGHSHCTRYLRTVENLSVEHRVLSRDPSAELEAKQPDSGMSSPNTTVSVQPLNFDLSSPTSTLSNYDSCSSSHSSIKGQHPPCGLSSARAADIQSYMDMLNPELGLPRGTIGKPTPPPPPPSFPPPPPPPGTQLPPPPPGYPAPKPPVGPQAADIYMQTKNKLRHVETEALKKELSSCDGHDGLRRQDSSRKPRAFSKQPSTGDYYRQLGRCPGETLAARPGMAHSEEVRARQPARAGCPRLGPAARGSLEGPSAPPQAALLPGNHVPNGCAADPKASRELPPPPPPPPPPLPEAASSPPPAPPLPLESAGPGCGQRRSSSSTGSTKSFNMMSPTGDNSELLAEIKAGKSLKPTPQSKGLTTVFSGIGQPAFQPDSPLPSVSPALSPVRSPTPPAAGFQPLLNGSLVPVPPTTPAPGVQLDVEALIPTHDEQGRPIPEWKRQVMVRKMQLKMQEEEEQRRKEEEEEARLASMPAWRRDLLRKKLEEEREQKRKEEERQKQEELRREKEQSEKLRTLGYDESKLAPWQRQVILKKGDIAKY | null | null | actin filament bundle assembly [GO:0051017]; microvillar actin bundle assembly [GO:0030034]; sensory perception of sound [GO:0007605] | brush border [GO:0005903]; cytoplasm [GO:0005737]; filamentous actin [GO:0031941]; microvillus [GO:0005902]; stereocilium [GO:0032420]; stereocilium tip [GO:0032426] | actin filament binding [GO:0051015]; SH3 domain binding [GO:0017124] | PF12796;PF02205; | 1.25.40.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9ET47}. Cell projection, stereocilium {ECO:0000269|PubMed:29572253}. Cell projection, microvillus {ECO:0000269|PubMed:29572253}. | null | null | null | null | null | FUNCTION: Multifunctional actin-bundling protein. Plays a major role in regulating the organization, dimension, dynamics and signaling capacities of the actin filament-rich microvilli in the mechanosensory and chemosensory cells (PubMed:29572253). Required for the assembly and stabilization of the stereociliary parallel actin bundles. Plays a crucial role in the formation and maintenance of inner ear hair cell stereocilia (By similarity). Involved in the elongation of actin in stereocilia (PubMed:29572253). In extrastriolar hair cells, required for targeting MYO3B to stereocilia tips, and for regulation of stereocilia diameter and staircase formation. {ECO:0000250|UniProtKB:Q9ET47, ECO:0000269|PubMed:29572253}. | Homo sapiens (Human) |
B1AL88 | NALF1_HUMAN | MTRGAWMCRQYDDGLKIWLAAPRENEKPFIDSERAQKWRLSLASLLFFTVLLSDHLWFCAEAKLTRARDKEHQQQQRQQQQQQQQQRQRQQQQQQRRQQEPSWPALLASMGESSPAAQAHRLLSASSSPTLPPSPGDGGGGGGKGNRGKDDRGKALFLGNSAKPVWRLETCYPQGASSGQCFTVENADAVCARNWSRGAAGGDGQEVRSKHPTPLWNLSDFYLSFCNSYTLWELFSGLSSPNTLNCSLDVVLKEGGEMTTCRQCVEAYQDYDHHAQEKYEEFESVLHKYLQSEEYSVKSCPEDCKIVYKAWLCSQYFEVTQFNCRKTIPCKQYCLEVQTRCPFILPDNDEVIYGGLSSFICTGLYETFLTNDEPECCDVRREEKSNNPSKGTVEKSGSCHRTSLTVSSATRLCNSRLKLCVLVLILLHTVLTASAAQNTAGLSFGGINTLEENSTNEE | null | null | calcium ion import across plasma membrane [GO:0098703] | plasma membrane [GO:0005886] | stretch-activated, monoatomic cation-selective, calcium channel activity [GO:0015275] | null | null | NALF family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32494638}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Auxillary component of the NALCN sodium channel complex, a channel that regulates the resting membrane potential and controls neuronal excitability. {ECO:0000269|PubMed:32494638}. | Homo sapiens (Human) |
B1AQJ2 | UBP36_MOUSE | MPIVDKLKEALKPGRKDSAEDGDLGRLLAASAKKVLLQRIEFEPASKSFSYQLESLKSKYVLLSARAEGASRHRSGDELQARKPGTERVSGSGGDGVPAPQKVLFPVERLSLRWERVFRVGAGLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCHQGGFCMLCLMQNHMVQAFANSGNAIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKACLNGYAKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQAANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYLRIPGSKKSPEGPVSRVGATLPSRPKVVPEHSKKSPGNGVVPSPLMAKRQDSVMMRKLPAPEEVGVPVSRNGSLPGLKLQNGCAPAKTPAGSPSPRLTPTPTHMPTILDEPGKKVKKSAPLQSLTTSPTTSQGSPGTGESRSQRPGSWASRDTIFSTSPKLLARAITNGHRLKGEGSGVDLEKGDSSSSSPEHSASSDPAKAPQTAESRAAHACDSQGTNCPTAGHPKALLNGVDAKMVKLKSPALSSTTTEPTSLMSPPPAKKLALSAKKASTLRRATGNDIGSPSPSAFCDLTSPMKATHPVVASTGPVSKTRTAAPAPRPSTHPHSASLSSSSAKPLGTSEPQSCRPSAWTPLPQVNGHFTSHLHQLPEASEALHSPSKKRKKTPNGDPQRLGIDTLLPQCLRGAPAAARRKRKKRCSEGEGATAPKQEGQFQDQSWSSGSQKEEGTQPQVNGHQVSHILDSYHVSSRKRRKRKRSEGLSQEATPSQDLIQHSCSPVDHSEPEARTELQKKKKKKRRKRKPEPQQDEESKHPGDQRSPRPSVTPVPALSVNGHLPSDCLGLGQAPLVTWNRDQEPDVVQALLQDSSDKAYGKKVLTWDGEPSAISQDAIKDSRLARTQTVVDDWDEEFDRGKEKKIKKFKREKKRNFNAFQKLQSRRNFWSVTHPAKVASLSYRR | 2.3.2.-; 3.4.19.12 | null | chromatin organization [GO:0006325]; negative regulation of macroautophagy [GO:0016242]; nucleolus organization [GO:0007000]; protein deubiquitination [GO:0016579]; protein stabilization [GO:0050821]; proteolysis [GO:0006508]; regulation of apoptotic process [GO:0042981]; regulation of protein stability [GO:0031647]; regulation of rRNA processing [GO:2000232] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; histone H2B deubiquitinase activity [GO:0140936]; K48-linked deubiquitinase activity [GO:1990380]; RNA binding [GO:0003723]; transferase activity [GO:0016740] | PF00443; | 3.90.70.10; | Peptidase C19 family | PTM: Polyubiquitinated by NEDD4L, no effect on USP36 protein levels. Both proteins interact with and regulate each other's ubiquitination levels. {ECO:0000250|UniProtKB:Q9P275}. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9P275}. Cytoplasm {ECO:0000250|UniProtKB:Q9P275}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q9P275}; | null | null | null | null | FUNCTION: Deubiquitinase essential for the regulation of nucleolar structure and function. Required for cell and organism viability (PubMed:29273634). Plays an important role in ribosomal RNA processing and protein synthesis, which is mediated, at least in part, through deubiquitination of DHX33, NPM1 and FBL, regulating their protein stability (PubMed:29273634). Functions as a transcriptional repressor by deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, such as CDKN1A, thereby preventing histone H3 'Lys-4' trimethylation (H3K4) (By similarity). Specifically deubiquitinates MYC in the nucleolus, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with isoform 3 of FBXW7 (FBW7gamma) in the nucleolus and counteracting ubiquitination of MYC by the SCF(FBW7) complex (By similarity). In contrast, it does not interact with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm (By similarity). Interacts to and regulates the actions of E3 ubiquitin-protein ligase NEDD4L over substrates such as NTRK1, KCNQ2 and KCNQ3, affecting their expression an functions (By similarity). Deubiquitinates SOD2, regulates SOD2 protein stability (By similarity). Deubiquitinase activity is required to control selective autophagy activation by ubiquitinated proteins (By similarity). Promotes CEP63 stabilization through 'Lys-48'-linked deubiquitination leading to increased stability (By similarity). Acts as a SUMO ligase to promote EXOSC10 sumoylation critical for the nucleolar RNA exosome function in rRNA processing (By similarity). Binds to pre-rRNAs (By similarity). {ECO:0000250|UniProtKB:Q9P275, ECO:0000269|PubMed:29273634}. | Mus musculus (Mouse) |
B1ARD8 | SLFN8_MOUSE | METHPSLAVKWSCPDLTIYAGEVTIGEEDRNKMDSKKRKLEKTRITEAACALLNSGGGLIAMQMTNKSEHPVEMGQDLEKSLRELIMSPNMQAFFETKQQEDQFYIFVKSWSCRPEDGSTKPRICSLGSSLYCRSITSKVAMDSREAFEFLKDKKACIKYRPTDDGAPPAKIPRAMCQNSLESNPAFEIFQSKKLEYGQCLLFSESTSIEFKQFSTKHVQAYMKNIIPEYISAFANTQGGYLFIGVDDKRIILGCPKDNVDRDSLKTVANETISKVPVFHFCSSKDKDKVSYETRVIDVFQEGNLYGYLCVIKVEPFCCAVFSEAPISWMVDKEKGVYRLNTEEWVRMMVDFGPEASSKDLSKDFECQLSLCNSPPHCRPVYSKKGLQHKVDLQQRLFQVSPDCLKYTPESLWKELCSQHKRLKGLVKQQIRSFSCGLLILYRSWAVDLNLKEKQEVICDALLIAQNSPPILYTILGEQDEQGQDYCNHTAFTLKQKLVNTGGYTGRVCVMTKVLCLSSQNNIETNGGSVSPINYPSSYNLANIQEMQDLLQALVIVLLNFRSFLSDQLGCEILNLLTAQQYEILSKSLRKTRELFVHGLPGSGKTIIAMKIMEKIRNTFHCETDSILYICENQPLRDFIRAKRICQAVTRKTFMNYRFKTNSFQHIIVDEAQNFRTEDGNWYGKAKAISRRVKSCPGMFWIFLDYFQTSHLKESGLPDFSRQYPREELTQVVRNGDKIAEFLQKELQKIRDNPPCSIPRQSLNIVHEFKWSQSVSGNIKTEQFTLEDMVIYVADKCYDFLRKGYSLQDIAVLFSTDKEKKTYESMFLGEMRKRRRASEMNHAYLCDSNMFDSIRRFSGLERSIVFGINPIATEQPISHNLLLCLASRAMKHLYILYFSTPEGHSSTEAC | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q5U311}; Note=Can also use Mn(2+). {ECO:0000250|UniProtKB:Q5U311}; | defense response to virus [GO:0051607]; immune system process [GO:0002376]; rRNA catabolic process [GO:0016075]; tRNA catabolic process [GO:0016078] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; RNA endonuclease activity [GO:0004521]; tRNA binding [GO:0000049]; zinc ion binding [GO:0008270] | PF17057;PF09848;PF04326;PF21026;PF13538; | 3.40.50.300;3.30.950.30; | Schlafen family, Subgroup III subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68D06}. | null | null | null | null | null | FUNCTION: Endoribonuclease that cleaves tRNAs and rRNAs (PubMed:29563550). Cleaves tRNAs 11 nucleotides from the 3'-terminus at the acceptor stem (PubMed:29563550). May be involved in immune system via regulation of inflammation (PubMed:29528433). {ECO:0000269|PubMed:29528433, ECO:0000269|PubMed:29563550}. | Mus musculus (Mouse) |
Subsets and Splits