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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B9DGI8 | BZP63_ARATH | MEKVFSDEEISGNHHWSVNGMTSLNRSASEWAFNRFIQESSAAADDGESTTACGVSVSSPPNVPVDSEEYRAFLKSKLNLACAAVAMKRGTFIKPQDTSGRSDNGGANESEQASLASSKATPMMSSAITSGSELSGDEEEADGETNMNPTNVKRVKRMLSNRESARRSRRRKQAHLSELETQVSQLRVENSKLMKGLTDVTQTFNDASVENRVLKANIETLRAKVKMAEETVKRLTGFNPMFHNMPQIVSTVSLPSETSNSPDTTSSQVTTPEIISSGNKGKALIGCKMNRTASMRRVESLEHLQKRIRSVGDQ | null | null | cellular response to abscisic acid stimulus [GO:0071215]; cellular response to glucose stimulus [GO:0071333]; cellular response to starvation [GO:0009267]; entrainment of circadian clock [GO:0009649] | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; protein heterodimerization activity [GO:0046982]; protein self-association [GO:0043621] | PF00170;PF12498; | 1.20.5.170; | BZIP family | PTM: Phosphorylated. The phosphorylation at Ser-29, Ser-294 and Ser-300 by KIN10 strongly enhances its ability to form homo- as well as heterodimers and are then essential for its transcriptional activity (PubMed:26263501). {ECO:0000269|PubMed:20047775, ECO:0000269|PubMed:26263501}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:16957775}. | null | null | null | null | null | FUNCTION: Transcription factor involved in controlling responses to starvation (PubMed:26263501). BZIP2-BZIP63-KIN10 complex binds to the ETFQO promoter to up-regulate its transcription (PubMed:29348240). {ECO:0000269|PubMed:26263501, ECO:0000269|PubMed:29348240}. | Arabidopsis thaliana (Mouse-ear cress) |
B9DGT7 | TBA2_ARATH | MRECISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPSDKTVGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTSVVEPYNSVLSTHSLLEHTDVSILLDNEAIYDICRRSLSIERPTYTNLNRLVSQVISSLTASLRFDGALNVDVTEFQTNLVPYPRIHFMLSSYAPVISAEKAFHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVGTIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTSVAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAEGGDDEDDEGEEY | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278] | cytoplasm [GO:0005737]; microtubule [GO:0005874] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250}.; PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P68363}; | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. | Arabidopsis thaliana (Mouse-ear cress) |
B9DGU7 | TPK1_ARATH | MSAMDVMIHSSSFLLPCDETSTGTRYALVVLNQSLPRFTPLLWEHAKLRLCADGGANRIYDELPLFFPNEDALAIRNRYKPDVIKGDMDSIRRDVLDFYINLGTKVIDESHDQDTTDLDKCILYIRHSTLNQETSGLQILATGALGGRFDHEAGNLNVLYRYPDTRIVLLSDDCLIQLLPKTHRHEIHIQSSLEGPHCGLIPIGTPSAKTTTSGLQWDLSNTEMRFGGLISTSNLVKEEKITVESDSDLLWTISIKKTGLSIQDHTP | 2.7.6.2 | null | phosphorylation [GO:0016310]; thiamine diphosphate biosynthetic process [GO:0009229]; thiamine metabolic process [GO:0006772] | cytosol [GO:0005829] | 8-oxo-dGDP phosphatase activity [GO:0044715]; ATP binding [GO:0005524]; kinase activity [GO:0016301]; thiamine binding [GO:0030975]; thiamine diphosphokinase activity [GO:0004788] | PF04265;PF04263; | 3.40.50.10240;2.60.120.320; | Thiamine pyrophosphokinase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17611796}. | CATALYTIC ACTIVITY: Reaction=ATP + thiamine = AMP + H(+) + thiamine diphosphate; Xref=Rhea:RHEA:11576, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385, ChEBI:CHEBI:30616, ChEBI:CHEBI:58937, ChEBI:CHEBI:456215; EC=2.7.6.2; Evidence={ECO:0000269|PubMed:17611796}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11577; Evidence={ECO:0000269|PubMed:17611796}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.28 uM for thiamine {ECO:0000269|PubMed:17611796}; Vmax=9.6 pmol/min/mg enzyme with thiamine as substrate {ECO:0000269|PubMed:17611796}; | PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1. {ECO:0000269|PubMed:17611796}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. Active between pH 6 and pH 8. {ECO:0000269|PubMed:17611796}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:17611796}; | FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate (TPP) (PubMed:17611796). TPP is an active cofactor for enzymes involved in glycolysis and energy production (PubMed:17611796). Plant leaves require high levels of TPP for photosynthesis and carbohydrate metabolism (PubMed:17611796). {ECO:0000269|PubMed:17611796}. | Arabidopsis thaliana (Mouse-ear cress) |
B9DGY1 | AB1K7_ARATH | MAALLASQSCCYGGETARVTKAIGFSSSLENHFTGEATQCYGSKSKRFRIEMRQSELPSKVGINGRSVKMVPASEVVKRKDGVNGSAGKGVNGASLVSSRNINGAASTLVKAPKKTTESYLPPPVEGVRVLPSDEGFSWADENYSSLQRSIDVWSFVISLRIRILFDNSKWAYVGGFTEEKQKSRRRETASWLRESVLQLGPTFIKLGQLSSTRSDLFPREFVDELSKLQDRVPAFSPEKAKRFIEAELGAPISVMYKEFEEQPIAAASLGQVHRAVLHNGEKVVVKVQRPGLKKLFDIDLRNLKLIAEYFQKSESFGTNDWVGIYEECALILYQEIDYINEAKNADRFRRDFRNINWVRVPLVYWDYSAMKVLTLEYVPGVKINNLDALAARGFNRSRIASRAIEAYLIQILKTGFFHADPHPGNLAIDVDESIIYYDFGMMGEIKTFTRKRLLDLFYSVYEKDAKKVMQNLIDLEALQPTGDLSSVRRSVQFFLDNLLSQSPDQQQTLAAIGEDLFAISQDQPFRFPSTFTFVIRAFSTLEGIGYILDPEFSFVKVAAPYAQELLDLKQRQRSGTQLVQEIRKQADDARSSTLSMPYRVQRIEEFVKELDSGDLKLRVRVLESERAARKATILQMATMYTVLGGTLLNIGVTFSNQGSQLVANGSFIGAGIFMLLVLRSMQRVNKLDKFEKMI | 2.7.11.1 | null | cellular response to oxidative stress [GO:0034599]; membrane lipid biosynthetic process [GO:0046467]; phosphorylation [GO:0016310]; regulation of response to reactive oxygen species [GO:1901031]; response to iron ion starvation [GO:1990641]; response to oxidative stress [GO:0006979] | chloroplast thylakoid membrane [GO:0009535]; plastoglobule [GO:0010287] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF03109; | null | Protein kinase superfamily, ADCK protein kinase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:24117441}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:22274653, ECO:0000305|PubMed:22694836}. | 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:Q9MA15}; 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:Q9MA15}; | null | null | null | null | FUNCTION: Involved in resistance to oxidative stress. Influences responses to reactive oxygen species (ROS) production. Regulates plastoglobules formation in thylakoids. Together with OSA1, regulates iron distribution within the chloroplast and mediates the oxidative stress response (PubMed:24117441). Together with ABC1K8, influences chloroplast lipid synthesis/accumulation and modulates chloroplast membrane composition in response to stress (PubMed:25809944). {ECO:0000269|PubMed:24117441, ECO:0000269|PubMed:25809944}. | Arabidopsis thaliana (Mouse-ear cress) |
B9DHQ0 | TBA5_ARATH | MREIISIHIGQAGIQVGNSCWELYCLEHGIQPDGMMPSDTTVGVAHDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTVGKEIVDLCLDRVRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQIISSLTTSLRFDGAINVDITEFQTNLVPYPRIHFMLSSYAPVISAAKAYHEQLSVPEITNAVFEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVGTIKTKRTVQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNNTAVAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAEGGDDEEDEGEDY | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278] | cytoplasm [GO:0005737]; microtubule [GO:0005874] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P68363}; | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. | Arabidopsis thaliana (Mouse-ear cress) |
B9DHT4 | ARIA_ARATH | MDQQPERREGRSFPERKGQKRKLEEGAAAVEDREISAVSTDGGQALLSEVAAQVSVLNSAFSWQESDRAAAKRATQVLAELAKNEDLVNVIVDGGAVPALMTHLQAPPYNDGDLAEKPYEHEVEKGSAFALGLLAIKPEYQKLIVDKGALPHLVNLLKRNKDGSSSRAVNSVIRRAADAITNLAHENSSIKTRVRVEGGIPPLVELLEFSDSKVQRAAAGALRTLAFKNDDNKNQIVECNALPTLILMLGSEDAAIHYEAVGVIGNLVHSSPHIKKEVLTAGALQPVIGLLSSCCPESQREAALLLGQFASTDSDCKVHIVQRGAVRPLIEMLQSPDVQLKEMSAFALGRLAQDAHNQAGIAHSGGLGPLLKLLDSRNGSLQHNAAFALYGLADNEDNVSDFIRVGGIQKLQDGEFIVQATKDCVSKTLKRLEEKIHGRVLRHLLYLMRISEKSIQRRVALALAHLCSPEDQRTIFIDDNGLELLLGLLGSLNTKQQLDGAAALYKLANKSMALSPVDAAPPSPTQRVYLGEQYVNNATLSDVTFLVEGRTFYAHRICLLASSDAFRAMFDGGYREKDARDIEIPNIKWEVFELMMRFIYTGSVDITNEISKDLLRAADQYLLEGLKRLCEYTIAQDITLESIGDMYELSEAFHAMSLRQACIMFILEHFDKLSSMPWQNELVQRTIPEIREYFCRALTKSTTNLQSLRL | null | null | negative regulation of seed germination [GO:0010187]; protein ubiquitination [GO:0016567]; response to abscisic acid [GO:0009737]; response to salt stress [GO:0009651] | nucleus [GO:0005634]; plasma membrane [GO:0005886] | null | PF00514;PF00651; | 1.25.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15516505}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Acts as a positive regulator of ABA response via the modulation of the transcriptional activity of ABF2, a transcription factor which controls ABA-dependent gene expression via the G-box-type ABA-responsive elements. Negative regulator of seed germination and young seedling growth. {ECO:0000250, ECO:0000269|PubMed:15516505}. | Arabidopsis thaliana (Mouse-ear cress) |
B9E972 | OLHYD_MACCJ | MYYSNGNYEAFARPKKPEGVDNKSAYLVGSGLASLAAASFLIRDGQMKGENIHILEELDLPGGSLDGILNPERGYIMRGGREMENHFECLWDLFRSVPSLEVEDASVLDEFYWLNKEDPNYSKCRVIENRGQRLESDGKMTLTKKANKEIIQLCLMKEEQLNDVKISDVFSKDFLDSNFWIYWKTMFAFEPWHSAMEMRRYLMRFIHHIGGLADFSALKFTKFNQFESLVMPLIEHLKAKNVTFEYGVTVKNIQVECSKESKVAKAIDIVRRGNEESIPLTENDLVFVTNGSITESTTYGDNDTPAPPTSKPGGAWQLWENLSTQCEEFGNPAKFYKDLPEKSWFVSATATTNNKEVIDYIQKICKRDPLSGRTVTGGIVTVDDSNWQLSFTLNRQQQFKNQPDDQVSVWIYALYSDERGERTNKTIVECSGKEICEEWLYHMGVPEEKISALAAECNTIPSYMPYITAYFMPRKEGDRPLVVPHGSKNIAFIGNFAETERDTVFTTEYSVRTAMEAVYKLLEVDRGVPEVFASVYDVRILLHALSVLNDGKKLDEIDMPFYERLVEKRLLKKASGTFIEELLEEANLI | 4.2.1.53 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:22203098}; Note=Binds 1 FAD per subunit. FAD does not seem to be involved in catalysis but rather in the structural stabilization of the enzyme. {ECO:0000269|PubMed:22203098}; | fatty acid metabolic process [GO:0006631]; response to toxic substance [GO:0009636] | null | FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; oleate hydratase activity [GO:0050151]; protein homodimerization activity [GO:0042803] | PF06100; | 3.30.9.80;3.50.50.60; | Oleate hydratase family | null | null | CATALYTIC ACTIVITY: Reaction=(R)-10-hydroxyoctadecanoate = (9Z)-octadecenoate + H2O; Xref=Rhea:RHEA:21852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15683, ChEBI:CHEBI:30823; EC=4.2.1.53; Evidence={ECO:0000305|PubMed:22203098}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21854; Evidence={ECO:0000305|PubMed:22203098}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + H2O = 10-hydroxyoctadecanoate; Xref=Rhea:RHEA:75751, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:143089; Evidence={ECO:0000269|PubMed:22203098}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75752; Evidence={ECO:0000305|PubMed:22203098}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoate + H2O = 10-hydroxyhexadecanoate; Xref=Rhea:RHEA:75767, ChEBI:CHEBI:15377, ChEBI:CHEBI:32372, ChEBI:CHEBI:194446; Evidence={ECO:0000269|PubMed:22203098}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75768; Evidence={ECO:0000305|PubMed:22203098}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z)-octadecatrienoate + H2O = (10S)-hydroxy-(6Z,12Z)-octadecadienoate; Xref=Rhea:RHEA:75775, ChEBI:CHEBI:15377, ChEBI:CHEBI:32391, ChEBI:CHEBI:194448; Evidence={ECO:0000305|PubMed:22203098}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75776; Evidence={ECO:0000305|PubMed:22203098}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=340 uM for oleate {ECO:0000269|PubMed:22203098}; KM=300 uM for myristoleate {ECO:0000269|PubMed:22203098}; KM=570 uM for palmitoleate {ECO:0000269|PubMed:22203098}; KM=390 uM for linoleate {ECO:0000269|PubMed:22203098}; KM=320 uM for alpha-linolenate {ECO:0000269|PubMed:22203098}; KM=590 uM for gamma-linolenate {ECO:0000269|PubMed:22203098}; Note=kcat is 470 min(-1) with oleate as substrate. The catalytic efficiency with oleate as substrate is 3.5-fold higher than that with palmitoleate, the second favored substrate.; | PATHWAY: Lipid metabolism; fatty acid metabolism. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 with oleate as substrate. {ECO:0000269|PubMed:22203098}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25 degrees Celsius with oleate as substrate. After 120 minutes, the enzyme activity is nearly unchanged at 25 degrees Celsius, but is reduced to only 25% at 35 degrees Celsius. {ECO:0000269|PubMed:22203098}; | FUNCTION: Catalyzes the hydration of oleate at its cis-9-double bond to yield 10-hydroxyoctadecanoate, probably in the (R) configuration. Cannot catalyze the reverse reaction. Is not active with saturated fatty acids and trans-, cis-5-, cis-6-, cis-8-, cis-11-, cis-13-, cis-14-, and cis-15-double bond unsaturated fatty acids as substrate; is only active on cis-9- and/or cis-12-double bond of unsaturated fatty acids without any trans-configurations, producing 10-hydroxy and, to a lesser extent, 10,13-dihydroxy fatty acids. The hydration of unsaturated fatty acids is suggested to be a detoxification mechanism and a survival strategy for living in fatty acid-rich environments. {ECO:0000269|PubMed:22203098}. | Macrococcus caseolyticus (strain JCSC5402) (Macrococcoides caseolyticum) |
B9EHT4 | CLIP3_MOUSE | MTKTDPAPMAPPPRGEEEEEEEEDEPVPEAPSPTQERRQKPVVHPSAPAPLPKDYAFTFFDPNDPACQEILFDPKTTIPELFAIVRQWVPQVQHKIDVIGNEILRRGCHVNDRDGLTDMTLLHYACKAGAHGVGDPAAAVRLSQQLLALGADVTLRSRWTNMNALHYAAYFDVPDLVRVLLKGARPRVVNSTCSDFNHGSALHIAASNLCLGAAKCLLEHGANPALRNRKGQVPAEVVPDPMDMSLDKAEAALVAKELRTLLEEAVPLSCTLPKVTLPNYDNVPGNLMLSALGLRLGDRVLLDGQKTGTLRFCGTTEFASGQWVGVELDEPEGKNDGSVGGVRYFICPPKQGLFASVSKVSKAVDAPPSSVTSTPRTPRMDFSRVTGKGRREHKGKKKSPSSPSLGSLQQREGAKAEVGDQVLVAGQKQGIVRFYGKTDFAPGYWYGIELDQPTGKHDGSVFGVRYFTCAPRHGVFAPASRIQRIGGSTDPPGDSVGAKKVHQVTMTQPKRTFTTVRTPKDIASENSISRLLFCCWFPWMLRAEMQS | null | null | cytoplasmic microtubule organization [GO:0031122]; fat cell differentiation [GO:0045444]; membrane biogenesis [GO:0044091]; negative regulation of microtubule polymerization [GO:0031115]; peptidyl-L-cysteine S-palmitoylation [GO:0018230]; positive regulation of apoptotic process [GO:0043065]; positive regulation of endocytosis [GO:0045807]; positive regulation of glucose transmembrane transport [GO:0010828]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of protein phosphorylation [GO:0001934]; protein transport along microtubule [GO:0098840] | cell cortex [GO:0005938]; early endosome membrane [GO:0031901]; Golgi stack [GO:0005795]; membrane raft [GO:0045121]; microtubule plus-end [GO:0035371]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588] | ganglioside binding [GO:0035594]; microtubule binding [GO:0008017]; microtubule plus-end binding [GO:0051010] | PF12796;PF01302; | 1.25.40.20;2.30.30.190; | null | PTM: Palmitoylation by ZDHHC17 regulates association with the plasma membrane. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000250}. Golgi apparatus, Golgi stack {ECO:0000250}. Note=Localized to Golgi stacks as well as on tubulovesicular elements juxtaposed to Golgi cisternae. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Functions as a cytoplasmic linker protein. Involved in TGN-endosome dynamics. May modulate the cellular compartmentalization of AKT kinase family and promote its cell membrane localization, thereby playing a role in glucose transport in adipocytes (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
B9EJ57 | MTF1B_MOUSE | MASRNIWCVRRNFLFDLRGWMLQYSAEVFLKSISFRTFSVECDSKDKESLEEEREDLLSNLVTMGVDIDMARRRQPGVFNKAVTNEQELKIFLLSKGASDKVIGSIISRYPRAITRTPESLSKRWDLWRKIMASDLEIVNILERSPESFFRSNNNLNLENNIKFLCSVGLTHKCLCRLLTNAPRTFSNSLNLNKQMVEFLQETGMSLGHNDPRDFVRKIISKNPSILIQSTKRVKTNIEFLQSTFNLNKQDLLLLICGPGARILDLSNDCTKKNYTNIRERLLSLGCSEEEVQRFVLSYLNMVFLSEKKFNDKIDCLIEEKISASQIIENPRILDSSINTLKTRIRELSHAGYDLSTSSIALLSWSQRRYEAKLKRLCG | null | null | regulation of DNA-templated transcription [GO:0006355]; termination of mitochondrial transcription [GO:0006393]; transcription initiation at mitochondrial promoter [GO:0006391] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | double-stranded DNA binding [GO:0003690]; nucleic acid binding [GO:0003676]; sequence-specific DNA binding [GO:0043565] | PF02536; | 1.25.70.10; | MTERF family | PTM: Phosphoprotein with mostly four phosphate groups. While the DNA-binding activity is unaffected by the phosphorylation state, only the phosphorylated form of the protein is active for termination activity. Functioning seems to be regulated by phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q99551}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q99551}. | null | null | null | null | null | FUNCTION: Transcription termination factor. Binds to a 28 bp region within the tRNA(Leu(uur)) gene at a position immediately adjacent to and downstream of the 16S rRNA gene; this region comprises a tridecamer sequence critical for directing accurate termination. Binds DNA along the major grove and promotes DNA bending and partial unwinding. Promotes base flipping. Transcription termination activity appears to be polarized with highest specificity for transcripts initiated on the light strand. {ECO:0000269|PubMed:23562081}. | Mus musculus (Mouse) |
B9EJ80 | PDZD8_MOUSE | MGLLLLILASAVLGSFLTLLAQFLLLYRRQPEPRADEAARAGDGFRYLKPVPGLPLREYLYGGGAEELAACSSEAGASSTPTPDSPAPPTLETCYFLNATILFLFRELRDTALARRWVTKKIKVEFEELLQTKTAGRLLEGLSLRDVFLGDTVPFIKTIRLVRPVVASGTGEPDDPDGDALPATCPEELAFEAEVEYNGGFHLAIDVDLVFGKSAYLFVKLSRVVGRLRFVLTRVPFTHWFFSFVEDPLIDFEVRSQFEGRPMPQLTSIIVNQLKKIIKRKHTLPSYKIRFKPFFPYQALQGFEEDEELIHIQQWALTEGRLKVTLLECSRLFIFGSYDRETNVHCTLELSSGVWEEKQRSSIKTVELIKGNLQSVGLTLRLVQSTDGYAGHVIIETVAPNSPAAMADLQRGDRLIAIGGVKITSTLQVLKLIKQAGDRVLVYYQRPAGQSSQDSLGQLEESFLSSSCQAAYEEDAAGLSADTENRDLDSEFEDLASDVRVQTELKEETQPLSHSPKRTPTTLSIKPLGAISPVLNRKLISGIHPPPQKLPSKEGNKPSTLKTSETTEAAQVSKPQGPTFKPPVPPRPQGRVPLPPTDTSAQADPEAPEKPDKVLLPPPPADKPAEKQVKSVDQGEDVAAGKQSSAKQEGVKDLPSESSAPTKDSSDDPQMWESSEVLYRNKVGKWSRTRASCVFDIEACHRYLNIALWCRDPFKLGGLICLGHVSLKLEEVALGCLATSNMEYLTKFRLEPPTPKAMVTRTALRNLSMQKGFNDKFCFGDITIHFKYLKEGEPDHHIVPNVEKEKELHLVEEVSTLPKEEHFVGQMSLSENKHSFQDTQFQNPTWCDYCKKKVWTKAASQCMFCAYVCHKKCQEKCLAETPLCGATERRIDRTLKNLRLEGQDPLLGLPPRVEIEANKSVNKTTGLTRHIINTSSRLLNLRQVSKTRLSEPGTDLVEPSPKHTPNTSDNEGSDTEVCGSNSPSKRGNSAGIKLMRKEGGLDDSVFIAVKEIGRDLYRGLPTEERIQKLEFMLDKLQNEIDQELEHNNSLVREEKETNDTRKKSVLSAALAKSGERLQALTLLMIHYRAGIEDIETLENLSLDQHSKKMNKYADDTEEDLDSEISQLIDSQPFSNISDDLFGPSESV | null | null | cytoskeleton organization [GO:0007010]; lipid transport [GO:0006869]; mitochondrial calcium ion homeostasis [GO:0051560]; mitochondrion-endoplasmic reticulum membrane tethering [GO:1990456]; regulation of cell morphogenesis [GO:0022604] | endoplasmic reticulum membrane [GO:0005789]; mitochondria-associated endoplasmic reticulum membrane [GO:0044233]; mitochondrion [GO:0005739] | lipid binding [GO:0008289]; metal ion binding [GO:0046872] | PF00130;PF17820; | 2.30.42.10;3.30.60.20; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29097544}; Single-pass membrane protein {ECO:0000255}. Note=Localizes at mitochondria-endoplasmic reticulum contact sites. {ECO:0000269|PubMed:29097544}. | null | null | null | null | null | FUNCTION: Molecular tethering protein that connects endoplasmic reticulum and mitochondria membranes (PubMed:29097544). PDZD8-dependent endoplasmic reticulum-mitochondria membrane tethering is essential for endoplasmic reticulum-mitochondria Ca(2+) transfer (PubMed:29097544). In neurons, involved in the regulation of dendritic Ca(2+) dynamics by regulating mitochondrial Ca(2+) uptake in neurons (PubMed:29097544). {ECO:0000269|PubMed:29097544}. | Mus musculus (Mouse) |
B9EJ86 | OSBL8_MOUSE | MEAALADGEPDRSSLLGDSKDVLGPSTVVANSDEPQHLTPGKMSQRQGRDANPTPTRDLPQPSLSPASLHSQGFERGKEDISQNKDDSSLSMSKSKSESKLYNGSEKDSSTSSKLTKKESLKVQKKNYREEKKRATKELLSTITDPSVIVMADWLKIRGTLKSWTKLWCVLKPGVLLIYKTQKNGQWVGTVLLNACEIIERPSKKDGFCFKLFHPLEQSIWAVKGPKGEAVGSITQPLPSSYLIIRATSESDGRCWMDALELALKCSSLLKRTMVREGKEHDLSISSDSTHVTLYGLLRANNLHSGDNFQLNDSEIERQHFKDQDLYSDKSDKENDPEHDESDNEVLGKSEESDTDTSERQDDSYIDPEPVEPLKETTYMEQSHEELGEAGEASQTETVSEENKSLIWTLLKQVRPGMDLSRVVLPTFILEPRSFLDKLSDYYYHADFLSEAALEENPYFRLKKVVKWYLSGFYKKPKGLKKPYNPILGETFRCLWIHPRTNSKTFYIAEQVSHHPPISAFYVSNRKDGFCLSGSILAKSKFYGNSLSAILEGEARLTFLNRGEDYVMTMPYAHCKGILYGTMTLELGGTVNITCQKTGYSAILEFKLKPFLGSSDYVNQISGKLKLGKEVLATLEGHWDSEVFINDKKTDNSEIFWNPTPDIKQWRLIRHTVKFEEQDDFESEKLWQRVTKAINAKDQTEATQEKYVLEEAQRQAARDRKTKTQEWVCKLFELDPLTGEWHYKFSDTRPWDPLNDMIQFEKDGVIQTKVKHRTPMVSVPKMKHKPTRQQKKVVKGYSSPEPDIQDSSGSEAQSVKPSTRRKKGIDLGDIQSSIESIKQTQEEIKRNIMALRNHLLSSTPATDYFLQQKDYFVIFLLILLQVIINFIFK | null | null | fat cell differentiation [GO:0045444]; negative regulation of cell migration [GO:0030336]; negative regulation of sequestering of triglyceride [GO:0010891]; phospholipid transport [GO:0015914]; positive regulation of glucose import [GO:0046326]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; protein localization to nuclear pore [GO:0090204] | cortical endoplasmic reticulum [GO:0032541]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nuclear membrane [GO:0031965] | cholesterol binding [GO:0015485]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylserine binding [GO:0001786]; phosphatidylserine transfer activity [GO:0140343]; sterol transporter activity [GO:0015248] | PF01237;PF00169; | 1.10.287.2720;2.40.160.120;3.30.70.3490;2.30.29.30; | OSBP family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BZF1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9BZF1}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BZF1}. Note=The presence of the N-terminus extension contains an overall negative charge that may explain the weak localization to the cortical endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9BZF1}. | null | null | null | null | null | FUNCTION: Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner. Binds oxysterol, 25-hydroxycholesterol and cholesterol. {ECO:0000250|UniProtKB:Q9BZF1}. | Mus musculus (Mouse) |
B9EJA2 | CTTB2_MOUSE | MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALLIRPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAGTCPPVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSPQLPPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGNSLSSEEPKSGLFSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQPSNDVSDDFECEHTICTLNIRKQTSWEDFSKAVSQALTNHFQAISSDGWWSLEDGTFNNATDSCIGLGTSSIRSIMLGSMPWSTGQSFSQSPWDFLKKKKVEQVLALLSGPQEGCLSSVTYASMIPLQMLQNYLRLVEQYHNVIFHGPEGSLQDYIANQLALCMKYRQMAAGFPCEIVRAEVDSGFSKEQLVDVFIRNACLIPVKQFPVKKKIIVILENLEKSSLSELLGDFLAPLENRSTESPCTFQKGNGTSECYYFHENCFLVGTIAKACLQGSDLLVQQHFRWVQLRWDCEPIQGLLQRFLRRKVVSKFRGQLPAPCDPVCKIVDWALSVWRQLNSCLARLGTPEALLGPKYFLSCPVVPGHAQATVKWMSKLWNAVIAPRVQEAILSRASMNKQPGTGQTASKKYPSQGQQAVVRAALSILLNKAVLHGCPLPRAELDQQIADFKGGSFPLSIVSSYSKKKVESGAWRKVNTSPRKKPGHFSSPTWNKPDPKREGMRNKTIPHLNTNRNSSLSKQQSLENDLSVTLTLDHRLSLGSDDEADLVKELQSMCSSKSESDISKIADSRDDLRKFDSSRTNPGTSAPLNLRTPVPQKEASPPSSRQTAECSNSKSKTEMGVSSVKSFLPVPRSKVAQCSQNTKRNSSSSNTRQLEINNNSKEENWTLDKHEQVEKPNK | null | null | regulation of modification of postsynaptic actin cytoskeleton [GO:1905274]; regulation of synapse organization [GO:0050807] | cell cortex [GO:0005938]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; postsynaptic actin cytoskeleton [GO:0098871]; synaptic vesicle [GO:0008021] | SH3 domain binding [GO:0017124] | PF12796;PF09727; | 1.25.40.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:22262902, ECO:0000269|PubMed:23015759}. Cell projection, dendritic spine {ECO:0000269|PubMed:22262902, ECO:0000269|PubMed:23015759}. Note=Remains associated with dendritic spines even after glutamate stimulation. {ECO:0000269|PubMed:22262902, ECO:0000269|PubMed:23015759}. | null | null | null | null | null | FUNCTION: Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, and thus controls dendritic spinogenesis and dendritic spine maintenance (PubMed:22262902). Associates with the striatin-interacting phosphatase and kinase (STRIPAK) core complex to regulate dendritic spine distribution of the STRIPAK complex in hippocampal neurons (PubMed:23015759). {ECO:0000269|PubMed:22262902, ECO:0000269|PubMed:23015759}. | Mus musculus (Mouse) |
B9EJV3 | GRB1L_MOUSE | MGNSYAGQLKSARFEEALHNSIEASLRCSTAVPRPIFSQLYLDPDQHPFSTADVKPKVEDLDKDLVHPYTQNGSVDFSHNVAMNEMEDDEDEEEMSDSNSPPIPYSQKPAPEGSCTTDGFCQAGKDLRLVSLCMEQIDIPAGFLLVGAKSPNLPEHILVCAVDKRFLPDDHGKNALLGFSGNCIGCGERGFRYFTEFSNHINLKLTTQPKKQKHLKYYLVRTSQGVLSKGPLICWKECRSRQSSALCHSTKPISSVSSAVAPENGTANGYKAGFTVTEAANGTSGHGGKSSSCSSTPSRPGNYSLSPRPTFTSVDQANMFISGPPKKRHRGWYPGSPVSQSALVVPAPTVRPLSRTEPLLSTPVPQTPLTGILQPRPVLAGETVIVPENLLSNSGVRPVILIGYGTLPYFYGNVGDIVVSPLLVNCYKIPQLENKDLEQLGLTSTHLLSVENMILLTIQYLVRLGPDQIPLREEFEQIMLTAMQEFSVRERALPLGAPCAPMSPAQLPWLARLAASVSQDLVHVIVTQNSLAEGISETLRLLSEMKHYQRLPDYVVAICASKIRGNEFCVVVLGQHQSRALAESMLTTSEFLKEISYELITGKVSFLASHFKTTSLGDDLDKLLEKMQQRRGDSVVTPFNGDLDECVSPQEAAAMIPTQNLDVDNETFQIYQPQLTVARRLLSQVCAIADSGSQSLDLGHFSKVDFIIIVPRSEVLVQQTLQRVRQSGVLVDLGLEESGLAHQRAERYVVRLDNEIQSKFEVFMRRVKQNPYTLFVLVHDNSHVELTSVISGSLSHGEPTHGLADRVINCREVLEAFNLLVLQVSSFPYTLQTQQSRISSSNEVHWIQLDTMEDAGCEKLYFGLDEYSKSLQWGITSPLLRCDETFEKMVSTLLERYPRLHSMVVRCYLLIQQYSEALMALTTMASLRDHSTPETLSIMDDLITSPGKNKSGKGHMLVIRVPSVQLAMLAKERLQEVRDKLGLQYRFEIILGSPASELTVETHFVTRLKTWRGNDQDEWIPRTYQDLEGLPCIVILTGKDPLGETFPRSLKYCDLRLIDSSYLTRTALEQEVGLACCYVSKEVIRGPAAALDLSAKEAERVPASENDSEELLIDLERPQSNSSAVTGTSGSIMENGVSSSSTAGKPQQQLLTPTSSIRLDEGVSASTAVVGEILKQECDSLDPPMASSTTSKPSSSSSSSAQALAWSRQPRGLHTALPPVIILSKAAYSLLGSQKGGRLPSSSSLLPHADVAWVSSLRPGLHKDMSSEEQSLYYRQWTSARQHHADYSNQPDPISGARTLHPRRLLLTGPPQVGKTGSYLQFLRILFRMLIRLLEVDVYNEEEINTDHSDDSELSQSEGEPWPDIETFSKMPFDVSVHDPKYRLMSLVYSEKLAGIKQEVIKEYKVEEPRQRETMSMMLTQYAAYNTFHHCEQCQQYMAFTPASQMSDSTLHAFTFSSSMLGEEVQLYFIIPKSKESHFVFSKQGRHLESMRLPLVSDKNLNAVKSPIFTPSSGRHEHGLLNLFHAMEGISHLHLLVVKEYEMPLYRKYWPNHIMLVLPGMFNNAGVGAARFLIKELSYHNLELERNRLEELGVKRQCVWPFIVVMDDSCVLWNIHSVQEQTSQPTEAGISSKNVSLKSVLQHIEATPKIIHYAILGIQKWNSKLTSQSLKAPFSRCHVHDFILLNIDLTQNVQYDFNRYFCEDVDFNLRTNSSGLLICRFNNFSLMKKHVQVGGQRDFIIKPKLMVSENVVPILPLQYVCAPDSEHTLLAAPAQFLLEKFLQHASYKLFPKAIHNFKSPVLAIDCYLNIGQEVAICYVSSRPHSSNVNCEGVFFSGLLLYLCDSFVGADLLKKFKFLKGATLCVICQDRSSLRQTIVRLELEDEWQFRLRDEFQTANSSDDKPLYFLTGRHV | null | null | branching involved in ureteric bud morphogenesis [GO:0001658]; cardiac ventricle development [GO:0003231]; epithelial tube morphogenesis [GO:0060562]; kidney development [GO:0001822]; male genitalia development [GO:0030539]; mesonephric duct development [GO:0072177]; metanephros development [GO:0001656]; paramesonephric duct development [GO:0061205]; uterus development [GO:0060065] | membrane [GO:0016020] | null | PF20692;PF20688;PF20267;PF15782;PF20691; | null | GREB1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Plays a major role in early metanephros and genital development. {ECO:0000269|PubMed:29100091}. | Mus musculus (Mouse) |
B9EKI3 | TMF1_MOUSE | MSWFNASQLSSFAKQALSQAQKSIDRVLDIQEEEPSAWAEAIPYGEPGISPPVSGGWDTSTWGLNSTSSEPQSPPTASQAITKPVRRTVVDESENFFSAFLSPSDAHTIQKSPVVSKPPSKSQRPEEEVKSSLQESSSPGQSRVSETAEVRDSVCVSGETSAVGTPSPVPEDKHEETAGEESEVKVPTVRLKASENVVNVNTTEDVSTTSTQSLTAETKDMALEPKEQKHEDRQSNTPSPPVSSFSSGTSTTSDIEVLDHESVISESSASSRQETSDAKSSLHLMQTSFQLLSASACPEYSRLDDFQKLNESCCSSDAFERIDSFSVQSLDSRSVSEINSDDELPGKGYALVPIIVSPSTPKTKVVESTEENAEEEEGNETLVAPSEEAELEESGRSATPVNCDQPDILASPTAGSGGHSASGPATEQCEAVENQPKAPPEKEDVCKTVEFLNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEMKTIKEELATRLNSSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNIIKKLRAKDKDNENVIAKLNRKAKELEEELQHLRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAALRREMKAKEELSGALEKAQEEARQQQEALVLQVGDLRLALQRAEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSSTARPLLRQIENLQATLGSQTSSWETLEKSLSDRLGESQTLLAAAVERERAATEELLANKIQMSSVESQNTLLRQENSRLQAQLESEKNKLRKLEDENSRYQVELENLKDEYVRTLEESRKEKTLLSSQLEMERMKVEQERKKTIFTQEALKEKDHKLFSVCSTPTMSRSSSISGVDAAGLQASFLSQDESHDHSFGPMSTSASGSNLYEAVRMGAGSSIIENLQSQLKLREGEISHLQLEISNLEKTRSIMSEELVKLTNQNDELEEKVKEIPKLRVQLRDLDQRYNTILQMYGEKAEEAEELRLDLEDVKNMYKTQIDELLRQRLS | null | null | acrosome assembly [GO:0001675]; androgen receptor signaling pathway [GO:0030521]; apoptotic process [GO:0006915]; cellular response to organic cyclic compound [GO:0071407]; defense response to bacterium [GO:0042742]; epithelial cell apoptotic process [GO:1904019]; flagellated sperm motility [GO:0030317]; Leydig cell differentiation [GO:0033327]; luteinizing hormone secretion [GO:0032275]; male gonad development [GO:0008584]; negative regulation of epithelial cell apoptotic process [GO:1904036]; negative regulation of gene expression [GO:0010629]; positive regulation of cytokine production [GO:0001819]; positive regulation of testosterone secretion [GO:2000845]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of proteasomal protein catabolic process [GO:0061136]; spermatid development [GO:0007286]; spermatid nucleus differentiation [GO:0007289] | endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleus [GO:0005634] | DNA binding [GO:0003677]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivator activity [GO:0030374] | PF12329;PF12325; | null | null | PTM: Phosphorylated by FER. {ECO:0000269|PubMed:9742951}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Note=Concentrated at the budding structures localized at the tips of cisternae. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Potential coactivator of the androgen receptor. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER (By similarity). Mediates STAT3 degradation. {ECO:0000250, ECO:0000269|PubMed:15467733}. | Mus musculus (Mouse) |
B9EKR1 | PTPRZ_MOUSE | MRILQSFLACVQLLCLCRLDWAYGYYRQQRKLVEEIGWSYTGALNQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTFIHNTGKTVEINLTNDYYLSGGLSEKVFKASKITFHWGKCNVSSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMDYLQNNFREQQYKFSRQVFSSYTGKEEIHEVVCSSEPENVQADPENYTSLLVTWERPRVVYDAMIEKFAVLYQPLAGNDQAKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAVCSNGLYGKYSDQLIVDMPTEDAELDLFPELIGTEEIIKEEEYGKDNEEDTGLNPGRDSVTNQIRKKEPQVSTTTHYNHMGTKYNEAKTNRSPTRGSEFSGKSDVPNTSPNSTSQHVAEFETERGISLPSQTGTNLPPHNVEGTSASLNSGSKTLFIFPQMNLSGTAESLNTVPITEYKEVSADVSEEENFLTDFKLDTGADDSSGSSPSTSTVPFSSDNLSHGYITSSDMPEAITYDVLKPGSTRNAPEDSAPSGSEESLKDPSLEGSVWFPGSTDLTTQSETGSGRESFLQVNSTDIQIDESRETTESFSPDATVSQDPSVTDMGMPHYSTFAYLPTEVTPQAFTPSSRPLDLAPTINILHSQTTQPVYNGETPLQPSYSSEVFPLATPLLLDNQTLNTTPAASSSDSALHATPVSPSVGVSFESILSSYDDAPLLPFSSASFSSEMFRHLHTVSQTLPQVTSAAERDELSLHASLLVARGDLLLEPSLVQYSDVASHQATTRAASDTLGFGSESAVFYKTSMVSQIESPRSDVVMHAYSSGPEPSYTVEGSHHVPTVSYSSAMPLHGSVDVSDQGSLLINPSHISMPESSFITPTASLLQPPPALSGDGEWSGASSDSELLLPDADGLRTLNISSPVSVAEFTYTTSVFADGIKPLSKSEMMYGNETELKMSSFSDMAYPSKSTVVPKMSDVVHKWSESLKETSVSISSMKSVFPESLVYPTTKGFEQGVSHVPEIIFPVQPTHTASQASGDTWLKPGLSANSEAAFSDTASREVVHPSTQPLLYEAATPFNTEALLQPSFQASDVDTLLKTALPSVPSDPILAGTPQVEQSSSSVSHPMASESGSSESMLHFTSVPILDISPSKVHSTPLQGLTVPHSSKKFSEQGLLKSKSPQQVLPSLFSNDEFFQSAHLDVSQAYPPKGRHAFVTPVLSIDEPQNTLINKLVYSEDIFSSTEISITDKVLTGLPTLASDVLSSTDHSVPLGSGPISLTMVSPNRDDSVTTAKLLLPSTATSKLTQSARSDADLVGGGEDGDDYDDDDYDDIDRGRFPVNKCMSCLPYRESREKVMNDSDTQESSLVDQSDPISPLLFENTEEENGGTGVTRVDKSPPPSMLPQNHNDGKEDSDIQMGSAVLPHTPGSKAWAVLTSDEESGSGQGTSDSLNDNETSTDFSFPDVNEKDTDGVLETDDTGIAPGSPRSSTPSVTSGHSGVSNSSEAEASNSSHESRIGLAEGLESEKKAVIPLVIVSALTFICLVVLVGILIYWRKCFQTAHFYLEDNTSPRVISTPPTPIFPISDDIGAIPIKHFPKHVADLHASNGFTEEFETLKEFYQEVQSCTADLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTKLKKGSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAILSKETEVPDSHIHSYVNTLLIPGPTGKTKLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMSEEHKCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLSLVSTRQEENPSTSLDSNGAALPDGNIAESLESLV | 3.1.3.48 | null | axonal fasciculation [GO:0007413]; axonogenesis [GO:0007409]; hematopoietic progenitor cell differentiation [GO:0002244]; learning or memory [GO:0007611]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of dendrite development [GO:2000171]; negative regulation of neuron apoptotic process [GO:0043524]; oligodendrocyte differentiation [GO:0048709]; peptidyl-tyrosine dephosphorylation [GO:0035335]; positive regulation of cell migration [GO:0030335]; positive regulation of dendrite development [GO:1900006]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of neuron migration [GO:2001224]; positive regulation of neuron projection development [GO:0010976]; positive regulation of oligodendrocyte differentiation [GO:0048714]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of Schwann cell migration [GO:1900149]; regulation of dendrite morphogenesis [GO:0048814]; regulation of myelination [GO:0031641]; regulation of oligodendrocyte progenitor proliferation [GO:0070445] | axon [GO:0030424]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; filopodium [GO:0030175]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; neuronal cell body [GO:0043025]; perineuronal net [GO:0072534]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; postsynaptic membrane [GO:0045211]; ruffle membrane [GO:0032587]; synapse [GO:0045202] | fibroblast growth factor binding [GO:0017134]; integrin binding [GO:0005178]; phosphatase activity [GO:0016791]; protein tyrosine phosphatase activity [GO:0004725] | PF00194;PF00041;PF00102; | 3.10.200.10;2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 5 subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21969550}; Single-pass type I membrane protein {ECO:0000269|PubMed:21969550}. Secreted {ECO:0000269|PubMed:21969550}. Note=A secreted form is apparently generated by shedding of the extracellular domain. | 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:16513268}; | null | null | null | null | FUNCTION: Protein tyrosine phosphatase that negatively regulates oligodendrocyte precursor proliferation in the embryonic spinal cord. Required for normal differentiation of the precursor cells into mature, fully myelinating oligodendrocytes. May play a role in protecting oligondendrocytes against apoptosis. May play a role in the establishment of contextual memory, probably via the dephosphorylation of proteins that are part of important signaling cascades. {ECO:0000269|PubMed:12355066, ECO:0000269|PubMed:16513268, ECO:0000269|PubMed:21969550}. | Mus musculus (Mouse) |
B9EXM2 | CARB_ORYSJ | MATSLSSAPTQLRPSPSPSHHRLLHRSSLLPFPRRHHHRRRRCGALSIARASASAKDGVTVRRFPAAPTEGGRLAGVRKIMILGAGPIVIGQACEFDYSGTQACKALAEEGYEVVLVNSNPATIMTDPDLAHRTYIGPMTPPLVERIIAAERPDALLPTMGGQTALNLAVSLADSGALDRLGVRLIGASLPAIRAAEDRQLFKQAMDRIGLKTPPSGIGTTLEECISIAEDIGEFPLIVRPAFTLGGTGGGIAYNRAEFEDICRAGLAASHTQQVLVEKSLLGWKEYELEVMRDMADNVVIICSIENIDPMGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSNVQFAVNPADGEVMVIEMNPRVSRSSALASKATGFPIAKMAAKLSVGYTLDQIPNDITKKTPASFEPSIDYVVTKIPRFAFEKFPGSEPVLTTQMKSVGEAMALGRTFQESFQKAVRSLETGFAGWGCAPIKELDWDWEKLKYSLRVPNPDRIHAIYAAFKKGMRIQDIHEISFIDKWFLTELKELVDVEQFLISRGLDQLSKDDFYQVKRRGFSDTQIAFATSSSETDVRLRRLALEVAPTYKRVDTCAAEFEANTPYMYSSYEYECESVPTNKKKVLILGGGPNRIGQGIEFDYCCCHASFALREAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVTNVIDLERPDGIIVQFGGQTPLKLALPIQQYLEDKKLVSASGTGLVKIWGTSPDSIDAAEDRKRFNAILEELGIEQPKGGIARSESDALSIASEVGYPVVVRPSYVLGGRAMEIVYNDEKLIKYLATAVQVDPERPVLVDKYLIDAIEIDVDALADSVGNVVIGGIMEHIEQAGIHSGDSACSLPTRTVSAKCLDIIRSWTTKLAKRLNVCGLMNCQYAITTSGEVFLLEANPRASRTVPFVSKAIGHPLAKYASLVMSGVTLPELGYTQEVVPKHVSVKEAVLPFEKFQGCDILLGPEMRSTGEVMGIDYEFSGAFAKAQIAAGQKLPLNGTVFLSLNDLTKRHLAEIGRGFRELGFNIIATSGTAKVLQLEGIPVEPVLKIHEGRPNARDMLKNGQIQVMVITSSGDALDSKDGLQLRRLALAYKVPIITTVDGARATIDAIKSLKNKSIETLALQDYFQTTDASQNLQAAQSAS | 6.3.4.16; 6.3.5.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409}; | arginine biosynthetic process [GO:0006526]; glutamine metabolic process [GO:0006541]; pyrimidine nucleotide biosynthetic process [GO:0006221] | chloroplast [GO:0009507]; cytoplasm [GO:0005737] | ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; metal ion binding [GO:0046872] | PF02786;PF02787;PF02142; | 3.40.50.20;3.30.1490.20;3.30.470.20;1.10.1030.10;3.40.50.1380; | CarB family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000250|UniProtKB:Q42601}; CATALYTIC ACTIVITY: [Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic]: Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000250|UniProtKB:P03965}; | null | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000250|UniProtKB:P03965}. | null | null | FUNCTION: Large subunit of the arginine-specific carbamoyl phosphate synthase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, hydrogencarbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate. {ECO:0000250|UniProtKB:Q42601}. | Oryza sativa subsp. japonica (Rice) |
B9F1C0 | SHOC1_ORYSJ | MRTRFLATDYFAPSSSSAAGKALALEFFSFPSLPVPALPPDPHFLPFTSADELPAATVADDGLGPLPIASALSDFLAAVIPQALPVPTVPAADEVLDDFLYDRGGYGEDFSSWEFGAFRIPKASEGYGVINREKDEKGEGSRSDGLEISSVMKRWEQLKELRFEVVEVDLLMALQEDIASFGEEESGGGVTLLLRVPDMKIHLDFIDIETDIKIRYQSDLPESVYQVEKVPVKDNDGNGHSSLREDCCLEIAALDHGAVIPRLEVSRNSWELDDCLTETDRYGVFDNVVRHLDEAQIQHSVFKSTEFLRSTDMDMLTFVCEDAPCHDIQVDKPAEIKAAVEMDVVRINGNILLEKNSALYPLKPDGTCSDLPCSILLEEVQIIDFPSDNVFKMLVQSETNKMNISDEIFKDDFDPARRLYESMVSCELALVDDTFRSLPTPILNDDIAVRSRVPPIQEILCSLKPHPLSASDGIYLDWHLLLEGPCNREICCSYASMVEEAKTCHLSSELQRSCQSTSVFVSDFLEDFQRSPKLQDEDKHSDIYVPAPLSHDPQKLEATQKCEQEGGTRNHSSMKRPSPEKSSSFPELISHSGDLNFYLNVRSATKSGTNNENTSTLDVPHSEEQALSLSTRAKVDKLIEIHPVSPSNLIQGLIEQIHASYTSALQESTYWRHSFSDEQGLGISKQKLLELITGEGSEGSYNHCEHKDKMELIVLYALKQVAYYLCFFGLHAAHLYISNLTRSLENTPERLKHILWSISEAQRKSERQLFESHPSLSCIETILRSNKQIDQKILIVADRAFWLPLGQKLASMRMTFVEFGQNPATTFVDLVNKTNSTAWVLEELLKSDCILLDNKNIPASFPFDKFGIILEYGGPNKSSTLLSLAPKLDGLPPLHFLYVKVDGKDFPAALVEDNHKDQDLKSTLDKVLLTLQKDLQERMNKMRIVDSLNFIPATNQLQGLQEKRSKHFAADATKELLPDDQPHRLQNLNKKNTFDSHNVVLADEQLHIQQTLSNKPVVNSQCVPTVEKSSSTSSVSANVLKDPQENQSTTDLPSCVKNDCIMPGRLSVPDVVIVVNTGNHGKTMLVSRRSSYQQILALEKGGMQVVERDIDLPVDLILSAAVCLVWYETALFEANELTTSAETSGIKENVENIATNILMSVSFSFTGCIMVFEGEADFLSAVMDSSDSLYTAAASLDMNLQLFFSHTPRSTDEIILNCITNVTSCYKAPLPDIPESESLAESFLTSFPSINPVSAYMLLSSGGSLVEFLSWPHERRIQAVGKYLLSPKIISLFNALCKFGELGESRSVMTECSSVDSDISSAFLQSPRKRKQRSLQACAVPTNKLLFSDSLNQIPGDYAEHAEVFSPSKLRKFSDMDNTIPELPDVFTFDESLNMRSEGFSYQQKKHDVDAIPGNQVINDDFSNGLTPNNQAYNRRTGNMVDTFDLPWQPEFGGTHPSKSTFHTSRPSCSRTHSNPVFSTAFEINDDPGEWNISGGTKQTWKGLAHGGTVDDSYRYDMDNRYHEPRDEIMQHPASSLAFQKLDFGSHATSQGSCWEIDYLRQMSAKRKARQERSRCSNSPGMSIPRMRDSNSKILNPPPKESFRYRGDRDTPSRDQSPSIGTQHYGKGKEGAKAQNRRARKDFNVQPTSHKKRIEPSIDPTWTPIDKRARQKLSFVTYGKEKQSKLVWRNQNSPGVGCGFRKRFREEGT | null | null | reciprocal meiotic recombination [GO:0007131]; resolution of meiotic recombination intermediates [GO:0000712] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | null | null | null | XPF family | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:31266799}. Nucleus {ECO:0000269|PubMed:30589140, ECO:0000269|PubMed:31266799}. Cytoplasm {ECO:0000269|PubMed:30589140}. Cell membrane {ECO:0000269|PubMed:30589140}. Note=Predominantly localized in the nucleus (PubMed:30589140). Localized in punctuate foci onto meiocyte chromosomes from leptotene to early pachytene with a maximal number of foci at zygotene (PubMed:31266799). {ECO:0000269|PubMed:30589140, ECO:0000269|PubMed:31266799}. | null | null | null | null | null | FUNCTION: Essential for normal crossover (CO) formation during meiosis (PubMed:30589140, PubMed:31266799). Essential component for the formation of class I meiotic COs (PubMed:31266799). Interacts with PTD, another meiotic component, to regulate CO formation, possibly by stabilizing the recombination intermediates during meiosis (PubMed:30589140, PubMed:31266799). SHOC1 and PTD may form transient heterotrimeric or heterotetrametric complexes with HEI10 and/or ZIP4 to promote class I COs formation (PubMed:31266799). Does not seem to be involved in early meiotic recombination steps involving double-strand break (DSB) formation, processing, and single-strand invasion (PubMed:31266799). Does not seem to be involved in homologous pairing or synaptonemal complex (SC) assembly (PubMed:31266799). {ECO:0000269|PubMed:30589140, ECO:0000269|PubMed:31266799}. | Oryza sativa subsp. japonica (Rice) |
B9FDE0 | BSK3_ORYSJ | MGGRVSKAVACCCCRSQHHGVVVESSEKTAEEDHGESYELPAFQEFSFEQLRLATSGFAVENIVSEHGEKAPNVVYKGKLDAQRRIAVKRFNRSAWPDPRQFLEEAKSVGQLRSKRLANLLGCCCEGDERLLVAEYMPNDTLAKHLFHWEAQAMKWPMRLRVVLYLAEALEYCTSKGRALYHDLNAYRVLFDDDCNPRLSCFGLMKNSRDGKSYSTNLAFTPPEYMRTGRITPESVIYSFGTLLLDVLSGKHIPPSHALDLIRDRNFNMLTDSCLEGQFSNEEGTELVRLASRCLHYEPRERPNVRSLVQALAPLQKDLETPSYELMDIPRGGATSVQSLLLSPLAEACSRKDLTAIHEILEKTGYKDDEGTANELSFQMWTNQMQDTLNSKKKGDNAFRQKDFSSAIDCYSQFIEVGTMVSPTIYARRCLSYLMNDKAEQALSDAMQALVISPTWPTAFYLQAAALLSLGMENEAQEAIKDGCAHETSSSSGH | 2.7.11.1 | null | brassinosteroid mediated signaling pathway [GO:0009742]; phosphorylation [GO:0016310]; positive regulation of brassinosteroid mediated signaling pathway [GO:1900459] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF07714; | 1.25.40.10;1.10.510.10; | null | PTM: Phosphorylated at Ser-213 and Ser-215 by BRI1. Phosphorylation at Ser-215 is required for its function in the regulation of brassinosteroid signaling. Phosphorylation by BRI1 disrupts the interaction between its TPR and kinase domains, thereby increasing the binding between its kinase domain and BSL1. {ECO:0000269|PubMed:26697897}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26697897}; Lipid-anchor {ECO:0000305|PubMed:26697897}. Note=Plasma membrane localization is required for its function in the regulation of brassinosteroid signaling. {ECO:0000269|PubMed:26697897}. | 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:0000305}; 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:0000305}; | null | null | null | null | FUNCTION: Probable serine/threonine kinase that acts as a positive regulator of brassinosteroid (BR) signaling downstream of BRI1. {ECO:0000269|PubMed:26697897}. | Oryza sativa subsp. japonica (Rice) |
B9FMJ3 | KN13A_ORYSJ | MGDSGDAVMARWLQSAGLQHLAASSTSSSSASTAGGGVDPRGGGGVGVGALGGGAGGGSLLPSLLMQGYGPQSIEEKQRLYMLLRSLNFNGETAPPSISEPYTPTAQSFGGGNSLEGFYSPELRGELGAGLLDLHAMDDTELLSEDVASEPFEPSPFIPKEMDEDDDDMLPGSQPGPSDNYNAVANEKESTARENNVAKIKVVVRKRPLNRKEVSRKEEDIITVHDSSSLTVYEPKLKVDLTAYVEKHEFCFDAVLDEQVSNDEVYRETVEPIIPIIFQRTKATCFAYGQTGSGKTYTMQPLPLRAAQDMVRLLHQPVYRNQNFKLWLSYFEIYGGKLFDLLSDRRQLLMREDGKKQVCIVGLQEFEVSDVQIVKEYIERGNAARSTGSTGANEESSRSHAILQLAIKKHIIVTDTRRQRDRDANESKNTKAVGKISFIDLAGSERGADTTDNDRQTRIEGAEINKSLLALKECIRALDNDQIHIPFRGSKLTEVLRDSFVGNSRTVMISCISPNAGSCEHTLNTLRYADRVKSLSKGSNTRKEQPTGPTIPSSKDSSSAPSYPMPIETEEIANQIQEKRPVETSRKAAENFTSNSSMEPDRNPVSMIPSYSNRGKEENGSSGLNDRERVDLNSSRISYNSKPQSVQSSANLQEEEKVTKVSPPRRKAYRDDKPERQSNYAKKDSGPETSRPGYKVQQAKQLQQQQRPTSASASQNSSRQSEKESSCDDVEIDAILEEEEALIAAHRKEIENTMEIVREEMNLLAEVDQPGSLIDNYVTQLSFLLSRKAAGLVSLQARLARFQHRLKEQEILSRKKSSR | null | null | metaxylem development [GO:0090058]; microtubule depolymerization [GO:0007019]; microtubule-based movement [GO:0007018]; plant-type secondary cell wall biogenesis [GO:0009834]; regulation of cell wall organization or biogenesis [GO:1903338]; trichome morphogenesis [GO:0010090] | endoplasmic reticulum [GO:0005783]; Golgi stack [GO:0005795]; intracellular membrane-bounded organelle [GO:0043231]; microtubule [GO:0005874]; secondary cell wall [GO:0009531] | ATP binding [GO:0005524]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, KIN-13 subfamily | null | SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:20587735}. | null | null | null | null | null | null | Oryza sativa subsp. japonica (Rice) |
B9J3S4 | COLQ1_BACCQ | MNKKSKINKVMLSISTMALSLGALQAPASAEEKVPYNVLKTKPVGIEKPVDEIGHVSKAEETLSFQERLKVGDFSQRPASIPNKAAVKQVKESYSMADLNKMNDQELVETLGCIKWHQITDLFQFNEDAKAFYKDKGKMQVIIDELAHRGSTFTRDDSKGIQTFTEVLRSAFYLAFYNNELSELNERSFQDKCLPALKAIAKNPNFKLGTAEQDTVVSAYGKLISNASSDVETVQYASNILKQYNDNFNTYVNDRMKGQAIYDIMQGIDYDIQSYLIEARKEANETMWYGKVDGFINEINRIALLNEVTPENKWLVNNGIYFASRLGKFHSNPNKGLEVVTQAMHMYPRLSEPYFVAVEQITTNYNGKDYSGNTVDLEKIRKEGKEQYLPKTYTFDDGSIVFKTGDKVSEEKIKRLYWAAKEVKAQYHRVIGNDKALEPGNADDILTIVIYNSPEEYQLNRQLYGYETNNGGIYIEETGTFFTYERTPEQSIYSLEELFRHEFTHYLQGRYEVPGLFGRGDMYQNERLTWFQEGNAEFFAGSTRTNNVVPRKSIISGLSSDPASRYTAERTLFAKYGSWDFYNYSFALQSYLYTHQFETFDKIQDLIRANDVKNYDAYRENLSKDPKLNKEYQEYMQQLIDNQDKYNVPAVADDYLAEHAPKSLTAVEKEMTETLPMKDAKMTKHSSQFFNTFTLEGTYTGSVTKGESEDWNAMSKKVNEVLEQLAQKEWSGYKTVTAYFVNYRVNSSNEFEYDVVFHGIAKDDGENKAPTVNINGPYNGLVKEGIQFKSDGSKDEDGKIVSYLWDFGDGRTSTEVNPVHVYEREGSYKVALIVKDDKGKESKSETTVTVKDGSLTESEPNNRPEEANRIGLNTTIKGSLIGGDHTDVYTFNVASAKDIDISVLNEYGIGMTWVLHHESDMQNYAAYGQANGNHIEANFNAKPGEYYLYVYKYDNGDGTYKLSVK | 3.4.24.3 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q9X721}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9X721}; | proteolysis [GO:0006508] | extracellular region [GO:0005576] | metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF18496;PF01752;PF08453;PF18911;PF04151; | 1.10.390.20;2.60.120.380;3.30.980.50;3.40.30.160;2.60.40.10; | Peptidase M9B family, Collagenase subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33603127}. | CATALYTIC ACTIVITY: Reaction=Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3'.; EC=3.4.24.3; Evidence={ECO:0000269|PubMed:33603127}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.36 uM for gelatin {ECO:0000269|PubMed:33603127}; KM=1.72 uM for native collagen from rat tail {ECO:0000269|PubMed:33603127}; Note=kcat is 7.7 sec(-1) with gelatin as substrate (PubMed:33603127). kcat is 2.1 sec(-1) with native collagen from rat tail as substrate (PubMed:33603127). {ECO:0000269|PubMed:33603127}; | null | null | null | FUNCTION: Acts as a true collagenase, which is highly active and cleaves natively folded collagen (PubMed:33603127). In vitro, can also cleave gelatin and the synthetic peptide FALGPA (furylacryloyl-Leu-Gly-Pro-Ala) (PubMed:33603127). Causes damage on dermal collagen (COL), resulting in gaps in the tissue, which might lead to an accelerated bacterial infiltration and penetration into deeper sites of the host (PubMed:35310821). {ECO:0000269|PubMed:33603127, ECO:0000269|PubMed:35310821}. | Bacillus cereus (strain Q1) |
B9J8S0 | PDA_RHIR8 | MSYSFMSPPNAARFVLSNATVPAVTVVGFTGPSSEGLMKADIVVADGLIKDILPAGTAPAELAKADMRDGMVWPTFADMHTHLDKGHIWERRANPDGSFMGALDAVRSDREANWSAADVRKRMEFSLRAAYAHGTSLIRTHLDSLAPQHRISFEVFSEVREAWKDKIALQAVALFPLDFMVDDAFFADLTTVVREAGGLLGGVTQMNPDIDAQLDKLIRAAAANGLDIDLHVDETEDREVLTLKAIAAAVLRNGFTGKVTAGHCCSLARQDENVAAATIDLVAKAGISIVALPMCNMYLQDRHPGRTPRWRGVTLLHELAAAGVPTAVASDNTRDPFYAYGDLDPVEVFREAVRILHLDHPLDTAARVVTTSPASILGRPDIGRIAVGGPADLVLFSARRWSEFLSRPQSDRVVLRKGKVIDRSLPDYRELDTVIGA | 3.5.4.11 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:P25524}; | cytosine catabolic process [GO:0006209] | null | cytosine deaminase activity [GO:0004131]; isoguanine deaminase activity [GO:0035888]; metal ion binding [GO:0046872]; pterin deaminase activity [GO:0050228]; sepiapterin deaminase activity [GO:0050279] | PF07969; | 3.20.20.140;2.30.40.10; | Metallo-dependent hydrolases superfamily, Pterin deaminase family | null | null | CATALYTIC ACTIVITY: Reaction=a 2-amino-4-hydroxypteridine + H(+) + H2O = a 2,4-dihydroxypteridine + NH4(+); Xref=Rhea:RHEA:36055, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:73184, ChEBI:CHEBI:73186; EC=3.5.4.11; Evidence={ECO:0000269|PubMed:23256477}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O + sepiapterin = NH4(+) + xanthopterin-B2; Xref=Rhea:RHEA:14025, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16095, ChEBI:CHEBI:17953, ChEBI:CHEBI:28938; Evidence={ECO:0000269|PubMed:23256477}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12 uM for formylpterin {ECO:0000269|PubMed:23256477}; KM=27 uM for pterin-6-carboxylate {ECO:0000269|PubMed:23256477}; KM=13 uM for pterin-7-carboxylate {ECO:0000269|PubMed:23256477}; KM=39 uM for pterin {ECO:0000269|PubMed:23256477}; KM=23 uM for hydroxymethylpterin {ECO:0000269|PubMed:23256477}; KM=47 uM for biopterin {ECO:0000269|PubMed:23256477}; KM=61 uM for D-(+)-neopterin {ECO:0000269|PubMed:23256477}; KM=5.7 uM for isoxanthopterin {ECO:0000269|PubMed:23256477}; KM=22 uM for sepiapterin {ECO:0000269|PubMed:23256477}; KM=50 uM for folate {ECO:0000269|PubMed:23256477}; KM=40 uM for xanthopterin {ECO:0000269|PubMed:23256477}; KM=37 uM for 7,8-dihydro-hydroxymethylpterin {ECO:0000269|PubMed:23256477}; KM=200 uM for 7,8-dihydroneopterin {ECO:0000269|PubMed:23256477}; KM=93 uM for 7,8-dihydrobiopterin {ECO:0000269|PubMed:23256477}; Note=kcat is 64 sec(-1) with formylpterin as substrate. kcat is 110 sec(-1) with pterin-6-carboxylate as substrate. kcat is 48 sec(-1) with pterin-7-carboxylate as substrate. kcat is 131 sec(-1) with pterin as substrate. kcat is 28 sec(-1) with hydroxymethylpterin as substrate. kcat is 46 sec(-1) with biopterin as substrate. kcat is 19 sec(-1) with D-(+)-neopterin as substrate. kcat is 1.6 sec(-1) with isoxanthopterin as substrate. kcat is 2.9 sec(-1) with sepiapterin as substrate. kcat is 6.4 sec(-1) with folate as substrate. kcat is 0.46 sec(-1) with xanthopterin as substrate. kcat is 1.2 sec(-1) with 7,8-dihydro-hydroxymethylpterin as substrate. kcat is 0.036 sec(-1) with 7,8-dihydroneopterin as substrate. kcat is 0.090 sec(-1) with 7,8-dihydrobiopterin as substrate. {ECO:0000269|PubMed:23256477}; | null | null | null | FUNCTION: Catalyzes the deamination of many pterin metabolites, such as formylpterin, pterin-6-carboxylate, pterin-7-carboxylate, pterin, hydroxymethylpterin, biopterin, D-(+)-neopterin, isoxanthopterin, sepiapterin, folate, xanthopterin, and 7,8-dihydrohydroxymethylpterin. May be involved in a degradative pathway for catabolizing pterin rings. {ECO:0000269|PubMed:23256477}. | Rhizobium rhizogenes (strain K84 / ATCC BAA-868) (Agrobacterium radiobacter) |
B9K712 | IYD_THENN | MKMLYDLAKKRKTVRRFKKEKPPLEDLIYSLKVANEAPSGMNAQPWRFLIVEDEKLKGQIRRVCERSEKTFYENVRGRLKEWLDEKRFTWRKPFLKEAPYLLLVFSEKSAPYSRESVWLAVGYLLLALEEKGLGSVPYTPPDFREVEKLVNTPSELRLEVILPVGYPDDPKPKYPRNEVIVRYNTF | 1.21.1.1 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:34748729}; | thyroid hormone metabolic process [GO:0042403]; tyrosine metabolic process [GO:0006570] | null | FMN binding [GO:0010181]; iodotyrosine deiodinase activity [GO:0140616]; tyrosine binding [GO:0072545] | PF00881; | 3.40.109.10; | Nitroreductase family | null | null | CATALYTIC ACTIVITY: Reaction=2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH; Xref=Rhea:RHEA:32479, ChEBI:CHEBI:15378, ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349; EC=1.21.1.1; Evidence={ECO:0000269|PubMed:34748729}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:32481; Evidence={ECO:0000269|PubMed:34748729}; CATALYTIC ACTIVITY: Reaction=iodide + L-tyrosine + NADP(+) = 3-iodo-L-tyrosine + NADPH; Xref=Rhea:RHEA:27453, ChEBI:CHEBI:16382, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:59898; Evidence={ECO:0000269|PubMed:34748729}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27455; Evidence={ECO:0000269|PubMed:34748729}; CATALYTIC ACTIVITY: Reaction=3-iodo-L-tyrosine + iodide + NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + NADPH; Xref=Rhea:RHEA:27457, ChEBI:CHEBI:15378, ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59898; Evidence={ECO:0000269|PubMed:34748729}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27459; Evidence={ECO:0000269|PubMed:34748729}; CATALYTIC ACTIVITY: Reaction=chloride + L-tyrosine + NADP(+) = 3-chloro-L-tyrosine + NADPH; Xref=Rhea:RHEA:70343, ChEBI:CHEBI:17996, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:189422; Evidence={ECO:0000269|PubMed:34748729}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70345; Evidence={ECO:0000269|PubMed:34748729}; CATALYTIC ACTIVITY: Reaction=bromide + L-tyrosine + NADP(+) = 3-bromo-L-tyrosine + NADPH; Xref=Rhea:RHEA:70347, ChEBI:CHEBI:15858, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:189423; Evidence={ECO:0000269|PubMed:34748729}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70349; Evidence={ECO:0000269|PubMed:34748729}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.22 uM for 3-iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:34748729}; KM=3.5 uM for 3-iodo-L-tyrosine (at pH 7.4 and 60 degrees Celsius) {ECO:0000269|PubMed:34748729}; KM=4200 uM for 2-iodophenol (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:34748729}; KM=0.14 uM for 3-bromo-L-tyrosine (at pH 7.4 and 60 degrees Celsius) {ECO:0000269|PubMed:34748729}; KM=5 uM for 3-chloro-L-tyrosine (at pH 7.4 and 60 degrees Celsius) {ECO:0000269|PubMed:34748729}; KM=6600 uM for 2-iodophenol (at pH 7.4 and 60 degrees Celsius) {ECO:0000269|PubMed:34748729}; Note=kcat is 1.6 min(-1) for the dehalogenation of 3-iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:34748729). kcat is 27 min(-1) for the dehalogenation of 3-iodo-L-tyrosine (at pH 7.4 and 60 degrees Celsius) (PubMed:34748729). kcat is 0.84 min(-1) for the dehalogenation of 2-iodophenol (at pH 7.4 and 25 degrees Celsius) (PubMed:34748729). kcat is 6.5 min(-1) for the dehalogenation of 2-iodophenol (at pH 7.4 and 60 degrees Celsius) (PubMed:34748729). kcat is 5.1 min(-1) for the dehalogenation of 3-bromo-L-tyrosine (at pH 7.4 and 60 degrees Celsius) (PubMed:34748729). kcat is 2.9 min(-1) for the dehalogenation of 3-chloro-L-tyrosine (at pH 7.4 and 60 degrees Celsius) (PubMed:34748729). {ECO:0000269|PubMed:34748729}; | null | null | null | FUNCTION: Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine (PubMed:34748729). Activity towards 2-iodophenol is weak (PubMed:34748729). {ECO:0000269|PubMed:34748729}. | Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E) |
B9K7M5 | BGLA_THENN | MKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGDVACDHYNRWKEDIEIIEKIGAKAYRFSISWPRILPEGTGKVNQKGLDFYNRIIDTLLEKNITPFITIYHWDLPFSLQLKGGWANRDIADWFAEYSRVLFENFGDRVKHWITLNEPWVVAIVGHLYGVHAPGMKDIYVAFHTVHNLLRAHAKSVKVFRETVKDGKIGIVFNNGYFEPASEREEDIRAARFMHQFNNYPLFLNPIYRGEYPDLVLEFAREYLPRNYEDDMEEIKQEIDFVGLNYYSGHMVKYDPNSPARVSFVERNLPKTAMGWEIVPEGIYWILKGVKEEYNPQEVYITENGAAFDDVVSEGGKVHDQNRIDYLRAHIEQVWRAIQDGVPLKGYFVWSLLDNFEWAEGYSKRFGIVYVDYNTQKRIIKDSGYWYSNVIKNNGLTD | 3.2.1.21; 3.2.1.74 | null | cellulose catabolic process [GO:0030245] | cytosol [GO:0005829] | glucan 1,4-beta-glucosidase activity [GO:0031217]; scopolin beta-glucosidase activity [GO:0102483] | PF00232; | 3.20.20.80; | Glycosyl hydrolase 1 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-linkages in (1->4)-beta-D-glucans, to remove successive glucose units.; EC=3.2.1.74; Evidence={ECO:0000269|PubMed:10960102}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.; EC=3.2.1.21; Evidence={ECO:0000269|PubMed:10960102}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=28.6 mM for cellobiose {ECO:0000269|PubMed:10960102}; KM=4.55 mM for cellotriose {ECO:0000269|PubMed:10960102}; KM=2.15 mM for cellotetraose {ECO:0000269|PubMed:10960102}; Note=kcat is 285.0, 345.7 and 333.7 sec(-1) for the hydrolysis of cellobiose, cellotriose and cellotetraose, respectively.; | PATHWAY: Glycan metabolism; cellulose degradation. {ECO:0000303|PubMed:10960102}.; PATHWAY: Glycan metabolism; beta-D-glucan degradation. {ECO:0000303|PubMed:10960102}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:10960102}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 95 degrees Celsius. Is highly thermostable, retaining 85% activity after incubation for 9 hours at 90 degrees Celsius and 88% activity after 1 hour at 95 degrees Celsius. {ECO:0000269|PubMed:10960102}; | FUNCTION: Broad substrate specificity glycosidase. Releases glucose from soluble glucooligomers, with a preference for longer oligomers; acts more readily on cellotetraose than on cellobiose. Displays similar activities towards the disaccharides lactose and cellobiose. Is also able to hydrolyze various aryl-beta-glycosides in vitro. {ECO:0000269|PubMed:10960102}. | Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E) |
B9KDD4 | PGLB_CAMLR | MKLQQNFTDNNSIKYTCILILIAFAFSVLCRLYWVAWASEFYEFFFNDQLMITTNDGYAFAEGARDMIAGFHQPNDLSYFGSSLSTLTYWLYSILPFSFESIILYMSAFFASLIVVPIILIAREYKLTTYGFIAALLGSIANSYYNRTMSGYYDTDMLVLVLPMLILLTFIRLTINKDIFTLLLSPVFIMIYLWWYPSSYSLNFAMIGLFGLYTLVFHRKEKIFYLTIALMIIALSMLAWQYKLALIVLLFAIFAFKEEKINFYMIWALIFISILILHLSGGLDPVLYQLKFYVFKASDVQNLKDAAFMYFNVNETIMEVNTIDPEVFMQRISSSVLVFILSFIGFILLCKDHKSMLLALPMLALGFMALRAGLRFTIYAVPVMALGFGYFLYAFFNFLEKKQIKLSLRNKNILLILIAFFSISPALMHIYYYKSSTVFTSYEASILNDLKNKAQREDYVVAWWDYGYPIRYYSDVKTLIDGGKHLGKDNFFSSFVLSKEQIPAANMARLSVEYTEKSFKENYPDVLKAMVKDYNKTSAKDFLESLNDKDFKFDTNKTRDVYIYMPYRMLRIMPVVAQFANTNPDNGEQEKSLFFSQANAIAQDKTTGSVMLDNGVEIINDFRALKVEGASIPLKAFVDIESITNGKFYYNEIDSKAQIYLLFLREYKSFVILDESLYNSSYIQMFLLNQYDQDLFEQITNDTRAKIYRLKR | 2.4.99.19 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21677752}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:21677752, ECO:0000269|PubMed:29058712}; | post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279] | plasma membrane [GO:0005886] | dolichyl-diphosphooligosaccharide-protein glycotransferase activity [GO:0004579]; glycosyltransferase activity [GO:0016757]; magnesium ion binding [GO:0000287] | PF02516;PF21436;PF18527; | 3.40.1380.40; | STT3 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000269|PubMed:21677752}. | CATALYTIC ACTIVITY: Reaction=tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine = tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine.; EC=2.4.99.19; Evidence={ECO:0000269|PubMed:21677752, ECO:0000269|PubMed:24149797}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 uM for an Asp-Gln-Asn-Ala-Thr pentapeptide {ECO:0000269|PubMed:23382388}; Note=Glycosylates at a rate of 1.55 peptides per second per OST. {ECO:0000269|PubMed:23382388}; | PATHWAY: Protein modification; protein glycosylation. {ECO:0000305|PubMed:23382388}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8. {ECO:0000269|PubMed:24149797}; | null | FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (GalNAc(2)GlcGalNAc(3)Bac(NAc)(2) in eubacteria, where Bac(NAc)(2) is di-N-acetyl bacillosamine) from the lipid carrier undecaprenol-pyrophosphate to an asparagine residue within an Asp/Glu-Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. {ECO:0000269|PubMed:21677752, ECO:0000269|PubMed:24149797}. | Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060) |
B9NAE4 | NRP31_POPTR | MPSPEEDPQPLLKDQEETAYDSDGKVLSFGIDYDTESGGSTVVPSFSWRKLWLFTGPGFLMCIAFLDPGNLEGDLQAGAIAGYSLLWLLLWATAMGLLVQLLSARLGVATGRHLAELCREEYPTWARMILWIMAELALIGADIQEVIGSAIAIQILSNGVLPLWAGVIITASDCFIFLFLENYGVRKLEAAFGILIGIMAVTFAWMFADAKPSAPELFLGILIPKLSSKTIKQAVGVVGCIIMPHNVFLHSALVQSREIDHNKKGQVQEALRYYSIESTAALAISFMINLFVTTIFAKGFHGTELANSIGLVNAGQYLQDKYGGGFFPILYIWGIGLLAAGQSSTITGTYAGQFIMGGFLNLGLKKWLRALITRSCAIIPTIIVALVFDTSEDSLDVLNEWLNMLQSIQIPFALIPLLCLVSKEQIMGTFTVGPILKMVSWLVAALVMLINGYLLLDFFSNEVTGVVFTTVVCAFTGAYVTFIIYLISREVTISTWYCPT | null | null | defense response to bacterium [GO:0042742]; intracellular iron ion homeostasis [GO:0006879]; intracellular manganese ion homeostasis [GO:0030026]; iron ion transmembrane transport [GO:0034755]; iron ion transport [GO:0006826]; manganese ion transmembrane transport [GO:0071421]; manganese ion transport [GO:0006828]; positive regulation of reactive oxygen species metabolic process [GO:2000379] | trans-Golgi network membrane [GO:0032588]; vacuolar membrane [GO:0005774] | cadmium ion transmembrane transporter activity [GO:0015086]; manganese ion transmembrane transporter activity [GO:0005384]; metal ion transmembrane transporter activity [GO:0046873] | PF01566; | null | NRAMP (TC 2.A.55) family | null | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:35700212}; Multi-pass membrane protein {ECO:0000255}. Note=Localized to intracellular punctuate structures. {ECO:0000269|PubMed:35700212}. | CATALYTIC ACTIVITY: Reaction=Mn(2+)(in) = Mn(2+)(out); Xref=Rhea:RHEA:28699, ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:35700212}; CATALYTIC ACTIVITY: Reaction=Fe(2+)(in) = Fe(2+)(out); Xref=Rhea:RHEA:28486, ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:35700212}; | null | null | null | null | FUNCTION: Divalent metal transporter (PubMed:35700212). Can transport manganese (Mn) and iron (Fe) (PubMed:35700212). Involved in the control of cell-to-cell transport of manganese (Mn) between organs and tissues to monitor Mn homeostasis (PubMed:35700212). {ECO:0000269|PubMed:35700212}. | Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa) |
B9TSP7 | FACR6_ARATH | MATTNVLATSHAFKLNGVSYFSSFPRKPNHYMPRRRLSHTTRRVQTSCFYGETSFEAVTSLVTPKTETSRNSDGIGIVRFLEGKSYLVTGATGFLAKVLIEKLLRESLEIGKIFLLMRSKDQESANKRLYDEIISSDLFKLLKQMHGSSYEAFMKRKLIPVIGDIEEDNLGIKSEIANMISEEIDVIISCGGRTTFDDRYDSALSVNALGPGRLLSFGKGCRKLKLFLHFSTAYVTGKREGTVLETPLCIGENITSDLNIKSELKLASEAVRKFRGREEIKKLKELGFERAQHYGWENSYTFTKAIGEAVIHSKRGNLPVVIIRPSIIESSYNEPFPGWIQGTRMADPIILAYAKGQISDFWADPQSLMDIIPVDMVANAAIAAMAKHGCGVPEFKVYNLTSSSHVNPMRAGKLIDLSHQHLCDFPLEETVIDLEHMKIHSSLEGFTSALSNTIIKQERVIDNEGGGLSTKGKRKLNYFVSLAKTYEPYTFFQARFDNTNTTSLIQEMSMEEKKTFGFDIKGIDWEHYIVNVHLPGLKKEFLSKKKTE | 1.2.1.84 | null | long-chain fatty-acyl-CoA metabolic process [GO:0035336]; response to wounding [GO:0009611]; suberin biosynthetic process [GO:0010345] | chloroplast [GO:0009507] | alcohol-forming long-chain fatty acyl-CoA reductase activity [GO:0102965]; alcohol-forming very long-chain fatty acyl-CoA reductase activity [GO:0080019] | PF07993;PF03015; | 3.40.50.720; | Fatty acyl-CoA reductase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:22166367}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + hexadecanoyl-CoA + 2 NADPH = CoA + hexadecan-1-ol + 2 NADP(+); Xref=Rhea:RHEA:36315, ChEBI:CHEBI:15378, ChEBI:CHEBI:16125, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.84; Evidence={ECO:0000269|PubMed:22166367}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36316; Evidence={ECO:0000269|PubMed:22166367}; CATALYTIC ACTIVITY: Reaction=2 H(+) + hexadecanoyl-[ACP] + 2 NADPH = hexadecan-1-ol + holo-[ACP] + 2 NADP(+); Xref=Rhea:RHEA:54328, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16125, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64479, ChEBI:CHEBI:78483; Evidence={ECO:0000269|PubMed:22166367}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54329; Evidence={ECO:0000269|PubMed:22166367}; CATALYTIC ACTIVITY: Reaction=a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+); Xref=Rhea:RHEA:52716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77396, ChEBI:CHEBI:83139; EC=1.2.1.84; Evidence={ECO:0000269|PubMed:19062129}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.48 uM for C16:0-ACP (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:22166367}; KM=3.36 uM for C16:0-CoA (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:22166367}; Vmax=293 pmol/min/mg enzyme with C16:0-ACP as substrate (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:22166367}; Vmax=357.6 pmol/min/mg enzyme with C16:0-CoA as substrate (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:22166367}; | null | null | null | FUNCTION: Catalyzes the reduction of fatty acyl-CoA and -ACP (acyl carrier protein) substrates to fatty alcohols (PubMed:19062129, PubMed:22166367). Triggers the accumulation of C16 and, to a lower extent, of C18 fatty alcohols; converts palmitoyl-acyl carrier protein to the corresponding C16:0 alcohol with NAD(P)H as electron donor (PubMed:22166367). Triggers also the formation of some C16:0 and C18:0 aldehydes (PubMed:22166367). May be involved in the generation of C30 primary alcohol (PubMed:16980563). {ECO:0000269|PubMed:16980563, ECO:0000269|PubMed:19062129, ECO:0000269|PubMed:22166367}. | Arabidopsis thaliana (Mouse-ear cress) |
B9U3F2 | DISP3_CHICK | MDTEDDPLLQDAWLDEEDEEVAFSSRKRREGALLCGKSSCRVRPLRVTLPVSGFWNIVGWIFTNPYCAGFILFLGCAIPAVLAVVMFLHYPALDIDISYNAFEIRNHESSQRFDALALALKSQFGSWGRNRRDLADFTSETLQRLIFEQLQQLHLNASHLQVSTRAKRSAPQGRTSSPEPRAHPHPGNETSRVTRGAPRWDYSNTYISANTQTHAHWRIELIFLARGDSENNIFTTERLVTIHEVERKIMDHPRFREFCWKPHEVLKDLPLGSYSYCSPPSSLMTYFFPTERGGKIYYDGMGQDLADIQGSLELAMTHPEFYWYVDEGLSAENKKSSLLRSEILFGAPLPNYYSVEDRWEEQRHKFQNFVVTYVAMLAKQSTSKVQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAVLVYILTSCSVFLSFFGIASIGLSCLVALFLYHVVFGIQYLGILNGVAAFVIVGIGVDDVFVFINTYRQATHLKDLRLRMIHTIQTAGKATFFTSLTTAAAYAANIFSQIPAVHDFGLFMSLIVSCCWVAVLFTMPAALGIWTLYVSPLESSCQNSCSQKCTKKSTLHLAEDLFVASEGTSRAGRETLPYLDDDIPLLSVEEEPVSLEMGDVPLVSVMPENLQLPVEKSNRGHLIAHLQELLEHWVLWSAVKSRWVIVGLFLLVLLLSIFFASRLRPASRAPVLFRPDTNIQVLLDLKYNLSAEGISCITCSGLFQEKPHSLQNNFRTSLEKKKRGSASPWGSKGSISDTGQQDLQGTVYISKSRSKGRPAIYRFSLNASIPAPWQMVSPGDGEVPSFQVYRVPFGNFTRKLTACVSTVGLLKQTSPRKWMMTTLSCDSKRGWKFDFSFYVAAKEQQRTRKLYFAQSHKPPYHGRVCVAPPGCLLSSSPDGPTKGILYVPSEKAAPKARLSATSGFNPCMNMGCGKPAVRPLVDTGAMVFVVFGIRGVNRTKNSDNHVIGDMGSVIYDDSFDLFKEIGNLCRLCKAIASNTELVKPGGAQCLPSGYSISSFLQMLHPECKNIPEPNLLPGQLSHGAVGVKDGKVQWISMAFESTTYKGKSSFQTYADYLKWETFLQQQLQLFPEGSALRHGFQTCEHWKQIFMEIIGVQSALYGLILSLVICVAAVAVFTTHILLLLPVLLSILGVVCLVVTIMYWSGWEMGAVEAISLSILVGSSVDYCVHLVEGYLLAGENLPLHHAEDPTACRQWRTIEAIRHVGVAIVSSAVTTVIATVPLFFCIIAPFAKFGKIVALNTGVSILYTLTVSTALLSIMGPGTFTRSRTSCLKAVAGVLLAGLLGLCICLALLKGGFKIPLPNGTAL | null | null | cell differentiation [GO:0030154]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; negative regulation of neuron differentiation [GO:0045665]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of neural precursor cell proliferation [GO:2000179]; response to hormone [GO:0009725] | cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nuclear membrane [GO:0031965] | null | PF02460; | 1.20.1640.10; | Patched family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19179482}; Multi-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:19179482}; Multi-pass membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:19179482}; Multi-pass membrane protein {ECO:0000305}. Note=Predominantly localized to cholesterol-enriched domains within membranes (PubMed:19179482). Localizes to cytoplasmic punctate vesicular structures (PubMed:19179482). {ECO:0000269|PubMed:19179482}. | null | null | null | null | null | FUNCTION: Plays a role in neuronal proliferation and differentiation (By similarity). Plays a role in the accumulation of cellular cholesterol (PubMed:19179482). Involved in intracellular lipid droplet formation (PubMed:19179482). May contribute to cholesterol homeostasis in neuronal cells (PubMed:19179482). {ECO:0000250|UniProtKB:Q9P2K9, ECO:0000269|PubMed:19179482}. | Gallus gallus (Chicken) |
B9V5F5 | CE63A_XENLA | MEALLQGLQRQDRMGALQDSCEAELQELMKQIDIMLDHKRSQWEAETETMKTRLELKEQELNCALDREERLNQEVRRLRQQLIQQEEETQNKTTQYEAQLSGFKEELNRLKKSYEKVQKKHLRSEMKAKAEEERSEVSRLTRRLEEFRQRSLDWEKQRLLYQQQLAGLEAQRKTLIEQTEMYQHQSHNRKQMLEQTSLVGRSELQNLSGQLHRANDSLCAKEEELETLKIQLRCAVEGQKRAEHETELSKQAVQALKEEKAELRATLQAHTEFLQGSRVQKHELLPEGYRGSEVLRENNSIRSVEERLQEMGQVGGETEVEAIRSKLSVSRMNEHRLQAEVTCLEDSVESVTSQCQLLAKELKGKEEYFHGVKEDHQKCLSENKKLKGQLSQAELTHKSVLDGMRKEISQLTQELHQRDIRMASSAGIDWERKIKAERQRAEREAAEHRMSLNALENLRQENCRLSELLQTQEPDVAQALVNLEQANQRLQRELLQTQEKLELIAQRRESEIQNAVDSISQELLNKQEQELRIMQERLKVYEQEMQTFRSQQDAASSGSSLESIFSEVWKEQATGSPISAASVDSAIEPVEDLASSLPVPPTSPANAVASRFLQEEEQRSHELLQRLNAHIEELKQESQRTVEHFTQAR | null | null | cell division [GO:0051301]; centriole replication [GO:0007099]; de novo centriole assembly involved in multi-ciliated epithelial cell differentiation [GO:0098535]; DNA damage checkpoint signaling [GO:0000077]; signal transduction in response to DNA damage [GO:0042770]; spindle assembly [GO:0051225] | centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; spindle pole [GO:0000922] | null | PF17045; | null | CEP63 family | PTM: Phosphorylation at Ser-560 by atm and atr promotes its delocalization from the centrosome and impairs its ability to promote centrosome dependent spindle assembly. {ECO:0000269|PubMed:19182792}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q96MT8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P0CB05}. | null | null | null | null | null | FUNCTION: Required for normal spindle assembly (PubMed:19182792). Plays a key role in mother-centriole-dependent centriole duplication (PubMed:19182792). Plays a role in DNA damage response (PubMed:19182792). Following DNA damage, such as double-strand breaks (DSBs), is removed from centrosomes; this leads to the inactivation of spindle assembly and delay in mitotic progression (PubMed:19182792). {ECO:0000269|PubMed:19182792}. | Xenopus laevis (African clawed frog) |
B9VRJ2 | COR15_PAPSO | MESNGVPMITLSSGIRMPALGMGTVETMEKGTEREKLAFLKAIEVGYRHFDTAAAYQTEECLGEAIAEALQLGLIKSRDELFITSKLWCADAHADLVLPALQNSLRNLKLDYLDLYLIHHPVSLKPGKFVNEIPKDHILPMDYKSVWAAMEECQTLGFTRAIGVCNFSCKKLQELMATANSPPVVNQVEMSPTLHQKNLREYCKANNIMITAHSVLGAVGAAWGTKAVMHSKVLHQIAVARGKSVAQVSMRWVYQQGASLVVKSFNEARMKENLKIFDWELTAEDMEKISEIPQSRTSSAAFLLSPTGPFKTEEEFWDEKD | 1.1.1.247 | null | alkaloid metabolic process [GO:0009820] | cytosol [GO:0005829] | alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; codeinone reductase (NADPH) activity [GO:0047036] | PF00248; | 3.20.20.100; | Aldo/keto reductase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11079569}. Note=Present in the cytosolic part of laticifer cells that secrete latex. {ECO:0000269|PubMed:11079569}. | CATALYTIC ACTIVITY: Reaction=codeine + NADP(+) = codeinone + H(+) + NADPH; Xref=Rhea:RHEA:19209, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57871, ChEBI:CHEBI:58349, ChEBI:CHEBI:58473; EC=1.1.1.247; Evidence={ECO:0000269|PubMed:22098111, ECO:0000269|PubMed:29779229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19210; Evidence={ECO:0000269|PubMed:29779229}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19211; Evidence={ECO:0000269|PubMed:29779229}; CATALYTIC ACTIVITY: Reaction=NADP(+) + neopine = H(+) + NADPH + neopinone; Xref=Rhea:RHEA:75135, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59950, ChEBI:CHEBI:194190; EC=1.1.1.247; Evidence={ECO:0000269|PubMed:29779229}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75137; Evidence={ECO:0000269|PubMed:29779229}; CATALYTIC ACTIVITY: Reaction=morphine + NADP(+) = H(+) + morphinone + NADPH; Xref=Rhea:RHEA:14321, ChEBI:CHEBI:15378, ChEBI:CHEBI:57728, ChEBI:CHEBI:57783, ChEBI:CHEBI:58097, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:29779229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14322; Evidence={ECO:0000269|PubMed:29779229}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14323; Evidence={ECO:0000269|PubMed:29779229}; CATALYTIC ACTIVITY: Reaction=NADP(+) + neomorphine = H(+) + NADPH + neomorphinone; Xref=Rhea:RHEA:75971, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:194188, ChEBI:CHEBI:194513; Evidence={ECO:0000269|PubMed:29779229}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75973; Evidence={ECO:0000269|PubMed:29779229}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.7 uM for codeinone {ECO:0000269|PubMed:29779229}; KM=32.1 uM for codeine {ECO:0000269|PubMed:29779229}; KM=36 uM for NADPH {ECO:0000269|PubMed:29779229}; KM=46.2 uM for NADP(+) {ECO:0000269|PubMed:29779229}; Vmax=38.2 nmol/min/mg enzyme with codeinone as substrate {ECO:0000269|PubMed:29779229}; Vmax=45.6 nmol/min/mg enzyme with codeine as substrate {ECO:0000269|PubMed:29779229}; Vmax=75.3 nmol/min/mg enzyme with NADPH as substrate {ECO:0000269|PubMed:29779229}; Vmax=113.1 nmol/min/mg enzyme with NADP(+) as substrate {ECO:0000269|PubMed:29779229}; Note=kcat is 0.023 sec(-1) with codeinone as substrate (PubMed:29779229). kcat is 0.027 sec(-1) with codeine as substrate (PubMed:29779229). kcat is 0.045 sec(-1) with NADPH as substrate (PubMed:29779229). kcat is 0.067 sec(-1) with NADP(+) as substrate (PubMed:29779229). {ECO:0000269|PubMed:29779229}; | PATHWAY: Alkaloid biosynthesis; morphine biosynthesis. {ECO:0000269|PubMed:29779229}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8 for reduction (forward reaction) of codeinone to codeine and 9.0-10.0 for the oxidation (reverse reaction) of codeine to codeinone. {ECO:0000269|PubMed:29779229}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-42 degrees Celsius. {ECO:0000269|PubMed:29779229}; | FUNCTION: NADPH-dependent codeinone reductase involved in biosynthesis of morphinan-type benzylisoquinoline and opiate alkaloids natural products (PubMed:15543134, PubMed:29779229). Reduces codeinone to codeine in the penultimate step in morphine biosynthesis (PubMed:15543134, PubMed:22098111, PubMed:29779229). Can use morphinone, hydrocodone and hydromorphone as substrate during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrate during oxidative reaction with NADP as cofactor (PubMed:29779229). Converts morphinone to morphine, and neomorphinone to neomorphine (By similarity). Reduces irreversibly neopinone, a spontaneous isomer of codeinone, to neopine; in planta, neopine levels are limited to low levels (PubMed:29779229). {ECO:0000250|UniProtKB:Q9SQ68, ECO:0000269|PubMed:15543134, ECO:0000269|PubMed:22098111, ECO:0000269|PubMed:29779229}. | Papaver somniferum (Opium poppy) |
B9VUU3 | POLG_HE71 | MGSQVSTQRSGSHENSNSATEGSTINYTTINYYKDSYAATAGKQSLKQDPDKFANPVKDIFTEMAAPLKSPSAEACGYSDRVAQLTIGNSTITTQEAANIIVGYGEWPSYCSDSDATAVDKPTRPDVSVNRFYTLDTKLWEKSSKGWYWKFPDVLTETGVFGQNAQFHYLYRSGFCIHVQCNASKFHQGALLVAVLPEYVIGTVAGGTGTEDSHPPYKQTQPGADGFELQHPYVLDAGIPISQLTVCPHQWINLRTNNCATIIVPYINALPFDSALNHCNFGLLVVPISPLDYDQGATPVIPITITLAPMCSEFAGLRQAVTQGFPTELKPGTNQFLTTDDGVSAPILPNFHPTPCIHIPGEVRNLLELCQVETILEVNNVPTNATSLMERLRFPVSAQAGKGELCAVFRADPGRNGPWQSTLLGQLCGYYTQWSGSLEVTFMFTGSFMATGKMLIAYTPPGGPLPKDRATAMLGTHVIWDFGLQSSVTLVIPWISNTHYRAHARDGVFDYYTTGLVSIWYQTNYVVPIGAPNTAYIIALAAAQKNFTMKLCKDASDILQTGTIQGDRVADVIESSIGDSVSRALTQALPAPTGQNTQVSSHRLDTGKVPALQAAEIGASSNASDESMIETRCVLNSHSTAETTLDSFFSRAGLVGEIDLPLEGTTNPNGYANWDIDITGYAQMRRKVELFTYMRFDAEFTFVACTPTGEVVPQLLQYMFVPPGAPKPDSRESLAWQTATNPSVFVKLSDPPAQVSVPFMSPASAYQWFYDGYPTFGEHKQEKDLEYGACPNNMMGTFSVRTVGTSKSKYPLVVRIYMRMKHVRAWIPRPMRNQNYLFKANPNYAGNSIKPTGTSRTAITTLGKFGQQSGAIYVGNFRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCNCQTGVYYCNSRRKHYPVSFSKPSLIYVEASEYYPARYQSHLMLAQGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQGVSDYIKGLGDAFGTGFTDAVSREVEALKSYLIGSEGAVEKILKNLIKLISALVIVIRSDYDMVTLTATLALIGCHGSPWAWIKAKTASILGIPIAQKQSASWLKKFNDMANAAKGLEWVSNKISKFIDWLKEKIVPAAKEKVEFLNNLKQLPLLENQISNLEQSAASQEDLEVMFGNVSYLAHFCRKFQPLYATEAKRVYALEKRMNNYMQFKSKHRIEPVCLIIRGSPGTGKSLATGIIARAIADKYHSSVYSLPPDPDHFDGYKQQVVTVMDDLCQNPDGKDMSLFCQMVSTVDFIPPMASLEEKGVSFTSKFVIASTNATNIIVPTVSDSDAIRRRFYMDCDIEVTDSYKTDLGRLDAGRAAKLCSENNTANFKRCSPLVCGKAIQLRDRKSKVRYSVDTVVSELIREYSNRSAIGNTIEALFQGPPKFRPIRIGLEEKPAPDAISDLLASVDSEEVRQYCRDQGWIIPETPTNVERHLNRAVLVMQSIATVVAVVSLVYVIYKLFAGFQGAYSGAPKQVLKKPALRTATVQGPSLDFALSLLRRNVRQVQTDQGHFTMLGVRDRLAVLPRHSQPGKTIWIEHKLVNVLDAVELVDEQGVNLELTLITLDTNEKFRDITKFIPENISTASDATLVINTEHMPSMFVPVGDVVQYGFLNLSGKPTHRTMMYNFPTKAGQCGGVVTSVGKVIGIHIGGNGRQGFCAGLKRSYFASEQGEIQWVKPNKETGRLNINGPTRTKLEPSVFHDVFEGSKEPAVLHSKDPRLEVDFEQALFSKYVGNTLHVPDEYIREAALHYANQLKQLDIDTTQMSMEEACYGTDNLEAIDLHTSAGYPYSALGIKKRDILDPTTRDVSKMKFYMDKYGLDLPYSTYVKDELRSIDKIKKGKSRLIEASSLNDSVYLRMAFGHLYETFHANPGTVTGSAVGCNPDVFWSKLPILLPGSLFAFDYSGYDASLSPVWFRALELVLREIGYSEEAVSLIEGINHTHHVYRNKTYCVLGGMPSGCSGTSIFNTMINNIIIRALLIKTFKGIDLDELNMVAYGDDVLASYPFPIDCLELAKTGKEYGLTMTPADKSPCFNEVNWENATFLKRGFLPDEQFPFLIHPTMPMKEIHESIRWTKDARNTQDHVRSLCLLAWHNGKQEYEKFVSSIRSVPIGKALAIPNYENLRRNWLELF | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence of 3CDpro or 3CPro (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03313}; | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:0039522]; symbiont genome entry into host cell via pore formation in plasma membrane [GO:0044694]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity [GO:0039554]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity [GO:0039540]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049] | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule activity [GO:0005198] | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP4]: Myristoylation is required during RNA encapsidation and formation of the mature virus particle. {ECO:0000250|UniProtKB:P03300}.; PTM: [Viral protein genome-linked]: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication. {ECO:0000250|UniProtKB:P03300}. | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Protein 3AB]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000250|UniProtKB:Q66478}.; SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm.; SUBCELLULAR LOCATION: [Protein 3CD]: Host nucleus {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000250|UniProtKB:P03300}. Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. | CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACTIVITY: [Protease 2A]: Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.; EC=3.4.22.29; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: [Protease 3C]: Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222}; | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of the capsid (By similarity). Capsid protein VP1, together with VP2, interacts with host cell receptor SCARB2 to provide virion attachment to target host cells (By similarity). This attachment induces virion internalization. This attachment induces virion internalization (By similarity). After binding to its receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (By similarity). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:Q66479}.; FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP2, together with VP1, interacts with host cell receptor SCARB2 to provide virion attachment to target host cells (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:Q66479}.; FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid shell (By similarity). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Capsid protein VP0]: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity). Allows the capsid to remain inactive before the maturation step (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protease 2A]: Cysteine protease that cleaves viral polyprotein and specific host proteins (By similarity). It is responsible for the autocatalytic cleavage between the P1 and P2 regions, which is the first cleavage occurring in the polyprotein (By similarity). Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation (By similarity). Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity). Counteracts stress granule formation probably by antagonizing its assembly or promoting its dissassembly (By similarity). Cleaves and inhibits host IFIH1/MDA5, thereby inhibiting the type-I IFN production and the establishment of the antiviral state (By similarity). Cleaves and inhibits host MAVS, thereby inhibiting the type-I IFN production and the establishment of the antiviral state (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:Q66478}.; FUNCTION: [Protein 2B]: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell (By similarity). In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (By similarity). Activates also the mitochondrial apoptotic pathway by activating host BAX (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:Q66478}.; FUNCTION: [Protein 2C]: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3AB]: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3A]: Localizes the viral replication complex to the surface of membranous vesicles (By similarity). It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction (By similarity). This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity). Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU (By similarity). The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (By similarity). Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity). During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3CD]: Involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the 5'UTR of the viral genome. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protease 3C]: Major viral protease that mediates proteolytic processing of the polyprotein (By similarity). Cleaves host EIF5B, contributing to host translation shutoff (By similarity). Cleaves also host PABPC1, contributing to host translation shutoff (By similarity). Disassembles host cytoplasmic stress granules by cleaving host G3BP1, although this effect is less prononced than the inhibition induced by protease 2A (By similarity). Cleaves host RIGI and thus contributes to the inhibition of type I interferon production (By similarity). Cleaves host IRF7 and thus contributes to the inhibition of type I interferon production (By similarity). Cleaves host HNRNPA1 thereby increasing the translation of apoptosis protease activating factor APAF1, leading to apoptosis of the host cell (By similarity). Cleaves host NLRP1, triggers host N-glycine-mediated degradation of the autoinhibitory NLRP1 N-terminal fragment (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03303, ECO:0000250|UniProtKB:Q66478}.; FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated. {ECO:0000250|UniProtKB:P03300}. | Human enterovirus 71 (EV71) (EV-71) |
B9VVJ6 | CK12_TRYBB | MSVELRVGNRFRIGQKIGSGSFGEIFRGTNIQTGDPVAIKLEQVKTRHPQLAFEARFYRVLNAGGGVVGIPNVLYHGVEGEFNVMVIDLLGPSLEDLFSFCGRRLSLKTTLMLAEQMIARIEFVHSKSIIHRDIKPDNFLMGTGKKGHHVYIIDFGLAKKYRDARTHQHIPYKEGKSLTGTARYCSINTHIGIEQSRRDDLEGIGYILMYFLRGSLPWQGLKAHTKQEKYARISDRKQTTSVETLCRSFPAEFAAYLNYTRSLHFEDKPDYSYLKRLFRELFVREGYHVDYVFDWTLKRIHDTLQEGRADQQQQQQQQQQRRGSEKEDEHPV | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19450734, ECO:0000269|PubMed:27002830}; | endocytosis [GO:0006897]; non-motile cilium assembly [GO:1905515]; phosphorylation [GO:0016310]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; regulation of circadian rhythm [GO:0042752]; regulation of ubiquitin-dependent protein catabolic process [GO:2000058]; signal transduction [GO:0007165]; spindle assembly [GO:0051225] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; spindle microtubule [GO:0005876] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | 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=2.7.11.1; Evidence={ECO:0000269|PubMed:19450734, ECO:0000269|PubMed:27002830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:19450734, ECO:0000269|PubMed:27002830}; 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:0000269|PubMed:19450734, ECO:0000269|PubMed:27002830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000269|PubMed:19450734, ECO:0000269|PubMed:27002830}; | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is about 27 degrees Celsius. Loses activity at 41 degrees Celsius. {ECO:0000269|PubMed:27002830}; | FUNCTION: Serine/threonine protein kinase (PubMed:19450734, PubMed:27002830). May phosphorylate ZC3H11 during unstressed conditions, leading to proteasome-dependent degradation of ZC3H11 (PubMed:27002830). {ECO:0000269|PubMed:19450734, ECO:0000269|PubMed:27002830}. | Trypanosoma brucei brucei |
B9W4V6 | APO1_CYCAE | MKYFPLFPTLVFAARVVAFPAYASLAGLSQQELDAIIPTLEAREPGLPPGPLENSSAKLVNDEAHPWKPLRPGDIRGPCPGLNTLASHGYLPRNGVATPVQIINAVQEGLNFDNQAAVFATYAAHLVDGNLITDLLSIGRKTRLTGPDPPPPASVGGLNEHGTFEGDASMTRGDAFFGNNHDFNETLFEQLVDYSNRFGGGKYNLTVAGELRFKRIQDSIATNPNFSFVDFRFFTAYGETTFPANLFVDGRRDDGQLDMDAARSFFQFSRMPDDFFRAPSPRSGTGVEVVIQAHPMQPGRNVGKINSYTVDPTSSDFSTPCLMYEKFVNITVKSLYPNPTVQLRKALNTNLDFFFQGVAAGCTQVFPYGRD | 1.11.2.1 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:15294788}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group. {ECO:0000269|PubMed:15294788}; | hydrogen peroxide catabolic process [GO:0042744] | null | heme binding [GO:0020037]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF01328; | 1.10.489.10; | Chloroperoxidase family | PTM: N-glycosylated. {ECO:0000269|PubMed:19434406}. | null | CATALYTIC ACTIVITY: Reaction=RH + H2O2 = ROH + H2O.; EC=1.11.2.1; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=37 uM for ABTS (at pH 4.5) {ECO:0000269|PubMed:15294788, ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254}; KM=1001 uM for benzyl alcohol (at pH 7) {ECO:0000269|PubMed:15294788, ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254}; KM=298 uM for dimethoxyphenol (at pH 7) {ECO:0000269|PubMed:15294788, ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254}; KM=1313 uM for hydrogen peroxide (at pH 7) {ECO:0000269|PubMed:15294788, ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254}; KM=320 uM for naphthalene (at pH 7) {ECO:0000269|PubMed:15294788, ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254}; KM=69 uM for pyridine (at pH 7) {ECO:0000269|PubMed:15294788, ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254}; KM=2367 uM for veratryl alcohol (at pH 7) {ECO:0000269|PubMed:15294788, ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.7 with ABTS as substrate. Optimum pH is 7.2 with benzyl alcohol as substrate, and there is another optimum at pH 6.2. Optimum pH is 7.2 with dimethoxyphenol as substrate. Optimum pH is 6.0 with naphthalene as substrate. Optimum pH is 7.0 with pyridine as substrate. Optimum pH is 7.0 with veratryl alcohol as substrate, and there is another optimum at pH 5.5. {ECO:0000269|PubMed:15294788, ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254}; | null | FUNCTION: Aromatic peroxidase that oxidizes aryl alcohols into the corresponding aldehydes and then into the corresponding benzoic acids. Oxidizes toluene and naphthalene. Catalyzes the regioselective peroxide-dependent hydroxylation of propranolol and diclofenac to 5-hydroxypropranolol and 4'-hydroxydiclofenac. Catalyzes the regioselective peroxide-dependent hydroxylation of naphthalene to 1-naphthol or 2-naphthol via a naphthalene 1,2-oxide intermediate. Catalyzes the regioselective peroxide-dependent oxidation of pyridine to pyridine N-oxide. Halogenates monochlorodimedone and phenol. Oxidizes the sulfur-containing heterocycle dibenzothiophene to yield ring-hydroxylation products and to a lesser extent sulfoxidation products. {ECO:0000269|PubMed:15294788, ECO:0000269|PubMed:16253244, ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:18815784, ECO:0000269|PubMed:19022254, ECO:0000269|PubMed:19039585, ECO:0000269|PubMed:19394224}. | Cyclocybe aegerita (Black poplar mushroom) (Agrocybe aegerita) |
B9W5G6 | ACTPC_ACTFR | SADVAGAVIDGAGLGFDVLKTVLEALGNVKRKIAVGIDNESGKTWTAMNTYFRSGTSDIVLPHKVAHGKALLYNGQKNRGPVATGVVGVIAYSMSDGNTLAVLFSVPYDYNWYSNWWNVRVYKGQKRADQRMYEELYYHRSPFRGDNGWHSRGLGYGLKSRGFMNSSGHAILEIHVTKA | null | null | cytolysis in another organism [GO:0051715]; monoatomic cation transport [GO:0006812]; pore complex assembly [GO:0046931] | extracellular region [GO:0005576]; nematocyst [GO:0042151]; other organism cell membrane [GO:0044218]; pore complex [GO:0046930] | channel activity [GO:0015267]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; toxin activity [GO:0090729] | PF06369; | 2.60.270.20; | Actinoporin family, Sea anemone subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19563820}. Nematocyst {ECO:0000250|UniProtKB:P07845}. Target cell membrane {ECO:0000269|PubMed:19563820, ECO:0000269|PubMed:21300287, ECO:0000269|PubMed:25716479}. Note=Forms an alpha-helical membrane channel in the prey. {ECO:0000269|PubMed:19563820, ECO:0000269|PubMed:21300287, ECO:0000269|PubMed:25716479}. | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Stable up to about 53 degrees Celsius. {ECO:0000269|PubMed:31295915}; | FUNCTION: Pore-forming toxin (PFT) that consists of a crown-shaped octamer or nonamer that forms cation-selective hydrophilic pores of about 1.5 nm (inside) and 13 nm (outside) (PubMed:21300287, PubMed:25716479). It causes cardiac stimulation and cytolysis (EC(50)=1.6 nM on erythrocytes) (PubMed:19563820, PubMed:25759390, PubMed:31295915). Interestingly, the Phe-16 is crucial for hemolysis (PubMed:25759390). Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of monomers (PubMed:19563820, PubMed:25716479). It is probable that a dimeric form is an assembly intermediate before the complete oligomerization (PubMed:25716479). The formation of stable pores occurs only in vesicles composed of DOPC/SM (there is no oligomerization when the PFT is treated with vesicles of DOPC or SM alone) (PubMed:25716479). The transmembrane pore displays 8 lateral perforations, one at each subunit-subunit interface, partially occupied by the acyl-chain region of a bridging lipid (PubMed:25716479). Each pore contains 24 lipid molecules, firmly bound to each subunit, that is, 3 lipids (L1, L2, L3, L4 and/or L5) are associated to each subunit (PubMed:25716479). Lipid L1 bridges 2 subunits, whereas lipids L2 and L3 bind to sites at single subunit (PubMed:25716479). {ECO:0000269|PubMed:19563820, ECO:0000269|PubMed:21300287, ECO:0000269|PubMed:25716479, ECO:0000269|PubMed:25759390}. | Actinia fragacea (Strawberry anemone) |
B9WFG1 | ARO1_CANDC | MSIERVPILGKETIHVGYGIADHIVNEVIANLASSTYVIVTDTNMARTPQYSKLTDDFKTNLSKKRPESRLLTYCVSPGENNKNRVTKAAVEDFLLQQGCTRDTVILAVGGGVIGDMIGFVAATFMRGVRVVQVPTTLLAMVDSSVGGKTAIDTPLGKNFIGAFHQPEYVFCDVSFLETLPARQFINGMAEVVKTAAIWNEEEFTRLENFSKKFLSVVTSKKPDLQSIKAELVKTVLESVRVKAGVVSSDEKEAGLRNLLNFGHTIGHAIEAVLTPEALHGECVSIGMIKEAELSRYLGILPPVAVARLSKCLVAYGLPVSIDDKEFLKKVGPKRHYVEIDILLKKMAIDKKNDGSKIRCVLLEKIGKCYQLKAHQVSKQDLSFVLTDEVLVHPFTNPPKENIIVPPGSKSISNRALILAALGNGTVRVKNLLHSDDTKHMLDAVASLKGAEISTEDNGETIVVKGNGGNLVTCGEELYLGNAGTASRFLTTVASLVGKSPASDDVILTGNARMQERPIGPLVDALRSNGSEIEYLNKQGSLPLKISAGNGLKGGRIELAATISSQYVSSILMCAPYAKEPVTLALVGGKPISQLYIDMTCAMMKSFGIEVTKSTTEEYTYHIPKGIYKNPTEYVIESDASSATYPLAFAAMTGTSCTIPNIGSSSLQGDARFAVDVLKPMGCKVEQTATSTTVTGPPRGHLKPLPHVDMEPMTDAFLTASVVAAVAKGGSTSITGIANQRVKECNRIEAMVTELAKFGVSANELPDGIEIHGIDIKDLKTPEISDRGVCSYDDHRVAMSFSLLAGLCKEPVLILERSTTGKTWPGWWDILHSKFKIELDGYEPPFNTDKHVIKSSDKGVIVIGMRGTGKSTLSEWLASFLGFKMLDMDKYLEEKLGTDIKSLIKAKGWEHFRKEEAIVAKECFTKFSKGYVLSTGGGIVEGEDARQQLKSYADNGGIVLHLHRDLDETVTFLAADTTRPAYSSEVQEVWLRREKWYHECSNYHFYSSHCSTEDEFNHLRKSFVNYIKLITGAERSVVPTGRSTAVVLTLPDLNNVAGDLESITIGADAVELRVDLLKDTSAAFVAAQIATTRKHADLPIIYTVRTVSQGGKFPDENVDELKSLLLLGIRLGVAYIDLQLTAPNELIEEISSKKGFTRIIGTYQDINGELKWNNVEWKNKYNQGVSMNADIVRLVGRANSIQDNLDLEDFKKQNTLKPLIAFNLGTQGKLSQVLNGTFTPISHQLLPNDDGLLTIGEINQTYFDIGGFTAKKFWVIGSPIEHSRSPNLHNAGYKALNLPYQFGRFEATDVDVVYDNLINKSDFGGLAITMPLKLDIMKFATKLSDAAETIGAVNTLIPVEGGYFGDNTDWVGISNSFIRAGVPPKSSSNGLVVGAGGTSRAAIYALHQMGCTKIYLVNRTVAKLEELVKSFPKDYNLEIVETEQQADKVNKVLLAVSCIPADKPLDSDVLKKIERILSNGSEQVAGFKPTLLEASYKPRVTPIMKLAEEQYKWKVIPGVEMLVNQGDRQFKLHTGFSAPYEIIHRAVVEE | 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}. | Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast) |
B9X187 | NMP1A_XENLA | MAGDVEGGGCRVSWGALLTLLLLPLPSLCTLASGKEPHVIKLYEGKVVRYNESKNFCYQRTYEPKWSDVWTKIQIRVNSTKMIRVTQVENEEKLKEMETFNMFDLFSSFLKEKLNDTFIYVDLYSNKTCIKVHVIDTDTYYSVALSRGFDPRLCFLFLCGLLLFFYGDALSRSQLFFYSTGITIGMLASMLILVFMLSKLMPKKSPFVALLLGGWSVSIYIIQLVFKNLQAICSEYWQYLLGYLGIVGFVSFAFCYKYGPLENDRSINILTWTLQLIGLLLMYISVQIQHIAVTMVVIAFCTKQIEYPVQWIYILYRKIKRKRAKPSPPRLLTEEEYRKQGEIETRKALEELRGYCSSPDFATWKMISRIQSPKRFADFVEGSSHLTPNEVSVHEHEYGLGGSFLEDELFGEDSDIEVEMDIEQPLYLVPRSCF | null | null | erythrocyte enucleation [GO:0043131]; erythrocyte maturation [GO:0043249]; eye development [GO:0001654] | nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637] | protein self-association [GO:0043621] | PF10225; | null | NEMP family | PTM: Phosphorylated. {ECO:0000269|PubMed:25946333}. | SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}; Multi-pass membrane protein; Nucleoplasmic side {ECO:0000269|PubMed:19167377}. Nucleus envelope {ECO:0000269|PubMed:19167377}. Note=Localization in the nuclear membrane is essential for its function. Colocalizes with lamins and banf1-a/b at the nuclear envelope. {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}. | null | null | null | null | null | FUNCTION: In concert with ran, required for proper eye development (PubMed:25946333). May be involved in the expression of early eye marker genes (PubMed:19167377). Contributes to nuclear envelope stiffness in germ cells (By similarity). Required for fertility (By similarity). Essential for normal erythropoiesis (By similarity). Required for efficient nuclear envelope opening and enucleation during the late stages of erythroblast maturation (By similarity). {ECO:0000250|UniProtKB:O14524, ECO:0000250|UniProtKB:Q6ZQE4, ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}. | Xenopus laevis (African clawed frog) |
B9XZG7 | RNJ_HELP8 | MTDNNHYENNESNENSSENSKVDEARAGAFERFTNRKKRFRENAQKNGESSHHEAPSHHKKEHRPNKKPNNHHKQKHAKTRNYAKEELDSNKVEGVTEILHVNERGTLGFHKELKKGVETNNKIQVEHLNPHYKMNLNSKASVKITPLGGLGEIGGNMMVIETPKSAIVIDAGMSFPKEGLFGVDILIPDFSYLHQIKDKIAGIIITHAHEDHIGATPYLFKELQFPLYGTPLSLGLIGSKFDEHGLKKYRSYFKIVEKRCPISVGEFIIEWIHITHSIIDSSALAIQTKAGTIIHTGDFKIDHTPVDNLPTDLYRLAHYGEKGVMLLLSDSTNSHKSGTTPSESTIAPAFDTLFKEAQGRVIMSTFSSNIHRVYQAIQYGIKYNRKIAVIGRSMEKNLDIARELGYIHLPYQSFIEANEVAKYPDNEVLIVTTGSQGETMSALYRMATDEHRHISIKPNDLVIISAKAIPGNEASVSAVLNFLIKKEAKVAYQEFDNIHVSGHAAQEEQKLMLRLIKPKFFLPVHGEYNHVARHKQTAISCGVPEKNIYLMEDGDQVEVGPAFIKKVGTIKSGKSYVDNQSNLSIDTSIVQQREEVASAGVFAATIFVNKNKQALLESSQFSSLGLVGFKDEKHLIKEIQGGLEMLLKSSNAEILNNPKKLEDHTRNFIRKALFKKFRKYPAIICHAHSF | 3.1.-.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01491}; Note=Binds up to 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or Mg(2+) is physiologically important. {ECO:0000255|HAMAP-Rule:MF_01491}; | mRNA processing [GO:0006397]; rRNA processing [GO:0006364] | cytoplasm [GO:0005737] | 5'-3' RNA exonuclease activity [GO:0004534]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521]; zinc ion binding [GO:0008270] | PF00753;PF07521;PF17770; | 3.10.20.580;3.40.50.10710;3.60.15.10; | Metallo-beta-lactamase superfamily, RNA-metabolizing metallo-beta-lactamase-like family, Bacterial RNase J subfamily | PTM: Acetylated on nine lysine residues. Some of the residues are acetylated by multiple different mechanisms. RimL is partially responsible for the acetylation of Lys-323, Lys-397 and Lys-649. HPB8_1270 homolog is partially responsible for the acetylation of Lys-323, Lys-397, Lys-511 and Lys-649. Acetyl-phosphate-mediated non-enzymatic acetylation pathway takes part in the acetylation of Lys-134, Lys-323, Lys-397, Lys-511 and Lys-649. Acetylation of the remaining residues Lys-140, Lys-337, Lys-547 and Lys-634 occurs by a yet undetermined mechanism. Acetylation on a number of these residues is important for growth regulation and proper cell morphology. {ECO:0000269|PubMed:38057323}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491, ECO:0000269|PubMed:23093592}. Note=The RNaseJ-RhpA complex co-localizes with 70S ribosomes and polysomes; remains associated with ribosomes in the absence of RhpA. {ECO:0000269|PubMed:23093592}. | null | null | null | null | null | FUNCTION: An RNase that has 5'-3' exoribonuclease and endoribonuclease activity (PubMed:23093592, PubMed:38057323). Degrades 5'-monophosphorylated ssRNA and dsRNA, considerably more active on ssRNA (PubMed:23093592). Association with RhpA significantly increases the dsRNase activity (PubMed:23093592). Degrades RNA substrate with hairpin structures at both ends with low activity, but presence of RhpA significantly increases the activity on this substrate (PubMed:38057323). Stimulates ATPase activity of RNA helicase RhpA (PubMed:23093592). Involved in stabilization of mRNA but apparently not rRNA (PubMed:23093592). {ECO:0000269|PubMed:23093592, ECO:0000269|PubMed:38057323}. | Helicobacter pylori (strain B128) |
C0H5F4 | RH2B_PLAF7 | MKTTLFCSISFCNIIFFFLELSHEHFVGQSSNTHGASSVTDFNFSEEKNLKSFEGKNNNNDNYASINRLYRKKPYMKRSLINLENDLFRLEPISYIQRYYKKNINRSDIFHNKKERGSKVYSNVSSFHSFIQEGKEEVEVFSIWGSNSVLDHIDVLRDNGTVVFSVQPYYLDIYTCKEAILFTTSFYKDLDKSSITKINEDIEKFNEEIIKNEEQCLVGGKTDFDNLLIVLENAEKANVRKTLFDNTFNDYKNKKSSFYNCLKNKKNDYDKKIKNIKNEITKLLKNIESTGNMCKTESYVMNNNLYLLRVNEVKSTPIDLYLNRAKELLESSSKLVNPIKMKLGDNKNMYSIGYIHDEIKDIIKRYNFHLKHIEKGKEYIKRITQANNIADKMKKDELIKKIFESSKHFASFKYSNEMISKLDSLFIKNEEILNNLFNNIFNIFKKKYETYVDMKTIESKYTTVMTLSEHLLEYAMDVLKANPQKPIDPKANLDSEVVKLQIKINEKSNELDNAISQVKTLIIIMKSFYDIIISEKASMDEMEKKELSLNNYIEKTDYILQTYNIFKSKSNIINNNSKNISSKYITIEGLKNDIDELNSLISYFKDSQETLIKDDELKKNMKTDYLNNVKYIEENVTHINEIILLKDSITQRIADIDELNSLNLININDFINEKNISQEKVSYNLNKLYKGSFEELESELSHFLDTKYLFHEKKSVNELQTILNTSNNECAKLNFMKSDNNNNNNNSNIINLLKTELSHLLSLKENIIKKLLNHIEQNIQNSSNKYTITYTDINNRMEDYKEEIESLEVYKHTIGNIQKEYILHLYENDKNALAVHNTSMQILQYKDAIQNIKNKISDDIKILKKYKEMNQDLLNYYEILDKKLKDNTYIKEMHTASLVQITQYIPYEDKTISELEQEFNNNNQKLDNILQDINAMNLNINILQTLNIGINACNTNNKNVEHLLNKKIELKNILNDQMKIIKNDDIIQDNEKENFSNVLKKEEEKLEKELDDIKFNNLKMDIHKLLNSYDHTKQNIESNLKINLDSFEKEKDSWVHFKSTIDSLYVEYNICNQKTHNTIKQQKNDIIELIYKRIKDINQEIIEKVDNYYSLSDKALTKLKSIHFNIDKEKYKNPKSQENIKLLEDRVMILEKKIKEDKDALIQIKNLSHDHFVNADNEKKKQKEKEEDDEQTHYSKKRKVMGDIYKDIKKNLDELNNKNLIDITLNEANKIESEYEKILIDDICEQITNEAKKSDTIKEKIESYKKDIDYVDVDVSKTRNDHHLNGDKIHDSFFYEDTLNYKAYFDKLKDLYENINKLTNESNGLKSDAHNNNTQVDKLKEINLQVFSNLGNIIKYVEKLENTLHELKDMYEFLETIDINKILKSIHNSMKKSEEYSNETKKIFEQSVNITNQFIEDVEILKTSINPNYESLNDDQIDDNIKSLVLKKEEISEKRKQVNKYITDIESNKEQSDLHLRYASRSIYVIDLFIKHEIINPSDGKNFDIIKVKEMINKTKQVSNEAMEYANKMDEKNKDIIKIENELYNLINNNIRSLKGVKYEKVRKQARNAIDDINNIHSNIKTILTKSKERLDEIKKQPNIKREGDVLNNDKTKIAYITIQINNGRIESNLLNILNMKHNIDTILNKAMDYMNDVSKSDQIVINIDSLNMNDIYNKDKDLLINILKEKQNMEAEYKKMNEMYNYVNETEKEIIKHKKNYEIRIMEHIKKETNEKKKKFMESNNKSLTTLMDSFRSMFYNEYINDYNINENFEKHQNILNEIYNGFNESYNIINTKMTEIINDNLDYNEIKEIKEVAQTEYDKLNKKVDELKNYLNNIKEQEGHRLIDYIKEKIFNLYIKCSEQQNIIDDSYNYITVKKQYIKTIEDVKFLLDSLNTIEEKNKSVANLEICTNKEDIKNLLKHVIKLANFSGIIVMSDTNTEITPENPLEDNDLLNLQLYFERKHEITSTLENDSDLELDHLGSNSDESIDNLKVYNDIIELHTYSTQILKYLDNIQKLKGDCNDLVKDCKELRELSTALYDLKIQITSVINRENDISNNIDIVSNKLNEIDAIQYNFEKYKEIFDNVEEYKTLDDTKNAYIVKKAEILKNVDINKTKEDLDIYFNDLDELEKSLTLSSNEMEIKTIVQNSYNSFSDINKNINDIDKEMKTLIPMLDELLNEGHNIDISLYNFIIRNIQIKIGNDIKNIREQENDTNICFEYIQNNYNFIKSDISIFNKYDDHIKVDNYISNNIDVVNKHNSLLSEHVINATNIIENIMTSIVEINEDTEMNSLEETQDKLLELYENFKKEKNIINNNYKIVHFNKLKEIENSLETYNSISTNFNKINETQNIDILKNEFNNIKTKINDKVKELVHVDSTLTLESIQTFNNLYGDLMSNIQDVYKYEDINNVELKKVKLYIENITNLLGRINTFIKELDKYQDENNGIDKYIEINKENNSYIIKLKEKANNLKENFSKLLQNIKRNETELYNINNIKDDIMNTGKSVNNIKQKFSSNLPLKEKLFQMEEMLLNINNIMNETKRISNTDAYTNITLQDIENNKNKENNNMNIETIDKLIDHIKIHNEKIQAEILIIDDAKRKVKEITDNINKAFNEITENYNNENNGVIKSAKNIVDKATYLNNELDKFLLKLNELLSHNNNDIKDLGDEKLILKEEEERKERERLEKAKQEEERKERERIEKEKQEKERLEREKQEQLKKEALKKQEQERQEQQQKEEALKRQEQERLQKEEELKRQEQERLEREKQEQLQKEEELRKKEQEKQQQRNIQELEEQKKPEIINEALVKGDKILEGSDQRNMELSKPNVSMDNTNNSPISNSEITESDDIDNSENIHTSHMSDIESTQTSHRSNTHGQQISDIVEDQITHPSNIGGEKITHNDEISITGERNNISDVNDYSESSNIFENGDSTINTSTRNTSSTHDESHISPISNAYDHVVSDNKKSMDENIKDKLKIDESITTDEQIRLDDNSNIVRIDSTDQRDASSHGSSNRDDDEISHVGSDIHMDSVDIHDSIDTDENADHRHNVNSVDSLSSSDYTDTQKDFSSIIKDGGNKEGHAENESKEYESQTEQTHEEGIMNPNKYSISEVDGIKLNEEAKHKITEKLVDIYPSTYRTLDEPMETHGPNEKFHMFGSPYVTEEDYTEKHDYDKHEDFNNERYSNHNKMDDFVYNAGGVVCCVLFFASITFFSMDRSNKDECDFDMCEEVNNNDHLSNYADKEEIIEIVFDENEEKYF | null | null | adhesion of symbiont to host cell [GO:0044650]; cell-cell adhesion [GO:0098609]; symbiont entry into host [GO:0044409] | apical plasma membrane [GO:0016324]; cytoplasmic vesicle [GO:0031410]; extracellular space [GO:0005615]; host-symbiont bicellular tight junction [GO:0044647]; membrane [GO:0016020]; plasma membrane [GO:0005886]; rhoptry [GO:0020008]; rhoptry neck [GO:1990225]; tight junction [GO:0070160] | heparin binding [GO:0008201]; host cell surface receptor binding [GO:0046789] | null | null | null | PTM: Proteolytically processed into multiple fragments following schizont rupture (PubMed:12228308, PubMed:21698217, PubMed:27438226). In the mature schizont stage prior to merozoite release, full length RH2b is processed post-Golgi into C-terminal 297 kDa and N-terminal 85 kDa forms (PubMed:21698217, PubMed:27438226). Alternatively, full length RH2b can also be processed into C-terminal 250 kDa and N-terminal 130 kDa forms (PubMed:27438226). During merozoite invasion of host erythrocytes, further processing occurs generating a 160 kDa form (PubMed:27438226). At the same time, the C-terminal transmembrane region is cleaved, probably by a rhomboid protease, to shed all the different processed protein forms from the membrane leaving a transmembrane 7 kDa form on the merozoite surface (PubMed:21698217, PubMed:27438226). {ECO:0000269|PubMed:12228308, ECO:0000269|PubMed:21698217, ECO:0000269|PubMed:27438226}.; PTM: Phosphorylated at Ser-3233 by CK2alpha in schizonts. {ECO:0000269|PubMed:23544851}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27438226}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, rhoptry {ECO:0000269|PubMed:12228308, ECO:0000269|PubMed:27438226}. Cell junction, tight junction {ECO:0000269|PubMed:27438226}. Secreted {ECO:0000269|PubMed:27438226}. Note=Localizes to the rhoptry neck at the apical end of the merozoite (PubMed:12228308, PubMed:27438226). During merozoite invasion, mainly localizes to the tight junction formed between the parasite and the host erythrocyte membranes and then moves with the tight junction to the posterior end as the parasite enters the erythrocyte (PubMed:27438226). Also, the different processed forms are released from the membrane following proteolytic cleavage (PubMed:27438226). The remaining 7 kDa processed transmembrane fragment is incorporated into the newly formed ring stage (PubMed:21698217). {ECO:0000269|PubMed:12228308, ECO:0000269|PubMed:21698217, ECO:0000269|PubMed:27438226}.; SUBCELLULAR LOCATION: [Reticulocyte-binding protein homolog 2b 85 kDa form]: Secreted {ECO:0000269|PubMed:21698217}. Cell membrane {ECO:0000269|PubMed:21698217}; Peripheral membrane protein {ECO:0000269|PubMed:21698217}; Extracellular side {ECO:0000269|PubMed:21698217}. Note=In mature schizont, co-localizes to the apical end of the schizont and the merozoite with reticulocyte-binding protein homolog 2b 297 kDa form. During merozoite invasion, shed from the cell surface. {ECO:0000269|PubMed:21698217}.; SUBCELLULAR LOCATION: [Reticulocyte-binding protein homolog 2b 297 kDa form]: Secreted {ECO:0000269|PubMed:21698217}. Cell membrane {ECO:0000269|PubMed:21698217}; Single-pass type I membrane protein {ECO:0000305}. Note=In mature schizont, co-localizes to the apical end of the schizont and the merozoite with reticulocyte-binding protein homolog 2b 85 kDa form. During merozoite invasion, shed from the cell surface. {ECO:0000269|PubMed:21698217}. | null | null | null | null | null | FUNCTION: [Reticulocyte-binding protein homolog 2b]: During the asexual blood stage, binds to a chymotrypsin sensitive, neuraminidase and trypsin resistant receptor on the surface of the host erythrocyte and thus is involved in merozoite invasion (PubMed:12606570, PubMed:27438226). The various processed forms have different binding affinities for the erythrocyte receptor; full length form binds with higher affinity followed by the 250 kDa form and finally the 300 kDa form while the 160 kDa form does not bind erythrocytes (PubMed:27438226). After merozoite attachment and reorientation, RH2b binding to its erythrocyte receptor triggers an increase in intracellular Ca(2+) within the parasite resulting in the release of microneme proteins such as EBA175 which in turn leads to the formation of the tight junction between parasite and host cell (PubMed:27438226). {ECO:0000269|PubMed:12606570, ECO:0000269|PubMed:27438226}.; FUNCTION: [Reticulocyte-binding protein homolog 2b 85 kDa form]: During the asexual blood stage, binds to a trypsin-resistant and chymotrypsin and neuraminidase sensitive receptor on the surface of the host erythrocyte and thus is involved in merozoite invasion. {ECO:0000269|PubMed:21698217}. | Plasmodium falciparum (isolate 3D7) |
C0H9B6 | ZPLD1_SALSA | MEQICLIILLISKALSVGAQFNGYNCDANFHSRFPAERDISVYCGVQTITLKINFCPVLFSGYTDTDLALNGRHGDAHCRGFINNNTFPTVVLFSISLATLETCGNALVVSTAQGPNAYGNLSLVQIGNISGYIDTPDPPTIISYLPGLLYKFSCSYPLEYLVNNTQLASSAAAISVKDSNGTFVSTLSLLLYNDSSYVQQLSIPMAGLTLKTRVFAAVKATNLDRRWNVLMDYCYTTASGNPNDELRYDLFFSCDKDPQTTVFENGKSQMGRFAFEVFRFVKHKNQKMSTVFLHCVTKLCRADDCPMLMPICGSRKKRDVSERTESNSASGNAIITAGPIITRSDDTPMNNSQLAQLNSPVFRMNTVTSALISGIIILGVMSLCFFILSLTLLKGKRAPPTILSGARNPAFN | null | null | null | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasmic vesicle membrane [GO:0030659]; extracellular space [GO:0005615] | null | PF00100; | 2.60.40.4100; | null | PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted form found in the extracellular matrix of the cupula. {ECO:0000305|PubMed:25369234}.; PTM: N-glycosylated. {ECO:0000269|PubMed:25369234}. | SUBCELLULAR LOCATION: [Zona pellucida-like domain-containing protein 1]: Cytoplasmic vesicle membrane {ECO:0000305|PubMed:25369234}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Zona pellucida-like domain-containing protein 1, secreted form]: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:25369234}. | null | null | null | null | null | FUNCTION: Glycoprotein which is a component of the gelatinous extracellular matrix in the cupulae of the vestibular organ. {ECO:0000269|PubMed:25369234}. | Salmo salar (Atlantic salmon) |
C0HJB3 | MANA_CANEN | MKYNTGAGTVPEQLNVHLVPHSHDDVGWLKTVDQYYVGSENYIQEACVENVLDSVVMSLQRDPNRKFVFGEMAFFHRWWLEQTPETKELXXKLVKAGQLEFVNGGWCMHDEATTHYIDMIDHTTLGHRFLQEQFNKIPRAGWQIDPFGHSAVQGYLLGAELGFDSVHFARIDYQDREKRKGEKSLEVVWRGSKTFGSSAQIFANAFPGHYGPPNGFNFEVRNNFVPLQDDPRLFDTNVEERVQNFLDAALTQAKLTRTNHLMWTMGDDFQYQYAESWFKQMDKLLHHVNKDGRVNALYSTPSLYTEAKNAANQTWPLKIDDYFPYADGRNAYWTGFYTSRXXXXXXXXMLSGYYLATRHSGFFAGKKSTKYHAFDLADALGIAQHHDAVSGTAKQHTTNDYAKRLALGASKAEAVVSSSLACLTSKQSADQCSAPASAFSQCHLFNISYCPPTESSLPDDKSLVVVVYNPLGWSRNEIVRIPVNDANLVVKDSSGNKLEVQYVEMDDVTANLRSFYVKXXXXXXXXXXXXYWSLFKASVPPLGWSTYFISEATGKGTRNALTLSQKGETLNIGPGDLKMSFSSLTGQLKRMYNSKTGVDLPIQQNYLWYESSEGDFSDYQASGAYLFRPNGQPPPHTVSRSSVTRVTRGPLVDEVHQKFNSWISQVTRLYKDKDHAEIEFTIGPIPTDDGVGKEVITRMTSTMATNKEFYTDSNGRDFLKRVRDYREDWPLEVTQPVAGNYYPLNLGLYTKDEKSEFSVLVDRATGGASIKDGEVELMLHRRTLRDDGRGVGEPLDEQVCMNKEYTCEGLTVRGNYYLSIHKPAGGSRWRRTTGQEIYSPMLLAFTQENMENWKSSHSTKAYAMDPNYSLPPSVALITLEELDDGLVLLRLAHLYEPSEDAEYSTLTKVELKKLFATQKLEELREVSLSANQEKSEMKKMKWSVEGDNEQEPQAVRGGPVSNADFVVELGPMEIRTFLLQF | 3.2.1.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:1156387, ECO:0000269|PubMed:21924285, ECO:0000269|PubMed:4973951}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q29451}; | mannose metabolic process [GO:0006013] | protein storage vacuole [GO:0000326] | alpha-mannosidase activity [GO:0004559]; carbohydrate binding [GO:0030246]; metal ion binding [GO:0046872] | PF09261;PF07748;PF01074; | 2.60.40.1360;3.20.110.10;1.20.1270.50;2.60.40.1180; | Glycosyl hydrolase 38 family | PTM: Produced as a precursor which is then proteolytically cleaved into a 66kD heavy subunit and a 44kD light subunit. Cleavage probably occurs in protein bodies/protein storage vacuoles. {ECO:0000269|PubMed:24221485, ECO:0000269|PubMed:24295789, ECO:0000269|PubMed:9442045, ECO:0000303|PubMed:24221485}. | SUBCELLULAR LOCATION: Protein storage vacuole {ECO:0000269|PubMed:24221485}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.; EC=3.2.1.24; Evidence={ECO:0000269|PubMed:1156387, ECO:0000269|PubMed:12325362, ECO:0000269|PubMed:4973951, ECO:0000269|PubMed:5145}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.5 mM for p-nitrophenyl-alpha-D-mannoside {ECO:0000269|PubMed:12325362}; KM=31 mM for benzyl-alpha-D-mannoside {ECO:0000269|PubMed:12325362}; KM=0.12 M for methyl-alpha-D-mannoside {ECO:0000269|PubMed:12325362}; KM=10.52 uM for 4-methylumbellideryl-alpha-mannoside {ECO:0000269|PubMed:21924285}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-5 (PubMed:12325362, PubMed:21924285, PubMed:5145). Activity is stable between pH 4.0 and pH 7.0 in the presence of Zn(2+) (PubMed:4973951). Activity is stable between pH 6.0 and pH 8.5, decreases below pH 5.5 at 25 degrees Celsius (PubMed:12325362). Activity is lost at pH 3 and lower, rapidly diminishes at pH 7-10 but is higher and longest at pH 11-12 (PubMed:21924285). {ECO:0000269|PubMed:21924285, ECO:0000269|PubMed:4973951, ECO:0000269|PubMed:5145}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Retains 50% activity after 5 min at 70 degrees Celsius (PubMed:12325362). Retains full activity after 5 min at 70 degrees Celsius but is completely inactive after 5 min at 80 degrees Celsius (PubMed:5145). Retains 100%, 50% and <10% activity after 2 hours at 40, 55 and 70 degrees Celsius, respectively (PubMed:21924285). {ECO:0000269|PubMed:12325362, ECO:0000269|PubMed:21924285, ECO:0000269|PubMed:5145}; | FUNCTION: Liberates mannose from p-nitrophenyl-alpha-D-mannoside (PubMed:1156387, PubMed:12325362, PubMed:4973951). Liberates mannose from further alpha-D-mannosides including methyl-, benzyl-alpha-D-mannoside, 1-6-linked di-, tri- and tetrasaccharides of alpha-D-mannose and mannosyl-rhamnose (PubMed:12325362). Liberates mannose from various glycoproteins like ovalbumin and ovomucoid (PubMed:12325362, PubMed:5145). Does not hydrolyze beta-D-mannosides (PubMed:12325362). Has glycosyltransferase activity, forming disaccharides from mannose and lyxose but not from glucose, galactose, ribose, xylose or arabinose (PubMed:12325362). {ECO:0000269|PubMed:1156387, ECO:0000269|PubMed:12325362, ECO:0000269|PubMed:4973951, ECO:0000269|PubMed:5145}. | Canavalia ensiformis (Jack bean) (Dolichos ensiformis) |
C0HJD3 | 3NB_OXYFU | QAIGPPFGLCFQCNQKTSSDCFNAKRCPPFHRTCYTLYKPDGGEEWAVKGCAKGCPTAGPDERVKCCHTPRCNN | null | null | null | extracellular region [GO:0005576] | toxin activity [GO:0090729] | PF00087; | 2.10.60.10; | Snake three-finger toxin family, Ancestral subfamily, Boigatoxin sub-subfamily | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:23851011}.; PTM: Contains 5 disulfide bonds. {ECO:0000269|PubMed:23851011}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23851011}. | null | null | null | null | null | FUNCTION: Reptile-specific three-finger toxin that is lethal at low doses for lizards, but not for mice. Probably acts as a neurotoxin. {ECO:0000269|PubMed:23851011}. | Oxybelis fulgidus (Green vine snake) (Coluber fulgidus) |
C0HJD9 | K6TX1_ACTBE | RCKTCSKGRCRPKPNCG | null | null | null | extracellular region [GO:0005576]; nematocyst [GO:0042151] | potassium channel regulator activity [GO:0015459]; toxin activity [GO:0090729] | null | null | Sea anemone type 6 potassium channel toxin family | null | SUBCELLULAR LOCATION: Secreted. Nematocyst {ECO:0000269|PubMed:30275388}. | null | null | null | null | null | FUNCTION: Potassium channel inhibitor that is the most potent on Kv1.1/KCNA1 (IC(50)=671.95 nM), Kv1.2/KCNA2 (IC(50)=167.36 nM), and Kv1.6/KCNA6 (IC(50)=115.68 nM), and less potent on Kv1.3/KCNA3 (20% inhibition at 3 uM) and on shaker IR (15% inhibition at 3 uM). It inhibits potassium currents, not only by blocking the potassium current of Kv1.2/KCNA2, but by altering the energetics of activation of Kv1.1/KCNA1 and Kv1.6/KCNA6. {ECO:0000269|PubMed:30275388}. | Actinia bermudensis (Maroon anemone) |
C0HJE7 | OXLA_CRODU | MNVFFMFSLLFLAALGSCAHDRNPLEECFRETDYEEFLEIARNGLTVTSNPKHVVIVGAGMAGLSAAYVLAGAGHQVTVLEASERVGGRVRTYRKKDWYANLGPMRLPTKHRIVREYIRKFGLQLNEFFQENENAWYFIKNIRKRVREVKNNPGILEYPVKPSEEGKSAAQLYVESLRKVVKELKRTNCKYILDKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVGGMDQLPTSMYEAIKEKVQVHFNARVIEIQQNDRETKVTYQTSANEMSSVTADYVIVCTTSRAARRIKFEPPLPPKKAHALRSVHYRSGTKIFLTCKRKFWEDDGIRGGKSTTDLPSRFIYYPNHNFTSGVGVIIAYGIGDDANFFQALDFKDCADIVINDLSLIHQLPKEDIQTFCRPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPFKRIYFAGEYTAQFHGWIDSTIKSGLTAARDVNRASENPSGIHLSNDNEF | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P0C2D2}; | amino acid catabolic process [GO:0009063]; apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | L-phenylalaine oxidase activity [GO:0106329]; toxin activity [GO:0090729] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family, FIG1 subfamily | PTM: N-glycosylated (PubMed:26273287, PubMed:31078582). N-glycan probably consists of the disaccharide N-acetylglucosamine-fucose (HexNAc-Fuc) (PubMed:31078582). {ECO:0000269|PubMed:26273287, ECO:0000269|PubMed:31078582}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26273287}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:26273287, ECO:0000269|PubMed:31078582}; CATALYTIC ACTIVITY: Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:31078582}; CATALYTIC ACTIVITY: Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938, ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:31078582}; CATALYTIC ACTIVITY: Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+); Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938, ChEBI:CHEBI:57912; Evidence={ECO:0000269|PubMed:31078582}; CATALYTIC ACTIVITY: Reaction=H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:61236, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723, ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; Evidence={ECO:0000269|PubMed:31078582}; CATALYTIC ACTIVITY: Reaction=H2O + L-isoleucine + O2 = (S)-3-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:61232, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; Evidence={ECO:0000269|PubMed:31078582}; CATALYTIC ACTIVITY: Reaction=H2O + L-arginine + O2 = 5-guanidino-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:51404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32682, ChEBI:CHEBI:58489; Evidence={ECO:0000269|PubMed:31078582}; CATALYTIC ACTIVITY: Reaction=H2O + L-histidine + O2 = 3-(imidazol-5-yl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61228, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57595, ChEBI:CHEBI:58133; Evidence={ECO:0000269|PubMed:31078582}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.14 mM for L-Phe {ECO:0000269|PubMed:31078582}; KM=0.48 mM for L-Trp {ECO:0000269|PubMed:31078582}; KM=0.58 mM for L-Leu {ECO:0000269|PubMed:31078582}; KM=0.97 mM for L-Met {ECO:0000269|PubMed:31078582}; KM=3.9 mM for L-Ile {ECO:0000269|PubMed:31078582}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. Activity is reduced to about 70% and 60% after incubation at pH 5.0 and pH 9.0, respectively, for 1 hour. {ECO:0000269|PubMed:26273287}; | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:26273287, PubMed:31078582). Is highly active on L-Met, L-Leu, L-Trp, and L-Phe, moderately active on L-Ile, L-His, and L-Arg, and weakly or not active on L-Gln, L-Val, L-Asn, L-Ala, L-Lys, L-Ser, L-Thr, L-Pro, L-Asp, L-Gly, L-Tyr, L-Cys and L-Glu (PubMed:31078582). This enzyme exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation (PubMed:26273287). Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation (PubMed:26273287). These different effects are probably due to different experimental conditions (PubMed:26273287). In vitro, the enzyme exhibits cytotoxicity against fibroblast cell line and kills Leishmania amazonensis promastigotes, intensified by substrate addition (PubMed:31078582). {ECO:0000269|PubMed:26273287, ECO:0000269|PubMed:31078582}. | Crotalus durissus terrificus (South American rattlesnake) |
C0HJG9 | ANXA2_MESAU | STVHEILCKLSLEGDHSTPPSAYGSVKDALNIETAVKGVDEVTIVNILTNRQDIAFAYQRKELPSALKTPAQYDASELKGLGTDEDSLIEIICSRTNQELQEINRTDLEKDIISDTSGDFRKLMVALAKRAEDGSVIDYELIDQDARDLYDAGVKRWISIMTERSVCHLQKDKVLIRIMVSRSEVDMLSLYYYIQQDTK | null | null | null | basement membrane [GO:0005604]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; vesicle [GO:0031982] | cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; cytoskeletal protein binding [GO:0008092]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786]; phospholipase A2 inhibitor activity [GO:0019834]; protease binding [GO:0002020]; virion binding [GO:0046790] | PF00191; | 1.10.220.10; | Annexin family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:P07355}. | null | null | null | null | null | FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity (By similarity). {ECO:0000250|UniProtKB:P07355}. | Mesocricetus auratus (Golden hamster) |
C0HJL8 | PA2B_BOTNI | NLLQFNRMIKLETKKNAVPFYAFYGCYCGWGGQGQPKDATDRCCFEHDCCYGKLTKCNTKSDLYSYSSKYGFLLCGKGTWCEEQICECDRIAATCLRRSLDTYKLKYMFYLDSYCKGPSEKC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P24027}; Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P24027}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20590130, ECO:0000269|PubMed:25434534}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035}; | null | null | null | null | FUNCTION: Heterodimer A-B: Nigroviriditoxin possesses phospholipase A2 (PLA2) activity. It consists of a non-covalent association of a basic PLA2 subunit B with a non-enzymatic subunit A. {ECO:0000269|PubMed:25434534}.; FUNCTION: Subunit B: Snake venom phospholipase A2 (PLA2) that induces myonecrosis in mice. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:25434534}. | Bothriechis nigroviridis (Black-speckled palm pit viper) |
C0HJM9 | SCX2_TITFA | MKRFLLFISILMMIGTIVVGKEGYAMDHEGCKFSCFIRPSGFCDGYCKTHLKASSGYCAWPACYCYGVPSNIKVWDYATNKCGK | null | null | defense response [GO:0006952]; envenomation resulting in negative regulation of voltage-gated sodium channel activity in another organism [GO:0044493] | extracellular region [GO:0005576] | sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729] | PF00537; | 3.30.30.10; | Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Beta subfamily | PTM: Contains 4 disulfide bonds. {ECO:0000269|PubMed:26083731}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26083731}. | null | null | null | null | null | FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is active against hNav1.3/SCN3A. {ECO:0000269|PubMed:26083731}. | Tityus fasciolatus (Central Brazilian scorpion) |
C0HJQ2 | KA192_BUTOC | AACYSSDCRVKCRAMGFSSGKCIDSKCKCYK | null | null | negative regulation of voltage-gated potassium channel activity in another organism [GO:0044361] | extracellular region [GO:0005576] | potassium channel inhibitor activity [GO:0019870]; toxin activity [GO:0090729] | PF00451; | 3.30.30.10; | Short scorpion toxin superfamily, Potassium channel inhibitor family, Alpha-KTx 19 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26398235}. | null | null | null | null | null | FUNCTION: Blocks voltage-gated potassium channels rKv1.1/KCNA1, rKv1.2/KCNA2, hKv1.3/KCNA3, rKv1.6/KCNA6 (IC(50)=75.9 nM) and, to a lesser extent, Shaker IR (with the inactivation domain removed). {ECO:0000269|PubMed:26398235}. | Buthus occitanus tunetanus (Common European scorpion) (Buthus tunetanus) |
C0HJQ3 | H2A_ACIGU | MSGRGKTGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAQRVGAGAPVYLILELAGNAARDNKKTRIIPRHLQL | null | null | defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; immune system process [GO:0002376]; killing of cells of another organism [GO:0031640] | nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | null | 1.10.20.10; | Histone H2A family | PTM: Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 directly represses transcription. {ECO:0000250|UniProtKB:P0C0S8}. | SUBCELLULAR LOCATION: [Histone H2A]: Nucleus {ECO:0000250|UniProtKB:P02264}. Chromosome {ECO:0000250|UniProtKB:P02264}. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000305}.; FUNCTION: Acipensins are antimicrobial peptides. Acipensins 1 and 2 have antibacterial activity against Gram-positive bacteria L.monocytogenes EGD (MIC are 1.1 uM and 1.0 uM, respectively) and S.aureus ATCC 33591 (MIC are 0.9 uM and 0.6 uM, respectively), against Gram-negative bacterium E.coli ML-35p (MIC are 0.7 uM and 0.3 uM, respectively) and antifungal activity against C.albicans 820 (MIC are 1.0 uM and 0.9 uM, respectively). Acipensin 6 has antibacterial activity against Gram-negative bacterium E.coli ML-35p (MIC=2.5 uM). Antimicrobial activity is reduced by high ionic strength. Acipensins 1, 2 and 6 have no hemolytic (up to 40 uM) or cytotoxic (up to 20 uM) effects on human cells in vitro. {ECO:0000269|PubMed:25558400}. | Acipenser gueldenstaedtii (Russian sturgeon) (Danube sturgeon) |
C0HJQ9 | MYG_HYSCR | MGLSDGEWQLVLNVWGKVEGDIGGHGQEVLIRLFKGHPETLEKFDKFKHLKAEDEMRASEDLKKHGTTVLTALGGILKKKGQHAAELAPLAQSHATKHKIPVKYLEFISEAIIQVLQSKHPADFGADTQGAMSKALELFRNDIAAKYKELGFQG | 1.11.1.-; 1.7.-.- | null | removal of superoxide radicals [GO:0019430] | extracellular exosome [GO:0070062]; sarcoplasm [GO:0016528] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitrite reductase activity [GO:0098809]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 6.10.140.2100;6.10.140.2110; | Globin family | null | SUBCELLULAR LOCATION: Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:P02144}. | CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P02144}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000250|UniProtKB:P02144}; CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; Evidence={ECO:0000250|UniProtKB:P02144}; | null | null | null | null | FUNCTION: Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand. Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide. Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity. {ECO:0000250|UniProtKB:P02144}. | Hystrix cristata (North African crested porcupine) |
C0HJR0 | MYG_RANTA | MGLSDGEWQLVLNAWGKVEADVAGHGQEVLIRLFTGHPETLEKFDKFKHLKTEAEMKASEDLKKHGNTVLTALGGILKKKGHHEAEVKHLAESHANKHKIPVKYLEFISDAIIHVLHAKHPSDFGADAQGAMSKALELFRNDMAAQYKVLGFQG | 1.11.1.-; 1.7.-.- | null | removal of superoxide radicals [GO:0019430] | extracellular exosome [GO:0070062]; sarcoplasm [GO:0016528] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitrite reductase activity [GO:0098809]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 6.10.140.2100;6.10.140.2110; | Globin family | null | SUBCELLULAR LOCATION: Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:P02144}. | CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P02144}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000250|UniProtKB:P02144}; CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; Evidence={ECO:0000250|UniProtKB:P02144}; | null | null | null | null | FUNCTION: Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand. Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide. Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity. {ECO:0000250|UniProtKB:P02144}. | Rangifer tarandus (Reindeer) (Cervus tarandus) |
C0HJU3 | PA2A1_BOTPA | NLVQFKTLIMKIAGRSVVYKYFYYGCYCGWGGIGQPRDATDRCCFVHD | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:17451767}; Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P14418}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17451767}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:17451767}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-8.5. Activity decreases rapidly at basic or acidic pH and is virtually absent at pH 12 and pH 3.5, respectively. {ECO:0000269|PubMed:17451767}; | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that shows myotoxicity and induces paw edema in mice (PubMed:17451767). Exhibits indirect hemolytic activity (PubMed:17451767). Inhibits platelet aggregation induced by ADP and collagen (PubMed:17451767). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:17451767). {ECO:0000269|PubMed:17451767}. | Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis) |
C0HJY1 | CONV_CANCT | ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVGKRLSAVVSYPNGDSATVSYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHETNALHFVFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFDATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN | null | null | vasodilation [GO:0042311] | null | calcium ion binding [GO:0005509]; glucose binding [GO:0005536]; manganese ion binding [GO:0030145]; mannose binding [GO:0005537] | PF00139; | 2.60.120.200; | Leguminous lectin family | PTM: Concanavalin A-like lectins of the Diocleinae subtribe undergo proteolytic processing referred to as circular permutation. The propeptide is split into an N-terminal and a C-terminal part, the gamma and beta chain, respectively. These are then religated in beta-gamma order to form the mature alpha chain. The beta and gamma chains can often be detected in cell extracts (By similarity). Residues 1-118 of the mature chain, as displayed here, probably constitute the beta chain in the propeptide, residues 119-237 the gamma chain (Probable). {ECO:0000250|UniProtKB:C0HK27, ECO:0000305|PubMed:27737777}. | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-9 with activity decreasing quickly at higher or lower pH. {ECO:0000269|PubMed:24519628}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Hemagglutinating activity stable up to incubation at 80 degrees Celsius for 1 hour but diminishes with higher temperatures and is absent at 100 degrees Celsius. {ECO:0000269|PubMed:24519628}; | FUNCTION: D-mannose/D-glucose-binding lectin which binds alpha-methyl-D-mannoside, D-mannose and D-glucose in that order (PubMed:24519628, PubMed:27737777). Also binds to serum fetuin and ovalbumin (PubMed:24519628). Has hemagglutinating activity towards rabbit erythrocytes (PubMed:24519628). Is not toxic towards larvae of the brine shrimp Artemia (PubMed:24519628). Induces relaxation in rat endothelized aorta (PubMed:24519628). Shows a transient edematogenic effect in rat (PubMed:27737777). {ECO:0000269|PubMed:24519628, ECO:0000269|PubMed:27737777}. | Canavalia cathartica (Jackbean) (Canavalia virosa) |
C0HJY4 | PON1A_ANOEM | WCASGCRKKRHGGCSC | null | null | null | extracellular region [GO:0005576] | calcium channel regulator activity [GO:0005246]; toxin activity [GO:0090729] | null | null | Poneritoxin-Ae1 family | PTM: C-terminal amidation is necessary for channel blocking activity. {ECO:0000269|PubMed:27474999}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27474999}. | null | null | null | null | null | FUNCTION: Weakly inhibits human L-type voltage-gated calcium channel Cav1 (CACNA1S, CACNA1C, CACNA1D, CACNA1F) (IC(50)=4.6 uM). In vivo, it induces reversible paralysis in blowfly L.cuprina. {ECO:0000269|PubMed:27474999}. | Anochetus emarginatus (Ant) (Stenomyrmex emarginatus) |
C0HK05 | PA2BC_CROOL | HLLQFNKMIKFETRKNAIPFYAFYGCYCGWGGRGRPKDATDRCCFVH | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:26996495}; Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P14421}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26996495}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:26996495}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.09 mM for 4-nitro-3-octanoyl benzioc acid (NOBA) {ECO:0000269|PubMed:26996495}; Vmax=15.97 nmol/min/mg enzyme with NOBA as substrate {ECO:0000269|PubMed:26996495}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:26996495}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:26996495}; | FUNCTION: Snake venom phospholipase A2 (PLA2) that shows edema-inducing activity and local and systemic myotoxicity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:26996495}. | Crotalus oreganus lutosus (Great basin rattlesnake) (Crotalus viridis lutosus) |
C0HK25 | ADEL_APLDA | DPDKCKTIRVESWSYKYAEKVVEDASYVLNMTVVDRQSAAACTLGESFGYQKATLWVDHGCRADFKVCYLPVMPTECQTLRVESWNYKYAEKVVEGAALFINMTVEDRQSEASCDLDKSFGFYNQNSTVWVNHGCRADFNICYLKGAVTTSTINVSSWNYQYATKVLPAASCIYSMRVVNQQSAAPCTLGTTYGFVANTMWVDDGCRADFKPSYYSP | null | null | positive regulation of erythrocyte aggregation [GO:0034120] | null | galactose binding [GO:0005534]; galactoside binding [GO:0016936]; galacturonate binding [GO:0048032]; lactose binding [GO:0030395]; melibiose binding [GO:1903777] | PF11218; | null | null | PTM: Contains disulfide bonds. {ECO:0000269|PubMed:28150103}. | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-7. {ECO:0000269|PubMed:28150103}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Activity is stable up to 60 degrees Celsius, then decreases and is lost at 80 degrees Celsius. {ECO:0000269|PubMed:28150103}; | FUNCTION: Binds in decreasing order of affinity: galacturonic acid, D-galactosamine, methyl-alpha-D-galactopyranoside and further galactose-containing carbohydrates. Has hemagglutinating activity against human and rabbit erythrocytes. {ECO:0000269|PubMed:28150103}. | Aplysia dactylomela (Spotted sea hare) |
C0HK27 | LECA_DIOLA | MGISKKSQLVPLLAFITMFLMVVSRVSSSIADANSLHFSFSQFSQNPKDLILQGDATTDSDGNLQLTRVSSDGSPQGSSVGRALFYAPVHIWEKSAVVASFDATFTFLIKSPDRDPADGITFFIANTDTSIPSGSGGRLLGLFPDANIIKNSTNLDFNAAYNADTIVAVELDSYPNTDIGDPSYPHIGIDIKSIRSKSTARWNMQTGKVGTAHISYNSVAKRLSAVVSYSGTSSTTVSYDVDLNNVLPEWVRVGLSATTGLYKETNTILSWSFTSKLKTNQLQDLRIASVV | null | null | null | null | mannose binding [GO:0005537]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | PF00139; | 2.60.120.200; | Leguminous lectin family | PTM: The mature chain consists of residues 163-280 followed by residues 29-147. Concanavalin A-like lectins of the Diocleinae subtribe undergo proteolytic processing referred to as circular permutation. The propeptide is split into an N-terminal and a C-terminal part, the gamma and beta chain, respectively. These are then religated in beta-gamma order to form the mature alpha chain. The beta and gamma chains can often be detected in cell extracts. {ECO:0000269|PubMed:28196677}. | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH for hemagglutinating activity is 8. Activity drops with more acidic and basic pH and is lost at pH 5 and pH 8, respectively. {ECO:0000269|PubMed:24008245}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Hemagglutinating activity is stable after incubation at 70 degrees Celsius for 1 hour but lost at higher temperatures. {ECO:0000269|PubMed:24008245}; | FUNCTION: D-mannose-binding lectin that also binds alpha-methyl-D-mannoside with even higher affinity (PubMed:24008245). Has hemagglutinating activity against rabbit erythrocytes (PubMed:24008245). Shows toxicity against the brine shrimp A.nauplii (PubMed:24008245). Induces reversible paw edema and hypernociceptivity in rats (PubMed:28196677). {ECO:0000269|PubMed:24008245, ECO:0000269|PubMed:28196677}. | Dioclea lasiophylla |
C0HK44 | LL3_LASLA | VNWKKILGKIIKVVK | null | null | defense response to bacterium [GO:0042742] | extracellular region [GO:0005576] | DNA binding [GO:0003677] | null | null | Lasioglossin-like family | PTM: The C-terminal amidation is required for full activity. {ECO:0000269|PubMed:19591185}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19591185}. | null | null | null | null | null | FUNCTION: Antimicrobial peptide which assumes an amphiphilic alpha-helix conformation upon contact with membranes (PubMed:19591185). Insertion into membranes involves Trp-3 (By similarity). Penetrates into cells once membrane has been permeated (PubMed:22100226). Active against Gram-negative bacteria E.coli (MIC=1.4 uM), P.aeruginosa (MIC=18.7 uM) and Gram-positive bacteria S.aureus (MIC=3.9 uM) and B.subtilis (MIC=0.7 uM) (PubMed:19591185). Has cytotoxic but no hemolytic activity (PubMed:19591185, PubMed:22100226). Binds DNA in vitro (By similarity). In the context of inflammation and cancer tests, a 3-residues C-terminally truncated lasioglossin-3 is weakly cytotoxic to normal cells, induces calcium signaling but does not impact cAMP production (PubMed:36548715). In addition, this truncated peptide prevents LPS-induced nitric oxid (NO) synthesis but does not affect the IP3 signaling and pro-inflammatory activation of endothelial cells (PubMed:36548715). This truncated peptide does not show significant antiproliferative activity on the breast cancer cell line MDA-MB-231 (PubMed:36548715). {ECO:0000250|UniProtKB:C0HK43, ECO:0000269|PubMed:19591185, ECO:0000269|PubMed:22100226, ECO:0000269|PubMed:36548715}. | Lasioglossum laticeps (Bee) |
C0HK49 | DEF_NICSU | KDCKRESNTFPGICITKPPCRKACIREKFTDGHCSKILRRCLCTKPC | null | null | defense response [GO:0006952]; killing of cells of another organism [GO:0031640] | vacuole [GO:0005773] | phosphatidic acid binding [GO:0070300] | PF00304; | 3.30.30.10; | DEFL family | null | SUBCELLULAR LOCATION: Vacuole {ECO:0000250|UniProtKB:Q8GTM0}. | null | null | null | null | null | FUNCTION: Plant defense peptide (Probable). Disrupts membranes containing phosphatidic acid (PA) via a PA-dependent oligomerization process. {ECO:0000269|PubMed:27647905, ECO:0000303|PubMed:27647905}. | Nicotiana suaveolens (Australian tobacco) |
C0HK69 | SCXD_CENLI | KEGYLVDYHTGCKYTCAKLGDNDYCVRECRLRYYQSAHGYCYAFACWCTHLYEQAVVWPLPNKRCKGK | null | null | defense response [GO:0006952] | extracellular region [GO:0005576] | sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729] | PF00537; | 3.30.30.10; | Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Beta subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27871874}. | null | null | null | null | null | FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing (By similarity). Inhibits sodium channels Nav1.4/SCN4A, Nav1.5/SCN5A and Nav1.6/SCN8A (PubMed:27871874). Also has a weak inhibitory effect on Nav1.2/SCN2A (PubMed:27871874). Is lethal to mice (PubMed:27871874). {ECO:0000250|UniProtKB:P60266, ECO:0000269|PubMed:27871874}. | Centruroides limpidus (Mexican scorpion) |
C0HK98 | SC1A_DROME | MVSKVALLLAVLVCSQYMAQGVYVVSKAEWGGRGAKWTVGLGNYLSYAIIHHTAGSYCETRAQCNAVLQSVQNYHMDSLGWPDIGYNFLIGGDGNVYEGRGWNNMGAHAAEWNPYSIGISFLGNYNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQVSATECPGTHIWNEIRGWSHWSG | 3.5.1.28 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8INK6}; | defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087]; negative regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria [GO:0002814]; negative regulation of peptidoglycan recognition protein signaling pathway [GO:0061060]; peptidoglycan catabolic process [GO:0009253]; positive regulation of phagocytosis [GO:0050766]; Toll receptor ligand protein activation cascade [GO:0160032] | extracellular region [GO:0005576] | N-acetylmuramoyl-L-alanine amidase activity [GO:0008745]; peptidoglycan binding [GO:0042834]; zinc ion binding [GO:0008270] | PF01510; | 3.40.80.10; | N-acetylmuramoyl-L-alanine amidase 2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28; Evidence={ECO:0000250|UniProtKB:C0HK99}; | null | null | null | null | FUNCTION: N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity. {ECO:0000250|UniProtKB:C0HK99}. | Drosophila melanogaster (Fruit fly) |
C0HK99 | SC1B_DROME | MVSKVALLLAVLVCSQYMAQGVYVVSKAEWGGRGAKWTVGLGNYLSYAIIHHTAGSYCETRAQCNAVLQSVQNYHMDSLGWPDIGYNFLIGGDGNVYEGRGWNNMGAHAAEWNPYSIGISFLGNYNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQVSATECPGTHIWNEIRGWSHWSG | 3.5.1.28 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:12496260}; | innate immune response [GO:0045087]; negative regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria [GO:0002814]; negative regulation of peptidoglycan recognition protein signaling pathway [GO:0061060]; peptidoglycan catabolic process [GO:0009253]; Toll receptor ligand protein activation cascade [GO:0160032] | extracellular region [GO:0005576] | N-acetylmuramoyl-L-alanine amidase activity [GO:0008745]; peptidoglycan binding [GO:0042834]; zinc ion binding [GO:0008270] | PF01510; | 3.40.80.10; | N-acetylmuramoyl-L-alanine amidase 2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28; Evidence={ECO:0000269|PubMed:12496260}; | null | null | null | null | FUNCTION: N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN) (PubMed:11106397, PubMed:12496260). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments (PubMed:12496260). Has no direct bacteriolytic activity (PubMed:12496260). {ECO:0000269|PubMed:11106397, ECO:0000269|PubMed:12496260}. | Drosophila melanogaster (Fruit fly) |
C0HKB8 | PA2A1_MICDM | NLIDFKNMIKCTTKRSVLDFADYGCYCGSGGSGTPVDDLDRCCKVHDDCYGEAEKVHGCWPKWTLYSYDCSNGQLTCKDNNTKCKDFVCNCDRTAAICFAKAPYDDNNFMINNPRCQ | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P15445}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P15445}; | arachidonic acid secretion [GO:0050482]; phosphatidylcholine catabolic process [GO:0034638] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; phospholipid binding [GO:0005543] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28315380}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000269|PubMed:28315380}; | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that shows strong myotoxicity and induces edema in mice. Shows no cytotoxicity in vitro. Has a strong anticoagulant effect in vitro. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:28315380}. | Micrurus dumerilii (Coral snake) |
C0HKB9 | PA2B1_MICMP | NLIHFSSMIKCTIPGSKPVPDYSDYGCYCGKGGSGTPVDALDRCCQVHDKCYGDAESIYGCTPFLTYYSYECSERQDLCRGNGTKCKAFVCNCDRLAALCFAKAPYNKKNYNINLNRCK | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P15445}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P15445}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21963438, ECO:0000269|PubMed:28315380}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000269|PubMed:21963438, ECO:0000269|PubMed:28315380}; | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that shows weak myotoxicity and induces edema in mice (PubMed:28315380). Shows no cytotoxicity in vitro (PubMed:28315380). Has an anticoagulant effect in vitro (PubMed:21963438, PubMed:28315380). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:21963438, PubMed:28315380). {ECO:0000269|PubMed:21963438, ECO:0000269|PubMed:28315380}. | Micrurus mipartitus (Red-tailed coral snake) |
C0HKC3 | PA2B9_AGKPL | MRTLWIMAVLLLGVEGNLFQFEKLIKKMTGKSGMLWYSAYGCYCGWGGQGRPKDATDRCCFVHDCCYGKVTGCNPKMDIYTYSVENGNIVCGGTNPCKKQICECDRAAAICFRDNLKTYDSKTYWKYPKKNCKEESEPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P14418}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P14418}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | PTM: Acylation causes dimerization. {ECO:0000250|UniProtKB:P51972}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28633930}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000269|PubMed:28633930}; | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that does not show antibacterial activity (PubMed:29928892). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:28633930). {ECO:0000269|PubMed:28633930, ECO:0000269|PubMed:29928892}. | Agkistrodon piscivorus leucostoma (Western cottonmouth) (Acontias leucostoma) |
C0HKC4 | PA2B1_AGKCN | NLFQFEKLIKKMTGKSGMLWYSAYGCYCGWGGQGRPKDATDRCCFVHDCCYGKVTGCNPKMDIYTYSVDNGNIVCGGTNPCKKQICECDRAAAICFRDNLKTYDSKTYWKYPKKNCKEESEPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P14418}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P14418}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28633930}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000269|PubMed:28633930}; | null | null | null | null | FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:28633930}. | Agkistrodon conanti (Florida cottonmouth) (Agkistrodon piscivorus conanti) |
C0HKE1 | H2A1B_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | chromatin organization [GO:0006325]; heterochromatin organization [GO:0070828]; protein localization to CENP-A containing chromatin [GO:0061644] | CENP-A containing nucleosome [GO:0043505]; nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}.; PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription. {ECO:0000250|UniProtKB:P0C0S5}. | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Mus musculus (Mouse) |
C0HKE2 | H2A1C_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}.; PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription. {ECO:0000250|UniProtKB:P0C0S5}. | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Mus musculus (Mouse) |
C0HKE3 | H2A1D_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}.; PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription. {ECO:0000250|UniProtKB:P0C0S5}. | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Mus musculus (Mouse) |
C0HKE4 | H2A1E_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}.; PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription. {ECO:0000250|UniProtKB:P0C0S5}. | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Mus musculus (Mouse) |
C0HKE5 | H2A1G_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}.; PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription. {ECO:0000250|UniProtKB:P0C0S5}. | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Mus musculus (Mouse) |
C0HKE6 | H2A1I_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}.; PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription. {ECO:0000250|UniProtKB:P0C0S5}. | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Mus musculus (Mouse) |
C0HKE7 | H2A1N_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}.; PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription. {ECO:0000250|UniProtKB:P0C0S5}. | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Mus musculus (Mouse) |
C0HKE8 | H2A1O_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}.; PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription. {ECO:0000250|UniProtKB:P0C0S5}. | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Mus musculus (Mouse) |
C0HKE9 | H2A1P_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}.; PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription. {ECO:0000250|UniProtKB:P0C0S5}. | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Mus musculus (Mouse) |
C0HKG7 | TX1A_CHEPU | MKFSLFFSVFFLAVLHACLSESEIDLEDEEHFMSSDSFLSEIQDESRGKTCIERNKECTNDRHGCCRGKIFKDKCTCVKNGKTEKCVCTQKKWAKIIESYIGDIPALPKPVDDKCVPKHADCSKRKDDCCKGGIFKYQCKCYDMYDDDGEKTDLCGCVSPVEHQAIEGALRIAKKLIGDRWGR | null | null | killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | PF10530; | null | Neurotoxin 19 (CSTX) family, Double-CSTX subfamily | PTM: Cleavage of the propeptide depends on the processing quadruplet motif (XXXR, with at least one of X being E). {ECO:0000303|PubMed:20657014, ECO:0000303|PubMed:24717175}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20657014}. Target cell membrane {ECO:0000269|PubMed:20657014}. Note=Probably forms a transmembrane alpha-helix in the target cell membrane. | null | null | null | null | null | FUNCTION: Spider venom toxin that exhibits cytolytic activity by forming an alpha-helix across the membrane (PubMed:20657014). Lethal to insect larvae (PubMed:20657014, PubMed:24717175). Causes instant paralysis and death in the larvae of the flesh fly (S.carnaria) at doses of 20 ug/g, at doses of less than 10 ug/g causes reversible paralysis (PubMed:20657014). Has cytolytic activity against insect Sf9 cells (PubMed:20657014). Causes stable and irreversible depolarization of fly muscle fibers, leading to contracture at higher toxin concentrations (PubMed:20657014). Destabilizes membranes (PubMed:20657014). {ECO:0000269|PubMed:20657014, ECO:0000269|PubMed:24717175}. | Cheiracanthium punctorium (Yellow sac spider) (Aranea punctoria) |
C0HKG8 | TX1B_CHEPU | MKFSLFFSVFFLAVLHACLSESEIDLEDEEHFMSSDSFLSEIQDESRGKTCIERNKECTNDRHGCCRGKIFKDKCTCVKNGKTEKCVCTQKKWAKIIESYIGDIPALPKPVDDKCVPKHADCSKRKDECCKGGIFKYQCKCYDMYDDDGEKTDLCGCVSPVEHQAIEGALRIAKKLIGDRWGR | null | null | killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | PF10530; | null | Neurotoxin 19 (CSTX) family, Double-CSTX subfamily | PTM: Cleavage of the propeptide depends on the processing quadruplet motif (XXXR, with at least one of X being E). {ECO:0000303|PubMed:20657014, ECO:0000303|PubMed:24717175}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20657014}. Target cell membrane {ECO:0000269|PubMed:20657014}. Note=Probably forms a transmembrane alpha-helix in the target cell membrane. | null | null | null | null | null | FUNCTION: Spider venom toxin that exhibits cytolytic activity by forming an alpha-helix across the membrane (PubMed:20657014). Lethal to insect larvae (PubMed:20657014, PubMed:24717175). Causes instant paralysis and death in the larvae of the flesh fly (S.carnaria) at doses of 20 ug/g, at doses of less than 10 ug/g causes reversible paralysis (PubMed:20657014). Has cytolytic activity against insect Sf9 cells (PubMed:20657014). Causes stable and irreversible depolarization of fly muscle fibers, leading to contracture at higher toxin concentrations (PubMed:20657014). Destabilizes membranes (PubMed:20657014). {ECO:0000269|PubMed:20657014, ECO:0000269|PubMed:24717175}. | Cheiracanthium punctorium (Yellow sac spider) (Aranea punctoria) |
C0HKG9 | TX1C_CHEPU | MKFSLFFSVFFLAVLHACLSESEIDLEDEEHFMSSDSFLSEIQDESRGKTCIERNKECTNDRHGCCRGKIFKDKCTCVKSGKTEKCVCTQKKWAKIIESYIGDIPALPKPVDDKCVPKHADCSKRKDDCCKGGIFKYQCKCYDMYDDDGEKTDLCGCVSPVEHQAIEGALRIAKKLIGDRWGR | null | null | killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | PF10530; | null | Neurotoxin 19 (CSTX) family, Double-CSTX subfamily | PTM: Cleavage of the propeptide depends on the processing quadruplet motif (XXXR, with at least one of X being E). {ECO:0000303|PubMed:20657014, ECO:0000303|PubMed:24717175}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20657014}. Target cell membrane {ECO:0000269|PubMed:20657014}. Note=Probably forms a transmembrane alpha-helix in the target cell membrane. | null | null | null | null | null | FUNCTION: Spider venom toxin that exhibits cytolytic activity by forming an alpha-helix across the membrane (PubMed:20657014). Lethal to insect larvae (PubMed:20657014, PubMed:24717175). Causes instant paralysis and death in the larvae of the flesh fly (S.carnaria) at doses of 20 ug/g, at doses of less than 10 ug/g causes reversible paralysis (PubMed:20657014). Has cytolytic activity against insect Sf9 cells (PubMed:20657014). Causes stable and irreversible depolarization of fly muscle fibers, leading to contracture at higher toxin concentrations (PubMed:20657014). Destabilizes membranes (PubMed:20657014). {ECO:0000269|PubMed:20657014, ECO:0000269|PubMed:24717175}. | Cheiracanthium punctorium (Yellow sac spider) (Aranea punctoria) |
C0HKM3 | HYAL_CONPU | MRVVVVVTGLVVVVVATALSLPDHDVKSASSPLSSSSVYQGSSGDDCDEGLPPPDRPFYVVWNHPDTCKRNRIPLHLDHYGFIFNKNRLFLGEEIQTLYNTGLWPNISETGEFFNGGLPQLFTHHDYSETVEILGRYRTENFTGLGILDFEEWRAIYDTNFGIMRKYQDESIKLAKQRYPSYNKKELTMVAEQEWDQAAREIMSTKLAIGQALMPGGHWGYYGYPRTWGSKRNTQLRNNRIDWLWRQSTGLYPSIYIKDPNMTESAIAEFVSGNVEEAVRVQDEFSPPNTPIYPYAMLQSGDHIFFQVDHLKISLGLPAKMGTSGVILWASSNRYKNATRQCSRMRVHIDNVLGPYVENLTQVMADCSTTLCGGHGRCVHNSHDVLLGETDSQRLSGLCTPRHSRFRDYHCRCYSDWEGACCQTVRPSRCHKQQQGNVHEGGDLQEGHVVNVVNPLIG | 3.2.1.35 | null | carbohydrate metabolic process [GO:0005975]; hyaluronan catabolic process [GO:0030214] | cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576] | hyalurononglucosaminidase activity [GO:0004415] | PF01630; | 3.20.20.70; | Glycosyl hydrolase 56 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28479398}. | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35; Evidence={ECO:0000269|PubMed:28479398}; | null | null | null | null | FUNCTION: Hyaluronidase catalyzes the hydrolysis of hyaluronic acid (HA), an anionic, nonsulfated glycosaminoglycan distributed widely throughout connective, epithelial, and neural tissues (PubMed:28479398). In venom, they are known to enhance diffusion of the venom by degrading the extracellular matrix (Probable). {ECO:0000269|PubMed:28479398, ECO:0000305}. | Conus purpurascens (Purple cone) |
C0HKQ7 | CECA1_DROME | MNFYNIFVFVALILAITIGQSEAGWLKKIGKKIERVGQHTRDATIQGLGIAQQAANVAATARG | null | null | antibacterial humoral response [GO:0019731]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; defense response to insect [GO:0002213]; humoral immune response [GO:0006959]; innate immune response [GO:0045087]; response to bacterium [GO:0009617] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | null | PF00272; | null | Cecropin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16510152}. | null | null | null | null | null | FUNCTION: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria (PubMed:11266367, PubMed:2390977). Functions in the imd/NF-kappa-B (Imd) epithelial and humoral immune response to Gram-negative bacteria (PubMed:11266367). {ECO:0000269|PubMed:11266367, ECO:0000269|PubMed:2390977}. | Drosophila melanogaster (Fruit fly) |
C0HKQ8 | CECA2_DROME | MNFYNIFVFVALILAITIGQSEAGWLKKIGKKIERVGQHTRDATIQGLGIAQQAANVAATARG | null | null | antibacterial humoral response [GO:0019731]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; defense response to insect [GO:0002213]; humoral immune response [GO:0006959]; innate immune response [GO:0045087] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | null | PF00272; | null | Cecropin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. {ECO:0000269|PubMed:2390977}. | Drosophila melanogaster (Fruit fly) |
C0HL12 | AGRB1_RAT | MRGQAAAPGPIWILAPLLLLLLLLGRWARAASGADIGPGTEQCTTLVQGKFFGYFSAAAVFPANASRCSWTLRNPDPRRYTLYMKVAKAPAPCSGPGRVRTYQFDSFLESTRTYLGVESFDEVLRLCDPSAPLAFLQASKQFLQMQRQQPPQDGDLGPQGSGDDFSVEYLVVGNRNPSHAACQMLCRWLDACLAGSRSSHPCGIMQTPCACLGGEAGDTASSPLVPRGDVCLRDGVAGGPENCLTSLTQDRGGHGSAGGWKLWSLWGECTRDCGGGLQTRTRTCSPTLGVEGRGCEGVLEEGRLCNRKACGPTGRTSSRSQSLRSTDARRREEFGDELQQFGFPSPQTGDPAAEEWSPWSVCSSTCGEGWQTRTRFCVSSSYSTQCSGPLREQRLCNNSAVCPVHGAWDEWSPWSLCSSTCGRGFRDRTRTCRPPQFGGNPCEGPEKQTKFCNIALCPGRAVDGNWNEWSSWSTCSASCSQGRQQRTRECNGPSYGGAECQGHWVETRDCFLQQCPVDGKWQAWASWGSCSVTCGGGSQRRERVCSGPFFGGAACQGPQDEYRQCGAQRCPEPHEICDEDNFGAVVWKETPAGEVAAVRCPRNATGLILRRCELDEEGIAFWEPPTYIRCVSIDYRNIQMMTREHLAKAQRGLPGEGVSEVIQTLLEISQDGTSYSGDLLSTIDVLRNMTEIFRRAYYSPTPGDVQNFVQIISNLLAEENRDKWEEAQLMGPNAKELFRLVEDFVDVIGFRMKDLRDAYQVTDNLVLSIHKLPASGATDISFPMKGWRATGDWAKVPEDRVTVSKSVFSTGLAEADDSSVFVVGTVLYRNLGSFLALQRNTTVLNSKVISVTVKPPPRSLLTPLEIEFAHMYNGTTNQTCILWDETDGPSSSAPPQLGPWSWRGCRTVPLDALRTRCLCDRLSTFAILAQLSADATMDKVTVPSVTLIVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTEAWQSYMAVTGRLRSRLVRKRFLCLGWGLPALVVAISVGFTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSKDGITDKKLKERAGASLWSSCVVLPLLALTWMSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRVVDRQEEGNGDSGGSFQNGHAQLMTDFEKDVDLACRSVLNKDIAACRTATITGTFKRPSLPEEEKMKLAKGPPPTFNSLPANVSKLHLHGSPRYPGGPLPDFPNHSLTLKKDKAPKSSFIGDGDIFKKLDSELSRAQEKALDTSYVILPTATATLRPKPKEEPKYSINIDQMPQTRLIHLSMAPDASFPTRSPPAREPPGGAPPEVPPVQPPPPPPPPPPPQQPIPPPPSLEPAPPSLGDTGEPSAHPGPSSGAGTKNENVATLSVSSLERRKSRYAELDFEKIMHTRKRHQDMFQDLNRKLQHAAEKEKEVPGVDNKPEKQQTPNKRAWESLRKPHGTPAWVKKELEPLPPSPLELRSVEWEKAGATIPLVGQDIIDLQTEV | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; apoptotic cell clearance [GO:0043277]; cell surface receptor signaling pathway [GO:0007166]; defense response to Gram-negative bacterium [GO:0050829]; engulfment of apoptotic cell [GO:0043652]; innate immune response [GO:0045087]; muscle organ development [GO:0007517]; negative regulation of angiogenesis [GO:0016525]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of protein ubiquitination [GO:0031397]; nervous system development [GO:0007399]; phagocytosis, engulfment [GO:0006911]; phagocytosis, recognition [GO:0006910]; positive regulation of myoblast fusion [GO:1901741]; positive regulation of reactive oxygen species biosynthetic process [GO:1903428]; positive regulation of synapse assembly [GO:0051965]; postsynaptic actin cytoskeleton organization [GO:0098974]; regulation of synaptic plasticity [GO:0048167] | dendrite [GO:0030425]; dendritic spine [GO:0043197]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; perinuclear region of cytoplasm [GO:0048471]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211] | G protein-coupled receptor activity [GO:0004930]; lipopolysaccharide binding [GO:0001530]; PDZ domain binding [GO:0030165]; phosphatidylserine binding [GO:0001786]; transmembrane signaling receptor activity [GO:0004888] | PF00002;PF19188;PF16489;PF01825;PF02793;PF00090; | 1.25.40.610;2.60.220.50;4.10.1240.10;1.20.1070.10;2.20.100.10; | G-protein coupled receptor 2 family, LN-TM7 subfamily | PTM: Proteolytically cleaved to produce vasculostatin-40 and vasculostatin-120. Vasculostatin-40 is the major form and is produced through proteolytic cleavage by MMP14 between residues 317 and 325 with cleavage likely to be between Ser-322 and Leu-323. {ECO:0000250|UniProtKB:O14514}.; PTM: Ubiquitinated. {ECO:0000250|UniProtKB:O14514}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14514}; Multi-pass membrane protein {ECO:0000255}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q3UHD1}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q3UHD1}. Cell projection, dendritic spine {ECO:0000269|PubMed:23595754}. Postsynaptic density {ECO:0000269|PubMed:23595754}.; SUBCELLULAR LOCATION: [Vasculostatin-120]: Secreted {ECO:0000250|UniProtKB:O14514}.; SUBCELLULAR LOCATION: [Vasculostatin-40]: Secreted {ECO:0000250|UniProtKB:O14514}. | null | null | null | null | null | FUNCTION: Phosphatidylserine receptor which enhances the engulfment of apoptotic cells (By similarity). Also mediates the binding and engulfment of Gram-negative bacteria (By similarity). Stimulates production of reactive oxygen species by macrophages in response to Gram-negative bacteria, resulting in enhanced microbicidal macrophage activity (By similarity). In the gastric mucosa, required for recognition and engulfment of apoptotic gastric epithelial cells (By similarity). Promotes myoblast fusion (By similarity). Activates the Rho pathway in a G-protein-dependent manner (By similarity). Inhibits MDM2-mediated ubiquitination and degradation of DLG4/PSD95, promoting DLG4 stability and regulating synaptic plasticity (By similarity). Required for the formation of dendritic spines by ensuring the correct dendritic localization of PARD3 and TIAM1 (PubMed:23595754). Potent inhibitor of angiogenesis in brain and may play a significant role as a mediator of the p53/TP53 signal in suppression of glioblastoma (By similarity). {ECO:0000250|UniProtKB:O14514, ECO:0000269|PubMed:23595754}.; FUNCTION: [Vasculostatin-120]: Inhibits angiogenesis in a CD36-dependent manner. {ECO:0000250|UniProtKB:O14514}.; FUNCTION: [Vasculostatin-40]: Inhibits angiogenesis. {ECO:0000250|UniProtKB:O14514}. | Rattus norvegicus (Rat) |
C0HL13 | LRP2_PIG | MERWAAAAACTLLLAFAACLAPASGRECLGNEFRCSNGHCITESWRCDGTRDCLDGSDEIGCPPSTCGSTQFHCENEDVCIPLYWVCDGEEDCSNGADEHQRCPPGRTCSSHHFTCTNGECIPVEYRCDHSTDCLDGTDEINCRYPVCQQQTCHNGACYNTSQRCDGEIDCRDASDELNCTQRCLRNEFQCGSGECIPRDYVCDHDPDCSDSSDEHSCSVYQPCKGNEFACSNGFCINQNWVCDGMADCLDNSDEDGCESSIIRTHECYPNEWACPEDGKCIPLSRVCDGIADCPRGGDENKQGRVCDVNMCPSLGCEYQCHKSPSGGTCNCPPGFIVNKNNTRSCVDFNDCQIWGICDHFCEDRIGHHQCFCAEGYVLEHEQHCRANSSSGQAFVIFSNGRNLLLGDIQGQSFEYLVRSQNRGSPVGVDFHYRLSKVFWTDTMQNKVFSLDIDGLVIREVLSVSIEDPENLAVDWINNKLYIVETNVNRIDLANLDGSHRITLITENLGRPRGIALDPTVGYLFFSDWQSISGQPKIERAYMDGSNRKDLVKIKLGWPGGITLDLVAKRVYWVDARFDYIETVTYDGTQRKTVLQGGSNIPHPFGITLFEDNLFFTDWTKFSVMKANKFTETNPRVYFRSSTRPFGVTVYHAIRQPSVRNPCGNNNGGCEHICVLSHRTDNGGLGYRCKCKLGYIPGLDDYSCVATKQFLFFSTDVAVRGIPLTPSNQKDVILPVTGSPSVFVGIDFDAKENAIFFSDTSKDMIFRQKINGTGREIITANRVPSVESLSFDWISRNLYWTDASYRSVTVMRLADKSRRTIVQNLNNPRSIVVHPIAGYIFFTDWFRPAKILRAWSDGSHMLPIVNTTLGWPNGLAIDWGSSRLYWVDAFLDKIEHTTFDGLDRRALNHLQQMTHPFGLTVFGEYVYFTDWRQRSIVRVRKTDGGEMTILRNGVGNVMRVKIFETSIQVGSNACNRPTNPNGDCSHFCFPVPNLQRVCGCPYGMRLASNRLNCVNDSSREPPMEQCGALSFPCNNGRCVPLHYRCDGVDDCHDNSDEVQCGAFNTSCAPSAFACGHGGGECIPSYWRCDNHNDCVDGSDEQNCSSQAQTSCRADYFTCDNHMCIPKNWLCDTDNDCGDGSDEKRCDLGETCSPTQFHCPNHRCIDLAFVCDGDKDCADGSDESACVINCTDSQFKCVGSNKCISNTYRCDGVSDCSDHSDEIDCPTRPPGMCRQDEFQCREDGICIPDSWECDGHPDCLTGSDEHSGCPPRTCPXSRFLCANGNCIFRDWLCDGDNDCRDMSDEKDCPTQPFLCPSWQWQCPGHSICVNLSSVCDGISDCPHGTDESPLCNQESCLHSNGGCTHLCIQGPFGAQCECPLGYRLANDSKTCEDIDECRIPGFCSQHCYNMRGSFRCWCDIEYSLEADQRTCKATASESLLLVVANQNQLIADNITKSMDHMRALIQDGSHIVAVDFDSVRGRIFWSDKTLGKIFSAFQNGTDRKPVFNSGNIMTESIAVDWVGRNLYWADFALETIEVSKLDGTLRTVLLSENVTSPRGIVLDPRVNDRVIFWTNWGSYPRIERASMDGEMRTVIVQQKIFWPNGLAIDYPTRLLYFADGNLDHIHFCKYDGSNRKQVISSGEGSGHLFAITIFEDSIYWTDRNSQDVRKANKWHGGNESVVLSASQPLGIVAVHPARQPTARNPCTIARCSHLCLLSSERLYSCACPSGWSLSQDSMTCVRDDDAFLIVVRRTTIFGISLNPEVNTDNAMVPISGMESGYDVEVDYSEQFLYYADYPGEIYKVKTDGTNRTLFDPLTKVGSTTTLALDWLSRNLYYTDSEARSIKVLTLRGNVRYRKTLITNDGTTLGIGVPVSITVDPAKGKLYWSDLGIEGRVPAKIACANMDGTSRKNLFTGHLENVGFITLDIQEQKLYWTVRSYISIERGNVDGTDRMSLVNSLPRPRGIAVYGPYLYYADEQNQVIERVDKATGANKVVVREGLPNLRALRIYRRRGSESSNGCSNNINACQQICLPVPGGLFTCACAVGFKLNPDNRTCSSHDSFIVVSMLTAIRGYSLDVSDHSEAMVPVELEGQNTLHVDVDVSSGFVYWADFNRNVQTDNAIRRIKIDGSGFADIITDGIGKDGIRGIAVDWVAGNLYFINAFVSETLIEVLRINTTHRRVLLKTTEDVPRDIVVDPKNRYLFWSDIGQTPKIERSFLDCTNRTVLVSEMVASPRGLALDHNSGYIYWVDDSLDLIARVSIHGGNSETIRFGSSYPTPYAIAVFGNSIIWVDRDLKTIFQASKEPFKTDPPTVIRNNINWLRDVTVFDKQAQPRSPAEVNYNPCLQNNGGCTHFCFALPQLRTPKCGCAFGVLQGDGRSCAISREDFLIYALDNSVRSLHFDPEDYNVPFTAISVEETAVAVDYDSIDNRIYFTQVLASGKGQISYISLNSRSHSPTVVISNLGSPDGIAFDWIGRRIYYSDYTNQTIQSMNMDGSRRTVVARVTKPRAIVLDPCQGYMYWTDWSTNAQIERATMAGNFRNSIVNRDLVWPNGLTLDYKENLLYWADASLQKIERSSVTGTGREVIVSRANAPFGLTVYGQYIYWTDWLTQKIYRANKYDGSGQTAMTTALPFLPNGIRAVVNNQELCHNPCGRFNGGCSHVCAPGPNGPECKCPHEGRWYLANNNKYCIVDDGKRCNSTQFTCLSGYCILESLKCNDIDECGDSSDELETLCAYHTCPPTSFTCANGRCIQRHFRCDHYNDCGDNSDESGCRFRSCNITTEFSCNNGKCLPLQLVCDGIDHCNDNNTSDEKNCAQHTCLPDYIKCANSNVCIPRLFLCDGDNDCGDMSDENPIYCVSPTCKNNEFQCTSGSCIPELWHCDGERDCDDGSDEPATCVYSPSTCSSDEFKCDNNRCIQMEWICDGDNDCGDMSDEDGRHHCENHNCSSYAFHCVNSAPPSRRCIPLSWVCDGDADCSDAYDEHQNCTRRNCSGTEFRCSNGLCIPNWFRCDRRNDCGDYSDERNCKYPACDENLFTCQNGICTYKSYICDGENDCGDNSDELEHLCHKEETTCPPHQFRCNNGNCIEMVKVCNHQADCSDNSDEERCGVNECNDPLLSGCDQNCTDTLTSFYCSCKPGYRLLPDKRTCVDIDECKETPSVCSQKCENLLGSYICKCAPGYTREPDGRSCRQNTNIEPYLIFSNRYYLRNLTIDGHIYSLILQGLGNAVALDFDRVEERLYWLDIENKVIERMFLNKTNREAVIKYNIPGTESLAVDWVTRKLYWSDSYLNCLSVSDLNGRYRRKLAEHCVDVNNTFCFDKPRGIALHPRYGYVYWADWTDRAYIGRVGMDGRNKSLIISSKIKWPNGITIDYTNDLLYWTDAHLGYIEYSDLEGSHRHTVYETGTLSHPFAVTIFEDTIYWTDWNTKTVEKGNKYNGSNREVLVNTTHRPYDIHVYHPYRQPFVSNPCGTNNGGCSHLCLIKAGGNGFTCECPDNFYTIQHGDTTQCLPMCSSTQFLCANNEMCIPIWWKCDGQKDCLDGSDEPNTCPQRFCRLGQFQCSDGNCTSSNFICNARQDCPDGSDEDAVLCEHHRCESNQWQCANKRCIPESWQCDSLNDCGDNSDEDSSHCARRTCLPGYFKCANGHCIPQSWKCDVDNDCGDYSDEPLQECMGPAYRCDNYTEFDCKTNYRCIPKWAVCNGFDDCRDNSDEQNCESLTCKPSGEFRCTNHHCIPLRWRCDGHNDCGDNSDEENCVPRQCSESEFRCDDQTCIPSRWICDQNNDCGDNSDERDCEVMTCHPGYFQCSSGHCIPDQMRCDGFADCLDASDEATCPTRFPNGAYCPATLFECKNHVCVQPSWKCDGDNDCGDGSDEELHLCLNITCDLTNRFRCDNNRCIYRHELCNHEDDCGDGSDEKKENCLAPTPRPCTEGEFKCSNGHCISQHLVCDDVDDCGDHFDETGCNTGEERSCAENLCEHNCTQLIGGGFICSCRPGFKASSLNRNSCEDINECEQFGVCPQNCHNTKGSYECTCAEGFRSMSEHYGERCAAEGNPPLLLLPENVRVRKYNLSSEKFSDYLEDQERIQALDYDWDPEGTGLSVVYYTVLGHGSKFGAIKRAYIPNFESGSNNPVKEVNLGLKYIVQPDGIAVDWVGRHIYWSDAKTQRIEVAELDGRYRKWLITTLLDQPAAIVVNPKQGLMYWTDWGKNPKIEIAWMDGQHRKVLVQEDLGWPTGLSIDYVNSDRIYWSDLKEDVIETIKHDGTDRKVVVTAAMNPYSLDIFESQLYWISKDKGEIWVQDKFERDRKEKLLIVNPWLTQVRIFHQRRYNQSVPNRCKKVCSHLCLLKPEGYTCACPQGSRFIAGSVTECDAAIESPVTMPPPCRCMNEGNCYFDKNNLPKCKCPSGYMGEYCEIGLSKGISPGTTVAVLVTLILIIIIGGLVALGFFHYRKTGSILISMPRLPSLSNLSKYTENGNGVTFRSGEDVNMDIGVSGFGPESAIDRSMAMSEHFAMDLEKPPIIFENPMYTSKDGTIRMAQPTTTQVSESGNVYNKNYGSPVNPDELAPDTKPASPSADETQVTKWNIFKRKPKQNTNFENPIYAETENEPKVGAAVTPPPSPSPPAKKTQKKGTTPAYSATEDTFKDTANLVREDSEA | null | null | coronary artery morphogenesis [GO:0060982]; folate import across plasma membrane [GO:1904447]; male gonad development [GO:0008584]; metal ion transport [GO:0030001]; negative regulation of BMP signaling pathway [GO:0030514]; neural tube closure [GO:0001843]; neuron projection arborization [GO:0140058]; outflow tract septum morphogenesis [GO:0003148]; positive regulation of lysosomal protein catabolic process [GO:1905167]; positive regulation of neurogenesis [GO:0050769]; positive regulation of oligodendrocyte progenitor proliferation [GO:0070447]; pulmonary artery morphogenesis [GO:0061156]; receptor-mediated endocytosis [GO:0006898]; secondary heart field specification [GO:0003139]; sensory perception of sound [GO:0007605]; vagina development [GO:0060068]; ventricular compact myocardium morphogenesis [GO:0003223] | apical plasma membrane [GO:0016324]; axon [GO:0030424]; brush border membrane [GO:0031526]; clathrin-coated pit [GO:0005905]; dendrite [GO:0030425]; endosome lumen [GO:0031904]; external side of plasma membrane [GO:0009897]; receptor complex [GO:0043235] | calcium ion binding [GO:0005509]; hormone binding [GO:0042562]; protein-folding chaperone binding [GO:0051087]; SH3 domain binding [GO:0017124] | PF12662;PF07645;PF14670;PF00057;PF00058; | 4.10.1220.10;2.10.25.10;4.10.400.10;2.120.10.30; | LDLR family | PTM: A fraction undergoes proteolytic cleavage of the extracellular domain at the cell membrane to generate a cytoplasmic tail fragment. This is internalized into the early endosome from where it trafficks in an LDLRAP1/ARH-dependent manner to the endocytic recycling compartment (ERC). In the ERC, it is further cleaved by gamma-secretase to release a fragment which translocates to the nucleus and mediates transcriptional repression. {ECO:0000250|UniProtKB:P98158}.; PTM: N-glycosylation is required for ligand binding. {ECO:0000250|UniProtKB:A2ARV4}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P98158}; Single-pass type I membrane protein {ECO:0000255}. Endosome lumen {ECO:0000250|UniProtKB:P98158}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:A2ARV4}. Cell projection, dendrite {ECO:0000250|UniProtKB:A2ARV4}. Cell projection, axon {ECO:0000250|UniProtKB:A2ARV4}. Note=Localizes to brush border membranes in the kidney. In the endolymphatic sac of the inner ear, located in the lumen of endosomes as a soluble form. {ECO:0000250|UniProtKB:P98158}. | null | null | null | null | null | FUNCTION: Multiligand endocytic receptor (By similarity). Acts together with CUBN to mediate endocytosis of high-density lipoproteins (By similarity). Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B (By similarity). In the kidney, mediates the tubular uptake and clearance of leptin (By similarity). Also mediates transport of leptin across the blood-brain barrier through endocytosis at the choroid plexus epithelium (By similarity). Endocytosis of leptin in neuronal cells is required for hypothalamic leptin signaling and leptin-mediated regulation of feeding and body weight (By similarity). Mediates endocytosis and subsequent lysosomal degradation of CST3 in kidney proximal tubule cells (By similarity). Mediates renal uptake of 25-hydroxyvitamin D3 in complex with the vitamin D3 transporter GC/DBP (By similarity). Mediates renal uptake of metallothionein-bound heavy metals (By similarity). Together with CUBN, mediates renal reabsorption of myoglobin (By similarity). Mediates renal uptake and subsequent lysosomal degradation of APOM (By similarity). Plays a role in kidney selenium homeostasis by mediating renal endocytosis of selenoprotein SEPP1 (By similarity). Mediates renal uptake of the antiapoptotic protein BIRC5/survivin which may be important for functional integrity of the kidney (By similarity). Mediates renal uptake of matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (By similarity). Mediates endocytosis of Sonic hedgehog protein N-product (ShhN), the active product of SHH (By similarity). Also mediates ShhN transcytosis (By similarity). In the embryonic neuroepithelium, mediates endocytic uptake and degradation of BMP4, is required for correct SHH localization in the ventral neural tube and plays a role in patterning of the ventral telencephalon (By similarity). Required at the onset of neurulation to sequester SHH on the apical surface of neuroepithelial cells of the rostral diencephalon ventral midline and to control PTCH1-dependent uptake and intracellular trafficking of SHH (By similarity). During neurulation, required in neuroepithelial cells for uptake of folate bound to the folate receptor FOLR1 which is necessary for neural tube closure (By similarity). In the adult brain, negatively regulates BMP signaling in the subependymal zone which enables neurogenesis to proceed (By similarity). In astrocytes, mediates endocytosis of ALB which is required for the synthesis of the neurotrophic factor oleic acid (By similarity). Involved in neurite branching (By similarity). During optic nerve development, required for SHH-mediated migration and proliferation of oligodendrocyte precursor cells (By similarity). Mediates endocytic uptake and clearance of SHH in the retinal margin which protects retinal progenitor cells from mitogenic stimuli and keeps them quiescent (By similarity). Plays a role in reproductive organ development by mediating uptake in reproductive tissues of androgen and estrogen bound to the sex hormone binding protein SHBG (By similarity). Mediates endocytosis of angiotensin-2 (By similarity). Also mediates endocytosis of angiotensis 1-7 (By similarity). Binds to the complex composed of beta-amyloid protein 40 and CLU/APOJ and mediates its endocytosis and lysosomal degradation (PubMed:9228033). Required for embryonic heart development (By similarity). Required for normal hearing, possibly through interaction with estrogen in the inner ear (By similarity). {ECO:0000250|UniProtKB:A2ARV4, ECO:0000250|UniProtKB:P98158, ECO:0000250|UniProtKB:P98164, ECO:0000269|PubMed:9228033}. | Sus scrofa (Pig) |
C0HL58 | NDB4B_ISOMC | FLGSLFSIGSKLLPGVIKLFQRKKQ | null | null | cytolysis in another organism [GO:0051715]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | PF08024; | null | Non-disulfide-bridged peptide (NDBP) superfamily, Medium-length antimicrobial peptide (group 3) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28941793}. Target cell membrane {ECO:0000305|PubMed:28941793}. | null | null | null | null | null | FUNCTION: May act by disrupting the integrity of the bacterial cell membrane. Has antibacterial activity against Gram-negative bacterium E.coli NBRC 3972 (MIC=10 uM) and against Gram-positive bacteria S.aureus NBRC 13276 (MIC=2.5-5 uM) and B.subtilis NBRC 3009 (MIC=0.5-1 uM). Toxic to cricket A.domestica. Has hemolytic activity against sheep erythrocytes. {ECO:0000269|PubMed:28941793}. | Isometrus maculatus (Lesser brown scorpion) (Scorpio maculatus) |
C0HL66 | H33A_DROME | MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | null | null | nucleosome assembly [GO:0006334] | nucleosome [GO:0000786]; nucleus [GO:0005634]; polytene chromosome [GO:0005700] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H3 family | PTM: Phosphorylation at Ser-11 by aurB/ial during mitosis and meiosis is crucial for chromosome condensation and cell-cycle progression. Phosphorylation at Ser-11 by JIL-1 during interphase is linked to gene activation and restricts the formation of heterochromatin at inappropriate sites. Phosphorylation at Ser-11 is enriched on male X chromosome compared to the autosome. {ECO:0000269|PubMed:11114889, ECO:0000269|PubMed:11266459, ECO:0000269|PubMed:11371341, ECO:0000269|PubMed:12514098}.; PTM: Acetylation is generally linked to gene activation. Acetylated on Lys-15 during prophase I of meiosis. Phosphorylation of H2A 'Thr-119' is a prerequisite for H3 Lys-15 acetylation. Acetylation on Lys-15 is enriched on male X chromosome compared to the autosome. {ECO:0000269|PubMed:11114889, ECO:0000269|PubMed:11371341, ECO:0000269|PubMed:14732680}.; PTM: Methylation at Lys-5 or Lys-80 is generally associated with active chromatin. Methylation at Lys-80 by gpp occurs at low levels in specific developmental stages and tissues undergoing active cell division, and at highest levels in epidermal cells undergoing differentiation. {ECO:0000269|PubMed:14732680, ECO:0000269|PubMed:15371351}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. | null | null | null | null | null | FUNCTION: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes and is specifically enriched in modifications associated with active chromatin. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:14732680}. | Drosophila melanogaster (Fruit fly) |
C0HL67 | H33B_DROME | MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | null | null | nucleosome assembly [GO:0006334] | nucleosome [GO:0000786]; nucleus [GO:0005634]; polytene chromosome [GO:0005700] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H3 family | PTM: Phosphorylation at Ser-11 by aurB/ial during mitosis and meiosis is crucial for chromosome condensation and cell-cycle progression. Phosphorylation at Ser-11 by JIL-1 during interphase is linked to gene activation and restricts the formation of heterochromatin at inappropriate sites. Phosphorylation at Ser-11 is enriched on male X chromosome compared to the autosome. {ECO:0000269|PubMed:11114889, ECO:0000269|PubMed:11266459, ECO:0000269|PubMed:11371341, ECO:0000269|PubMed:12514098}.; PTM: Acetylation is generally linked to gene activation. Acetylated on Lys-15 during prophase I of meiosis. Phosphorylation of H2A 'Thr-119' is a prerequisite for H3 Lys-15 acetylation. Acetylation on Lys-15 is enriched on male X chromosome compared to the autosome. {ECO:0000269|PubMed:11114889, ECO:0000269|PubMed:11371341, ECO:0000269|PubMed:14732680}.; PTM: Methylation at Lys-5 or Lys-80 is generally associated with active chromatin. Methylation at Lys-80 by gpp occurs at low levels in specific developmental stages and tissues undergoing active cell division, and at highest levels in epidermal cells undergoing differentiation. {ECO:0000269|PubMed:14732680, ECO:0000269|PubMed:15371351}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. | null | null | null | null | null | FUNCTION: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes and is specifically enriched in modifications associated with active chromatin. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:14732680}. | Drosophila melanogaster (Fruit fly) |
C0HL84 | PNG1_PANCL | LNWGAILKHIIK | null | null | cytolysis in another organism [GO:0051715]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; disruption of plasma membrane integrity in another organism [GO:0051673]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | null | null | null | null | null | SUBCELLULAR LOCATION: Target cell membrane {ECO:0000305|PubMed:23483218}. Secreted {ECO:0000269|PubMed:23483218}. | null | null | null | null | null | FUNCTION: Antimicrobial peptide active against Gram-positive bacteria M.luteus (MIC=1.5 uM), B.subtilis (MIC=1.3 uM) and S.aureus (MIC=10.6 uM), against Gram-negative bacteria E.coli (MIC=3.7 uM) and P.aeruginosa (MIC=51.7 uM) as well as against yeast C.albicans (MIC=7.3 uM). Has weak hemolytic activity against human erythrocytes. Probably acts by disrupting membranes of target cells. {ECO:0000269|PubMed:23483218}. | Panurgus calcaratus (Solitary bee) |
C0HL98 | MAC1_MACFV | GFGMALKLLKKVL | null | null | defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; disruption of plasma membrane integrity in another organism [GO:0051673]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | null | null | null | Lasioglossin-like family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24616110}. Target cell membrane {ECO:0000269|PubMed:24616110, ECO:0000269|PubMed:29185466}. Note=Adopts an alpha-helical structure in a membrane mimic environment. {ECO:0000269|PubMed:24616110, ECO:0000269|PubMed:29185466}. | null | null | null | null | null | FUNCTION: Antimicrobial peptide with activity against Gram-positive bacteria (B.subtilis, S.aureus and L.monocytogenes) and Gram-negative bacteria (E.coli and P.aeruginosa) (MIC=1.3-35 uM) (PubMed:24616110, PubMed:29185466). Also active against fungus C.albicans (MIC=6.3 uM) (PubMed:24616110). Has little hemolytic activity (PubMed:24616110, PubMed:29185466). Acts by disrupting membranes and bacterial cell wall structures (PubMed:29185466). Binds to peptidoglycan and lipopolysaccharide (LPS) (PubMed:29185466). In the context of inflammation and cancer tests, is weakly cytotoxic to normal cells, induces calcium signaling but does not impact cAMP production (PubMed:36548715). In addition, prevents LPS-induced nitric oxid (NO) synthesis but does not affect the IP3 signaling and pro-inflammatory activation of endothelial cells (PubMed:36548715). Does not show significant antiproliferative activity on the breast cancer cell line MDA-MB-231 (PubMed:36548715). {ECO:0000269|PubMed:24616110, ECO:0000269|PubMed:29185466, ECO:0000269|PubMed:36548715}. | Macropis fulvipes (Solitary bee) (Megilla fulvipes) |
C0HLF0 | PA2_POROP | NLFQFRKMIKKMTKKEPVVYYAFYGCYCGKGGRGKPKDATDRCCFVHDCCYEKVTGCNPKWGYYTYSMNKQIVCGGDDPCKKQVCECDKAAAICFRDNLKTYKKKYMSFPNFFCTDPSEKC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:29886171}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29886171}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036, ECO:0000269|PubMed:29886171}; | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that displays moderate myotoxic activity in vivo, and cytotoxic activity in vitro. In vitro, shows anticoagulant activity on human plasma and in mice causes inflammatory cell infiltration and myonecrosis in the gastrocnemius muscles of CD-1 mice 3 hours after injection (100 ug). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:29886171}. | Porthidium ophryomegas (Slender hognose viper) |
C0HLF7 | PA2B_OPHSH | HLLQFNKMIKEETGKNAIPFYAFYGCYCGWGGSGKPKDATDRCCFEHDCCYGKLTNCNTKWDIYSYSLKDGYITCGKGTWCEKEVCECDKCLRRNLRTYKYGYMFYL | 3.1.1.4 | null | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30205237}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000269|PubMed:30205237}; | null | null | null | null | FUNCTION: Heterodimer A-B: Sphenotoxin is a potent neurotoxin that possesses phospholipase A2 (PLA2) activity. It consists of a non-covalent association of a basic PLA2 subunit B with a non-enzymatic subunit A. {ECO:0000269|PubMed:30205237}.; FUNCTION: Monomer B: Not found in vivo. In vitro, potent neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission. Induces paralysis of the hind legs and neuromuscular blockade in mouse phrenic nerve-diaphragm preparations. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:30205237}. | Ophryacus sphenophrys (Broad-horned pitviper) (Bothrops sphenophrys) |
C0HLG3 | RNAG_CYCAE | MSESSTFTTAVVPEGEGVAPMAETVQYYNSYSDASIASCAFVDSGKDKIDKTKLVTYTSRLAASPAYQKVVGVGLKTAAGSIVPYVRLDMDNTGKGIHFNATKLSDSSAKLAAVLKTTVSMTEAQRTQLYMEYIKGIENRSAQFIWDWWRTGKAPA | 4.6.1.23 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:30262416}; | killing of cells of another organism [GO:0031640] | vacuolar lumen [GO:0005775] | lyase activity [GO:0016829]; magnesium ion binding [GO:0000287]; RNA endonuclease activity [GO:0004521]; rRNA endonuclease activity [GO:0033902] | null | null | Ribotoxin-like family | null | SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:32998313}. Note=Possibly sequestered into the vacuole to avoid its toxic activity on ribosomes. {ECO:0000305|PubMed:32998313}. | CATALYTIC ACTIVITY: Reaction=a 28S rRNA containing guanosine-adenosine pair + H2O = an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment].; EC=4.6.1.23; Evidence={ECO:0000269|PubMed:28232091, ECO:0000269|PubMed:30262416, ECO:0000269|PubMed:31444206}; | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Highly thermostable. Has a melting temperature of 78 degrees Celsius at pH 7.4. {ECO:0000269|PubMed:30262416}; | FUNCTION: Fungal ribonuclease involved in fungal defense. Highly specific and highly toxic fungal endonuclease that cleaves a single phosphodiester bond in the 28S RNA of eukaryotic ribosomes at a universally conserved GAGA tetraloop of the sarcin-ricin loop (SRL). The damage of the SRL inhibits the binding of translation elongation factors and halts protein biosynthesis, ultimately resulting in the death of the target cells (PubMed:28232091, PubMed:30262416, PubMed:31444206). Shows antitumor activity (PubMed:28232091, PubMed:30262416). Exerts cytotoxicity and induces apoptosis towards rat glial cells and human glioma cells, and also displays some activity towards human neurolastoma cell lines (PubMed:28232091). Shows a strong entomotoxicity against Aedes aegypti larvae, yet no nematotoxicity against nematodes (PubMed:31444206). {ECO:0000269|PubMed:28232091, ECO:0000269|PubMed:30262416, ECO:0000269|PubMed:31444206}. | Cyclocybe aegerita (Black poplar mushroom) (Agrocybe aegerita) |
C0HLG4 | KKX1U_UROMN | MKYFTLALTLLFLLLINPCKDMNFAWAESSEKVERASPQQAKYCYEQCNVNKVPFDQCYQMCSPLERS | null | null | null | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430] | ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | null | null | Short scorpion toxin superfamily, Potassium channel inhibitor kappa-KTx family, Kappa-KTx 1 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31447178}. Host cytoplasm {ECO:0000269|PubMed:31447178}. Note=Penetrates into cell via passive diffusion and binds to the cytoplasmic side of TRPA1 (PubMed:31447178). {ECO:0000269|PubMed:31447178}. | null | null | null | null | null | FUNCTION: Cell-penetrating peptide (CPP) with defensive purpose that induces pain by specifically activating mammalian sensory neuron TRPA1 channels. It non-covalently binds to the same region than other TRPA1 agonists (irritants), but acts via a distinct biochemical mechanism. Its binding stabilizes the TRPA1 open state and diminishes calcium-permeability. Consequently, it produces pain and pain hypersensitivity, but fails to trigger efferent release of neuropeptides (CGRP) and neurogenic inflammation typically produced by noxious electrophiles. Is not active on voltage-gated potassium channels and other TRP channels. {ECO:0000269|PubMed:31447178}. | Urodacus manicatus (Black rock scorpion) |
C0HLL2 | PA2_PITAZ | MAFLVFAFLTLMAVETYGSLFQFRLMINYLTGKLPILSHSFYGCYCGAGGSGWPKDAIDWCCQVHDCCYGRMSASGCDPYFQPYNFSYINKNLQCVETDTSGCPRRICECDRLASICFQQHDATYNSSNIDPKRKGCGTKSPPCPN | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:31173792}; | arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; glycerophospholipid catabolic process [GO:0046475]; positive regulation of fibroblast proliferation [GO:0048146] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102] | PF00068; | 1.20.90.10; | Phospholipase A2 family | PTM: N-glycosylated. Glycosylated with mannose chains including Man2(GlcNAc), Man2(GlcNAc)2, Man2(GlcNAc)3, Man2(GlcNAc)4 and Man2(GlcNAc)5. {ECO:0000269|PubMed:31173792}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31173792}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:31173792}; | null | null | null | null | FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:31173792}. | Pithecopus azureus (Orange-legged monkey tree frog) (Phyllomedusa azurea) |
C0HLR3 | SCX1_CENBA | KEGYIVNHSTGCKYECYKLGDNDYCLRECKAQYGKGAGGYCYAFGCWCTHLYEQAVVWPLPKKTCN | null | null | defense response [GO:0006952]; envenomation resulting in negative regulation of voltage-gated sodium channel activity in another organism [GO:0044493] | extracellular space [GO:0005615] | calcium channel regulator activity [GO:0005246]; sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729] | null | 3.30.30.10; | Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Beta subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32479835}. | null | null | null | null | null | FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and reduces peak current and shifts the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing (PubMed:32479835). Has an inhibitory effect on voltage-gated sodium channel hNav1.6/SCN8A, affecting both the activation and inactivation processes (PubMed:32479835). This toxin is active against mammals and lethal to mice (PubMed:32479835). {ECO:0000269|PubMed:32479835}. | Centruroides baergi (Scorpion) (Centruroides nigrovariatus baergi) |
C0HLV2 | NEPRN_NEPVE | MQAKFFTFVILSSVFYFNYPLAEARSIQARLANKPKGTIKTIKGDDGEVVDCVDIYKQPAFDHPLLKNHTLQMQPSSYASKVGEYNKLEQPWHKNGECPKGSIPIRRQVITGLPVVKKQFPNLKFAPPSANTNHQYAVIAYFYGNASLQGANATINIWEPNLKNPNGDFSLTQIWISAGSGSSLNTIEAGWQVYPGRTGDSQPRFFIYWTADGYTSTGCYDLTCPGFVQTNNYYAIGMALQPSVYGGQQYELNESIQRDPATGNWWLYLWGTVVGYWPASIYNSITNGADTVEWGGEIYDSSGTGGFHTTTQMGSGHFPTEGYGKASYVRDLQCVDTYGNVISPTANSFQGIAPAPNCYNYQFQQGSSELYLFYGGPGCQ | 3.4.21.26 | null | proteolysis [GO:0006508] | extracellular region [GO:0005576] | endopeptidase activity [GO:0004175]; oligopeptidase activity [GO:0070012] | PF03080;PF14365; | 3.90.1320.10; | Peptidase G3 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27481162}. Note=Secreted into the viscoelastic fluid of the pitcher. {ECO:0000269|PubMed:27481162}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.; EC=3.4.21.26; Evidence={ECO:0000269|PubMed:27481162, ECO:0000269|PubMed:28404794, ECO:0000269|PubMed:35915115}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.36 M for fluorogenic FS6 peptide {ECO:0000269|PubMed:35915115}; KM=2.74 M for fluorogenic FS6-QPQL peptide {ECO:0000269|PubMed:35915115}; Note=kcat is 1.81 sec(-1) for the cleavage of the fluorogenic FS6 peptide (PubMed:35915115). kcat is 6.55 sec(-1) for the cleavage of the fluorogenic FS6-QPQL peptide (PubMed:35915115). {ECO:0000269|PubMed:35915115}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 2.5 (PubMed:28404794). At pH 4.5, the enzyme retains approximately 50% of its activity but it is almost completely inactivated at pH 8 (PubMed:28404794). Optimum pH is 3 with fluorescent bovine serum albumin (BSA) as substrate (PubMed:35915115). {ECO:0000269|PubMed:28404794, ECO:0000269|PubMed:35915115}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 37-50 degrees Celsius. {ECO:0000269|PubMed:28404794}; | FUNCTION: Glutamic endopeptidase that preferentially cleaves peptide bonds on the C-terminal side of proline residues (PubMed:27481162, PubMed:28404794, PubMed:35915115). Also cleaves peptide bonds on the C-terminal side of alanine residues but with less efficiency (PubMed:28404794). In contrast to most proline-cleaving enzymes, effectively degrades proteins of any size (PubMed:28404794). Found in the viscoelastic fluid of the pitcher, and so likely functions in the digestion of their prey (PubMed:27481162). {ECO:0000269|PubMed:27481162, ECO:0000269|PubMed:28404794, ECO:0000269|PubMed:35915115}. | Nepenthes x ventrata (Red tropical pitcher plant) (Nepenthes ventricosa x Nepenthes alata) |
C0HLV6 | LACS_TRAHI | FQLNVIANMNNHTMLKQTSIHWHCHFQKGTNWADGHAFVNACPIASGHSFLYDFTAPDQHGTFWYHSHLSTQYCDGLRGHFVVYDPADPHHDLYDVDDEHTIITLADWYHVAAKLGHHFQLGADSTLINGSGRFAGDPTAHLTVIYVTQGKRYRFHLVSLSCDPNHVFSIDSNHMTVIEADAVSHEHCTVDSIQIYAGQRYSFHLTVDQDVDNYWIRAHPSFGTYSFHDGINSAIARY | 1.10.3.2 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000269|PubMed:34093489}; Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:D0VWU3}; | lignin catabolic process [GO:0046274] | extracellular region [GO:0005576] | copper ion binding [GO:0005507]; hydroquinone:oxygen oxidoreductase activity [GO:0052716] | PF00394;PF07732; | 2.60.40.420; | Multicopper oxidase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34093489}. | CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2; Evidence={ECO:0000269|PubMed:34093489}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=87.47 uM for ABTS (at pH 6.0 and 50 degrees Celsius); Note=kcat is 129.37 sec(-1) for ABTS oxidation (at pH 6.0 and 50 degrees Celsius). {ECO:0000269|PubMed:34093489}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 at 25 degrees Celsius (PubMed:34093489). Retains over 60 percent activity in the pH range from 4 to 10 (PubMed:34093489). Retains activity above 50% after incubation at pH 5-10 for 72 hours (PubMed:34093489). {ECO:0000269|PubMed:34093489}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius (PubMed:34093489). Retains over 57 percent activity when incubated for 2 hours at temperatures between 30-65 degrees Celsius (PubMed:34093489). {ECO:0000269|PubMed:34093489}; | FUNCTION: Lignin degradation and detoxification of lignin-derived products (By similarity). Has activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) (PubMed:34093489). {ECO:0000250|UniProtKB:D0VWU3, ECO:0000269|PubMed:34093489}. | Trametes hirsuta (White-rot fungus) (Coriolus hirsutus) |
C0HLV7 | LACF_GANAU | FQLNVIANNNNHTMLTQTTIHCHGFFQGTNSADGHAFVNCCPIASGHSFLYDFSHPDQHGTFCYHSHLSTQYCCGLRGHFVVYDPSDPHCGLYDVDHDSTVITLSDWYHVAAKLGHSFCLGADSTLINGSGRSTGDCAASLTVISVTQGKRYRFHLVSLSCDPNHTFSIDGHDMSVIEVDSIASQHVTVDSIQIFAGQRYSFVLTANQSINNYWIRANPSFGNIGFHDGINSAILRY | 1.10.3.2 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000269|PubMed:34467865}; Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:D0VWU3}; | cellular response to iron ion starvation [GO:0010106]; lignin catabolic process [GO:0046274]; reductive iron assimilation [GO:0033215] | extracellular region [GO:0005576]; high-affinity iron permease complex [GO:0033573] | copper ion binding [GO:0005507]; ferroxidase activity [GO:0004322]; hydroquinone:oxygen oxidoreductase activity [GO:0052716] | PF00394;PF07732; | 2.60.40.420; | Multicopper oxidase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34467865}. | CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2; Evidence={ECO:0000269|PubMed:34467865}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=164.14 uM for ABTS (at pH 6.0 and 55 degrees Celsius) {ECO:0000269|PubMed:34467865}; KM=156.55 uM for ABTS (at 55 degrees Celsius in the presence of 5 mM NaCl) {ECO:0000269|PubMed:34467865}; KM=147.48 uM for ABTS (at 55 degrees Celsius in the presence of 10 mM NaCl) {ECO:0000269|PubMed:34467865}; KM=150.56 uM for ABTS (at 55 degrees Celsius in the presence of 15 mM NaCl) {ECO:0000269|PubMed:34467865}; KM=159.75 uM for ABTS (at 55 degrees Celsius in the presence of 20 mM NaCl) {ECO:0000269|PubMed:34467865}; KM=201.34 uM for ABTS (at 55 degrees Celsius in the presence of 25 mM NaCl) {ECO:0000269|PubMed:34467865}; KM=203.47 uM for ABTS (at 55 degrees Celsius in the presence of 30 mM NaCl) {ECO:0000269|PubMed:34467865}; KM=211.2 uM for ABTS (at 55 degrees Celsius in the presence of 50 mM NaCl) {ECO:0000269|PubMed:34467865}; KM=214.5 uM for ABTS (at 55 degrees Celsius in the presence of 70 mM NaCl) {ECO:0000269|PubMed:34467865}; KM=217.08 uM for ABTS (at 55 degrees Celsius in the presence of 90 mM NaCl) {ECO:0000269|PubMed:34467865}; KM=221.65 uM for ABTS (at 55 degrees Celsius in the presence of 0.1 M NaCl) {ECO:0000269|PubMed:34467865}; KM=226.07 uM for ABTS (at 55 degrees Celsius in the presence of 0.3 M NaCl) {ECO:0000269|PubMed:34467865}; KM=228.12 uM for ABTS (at 55 degrees Celsius in the presence of 0.5 M NaCl) {ECO:0000269|PubMed:34467865}; KM=236.04 uM for ABTS (at 55 degrees Celsius in the presence of 0.7 M NaCl) {ECO:0000269|PubMed:34467865}; KM=243.32 uM for ABTS (at 55 degrees Celsius in the presence of 0.9 M NaCl) {ECO:0000269|PubMed:34467865}; KM=249.91 uM for ABTS (at 55 degrees Celsius in the presence of 1 M NaCl) {ECO:0000269|PubMed:34467865}; KM=258.45 uM for ABTS (at 55 degrees Celsius in the presence of 3 M NaCl) {ECO:0000269|PubMed:34467865}; KM=269.54 uM for ABTS (at 55 degrees Celsius in the presence of 5 M NaCl) {ECO:0000269|PubMed:34467865}; KM=274.22 uM for ABTS (at 55 degrees Celsius in the presence of 7 M NaCl) {ECO:0000269|PubMed:34467865}; KM=282.78 uM for ABTS (at 55 degrees Celsius in the presence of 9 M NaCl) {ECO:0000269|PubMed:34467865}; KM=170.67 uM for catechol (at pH 6.0 and 55 degrees Celsius) {ECO:0000269|PubMed:34467865}; KM=188.98 uM for 2,6-dimethylphenol (at pH 6.0 and 55 degrees Celsius) {ECO:0000269|PubMed:34467865}; KM=183.45 uM for levodopa (at pH 6.0 and 55 degrees Celsius) {ECO:0000269|PubMed:34467865}; KM=195.65 uM for ferulic acid (at pH 6.0 and 55 degrees Celsius) {ECO:0000269|PubMed:34467865}; KM=169.04 uM for gallic acid (at pH 6.0 and 55 degrees Celsius) {ECO:0000269|PubMed:34467865}; KM=172.91 uM for guaiacol (at pH 6.0 and 55 degrees Celsius) {ECO:0000269|PubMed:34467865}; KM=165.79 uM for hydroquinone (at pH 6.0 and 55 degrees Celsius) {ECO:0000269|PubMed:34467865}; KM=168.45 uM for phenol (at pH 6.0 and 55 degrees Celsius) {ECO:0000269|PubMed:34467865}; KM=192.07 uM for tyrosine (at pH 6.0 and 55 degrees Celsius) {ECO:0000269|PubMed:34467865}; KM=206.43 uM for veratryl alcohol (at pH 6.0 and 55 degrees Celsius) {ECO:0000269|PubMed:34467865}; Note=kcat is 273 sec(-1) for ABTS oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat is 259 sec(-1) for catechol oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat is 237 sec(-1) for 2,6-dimethylphenol oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat is 244 sec(-1) for levodopa oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat is 217 sec(-1) for ferulic acid oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat is 262 sec(-1) for gallic acid oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat is 256 sec(-1) for guaiacol oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat is 270 sec(-1) for hydroquinone oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat is 264 sec(-1) for phenol oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat is 220 sec(-1) for tyrosine oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat is 201 sec(-1) for veratryl alcohol oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat is 282 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 5 mM NaCl) (PubMed:34467865). kcat is 294 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 10 mM NaCl) (PubMed:34467865). kcat is 289 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 15 mM NaCl) (PubMed:34467865). kcat is 279 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 20 mM NaCl) (PubMed:34467865). kcat is 235 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 25 mM NaCl) (PubMed:34467865). kcat is 233 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 30 mM NaCl) (PubMed:34467865). kcat is 226 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 50 mM NaCl) (PubMed:34467865). kcat is 222 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 70 mM NaCl) (PubMed:34467865). kcat is 218 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 90 mM NaCl) (PubMed:34467865). kcat is 215 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 0.1 M NaCl) (PubMed:34467865). kcat is 209 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 0.3 M NaCl) (PubMed:34467865). kcat is 207 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 0.5 M NaCl) (PubMed:34467865). kcat is 201 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 0.7 M NaCl) (PubMed:34467865). kcat is 197 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 0.9 M NaCl) (PubMed:34467865). kcat is 194 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 1 M NaCl) (PubMed:34467865). kcat is 185 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 3 M NaCl) (PubMed:34467865). kcat is 176 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 5 M NaCl) (PubMed:34467865). kcat is 161 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 7 M NaCl) (PubMed:34467865). kcat is 152 sec(-1) for ABTS oxidation (at 55 degrees Celsius in the presence of 9 M NaCl) (PubMed:34467865). {ECO:0000269|PubMed:34467865}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 (PubMed:34467865). Retains over 72 percent activity in the pH range 5 to 8 (PubMed:34467865). Retains activity above 89% after incubation at pH 6 for 72 hours (PubMed:34467865). Retains activity above 61% after incubation at pH 5-8 for 72 hours (PubMed:34467865). {ECO:0000269|PubMed:34467865}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius (PubMed:34467865). Thermostable (PubMed:34467865). Retains over 84 percent activity when incubated for 3 hours at temperatures between 10-60 degrees Celsius (PubMed:34467865). {ECO:0000269|PubMed:34467865}; | FUNCTION: Lignin degradation and detoxification of lignin-derived products (By similarity). Multicopper oxidase that catalyzes the oxidation of a variety of substrates, including phenolic and non-phenolic compounds (PubMed:34467865). Has highest activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), also active towards hydroquinone, phenol, gallic acid, catechol, guaiacol, levodopa, 2,6-dimethoxyphenol (2,6-DMP), tyrosine, ferulic acid and veratryl alcohol (PubMed:34467865). {ECO:0000250|UniProtKB:D0VWU3, ECO:0000269|PubMed:34467865}. | Ganoderma australe (Bracket fungus) (Polyporus australis) |
C0HLX7 | GLEC_CHOCI | TYAEVESFGVGQSATAVYTAPGDGRDLNITIDADGGYVIHMDYRFDWGGNPSTGKPWEDILILNSKPAQTWGPQQHVNNFYFTPGTHVTLGDKSNDGHFAIIADGIQVATYDHRLPVNSVKEVKFSTTAGSGTDIWDLLLLP | null | null | aggregation of unicellular organisms [GO:0098630]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; defense response to protozoan [GO:0042832] | null | galactose binding [GO:0005534]; protein homodimerization activity [GO:0042803] | PF00337; | 2.60.120.200; | null | null | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH for hemagglutination activity is 9. {ECO:0000269|PubMed:29175164}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable at high temperatures. {ECO:0000269|PubMed:29175164}; | FUNCTION: Galactose-binding lectin (PubMed:29175164, PubMed:34508835). Displays antibacterial and hemagglutinin activity (PubMed:29175164, PubMed:34508835). Inhibits the growth of L.infantum promastigotes by damaging their membrane integrity and inducing cell apoptosis via the production of reactive oxygen species (ROS) (PubMed:34508835). Inhibition of L.infantum promastigotes appears to increase with time (MIC=1.2 uM/ml after 24 hours, MIC=0.9 uM/ml after 48 hours and MIC=0.6 uM/ml after 72 hours) (PubMed:34508835). Agglutinates Gram-negative and Gram-positive bacteria including E.coli, S.aureus and S.epidermidis, and inhibits biofilm formation by S.aureus and S.epidermidis (PubMed:29175164). Displays hemagglutination activity towards all types of human erythrocytes (O, A and B) and rabbit erythrocytes (PubMed:29175164). {ECO:0000269|PubMed:29175164, ECO:0000269|PubMed:34508835}. | Chondrilla caribensis (Chicken liver sponge) |
C0HLZ9 | BARA1_DROME | MKSFGLIALAICGVICVAAEPQHTYDGRNGPHVFGSPGNQVYIRGQNEGTYSVPGVGGQFQNAPQRGEHVYTDEAGNTFVNRKNAGGPASHTISGPNFSAKNLGPNGAKSVGIPQRARRSPQFHVERPGRTVDVGNGGFYIQRGRRSPQLHVARPDRTVTIGNGGVYIQRSRRSPQFHVERPDRTVDFGNGGFSAQRFRRGINDARVQGENFVARDDQAGIWDNNVSVWKRPDGRTVTIDRNGHTIVSGRGRPAQHY | null | null | antifungal innate immune response [GO:0061760]; killing of cells of another organism [GO:0031640]; response to Gram-positive bacterium [GO:0140459]; response to toxic substance [GO:0009636] | extracellular space [GO:0005615] | null | null | null | null | PTM: Proteolytically cleaved. {ECO:0000269|PubMed:34432851, ECO:0000269|PubMed:9736738}. | SUBCELLULAR LOCATION: [Immune-induced peptide 24]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 6]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 12]: Secreted {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 10]: Secreted {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851, ECO:0000269|PubMed:9736738}.; SUBCELLULAR LOCATION: [Immune-induced peptide 5]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 8]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 13]: Secreted {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851, ECO:0000269|Ref.7}.; SUBCELLULAR LOCATION: [Immune-induced peptide 22]: Secreted {ECO:0000269|PubMed:34432851}. | null | null | null | null | null | FUNCTION: Secreted immune-induced peptides induced by Toll signaling (PubMed:34432851, PubMed:9736738). Has a significant role in resistance to infection by the entomopathogenic fungus B.bassiana R444 and weak antifungal activity against M.rileyi PHP1705 (PubMed:34432851). In adult males, activity appears to be important for neuromuscular processes that mediate correct wing posture upon Toll activation (PubMed:34432851). {ECO:0000269|PubMed:34432851, ECO:0000269|PubMed:9736738}. | Drosophila melanogaster (Fruit fly) |
C0HM00 | BARA2_DROME | MKSFGLIALAICGVICVAAEPQHTYDGRNGPHVFGSPGNQVYIRGQNEGTYSVPGVGGQFQNAPQRGEHVYTDEAGNTFVNRKNAGGPASHTISGPNFSAKNLGPNGAKSVGIPQRARRSPQFHVERPGRTVDVGNGGFYIQRGRRSPQLHVARPDRTVTIGNGGVYIQRSRRSPQFHVERPDRTVDFGNGGFSAQRFRRGINDARVQGENFVARDDQAGIWDNNVSVWKRPDGRTVTIDRNGHTIVSGRGRPAQHY | null | null | antifungal innate immune response [GO:0061760]; defense response [GO:0006952]; humoral immune response [GO:0006959]; killing of cells of another organism [GO:0031640]; response to bacterium [GO:0009617] | extracellular space [GO:0005615] | null | null | null | null | PTM: Proteolytically cleaved. {ECO:0000269|PubMed:34432851, ECO:0000269|PubMed:9736738}. | SUBCELLULAR LOCATION: [Immune-induced peptide 24]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 6]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 12]: Secreted {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 10]: Secreted {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851, ECO:0000269|PubMed:9736738}.; SUBCELLULAR LOCATION: [Immune-induced peptide 5]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 8]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 13]: Secreted {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851, ECO:0000269|Ref.6}.; SUBCELLULAR LOCATION: [Immune-induced peptide 22]: Secreted {ECO:0000269|PubMed:34432851}. | null | null | null | null | null | FUNCTION: Secreted immune-induced peptides induced by Toll signaling (PubMed:34432851, PubMed:9736738). Has a significant role in resistance to infection by the entomopathogenic fungus B.bassiana R444 and weak antifungal activity against M.rileyi PHP1705 (PubMed:34432851). In adult males, activity appears to be important for neuromuscular processes that mediate correct wing posture upon Toll activation (PubMed:34432851). {ECO:0000269|PubMed:34432851, ECO:0000269|PubMed:9736738}. | Drosophila melanogaster (Fruit fly) |
C0HM14 | PA2BD_CRODU | HLLQFNKMIKFETRKNAIPFYAFYGCYCGWGGRGRPKDATDRCCFVHDCCYGKLAKCNTKWDIYRYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSLSTYKYGYMFYPDSRCRGPSETC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P62022}; Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P62022}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; ion channel regulator activity [GO:0099106]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3753003, ECO:0000269|PubMed:8033889}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036, ECO:0000269|PubMed:8513799}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.06 uM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (monomer CBd) {ECO:0000269|PubMed:8513799}; KM=0.35 uM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (class 1 heterodimer CA2-CBd) {ECO:0000269|PubMed:8513799}; KM=0.3 uM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (class 1 heterodimer CA3-CBd) {ECO:0000269|PubMed:8513799}; Vmax=19.7 umol/min/mg enzyme (monomer CBd) {ECO:0000269|PubMed:8513799}; Vmax=4.6 umol/min/mg enzyme (class 1 heterodimer CA2-CBd) {ECO:0000269|PubMed:8513799}; Vmax=4 umol/min/mg enzyme (class 1 heterodimer CA3-CBd) {ECO:0000269|PubMed:8513799}; | null | null | null | FUNCTION: Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission (PubMed:8513799). It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non-enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4) (PubMed:8513799). The complex acts by binding to a specific 48-kDa protein (R48) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit (PubMed:12657321). At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor (PubMed:12657321). In addition to neurotoxicity, crotoxin has been found to exert myotoxicity, nephrotoxicity, and cardiovascular toxicity (By similarity). Moreover, anti-inflammatory, immunomodulatory, anti-tumor and analgesic effects of crotoxin have also been reported (By similarity). {ECO:0000250|UniProtKB:P62022, ECO:0000269|PubMed:12657321, ECO:0000269|PubMed:8513799}.; FUNCTION: Monomer CBd: The basic subunit of crotoxin is a snake venom phospholipase A2 (PLA2) that exhibits weak neurotoxicity (10-fold less than the heterodimer) and very strong anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (By similarity). In addition, it shows the same effects described for the heterodimer and binds the nucleotide-binding domain (NBD1) of CFTR chloride channels and increases the channel current (By similarity). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:8513799). {ECO:0000250|UniProtKB:P62022, ECO:0000269|PubMed:8513799}. | Crotalus durissus terrificus (South American rattlesnake) |
C0HM45 | LEC_NARPS | DNILYSGETLSPGEFLNNGRYVFIMQEDCNLVLYDVDKPIWATNTGGLDRRCHLSMQSDGNLVVYSPRNNPIWASNTGGENGNYVCVLQKDRNVVIYGTARWATGTNIH | null | null | defense response to virus [GO:0051607]; regulation of defense response to virus [GO:0050688]; response to virus [GO:0009615] | extracellular space [GO:0005615] | mannose binding [GO:0005537]; protein homodimerization activity [GO:0042803] | null | 2.90.10.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10388566}. | null | null | null | null | null | FUNCTION: D-mannose-binding lectin which binds alpha-D-linked mannose (PubMed:10388566, PubMed:14505313, PubMed:1645507, PubMed:1874921, PubMed:2350177). Displays a high affinity for alpha-(1-6)-mannose oligomers (PubMed:1645507, PubMed:2350177). Able to interact with both terminal and internal alpha-D-mannosyl residues (PubMed:2350177). Displays antiviral activity and therefore may contribute to defense against infections (PubMed:1645507, PubMed:7481093). {ECO:0000269|PubMed:10388566, ECO:0000269|PubMed:14505313, ECO:0000269|PubMed:1645507, ECO:0000269|PubMed:1874921, ECO:0000269|PubMed:2350177, ECO:0000269|PubMed:7481093}. | Narcissus pseudonarcissus (Daffodil) |
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