ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q1Q0T3 | MAREMRLGGKERMKTGVVKIGLVAALGVVGLISAGGVYAGQPRVISTIQTGATWEPLGREEPLTVPEVHFRVKHSPFKSELVRYGQFQFNDAAWSLQGSYSCASCHYERGQTTGLIWDLGDEGWGSWKNTKYIRGGRYLPPFRHEGFTGHPDEIVGATSSLDRVCGRDPGFVFRSENFSPMRLEALICYIRALEFTGSPFRNADGSLTEAQKRGQKIFEDPKVGCLECHPGDPMDPRALFSDAQTHDVGTGRVGVNGFRSTPGKVFNISALEAGEDPYGVESNTPIIGLDLVKEFDTPTLRDIYASGTYFHDGGARTLMDTINNTVNDKDMHGRTSHLKQQELQDLVEYLKAL | Cofactor: Binds two heme c groups per subunit. Heme 1 appears to be in the active site, whereas heme 2 probably functions in electron transfer.
Function: Component of the hydrazine synthase complex that catalyzes the condensation of nitric oxide (NO) with ammonium to form hydrazine . The gamma subunit catalyzes the first half-reaction, i.e. the three-electron reduction of nitric oxide to hydroxylamine; it may obtain electrons from the triheme cytochrome c kuste2854 . Is involved in anaerobic ammonium oxidation (anammox), a biological process in which nitrite is used as the electron acceptor in the conversion of ammonium to dinitrogen gas (N2) and water; this bacterial process has a major role in the Earth's nitrogen cycle and has been estimated to synthesize up to 50% of the dinitrogen gas emitted into our atmosphere from the oceans .
Catalytic Activity: 3 Fe(III)-[cytochrome c] + H2O + hydrazine = 3 Fe(II)-[cytochrome c] + 2 H(+) + NH4(+) + nitric oxide
Sequence Mass (Da): 38925
Sequence Length: 353
Domain: Consists of two alpha-helical lobes, each of which contains one c-type heme.
Pathway: Nitrogen metabolism.
Subcellular Location: Anammoxosome
EC: 1.7.2.7
|
Q13651 | MLPCLVVLLAALLSLRLGSDAHGTELPSPPSVWFEAEFFHHILHWTPIPNQSESTCYEVALLRYGIESWNSISNCSQTLSYDLTAVTLDLYHSNGYRARVRAVDGSRHSNWTVTNTRFSVDEVTLTVGSVNLEIHNGFILGKIQLPRPKMAPANDTYESIFSHFREYEIAIRKVPGNFTFTHKKVKHENFSLLTSGEVGEFCVQVKPSVASRSNKGMWSKEECISLTRQYFTVTNVIIFFAFVLLLSGALAYCLALQLYVRRRKKLPSVLLFKKPSPFIFISQRPSPETQDTIHPLDEEAFLKVSPELKNLDLHGSTDSGFGSTKPSLQTEEPQFLLPDPHPQADRTLGNREPPVLGDSCSSGSSNSTDSGICLQEPSLSPSTGPTWEQQVGSNSRGQDDSGIDLVQNSEGRAGDTQGGSALGHHSPPEPEVPGEEDPAAVAFQGYLRQTRCAEEKATKTGCLEEESPLTDGLGPKFGRCLVDEAGLHPPALAKGYLKQDPLEMTLASSGAPTGQWNQPTEEWSLLALSSCSDLGISDWSFAHDLAPLGCVAAPGGLLGSFNSDLVTLPLISSLQSSE | Function: Cell surface receptor for the cytokine IL10 that participates in IL10-mediated anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Upon binding to IL10, induces a conformational change in IL10RB, allowing IL10RB to bind IL10 as well . In turn, the heterotetrameric assembly complex, composed of two subunits of IL10RA and IL10RB, activates the kinases JAK1 and TYK2 that are constitutively associated with IL10RA and IL10RB respectively . These kinases then phosphorylate specific tyrosine residues in the intracellular domain in IL10RA leading to the recruitment and subsequent phosphorylation of STAT3. Once phosphorylated, STAT3 homodimerizes, translocates to the nucleus and activates the expression of anti-inflammatory genes. In addition, IL10RA-mediated activation of STAT3 inhibits starvation-induced autophagy .
PTM: Phosphorylated. Phosphorylation of the cytoplasmic tail induced STAT3 activation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 63003
Sequence Length: 578
Subcellular Location: Cell membrane
|
Q08334 | MAWSLGSWLGGCLLVSALGMVPPPENVRMNSVNFKNILQWESPAFAKGNLTFTAQYLSYRIFQDKCMNTTLTECDFSSLSKYGDHTLRVRAEFADEHSDWVNITFCPVDDTIIGPPGMQVEVLADSLHMRFLAPKIENEYETWTMKNVYNSWTYNVQYWKNGTDEKFQITPQYDFEVLRNLEPWTTYCVQVRGFLPDRNKAGEWSEPVCEQTTHDETVPSWMVAVILMASVFMVCLALLGCFALLWCVYKKTKYAFSPRNSLPQHLKEFLGHPHHNTLLFFSFPLSDENDVFDKLSVIAEDSESGKQNPGDSCSLGTPPGQGPQS | Function: Shared cell surface receptor required for the activation of five class 2 cytokines: IL10, IL22, IL26, IL28, and IFNL1. The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 36995
Sequence Length: 325
Subcellular Location: Membrane
|
Q14626 | MSSSCSGLSRVLVAVATALVSASSPCPQAWGPPGVQYGQPGRSVKLCCPGVTAGDPVSWFRDGEPKLLQGPDSGLGHELVLAQADSTDEGTYICQTLDGALGGTVTLQLGYPPARPVVSCQAADYENFSCTWSPSQISGLPTRYLTSYRKKTVLGADSQRRSPSTGPWPCPQDPLGAARCVVHGAEFWSQYRINVTEVNPLGASTRLLDVSLQSILRPDPPQGLRVESVPGYPRRLRASWTYPASWPCQPHFLLKFRLQYRPAQHPAWSTVEPAGLEEVITDAVAGLPHAVRVSARDFLDAGTWSTWSPEAWGTPSTGTIPKEIPAWGQLHTQPEVEPQVDSPAPPRPSLQPHPRLLDHRDSVEQVAVLASLGILSFLGLVAGALALGLWLRLRRGGKDGSPKPGFLASVIPVDRRPGAPNL | Function: Receptor for interleukin-11 (IL11). The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex may be involved in the control of proliferation and/or differentiation of skeletogenic progenitor or other mesenchymal cells (Probable). Essential for the normal development of craniofacial bones and teeth. Restricts suture fusion and tooth number.
PTM: A short soluble form is also released from the membrane by proteolysis . The sIL11RA is formed either by limited proteolysis of membrane-bound receptors, a process referred to as ectodomain shedding, or directly secreted from the cells after alternative mRNA splicing . mIL11RA is cleaved by the proteases ADAM10, ELANE and PRTN3 .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 45222
Sequence Length: 422
Subcellular Location: Membrane
|
Q64385 | MSSSCSGLTRVLVAVATALVSSSSPCPQAWGPPGVQYGQPGRPVMLCCPGVSAGTPVSWFRDGDSRLLQGPDSGLGHRLVLAQVDSPDEGTYVCQTLDGVSGGMVTLKLGFPPARPEVSCQAVDYENFSCTWSPGQVSGLPTRYLTSYRKKTLPGAESQRESPSTGPWPCPQDPLEASRCVVHGAEFWSEYRINVTEVNPLGASTCLLDVRLQSILRPDPPQGLRVESVPGYPRRLHASWTYPASWRRQPHFLLKFRLQYRPAQHPAWSTVEPIGLEEVITDAVAGLPHAVRVSARDFLDAGTWSAWSPEAWGTPSTGPLQDEIPDWSQGHGQQLEAVVAQEDSPAPARPSLQPDPRPLDHRDPLEQVAVLASLGIFSCLGLAVGALALGLWLRLRRSGKDGPQKPGLLAPMIPVEKLPGIPNLQRTPENFS | Function: Receptor for interleukin-11. The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex may be involved in the control of proliferation and/or differentiation of skeletogenic progenitor or other mesenchymal cells. Essential for the normal development of craniofacial bones and teeth.
PTM: A short soluble form is also released from the membrane by proteolysis . The sIL11RA is formed either by limited proteolysis of membrane-bound receptors, a process referred to as ectodomain shedding, or directly secreted from the cells after alternative mRNA splicing . mIL11RA is cleaved by the proteases ADAM10, ELANE and PRTN3 .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 46655
Sequence Length: 432
Subcellular Location: Membrane
|
Q5RF19 | MSSSCSGLSRVLVAVATALVSASSPCPQAWGPPGVQYGQPGRSVKLCCPGVTAGDPVSWFRDGEPKLLQGPDSGLGHELVLAQADSTDEGTYICRTLDGALGGTVTLQLGYPPARPVVSCQAADYENFSCTWSPSQISGLPTRYLTSYRKKTVLGADSQRRSPSTGPWPCPQDPLGAARCVVHGAEFWSQYRINVTEVNPLGASTRLLDVSLQSILRPDPPQGLRVESVPGYPRRLRASWTYPASWPRQPHFLLKFRLQYRPAQHPAWSTVEPAGLEEVITDAVAGLPHAVRVSARDFLDAGTWSTWSPEAWGTPSTGTVPKEIPAWGQLHTQPEVEPQVDSPAPPRPSLQPHPRLLDHRDSVEQVAVLVSLGILSFLGLVAGALALGLWLRLRRGGKDGSPKPGFLASVIPVDRHPGAPNL | Function: Receptor for interleukin-11 (IL11). The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex may be involved in the control of proliferation and/or differentiation of skeletogenic progenitor or other mesenchymal cells. Essential for the normal development of craniofacial bones and teeth. Restricts suture fusion and tooth number.
PTM: A short soluble form is also released from the membrane by proteolysis. The sIL11RA is formed either by limited proteolysis of membrane-bound receptors, a process referred to as ectodomain shedding, or directly secreted from the cells after alternative mRNA splicing. mIL11RA is cleaved by the proteases ADAM10, ELANE and PRTN3.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 45298
Sequence Length: 422
Subcellular Location: Membrane
|
P42701 | MEPLVTWVVPLLFLFLLSRQGAACRTSECCFQDPPYPDADSGSASGPRDLRCYRISSDRYECSWQYEGPTAGVSHFLRCCLSSGRCCYFAAGSATRLQFSDQAGVSVLYTVTLWVESWARNQTEKSPEVTLQLYNSVKYEPPLGDIKVSKLAGQLRMEWETPDNQVGAEVQFRHRTPSSPWKLGDCGPQDDDTESCLCPLEMNVAQEFQLRRRQLGSQGSSWSKWSSPVCVPPENPPQPQVRFSVEQLGQDGRRRLTLKEQPTQLELPEGCQGLAPGTEVTYRLQLHMLSCPCKAKATRTLHLGKMPYLSGAAYNVAVISSNQFGPGLNQTWHIPADTHTEPVALNISVGTNGTTMYWPARAQSMTYCIEWQPVGQDGGLATCSLTAPQDPDPAGMATYSWSRESGAMGQEKCYYITIFASAHPEKLTLWSTVLSTYHFGGNASAAGTPHHVSVKNHSLDSVSVDWAPSLLSTCPGVLKEYVVRCRDEDSKQVSEHPVQPTETQVTLSGLRAGVAYTVQVRADTAWLRGVWSQPQRFSIEVQVSDWLIFFASLGSFLSILLVGVLGYLGLNRAARHLCPPLPTPCASSAIEFPGGKETWQWINPVDFQEEASLQEALVVEMSWDKGERTEPLEKTELPEGAPELALDTELSLEDGDRCKAKM | Function: Functions as an interleukin receptor which binds interleukin-12 with low affinity and is involved in IL12 transduction. Associated with IL12RB2 it forms a functional, high affinity receptor for IL12. Associates also with IL23R to form the interleukin-23 receptor which functions in IL23 signal transduction probably through activation of the Jak-Stat signaling cascade.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 73109
Sequence Length: 662
Domain: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
Subcellular Location: Membrane
|
Q60837 | MDMMGLAGTSKHITFLLLCQLGASGPGDGCCVEKTSFPEGASGSPLGPRNLSCYRVSKTDYECSWQYDGPEDNVSHVLWCCFVPPNHTHTGQERCRYFSSGPDRTVQFWEQDGIPVLSKVNFWVESRLGNRTMKSQKISQYLYNWTKTTPPLGHIKVSQSHRQLRMDWNVSEEAGAEVQFRRRMPTTNWTLGDCGPQVNSGSGVLGDIRGSMSESCLCPSENMAQEIQIRRRRRLSSGAPGGPWSDWSMPVCVPPEVLPQAKIKFLVEPLNQGGRRRLTMQGQSPQLAVPEGCRGRPGAQVKKHLVLVRMLSCRCQAQTSKTVPLGKKLNLSGATYDLNVLAKTRFGRSTIQKWHLPAQELTETRALNVSVGGNMTSMQWAAQAPGTTYCLEWQPWFQHRNHTHCTLIVPEEEDPAKMVTHSWSSKPTLEQEECYRITVFASKNPKNPMLWATVLSSYYFGGNASRAGTPRHVSVRNQTGDSVSVEWTASQLSTCPGVLTQYVVRCEAEDGAWESEWLVPPTKTQVTLDGLRSRVMYKVQVRADTARLPGAWSHPQRFSFEVQISRLSIIFASLGSFASVLLVGSLGYIGLNRAAWHLCPPLPTPCGSTAVEFPGSQGKQAWQWCNPEDFPEVLYPRDALVVEMPGDRGDGTESPQAAPECALDTRRPLETQRQRQVQALSEARRLGLAREDCPRGDLAHVTLPLLLGGVTQGASVLDDLWRTHKTAEPGPPTLGQEA | Function: Functions as an interleukin receptor which binds interleukin-12 with low affinity and is involved in IL12 transduction. Associated with IL12RB2 it forms a functional, high affinity receptor for IL12. Associates also with IL23R to form the interleukin-23 receptor which functions in IL23 signal transduction probably through activation of the Jak-Stat signaling cascade.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 81788
Sequence Length: 738
Domain: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
Subcellular Location: Membrane
|
Q5P5Z3 | MKRRTVLSMEQALSMPYATLRFAQLGWRVIRLESTPSRGGLPGDPNRYIGANVVDDDRRTYFIAPNVGKEAIAINLKEPDGQALLRRLLVELDVDVFCCNTVPRRYEQLGIDYETLSRTKPDLIWAGISAMGPDYPDAPGYDPVLQAMAGYMELTGDADGPPTLAGVPIVDLKAGDEVFANVMLALLERAETGKGSRIDVSMLQAAASWLITTLPLLDFDCQPAEITRCGNAHRKFIPTNVYPTADGFIYMAIGSDVQWRRLTEIPKFASLGAAPRATNEGRHKERDAIHRDMAAVTTRFATAEIAADFRDATIPHAPIHDIPAVRDMEAVRRRLTTTRTPDGRLVHMQPMAVDVAGASGELAFPAKYGQDTCAVLREAGYADEAIAQLRERGIVAG | Function: Involved in degradation of indoleacetate, the most common member of the auxin class of plant hormones . CoA-transferase that catalyzes the succinyl-CoA-dependent activation of phenylsuccinate to phenylsuccinyl-CoA . Acts as a rather unspecific CoA-transferase that shows a broad substrate specificity for C4-dicarboxylic acids, including succinate, (R/S)-phenylsuccinate, (S)- and (R)-benzylsuccinate and their CoA-thioesters, indicating a fully reversible catalytic process . It can also use indole-3-acetate and 2-oxindole-3-acetate, and it also appears to mediate the intramolecular CoA-transfer between the two phenylsuccinyl-CoA regioisomers . Cannot use acetyl-CoA as CoA donor . In vivo, probably catalyzes the isomerization of 3'-(2-aminophenyl)succinyl-CoA to the other regioisomer, 2'-(2-aminophenyl)succinyl-CoA .
Catalytic Activity: phenylsuccinate + succinyl-CoA = 2-phenylsuccinyl-CoA + succinate
Sequence Mass (Da): 43480
Sequence Length: 397
EC: 2.8.3.28
|
P18204 | MTAYDMEKEWSRISITAAKIHQNNDFEGFTYQDFRTHVPIMDKDGFAAQTERCLERNERNCLIGFTSGTSGNIKRCYYYYDCEVDEDSSLSNVFRSNGFILPGDRCANLFTINLFSALNNTITMMAGNCGAHVVSVGDITLVTKSHFEALNSIKLNVLLGVPSTILQFINAMQHNGVHINIEKVVFTGESLKTFQKKIIRQAFGEQVSIVGVYGSSEGGILGFTNSPCHTEYEFLSDKYFIEKEGDSILITSLTRENFTPLLRYRLGDTATLSMKGDKLYLTDIQREDMSFNFMGNLIGLGIIQQTIKQTLGRSLEIQVHLSVTEERKELVTVFVQASEVDEDERVRIETAIADIPDIKEAYQKNQGTVSVLRKDARDYAVSERGKMLYIIDRRN | Function: Conversion of IAA to IAA-lysine.
Catalytic Activity: (indol-3-yl)acetate + ATP + L-lysine = ADP + H(+) + N(6)-[(indole-3-yl)acetyl]-L-lysine + phosphate
Sequence Mass (Da): 44624
Sequence Length: 395
EC: 6.3.2.20
|
P16969 | MASDHRRFVLSGAVLLSVLAVAAATLESVKDECQLGVDFPHNPLATCHTYVIKRVCGRGPSRPMLVKERCCRELAAVPDHCRCEALRILMDGVRTPEGRVVEGRLGDRRDCPREEQRAFAATLVTAAECNLSSVQAPGVRLVLLADG | Function: Alpha-amylase/trypsin inhibitor.
PTM: Five disulfide bonds, which are essential for the inhibitor activity, are probably present.
Sequence Mass (Da): 15965
Sequence Length: 147
Subcellular Location: Secreted
|
P83048 | SEDCTPWTATPITVLAGCRDYVGEQ | Function: Inhibits alpha-amylases but not trypsin. Is more effective against insect alpha-amylases than those of mammals.
PTM: May exist both in a glycosylated and in an unglycosylated form.
Sequence Mass (Da): 2713
Sequence Length: 25
Subcellular Location: Secreted
|
P94531 | MKKARMIVDKEYKIGEVDKRIYGSFIEHMGRAVYEGIYEPDHPEADEDGFRKDVQSLIKELQVPIIRYPGGNFLSGYNWEDGVGPVENRPRRLDLAWQTTETNEVGTNEFLSWAKKVNTEVNMAVNLGTRGIDAARNLVEYCNHPKGSYWSDLRRSHGYEQPYGIKTWCLGNEMDGPWQIGHKTADEYGRLAAETAKVMKWVDPSIELVACGSSNSGMPTFIDWEAKVLEHTYEHVDYISLHTYYGNRDNNLPNYLARSMDLDHFIKSVAATCDYVKAKTRSKKTINLSLDEWNVWYHSNEADKKVEPWITARPILEDIYNFEDALLVGSLLITMLQHADRVKIACLAQLVNVIAPIMTEKGGEAWRQPIFYPYMHASVYGRGESLKPLISSPKYDCSDFTDVPYVDAAVVYSEEEETLTIFAVNKAEDQMETEISLRGFESYQIAEHIVLEHQDIKATNQHNRKNVVPHSNGSSSVSENGLTAHFTPLSWNVIRLKKQS | Function: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-(1->5)-arabinofuranosyl bonds in different hemicellulosic homopolysaccharides (branched and debranched arabinans). It acts preferentially on arabinotriose, arabinobiose and linear alpha-(1->5)-L-arabinan, and is much less effective on branched sugar beet arabinan.
Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
Sequence Mass (Da): 57034
Sequence Length: 500
Pathway: Glycan metabolism; L-arabinan degradation.
Subcellular Location: Cytoplasm
EC: 3.2.1.55
|
P94552 | MSEHQAVIQTDIAKGTINKNIYGHFAEHLGRGIYEGIWVGTDSDIPNINGIRKDVLEALKQLHIPVLRWPGGCFADEYHWANGVGDRKTMLNTHWGGTIESNEFGTHEFMMLCELLECEPYICGNVGSGTVQEMSEWIEYMTFEEGTPMSDWRKQNGREEPWKLKYFGVGNENWGCGGNMHPEYYADLYRRFQTYVRNYSGNDIYKIAGGANVDDFNWTDVLMKKAAGLMDGLSLHYYTIPGDFWKGKGSATEFTEDEWFITMKKAKYIDELIQKHGTIMDRYDPEQRVGLIIDEWGTWFDPEPGTNPGFLYQQNTIRDALVAASHFHIFHQHCRRVQMANIAQTVNVLQAMILTEGERMLLTPTYHVFNMFKVHQDASLLATETMSADYEWNGETLPQISISASKQAEGDINITICNIDHQNKAEAEIELRGLHKAADHSGVILTAEKMNAHNTFDDPHHVKPESFRQYTLSKNKLKVKLPPMSVVLLTLRADS | Function: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-L-arabinofuranosyl residues in different hemicellulosic homopolysaccharides (branched and debranched arabinans) and heteropolysaccharides (arabinoxylans). It is able to hydrolyze the alpha-(1->5)-glycosidic linkages of linear alpha-(1->5)-L-arabinan (debranched), sugar beet arabinan (branched) and wheat arabinoxylan. Moreover, it displays higher activity towards branched arabinan, a molecule comprising a backbone of alpha-(1->5)-linked L-arabinofuranosyl residues decorated with alpha-(1->2)-, and alpha-(1->3)-linked L-arabinofuranosyl units, than towards debranched arabinan. In addition, arabinoxylan, which has L-arabinofuranose residues attached to the main chain by alpha-(1->2)- and/or alpha-(1->3)-glycosidic linkages, is preferred to linear alpha-(1->5)-L-arabinan.
Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
Sequence Mass (Da): 56475
Sequence Length: 495
Pathway: Glycan metabolism; L-arabinan degradation.
Subcellular Location: Cytoplasm
EC: 3.2.1.55
|
Q59219 | MKAKLLVSTAFLAASVSLSAQKSATITVHADQGKEIIPKEIYGQFAEHLGSCIYGGLWVGENSDIPNIKGYRTDVFNALKDLSVPVLRWPGGCFADEYHWMDGIGPKENRPKMVNNNWGGTIEDNSFGTHEFLNLCEMLGCEPYVSGNVGSGTVEELAKWVEYMTSDGDSPMANLRRKNGRDKAWKLKYLGVGNESWGCGGSMRPEYYADLYRRYSTYCRNYDGNRLFKIASGASDYDYKWTDVLMNRVGHRMDGLSLHYYTVTGWSGSKGSATQFNKDDYYWTMGKCLEVEDVLKKHCTIMDKYDKDKKIALLLDEWGTWWDEEPGTIKGHLYQQNTLRDAFVASLSLDVFHKYTDRLKMANIAQIVNVLQSMILTKDKEMVLTPTYYVFKMYKVHQDATYLPIDLTCEKMSVRDNRTVPMVSATASKNKDGVIHISLSNVDADEAQEITINLGDTKAKKAIGEILTASKLTDYNSFEKPNIVKPAPFKEVKINKGTMKVKLPAKSIVTLELQ | Function: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-L-arabinofuranosyl residues in different hemicellulosic homopolysaccharides (branched and debranched arabinans) and heteropolysaccharides (arabinoxylans) (By similarity).
Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
Sequence Mass (Da): 57979
Sequence Length: 514
Pathway: Glycan metabolism; L-arabinan degradation.
Subcellular Location: Cytoplasm
EC: 3.2.1.55
|
Q841V6 | MTTHNSQYSAETTHPDKQESSPAPTAAGTTASNVSTTGNATTPDASIALNADATPVADVPPRLFGSFVEHLGRCVYGGIYEPSHPTADENGFRQDVLDLVKELGVTCVRYPGGNFVSNYNWEDGIGPRENRPMRRDLAWHCTETNEMGIDDFYRWSQKAGTEIMLAVNMGTRGLKAALDELEYVNGAPGTAWADQRVANGIEEPMDIKMWCIGNEMDGPWQVGHMSPEEYAGAVDKVAHAMKLAESGLELVACGSSGAYMPTFGTWEKTVLTKAYENLDFVSCHAYYFDRGHKTRAAASMQDFLASSEDMTKFIATVSDAADQAREANNGTKDIALSFDEWGVWYSDKWNEQEDQWKAEAAQGLHHEPWPKSPHLLEDIYTAADAVVEGSLMITLLKHCDRVRSASRAQLVNVIAPIMAEEHGPAWRQTTFYPFAEAALHARGQAYAPAISSPTIHTEAYGDVPAIDAVVTWDEQARTGLLLAVNRDANTPHTLTIDLSGLPGLPGLGTLALGKAQLLHEDDPYRTNTAEAPEAVTPQPLDIAMNATGTCTATLPAISWISVEFHG | Function: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-(1->5)-arabinofuranosyl bonds in different hemicellulosic homopolysaccharides (branched and debranched arabinans). It is active with sugar beet arabinan and wheat arabinoxylan. It also exhibited activity against alpha-(1->5)-linked arabinobiose, arabinotriose, arabinotetraose, and arabinopentaose.
Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
Sequence Mass (Da): 61548
Sequence Length: 566
Pathway: Glycan metabolism; L-arabinan degradation.
Subcellular Location: Cytoplasm
EC: 3.2.1.55
|
H7FWB6 | MKILKRIPVLAVLLVGLMTNCSNDSDSSSLSVANSTYETTALNSQKSSTDQPNSGSKSGQTLDLVNLGVAANFAILSKTGITDVYKSAITGDVGASPITGAAILLKCDEVTGTIFSVDAAGPACKITDASRLTTAVGDMQIAYDNAAGRLNPDFLNLGAGTIGGKTLTPGLYKWTSTLNIPTDITISGSSTDVWIFQVAGNLNMSSAVRITLAGGAQAKNIFWQTAGAVTLGSTSHFEGNILSQTGINMKTAASINGRMMAQTAVTLQMNTVTIPQ | Function: Has antifreeze activity for survival in a subzero environment. Binds to the surface of ice crystals and inhibits their growth. Has high thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point, and thus the freezing of the cell fluid can be prevented protecting the organism from ice damage . The TH activity of this protein is 2.2 degrees Celsius at 5 uM and 2.5 degrees Celsius at 50 uM .
Sequence Mass (Da): 28447
Sequence Length: 276
Domain: The ice-binding site is formed by three T-A/G-X-T/N motifs.
Subcellular Location: Secreted
|
C7F6X3 | MSLLSIITIGLAGLGGLVNGQRDLSVELGVASNFAILAKAGISSVPDSAILGDIGVSPAAATYITGFGLTQDSSTTYATSPQVTGLIYAADYSTPTPNYLAAAVANAETAYNQAAGFVDPDFLELGAGELRDQTLVPGLYKWTSSVSVPTDLTFEGNGDATWVFQIAGGLSLADGVAFTLAGGANSTNIAFQVGDDVTVGKGAHFEGVLLAKRFVTLQTGSSLNGRVLSQTEVALQKATVNSPFVPAPEVVQKRSNARQWL | Function: Confers freeze tolerance. Binds to the surface of ice crystals and inhibits their growth. Has low thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point . The TH activity of this protein is approximately 0.2 degrees Celsius at 50 uM and 0.3 degrees Celsius at 400 uM .
PTM: Glycosylated . Glycosylation is not required for the thermal hysteresis (TH) activity . Glycosylation may increase stability and secretion of this protein (Probable).
Sequence Mass (Da): 26807
Sequence Length: 261
Subcellular Location: Secreted
|
A0A7D5JNZ7 | MLKINRKYAIILAIVAFSSFQTEAKAASISMLGTASNFGVLGGSTVTNTGPSVITESLGVSTGSSATGFPPAIVNGTIFTSDTVAAQAQVDNATAYNKLASLIPNKDLTGLDLGGLTLTPGVYSFSSSAQLTGILTLDNLGDPNALFVFQIGSTLTTASNSSIVTTNGDAPNVFFQIGSSATLGTGTQFMGNILALTSITLTTGVNIDCGRALAQNGAVTMDTNKVSNACYTKPQEKAVVPEPDSSLAVLGSGLVSLLFAFRKRFRKGW | Function: A probable ice-binding protein that has ice-structuring activities in vitro. Thought not to anchor the cyanobacterium to ice surfaces, as its habitat is shallow puddles fed by glacier meltwater.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27596
Sequence Length: 269
Domain: The ice-binding site may be formed by 7 T/S-X-T motifs.
Subcellular Location: Cell outer membrane
|
Q8RWZ3 | MGSSTGDLVTRIQSAHRFDHDALFRFAADNVSGFPTNPSQFKVSQFGHGQSNPTFLIEVGSGSSLKRYVLRKKPPGKLLQSAHAVDREFQVLRALGEHTQVPVPKVFCLCTDPAVIGTAFYIMEFMEGRIFIDPKLPNVAPERRNAIYRATAKALASLHSADVDAIGLEKYGRRGNYCKRQIDRWFKQYLASTSEGKPERNPKMFELVDWLRKNIPAEDSTGATSGLVHGDFRIDNLVFHPSEDRVIGIIDWELSTLGNQMCDVAYSCMHYIVNVQLDKEHVSEGFETTGLPEGMLSMPEFLLEYCSASGKPWPAANWKFYVAFSLFRAASIYTGVYSRWLMGNASAGERARNTGVQANELVESALGYIARENVLPEHPPSVQRDVSPSYESLVDGSGRFIPNRKVLELRQKLIKFMETHIYPMENEFSKLAQSDMRWTVHPQEEKLKEMAKREGLWNLFVPVDSAARARRELAATENKHNLSGKSFDQLFGEGLTNLEYGYLCEIMGRSVWAPQVFNCGAPDTGNMEVILRYGNKEQISEWLIPLLEGRIRSGFAMTEPQVASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLILMGKTDFNAPKHKQQSMILVDMRTPGISVKRPLTVFGFDDAPHGHAEISFENVVVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMELMAQRALSRKTFGKFIAQHGSFVSDLAKLRVELEGTRLLVLEAADHLDKFGNKKARGILAMAKVAAPNMALKVLDTAIQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIGKLELQRASKL | Function: Involved with IBR1 and IBR10 in the peroxisomal beta-oxidation of indole-3-butyric acid (IBA) to form indole-3-acetic acid (IAA), a biologically active auxin . May be responsible for catalyzing the first step in IBA-CoA beta-oxidation . May play a role in defense response to pathogenic bacteria .
Catalytic Activity: A + a 2,3-saturated acyl-CoA = a 2,3-dehydroacyl-CoA + AH2
Sequence Mass (Da): 91713
Sequence Length: 824
Subcellular Location: Peroxisome
EC: 1.3.99.-
|
Q84JU4 | MRKRERENPCSICGHYHKYEEGEVCGVCGHCMPVSSDTVAPQQVHVSAFPSEILPEFLYLGSYDNASRSELLKTQGISRVLNTVPMCQNLYRNSFTYHGLDNEKVLQFDDAIKFLDQCEKDKARVLVHCMSGKSRSPAVVVAYLMKRKGWRLAESHQWVKQRRPSTDISPEFYQQLQEFEQGIFGSEMMSAMNINDAPTFGFGFPKIDNQAQAPVFNNAPTSSIFSSPASSIPPQEFTFGATPPKPTTGGDIAMDGS | Function: Required for the transduction of auxin and abscisic acid (ABA) signaling pathways. Dephosphorylates and inactivates the MAP kinase MPK12.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 28690
Sequence Length: 257
Subcellular Location: Nucleus
EC: 3.1.3.48
|
C1P616 | MMKLVIILIVLLLVSFAAY | Function: Toxic component of a type I toxin-antitoxin (TA) system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 2151
Sequence Length: 19
Subcellular Location: Membrane
|
P09255 | MFCTSPATRGDSSESKPGASVDVNGKMEYGSAPGPLNGRDTSRGPGAFCTPGWEIHPARLVEDINRVFLCIAQSSGRVTRDSRRLRRICLDFYLMGRTRQRPTLACWEELLQLQPTQTQCLRATLMEVSHRPPRGEDGFIEAPNVPLHRSALECDVSDDGGEDDSDDDGSTPSDVIEFRDSDAESSDGEDFIVEEESEESTDSCEPDGVPGDCYRDGDGCNTPSPKRPQRAIERYAGAETAEYTAAKALTALGEGGVDWKRRRHEAPRRHDIPPPHGV | Function: Immediate early (EI) protein that functions as a transcriptional regulator of cellular and viral mRNAs mainly by interacting with several general transcription factors thereby disorganizing the preinitiation complex at certain promoters. May additionally help to regulate levels of histones in virus-infected cells by interacting with host ASF1. By inhibiting host transcriptional program, IE63 plays a major role in the ability of VZV to overcome the innate immune response to the virus.
PTM: Phosphorylated in vitro by host and by protein kinase ORF47.
Sequence Mass (Da): 30495
Sequence Length: 278
Subcellular Location: Host cytoplasm
|
Q04360 | MVPSQRLSRTSSISSNEDPAESHILELEAVSDTNTDCDLDPMEGSEEHSTDGEISSSEEEDEDPTPAHAIPARPSSVVITPTSASFVIPRKKWDLQDKTVTLHRSPLCRDEDEKEETGNSSYTRGHKRRRGEVHGCTDESYGKRRHLPPGARAPRAPRAPRVPRAPRSPRAPRSNRATRGPRSESRGAGRSTRKQARQERSQRPLPNKPWFDMSLVKPVSKITFVTLPSPLASLTLEPIQDPFLQSMLAVAAHPEIGAWQKVQPRHELRRSYKTLREFFTKSTNKDTWLDARMQAIQNAGLCTLVAMLEETIFWLQEITYHGDLPLAPAEDILLACAMSLSKVILTKLKELAPCFLPNTRDYNFVKQLFYITCATARQNKVVETLSSSYVKQPLCLLAAYAAVAPAYINANCRRRHDEVEFLGHYIKNYNPGTLSSLLTEAVETHTRDCRSASCSRLVRAILSPGTGSLGLFFVPGLNQ | Function: Promotes the nuclear export of a subset of early and late viral mRNAs by interacting with mRNAs and cellular export proteins. Additionally may prevent the establishment of cellular antiviral state, by acting as an alternative splicing factor for cellular RNAs such as STAT1, resulting in a STAT1 mRNA incapable of producing the STAT1alpha isoform.
PTM: Phosphorylated by cellular protein kinase CK2.
Sequence Mass (Da): 53492
Sequence Length: 479
Subcellular Location: Host nucleus
|
Q05906 | MALSSVSSCEPMEDEMSIMGSDTEDNFTGGDTCAEATRGLVNKSAFVPTQTVGTVSALRNVVGNPPKSVVVSFSASPQRAQPSNPKSERPAFGHGRRNRRRPFRRNNWKQQQRGWEKPEPENVPARQSAGSWPKRSSLPVHMRLGQRGGDSSSADSGHGGAGPSDRWRFKTRTQSVARVHRNRRRGNANHGSNTPGRSAGDRLNAAAARSIADVCRRVTSSRIGEMFHGARETLTTPVKNGGFRAENSSPWAPVLGFGSDQFNPEARRITWDTLVEHGVNLYKLFEVRSHAAEAARSLRDAVMRGENLLEALASADETLSWCKMIVTKNLPMRTRDPIISSSVALLDNLRLKLEPFMRCYLSSSGSPTLAELCDHQRLSDVACVPTFMFVMLARIARAVGSGAETVSRDALGPDGRVLADYVPGACLAGTLEAIDAHKRRCKADTCSLVSAYTLVPVYLHGKYFYCNQIF | Function: Multifunctional regulator of the expression of viral genes that mediates nuclear export of viral intronless mRNAs. This immediate early (EI) protein promotes the nuclear export of viral intronless mRNAs by interacting with mRNAs and host NXF1/TAP (By similarity).
Sequence Mass (Da): 51389
Sequence Length: 470
Domain: Binds viral intronless RNAs and SR proteins through the Arg-rich region.
Subcellular Location: Host cytoplasm
|
P16749 | MELHSRGRHDAPSLSSLSERERRARRARRFCLDYEPVPRKFRRERSPTSPSTRNGAAASEHHLAEDTVGAASHHHRPCVPARRPRYSKDDDTEGDPDHYPPPLPPSSRHALGGTGGHIIMGTAGFRGGHRASSSFKRRVAASASVPLNPHYGKSYDNDDGEPHHHGGDSTHLRRRVPSCPTTFGSSHPSSANNHHGSSAGPQQQQMLALIDDELDAMDEDELQQLSRLIEKKKRARLQRGAASSGTSPSSTSPVYDLQRYTAESLRLAPYPADLKVPTAFPQDHQPRGRILLSHDELMHTDYLLHIRQQFDWLEEPLLRKLVVEKIFAVYNAPNLHTLLAIIDETLSYMKYHHLHGLPVNPHDPYLETVGGMRQLLFNKLNNLDLGCILDHQDGWGDHCSTLKRLVKKPGQMSAWLRDDVCDLQKRPPETFSQPMHRAMAYVCSFSRVAVSLRRRALQVTGTPQFFDQFDTNNAMGTYRCGAVSDLILGALQCHECQNEMCELRIQRALAPYRFMIAYCPFDEQSLLDLTVFAGTTTTTASNHATAGGQQRGGDQIHPTDEQYANMESRTDPATLTAYDKKDREGSHRHPSPMIAAAPPAQPPSQPQQHYSEGELEEDEDSDDASSQDLVRATDRHGDTVVYKTTAVPPSPPAPLAGVRSHRGELNLMTPSPSHGGSPPQVPHKQPIIPVQSANGNHSTTATQQQQPPPPPPPPPVPQEDDSVVMRCQTPDYEDMLCYSDDMDD | Function: Immediate early (EI) protein that plays many roles during productive infection including regulation of host cell cycle progression, regulation of viral gene expression or nuclear export of intronless viral RNAs. Acts as a transcriptional transactivator via interaction with the cellular transcription elongation factor SUPT6H . In addition, acts as a post-transcriptional transactivator that mediates the nuclear export of unspliced mRNAs via interaction with DDX39B, a component of the cellular mRNA export machinery .
PTM: Phosphorylated by UL97 and host CDK1, CDK7 and CD9. Phosphorylation by CDKs impacts on UL69 nuclear localization and activity (By similarity).
Sequence Mass (Da): 82678
Sequence Length: 744
Subcellular Location: Virion tegument
|
P10238 | MATDIDMLIDLGLDLSDSDLDEDPPEPAESRRDDLESDSSGECSSSDEDMEDPHGEDGPEPILDAARPAVRPSRPEDPGVPSTQTPRPTERQGPNDPQPAPHSVWSRLGARRPSCSPEQHGGKVARLQPPPTKAQPARGGRRGRRRGRGRGGPGAADGLSDPRRRAPRTNRNPGGPRPGAGWTDGPGAPHGEAWRGSEQPDPPGGQRTRGVRQAPPPLMTLAIAPPPADPRAPAPERKAPAADTIDATTRLVLRSISERAAVDRISESFGRSAQVMHDPFGGQPFPAANSPWAPVLAGQGGPFDAETRRVSWETLVAHGPSLYRTFAGNPRAASTAKAMRDCVLRQENFIEALASADETLAWCKMCIHHNLPLRPQDPIIGTTAAVLDNLATRLRPFLQCYLKARGLCGLDELCSRRRLADIKDIASFVFVILARLANRVERGVAEIDYATLGVGVGEKMHFYLPGACMAGLIEILDTHRQECSSRVCELTASHIVAPPYVHGKYFYCNSLF | Function: Multifunctional regulator of the expression of viral genes that contributes to the shutoff of host protein synthesis and mediates nuclear export of viral intronless mRNAs. Early in infection, this immediate early (EI) protein mediates the inhibition of cellular splicing. This results in the accumulation of unprocessed 3'end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off early after virus infection. Later in the infection, it helps recruit cellular RNA polymerase II to viral replication sites and promotes the nuclear export of viral intronless mRNAs by interacting with mRNAs and host NXF1/TAP. ICP27 binds to NUP62 which may provide facilitated viral mRNA export and may indirectly compete with some host cell transport receptors for binding and inhibit cellular nucleocytoplasmic transport pathways . Also stimulates translation of viral transcripts. Repression of host gene expression blocks the cell cycle at the G1 phase and prevents apoptosis. Seems to silence the 3' splice site of the promyelocytic leukemia (PML) intron 7a, thereby switching PML isoforms from PML-II to PML-V. This could be linked to the accelerated mRNA export induced by ICP27 which might not provide sufficient time for PML pre-mRNA to be spliced in the nucleus.
PTM: Methylated within the RGG box possibly by host PRMT1. When hypomethylated, ICP27 is exported to the cytoplasm earlier and more rapidly.
Sequence Mass (Da): 55253
Sequence Length: 512
Domain: Binds viral intronless RNAs through the RGG region.
Subcellular Location: Host cytoplasm
|
Q2HR75 | MVQAMIDMDIMKGILEDSVSSSEFDESRDDETDAPTLEDEQLSEPAEPPADERIRGTQSAQGIPPPLGRIPKKSQGRSQLRSEIQFCSPLSRPRSPSPVNRYGKKIKFGTAGQNTRPPPEKRPRRRPRDRLQYGRTTRGGQCRAAPKRATRRPQVNCQRQDDDVRQGVSDAVKKLRLPASMIIDGESPRFDDSIIPRHHGACFNVFIPAPPSHVPEVFTDRDITALIRAGGKDDELINKKISAKKIDHLHRQMLSFVTSRHNQAYWVSCRRETAAAGGLQTLGAFVEEQMTWAQTVVRHGGWFDEKDIDIILDTAIFVCNAFVTRFRLLHLSCVFDKQSELALIKQVAYLVAMGNRLVEACNLLGEVKLNFRGGLLLAFVLTIPGMQSRRSISARGQELFRTLLEYYRPGDVMGLLNVIVMEHHSLCRNSECAAATRAAMGSAKFNKGLFFYPLS | Function: Early protein that promotes the accumulation and nuclear export of viral intronless RNA transcripts by interacting with mRNAs and cellular export proteins. Probably acts as a viral splicing factor that regulates viral RNA splicing. Functions as a multifunctional regulator of the expression of viral lytic genes.
PTM: Proteolytically cleaved by host caspase-7 (CASP7), leading to its inactivation, thereby preventing expression of viral lytic genes.
Sequence Mass (Da): 51012
Sequence Length: 455
Domain: Binds viral intronless RNAs.
Subcellular Location: Host cytoplasm
|
Q9USP8 | MSMLSTLRTAGSLRTFSRSACYSFQRFSSTKAAAGTYEGVKNANGNYTVTMIAGDGIGPEIAQSVERIFKAAKVPIEWERVKVYPILKNGTTTIPDDAKESVRKNKVALKGPLATPIGKGHVSMNLTLRRTFGLFANVRPCVSITGYKTPYDNVNTVLIRENTEGEYSGIEHEVIPGVVQSIKLITRAASERVIRYAFQYARQTGKNNITVVHKATIMRMADGLFLECAKELAPEYPDIELREEILDNACLKIVTDPVPYNNTVMVMPNLYGDIVSDMCAGLIGGLGLTPSGNIGNQASIFEAVHGTAPDIAGKGLANPTALLLSSVMMLKHMNLNDYAKRIESAIFDTLANNPDARTKDLGGKSNNVQYTDAIISKLK | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Performs an essential role in the oxidative function of the citric acid cycle and is involved in glutamate biosynthesis . Also binds RNA; specifically to the 5'-untranslated leaders of mitochondrial mRNAs .
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 41188
Sequence Length: 379
Subcellular Location: Mitochondrion
EC: 1.1.1.41
|
P28241 | MLRNTFFRNTSRRFLATVKQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKIFSAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVALKGPLATPIGKGHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYENVDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASERVIRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKELSKEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGDILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDIAGQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIASGPENRTGDLAGTATTSSFTEAVIKRL | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Performs an essential role in the oxidative function of the citric acid cycle. Also binds RNA; specifically to the 5'-untranslated leaders of mitochondrial mRNAs.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 39739
Sequence Length: 369
Subcellular Location: Mitochondrion matrix
EC: 1.1.1.41
|
Q93714 | MLGKCIKKASSTVGQSIRYSSGDVRRVTLIPGDGIGPEISASVQKIFEAADAPIAWDPVDVTPVKGRDGVFRIPSRCIELMHANKVGLKGPLETPIGKGHRSLNLAVRKEFSLYANVRPCRSLEGHKTLYDNVDVVTIRENTEGEYSGIEHEIVPGVVQSIKLITETASRNVASFAFEYARQNGRKVVTAVHKANIMRQSDGLFLSICREQAALYPDIKFKEAYLDTVCLNMVQDPSQYDVLVMPNLYGDILSDLCAGLVGGLGVTPSGNIGKGAAVFESVHGTAPDIAGQDKANPTALLLSAVMMLRYMNLPQHAARIEKAVFDAIADGRAKTGDLGGTGTCSSFTADVCARVKDLE | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 38466
Sequence Length: 358
Subcellular Location: Mitochondrion
EC: 1.1.1.41
|
P54836 | AIEVQTVTLIPGD | Function: Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 1356
Sequence Length: 13
Subcellular Location: Mitochondrion
EC: 1.1.1.41
|
Q9VWH4 | MAARFIQKILNQLGLIAARDAPAVTATPAVSQVNATPAASRSYSSGTKKVTLIPGDGIGPEISAAVQKIFTAANVPIEWEAVDVTPVRGPDGKFGIPQAAIDSVNTNKIGLKGPLMTPVGKGHRSLNLALRKEFNLYANVRPCRSLEGYKTLYDDVDVVTIRENTEGEYSGIEHEIVDGVVQSIKLITEEASKRVAEYAFQYAKNNNRKKVTVVHKANIMRMSDGLFLRCVRDMAQKFPEIQFEEKYLDTVCLNMVQNPGKYDVLVMPNLYGDILSDMCAGLVGGLGLTPSGNMGLNGALFESVHGTAPDIAGKDLANPTALLLSAVMMLRHMELNTYADKIERAAFETIKEGKYLTGDLGGRAKCSEFTNEICAKL | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Probable catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 40844
Sequence Length: 377
Subcellular Location: Mitochondrion
EC: 1.1.1.41
|
P50213 | MAGPAWISKVSRLLGAFHNPKQVTRGFTGGVQTVTLIPGDGIGPEISAAVMKIFDAAKAPIQWEERNVTAIQGPGGKWMIPSEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEGASKRIAEFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAESCKDIKFNEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGLFDHAARIEAACFATIKDGKSLTKDLGGNAKCSDFTEEICRRVKDLD | Cofactor: Divalent metal cations; Mn(2+) or Mg(2+). Activity higher in presence of Mn(2+) than of Mg(2+). Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 39592
Sequence Length: 366
Subcellular Location: Mitochondrion
EC: 1.1.1.41
|
P86225 | MRPGVAAVAAVRIFDAAKAPIQWEERNVTAIQGPGGKWMIPPEAKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRRIAEFAFEYARDMANPTALLLSAVMMLRCSDFTEEICRR | Cofactor: Divalent metal cations; Mn(2+) or Mg(2+). Activity higher in presence of Mn(2+) than of Mg(2+). Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 14881
Sequence Length: 134
Subcellular Location: Mitochondrion
EC: 1.1.1.41
|
Q9D6R2 | MAGSAWVSKVSRLLGAFHNTKQVTRGFAGGVQTVTLIPGDGIGPEISASVMKIFDAAKAPIQWEERNVTAIQGPGGKWMIPPEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEEASKRIAEFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAENCKDIKFNEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGLFDHAAKIEAACFATIKDGKSLTKDLGGNAKCSDFTEEICRRVKDLD | Cofactor: Divalent metal cations; Mn(2+) or Mg(2+). Activity higher in presence of Mn(2+) than of Mg(2+). Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 39639
Sequence Length: 366
Subcellular Location: Mitochondrion
EC: 1.1.1.41
|
Q5R678 | MAGPAWISKVSRLLGAFHNPKQVTRGFTGGVQTVTLIPGDGIGPEISAAVMKIFDAAKAPIQWEERNVTAIQGPGGKWMIPSEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEGASKRIAEFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAENCKDIKFNEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGLFDHAARIEAACFATIKDGKSLTKDLGGNAKCSDFTEEICRRVKDLD | Cofactor: Divalent metal cations; Mn(2+) or Mg(2+). Activity higher in presence of Mn(2+) than of Mg(2+). Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 39619
Sequence Length: 366
Subcellular Location: Mitochondrion
EC: 1.1.1.41
|
Q93353 | MLSRTVSSLSRVAPQTLGAVNAASSRQYSITAPRPPTELNQKLKVTIIPGDGVGPELIYTVQDIVKQTGIPIEFEEIFLSEVHYTRSSSIENAVESIGRNNNVALKGAIEESAVLHTEGELQGLNMRLRRSLDLFANVVHIKTLDGIKTRHGKQLDFVIVREQTEGEYSSLEHELVPGVIECLKISTRTKAERIAKFAFDYATKTGRKKVTAVHKANIMKLGDGLFLRTCEGVAKQYPKIQFESMIIDNTCMQLVSKPEQFDVMVMPNLYGNIIDNLAAGLVGGAGVVPGQSVGRDFVIFEPGSRHSFQEAMGRSIANPTAMILCAANMLNHLHLDAWGNSLRQAVADVVKEGKVRTRDLGGYATTVDFADAVIDKFRI | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 41553
Sequence Length: 379
Subcellular Location: Mitochondrion
EC: 1.1.1.41
|
Q92HM7 | MLKDQNLDIERKQDHIEINLTKNVESTLKSGFESIHFIHNALPEINYDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAQVAQKAGIAMGLGSMRVLLTEPDTIKTFAVRHIAPDIPLLANIGAVQLNYGVTPKECQYLVDAIKADALILHLNVLQELTQPEGNRNWEKLLPKIREVVNYLSIPVIVKEVGYGLSKKVAESLIDAGVKVLDIAGSGGTSWSQVEAYRATNSLQNRIASSFINWGIPTLDSLKMVREVSKDIPIITSGGFKSGIDGAKAIRIGANIFGLAGQFLKAADTSESLLSEEIQLIIEQLKITMLCTGSRTLKDLAKAEIRL | Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 37336
Sequence Length: 342
Subcellular Location: Cytoplasm
EC: 5.3.3.2
|
Q9ZD90 | MPKEQNLDIERKQEHIEINLKQNVNSTLKSGLESIKFIHNALPEINYDSIDTTTTFLGKDMKAPILISSMTGGTARARDINYRLAQAAQKSGIAMGLGSMRILLTKPDTIKTFTVRHVAPDIPLLANIGAVQLNYGVTPKECQYLIDTIKADALILHLNVLHELTQPEGNKNWENLLPKIKEVINYLSVPVIVKEVGYGLSKQVAKKLIKAGVKVLDIAGSGGTSWSQVEAYRAKNSMQNRIASSFINWGITTLDSLKMLQEISKDITIIASGGLQSGIDGAKAIRMGANIFGLAGKLLKAADIAESLVLEEIQVIIEQLKITMLCTGSCTLKDLAKAEIMW | Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 37364
Sequence Length: 342
Subcellular Location: Cytoplasm
EC: 5.3.3.2
|
P61615 | MPDIVNRKVEHVEIAAFENVDGLSSSTFLNDVILVHQGFPGISFSEINTKTKFFRKEISVPVMVTGMTGGRNELGRINKIIAEVAEKFGIPMGVGSQRVAIEKAEARESFAIVRKVAPTIPIIANLGMPQLVKGYGLKEFQDAIQMIEADAIAVHLNPAQEVFQPEGEPEYQIYALEKLRDISKELSVPIIVKESGNGISMETAKLLYSYGIKNFDTSGQGGTNWIAIEMIRDIRRGNWKAESAKNFLDWGVPTAASIMEVRYSVPDSFLVGSGGIRSGLDAAKAIALGADIAGMALPVLKSAIEGKESLEQFFRKIIFELKAAMMLTGSKDVDALKKTSIVILGKLKEWAEYRGINLSIYEKVRKRE | Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 40427
Sequence Length: 368
Subcellular Location: Cytoplasm
EC: 5.3.3.2
|
Q53479 | MTEVLDILRKYSEVADKRIMECISDITPDTLLKASEHLITAGGKKIRPSLALLSCEAVGGNPEDAAGVAAAIELIHTFSLIHDDIMDDDEMRRGEPSVHVIWGEPMAILAGDVLFSKAFEAVIRNGDSERVKDALAVVVDSCVKICEGQALDMGFEERLDVTEDEYMEMIYKKTAALIAAATKAGAIMGGASEREVEALEDYGKFIGLAFQIHDDYLDVVSDEESLGKPVGSDIAEGKMTLMVVKALEEASEEDRERLISILGSGDEGSVAEAIEIFERYGATQYAHEVALDYVRMAKERLEILEDSDARDALMRIADFVLEREH | Cofactor: Binds 2 Mg(2+) ions per subunit.
Sequence Mass (Da): 35636
Sequence Length: 325
Subcellular Location: Cytoplasm
EC: 2.5.1.-
|
P22304 | MPPPRTGRGLLWLGLVLSSVCVALGSETQANSTTDALNVLLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKVFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANLLCPVDVLDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPEVPDGLPPVAYNPWMDIRQREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATHVPLIFYVPGRTASLPEAGEKLFPYLDPFDSASQLMEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCPVPSFHVELCREGKNLLKHFRFRDLEEDPYLPGNPRELIAYSQYPRPSDIPQWNSDKPSLKDIKIMGYSIRTIDYRYTVWVGFNPDEFLANFSDIHAGELYFVDSDPLQDHNMYNDSQGGDLFQLLMP | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Lysosomal enzyme involved in the degradation pathway of dermatan sulfate and heparan sulfate.
PTM: Synthesized as a 75-kDa precursor form in the endoplasmic reticulum (ER), and then processed by proteolytic cleavage through various intermediates to yield a 55-kDa mature form, with the release of an 18 kDa polypeptide.
Catalytic Activity: Hydrolysis of the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate and heparin.
Sequence Mass (Da): 61873
Sequence Length: 550
Subcellular Location: Lysosome
EC: 3.1.6.13
|
Q08890 | MSPPPPPPIWRQLSFSLLLGSFCIALESAAQGNSATDALNILLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNFSTIPQYFKENGYVTMSVGKVFHPGISSNHSDDYPYSWSFPPYHPSSEKYENTKTCKGQDGKLHANLLCPVDVADVPEGTLPDKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPHVPDSLPPVAYNPWMDIREREDVQALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRVPLMLYVPGRTAPLPAAGQKLFPYRDPFDPASDWMDAGRHTEDLVELVSLFPTLAGLAGLPVPPRCPIPSFHVELCREGQNLQKHLQLHDLEEEPDLFGNPRELIAYSQYPRPADFPQWNSDKPSLNDIKVMGYSIRTVDYRYTVWVGFDPSEFLANFSDIHAGELYFVDSDPLQDHNVYNDSQHGGLLHSLRP | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Lysosomal enzyme involved in the degradation pathway of dermatan sulfate and heparan sulfate.
PTM: Synthesized as a 75-kDa precursor form in the endoplasmic reticulum (ER), and then processed by proteolytic cleavage through various intermediates to yield a 55-kDa mature form, with the release of an 18 kDa polypeptide.
Catalytic Activity: Hydrolysis of the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate and heparin.
Sequence Mass (Da): 62186
Sequence Length: 552
Subcellular Location: Lysosome
EC: 3.1.6.13
|
J7FIJ6 | MDGFSILHEPPAAYKEVKWMADTFVAGMGLGWIVNYALMIRFSWKGRPHCMALLPLCNNIAWELTYTIVYPSANRVELLVFAIGLTLNFFIMVGARRSARVEWRHSPLLSEHAGFILLVGTLLCFTGHVALAMEIGPGLAYSWGAVVCQLALSIGGLFQLLQRNSTAGTSWTLWSSRFLGSCCTVAFAGLRCKYWPEVFGWLASPLVLWSLVTFLLADSAYGFCLYRVSHAETKARKKH | Function: Terpene cyclase; part of the gene cluster that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that are potent tremorgens in mammals . The geranylgeranyl diphosphate (GGPP) synthase idtG is proposed to catalyze the first step in IDT biosynthesis via catalysis of a series of iterative condensations of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyltransferase idtC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation of the two terminal alkenes of the geranylgeranyl moiety by the FAD-dependent monooxygenase idtM, and cyclization by the terpene cyclase idtB then leads to the production of paspaline (Probable). The cytochrome P450 monooxygenase idtP then catalyzes oxidative elimination of the pendant methyl group at C-12 of paspaline and generates the C-10 ketone to yield 13-desoxypaxilline . The cytochrome P450 monooxygenase idtQ may catalyze the C-13 oxidation of 13-desoxypaxilline to afford paxilline (Probable). Considering that both paspalicine and paxilline were detected in C.paspali, idtQ also catalyzes the formation of paspalinine from 13-desoxypaxilline via paspalicine as an intermediate (Probable). Finally, the alpha-prenyltransferase idtF prenylates paspalinine at the C-20 or the C-21 positions to yield paspalitrems A and C, respectively . The hydroxylation of paspalitrem A at C-32 by a still unknown oxidase affords paspalitrem B (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26633
Sequence Length: 239
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 4.2.3.-
|
J7FJH2 | MTTLAWFAGRSMVLDLAALTSAFTVGYLLKSTSTPTSTPTSTDKAGTPPGSTIHHYGYPQGSVTKPNNSKTEKENGSPKDSKGNVPDCPYKYLVGLYGHHHFAGFVEALQPTLKDEDPEKYTLVLDIMDAVHLCLILVDDICDDSPKRKNQTTAHLLFGSCETANRAYLVLTKVINRAMRTRPVLGAELVRALELILEGQDLSLVWRRDGLAAFDAEEGGDKVSVYKKMAQLKTGTLFVLLGRLLNDGGAQLDDVLLRLGWYSQLQNDCKNIYSGEYANNKGAIAEDLRNGEMSFPVVVALGDQTTSSQIRKAFGSHSDGDIFDALDALQSSCIKNKCSQALQEAGRGLENLLAIWGRREHMDSLGS | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that are potent tremorgens in mammals . The geranylgeranyl diphosphate (GGPP) synthase idtG is proposed to catalyze the first step in IDT biosynthesis via catalysis of a series of iterative condensations of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyltransferase idtC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation of the two terminal alkenes of the geranylgeranyl moiety by the FAD-dependent monooxygenase idtM, and cyclization by the terpene cyclase idtB then leads to the production of paspaline (Probable). The cytochrome P450 monooxygenase idtP then catalyzes oxidative elimination of the pendant methyl group at C-12 of paspaline and generates the C-10 ketone to yield 13-desoxypaxilline . The cytochrome P450 monooxygenase idtQ may catalyze the C-13 oxidation of 13-desoxypaxilline to afford paxilline (Probable). Considering that both paspalicine and paxilline were detected in C.paspali, idtQ also catalyzes the formation of paspalinine from 13-desoxypaxilline via paspalicine as an intermediate (Probable). Finally, the alpha-prenyltransferase idtF prenylates paspalinine at the C-20 or the C-21 positions to yield paspalitrems A and C, respectively . The hydroxylation of paspalitrem A at C-32 by a still unknown oxidase affords paspalitrem B (Probable).
Sequence Mass (Da): 40020
Sequence Length: 367
Pathway: Secondary metabolite biosynthesis.
EC: 2.5.1.-
|
J7FIP8 | MFLLHILAIGACLLWYFVRSDKRKQGSNIPTIRRWPALFPEFLDRLSYNSCAARLVENGYREHKDRPFRLLKMDMDLVVIPLKYAQEMRALTSDELDPLTAVFDDNVGKVTGILLDSQLHTHAIQRRLTPRLPNIIPAMMDELNYAFQQVIPSEAGERLQTSWVPINPYDMVLELSTRAAARLFVGEPICRDEVFLKTSAAYSRNIFDTIHVSRSLGHIITPYLGSLIPSVRQFHQQFEYIQNLVLGEIAHRKQHSEDNKADDFLQWCMELARTKEESTPTALAQRTVGILSMAVVHTSAMATTHLLFDMISNQELREQLRTEQKQVLKQGWMGITQQTMLDMKQLDSVMRESQRINPVGEFTFRRIVRKPITLSDGFQLHPGQQIAIAARCINTDGDVLPDAETFKPMRWMEKESAASTGFAHSSDSNLHFGLGRYACPGRFLASYMIKAIISRVLFDYEFKLQDDSAAGRPPNLIHGDKIFPSRDVTVLFRRRHDE | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that are potent tremorgens in mammals . The geranylgeranyl diphosphate (GGPP) synthase idtG is proposed to catalyze the first step in IDT biosynthesis via catalysis of a series of iterative condensations of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyltransferase idtC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation of the two terminal alkenes of the geranylgeranyl moiety by the FAD-dependent monooxygenase idtM, and cyclization by the terpene cyclase idtB then leads to the production of paspaline (Probable). The cytochrome P450 monooxygenase idtP then catalyzes oxidative elimination of the pendant methyl group at C-12 of paspaline and generates the C-10 ketone to yield 13-desoxypaxilline . The cytochrome P450 monooxygenase idtQ may catalyze the C-13 oxidation of 13-desoxypaxilline to afford paxilline (Probable). Considering that both paspalicine and paxilline were detected in C.paspali, idtQ also catalyzes the formation of paspalinine from 13-desoxypaxilline via paspalicine as an intermediate (Probable). Finally, the alpha-prenyltransferase idtF prenylates paspalinine at the C-20 or the C-21 positions to yield paspalitrems A and C, respectively . The hydroxylation of paspalitrem A at C-32 by a still unknown oxidase affords paspalitrem B (Probable).
Sequence Mass (Da): 57051
Sequence Length: 498
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
|
J7FJH1 | MLTEQFDPSTFYSPKTVAIAGLILGCVLIYVYNDYPTNVNVPVIGVGVRYTKWLAAVRNVFYARDSVAEGYKKANFAFQIPTLNRMEIFICDRKMTREYQNLDSDRMSLDAVVVEEFEFDLLSPGHGHGHRRGPDSVPIPVVAKALAWQRRRTANTNDPFFQEFMAEVSYGFQQEVQRLSQDPRSSTTTPVFTVPCFSFALQVVGRITTFALFGRPMCRDRAFLDLCGKYSDGLPRGAMLLRPWPKWMRPFIAKHMEAPQVLAKLKEIIGAEIERRKASDGESPMENIMDYFVDWAYKGRDTVPADADDTVAHVLANLIFASFHTTSQLLTDCLFEIAMRPEYVEPLREEIKDCFEKHGRETRAVLDSLFKMDSFIKETHRWNPLDASALARIAMQDFTFSNGLHIPKGSFIFTPNAPIFQDERHYSNPKIFDGFRFAKMRDDPKLKLTCDLATVGEYSLNFGLGRHACPGRYLASDEVKLSLIHLLQNFDITVDPSELPLKRVRYGKFSLADMSAKVSLRRLRSEVKG | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that are potent tremorgens in mammals . The geranylgeranyl diphosphate (GGPP) synthase idtG is proposed to catalyze the first step in IDT biosynthesis via catalysis of a series of iterative condensations of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyltransferase idtC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation of the two terminal alkenes of the geranylgeranyl moiety by the FAD-dependent monooxygenase idtM, and cyclization by the terpene cyclase idtB then leads to the production of paspaline (Probable). The cytochrome P450 monooxygenase idtP then catalyzes oxidative elimination of the pendant methyl group at C-12 of paspaline and generates the C-10 ketone to yield 13-desoxypaxilline . The cytochrome P450 monooxygenase idtQ may catalyze the C-13 oxidation of 13-desoxypaxilline to afford paxilline (Probable). Considering that both paspalicine and paxilline were detected in C.paspali, idtQ also catalyzes the formation of paspalinine from 13-desoxypaxilline via paspalicine as an intermediate (Probable). Finally, the alpha-prenyltransferase idtF prenylates paspalinine at the C-20 or the C-21 positions to yield paspalitrems A and C, respectively . The hydroxylation of paspalitrem A at C-32 by a still unknown oxidase affords paspalitrem B (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60321
Sequence Length: 529
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
|
J7FIP9 | MSRTEASGWGFSLLQILLVLAGMVWKAREGFPIVDFLDTSGDTCSWLNPCIVPPALSCWNNWPWFALHLFLYTTQLVGLSAIILPPVYLIRMLGLSTALPLISLWVLHRRRRTGKGWATTFPPRHGEEAFLWRVLWFTGLAHVASFLVATAASFLGREDMAPWHLTNTLLGTPDCSYLPCSQIAERQARLRQINEMTGTSSGFFLAVALFSQHLEMNGARLGAGLLARLFFVSLIAGPAAGAADALLLRSAFMRTRRST | Function: Part of the gene cluster that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that are potent tremorgens in mammals . The geranylgeranyl diphosphate (GGPP) synthase idtG is proposed to catalyze the first step in IDT biosynthesis via catalysis of a series of iterative condensations of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyltransferase idtC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation of the two terminal alkenes of the geranylgeranyl moiety by the FAD-dependent monooxygenase idtM, and cyclization by the terpene cyclase idtB then leads to the production of paspaline (Probable). The cytochrome P450 monooxygenase idtP then catalyzes oxidative elimination of the pendant methyl group at C-12 of paspaline and generates the C-10 ketone to yield 13-desoxypaxilline . The cytochrome P450 monooxygenase idtQ may catalyze the C-13 oxidation of 13-desoxypaxilline to afford paxilline (Probable). Considering that both paspalicine and paxilline were detected in C.paspali, idtQ also catalyzes the formation of paspalinine from 13-desoxypaxilline via paspalicine as an intermediate (Probable). Finally, the alpha-prenyltransferase idtF prenylates paspalinine at the C-20 or the C-21 positions to yield paspalitrems A and C, respectively . The hydroxylation of paspalitrem A at C-32 by a still unknown oxidase affords paspalitrem B (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28679
Sequence Length: 259
Subcellular Location: Membrane
|
Q9VKJ8 | MLSLLLVLTTLARIHAHYTSGDVVYHTMPHFWTGVGFCPAGRIDHEGISAALGDPALRLNLRLIAALPVGAVTHIRIHWLLELIQFWQYDPSGIPIYDFSKFDDFIDFLHEELRLSPVLEWMGNLGGVFSENPMQQSFYWEHLVKTTINHQIARHGSSRLVNWRYETWNEPDLRGYNKQNFTAHTFLDYVQAVRRGLSKAGNLDNQDGKVPLPMYRSLRGPAGLFKDSNHPLCWNLLELCSQRVVYCPIDILTFHRKGIEGTATEIVNGSLSLMAKIYEEYPNLKQLPVANDEADPVAGWSTSRDFQADVRYGITLISTVMQFWHAKLAGGPLSRLESISHDNAFLSYHPHEFTQRTLLAHFRMNETKPPHSQLVQKPVYAALGMLAKLGTRAADVEMVNMDTKHSVQVLRTVSGGLGGPGQYMATIFLSPEEAGPKMTAFHHKYTLNMSIANESAFVTELLVPKETDPYYIWQQAGSPAYPNATLREAMRRAQAPRLYKTGPIWQYNSELVINSASIPLPWAMLLRVCSASWPKLRRPQQLSIAEVTQREVFISWMEHPKSTQCLLSYEVWFKERDNLGRSADWMLISQGWHLPYPSFQYAPGDKGSVNGFYKVRGVDVFNETSPYSQIVEYLEL | Function: Essential lysosomal hydrolase responsible for the degradation of the glycosaminoglycans (GAG) heparan sulfate and dermatan sulfate (Probable). Required for lysosome function and autophagy . Consequently, has an essential role in the development, maintenance and function of various cells, tissues, and organs, including the muscles and the central nervous system (CNS) .
Catalytic Activity: Hydrolysis of unsulfated alpha-L-iduronosidic linkages in dermatan sulfate.
Sequence Mass (Da): 72300
Sequence Length: 636
Subcellular Location: Lysosome
EC: 3.2.1.76
|
P35475 | MRPLRPRAALLALLASLLAAPPVAPAEAPHLVHVDAARALWPLRRFWRSTGFCPPLPHSQADQYVLSWDQQLNLAYVGAVPHRGIKQVRTHWLLELVTTRGSTGRGLSYNFTHLDGYLDLLRENQLLPGFELMGSASGHFTDFEDKQQVFEWKDLVSSLARRYIGRYGLAHVSKWNFETWNEPDHHDFDNVSMTMQGFLNYYDACSEGLRAASPALRLGGPGDSFHTPPRSPLSWGLLRHCHDGTNFFTGEAGVRLDYISLHRKGARSSISILEQEKVVAQQIRQLFPKFADTPIYNDEADPLVGWSLPQPWRADVTYAAMVVKVIAQHQNLLLANTTSAFPYALLSNDNAFLSYHPHPFAQRTLTARFQVNNTRPPHVQLLRKPVLTAMGLLALLDEEQLWAEVSQAGTVLDSNHTVGVLASAHRPQGPADAWRAAVLIYASDDTRAHPNRSVAVTLRLRGVPPGPGLVYVTRYLDNGLCSPDGEWRRLGRPVFPTAEQFRRMRAAEDPVAAAPRPLPAGGRLTLRPALRLPSLLLVHVCARPEKPPGQVTRLRALPLTQGQLVLVWSDEHVGSKCLWTYEIQFSQDGKAYTPVSRKPSTFNLFVFSPDTGAVSGSYRVRALDYWARPGPFSDPVPYLEVPVPRGPPSPGNP | PTM: N-glycosylation at Asn-372 contributes to substrate binding and is required for full enzymatic activity.
Catalytic Activity: Hydrolysis of unsulfated alpha-L-iduronosidic linkages in dermatan sulfate.
Sequence Mass (Da): 72670
Sequence Length: 653
Subcellular Location: Lysosome
EC: 3.2.1.76
|
P11138 | MTQINFNASYTSASTPSRASFDNSYSEFCDKQPNDYLSYYNHPTPDGADTVISDSETAAASNFLASVNSLTDNDLVECLLKTTDNLEEAVSSAYYSESLEQPVVEQPSPSSAYHAESFEHSAGVNQPSATGTKRKLDEYLDNSQGVVGQFNKIKLRPKYKKSTIQSCATLEQTINHNTNICTVASTQEITHYFTNDFAPYLMRFDDNDYNSNRFSDHMSETGYYMFVVKKSEVKPFEIIFAKYVSNVVYEYTNNYYMVDNRVFVVTFDKIRFMISYNLVKETGIEIPHSQDVCNDETAAQNCKKCHFVDVHHTFKAALTSYFNLDMYYAQTTFVTLLQSLGERKCGFLLSKLYEMYQDKNLFTLPIMLSRKESNEIETASNNFFVSPYVSQILKYSESVQFPDNPPNKYVVDNLNLIVNKKSTLTYKYSSVANLLFNNYKYHDNIASNNNAENLKKVKKEDGSMHIVEQYLTQNVDNVKGHNFIVLSFKNEERLTIAKKNKEFYWISGEIKDVDVSQVIQKYNRFKHHMFVIGKVNRRESTTLHNNLLKLLALILQGLVPLSDAITFAEQKLNCKYKKFEFN | Function: Regulatory transcriptional protein, which trans-activates gene expression from early baculovirus promoters. Can also trans-activate its own promoter, suggesting an autoregulation during infection of host cells. Promotes also viral DNA genome replication via the N-terminal region.
PTM: Phosphorylated.
Sequence Mass (Da): 66881
Sequence Length: 582
Domain: The N-terminal region is required for origin-specific DNA replication and phosphorylation.
Subcellular Location: Host nucleus
|
Q9NZI8 | MNKLYIGNLNESVTPADLEKVFAEHKISYSGQFLVKSGYAFVDCPDEHWAMKAIETFSGKVELQGKRLEIEHSVPKKQRSRKIQIRNIPPQLRWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYSNREQTRQAIMKLNGHQLENHALKVSYIPDEQIAQGPENGRRGGFGSRGQPRQGSPVAAGAPAKQQQVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKAISVHSTPEGCSSACKMILEIMHKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTLYNPERTITVKGAIENCCRAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSSAVPPPPSSVTGAAPYSSFMQAPEQEMVQVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVIITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENDQVIVKIIGHFYASQMAQRKIRDILAQVKQQHQKGQSNQAQARRK | Function: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability . Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to and stabilizes ABCB1/MDR-1 mRNA (By similarity). During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing (By similarity). Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence preventing MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD . Binding to MYC mRNA is enhanced by m6A-modification of the CRD . Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to the oncofetal H19 transcript and to the neuron-specific TAU mRNA and regulates their localizations. Binds to and stabilizes BTRC/FBW1A mRNA. Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2. Promotes the directed movement of tumor-derived cells by fine-tuning intracellular signaling networks. Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN transcript open reading frame (ORF) and prevents mRNA decay. This combined action on MAPK4 (down-regulation) and PTEN (up-regulation) antagonizes HSPB1 phosphorylation, consequently it prevents G-actin sequestration by phosphorylated HSPB1, allowing F-actin polymerization. Hence enhances the velocity of cell migration and stimulates directed cell migration by PTEN-modulated polarization. Interacts with Hepatitis C virus (HCV) 5'-UTR and 3'-UTR and specifically enhances translation at the HCV IRES, but not 5'-cap-dependent translation, possibly by recruiting eIF3. Interacts with HIV-1 GAG protein and blocks the formation of infectious HIV-1 particles. Reduces HIV-1 assembly by inhibiting viral RNA packaging, as well as assembly and processing of GAG protein on cellular membranes. During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts.
PTM: Phosphorylated. Phosphorylation may impair association with ACTB mRNA and hence abolishes translational repression (By similarity).
Sequence Mass (Da): 63481
Sequence Length: 577
Domain: Domains KH3 and KH4 are the major RNA-binding modules, although KH1 and KH2 may also contribute . KH1 and KH2, and possibly KH3 and KH4, promote the formation of higher ordered protein-RNA complexes, which may be essential for IGF2BP1 cytoplasmic retention. KH domains are required for RNA-dependent homo- and heterooligomerization and for localization to stress granules. KH3 and KH4 mediate association with the cytoskeleton. Two nuclear export signals (NES) have been identified in KH2 and KH4 domains, respectively. Only KH2 NES is XPO1-dependent. Both NES may be redundant, since individual in vitro mutations do not affect subcellular location of the full-length protein. The 4 KH domains are important to suppress HIV-1 infectivity.
Subcellular Location: Nucleus
|
Q0GRC4 | MVVEDTPKSIITDDQITTNPNRVIEDDNNLEEGEILDEDDSSATSKPVVHQPHLLENSWTFLFDTPAAKSKQDDWGSSMRPIYTFSTVEEFWSIYNNIHHPGKLAVRADFYCFKHKIEPKWEDPICANGGKWTANYPKGKSDTSWLYTLLAMIGEQFDHGDEICGAVVKVRGRAEKISIWTKNASNEAAQVSIGKQWKEFLDYNETMGFIFHDDARKLDRNAKNKYVV | Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome . Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures . Key component of recessive resistance to potyviruses .
PTM: According to the redox status, the Cys-126-Cys-164 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA.
Sequence Mass (Da): 26095
Sequence Length: 228
Subcellular Location: Nucleus
|
M1JJT8 | MVVEDALKTSASEDQAKTETNPKPREEDDEPEEGEIVGDEESASKPSKGIAPESHALEHSWTFWFDSPAAKSAKTKQEDWGSSIRPIYTFSTVEEFWSIYNNIRHPSKLAIGTDFHCFKYKIEPKWEDPVCANGGKWTVTLPKGKSDTSWLYTLLGMIGEQFDHGDEICGAVVNVRNRQEKISIWTKNAINEAAQLSIGKQWKGLLDYNETIGFIFHEDAMRHERSAKNKYVV | Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity).
PTM: According to the redox status, the Cys-131-Cys-169 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA.
Sequence Mass (Da): 26429
Sequence Length: 233
Subcellular Location: Nucleus
|
Q4VQY3 | MAAAEMERTMSFDAAEKLKAADGGGGEVDDELEEGEIVEESNDTASYLGKEITVKHPLEHSWTFWFDNPTTKSRQTAWGSSLRNVYTFSTVEDFWGAYNNIHHPSKLIMGADFHCFKHKIEPKWEDPVCANGGTWKMSFSKGKSDTSWLYTLLAMIGHQFDHGDEICGAVVSVRAKGEKIALWTKNAANETAQVSIGKQWKQFLDYSDSVGFIFHDDAKRLDRNAKNRYTV | Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome . Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures . Key component of recessive resistance to potyviruses .
PTM: According to the redox status, the Cys-129-Cys-167 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA.
Sequence Mass (Da): 26042
Sequence Length: 231
Subcellular Location: Nucleus
|
A0A075QQ08 | MVDEVEKPASLEESKTNTREVEEGAEEVIESDDTMSSLGNPCKAMKHPLEHSWTFWFDNPSGKSKQAAWGSSIRPIYTFSTVEDFWSVYNNIHHPSKLAVGADFHCFKNKIEPKWEDPVCASGGKWTMSFSRGKSDTCWLYTLLAMIGEQFDCGDEICGAVINVRVRQEKIALWTRNAANETAQVSIGKQWKEFLDYNDSIGFIFHDDAKKLDRAAKNRYSV | Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome . Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures . Key component of recessive resistance to potyviruses (Ref.2).
PTM: According to the redox status, the Cys-120-Cys-158 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA.
Sequence Mass (Da): 25217
Sequence Length: 222
Subcellular Location: Nucleus
|
O60573 | MNNKFDALKDDDSGDHDQNEENSTQKDGEKEKTERDKNQSSSKRKAVVPGPAEHPLQYNYTFWYSRRTPGRPTSSQSYEQNIKQIGTFASVEQFWRFYSHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKMPGRLGPQRLLFQNLWKPRLNVP | Function: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation. Acts as a repressor of translation initiation . In contrast to EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3), suggesting that it acts by competing with EIF4E and block assembly of eIF4F at the cap (By similarity). In P-bodies, component of a complex that promotes miRNA-mediated translational repression . Involved in virus-induced host response by mediating miRNA MIR34A-induced translational silencing which controls IFNB1 production by a negative feedback mechanism .
PTM: Ubiquitinated by ARIH1 . The consequences of ubiquitination are however unclear: according to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest . According to another report ubiquitination leads to its subsequent degradation .
Sequence Mass (Da): 28362
Sequence Length: 245
Subcellular Location: Cytoplasm
|
A0A3Q7FGP1 | MADELNKAALEEYKSSSVEDRGEEGEIVGESDDTASSLGKQITMKHPLEHSWTFWFDNPSGKSKQAAWGSSIRPIYTFSTAEDFWSVYNNIHHPSKLAVGADFHCFKNKIEPKWEDPVCANGGKWTMNFSRGKSDTCWLYTLLALIGEQFDYGDEICGAVINVRVRQEKIALWTRNAANETAQVSIGKQWKEFLDYNDTIGFIFHDDAKKLDRAAKNRYSV | Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses .
PTM: According to the redox status, the Cys-119-Cys-157 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA.
Sequence Mass (Da): 25104
Sequence Length: 221
Subcellular Location: Nucleus
|
Q5A7R7 | MLLSNLVIPLLATSATVSATFDVTSSLTKYAAFDFGVGDISIQKSASFSLINTFDCAFQGDINIEKDCEFLIASTAKALKLTFNNIFHKIENKGKWIVHTLESAAASTCNIIVKSFVNTGEIILAFKGHVLAPIINIAASHWVNHGCLHLFQEIKSISVAILGVVGGTIENHGTICLTNQLCKQVTKIIGSGCIALEKSSSFFISNSFLSIDAQHTFYLGEGNPTIQAQAVSLPQTFKVANFGANGSHKIGLNLPLLSITIAGKKGWSYDTKTGILTLTANGFISQKFDIGLGYDPSKFEVCTDNSVGIVSVIKGSIKYNGPCPHAGRPSVCQICPGVPTPPVITSSATAITSTQSKTTSSSSTSSIATTSTTSSKPKPTTVSTSSIASTTTPDGSYSTSFVTVTAETTKVVTITSCSNNACHPTTAPTGLTVVTLTTSDVKTVVTTYCPLTQTVTLGVTGTKTVDLGCPTGYFGYNGYIGKGVSIGHGGAAASASAGFQIGFDIFKNHHF | Function: GPI-anchored cell wall protein involved in cell wall organization, hyphal growth, as well as in host-fungal interaction and virulence.
PTM: O-glycosylated.
Sequence Mass (Da): 53359
Sequence Length: 511
Subcellular Location: Secreted
|
Q59XB0 | MLFTLSILSTLLFSTSISAIEITQNRVDHGTITTSIGDITIDSGAYWSIIDNSISTFIGNLDIKSNAGLYISSTISNLPLLVLLNSGSASITNDGIVSLDARTSTQGSSQFNLVGGSFENNGEFYLAASGAIPMTMGLTGKSWNNNGLIVAYQNERSSGSVKFGVIGQTITNKGQICLTNQVYQQTSKIDGSGCVTAKKNASIYISNVLDPQSVSTEQNYFLADDKSSIITQAVGFNTQVINVFGFGNGNKIGLTLPLKSGNGGQAYSYDSDSGVLSLSSGLFGQKFNIGPGYDSKLFSIVTDNSEGIPSVNNGAVSYSGPVPSQKSLPSACNVECKPVPNAPDDGSSSSSSVVSSTTSTASTDSASLSSTSGEESSASTTTTESSETSNTSSNASETNGSSTESETTGSATTSEASETINSSESSETSGASETSQSTGTSESSETESSVTESSETDSITATTSDTTSSGNDNSSVTSSSDASTDSITSETASSSSTPLSGDSSQVSSLTTGTSPDTIASFQTDSTSFGFGSGSPSSGAVQSSGVTNSTPNTGDVNTQSNTANIATSDNTATSTASNDTGVNTATATTTGTGTGPDNNNNNNNNNNNNNNNNNNNNNNNNNNTNNSGVSAADSKASGDISTVTASSTTLISVASVSSTYPIANESSSPSSSSSSSSSSSGTPGEVIPNANGSSKLSIGMTFMISGFATMFALFM | Function: GPI-anchored cell wall protein involved in cell wall organization, hyphal growth, as well as in host-fungal interaction and virulence.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Location Topology: Lipid-anchor
Sequence Mass (Da): 72110
Sequence Length: 714
Subcellular Location: Secreted
|
Q5A6U1 | MQLFQNILVSIALLTQIVFAIEITENKVDRGTVTLNLSDITIYPGASWSIIDNAYTSFVGKLDVRDGAGLYISSTSHLLALQVSLTALLHSITNNGVVSFDSRISRTSSSYDLRGVSFTNNGEMYFAASGEFSSPTALTSASWTNTGLLSFYQNQRTSGTVSLGMPLGSITNTGQVCLNNQVYEQTTQIKGSGCFTANGDSTIYISNVLLAVSPKQNFYLTDKGSSMIVQAVSTTQTFNVYGFGEGNKIGLTIPLMGNLWNSAYAYDTTSGILTLRNLLLEQKFNIGTGYDPSKFQVVTDSGSGIPSTILGSVAYYGRVPERTLPKSCQIPCKPIPEAPGTTPTQYTTTITKTNTAGNTVTESGVVNVSTDKGGSWFTTTSMFPALSTAPSTATVFSSDTIMSTVEPDTTELASLTDIPIETSSVEELLSVMSNWEISSAPTLSIETPVSSHHSSMQHSSFESSADINTVFSSESAFETASDYIVSTPSSISHSTMVPQSSVSALSVVSESLASAEPSFVVPSESFIFSASSAAPQPSSSTYSVSFTTQFETPSSAGPSLVTSVESNTELISSATQSSDIQTEFTSTWTTTNSDGSVVTESGIISQSGTSLTTLTTFQPATSLVVPPYSVIETEFTSTWTTTNSDSSVATESGVVSQSDTLLTTVTTFPPAPSAIVPEFTSPWKINTSIESSETLTVSASSYETVGESLAAATSSYLSSATVVVAPSESEINTSSSILNNEEIASAPVSDTTSIAEHHDGSLSMTTTEFVNSNSLPSSHSIVTATITSCNKSKCSESVVTYVSSVSCATITVGDSEKNISTVGNNVSSIVGDDVSNTQAITMATSTEGATTLTSVSGAKPSVANDATNSVHTTDYTTATTGVQNGSSLSIPSDIPIEISVITPTNSSSSAITIPYENGSNKESIENIKYLALVVFGLMMFM | Function: GPI-anchored cell wall protein involved in cell wall organization, hyphal growth, as well as in host-fungal interaction and virulence.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Location Topology: Lipid-anchor
Sequence Mass (Da): 98606
Sequence Length: 941
Subcellular Location: Secreted
|
Q18235 | MEDLNFEERGSTQIPASLQQHFSAKLGRQNELEKTPSRGGLGLVVNSSKTPGGKSLQSLASACKVPPSTKKNTIPIAFECYEDETDDQIADVATIKKTEKHPCSPIDTANRCETFDSLAADIEDDMLNLEDQDVVLSEDRPYGDVIDPAESEAEALAELGVEEWDSYPPIDPASRIGDDFNYVLRTEDFAEEGDVKLEETRHRTVIADIDEVKMSKAERNELFSMLADDLDSYDLLAEEANLPL | Function: Acts as a chaperone and as an inhibitor for separase sep-1 . Plays an essential role in maintaining chromosome cohesion prior to meiotic and mitotic anaphase, in cytokinesis and in organizing the spindle and the centrosome . Ubiquitination-dependent degradation at the onset of anaphase is likely to activate sep-1 resulting in the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes . Also required for cortical granule exocytosis .
PTM: Ubiquitinated by etc-1 likely at the onset of anaphase, resulting in its degradation.
Sequence Mass (Da): 27002
Sequence Length: 244
Subcellular Location: Cytoplasm
|
Q9LPU5 | MGYLFQETLSSNPKTPIVVDDDNELGLMAVRLANAAAFPMVLKAALELGVFDTLYAAASRTDSFLSPYEIASKLPTTPRNPEAPVLLDRMLRLLASYSMVKCGKALSGKGERVYRAEPICRFFLKDNIQDIGSLASQVIVNFDSVFLNTWAQLKDVVLEGGDAFGRAHGGMKLFDYMGTDERFSKLFNQTGFTIAVVKKALEVYEGFKGVKVLVDVGGGVGNTLGVVTSKYPNIKGINFDLTCALAQAPSYPGVEHVAGDMFVDVPTGDAMILKRILHDWTDEDCVKILKNCWKSLPENGKVVVIELVTPDEAENGDINANIAFDMDMLMFTQCSGGKERSRAEFEALAAASGFTHCKFVCQAYHCWIIEFCK | Function: Involved in indole glucosinolate biosynthesis. Catalyzes methoxylation reactions of the glucosinolate indole ring. Converts the hydroxy intermediates 4-hydroxy-indol-3-yl-methylglucosinolate (4OH-I3M) and 1-hydroxy-indol-3-yl-methylglucosinolate (1OH-I3M) to 4-methoxy-indol-3-yl-methylglucosinolate (4MO-I3M) and 1-methoxy-indol-3-yl-methylglucosinolate (1MO-I3M), respectively.
Sequence Mass (Da): 40869
Sequence Length: 373
Pathway: Secondary metabolite biosynthesis.
EC: 2.1.1.-
|
Q9P305 | MSEDLSPTSSRVDLSNPHGFTKEGVDLSKLSPQELKLYKMYGKLPSKKDLLRHKMQDRQYFDSGDYALKKAGVIKSDDVIVNNSSNNLPVTNPSGLRESIIRRRMSSSSGGDSISRQGSISSGPPPRSPNK | Function: Required for TORC1 to properly control gene expression and chronological life span. Plays an essential role in initiation of the G0 program by preventing the degradation of specific nutrient-regulated mRNAs via the 5'-3' mRNA decay pathway.
PTM: Phosphorylated by RIM15.
Sequence Mass (Da): 14395
Sequence Length: 131
Subcellular Location: Cytoplasm
|
Q08DK1 | MTCRGSPLAPLLLFSLHGVAASLEVSESPGSVQVARGQTAVLPCTFTTSAALINLNVIWMVIPLSNANQPEQVILYQGGQMFDGAPRFHGRVGFTGTMPATNVSIFINNTQLSDTGTYQCLVNNLPDRGGRNIGVTGLTVLVPPSAPHCQIQGSQDIGSDVILLCSSEEGIPRPTYLWEKLDNTLKLPPTATQDQVQGTVTIRNISALSSGLYQCVASNAIGTSTCLLDLQVISPQPRSIGLIAGAIGTGAVIIIFCIALILGAFFYWRSKNKEEEEEEIPNEIREDDLPPKCSSSAKAFHMEISSSENNTLTSSNTYNSRYWSSNPKAHRNTESFGHFGDLRQSFSLHSGNASVPAIYANGSHLAPAPHKTLVVTANRGSSLPAVSRSNGSVSRKARPPPVPSLHTHSYTVSQATLERIGAVPVMVPAQSRAGSLV | Function: Functions as a cell adhesion molecule through homophilic interaction. Stimulates cell growth (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 46530
Sequence Length: 437
Subcellular Location: Cell membrane
|
Q5DX21 | MTSQRSPLAPLLLLSLHGVAASLEVSESPGSIQVARGQPAVLPCTFTTSAALINLNVIWMVTPLSNANQPEQVILYQGGQMFDGAPRFHGRVGFTGTMPATNVSIFINNTQLSDTGTYQCLVNNLPDIGGRNIGVTGLTVLVPPSAPHCQIQGSQDIGSDVILLCSSEEGIPRPTYLWEKLDNTLKLPPTATQDQVQGTVTIRNISALSSGLYQCVASNAIGTSTCLLDLQVISPQPRNIGLIAGAIGTGAVIIIFCIALILGAFFYWRSKNKEEEEEEIPNEIREDDLPPKCSSAKAFHTEISSSDNNTLTSSNAYNSRYWSNNPKVHRNTESVSHFSDLGQSFSFHSGNANIPSIYANGTHLVPGQHKTLVVTANRGSSPQVMSRSNGSVSRKPRPPHTHSYTISHATLERIGAVPVMVPAQSRAGSLV | Function: Functions as a cell adhesion molecule through homophilic interaction. Stimulates cell growth.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 46120
Sequence Length: 431
Subcellular Location: Cell membrane
|
Q15GI3 | MTTGKGKILILGATGYLGKYMVKASISLGHPTYAYVMPLKKNSDDSKLQLLKEFESLGVTIFYGELSEHDKLVAVFKEVDIVISTLAVPQYLEQLKVIEAIKEAGNIKRFVPSEFGNEVDRVRALPRFQAVLDNKKKIRRATEAAGIPFTFVSANSLTAYFVDYLLHPRQKSEQVTIYGSGDAKAVLNYEEDVAAYTIKAADDPRAANRVLIIKPPKNIVSQLDLVSSWEKTTGSTLKMTHISEQEIIKLSESINFPENIHASILHNIFIAGAQLSFELTQDHDLEASELYPNYNYTSVDEYLKICLVNPPKPKLATYAQPST | Function: Involved in the biosynthesis of the floral volatile isoeugenol . Catalyzes the synthesis of the phenylpropene isoeugenol from coniferyl acetate . Phenylpropenes are the primary constituents of various essential plant oils . They are produced as antimicrobial and antianimal compounds, or as floral attractants of pollinators . Isoeugenol is a characteristic aromatic constituent of spices and a floral volatile compound .
Catalytic Activity: (E)-isoeugenol + acetate + NADP(+) = (E)-coniferyl acetate + NADPH
Sequence Mass (Da): 35992
Sequence Length: 323
Pathway: Aromatic compound metabolism; phenylpropanoid biosynthesis.
EC: 1.1.1.319
|
Q9KXR9 | MALPPLTPEQRAAALEKAAAARRERAEVKNRLKHSGASLHEVIKQGQENDVIGKMKVSALLESLPGVGKVRAKQIMERLGISESRRVRGLGSNQIASLEREFGSTGS | Function: A nucleoid-associated protein (NAP) that probably plays a role in chromosome compactation. Contributes to development and secondary metabolism, but is dispensable for growth and viability . Binds to the promoter region of a number of genes (including itself); multiple molecules of the protein bind to the DNA simultaneously, deletion alters the expression of about 30 genes (both up- and down-regulation occurs). Plays a role in controlling viability . Binds dsDNA without any obvious sequence specificity, in a concentration and length-dependent manner. Promotes supercoiling in a topoisomerase-dependent manner (counteracts TopA plasmid relaxation). Binds DNA as a monomer, contacting 8 base pairs via the phosphate backbone; each monomer can bind 2 DNA duplexes, allowing a bridging function . Alters DNA topology, constraining negative supercoils, possibly by DNA twist. Longer dsDNA binds more than one sIHF subunit .
Sequence Mass (Da): 11555
Sequence Length: 107
Domain: The N-terminus (up to residue 33) is important in DNA binding in solution but not in the crystal structures . The lid region binds the phosphate backbone of one DNA duplex, while the H2TH motif contacts another duplex .
Subcellular Location: Cytoplasm
|
P79693 | VMNLWPGVRLRVTEGWDEDGHHSEESLHYEGRAVDITTSDRDRNKYAMLARLAVEAGF | Function: Intercellular signal essential for a variety of patterning events during development.
PTM: The C-terminal domain displays an autoproteolysis activity and a cholesterol transferase activity. Both activities result in the cleavage of the full-length protein and covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-terminal fragment (N-product). The N-product is the active species in both local and long-range signaling, whereas the C-product has no signaling activity (By similarity).
Sequence Mass (Da): 6658
Sequence Length: 58
Domain: The indian hedgehog protein N-product binds calcium and zinc ions; this stabilizes the protein fold and is essential for protein-protein interactions mediated by this domain.
Subcellular Location: Cell membrane
|
Q14623 | MSPARLRPRLHFCLVLLLLLVVPAAWGCGPGRVVGSRRRPPRKLVPLAYKQFSPNVPEKTLGASGRYEGKIARSSERFKELTPNYNPDIIFKDEENTGADRLMTQRCKDRLNSLAISVMNQWPGVKLRVTEGWDEDGHHSEESLHYEGRAVDITTSDRDRNKYGLLARLAVEAGFDWVYYESKAHVHCSVKSEHSAAAKTGGCFPAGAQVRLESGARVALSAVRPGDRVLAMGEDGSPTFSDVLIFLDREPHRLRAFQVIETQDPPRRLALTPAHLLFTADNHTEPAARFRATFASHVQPGQYVLVAGVPGLQPARVAAVSTHVALGAYAPLTKHGTLVVEDVVASCFAAVADHHLAQLAFWPLRLFHSLAWGSWTPGEGVHWYPQLLYRLGRLLLEEGSFHPLGMSGAGS | Function: The C-terminal part of the indian hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (By similarity). Both activities result in the cleavage of the full-length protein into two parts followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Both activities occur in the reticulum endoplasmic (By similarity). Plays a role in hedgehog paracrine signaling . Associated with the very-low-density lipoprotein (VLDL) particles to function as a circulating morphogen for endothelial cell integrity maintenance .
PTM: Cholesterylation is required for N-product targeting to lipid rafts and multimerization.
Location Topology: Lipid-anchor
Catalytic Activity: cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]
Sequence Mass (Da): 45251
Sequence Length: 411
Domain: Binds calcium and zinc ions; this stabilizes the protein fold and is essential for protein-protein interactions mediated by this domain.
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
P97812 | MSPAWLRPRLRFCLFLLLLLLVPAARGCGPGRVVGSRRRPPRKLVPLAYKQFSPNVPEKTLGASGRYEGKIARSSERFKELTPNYNPDIIFKDEENTGADRLMTQRCKDRLNSLAISVMNQWPGVKLRVTEGWDEDGHHSEESLHYEGRAVDITTSDRDRNKYGLLARLAVEAGFDWVYYESKAHVHCSVKSEHSAAAKTGGCFPAGAQVRLENGERVALSAVKPGDRVLAMGEDGTPTFSDVLIFLDREPNRLRAFQVIETQDPPRRLALTPAHLLFIADNHTEPAAHFRATFASHVQPGQYVLVSGVPGLQPARVAAVSTHVALGSYAPLTRHGTLVVEDVVASCFAAVADHHLAQLAFWPLRLFPSLAWGSWTPSEGVHWYPQMLYRLGRLLLEESTFHPLGMSGAGS | Function: The C-terminal part of the indian hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (By similarity). Both activities result in the cleavage of the full-length protein into two parts followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Both activities occur in the reticulum endoplasmic (By similarity). Plays a role in hedgehog paracrine signaling. Associated with the very-low-density lipoprotein (VLDL) particles to function as a circulating morphogen for endothelial cell integrity maintenance (By similarity).
PTM: Cholesterylation is required for N-product targeting to lipid rafts and multimerization.
Location Topology: Lipid-anchor
Catalytic Activity: cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]
Sequence Mass (Da): 45485
Sequence Length: 411
Domain: Binds calcium and zinc ions; this stabilizes the protein fold and is essential for protein-protein interactions mediated by this domain.
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
Q5VWK5 | MNQVTIQWDAVIALYILFSWCHGGITNINCSGHIWVEPATIFKMGMNISIYCQAAIKNCQPRKLHFYKNGIKERFQITRINKTTARLWYKNFLEPHASMYCTAECPKHFQETLICGKDISSGYPPDIPDEVTCVIYEYSGNMTCTWNAGKLTYIDTKYVVHVKSLETEEEQQYLTSSYINISTDSLQGGKKYLVWVQAANALGMEESKQLQIHLDDIVIPSAAVISRAETINATVPKTIIYWDSQTTIEKVSCEMRYKATTNQTWNVKEFDTNFTYVQQSEFYLEPNIKYVFQVRCQETGKRYWQPWSSLFFHKTPETVPQVTSKAFQHDTWNSGLTVASISTGHLTSDNRGDIGLLLGMIVFAVMLSILSLIGIFNRSFRTGIKRRILLLIPKWLYEDIPNMKNSNVVKMLQENSELMNNNSSEQVLYVDPMITEIKEIFIPEHKPTDYKKENTGPLETRDYPQNSLFDNTTVVYIPDLNTGYKPQISNFLPEGSHLSNNNEITSLTLKPPVDSLDSGNNPRLQKHPNFAFSVSSVNSLSNTIFLGELSLILNQGECSSPDIQNSVEEETTMLLENDSPSETIPEQTLLPDEFVSCLGIVNEELPSINTYFPQNILESHFNRISLLEK | Function: Associates with IL12RB1 to form the interleukin-23 receptor. Binds IL23 and mediates T-cells, NK cells and possibly certain macrophage/myeloid cells stimulation probably through activation of the Jak-Stat signaling cascade. IL23 functions in innate and adaptive immunity and may participate in acute response to infection in peripheral tissues. IL23 may be responsible for autoimmune inflammatory diseases and be important for tumorigenesis.
PTM: Phosphorylated in response to IL23.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 71722
Sequence Length: 629
Subcellular Location: Cell membrane
|
Q13007 | MNFQQRLQSLWTLARPFCPPLLATASQMQMVVLPCLGFTLLLWSQVSGAQGQEFHFGPCQVKGVVPQKLWEAFWAVKDTMQAQDNITSARLLQQEVLQNVSDAESCYLVHTLLEFYLKTVFKNYHNRTVEVRTLKSFSTLANNFVLIVSQLQPSQENEMFSIRDSAHRRFLLFRRAFKQLDVEAALTKALGEVDILLTWMQKFYKL | Function: Multifunctional cytokine mainly produced by T-cells that plays a regulatory role in immune response, tissue homeostasis, host defense, and oncogenesis . Possesses antiviral functions and induces the type I intereferon response during influenza infection . Signals through two receptor complexes IL20RA/IL20RB or IL20RB/IL22RA1 . In turn, stimulates the JAK1-STAT3 and MAPK pathways and promotes the secretion of pro-inflammatory mediators including IL8 and MMP1 . Intracellularly, maintains endoplasmic reticulum homeostasis by restricting the eIF2alpha-CHOP pathway-mediated stress signal (By similarity). In addition, acts as a quality control mechanism for the ubiquitin proteasome system by alerting the cell to proteasome dysfunction through activation of PKR/EIF2AK2 (By similarity).
PTM: Glycosylated.
Sequence Mass (Da): 23825
Sequence Length: 206
Subcellular Location: Secreted
|
Q8NEV9 | MGQTAGDLGWRLSLLLLPLLLVQAGVWGFPRPPGRPQLSLQELRREFTVSLHLARKLLSEVRGQAHRFAESHLPGVNLYLLPLGEQLPDVSLTFQAWRRLSDPERLCFISTTLQPFHALLGGLGTQGRWTNMERMQLWAMRLDLRDLQRHLRFQVLAAGFNLPEEEEEEEEEEEEERKGLLPGALGSALQGPAQVSWPQLLSTYRLLHSLELVLSRAVRELLLLSKAGHSVWPLGFPTLSPQP | Function: Associates with EBI3 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. IL-27 has pro- and anti-inflammatory properties, that can regulate T-helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells, and that has diverse effects on innate immune cells. Among its target cells are CD4 T-helper cells which can differentiate in type 1 effector cells (TH1), type 2 effector cells (TH2) and IL17 producing helper T-cells (TH17). It drives rapid clonal expansion of naive but not memory CD4 T-cells. It also strongly synergizes with IL-12 to trigger interferon-gamma/IFN-gamma production of naive CD4 T-cells, binds to the cytokine receptor WSX-1/TCCR which appears to be required but not sufficient for IL-27-mediated signal transduction. IL-27 potentiate the early phase of TH1 response and suppress TH2 and TH17 differentiation. It induces the differentiation of TH1 cells via two distinct pathways, p38 MAPK/TBX21- and ICAM1/ITGAL/ERK-dependent pathways. It also induces STAT1, STAT3, STAT4 and STAT5 phosphorylation and activates TBX21/T-Bet via STAT1 with resulting IL12RB2 up-regulation, an event crucial to TH1 cell commitment. It suppresses the expression of GATA3, the inhibitor TH1 cells development. In CD8 T-cells, it activates STATs as well as GZMB. IL-27 reveals to be a potent inhibitor of TH17 cell development and of IL-17 production. Indeed IL27 alone is also able to inhibit the production of IL17 by CD4 and CD8 T-cells. While IL-27 suppressed the development of pro-inflammatory Th17 cells via STAT1, it inhibits the development of anti-inflammatory inducible regulatory T-cells, iTreg, independently of STAT1. IL-27 has also an effect on cytokine production, it suppresses pro-inflammatory cytokine production such as IL2, IL4, IL5 and IL6 and activates suppressors of cytokine signaling such as SOCS1 and SOCS3. Apart from suppression of cytokine production, IL-27 also antagonizes the effects of some cytokines such as IL6 through direct effects on T-cells. Another important role of IL-27 is its antitumor activity as well as its antiangiogenic activity with activation of production of antiangiogenic chemokines such as IP-10/CXCL10 and MIG/CXCL9. In vein endothelial cells, it induces IRF1/interferon regulatory factor 1 and increase the expression of MHC class II transactivator/CIITA with resulting up-regulation of major histocompatibility complex class II. IL-27 also demonstrates antiviral activity with inhibitory properties on HIV-1 replication.
PTM: O-glycosylated.
Sequence Mass (Da): 27493
Sequence Length: 243
Subcellular Location: Secreted
|
Q8K3I6 | MGQVTGDLGWRLSLLLLPLLLVQAGSWGFPTDPLSLQELRREFTVSLYLARKLLSEVQGYVHSFAESRLPGVNLDLLPLGYHLPNVSLTFQAWHHLSDSERLCFLATTLRPFPAMLGGLGTQGTWTSSEREQLWAMRLDLRDLHRHLRFQVLAAGFKCSKEEEDKEEEEEEEEEEKKLPLGALGGPNQVSSQVSWPQLLYTYQLLHSLELVLSRAVRDLLLLSLPRRPGSAWDS | Function: Associates with EBI3 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. IL-27 has pro- and anti-inflammatory properties, that can regulate T-helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells, and that has diverse effects on innate immune cells. Among its target cells are CD4 T-helper cells which can differentiate in type 1 effector cells (TH1), type 2 effector cells (TH2) and IL17 producing helper T-cells (TH17). It drives rapid clonal expansion of naive but not memory CD4 T-cells. It also strongly synergizes with IL-12 to trigger interferon-gamma/IFN-gamma production of naive CD4 T-cells, binds to the cytokine receptor WSX-1/TCCR which appears to be required but not sufficient for IL-27-mediated signal transduction. IL-27 potentiate the early phase of TH1 response and suppress TH2 and TH17 differentiation. It induces the differentiation of TH1 cells via two distinct pathways, p38 MAPK/TBX21- and ICAM1/ITGAL/ERK-dependent pathways. It also induces STAT1, STAT3, STAT4 and STAT5 phosphorylation and activates TBX21/T-Bet via STAT1 with resulting IL12RB2 up-regulation, an event crucial to TH1 cell commitment. It suppresses the expression of GATA3, the inhibitor TH1 cells development. In CD8 T-cells, it activates STATs as well as GZMB. IL-27 reveals to be a potent inhibitor of TH17 cell development and of IL-17 production. Indeed IL27 alone is also able to inhibit the production of IL17 by CD4 and CD8 T-cells. While IL-27 suppressed the development of pro-inflammatory Th17 cells via STAT1, it inhibits the development of anti-inflammatory inducible regulatory T-cells, iTreg, independently of STAT1. IL-27 has also an effect on cytokine production, it suppresses pro-inflammatory cytokine production such as IL2, IL4, IL5 and IL6 and activates suppressors of cytokine signaling such as SOCS1 and SOCS3. Apart from suppression of cytokine production, IL-27 also antagonizes the effects of some cytokines such as IL6 through direct effects on T-cells. Another important role of IL-27 is its antitumor activity as well as its antiangiogenic activity with activation of production of antiangiogenic chemokines such as IP-10/CXCL10 and MIG/CXCL9.
PTM: O-glycosylated.
Sequence Mass (Da): 26542
Sequence Length: 234
Subcellular Location: Secreted
|
P30740 | MEQLSSANTRFALDLFLALSENNPAGNIFISPFSISSAMAMVFLGTRGNTAAQLSKTFHFNTVEEVHSRFQSLNADINKRGASYILKLANRLYGEKTYNFLPEFLVSTQKTYGADLASVDFQHASEDARKTINQWVKGQTEGKIPELLASGMVDNMTKLVLVNAIYFKGNWKDKFMKEATTNAPFRLNKKDRKTVKMMYQKKKFAYGYIEDLKCRVLELPYQGEELSMVILLPDDIEDESTGLKKIEEQLTLEKLHEWTKPENLDFIEVNVSLPRFKLEESYTLNSDLARLGVQDLFNSSKADLSGMSGARDIFISKIVHKSFVEVNEEGTEAAAATAGIATFCMLMPEENFTADHPFLFFIRHNSSGSILFLGRFSSP | Function: Neutrophil serine protease inhibitor that plays an essential role in the regulation of the innate immune response, inflammation and cellular homeostasis . Acts primarily to protect the cell from proteases released in the cytoplasm during stress or infection. These proteases are important in killing microbes but when released from granules, these potent enzymes also destroy host proteins and contribute to mortality. Regulates the activity of the neutrophil proteases elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and kallikrein-3 . Acts also as a potent intracellular inhibitor of GZMH by directly blocking its proteolytic activity . During inflammation, limits the activity of inflammatory caspases CASP1, CASP4 and CASP5 by suppressing their caspase-recruitment domain (CARD) oligomerization and enzymatic activation . When secreted, promotes the proliferation of beta-cells via its protease inhibitory function .
Sequence Mass (Da): 42742
Sequence Length: 379
Domain: Reactive bond 1 is specific for reaction with chymotrypsin-like protease such as cathepsin G, chymotrypsin, chymase or granzyme H, while reactive bond 2 is specific for reaction with elastase-like protease such as neutrophil elastase, proteinase-3, pancreatic elastase or PSA.
Subcellular Location: Secreted
|
Q12905 | MRGDRGRGRGGRFGSRGGPGGGFRPFVPHIPFDFYLCEMAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQASILSLVTKINNVIDNLIVAPGTFEVQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTLEAVAALGNKVVESLRAQDPSEVLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRILSHGGFRKILGQEGDASYLASEISTWDGVIVTPSEKAYEKPPEKKEGEEEEENTEEPPQGEEEESMETQE | Function: Chromatin-interacting protein that forms a stable heterodimer with interleukin enhancer-binding factor 3/ILF3 and plays a role in several biological processes including transcription, innate immunity or cell growth . Essential for the efficient reshuttling of ILF3 (isoform 1 and isoform 2) into the nucleus. Together with ILF3, forms an RNA-binding complex that is required for mitotic progression and cytokinesis by regulating the expression of a cluster of mitotic genes. Mechanistically, competes with STAU1/STAU2-mediated mRNA decay . Also plays a role in the inhibition of various viruses including Japanese encephalitis virus or enterovirus 71.
PTM: Ubiquitinated at Lys-45 by CRBN with polyubiquitin chains by the CUL4-RING E3 ligase (CRL4-CRBN) and then degraded by the proteasome.
Sequence Mass (Da): 43062
Sequence Length: 390
Subcellular Location: Nucleus
|
Q7TP98 | MVSTHLTSTTLPDCYRSLIVNSELGSSALMDLNSPSFLYPLLHTPADKGTLCTYQAALGKVYASLEVIGVGDDKLQAVHGLNGGKPHRDILGSRITRPTGIKPLCLPRHILAYDWLAQSLLGIVIGSISLAYNELLMMEKLKGFRPFVPHIPFDFYLCEMAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTFLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRILSHGGFRKILGQEGDASYLASEISTWDGVIVTPSEKAYEKPPEKKEGEEEEENTEEPPQGEEEESMETQE | Function: Chromatin-interacting protein that forms a stable heterodimer with interleukin enhancer-binding factor 3/ILF3 and plays a role in several biological processes including transcription, innate immunity or cell growth. Essential for the efficient reshuttling of ILF3 (isoform 1 and isoform 2) into the nucleus. Together with ILF3, forms an RNA-binding complex that is required for mitotic progression and cytokinesis by regulating the expression of a cluster of mitotic genes. Mechanistically, competes with STAU1/STAU2-mediated mRNA decay. Plays also a role in the inhibition of various viruses including Japanese encephalitis virus or enterovirus 71.
PTM: Ubiquitinated at Lys-166 by CRBN with polyubiquitin chains by the CUL4-RING E3 ligase (CRL4-CRBN) and then degraded by the proteasome.
Sequence Mass (Da): 51381
Sequence Length: 463
Subcellular Location: Nucleus
|
Q91550 | MRPMRIFLNDDRHVMAKHSVVYPTQEELEAVQNMVSHTERALKAVSDWIDQQEKDCSGEQEQPMAEETETTEEGKDSEMKTGENPTRTLRGVMRVGLVAKGLLLKGDLDLELVLLCRDKPTISLLKRVADNLVLQFETVSEDKYEVIQNIREALIVVKSTKEPPLTLNIRLTSPLVREEMEKLSAGETLTVSDPPDVLDRHKCLAALASLRHAKWFQARANGLKSCVIVIRVLRDLCTRVPTWEPLRGWPLELLCEKAIGTANRPMGAGEALRRVLECLSSGILMPDGSGLYDPCEKDASDALEHLERQQREDITQSAQHALRLAAFGQLHKVLGMDPLPSKMPKKTKVETPVIDYTVQIPPSTTYAMPPLKRPIEEDGDDKSPSKKKKKIQKKDEKSEPPQVMNALMRLNQLKPGLQYKLISQTGPVHAPVFTMSVEVDDKTFEASGPSKKTAKLHVAVKVLQDMGLPTGMEEKEEGTDESEQKPVVQTPAQPDDSAEVDSAALDQAESAKQQGPILTKHGKNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGVKFQGSGSNKKVAKAYAALSALEKLFPDYTMYTEAPKKKRPPMMPRGGPKFAGKHNQGFGMMYSEVPPPQAMRGRGRGGMNRGRGRGRGGFGGGYMNSGGYGGGYGGNYNYQTSATAGYSQFYSNGGASGNAGGGGAGTGGYSSYYQGDSYSAPTPPKPFVNKKPPPPQQQQQQQPPPQHASNPPKPSYNQGYQGHQGGQQQQQQQQQQQTYNQNQYSNYGPPQKQKGGYNQGAQGAGSGGSYNYSNSYTGGTAPLGTAVERVQEGEAAALTQRQALVTTQAHTPAMVEPAVLRRTKVTRSLITIKVPPDRTTVALQIITSSLREELGVTAGIQNTT | Function: RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Within the nucleus, promotes circRNAs processing by stabilizing the regulatory elements residing in the flanking introns of the circularized exons (By similarity). Plays thereby a role in the back-splicing of a subset of circRNAs (By similarity). As a consequence, participates in a wide range of transcriptional and post-transcriptional processes (By similarity). Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs (By similarity). Upon viral infection, ILF3 accumulates in the cytoplasm and participates in the innate antiviral response (By similarity). Mechanistically, ILF3 becomes phosphorylated and activated by the double-stranded RNA-activated protein kinase/PKR which releases ILF3 from cellular mature circRNAs. In turn, unbound ILF3 molecules are able to interact with and thus inhibit viral mRNAs (By similarity). Has a cytoplasmic role early in development as part of a ribonucleoprotein (mRNP) complex which may regulate mRNA transport and/or translation. Following nuclear localization at the mid-blastula transition, acts as a transcription factor and binds the 5'-CCAAT-3' promoter sequence to regulate transcription of the gata2 gene as a subunit of the CCAAT box transcription factor (CBTF). Its role as an mRNP component negatively regulates its activity as a transcription factor by precluding its nuclear localization .
PTM: Phosphorylated. Phosphorylation affects nuclear translocation.
Sequence Mass (Da): 98121
Sequence Length: 897
Subcellular Location: Nucleus
|
Q12906 | MRPMRIFVNDDRHVMAKHSSVYPTQEELEAVQNMVSHTERALKAVSDWIDEQEKGSSEQAESDNMDVPPEDDSKEGAGEQKTEHMTRTLRGVMRVGLVAKGLLLKGDLDLELVLLCKEKPTTALLDKVADNLAIQLAAVTEDKYEILQSVDDAAIVIKNTKEPPLSLTIHLTSPVVREEMEKVLAGETLSVNDPPDVLDRQKCLAALASLRHAKWFQARANGLKSCVIVIRVLRDLCTRVPTWGPLRGWPLELLCEKSIGTANRPMGAGEALRRVLECLASGIVMPDGSGIYDPCEKEATDAIGHLDRQQREDITQSAQHALRLAAFGQLHKVLGMDPLPSKMPKKPKNENPVDYTVQIPPSTTYAITPMKRPMEEDGEEKSPSKKKKKIQKKEEKAEPPQAMNALMRLNQLKPGLQYKLVSQTGPVHAPIFTMSVEVDGNSFEASGPSKKTAKLHVAVKVLQDMGLPTGAEGRDSSKGEDSAEETEAKPAVVAPAPVVEAVSTPSAAFPSDATAEQGPILTKHGKNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGQKFQGAGSNKKVAKAYAALAALEKLFPDTPLALDANKKKRAPVPVRGGPKFAAKPHNPGFGMGGPMHNEVPPPPNLRGRGRGGSIRGRGRGRGFGGANHGGYMNAGAGYGSYGYGGNSATAGYSQFYSNGGHSGNASGGGGGGGGGSSGYGSYYQGDNYNSPVPPKHAGKKQPHGGQQKPSYGSGYQSHQGQQQSYNQSPYSNYGPPQGKQKGYNHGQGSYSYSNSYNSPGGGGGSDYNYESKFNYSGSGGRSGGNSYGSGGASYNPGSHGGYGGGSGGGSSYQGKQGGYSQSNYNSPGSGQNYSGPPSSYQSSQGGYGRNADHSMNYQYR | Function: RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Within the nucleus, promotes circRNAs processing by stabilizing the regulatory elements residing in the flanking introns of the circularized exons. Plays thereby a role in the back-splicing of a subset of circRNAs . As a consequence, participates in a wide range of transcriptional and post-transcriptional processes. Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs . Upon viral infection, ILF3 accumulates in the cytoplasm and participates in the innate antiviral response . Mechanistically, ILF3 becomes phosphorylated and activated by the double-stranded RNA-activated protein kinase/PKR which releases ILF3 from cellular mature circRNAs. In turn, unbound ILF3 molecules are able to interact with and thus inhibit viral mRNAs .
PTM: Phosphorylated at Thr-188 and Thr-315 by PKR in response to certain RNA viruses. This phosphorylation results in the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3 where it can bind to viral RNAs and impede viral replication.
Sequence Mass (Da): 95338
Sequence Length: 894
Subcellular Location: Nucleus
|
Q9AQ97 | KKNSILKKNHSWMNAIKNNFQVDDYESLIPNADLVINLTPDKEHHNVIKILQQLMKKNSCLGYSHGFNIVEFGEKIREDITVIMVAPKCPGTEVREEYNRGFGVPTLIAVHDANDIHKQGLEIAKAWSFSIGGHRAGVLESSFIAEVKSDLMGEQTILCGMLQTASLLCYEKLITDKHNPAYAAKLIQNGWETITESLKHGGITLMMDRLSNSSKIRAYNLSENIKKILAPLFQKHMDDIISGEFSAEMMKDWKNHDQKLLFWRQKIKNTSFETAPMYNKKIPEQEYYDHGILMVAILKSGIELSFEKMINAGIIAESAYYESLHELPLIANTIARKKLYEMNKVI | Cofactor: Binds 2 magnesium ions per subunit.
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH
Sequence Mass (Da): 39403
Sequence Length: 346
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4.
EC: 1.1.1.86
|
Q03UU4 | MTTKMFYDKDIDTTPLENKKIAVIGYGAQGHAQANNLRDSGFDVIMGLRPGKSFDSAKKDGFEVYSAAEATAQADVVMMETPDELQAAVWEKEVEPNLKAGSYLGFSHGFNIVYGLIKPNADINVMIIAPKGPGNIERRQFVEGGGIPSLYGVHQDPTGDTAEVAKAYAKGIGSGRAGILETTFEEETTEDLFGEQAVLCGGLTQLIEAGFNTLVEAGYSPELAYFETSHEMKMIVDLIFEGGFEKMRHDCSNTCEYGEMLNGPRIITEESKQGMRDVLKDIQDGTYAKKWLAEYNSGLKDLEKMRTEYKSGLYEQTGKKVRAMMPWISDADKYSTAADTEQFSAAK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH
Sequence Mass (Da): 38147
Sequence Length: 347
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4.
EC: 1.1.1.86
|
Q9PJ98 | MRSDAIKKGHLRAPNRSLLRACGLKDEDFDKPFIGVANSYIDIIPGHYFLNDYAKIIKDEIRKNGCVPFEFNTIGVDDGIAMGHEGMLYSLPSRELIANSIETVMNAHQLDALICIPNCDKITPGMLMGALRVNVPTIFVSGGPMASGVTKKGEKISLSSVFEAVGAYESKKISEEEFKDIECSACPSGGSCSGMFTANSMNTLCEAMGIALEGNGTILALSKEREELLRKAARRICEIALDERFKIRNIITQKAVRNAMVVDMAMGGSSNTVLHMLAISREAGVALDIKDLNFISSKVAHIAKIAPSLNSVYMDDIHKAGGVSAVMAEISSRQGHILELDALTITGESLKERLKNAKIKDENIIRKVDNAYSKVGGLAILFGNLAKQGCVIKTAGIIGERKFKGKAVCFNSQDEAIKGIIKGKVQKGNVCVIRYEGPKGGPGMQEMLSPTSLLMGMGLGADVALITDGRFSGATRGLSVGHISPEAAEGGLIGLLKDGDEIEIDVDAYTIHANVSEEEIAKRKKEFALPQKEVSSRWLRMYQKLVSNASKGAVLDME | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
Sequence Mass (Da): 60105
Sequence Length: 558
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4.
EC: 4.2.1.9
|
A7I7L0 | MTDLRSDTIRKGYERAPNRSLLRSLGVTDREIELPFIGIANAFNTIVPGHTHLRQLSDKVKEGIAAAGGVPFEFGVIGICDGIAMGHEGMRYSLPSRENIADSIELMVQAHRFDGLVCVGTCDKIVPGMLMAAVRTNIPTIVVTGGAMLPGSSGGKDLSLIDVFEGVGKVAAGTMEEDALKELECCAMPGCGSCQGLYTANTMACMTETMGMSLPGCAAVPAVEAAKLRIARESGEAIIPLVKKNSTARDIVTKKSLENAIRVDMALGGSTNTVLHLMAIATEAEIPLSLADFNRIADEIPHICHMLPAGPYSMQALYRAGGIPAVLKRLEKHLDDCPTVSGLSLYQVARNAMIKNEQVIRSLDAPVSPAGGLRILFGSLAPDGAVVKSAAVPKEIWKHTGPARVFESEEPAMAAILSRQIHEGDAVIIRNEGPRGGPGMPEMLSATSALMGVGYKNVVLITDGRFSGGTRGPCIGHVAPEAAVGGPIALVQDGDRIAVDLFMRTIDLLVDPEVLTSRKAAWKPVMRPVTGVLARYAKTVGQANLGAVLR | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
Sequence Mass (Da): 58026
Sequence Length: 550
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4.
EC: 4.2.1.9
|
Q58672 | MISDRVKKGLKRAPNRSLLKACGYTDEELERPFIGVVNSFTEVVPGHIHLRDIAEAVKKGIYANGGTAFEFNTMAICDGIAMGHEGMKYSLPSREIIADTVESMAKAHGFDGLVLIPSCDKIVPGMIMGAIRTGLPFIVVTGGPMFPGELRGKKYDLISVFEGVGACAAGKITEEELKEIEDIACPGAGSCAGLFTANTMACLTEAMGLSLPYCATSHATTAEKIRIAKRSGMRIVDLVRNNITPDKILTKEAFENAILVDLALGGSTNTTLHIPAIANEVKPKFITLDDFDRLSGEVPHIASLRPGGEHFIIDLHRAGGIPAVLKVLEEKIRKECLTVSGKTIGEIIKEVKYIDYSVIRPVDNPVHETAGLRILKGSLAPNGAVVKIGAVNPKMYKHEGPARVFDSEEEAVDAILGGDIERGDVVVIRYEGPAGGPGMREMLAPTSAICGMGLDDSVALITDGRFSGGSRGPCIGHVSPEAMAGGPIAIVEDGDIIKIDMINKKLDLALDEEEIKERLAKWKKPEPKVKKGYLARYAKLVSSADEGAVLRYD | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
Sequence Mass (Da): 59198
Sequence Length: 553
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4.
EC: 4.2.1.9
|
A7X4M5 | MRSDMIKKGDHQAPARSLLHATGALKSPTDMNKPFVAICNSYIDIVPGHVHLRELADIAKEAIREAGAIPFEFNTIGVDDGIAMGHIGMRYSLPSREIIADAAETVINAHWFDGVFYIPNCDKITPGMILAAMRTNVPAIFCSGGPMKAGLSAHGKALTLSSMFEAVGAFKEGSISKEEFLDMEQNACPTCGSCAGMFTANSMNCLMEVLGLALPYNGTALAVSDQRREMIRQAAFKLVENIKNDLKPRDIVTREAIDDAFALDMAMGGSTNTVLHTLAIANEAGIDYDLERINAIAKRTPYLSKIAPSSSYSMHDVHEAGGVPAIINELMKKDGTLHPDRITVTGKTLRENNEGKEIKNFDVIHPLDAPYDAQGGLSILFGNIAPKGAVIKVGGVDPSIKTFTGKAICFNSHDEAVEAIDNRTVRAGHVVVIRYEGPKGGPGMPEMLAPTSSIVGRGLGKDVALITDGRFSGATRGIAVGHISPEAASGGPIALIEDGDEITIDLTNRTLNVNQPEDVLARRRESLTPFKAKVKTGYLARYTALVTSANTGGVMQVPENLI | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
Sequence Mass (Da): 60022
Sequence Length: 562
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4.
EC: 4.2.1.9
|
P00894 | MRRILSVLLENESGALSRVIGLFSQRGYNIESLTVAPTDDPTLSRMTIQTVGDEKVLEQIEKQLHKLVDVLRVSELGQGAHVEREIMLVKIQASGYGRDEVKRNTEIFRGQIIDVTPSLYTVQLAGTSGKLDAFLASIRDVAKIVEVARSGVVGLSRGDKIMR | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 17977
Sequence Length: 163
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
|
P45260 | MRRILSVLLENESGALSRVVGLFSQRAFNIESLTVAPTDDPTLSRMTIEAVGDAQALEQIEKQLHKLVDVFKVVNLSEQEHIEREIVLAKVRAVGSSRDEIKRLADIFRGQIVDVTPKSYTIQLSGTNDKVDAFISALKEETTLLEIVRSGLISVSRGEKNIL | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 18087
Sequence Length: 163
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
|
Q02140 | MRRMIIAKLHNVTGIMNRFTAVLNRRQVNILSITAGVTESQDLTHTTFVIEVDHLDEVEQIIKQLNRLIDVIEVADITDLPHVEREVVLIKVSAPPTIRAEIFTMIEPFRVNVVDVNLENVTIQLTGDSAKIEALIDVVSPYGILNMARTGSAGFERG | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 17641
Sequence Length: 158
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
|
Q57625 | MVNIMEHRHVISALVLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDKILEQVIKQLNKLIDVIKVSELEEKKSVQRELCLIKIYAPTESAKSQVIQYTSIFRGNVVDLSPESLIVEITGSEDKINAFIDLVKPLGIKEMARTGITALARGPKILKPKS | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 19057
Sequence Length: 172
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
|
Q59499 | MSPQTHTLSVLVEAKPGVLARVAALFSRRGFNIESLAVGATEQKDMSRMTIVVSAEETPLEQITKQLNKLINVIKIVELEDGNSVSRELALIKVRADAGTRSQVIEAVNLFRAKVIDVSPEALTIEATGDRGKIEALLRVLEPSVSVRSSNREWCRCPGPRGIGTAK | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 18131
Sequence Length: 167
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
|
P65162 | MSPKTHTLSVLVEDKPGVLARVAALFSRRGFNIESLAVGATECKDRSRMTIVVSAEDTPLEQITKQLNKLINVIKIVEQDDEHSVSRELALIKVQADAGSRSQVIEAVNLFRANVIDVSPESLTVEATGNRGKLEALLRVLEPFGIREIAQSGMVSLSRGPRGIGTAK | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 18187
Sequence Length: 168
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
|
O33113 | MVGLPTHTLSVLVEDTPGVLARVAALFSRRGFNIESLAVGATECKTMSRMTIVVSAEETPLEQVTKQLHKLINVIKVVEQEADNSLSRELALIKVRAEAGTRSQVIEAVHLFRARVIDVSLESLTVEATGDCSKIEALLRVLEPFGVREIVQSGVVSLSRGPRGIGTVR | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 18284
Sequence Length: 169
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
|
A0QUX7 | MSNGTPTHTLSVLVEDKPGVLARVSSLFSRRGFNIQSLAVGATEQKDMSRMTIVVSVEDSPLEQITKQLNKLINVIKIVEQEEDNSVSRELALIKVRADATTRGQIIEAVNLFRAKVVDVSTESLTIEATGTPEKLEALLRVLEPYGIREIAQSGVVSVSRGPRGIGAAK | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 18395
Sequence Length: 170
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
|
Q9SMC2 | MEHIQTRTTLSQLSTLPSDKRLGAIRFKCLLVMKVEMINRIAGVFARRGYNIESLAVGLNKDKALFTIVVSGTERVLQQVMEQLQKLVNVIKVEDLSKEPQVERELMLIKISADPKYRAEVMWLVDVFRAKIVDISDQSLTIEVTGDPGKMVAVQRNLSKFGIREIARTGKIALRREKMGESAPFWRFSAASYPDLEGAMSAGTISRTIKRTPNGESMSMAEGDVYPVETDDNSGVSQVLDAHWGVLNDEDTSGLRSHTLSMLVNDTPGVLNIVTGVFARRGYNIQSLAVGHAEVEGLSRITTVVPGTDESVSKLVQQLYKLVDIHEVRDITHLPFAERELMLIKIAVNAAARRNVLDIASIFRAKAVDVSDHTITLELTGDLHKMVRLQRLLEPYGICEVARTDVWHWYVNQVWIRSTCEDIHTLCSLKSSNLRKIPALCGMCANVDD | Function: Regulatory subunit of acetohydroxy-acid synthase. Probably involved in feedback inhibition by branched-chain amino acids. Not involved in herbicide tolerance.
Sequence Mass (Da): 50113
Sequence Length: 449
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
Subcellular Location: Plastid
|
Q55141 | MKHTLSVLVEDEAGVLTRIAGLFARRGFNIESLAVGSAEQGDVSRITMVVPGDENTIEQLTKQLYKLVNVIKVQDITETPCVERELMLVKVSANAPNRAEVIELAQVFRARIVDISEDTVTIEVVGDPGKMVAILQMLAKFGIKEVARTGKIALVRESGVNTEYLKSLESKF | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 18871
Sequence Length: 172
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
|
O58045 | MGKFVEKLEKAIKGYTFDDVLLIPQATEVEPKDVDVSTRITPNVKLNIPILSAAMDTVTEWEMAVAMAREGGLGVIHRNMGIEEQVEQVKRVKRAERLIVEDVITIAPDETVDFALFLMEKHGIDGLPVVEDEKVVGIITKKDIAAREGKLVKELMTKEVITVPESIEVEEALKIMIENRIDRLPVVDERGKLVGLITMSDLVARKKYKNAVRDENGELLVAAAVSPFDIKRAIELDKAGVDVIVVDTAHAHNLKAIKSMKEMRQKVDADFIVGNIANPKAVDDLTFADAVKVGIGPGSICTTRIVAGVGVPQITAVAMVADRAQEYGLYVIADGGIRYSGDIVKAIAAGADAVMLGNLLAGTKEAPGKEVIINGRKYKQYRGMGSLGAMMKGGAERYYQGGYMKTRKFVPEGVEGVVPYRGTVSEVLYQLVGGLKAGMGYVGARNIRELKEKGEFVIITHAGIKESHPHDIIITNEAPNYPLEKF | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XMP
Sequence Mass (Da): 52933
Sequence Length: 486
Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
EC: 1.1.1.205
|
Q9KH33 | MARIIETSTGLDALTFDDVLLQPGHSEVMPGQTNIATRIAQDIELNVPILSAAMDTVTESRLAIAMAQAGGMGVIHRNLTPVQQAEEVRQVKKFESGMVVNPVTIGPDATLAEALSLDEGPRHFRASPVVEKSHRLVGILTNRDVRFASDPEQKIYELMTRENLVTVKDGVQQHEAKRLLHTHRIEKXLVVDADSRFVGLITVKDIEKSQLNPHASKDAQGRLRAAAAISVGDDGYERAERLIDAGVDLLVVDTAHGHSQRVLDAVTRVKKLSNSVRIMAGNVATYDGTRALIDAGADAVKVGIGPGSICTTRIVAGVGVPQLAAIMSAVQAAQDQNIPIIADGGIKFSGDLAKAIAAGASAAMIGSLLAGTDESPGEVYLYQGRSFKAYRGMGSVGAMARGSADRYFQAEVRDTLKLVPEGIEGXVPYKGPVSGVLHQLAGGLKAAMGYVGGADLKDFQERATFVRISGAGLRESHAHDVTITPRKARIIPAQAADR | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XMP
Sequence Mass (Da): 52838
Sequence Length: 498
Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
EC: 1.1.1.205
|
Q7UJL3 | MGASTRFRRQSGKVPYNSTAASVIIARFPHRITFGCPRPRGNENGMFDDKIGDLGVTFDDVLLQPRYSEVVPSEVDVSSQMTQRIRLQIPLISSPMDTVTESEMAIALAKEGGLGIVHKNLSVRRQTEEVLKVKRSANGIIVNPVTLNPAQKVSAAAELMDRANVSGIPIVEDDRTLAGILTRRDLRFLEDPDMPISQVMTRENLVTAVGNVTLAQAEKILTEKRVEKLLLIDEERKLTGLITIRDIDMMKRYPRACKDPQGRLRVGAAIGVGDYERAESLIGKGVDVLVVDSAHGHSRNVIETVREIKQNKSWDIDVVAGNVATAEGAADLIAAGADAVKVGIGPGSICTTRVISGIGVPQVTAILSAVKVAQEKNIPVIADGGIRFSGDITKAIAAGASTVMIGSLFAGLAESPGKMILYQGRTFKAYRGMGSMGAMVKGSSDRYRQKGTEAGKLVPEGVEGRVPFKGPLSDYAYQLVGGLRAGMGYVGTRTIEELRRDAKFIRVSAATVRENHPHDIAITQEAPNYSPDVHSGDAG | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XMP
Sequence Mass (Da): 57876
Sequence Length: 539
Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
EC: 1.1.1.205
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.