entry
stringlengths 6
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| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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A2XDA1
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PDS_ORYSI
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15-cis-phytoene desaturase, chloroplastic/chromoplastic (EC 1.3.5.5) (Phytoene dehydrogenase) (Phytoene desaturase)
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MDTGCLSSMNITGTSQARSFAGQLPTHRCFASSSIQALKSSQHVSFGVKSLVLRNKGKRFRRRLGALQVVCQDFPRPPLENTINFLEAGQLSSFFRNSEQPTKPLQVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKIAAWKDEDGDWYETGLHIFFGAYPNIQNLFGELGINDRLQWKEHSMIFAMPNKPGEFSRFDFPETLPAPLNGIWAILRNNEMLTWPEKVKFALGLLPAMVGGQAYVEAQDGFTVSEWMKKQGVPDRVNDEVFIAMSKALNFINPDELSMQCILIALNRFLQEKHGSKMAFLDGNPPERLCMPIVDHVRSLGGEVRLNSRIQKIELNPDGTVKHFALTDGTQITGDAYVFATPVDILKLLVPQEWKEISYFKKLEKLVGVPVINVHIWFDRKLKNTYDHLLFSRSSLLSVYADMSVTCKEYYDPNRSMLELVFAPAEEWVGRSDTEIIEATMQELAKLFPDEIAADQSKAKILKYHVVKTPRSVYKTIPDCEPCRPLQRSPIEGFYLAGDYTKQKYLASMEGAVLSGKLCAQSVVEDYKMLSRRSLKSLQSEVPVAS
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Converts phytoene into zeta-carotene via the intermediary of phytofluene by the symmetrical introduction of two double bonds at the C-11 and C-11' positions of phytoene with a concomitant isomerization of two neighboring double bonds at the C9 and C9' positions from trans to cis. Active with decylplastoquinone (DPQ) as substrate. Also active with other benzoquinones, which are strongly preferred over naphthoquinones as substrates.
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A2XFC1
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TOP6A_ORYSI
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DNA topoisomerase 6 subunit A3 (OsTOP6A3) (EC 5.6.2.2) (DNA topoisomerase 6 subunit A) (OsTOP6A) (Meiotic recombination protein SPO11-3)
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MSEKKRRGGAGAGAASGSASKKPRVSTAASYAESLRSKLRPDASILATLRSLASACSKSKPAGSSSSSSSASKALAAEDDPAASYIVVADQDSASVTSRINRLVLAAARSILSGRGFSFAVPSRAASNQVYLPDLDRIVLVRRESARPFANVATARKATITARVLSLVHAVLRRGIHVTKRDLFYTDVKLFGDQAQSDAVLDDVSCMLGCTRSSLHVVASEKGVVVGRLTFADDGDRIDCTRMGVGGKAIPPNIDRVSGIESDALFILLVEKDAAFMRLAEDRFYNRFPCIILTAKGQPDVATRLFLRRLKVELKLPVLALVDSDPYGLKILSVYMCGSKNMSYDSANLTTPDIKWLGVRPSDLDKYRVPEQCRLPMTDHDIKVGKELLEEDFVKQNEGWVKELETMLRTRQKAEIQALSSFGFQYLTEVYLPLKLQQQDWI
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Component of the DNA topoisomerase VI involved in chromatin organization and progression of endoreduplication cycles. Relaxes both positive and negative superturns and exhibits a strong decatenase activity (By similarity). May be involved in cell proliferation and stress tolerance. {ECO:0000255|HAMAP-Rule:MF_03164}.
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A2XFC8
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MPK5_ORYSI
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Mitogen-activated protein kinase 5 (MAP kinase 5) (EC 2.7.11.24) (Benzothiadiazole-induced MAP kinase 1) (MAP kinase 2) (Multiple stress-responsive MAP kinase 2) (OsBIMK1) (OsMAP1) (OsMAPK2) (OsMAPK5) (OsMPK3) (OsMSRMK2)
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MDGAPVAEFRPTMTHGGRYLLYDIFGNKFEVTNKYQPPIMPIGRGAYGIVCSVMNFETREMVAIKKIANAFNNDMDAKRTLREIKLLRHLDHENIIGIRDVIPPPIPQAFNDVYIATELMDTDLHHIIRSNQELSEEHCQYFLYQILRGLKYIHSANVIHRDLKPSNLLLNANCDLKICDFGLARPSSESDMMTEYVVTRWYRAPELLLNSTDYSAAIDVWSVGCIFMELINRQPLFPGRDHMHQMRLITEVIGTPTDDELGFIRNEDARKYMRHLPQYPRRTFASMFPRVQPAALDLIERMLTFNPLQRITVEEALDHPYLERLHDIADEPICLEPFSFDFEQKALNEDQMKQLIFNEAIEMNPNIRY
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Involved in disease resistance and abiotic stress tolerance signaling pathways.
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A2XID3
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AOC_ORYSI
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Allene oxide cyclase, chloroplastic (OsAOC) (EC 5.3.99.6)
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MAAAAPSRVSVRAAAPGQTGGFAKIRPQVVVAAAARSAGVSGRRARSVRASLFSPKPATPKDARPAKVQEMFVYEINERDRESPAYLRLSAKQTENALGDLVPFTNKLYSGSLDKRLGISAGICILIQHVPERNGDRYEAIYSFYFGDYGHISVQGPYLTYEESYLAVTGGSGVFEGAYGQVKLNQIVFPFKIFYTFYLKGIPDLPRELLCTPVPPSPTVEPTPAAKATEPHACLNNFTN
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Involved in the production of 12-oxo-phytodienoic acid (OPDA), a precursor of jasmonic acid (JA). Required for the production of JA in response to wounding. Necessary for flower and coleoptile development regulation by light, including blue (BL), red (RL) and far red (FR) lights. Involved in the auxin-mediated signaling pathway leading to growth stimulation. Essential for photodestruction of phyA upon activation by RL and FR. Implicated in responses to salt stress (NaCl). Confers resistance to incompatible strains of the blast fungus Magnaporthe grisea, jasmonic acid (JA) thus playing a significant role in the resistance to fungal infection. Implicated in riboflavin-induced resistance to the sheath blight Rhizoctonia solani. Required for Pseudomonas fluorescens-mediated JA-dependent induced systemic resistance (ISR). Confers some resistance, independently of the JA pathway but probably via OPDA accumulation, to brown planthopper (BPH, Nilaparvata lugens), a destructive, monophagous, piercing-sucking insect, mainly by reducing its feeding activity and survival rate. Triggers resistance to the chewing insect striped stem borer (SSB) Chilo suppressalis, to the root hemiparasite witchweed Striga hermonthica, and to the root feeder insect rice water weevil Lissorhoptrus oryzophilus, in a JA-dependent manner, by attenuating both the growth mass and growth rate of caterpillars.
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A2XKG2
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RH10_ORYSI
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DEAD-box ATP-dependent RNA helicase 10 (EC 3.6.4.13) (DEAD-box RNA helicase TOGR1) (Protein THERMOTOLERANT GROWTH REQUIRED1)
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MAKKKDVEVEELDEEVVAAAAAPAADGGEEQEAEPPARRPSTFAELGVVPELVAACDAMGWKEPTRIQAEAIPHALEGRDLIGLGQTGSGKTGAFALPIIQALLKQDKPQALFACVLSPTRELAFQIGQQFEALGSAIGLSCTVLVGGVDRVQQAVSLAKRPHIVVGTPGRLLDHLTDTKGFSLNKLKYLVLDEADKLLNVEFQKALDDILNVIPKERRTFLFSATMTNKVSKLQRACLRNPVKVEVASKYSTVDTLRQEFYFVPADYKDCFLVHVLNELPGSMIMIFVRTCESTRLLALTLRNLRFKAISISGQMSQDKRLGALNRFKTKDCNILICTDVASRGLDIQGVDVVINYDIPMNSKDYVHRVGRTARAGNTGYAVSLVNQYEAMWFKMIEKLLGYEIPDRKVDNAEIMILRERISDSKRIALTTMKEGGGHKKKRRKNEDDEEEEERNAPVSRKSKSFNKSRRR
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Has ATP-dependent RNA helicase activity in vitro. Acts as a thermosensitive RNA chaperone required for normal processing of pre-rRNA intermediates. Required for normal cell division at high temperatures. Required for a primary metabolism adaptation to high temperatures to support thermotolerant growth by regulating gene expression. Partially rescues the yeast rRNA helicase RRP3 mutant which has repressed cell proliferation at 38 degrees Celsius.
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A2XW02
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STRK1_ORYSI
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Salt tolerance receptor-like cytoplasmic kinase 1 (EC 2.7.12.1) (Receptor-like cytoplasmic kinase 154) (OsRLCK154)
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MFTGCGLFACVRRCDGGDVRKRGEAGAMSSRVAADPAGVEEEGSCKNVAAASARQLAWADVESVTGGFSSRVIGHGGFSTVYLASLSSSRLGAVKVHCSSERLHRAFRQELEVLLSLRHPHIVRLLGYCDERDEGVLVFEYAPNGDLHERLHCSEVAGGVASVLPWARRVAIAFQVAMALEYLHESRHPAVIHGDIKASNVLLDANMNAKLCDFGFAHVGFSATVGCRPSARAVMGSPGYVDPHLIRSGVATKKSDVYSFGVLLLELVTGKEAVCRDTGRRLTAAVGPMLSEGKVADVVDRRLGGEHDGAEAAVMAELAMQCIGDSPGLRPSMADVVRALQEKTSALASAVGSRLDRKMMF
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Acts probably as a dual specificity protein kinase (Probable). Regulates hydrogen peroxide (H(2)O(2)) homeostasis and improves salt tolerance by phosphorylating tyrosine residues of CATC thus activating its catalase activity. Promotes growth at the seedling stage and prevents grain yield loss under salt stress conditions (By similarity).
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A2Y5T7
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SNAT1_ORYSI
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Serotonin N-acetyltransferase 1, chloroplastic (OsSNAT1) (EC 2.3.1.87) (Nuclear shuttle protein-interacting protein homolog) (Probable acetyltransferase NSI) (EC 2.3.1.-)
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MASAASASASAVVTPSSFRCVPTASCGLGARGKAPAPRRLLHDHAQGKKRAAATWSLKAGLWDSLRSGFLKSNNSTETVEPPSAPIEEEEPLPEELVLLERTLADGSTEQIIFSSAGDVNVYDLQALCDKVGWPRRPLTKIAASLRNSYLVATLHSVTTPSKAEGEERKQLIGMARATSDHAFNATIWDVLVDPSYQGQGLGKALMEKVIRTLLQRDISNITLFADNKVVDFYKNLGFEADPQGIKGMFWYPRF
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Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin. Catalyzes in vitro the N-acetylation of tryptamine to produce N-acetyltryptamine, 5-methoxytryptamine to produce melatonin and tyramine to produce N-acetyltyramine (By similarity). Acetyltransferase required for geminivirus infection and systemic spread (By similarity).
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A2Z1C8
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CESA9_ORYSI
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Cellulose synthase A catalytic subunit 9 [UDP-forming] (EC 2.4.1.12) (OsCesA9)
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MEASAGLVAGSHNRNELVLIRGHEEPKPLRALSGQVCEICGDEVGRTVDGDLFVACNECGFPVCRPCYEYERREGTQNCPQCKTRYKRLKGSPRVPGDEDEEDIDDLEHEFNIDDEKQKQLQQDQDGMQNSHITEAMLHGKMSYGRGPDDGDGNSTPLPPIITGARSVPVSGEFPISNSHGHGEFSSSLHKRIHPYPVSEPGSAKWDEKKEVSWKERMDDWKSKQGIVAGGAPDPDDYDADVPLNDEARQPLSRKVSIASSKVNPYRMVIILRLVVLGFFLRYRILHPVPDAIPLWLTSIICEIWFAVSWILDQFPKWYPIDRETYLDRLSLRYEREGEPSLLSAVDLFVSTVDPLKEPPLVTANTVLSILAVDYPVDKVSCYVSDDGASMLTFESLSETAEFARKWVPFCKKFSIEPRAPEFYFSQKVDYLKDKVHPNFVQERRAMKREYEEFKVRINALVAKAQKVPAEGWIMKDGTPWPGNNTRDHPGMIQVFLGHSGGHDTEGNELPRLVYVSREKRPGFQHHKKAGAMNALIRVSAVLTNAPFMLNLDCDHYINNSKAIREAMCFLMDPQVGRKVCYVQFPQRFDGIDVHDRYANRNTVFFDINMKGLDGIQGPVYVGTGCVFRRQALYGYNPPKGPKRPKMVTCDCCPCFGRKKRKHGKDGLPEAVAADGGMDSDKEMLMSQMNFEKRFGQSAAFVTSTLMEEGGVPPSSSPAALLKEAIHVISCGYEDKTDWGLELGWIYGSITEDILTGFKMHCRGWRSVYCMPKRAAFKGSAPINLSDRLNQVLRWALGSVEIFFSRHSPLLYGYKNGNLKWLERFSYINTTIYPFTSLPLLAYCTLPAVCLLTGKFIMPPISTFASLFFIALFISIFATGILEMRWSGVSIEEWWRNEQFWVIGGVSAHLFAVVQGLLKVLAGIDTNFTVTSKATGDEDDEFAELYAFKWTTLLIPPTTLLILNIIGVVAGVSDAINNGSEAWGPLFGKLFFAFWVIVHLYPFLKGLMGRQNRTPTIVVIWSVLLASIFSLLWVRIDPFTIKARGPDVRQCGINC
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Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation (By similarity). Involved in the secondary cell wall formation.
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A2ZVI7
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CDPK1_ORYSJ
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Calcium-dependent protein kinase 1 (OsCDPK1) (OsCPK1) (EC 2.7.11.1)
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MGNRTSRHHRAAPEQPPPQPKPKPQPQQQQQQWPRPQQPTPPPAAAPDAAMGRVLGRPMEDVRATYTFGRELGRGQFGVTYLVTHKATGKRFACKSIATRKLAHRDDIEDVRREVQIMHHLTGHRNIVELRGAYEDRHSVNLIMELCEGGELFDRIIARGHYSERAAAALCREIVAVVHSCHSMGVFHRDLKPENFLFLSKSEDSPLKATDFGLSVFFKPGEHFKDLVGSAYYVAPEVLKRNYGAEADIWSAGVILYILLSGVPPFWAESEDGIFDAVLRGHIDFSSEPWPSISNGAKDLVKKMLRQDPKERLTSAEILNHPWIREDGEAPDKPLDITVISRMKQFRAMNKLKKVALKVVAENLSDEEITGLKEMFRSLDTDNSGTITLEELRSGLPKLGTKISESEIRQLMEAADVDGNGTIDYAEFISATMHMNRLEKEDHILKAFEYFDKDHSGYITVDELEEALKKYDMGDDKTIKEIIAEVDTDHDGRINYQEFVAMMRNNNPEIAPNRRRMF
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May play a role in signal transduction pathways that involve calcium as a second messenger.
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A3BF39
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HMA2_ORYSJ
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Cadmium/zinc-transporting ATPase HMA2 (EC 7.2.2.12) (EC 7.2.2.21) (Protein HEAVY METAL ATPASE 2) (OsHMA2)
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MAAEGGRCQKSYFDVLGICCPSEVPLVEKLLQPLEGVQKVTVIVPSRTVIVVHDVDAISQSQIVKALNQARLEASVRAYGNGSEKITNKWPSPYVLLCGLLLVVSLFEHFWHPLKWFALVAAAAGLPPIVLRSIAAIRRLTLDVNILMLIAVAGAIALKDYSEAGFIVFLFTTAEWLETRASHKATAGMSALMSMAPQKAILAETGEVVAARDVKVNTVIAVKAGEVIPIDGVVVDGRSEVDESTLTGESFPVSKQPDSQVWAGTLNIDGYIAVRTTAMADNSAVAKMARLVEEAQNSRSSTQRLIDTCAKYYTPAVVVMAGSVAAIPAIAKAHNLKHWFQLALVLLVSACPCALVLSTPIATFCALLRAARTGLLIKGGDVLESLASIKVAAFDKTGTITRGEFSVEEFQPVGERVSLQQLLYWVSSVESRSSHPMASVLVDYAQSKSVEPKSENVSEFQIYPGEGIYGEIDGAGIYIGNKRILSRASCETVPDMKDMKGVTIGYVACNNELIGVFTLSDACRTGSAEAIKELRSLGIKSVMLTGDSSAAATYAQNQLGNILAEVHAELLPEDKVRIVGELKEKDGPTLMVGDGMNDAPALAKADVGVSMGVSGSAVAMETSHVALMSNDIRRIPKAVRLARRTHRTIIVNIIFSVITKLAIVGLAFAGHPLIWAAVLADVGTCLLVIMYSMLLLREKDSRKAKKCAASHHGSPKKCCSSSHHGSHAKKNHGVSHHCSDGPCKSMVSCKESSVAKNACHDHHHEHNHHEEPAHKHSSNQHGCHDHSHGHSNCKEPSNQLITNKHACHDGHNHCADTSNLHDTKKHDCHGHEHSTCKEELNALPPTNDHACHGHEHSHCEEPVALHSTGEHACHEHEHEHIHCDEPIGSHCADKHACHDHEQVHEHHCCDEQQTPHTADLHPCHDHDHDNLEVEEVKDCHAEPPHHHNHCCHEPHDQVKNDTHPVQEHSISIEESSDHHEHHHNEEHKAEDCGHHPKPKDCAPPPTDCISRNCCSNTSKGKDICSSLHRDHHTSQASRCCRSYVKCSRPSRSCCSHSIVKLPEIVVE
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Zinc/cadmium transporter that plays an essential role in promoting translocation of zinc and cadmium from roots to shoots. May control cadmium loading into xylem. In roots, transports zinc and cadmium from the apoplast to the symplast to facilitate translocation via the phloem. In nodes, functions to load zinc and cadmium to the phloem for the preferential distribution to the upper nodes and panicles.
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A3BLS0
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GH38_ORYSI
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Indole-3-acetic acid-amido synthetase GH3.8 (EC 6.3.2.-) (Auxin-responsive GH3-like protein 8) (OsGH3-8)
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MAVMTDVSTTGTALRTPAAGAVKEGDVEKLRFIDEMTTNVDAVQERVLGEILGRNAGTEYLTKCGLDGATDRAAFRAKVPVVSYDDLQPYIQRIANGDRSPILSTHPVSEFLTSSGTSAGERKLMPTIMDELDRRQLLYSLLMPVMNLYVPGLDKGKGLYFLFVKSETKTPGGLTARPVLTSYYKSDHFKNRPYDPYHNYTSPTAAILCADAFQSMYAQMVCGLCQRNDVLRLGAVFASGLLRAIRFLQLNWEQLADDIESGELTPRVTDPSVREAVAAILLPDPELAKLIRAECSKGDWAGIITRVWPNTKYLDVIVTGAMAQYIPTLEFYSGGLPMACTMYASSECYFGLNLRPMCDPSEVSYTIMPNMGYFEFLPVDETGAASGDATQLVDLARVEVGREYELVITTYAGLNRYRVGDVLRVTGFHNAAPQFRFVRRKNVLLSIESDKTDEAELQRAVERASALLRPHGASVVEYTSQACTKRIPGHYVIYWELLTKGAGATVVDADTLGRCCLEMEEALNTVYRQSRVADGSIGPLEIRVVRPGTFEELMDYAISRGASINQYKVPRCVTFPPIVELLDSRVVSSHFSPALPHWTPARRSE
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Catalyzes the synthesis of indole-3-acetic acid (IAA)-amino acid conjugates, providing a mechanism for the plant to cope with the presence of excessive free auxin. Produces more IAA-Asp levels than IAA-Ala levels in vitro. May participate in the activation of disease resistance by preventing the accumulation of free IAA, which reduces the expression of a group of auxin-responsive genes encoding expansins that control cell wall loosening and expansion. Contributes to late events in stamen and carpel differentiation, and influences floret fertility.
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A3BMZ5
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BGL26_ORYSJ
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Beta-glucosidase 26 (Os7bglu26) (EC 3.2.1.21)
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MRKFIAALRLALAAAAHLLLTLPPAQCYWLNPEIYDAGGLSRRAFPEGFVFGTAASAYQVEGMAKQGGRGPSIWDAFIEKPGTIPNNATADVTVDEYHRYKEDVNIMKNMGFDAYRFSISWSRIFPNGTGMVNQEGVDYYNRLIDYMVKKGIKPYANLYHYDLPLALHEQYLGWLSPNIVEAFADYADFCFQTFGDRVKDWFTFNEPRCVAALGYDNGFHAPGRCSGCDAGGNSTTEPYLAAHHLILSHAAAVKRYREKYQLYQKGRIGILLDFVWYEPFSDSNADRAAAQRARDFHLGWFLDPIIHGRYPYSMLEIVKDRMPTFSDEESRMVKDSIDYVGINHYTSFYMKDPGPWNLTPTSYQDDWHVGFAYERNGVPIGAQANSYWLYIVPWGINKAVTYVKETYGNPTMILSENGMDQPGNVSITQGVHDTVRIRYYRNYITELKKAIDDGAKVIGYFAWSLLDNFEWRLGYTSRFGIVYVDYKTLKRYPKDSAFWFKNMLSSKKRN
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Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-arabinoside, cello-oligosaccharides, laminari-oligosaccharides and sophorose.
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A3BV95
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BCL1_ORYSJ
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Basic helix-loop-helix protein 80 (OsbHLH080) (Protein BC-like 1) (OsBC1-like1) (OsBCL1)
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MADFSPHHSLLLKATAAGAAIATTNDPNISSFFLYNHSHGSQAPQPANAAAAAIVEDASLESSVSAVLDTSPSVDRKRKAAEDSAHSKDSCKDGKSRRGKKASKEVEEKSTTEDEPPKGYIHVRARRGQATDSHSLAERVRRERISERMRMLQALVPGCDKVTGKALILDEIINYVQSLQNQVEFLSMRIASMSPVLYGFGMDSDGLHDQKIGGMFQEALAMPNPVLNQSSPAPSQAIMDTTSTTSYSLQSQHGAISFSQDNGSYLMQAVGEPRQQEMLNQLVFNNMCSFQ
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Together with BCL2, positive regulator of cell elongation at least partially through increased gibberellic acid (GA) biosynthesis.
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A3CYJ4
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FADB_SHEB5
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MIYQSPTIQVELLEDNIAKLCFNAPGSVNKFDRETLTSLDAALDSIKQDSNIKALVLTSSKDTFIVGADITEFLGLFAQDDAVLLSWVEQANAVFNKLEDLPFPTASAIKGFALGGGCETILATDFRIADTTAKIGLPETKLGIIPGFGGTVRLPRVIGADNALEWITTGKDQRAEDALKVGAVDAVVAPQALEAAAIQMLKDAVAEKLDWQARRNRKLSALTLPKLEAMMSFTTAKGMVFAVAGKHYPAPMAAVSVIEQASTKGRAEALQIEHQAFIKLAKTDVAKALIGIFLNDQFVKGKAKKAGKLAKEVNNAAVLGAGIMGGGIAYQSASKGTPIVMKDIAQPALDLGLNEAAKLLSAQVARGRSTPEKMAKVLNNITPSLDYAAIKHSDVVVEAVVEHPKIKAQVLAEVEGYVSEDAIIASNTSTISINLLAKSMKKPERFCGMHFFNPVHKMPLVEIIRGEHSSEETIASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFNGLLAEGGDFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMAEGFPDRMGKSGTDAIDVMFENKRLGQKNGKGFYVYSVDSRGKPKKDVDPTSYGLLKDAFGELKAFEADDIIARTMIPMIIETVRCLEEGIVASPAEADMGLVYGLGFPPFRGGVFRYLDTMGVANFVALADKYAHLGGLYQVTDAMRTLAANNGSYYQA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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A3DD66
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ENG1_ACET2
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Glucan endo-1,3-beta-D-glucosidase (Endo-1,3-beta-glucanase) (EC 3.2.1.39) (CtLam81A) (Laminarinase)
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MPPGAKVPQAEIYKTSNLQGAVPTNSWESSILWNQYSLPIYAHPLTFKFKAEGIEVGKPALGGSGIAYFGAHKNDFTVGHSSVYTFPDARADKISDFAVDAVMASGSGSIKATLMKGSPYAYFVFTGGNPRIDFSGTPTVFYGDSGSQCLGVTINGVNYGLFAPSGSKWQGIGTGTITCILPAGKNYFSIAVLPDNTVSTLTYYKDYAYCFVTDTKVEWSYNETESTLTTTFTAEVSVKEGTNKGTILALYPHQWRNNPHILPLPYTYSTLRGIMKTIQGTSFKTVYRYHGILPNLPDKGTYDREALNRYINELALQADAPVAVDTYWFGKHLGKLSCALPIAEQLGNISAKDRFISFMKSSLEDWFTAKEGETAKLFYYDSNWGTLIGYPSSYGSDEELNDHHFHYGYFLHAAAQIALRDPQWASRDNWGAMVELLIKDIANWDRNDTRFPFLRNFDPYEGHSWASGHAGFADGNNQESSSEAINAWQAIILWGEATGNKTIRDLGIYLYTTEVEAVCNYWFDLYKDIFSPSYGHNYASMVWGGKYCHEIWWNGTNSEKHGINFLPITAASLYLGKDPNYIKQNYEEMLRECGTSQPPNWKDIQYMYYALYDPAAAKNMWNESIVPEDGESKAHTYHWICNLDSLGLPDFSVTADTPLYSVFNKNNIRTYVVYNASSSAKKVTFSDGKVMTVGPHSMAVSTGSESEVLAGDLNGDGKINSTDISLMKRYLLKQIVDLPVEDDIKAADINKDGKVNSTDMSILKRVILRNYPL
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Cleaves internal linkages in 1,3-beta-glucan. May contribute to plant biomass degradation (By similarity).
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A3DH67
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GUNS_ACET2
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Cellulose 1,4-beta-cellobiosidase (reducing end) CelS (EC 3.2.1.176) (Cellobiohydrolase CelS) (Cellulase SS) (Endo-1,4-beta-glucanase) (Endoglucanase SS) (EGSS) (Exocellulase)
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MVKSRKISILLAVAMLVSIMIPTTAFAGPTKAPTKDGTSYKDLFLELYGKIKDPKNGYFSPDEGIPYHSIETLIVEAPDYGHVTTSEAFSYYVWLEAMYGNLTGNWSGVETAWKVMEDWIIPDSTEQPGMSSYNPNSPATYADEYEDPSYYPSELKFDTVRVGSDPVHNDLVSAYGPNMYLMHWLMDVDNWYGFGTGTRATFINTFQRGEQESTWETIPHPSIEEFKYGGPNGFLDLFTKDRSYAKQWRYTNAPDAEGRAIQAVYWANKWAKEQGKGSAVASVVSKAAKMGDFLRNDMFDKYFMKIGAQDKTPATGYDSAHYLMAWYTAWGGGIGASWAWKIGCSHAHFGYQNPFQGWVSATQSDFAPKSSNGKRDWTTSYKRQLEFYQWLQSAEGGIAGGATNSWNGRYEKYPAGTSTFYGMAYVPHPVYADPGSNQWFGFQAWSMQRVMEYYLETGDSSVKNLIKKWVDWVMSEIKLYDDGTFAIPSDLEWSGQPDTWTGTYTGNPNLHVRVTSYGTDLGVAGSLANALATYAAATERWEGKLDTKARDMAAELVNRAWYNFYCSEGKGVVTEEARADYKRFFEQEVYVPAGWSGTMPNGDKIQPGIKFIDIRTKYRQDPYYDIVYQAYLRGEAPVLNYHRFWHEVDLAVAMGVLATYFPDMTYKVPGTPSTKLYGDVNDDGKVNSTDAVALKRYVLRSGISINTDNADLNEDGRVNSTDLGILKRYILKEIDTLPYKN
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This enzyme catalyzes the exohydrolysis of 1,4-beta-glucosidic linkages in cellulose with a preference for amorphous or crystalline cellulose over carboxymethyl cellulose.
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A3DIH0
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IABF_ACET2
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Intracellular exo-alpha-(1->5)-L-arabinofuranosidase (ABF) (EC 3.2.1.55) (Intracellular arabinan exo-alpha-(1->5)-L-arabinosidase) (Arabinosidase)
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MKKARMTVDKDYKIAEIDKRIYGSFVEHLGRAVYDGLYQPGNSKSDEDGFRKDVIELVKELNVPIIRYPGGNFVSNYFWEDGVGPVEDRPRRLDLAWKSIEPNQVGINEFAKWCKKVNAEIMMAVNLGTRGISDACNLLEYCNHPGGSKYSDMRIKHGVKEPHNIKVWCLGNEMDGPWQVGHKTMDEYGRIAEETARAMKMIDPSIELVACGSSSKDMPTFPQWEATVLDYAYDYVDYISLHQYYGNKENDTADFLAKSDDLDDFIRSVIATCDYIKAKKRSKKDIYLSFDEWNVWYHSNNEDANIMQNEPWRIAPPLLEDIYTFEDALLVGLMLITLMKHADRIKIACLAQLINVIAPIVTERNGGAAWRQTIFYPFMHASKYGRGIVLQPVINSPLHDTSKHEDVTDIESVAIYNEEKEEVTIFAVNRNIHEDIVLVSDVRGMKDYRLLEHIVLEHQDLKIRNSVNGEEVYPKNSDKSSFDDGILTSMLRRASWNVIRIGK
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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 small oligosaccharides as alpha-(1->5)-linked arabinobiose/arabinotriose, but does not display significant activity against linear non-substituted arabinan. It is also highly efficient in the cleavage of alpha-(1->3)-linked arabinoside of xylobiose and of the alpha-(1->3)-linked arabinoside decorations of polymeric wheat arabinoxylan. It exhibits very low activity against sugar beet arabinan.
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A3DIJ8
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3PASE_ACET2
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Inorganic triphosphatase (PPPase) (EC 3.6.1.25) (Adenosinetriphosphatase) (ATPase) (Polyphosphatase)
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MGKEIEKKFIVSGDAYKSLAKGVLYRQGYIFFDKDKSVRVRVFNDKGYLTVKGTSTGISRLEYEYEIPVGEANEILEYLCEKPVIEKLRYKFQFEGFTWEVDEFLGENEGLVIAEIELPDENAVFKKPDWIGREVTGDPRYLNSNLVKNPYKNFKE
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Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes vigorously the hydrolysis of inorganic triphosphate (PPPi), however it can also catalyze the hydrolysis of ATP to ADP and phosphate. It can use ribonucleotides such as GTP, CTP, or UTP and deoxynucleotides such as dATP, dGTP, dCTP, and dTTP.
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A3DP49
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DNLI_STAMF
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DNA ligase (EC 6.5.1.7) (Polydeoxyribonucleotide synthase [ATP/ADP])
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MPFRELADTFERIEIITSRTQMTVLLVNLFKKTPPEIIDKVVYLLQGRLWPDWKGLPELGVGEKMLIKAIALATQSTESEVESLYKSLGDLGKAAEKLKAIYEEKLKKGAMSILAFVPVKRELTVSQVYETLSRVALATGEGSRDIKLKLLAGLLSDASPKEAKYIIRFVEGRLRLGIGDATIMDALAIVYGGGAHARPIVERAYNLRADLGHIAKILATQGLNALKGIKPQVGIPIRPMLAERLNNPVEILKKVGGIAFVEYKYDGERAQIHKLGDKIWIYSRRLENITHQYPDVVDYARKYIKANEAIVEGEIVAYDPDTGELRPFQELMHRKRKHDIHIAIKEVPVKVYLFDLLYVDGEDYTLKPLPERRAKLVEIIEQTETFQIAEYIRTNNPDELEKFFLKAIEDGAEGVMIKALHKNAIYQAGTRGWLWIKYKRDYKSEMIDTVDLVVIGAFYGRGRRGGKYGALLMASYNPDKDVFESVCKVGSGFKDEDIDKLPEMLKPYIIEHKHPRVVARMKPDVWVTPALVAEIIGAELTLSPLHTCCLDIIKPGVGISIRFPRFIRWRPDKGPEDATTSQELLEMYKRQLKKLSE
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DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Can use both ATP and ADP.
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A3DRP1
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M2_I96A2
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Matrix protein 2 (Proton channel protein M2)
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MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGIVHLILWIIDRLFFKCIYRIFKHGLKRGPSTEGVPESMREEYREEQQNAVDADEGHFVSIELE
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Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
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A3EWL3
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REV1_ARATH
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DNA repair protein REV1 (AtREV1) (EC 2.7.7.-) (Rev1-like terminal deoxycytidyl transferase)
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MKRSLGSNSSNNSGSGSNKKSKKNNNPSNQKTLGAAWGAASSRSSFRSSPFSDFGSYMEVKNRKLQNQFETEASAASRGVSGSEKLIFQGVSIFVDGFTIPSHQELKGYMMKYGGRFENYFSRRSVTHIICSNLPDSKVKNLRTFSRGLPVVKPTWIVDSISANRLLGWVPYQLDQLNDTQPKLSAFFAPRSHLTPQMASPVTSFQPDTGYSEAEEGSSIRADDSEEARDHIDDEIDGVYIENTTPELTEQTGTGDLKSSEMNAEGLGNYDIEEKEVSSELQSTTNLHSTSDNKSVHANGKNGGKSIATAAGSSTRRHSTLEDPNFVENYFKNSRLHFIGTWRNRYRKRFHGSSNGLKWADSGQNTAEMAKKSTIIHIDLDCFFVSVVIKNRLELHDKPVAVCHSDNPKGTAEISSANYPARAYGVKAGMFVRHAKDLCPQLVIVPYNFEAYEEVADQFYDILHRHCRKVQALSCDEAFLDVSDLSDVETEVLASTIRNEILETTGCSASAGIGGTMLMARLATRVAKPAGQLYISAEKVEEFLDQLPVGTLPGVGSVLKEKLVKQNIQTCGQLRLISKDSLQKDFGVKTGEMLWSYSRGLDLRSVTAVQESKSIGAEVNWGVRFRDQQDVFILVQHFLQCLCKEVSLRLQGCEMIGRTFTLKIKKRKKDAEEPTKYMGCGDCDNLSRSITVPAATDDIEVLQRISKKLFGSFCLDVKEVRGVGLQVSKLDSADPSNKGSRTLKSWLSSAPAVVQIEQDDNVFAAKVRENSDCNRPVTGGVSRLRESNSEESSIQSGDTNSSLPPMCYLDMEVLENLPPELLSELDGTYGGKLFELIEKKRGKRRINCNSPHVSLDGTAASIKELKSLSVKIHGLSTSGEKEYKEPYVPHPSIARTSNQHTIEMTDLLPSSLSQVDVSVLQELPEELRADVLGAFPSHRRQQSSSDVPKETCKKQDEEPIDLKGTENEIGLSFSSLWFGNPPLWTEKFKVSGNCTMEKLSAIYFKVAQSRPMLSLVLQHAISEMSSFPDAASASDLDKAIYDVCELLKQYINLKVGGDIEEIYLCFRLLKRLAARSQLFLQVYEILSPFIQASISEHYGGSLSIP
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Deoxycytidyl transferase involved in DNA repair and translesion synthesis (TLS). Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. Mediates also the insertion of dTMP or dGMP when the opposite base is G, and, with a low efficiency, dGMP insertions opposite G, T, and C, dAMP insertions opposite G, A, and T, and dTMP insertion opposite A. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents (e.g. UV and gamma ray), mostly via G to T transversions, and of spontaneous mutations in somatic cells. Confers resistance to ultraviolet-B (UV-B) and various DNA cross-linkers (e.g. mitomycin C MMC and cisplatin). Promotes stem growth.
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A3EX94
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SPIKE_BCHK4
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Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
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MTLLMCLLMSLLIFVRGCDSQFVDMSPASNTSECLESQVDAAAFSKLMWPYPIDPSKVDGIIYPLGRTYSNITLAYTGLFPLQGDLGSQYLYSVSHAVGHDGDPTKAYISNYSLLVNDFDNGFVVRIGAAANSTGTIVISPSVNTKIKKAYPAFILGSSLTNTSAGQPLYANYSLTIIPDGCGTVLHAFYCILKPRTVNRCPSGTGYVSYFIYETVHNDCQSTINRNASLNSFKSFFDLVNCTFFNSWDITADETKEWFGITQDTQGVHLYSSRKGDLYGGNMFRFATLPVYEGIKYYTVIPRSFRSKANKREAWAAFYVYKLHQLTYLLDFSVDGYIRRAIDCGHDDLSQLHCSYTSFEVDTGVYSVSSYEASATGTFIEQPNATECDFSPMLTGVAPQVYNFKRLVFSNCNYNLTKLLSLFAVDEFSCNGISPDSIARGCYSTLTVDYFAYPLSMKSYIRPGSAGNIPLYNYKQSFANPTCRVMASVLANVTITKPHAYGYISKCSRLTGANQDVETPLYINPGEYSICRDFSPGGFSEDGQVFKRTLTQFEGGGLLIGVGTRVPMTDNLQMSFIISVQYGTGTDSVCPMLDLGDSLTITNRLGKCVDYSLYGVTGRGVFQNCTAVGVKQQRFVYDSFDNLVGYYSDDGNYYCVRPCVSVPVSVIYDKSTNLHATLFGSVACEHVTTMMSQFSRLTQSNLRRRDSNIPLQTAVGCVIGLSNNSLVVSDCKLPLGQSLCAVPPVSTFRSYSASQFQLAVLNYTSPIVVTPINSSGFTAAIPTNFSFSVTQEYIETSIQKVTVDCKQYVCNGFTRCEKLLVEYGQFCSKINQALHGANLRQDESVYSLYSNIKTTSTQTLEYGLNGDFNLTLLQVPQIGGSSSSYRSAIEDLLFDKVTIADPGYMQGYDDCMKQGPQSARDLICAQYVSGYKVLPPLYDPNMEAAYTSSLLGSIAGAGWTAGLSSFAAIPFAQSMFYRLNGVGITQQVLSENQKLIANKFNQALGAMQTGFTTSNLAFSKVQDAVNANAQALSKLASELSNTFGAISSSISDILARLDTVEQDAQIDRLINGRLISLNAFVSQQLVRSETAARSAQLASDKVNECVKSQSKRNGFCGSGTHIVSFVVNAPNGFYFFHVGYVPTNYTNVTAAYGLCNNNNPPLCIAPIDGYFITNQTTTYSVDTEWYYTGSSFYKPEPITQANSRYVSSDVKFDKLENNLPPPLLENSTDVDFKDELEEFFKNVTSHGPNFAEISKINTTLLDLSDEMAMLQEVVKQLNDSYIDLKELGNYTYYNKWPWYVWLGFIAGLVALLLCVFFLLCCTGCGTSCLGKMKCKNCCDSYEEYDVEKIHVH
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[Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. {ECO:0000255|HAMAP-Rule:MF_04099}. [Spike protein S2]: Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099}. [Spike protein S2']: Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. {ECO:0000255|HAMAP-Rule:MF_04099}.
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A3EXD0
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SPIKE_BCHK5
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Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
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MIRSVLVLMCSLTFIGNLTRGQSVDMGHNGTGSCLDSQVQPDYFESVHTTWPMPIDTSKAEGVIYPNGKSYSNITLTYTGLYPKANDLGKQYLFSDGHSAPGRLNNLFVSNYSSQVESFDDGFVVRIGAAANKTGTTVISQSTFKPIKKIYPAFLLGHSVGNYTPSNRTGRYLNHTLVILPDGCGTILHAFYCVLHPRTQQNCAGETNFKSLSLWDTPASDCVSGSYNQEATLGAFKVYFDLINCTFRYNYTITEDENAEWFGITQDTQGVHLYSSRKENVFRNNMFHFATLPVYQKILYYTVIPRSIRSPFNDRKAWAAFYIYKLHPLTYLLNFDVEGYITKAVDCGYDDLAQLQCSYESFEVETGVYSVSSFEASPRGEFIEQATTQECDFTPMLTGTPPPIYNFKRLVFTNCNYNLTKLLSLFQVSEFSCHQVSPSSLATGCYSSLTVDYFAYSTDMSSYLQPGSAGAIVQFNYKQDFSNPTCRVLATVPQNLTTITKPSNYAYLTECYKTSAYGKNYLYNAPGAYTPCLSLASRGFSTKYQSHSDGELTTTGYIYPVTGNLQMAFIISVQYGTDTNSVCPMQALRNDTSIEDKLDVCVEYSLHGITGRGVFHNCTSVGLRNQRFVYDTFDNLVGYHSDNGNYYCVRPCVSVPVSVIYDKASNSHATLFGSVACSHVTTMMSQFSRMTKTNLLARTTPGPLQTTVGCAMGFINSSMVVDECQLPLGQSLCAIPPTTSSRVRRATSGASDVFQIATLNFTSPLTLAPINSTGFVVAVPTNFTFGVTQEFIETTIQKITVDCKQYVCNGFKKCEDLLKEYGQFCSKINQALHGANLRQDESIANLFSSIKTQNTQPLQAGLNGDFNLTMLQIPQVTTGERKYRSTIEDLLFNKVTIADPGYMQGYDECMQQGPQSARDLICAQYVAGYKVLPPLYDPYMEAAYTSSLLGSIAGASWTAGLSSFAAIPFAQSIFYRLNGVGITQQVLSENQKIIANKFNQALGAMQTGFTTTNLAFNKVQDAVNANAMALSKLAAELSNTFGAISSSISDILARLDTVEQEAQIDRLINGRLTSLNAFVAQQLVRTEAAARSAQLAQDKVNECVKSQSKRNGFCGTGTHIVSFAINAPNGLYFFHVGYQPTSHVNATAAYGLCNTENPQKCIAPIDGYFVLNQTTSTVADSDQQWYYTGSSFFHPEPITEANSKYVSMDVKFENLTNRLPPPLLSNSTDLDFKEELEEFFKNVSSQGPNFQEISKINTTLLNLNTELMVLSEVVKQLNESYIDLKELGNYTFYQKWPWYIWLGFIAGLVALALCVFFILCCTGCGTSCLGKLKCNRCCDSYDEYEVEKIHVH
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[Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. {ECO:0000255|HAMAP-Rule:MF_04099}. [Spike protein S2]: Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099}. [Spike protein S2']: Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. {ECO:0000255|HAMAP-Rule:MF_04099}.
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A3EXG6
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SPIKE_BCHK9
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Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
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MLLILVLGVSLAAASRPECFNPRFTLTPLNHTLNYTSIKAKVSNVLLPDPYIAYSGQTLRQNLFMADMSNTILYPVTPPANGANGGFIYNTSIIPVSAGLFVNTWMYRQPASSRAYCQEPFGVAFGDTFENDRIAILIMAPDNLGSWSAVAPRNQTNIYLLVCSNATLCINPGFNRWGPAGSFIAPDALVDHSNSCFVNNTFSVNISTSRISLAFLFKDGDLLIYHSGWLPTSNFEHGFSRGSHPMTYFMSLPVGGNLPRAQFFQSIVRSNAIDKGDGMCTNFDVNLHVAHLINRDLLVSYFNNGSVANAADCADSAAEELYCVTGSFDPPTGVYPLSRYRAQVAGFVRVTQRGSYCTPPYSVLQDPPQPVVWRRYMLYDCVFDFTVVVDSLPTHQLQCYGVSPRRLASMCYGSVTLDVMRINETHLNNLFNRVPDTFSLYNYALPDNFYGCLHAFYLNSTAPYAVANRFPIKPGGRQSNSAFIDTVINAAHYSPFSYVYGLAVITLKPAAGSKLVCPVANDTVVITDRCVQYNLYGYTGTGVLSKNTSLVIPDGKVFTASSTGTIIGVSINSTTYSIMPCVTVPVSVGYHPNFERALLFNGLSCSQRSRAVTEPVSVLWSASATAQDAFDTPSGCVVNVELRNTTIVNTCAMPIGNSLCFINGSIATANADSLPRLQLVNYDPLYDNSTATPMTPVYWVKVPTNFTLSATEEYIQTTAPKITIDCARYLCGDSSRCLNVLLHYGTFCNDINKALSRVSTILDSALLSLVKELSINTRDEVTTFSFDGDYNFTGLMGCLGPNCGATTYRSAFSDLLYDKVRITDPGFMQSYQKCIDSQWGGSIRDLLCTQTYNGIAVLPPIVSPAMQALYTSLLVGAVASSGYTFGITSAGVIPFATQLQFRLNGIGVTTQVLVENQKLIASSFNNALVNIQKGFTETSIALSKMQDVINQHAAQLHTLVVQLGNSFGAISSSINEIFSRLEGLAANAEVDRLINGRMMVLNTYVTQLLIQASEAKAQNALAAQKISECVKAQSLRNDFCGNGTHVLSIPQLAPNGVLFIHYAYTPTEYAFVQTSAGLCHNGTGYAPRQGMFVLPNNTNMWHFTTMQFYNPVNISASNTQVLTSCSVNYTSVNYTVLEPSVPGDYDFQKEFDKFYKNLSTIFNNTFNPNDFNFSTVDVTAQIKSLHDVVNQLNQSFIDLKKLNVYEKTIKWPWYVWLAMIAGIVGLVLAVIMLMCMTNCCSCFKGMCDCRRCCGSYDSYDDVYPAVRVNKKRTV
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[Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. {ECO:0000255|HAMAP-Rule:MF_04099}. [Spike protein S2]: Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099}. [Spike protein S2']: Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. {ECO:0000255|HAMAP-Rule:MF_04099}.
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A3FBE9
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IL6_MUSPF
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Interleukin-6 (IL-6)
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MNSLSTSAFSPVAFSLGLLLVMATAFPTPGPLGGDSKDDATSNRPPLTSADKMEDFIRFILGKISALKKEMCEKYNKCEDSKEALAENNLNLPKLAEEDKCFQSQFNQETCLTRITTGLQEFQIHLKYLEANYEGNKNNAHSVYISTKHLLQKLRPMNRVEVTTPDPTTDSSLQALFKSQDKWLKHVTIHLILRSLEDFLQFSLRAIRIM
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Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway. The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells. IL6 is a potent inducer of the acute phase response. Rapid production of IL6 contributes to host defense during infection and tissue injury, but excessive IL6 synthesis is involved in disease pathology. In the innate immune response, is synthesized by myeloid cells, such as macrophages and dendritic cells, upon recognition of pathogens through toll-like receptors (TLRs) at the site of infection or tissue injury (By similarity). In the adaptive immune response, is required for the differentiation of B cells into immunoglobulin-secreting cells. Plays a major role in the differentiation of CD4(+) T cell subsets. Essential factor for the development of T follicular helper (Tfh) cells that are required for the induction of germinal-center formation. Required to drive naive CD4(+) T cells to the Th17 lineage. Also required for proliferation of myeloma cells and the survival of plasmablast cells (By similarity). Acts as an essential factor in bone homeostasis and on vessels directly or indirectly by induction of VEGF, resulting in increased angiogenesis activity and vascular permeability. Induces, through 'trans-signaling' and synergistically with IL1B and TNF, the production of VEGF. Involved in metabolic controls, is discharged into the bloodstream after muscle contraction increasing lipolysis and improving insulin resistance (By similarity). 'Trans-signaling' in central nervous system also regulates energy and glucose homeostasis. Mediates, through GLP-1, crosstalk between insulin-sensitive tissues, intestinal L cells and pancreatic islets to adapt to changes in insulin demand (By similarity). Also acts as a myokine (By similarity). Plays a protective role during liver injury, being required for maintenance of tissue regeneration (By similarity). Also has a pivotal role in iron metabolism by regulating HAMP/hepcidin expression upon inflammation or bacterial infection (By similarity). Through activation of IL6ST-YAP-NOTCH pathway, induces inflammation-induced epithelial regeneration (By similarity).
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A3FEW8
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BGAL_ENTAG
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Beta-galactosidase (Beta-gal) (Bga) (EC 3.2.1.23) (Lactase) (Transglycosylating beta-galactosidase)
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MFTASPMSLSKILARRDWENPGVTQWHRLPAHAPFNSWRDEASARADDNASRKRSLNGDWQFSYYAAPEQVPDSWVTEDCADAVTTPVPSNWQMQGFDTPIYTNDTYPIPVNPPFVPAENPTGCYSLTFEVDEQWLESGQTRIVFDGVNSAFYLWCNGKWMGYSQDSRLPAEFDLSAVLRPGTNRLAVLVLRWCDGSYLEDQDMWRMSGIFRDVSLLHKPHTHIADYHAVTELNADYDRAKLQVEVALAGEQFADCEVAVTLWRDGLSVATVSAKPGSAIIDERGNWAERLNVTLPVKDPALWSAETPELYRLTFALRDGQGEILDVEACDVGFRCVEISNGLLKVNGKPLLIRGVNRHEHHPENGQVMDEATMCRDIELMKQHNFNAVRCSHYPNHPLWYTLCDRYGLYVVDEANIETHGMVPMSRLADDPRWLPAMSERVTRMVLRDRNHPSIIIWSLGNESGHGANHDALYRWVKTTDPTRPVQYEGGGANTAATDIVCPMYARVDQDQPFEAVPKWSLKKWIGMPDETRPLILCEYAHAMGNSFGGFAKYWQAFRNHPRLQGGFVWDWVDQALTKKDDNGNAFWAYGGDFGDTPNDRQFCLNGLVFPDRTPHPALFEAQRAQQFFTFTLVSTSPLVIDVHSDYLFRQCDNEQLRWNIARDGEVLASGEVALTIAPQQTQRIEIDAPEFAAAAGEIWLNVDIVQTAATAWSPADHRCAWDQWQLPAPLYIAPPVEGTAKPDLKVKEDVLEVSHQSQRWHFDRASGNLTQWWNNGTATLLAPLSDNFTRAPLDNDIGVSEATRIDPNAWVERWKAAGMYNLTPRLLLCEGEQLAQAVTITTLHAWESNGKALFLSRKVWKIDRAGVLHGDVQVQVANDIPQPARIGLSCQLAQTPQTASWLGLGPDENYPDRKLAARQGRWTLPLDALHTAYIFPTDNGLRCDTRELTFDTHQMQGDFHFSLSRYSQQQLRDTSHHHLLEAEPGCWLNIDAFHMGVGGDDSWSPSVSPEFILQRREMRYAFSWRQD
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This beta-galactosidase is also able to catalyze glycosyl transfer to a series of acceptors, including hexose, pentose, beta- or alpha-disaccharides, hexahydroxy alcohol, cyclitol, and aromatic glycosides, resulting in the production of galacto-oligosaccharides (GOS).
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A3FFS8
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EPO_BOSMU
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Erythropoietin
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MGARDCTPLLMLSFLLFPLGFPVLGAPARLICDSRVLERYILEAREAENATMGCAEGCSFNENITVPDTKVNFYAWKRMEVQQQAQEVWQGLALLSEAILRGQALLANASQPCEALRLHVDKAVSGLRSLTSLLRALGAQKEAISLPDATPSAAPLRAFTVDALSKLFRIYSNFLRGKLTLYTGEACRRGDR
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Hormone involved in the regulation of erythrocyte proliferation and differentiation and the maintenance of a physiological level of circulating erythrocyte mass. Binds to EPOR leading to EPOR dimerization and JAK2 activation thereby activating specific downstream effectors, including STAT1 and STAT3.
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A3FIN4
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AT8B5_MOUSE
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Phospholipid-transporting ATPase FetA (EC 7.6.2.1) (ATPase class I type 8B member 2-like protein) (ATPase class I type 8B member 5) (Flippase expressed in testis A)
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MKYVKAFVSEISWDCSWYCSAMQERRNEDRQKEEEERILQANNRRFNSLFEYPDNSIKTSKYGFFNFLPMNLFEQFQRLANAYFLILLFLQLVPQISSLAWYTTVIPLIVVLSITGVKDAIDDVKRHRSDQQINNRSVSILVNGRVEEIKWRNVQVGDIIKLENNHPVTADMLLLSSSEPYGLTYIETADLDGETNLKVKQAISVTSAMEDNLELLSSFNGEVRCDPPNNKLDKFSGTLSYLGNTYLLNHERLLLRGCVIRNTDWCYGLVVYTGQDTKLMQNSGRSTFKRTHIDHLMNVLVVWIFMFLGGMCFLLSIGHGIWENSRGYYFQAFLPWKHYITSSATSSALIFWSYFIVLNTMVPISLYVSVEIIRLGNSYYINWDRKMFYAPKNMPAQARTTTLNEELGQVQYVFSDKTGTLTENVMIFNKCSINGKTYGYSYDDNGEYVPKSPKDKVDFSYNHLADPKFSFYDKTLVEAVKSEDPLVYLFFLCLSLCHTVMSEEKVEGELVYQAQSPDEGALVTATRNFGFVFCSRTPETITVIEMGKIRVYRLLAILDFSNERKRMSVIVRTPEDRVMLFCKGADTIIYELLHPSCASLSEVTMDHLDDFASEGLRTLMVAYRELDKAYFQTWIKKHGEAWLTLENRERKLALVYEEIERDLMLLGATAIEDKLQRGVPETIVTLSKAKIKIWVLTGDKQETAVNIAYSCRIFKDEMDGVFMVEGTDRETVLEELRTARKKMKPESLLESDPINMYLARKPKMPFKSLDEVANGNYGLVISGYSLAYALEGSLEFELLRTACMCKGVVCCRMTPLQKAQVVDLVKRYKKVVTLAIGDGANDISMIKAAHIGVGISNQEGMQATLSSDFSFCQFHFLQRLLLVHGRLSYNRMCKFLSYFFYKNFAFTLVHFWYAFFNGFSAQTVYDIWFITFYNLIYTSLPVLGLSLFEKDVNETWSLCYPELYEPGQHNLYFNKKEFVKCLLHGIYNSFVLFFVPMGTVFNSERNDGKDISDFQSFSLLVQTTLIGVMTMQIALRTTSWTMINHTFTWGSLGLYFCILILLCSDGLCLRYPSIFNFLGVARNSLSQPQIWLCLILSTILCMIPLIGYNFLRPLLWPINADKVLNRIHFCLKHPIPTQVQTKIKHPSLRRSAYAFSHKQGFGALITSGKTLKSSALAKSKRFL
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P4-ATPase flippase which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. May play a role in phospholid transport across membranes and in acrosome formation.
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A3FKF7
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G3P_MUSPF
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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-)
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MVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGKSISIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKAAKYDDIKKVVKQASEGPLKGILGYTEDQVVSCDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMVYMASKE
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Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (By similarity). Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity).
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A3FMB2
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POLG_HAVH2
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Genome polyprotein [Cleaved into: Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
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MNMSKQGIFQTVGSGLDHILSLADIEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGSHQIEPLKTSVDKPGSKKTQGEKFFLIHSADWLTTHALFHEVAKLDVVKLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQSYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQYPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDPEDWKSDPSQGGGIKITHFTTWTSIPTLAAQFPFNASDSVGQQIKVIPVDPYFFQMTNTNPDQKCITALASICQMFCFWRGDLVFDFQVFPTKYHSGRLLFCFVPGNELIDVTGITLKQATTAPCAVMDITGVQSTLRFRVPWISDTPYRVNRYTKSAHQKGEYTAIGKLIVYCYNRLTSPSNVASHVRVNVYLSAINLECFAPLYHAMDVTTQVGDDSGGFSTTVSTEQNVPDPQVGITTMRDLKGKANRGKMDVSGVQAPVGAITTIEDPVLAKKVPETFPELKPGESRHTSDHMSIYKFMGRSHFLCTFTFNSNNKEYTFPITLSSTSNPPHGLPSTLRWFFNLFQLYRGPLDLTIIITGATDVDGMAWFTPVGLAVDTPWVEKESALSIDYKTALGAVRFNTRRTGNIQIRLPWYSYLYAVSGALDGLGDKTDSTFGLVSIQIANYNHSDEYLSFSCYLSVTEQSEFYFPRAPLNSNAMLSTESMMSRIAAGDLESSVDDPRSEEDRRFESHIECRKPYKELRLEVGKQRLKYAQEELSNEVLPPPRKMKGLFSQAKISLFYTEEHEIMKFSWRGVTADTRALRRFGFSMAAGRSVWTLEMDAGVLTGRLVRLNDEKWTEMKDDKIVSLIEKFTSNKYWSKVSFPHGMLDLEEIAANSTDFPNMSETDLCFLLHWLNPKKINLADRMLGLSGVQEIKEQGVGLIAECRTFLDSIAGTLKSMMFGFHHSVTVEIINTVLCFVKSGILLYVIQQLNQDEHSHIIGLLRVMNYADIGCSVISCGKVFSKMLETVFNWQMDSRMMELRTQSFSNWLRDICSGITIFKSFKDAIYWLYTKLKDFYEVNYGKKKDILNILKDNQQKIEKAIEEADNFCILQIQDVEKFDQYQKGVDLIQKLRTVHSMAQVDPNLGVHLSPLRDCIARVHQKLKNLGSINQAMVTRCEPVVCYLYGKRGGGKSLTSIALATKICKHYGVEPEKNIYTKPVASDYWDGYSGQLVCIIDDIGQNTTDEDWSDFCQLVSGCPMRLNMASLEEKGRHFSSPFIIATSNWSNPSPKTVYVKEAIDRRLHFKVEVKPASFFKNPHNDMLNVNLAKTNDAIKDMSCVDLIMDGHNISLMDLLSSLVMTVEIRKQNMSEFMELWSQGISDDDNDSAVAEFFQSFPSGEPSNSKLSSFFQSVTNHKWVAVGAAVGILGVLVGGWFVYKHFSRKEEEPIPAEGVYHGVTKPKQVIKLDADPVESQSTLEIAGLVRKNLVQFGVGEKNGCVRWVMNALGVKDDWLLVPSHAYKFEKDYEMMEFYFNRGGTYYSISAGNVVIQSLDVGFQDVVLMKVPTIPKFRDITQHFIKKGDVPRALNRLATLVTTVNGTPMLISEGPLKMEEKATYVHKKNDGTTVDLTVDQAWRGKGEGLPGMCGGALVSSNQSIQNAILGIHVAGGNSILVAKLVTQEMFQNIDKKIESQRIMKVEFTQCSMNVVSKTLFRKSPIHHHIDKTMINFPAVMPFSKAEVDPMAVMLSKYSLPIVEEPEDYKEASIFYQNKIVGKTQLVDDFLDLDMAITGAPGIDAINMDSSPGFPYVQEKLTKRDLIWLDENGLLLGVHPRLAQRILFNTVMMENCSDLDVVFTTCPKDELRPLEKVLESKTRAIDACPLDYTILCRMYWGPAISYFHLNPGFHTGVAIGIDPDRQWDELFKTMIRFGDVGLDLDFSAFDASLSPFMIREAGRIMSELSGTPSHFGTALINTIIYSKHLLYNCCYHVCGSMPSGSPCTALLNSIINNINLYYVFSKIFGKSPVFFCQALRILCYGDDVLIVFSRDVQIDNLDLIGQKIVDEFKKLGMTATSADKNVPQLKPVSELTFLKRSFNLVEDRIRPAISEKTIWSLIAWQRSNAEFEQNLENAQWFAFMHGYEFYQKFYYFVQSCLEKEMIEYRLKSYDWWRMRFYDQCFICDLS
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[Capsid protein VP1]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. [Capsid protein VP2]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. [Capsid protein VP3]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. [Capsid protein VP4]: Plays a role in the assembly of the 12 pentamers into an icosahedral structure. Has not been detected in mature virions, supposedly owing to its small size. [Protein VP1-2A]: Precursor component of immature procapsids that corresponds to an extended form of the structural protein VP1. After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein. [Protein 2B]: Functions as a viroporin. Affects membrane integrity and causes an increase in membrane permeability. Involved in host intracellular membrane rearrangements probably to give rise to the viral factories. Does not disrupt calcium homeostasis or glycoprotein trafficking. Antagonizes the innate immune response of the host by suppressing IFN-beta synthesis, which it achieves by interfering with the RIG-I/IFIH1 pathway. [Protein 3ABC]: The precursor 3ABC is targeted to the mitochondrial membrane where protease 3C activity cleaves and inhibits the host antiviral protein MAVS, thereby disrupting activation of IRF3 through the IFIH1/MDA5 pathway. In vivo, the protease activity of 3ABC precursor is more efficient in cleaving the 2BC precursor than that of protein 3C. The 3ABC precursor may therefore play a role in the proteolytic processing of the polyprotein. Possible viroporin. [Protein 3AB]: Interacts with the 3CD precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Since the 3AB precursor contains the hydrophobic domain 3A, it probably anchors the whole viral replicase complex to intracellular membranes on which viral RNA synthesis occurs. [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease. Cleaves IKBKG/NEMO to impair innate immune signaling. Cleaves host PABPC1 which may participate in the switch of viral translation to RNA synthesis.
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A3KFM7
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CHD6_MOUSE
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Chromodomain-helicase-DNA-binding protein 6 (CHD-6) (EC 3.6.4.12) (ATP-dependent helicase CHD6)
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MKMKIQKKEKQLSKLRALNHSPMSDASVNFDYKSPSPFDCSPDQGENIEEAANHCLPHKNLYTTEEEADTLFSRKLTSHNGMEDSGGRGTGVKKKRKKKEPGEQEGTKGSKDREPKPKRKREPKEPKEPRRAKEPKRAKEPKETKQKDGVKKPRKHREASGTKEGKEKRSCTDYGSRTKSKKASREQGPTPVERKKKGKRKNETTVESLELDHSLPNPSLQSPEEPSESADSQKRRSGRQVKRRKYNEDLDFKVVDDDGETIAVLGAGRTSALSASTLAWQAEEPPEDDANIIEKILASKTVQEVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEKDPRIAQKIKRFRNKQAQMKHIFTEPDEDLFNPDYIEIDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQILPEVKHVERPASDAWQKLETSREYRNSNRLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYHGSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLAPKQETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNMPNLINTMMELRKCCNHPYLINGAEEKILEDFRKAHSSEASDFQLQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAILQDINRKGSTNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQRRTHTITIQSEGKGSTFAKASFVASGNRTDISLDDPNFWQKWAKIAELDTEANNEKESLVIDRPRVRKQTKHYNSFEEDELMEFSELDSDSDERPTRSRRLSDRARRYLRAECFRVEKNLLIFGWGRWKDILTHGRFKWPLNEKDMEMICRALLVYCVKHYKGDEKIKSFIWELITPSKDGQVQTLQNHSGLSAPVPRGRKGKKTKNQLLLPELKNADWLATCNPEVVLHDDGYKKHLKQHCNKVLLRVRMLYYLKAEILGEAADKAFEGTPARELDVLLPDIDYVEIPVDWWDAEADKSLLIGVFKHGYERYNAMRADPALCFLEKVGMPDEKSLSAEQGVTDGTSDIPERGNIDKEDSAEDKLDGLQKQTASPSDGSDGIFGEKKDDSQAAQDGSDPDKSPWPVSSALTARLRRLVTIYQRCNRKELCRPEILGPGNQGYWVQEEVFRRTSEMDLINKEAQKRWTRREQADFYRTVSSFGVVYDQEKKAFDWTQFRIISRLDKKSDESLEHYFYSFVAMCRNVCRLPAWKDDGPPDASIYVEPITEERAAKTLYRIELLRKVREQVLMCPQLHERLQLCRPSLYLPVWWECGKHDRDLLIGTAKHGLNRTDYYIMNDPQLSFLDAYRNYAQHKRTDTQAPGSLCCLYQSNSKLYESLTYTPVSRTSESLESEPENLMRMESRDDHLCLPEGGLPDITCENFVSKVQEVISLDHDENLLPESLENMIYGKTGLSQEPHSFQEAPTTNTQSRKNTITISASRNESCQPPGIEAEITSASSLMSSLEAGVAKMNIKNGKHLLVSISKEGEPCCSETGRRPETIGHREAKCLVSPTLDTGHESGFVDLCSLSVYDPKRNFSSDQQLIDLLENKSLESKLILNQSDEEEEENEDETLAIVASATEKPEVLDFPKPTVNIPRGKNLSFHQDEAKKGRLEVVSKTAGPQRVFPPPANQCHCKHIERWAHGLGSEDSEVEKPKAYQPDLYRSKANNSTVEGETAVIPTEPFKLKHELLKEPWKESSEGGKSFSMYAPEGSEPKPEDMDFENKDDYEKDGTCLSQDYPGKYSEEESKSSASGIAGDLGEEAQEVRAPTIAQLLQEKTLYSFSEWPKDRVIINRLDNICHVVLKGKWPCSHQYEPSGALPTPVLSSSAGSRSSLSEPEATEHGFSNGAALAAQIQKESFLAPVFTKDEQKHRRPYEFEVERDAKARSLEEYSATHGRPPIVLNGWHGESAIDLSCSSEGSPGATSPFPVSASTPKIGAISSLQGALGMDLSGILQAGLIHPVTGQIVNGSLRRDDAAMRRRRGRRKHIEGGMDLIFLKEQTLQAGILEVHEDAGQTTLSTTHPEVPGATSSAPEPTAAASSQAEKAVPSKSLLDWLRQQADYSLDVPGFGTSFSDKPKQRRPRCKEPGKLDISSLGGEERVPAVPKEPGLRGFLPESKFNHTLAEPVLRDAGPRRRGRRPRNELLKAPAIVADSPSGMGPLFMNGLIAGMDLVGLQNVRNIPGIPLTGLVGFPAGFATMPTGEEVKNTLSMLPMMLPGMAAVPQMFGVGGLLNTPMATTCTTTASASLASTKSGTSATEKSTEDKLSGHDVNTDALVDDKPGPSPFSDQSEPTITTSSPVAFNPFLIPGVSPGLIYPSMFLSPGMGMALPAMQQARHSEMVGLETQKRKKKKTKGDSPTQEPASVCEKEPGSDQNCTESSATVSPEREHVAQAREEGLKDSNEDTN
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DNA-dependent ATPase that plays a role in chromatin remodeling. Regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. Activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.
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A3KFX0
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5NT1A_MOUSE
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Cytosolic 5'-nucleotidase 1A (cN1A) (EC 3.1.3.5) (EC 3.1.3.89) (EC 3.1.3.99) (5'-deoxynucleotidase) (Cytosolic 5'-nucleotidase IA) (cN-IA)
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MEPGQPREAREPGPGAETAAVPRWEEAKTFYDNLSSKKKPKSPKPQNAVTIAVSSRALFRMDEEQRIYTEQGVEEYVRYQLEHENEPFSPGPAFPFVKALEAVNKRLRELYPDSEDIFDIVLMTNNHAQVGVRLINSINHYDLFIERFCMTGGNSPICYLKAYHTNLYLSADADKVREAIDEGIAAATIFSPSRDVVVSQSQLRVAFDGDAVLFSDESERIVKAHGLDRFFEHEKAHENKPLAQGPLKGFLEALGRLQKKFYSKGLRLECPIRTYLVTARSAASSGARALKTLRSWGLETDEALFLAGAPKGPLLEKIRPHIFFDDQMFHVAGAQEMGTVAAHVPYGVAQNPRRAAAAKQSLGAQ
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Catalyzes the hydrolysis of ribonucleotide and deoxyribonucleotide monophosphates, releasing inorganic phosphate and the corresponding nucleoside (By similarity). AMP is the major substrate but can also hydrolyze dCMP and IMP (By similarity).
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A3KG59
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P20D2_MOUSE
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Xaa-Arg dipeptidase (EC 3.4.13.4)
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MGPVVERPAEPGTSSAAELELLKRRAAERIDEAAERLGALSRAIWSAPELAYEEHRAHGELTRFFECEPPAASWAVQPHFGLPTAFRAEWAPPESAAGPRALQVAFLCEYDALPALGHACGHNLIAEVGVAAALGLRAALESIAAPPPVKVIVLGTPAEEDGGGKIDLIEAGAFENLDVVFMAHPSQENAAYLPDVAEHDVTVKYYGKASHAAAYPWEGVNALDAAVLAYTNLSVLRQQMKPTWRVHGIIKNGGVKPNIIPSYSELVYYFRAPSMKELQVLTKKAEDCFRAAALATGCTVDIESEAHDYYNVIPNKTLCSAYTENGKKLGMEFISEDAVLNGPSGSTDFGNVSFVVPGIHPYFYIGTDALNHTEQYTEAAGSQAAQLYTLRTAKALAMTALDVIFKPALLEGVRKEFKCKLQEEQLLNTAA
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Catalyzes the peptide bond hydrolysis in dipeptides having basic amino acids lysine, ornithine or arginine at C-terminus. Postulated to function in a metabolite repair mechanism by eliminating alternate dipeptide by-products formed during carnosine synthesis.
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A3KGF7
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PLCB2_MOUSE
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1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 (EC 3.1.4.11) (Phosphoinositide phospholipase C-beta-2) (Phospholipase C-beta-2) (PLC-beta-2)
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MSLLNPVLLPPNVKAYLSQGERFIKWDDETSIASPVILRVDPKGYYLYWTYQNQEMEFLDVTSIRDTRFGKFAKIPKSQKLREVFNMDFPDNHFLLKTLTVVSGPDMVDLTFYNFVSYKENVGKDWAEDVLALAKHPMTVNAPRSTFLDKILVKLKMQLNPEGKIPVKNFFQMFPADRKRVEAALGACHLAKGKNDAINPEDFPESVYKSFLMSLCPRPEIDEIFTSYHSKAKPYMTKEHLTKFINQKQRDPRLNSLLFPPARPEQVQVLIDKYEPSGINVQRGQLSPEGMVWFLCGPENSVLAHDTLLIHQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDILFKEAIEAIAESAFKTSPYPVILSFENHVDSPRQQAKMAEYCRSMFGETLLTDPLENFPLKPGIPLPSPEDLRGKILIKNKKNQFSGPASPSKKPGGVAEGSLPSSVPVEEDTGWTAEDRTEVEEEEVVEEEEEEESGNLDEEEIKKMQSDEGTAGLEVTAYEEMSSLVNYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMALFEFNGQSGYLLKHEFMRRLDKQFNPFSVDRIDVVVATTLSITIISGQFLSERSVRTYVEVELFGLPGDPKRRYRTKLSPTANSINPVWKEEPFIFEKILMPELASLRIAVMEEGSKFLGHRIIPINALHSGYHHLCLRSESNMALTMPALFVFLEMKDYIPDTWADLTVALANPIKYFNAQDKKSVKLKGVTGSLPEKLFSGTPVASQSNGAPVSAGNGSTAPGTKATGEEATKEVTEPQTASLEELRELKGVVKLQRRHEKELRELERRGARRWEELLQRGAAQLAELQTQAAGCKLRPGKGSRKKRTLPCEETVVAPSEPHDRADPRVQELKDRLEQELQQQGEEQYRSVLKRKEQHVTEQIAKMMELAREKQAAELKTFKETSETDTKEMKKKLEAKRLERIQAMTKVTTDKVAQERLKREINNSHIQEVVQAVKQMTETLERHQEKLEERQTACLEQIQAMEKQFQEKALAEYEAKMKGLEAEVKESVRAYFKDCFPTEAEDKPERSCEASEESCPQEPLVSKADTQESRL
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The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.
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A3KGS3
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RGPA2_MOUSE
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Ral GTPase-activating protein subunit alpha-2 (250 kDa substrate of Akt) (AS250) (P220)
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MFSRRSHGDVKKSTQKVLDPKKDVLTRLKHLRALLDNVDASDLKQFFETNYSQIYFIFYENFITLENSLKLKGNNKSQREELDSILFLFEKILQFLPERIFFRWHYQSIGSTLKKLLHTGNSIKIRCEGIRLFLLWLQALQTNCAEEQVLIFACLVPGFPAVLSSRGPCTLETLINPSPSIVDAKIYPEEITPLLPAISGEKIAEDQTCFFLQILLKYMVIQAASLEWKNKENQDTGFKFLFTLFRKYYLPHLFPSFTKLTNIYKPVLEIPHLRPKPVYVTVTRDNETIYSTKIPYMAARVVFIKWIVTFFLEKKYLTATQNTKNGVDVLPKIIQTVGGGAIQEKVPELDGAGSTEQDKSHSNSSTLSDRRLSNSSLCSIEEEHRTVYEMVQRILLSTRGYVNFVNEVFRQAFLLPSCEISVTRKVVQVYRKWILQNKPVFMEEPDKKDVAQEDADKLGLSETDSKEASSESSGHKRSSSWGRTYSFTSAMSRGCVTEEDNTNVKAGAQAMLQVFLTNAANVFLLEPCAEVPMLLREQVDASKAVLIIFRRMIMELTMNQKTWEQMLQILLRITEAVMQKPKDKHVKDLFAQSLAGLLFRTLIVAWIRANLCVYISRELWDDFLRVLSSLTEWEELITEWSNIMDSLTAVLARTVYGVEMTNLPLDKLSEQKEKKQRGKGCILEPQKGTAVGRSFSLSWRSHPDVTEPMRFRSATTSGAPGVEKARNTVRQKATEVEEFQQAESTAAADCDYLVVGQQQVPRSSSTSDITERLYSDSSQGQKVEHSQNLSSSEPKSVQESKGHVTHEHEGITMLVRRSSSPAELELKDDLQQAHGRCRQRQTSESTGSDTVVGYSNEAELPVSPWQACEEDPDLSTPTDAVADSDARHWLQLSPTDASNLTDSRECLADDCSIIAGGNLTGWHPDSAAVLWRRVLGILGDVNNIQSPKIHAKVFGYLYELWYKLAKIRDNLAISLDNQSSPSPPLLIPPLRMFASWLFKATTLPNEYKEGKLQAYKLICAMMTRRQDVLPNSDFLVHFYLVMHLGLTSEDQDVLNTIIKNCSPRFFSLGLPGFSMLVGDFITAAARVLSTDMLAAPRSEALTLLGSLVCFPNTYQEIPLLQSVPEVSDVVTGAEDVKHYLINILLKNATEEPNECARCIAICSLGVWICEELAQSASHPQVKDAINVIGVTLKFPNKIVAQVACDVLQLLVSYWEKLQMFETALPRKMAEILVATIAFLLPSAEYSSVETDKKFIVSLLLCLLDWCMALPVSALLHPVSTAVLEELHPSRAPLLDYIYRVLHCCVCGSSTYTQQSHYTLTLADLSSTDYDPFLPLANVRNSEPIQYHSSADLGNLLTVEEEKKRRSVELIPLTARMVMAHLVNHLGHYPLSGGPAVLHSLVSENHDNAHVEGTELSSEVFRSPNLQLFVFNDSTLISYLQTPAEGPAGGTSGGSLSDVRVIVRDISGKYSWDGKVLYGPLEGRLAPNGRNPSFQISGWHHHTCGPQKDLFNGEEGDDVLDKLLENIGHTSPECLLPSQLNLNEPSPTPCAMNWDQEKAIMEVILRQSAQEDEYVQRCNSDSSVTVTSQGQPSPVEPRGPFYFCRLLLDDLGMNSWDRRKNFHLLKKNSKLLRELKNLDSRQCRETHKIAVFYIAEGQEDKCSILANERGSQAYEDFVAGLGWEVDLSTHCGFMGGLQRNGSTGQTAPYYATSTVEVIFHVSTRMPSDSDDSLTKKLRHLGNDEVHIVWSEHSRDYRRGIIPTAFGDVSIIIYPMKNHMFFITITKKPEVPFFGPLFDGAIVSGKLLPSLICATCINASRAVKCLIPLYQSFYEERALYLEAIIQNHREVMTFEDFAAQVFSPSPSYSVSGTD
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Catalytic subunit of the heterodimeric RalGAP2 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB.
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A3KGV1
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ODFP2_MOUSE
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Outer dense fiber protein 2 (84 kDa outer dense fiber protein) (Cenexin) (Outer dense fiber of sperm tails protein 2)
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MSASSSGGSPRFPSCGKNGVTSLTQKKVLRTPCGAPSVTVTKSHKRGMKGDTVNVRRSVRVKTKVPWMPPGKSSARHVGCKWENPPHCLEITPPSSEKLVSVMRLSDLSTEDDDSGHCKMNRYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYANVFGDAPYTSSYLTSSPIRSRSPPA
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Seems to be a major component of sperm tail outer dense fibers (ODF). ODFs are filamentous structures located on the outside of the axoneme in the midpiece and principal piece of the mammalian sperm tail and may help to maintain the passive elastic structures and elastic recoil of the sperm tail. May have a modulating influence on sperm motility. Functions as a general scaffold protein that is specifically localized at the distal/subdistal appendages of mother centrioles. Component of the centrosome matrix required for the localization of PLK1 and NIN to the centrosomes. Required for the formation and/or maintenance of normal CETN1 assembly (By similarity). {ECO:0000250, ECO:0000269|PubMed:15852003}.
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A3KMH1
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VWA8_HUMAN
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von Willebrand factor A domain-containing protein 8 (PEX7-binding protein 2) (P7BP2)
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MQSRLLLLGAPGGHGGPASRRMRLLLRQVVQRRPGGDRQRPEVRLLHAGSGADTGDTVNIGDVSYKLKIPKNPELVPQNYISDSLAQSVVQHLRWIMQKDLLGQDVFLIGPPGPLRRSIAMQYLELTKREVEYIALSRDTTETDLKQRREIRAGTAFYIDQCAVRAATEGRTLILEGLEKAERNVLPVLNNLLENREMQLEDGRFLMSAERYDKLLRDHTKKELDSWKIVRVSENFRVIALGLPVPRYSGNPLDPPLRSRFQARDIYYLPFKDQLKLLYSIGANVSAEKVSQLLSFATTLCSQESSTLGLPDFPLDSLAAAVQILDSFPMMPIKHAIQWLYPYSILLGHEGKMAVEGVLKRFELQDSGSSLLPKEIVKVEKMMENHVSQASVTIRIADKEVTIKVPAGTRLLSQPCASDRFIQTLSHKQLQAEMMQSHMVKDICLIGGKGCGKTVIAKNFADTLGYNIEPIMLYQDMTARDLLQQRYTLPNGDTAWRSSPLVNAALEGKLVLLDGIHRVNAGTLAVLQRLIHDRELSLYDGSRLLREDRYMRLKEELQLSDEQLQKRSIFPIHPSFRIIALAEPPVIGSTAHQWLGPEFLTMFFFHYMKPLVKSEEIQVIKEKVPNVPQEALDKLLSFTHKLRETQDPTAQSLAASLSTRQLLRISRRLSQYPNENLHSAVTKACLSRFLPSLARSALEKNLADATIEINTDDNLEPELKDYKCEVTSGTLRIGAVSAPIYNAHEKMKVPDVLFYDNIQHVIVMEDMLKDFLLGEHLLLVGNQGVGKNKIVDRFLHLLNRPREYIQLHRDTTVQTLTLQPSVKDGLIVYEDSPLVKAVKLGHILVVDEADKAPTNVTCILKTLVENGEMILADGRRIVANSANVNGRENVVVIHPDFRMIVLANRPGFPFLGNDFFGTLGDIFSCHAVDNPKPHSELEMLRQYGPNVPEPILQKLVAAFGELRSLADQGIINYPYSTREVVNIVKHLQKFPTEGLSSVVRNVFDFDSYNNDMREILINTLHKYGIPIGAKPTSVQLAKELTLPEQTFMGYWTIGQARSGMQKLLCPVETHHIDIKGPALINIQEYPIERHEERSLNFTEECASWRIPLDEINIICDIATSHENEQNTLYVVTCNPASLYFMNMTGKSGFFVDFFDIFPRTANGVWHPFVTVAPLGSPLKGQVVLHEQQSNVILLLDTTGRALHRLILPSEKFTSKKPFWWNKEEAETYKMCKEFSHKNWLVFYKEKGNSLTVLDVLEGRTHTISLPINLKTVFLVAEDKWLLVESKTNQKYLLTKPAHIESEGSGVCQLYVLKEEPPSTGFGVTQETEFSIPHKISSDQLSSEHLSSAVEQKIASPNRILSDEKNYATIVVGFPDLMSPSEVYSWKRPSSLHKRSGTDTSFYRGKKKRGTPKQSNCVTLLDTNQVVRILPPGEVPLKDIYPKDVTPPQTSGYIEVTDLQSKKLRYIPIPRSESLSPYTTWLSTISDTDALLAEWDKSGVVTVDMGGHIRLWETGLERLQRSLMEWRNMIGQDDRNMQITINRDSGEDVSSPKHGKEDPDNMPHVGGNTWAGGTGGRDTAGLGGKGGPYRLDAGHTVYQVSQAEKDAVPEEVKRAAREMGQRAFQQRLKEIQMSEYDAATYERFSGAVRRQVHSLRIILDNLQAKGKERQWLRHQATGELDDAKIIDGLTGEKAIYKRRGELEPQLGSPQQKPKRLRLVVDVSGSMYRFNRMDGRLERTMEAVCMVMEAFENYEEKFQYDIVGHSGDGYNIGLVPMNKIPKDNKQRLEILKTMHAHSQFCMSGDHTLEGTEHAIKEIVKEEADEYFVIVLSDANLSRYGIHPAKFAQILTRDPQVNAFAIFIGSLGDQATRLQRTLPAGRSFVAMDTKDIPQILQQIFTSTMLSSV
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Exhibits ATPase activity in vitro.
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A3KNA7
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SRBP2_DANRE
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Sterol regulatory element-binding protein 2 (SREBP-2) (Sterol regulatory element-binding transcription factor 2) [Cleaved into: Processed sterol regulatory element-binding protein 2 (Transcription factor SREBF2)]
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MDASEFMDTMDPSLSELGDEFTLGDIDEMLQFVSNQVDFPDIFEDQMGGGATARTLPQAVPSAILTPPHTPVQTSSQTHTQTLTQAHTQTHTQTHTQTRTPPVLQPRPQPITQVQTQTFPMQTLAVQTQAQPQTVMITPTATPSRFIQNQVICQQNNATSFQVLQPQMQSIMTSPQVQPMTIQHQRVLTPAGQTIQTLSTAPTTVHTMSQQVPVLVHQPQILKTDSLLLTTKPDGTQVLSTVQSPTGITTLTTPIQTTALQMPTLMSSNILTTVPVVMGGGDKLPIKQLSSGPAHNIGGARVGVEQSPVVGPGGVVKEGERRTTHNIIEKRYRSSINDKILELRDLVLGNDAKMHKSGVLRKAIDYIKYLQQVNHKLRQENLTLKMANQKNKSACVSDVDLELKAEVSLISPPPSDSGSSSPAQLSPYCIDSEPGSPLLEHEQLKSEPDSPSCVGVMDRSRLLLCALSFLCLSLNPLPSLLGAEAPAGSPEVAGHGPTRTLFSLPAQTQSFGAWLWCVLPFLLVWVVSGVGVVWGCVRVLYLWEPVTPLHSPTSVRFWRHRKQADLQLYRGDYAGAVLSLQTCLSVLSRVLPVTTLDIMCSLSWNLIRYCLRRPAPLGWLVRLVGGRHEGEESQTSSRDAALVYHKLSQLQLTGQMERRPLWGVCVSLSAVNLCESAEGKLTATQQVQVYVTAAISVRAALGKHLTCLPAYLLSCAEALTCQSDSKPLPDCLRWIFTPLGRQFFLSCDWSVRSESDGQIFTSARDKADPIAQLHRCFCQKLLERATHTLIEPQSREDAGEFTGVLEFLQLLNSCTEDSAPSTAPFPALANQSSTSVRDPVCRWWASVLTAAVHWLQGDDASVRSLLAEAERMPRALHTLDHPLPKAVLALCKAVQMSVCPQKGEGVVSCLSHCQRASAQLHISVCQSHNNTWLHKGVELLVCDLLLTLRTSLWQRGGGSNGEPGPAPGSQLSGFQRDLSSLRRLGQAHRQAQHKLFLHETTVRLMAGASPTRTHQLLRHRTHNYTTTDGECVLGERERAHAILLACRHLPLPLLTPPGHRARLLAEAKRTLERVGDRRSLQDCQHILLRLSGGTTIAAS
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[Sterol regulatory element-binding protein 2]: Precursor of the transcription factor form (Processed sterol regulatory element-binding protein 2), which is embedded in the endoplasmic reticulum membrane. Low sterol concentrations promote processing of this form, releasing the transcription factor form that translocates into the nucleus and activates transcription of genes involved in cholesterol biosynthesis. [Processed sterol regulatory element-binding protein 2]: Key transcription factor that regulates expression of genes involved in cholesterol biosynthesis. Binds to the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3'). Has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3'). Regulates transcription of genes related to cholesterol synthesis pathway (By similarity). Activated by mediated cholesterol efflux, transactivates NOTCH and promotes hematopoietic stem and progenitor cell emergence.
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A3KNL5
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ATF1A_DANRE
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ATPase inhibitor A, mitochondrial (ATP synthase F1 subunit epsilon A) (Inhibitor of F(1)F(o)-ATPase A) (IF(1) A) (IF1 A) (Protein pinotage)
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MARLLLRRGFFSSHIRMSSDQLGELGTGAGKGGGGGGSVRAAGGSFGRREAAEEERYFRQKEREQLAALKNHHEEEIDHHKKEIERLQREIDRHKGKIRKLKHDD
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Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase (By similarity). Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing fech to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme.
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A3KPA0
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JAM3B_DANRE
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Junctional adhesion molecule 3B (Jam3b) (Junctional adhesion molecule C) (JAM-C)
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MALTPLACVLLLLSMQCYISTLAVLLKSTNSKPWVNEFESIELSCMIESITTTKPRIEWKKIKNGDPSYVYFDNQISGDLERRAKIREPATLVILNATRSDSADYRCEVTAPNDQKSFDEILISLTVRVKPVVPRCSVPKSIPVGKPAELHCLEDEGYPKSQYQWFRNKEEIPLDPKSSPKFFNSTYTLDGEMGTLKFSAVRKEDAGEYYCRAKNEAGISECGPQMMEVYDINIAGIILGVVVVVMVLLCITVGIFCAYKRGYFTSQKQTGNNYKPPAKGDGVDYVRTEDEGDFRHKSSFVI
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Junctional adhesion protein that mediates heterotypic cell-cell interactions to regulate different cellular processes (By similarity). During myogenesis, it is involved in myocyte fusion through the binding of jam2a on neighboring myocytes.
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A3KPF2
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ANM14_ARATH
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Probable histone-arginine methyltransferase 1.4 (AtPRMT14) (EC 2.1.1.319) (Coactivator-associated methyltransferase 1B) (Protein arginine N-methyltransferase 4A) (AtPRMT4A)
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MEIPSLNKQQEFTLASVTDLTSPSSSLSSSPVVATFSCVNEVKELRFQESKSSDGFSFDLSSTQLFKLGPLQFTCVSDGSISSAKEKSSFSRGVVIKFRDEKDSKEFCDSFEECKKDDAVKQGSALPNGTVVSANKSKFDDKIEAASAKMYFHYYGQLLHQQNMLQDYVRTGTYHAAVMENRSDFSGRVVVDVGAGSGILSMFAALAGAKHVYAVEASEMAEYARKLIAGNPLLAERITVIKGKIEDIELPEKADVLISEPMGTLLVNERMLETYVIARDRFLSPNGKMFPTVGRIHMAPFADEFLFVEMANKALFWQQQNYYGVDLTPLYVSAHQGYFSQPVVDAFDPRLLVAPSMFHVIDFTMMTEEQFYEIDIPLKFTASVCTRIHGLACWFDVLFDGSTVQRWFTTAPGAPTTHWYQIRCVLSQPIHVMAGQEITGRLHLIAHSAQSYTINLTLSAKMWGPGANQGGILQTSSCKLDLKEPYYRMSQPQVYPTQEPPAQSQDIHIHSDDLEELELLQQNANAQL
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Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, and mRNA stability. Recruited to promoters upon gene activation, methylates histone H3 and activates transcription via chromatin remodeling.
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A3KPP3
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MOG1_DANRE
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Ran guanine nucleotide release factor (RanGNRF) (Ran-binding protein MOG1)
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MSRPLFGGALSAVFPSSVMDISELRQIPDNQEVFAHSQTDQSIIIELLEYQSQVQDADAARYHFEDVAGSNKAIENGTWEVRVVEQVPQSEISMQECSSAWLLSGAQLVSKFNEEAKNTVNVHQCLFRLPQFTTDILMTFNDPVFINPLSSSAAGNMEAIPWTLQDFQGVLQSLRLLDSGVFG
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May regulate the intracellular trafficking of RAN. Promotes guanine nucleotide release from RAN and inhibits binding of new GTP. Plays a role in the regulation of the levels of GTP-bound RAN in the nucleus (By similarity). Required for normal expression of the ion channel hcn4 and for normal expression of the cardiac transcription factors nkx2.5, gata4 and hand2 during embryonic development. Required for normal embryonic heart development and normal heart rate.
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A3KPQ7
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CEIP2_DANRE
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Cell surface hyaluronidase (EC 3.2.1.35) (Cell migration-inducing hyaluronidase 2) (Protein frozen ventricle) (Protein wickham) (Transmembrane protein 2)
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MQVNDGPSSHPIFVAPVNGNAQRSSGYVPGRIVPVRSPPPAKAPPPPPLKPPVPPPARPSVFNLSEDGNRREQAQNQQRKNTYICVGIFFGIFLLILILVLSLTSKDVLDENCPHQNPALRSWKPGHDLKKVVVIHSGEHYRLDSSATLYSITIQAGGSVVFADDKKGSKNITLRTRHILIEDGGALHIGAPKCRYRSLATITLVGRSDETAVTEVPGMGRKFLGVNSGGTLELHGSERMSWTFLTRTVPASGLATGDHAFQKNFSRGINLRVVDQDTAEVLVNERFDTHESQDDSKRLGELLKALPAGRIVALATGDSAVKNLVFETKQTIHDLLGSNYISDLKYRDAWALVSVIGGGNGSCTEDVREHENHDTGGKALARQDFFTVDGVGFTVTAYSEWSNGYPTTGFQVDAVDKVVLNLQDDVSSWNPGDRIVVASTDYSMYQAEEFTLLPCPNCNRKQVQIQGKPQFSHVGEILDGVDMRAEVALLSRNILIHGEMENSCYGGNWCQYFSYDTFGGHIKILGNFTSVHLSHIELKHMGQQREKGRYPLNFHRCGDVDQSGGYSNPAYVDSLSIHHSFSRCVTVHATNGLLVKDTVGYDTLGHCFFLKDGIEQRNIFFHNLGLLTRPGTILPTDRNDSMCTEITDRVYKGYIPIPANECKAVSSFWIAHPNNHLISNSAAGSQDAGIWYVFHNSSTGDSHGMISETKAELTPLGTFFNNRVHSNFKAGLFIDRKVKSTNATAADPREYLCLDNSARFRPHESSDPSRPRVAAIIDTLISFKNNDLGAWIRGGDIIIRNSGDGSYPKDEGSSQEVSQSLFIGESRNRGTNGGQNKYWGIGGVDGKMRTLPRNKTFPIRGFQINDGPVRIFDSTFRAFSPTADRFTMAVGFSLKNIWQLTPRNNLSALAFHPSVTLRAFFGRPGDWFEQNDLDGDKNSIFHDLDGSISGYADTYVARADNFLIRHPQCVDMPQWNGVVCSGKYSQVYIQTQAASNLSLSISRDEYPDKPMVLRGIRTKTSPSQQYQPVLMMGKSYTMHWNGPAPRETVLSLINFDQDDWALLGLCYPNETVFQITSDIYNKQNNGFEGIEDYGPVTSIADLEKRQQERKYFFDKSAGLLWLYARARHRRDGNSYCSSAGCERVKIIATIRANQKTETCNCTANAYPKYSKPASNIVPMPKPNTEPCGACGASQFAFSSDPWNSYLQTQIKSLSVKEEQDNDTQAYITVNAQRFDLSQSGFLLVTVDACSGKVTKNSMFSSLDTKMEQFFKTGIMKRSIVLLATRGQPASFAGVAQYLESLGSAKTPDLQNKVAIAFFGFLGQGGPSPQPWSTLLTCQGAKILGLQERFIPLSLEEYSCPPKKDSPTRMDLELLKKIS
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Cell surface hyaluronidase that mediates the initial cleavage of extracellular high-molecular-weight hyaluronan into intermediate-size hyaluronan. Acts as a regulator of angiogenesis in embryos by mediating degradation of extracellular hyaluronan, thereby promoting VEGF signaling. Acts as a regulator of heart development during myocardial and endocardial morphogenesis: involved in the looping stage of heart morphogenesis. Stimulates migration of endocardial cells and increases both myocardial and endocardial fusion. Involved in the restriction of endocardial cushions (ECs) formation to the atrioventricular canal (AVC). Also required for muscle fiber attachment. Is very specific to hyaluronan not able to cleave chondroitin sulfate or dermatan sulfate (By similarity).
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A3KPW9
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BAG6_DANRE
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Large proline-rich protein BAG6 (BCL2-associated athanogene 6) (HLA-B-associated transcript 3)
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MEESGVIEVTVKTLDSQSRTFTVRGEWTVKQFKEHIAASVEISVDKQRLIYQGKVLQDERTLTEYNVDGKVIHLVERPPPQSSQPGGGGGGVSGSSGAADGGSSSSQSSAYTTSHDRNANNYVMLGTFNLPVNIMDPQQIQMSVQQMLAGVGEMGRNVRVSTSTGSSGSVDVHINVDQSVQSEPRMRLHLAENLLRETQALIHRLEGQSSEPSQQETPPPQPSSSSFSAHPMDSSPPPPSVSSSASQTEGETQSGPNHPSPLELVEVLSEVRRVEERLRPFMERTHSILGAATSADYNNNTQEREEDQRTLNLIGESLHLLGNTLVALSDLRCNLSAQPPRHLHVVRPMSHYTSPVMMQSGLPHIPIPMNLGSTVTMTSNSRQTSDGQPQPPHSSNQSDQQGQAPPTPANESNQQTGHGQGTPRVIRITHQTMEPVVMMQMNLDGTTVPLHVPGLPPEFMQAIMHQISQQAVTMATAASAGHQGQQQGTAGAGAQNGESPVPPPPQARVVITRPTLSPRVPQPMGTRGTTINLRAAVPPPSGQQTNQMVSGLVGQLLLPLHTGDQTSTTSSSHSFSFSTSSSTSSSSSFSSASPPLSSANTSGQTSTHTTSTASVGQAQESGPGDNLAQLLGSLLGGAAGAGGGVSGATPSITVTVPGVPAFIQGLSEFIQSGQPVFPSPNQQPPPSQATPPSAPSGPAPTTAPSGGAETLSPELFTGIVQGVLSTMMGSLGAGQGNTESIAQFIQRLSQTSNLFTPGAGDAVGFFGDLLSLVCQSFSMVDMVLLLHGNPQPLSRIQPQLTAFFTEHYLQGREPTDANIASASEDLINELEEYIAESFSTVTVREGVDIIQTNMSFLRQQFTRMATHILRCTDNTFGQRLLYLCTQGLFECLALNLYCLRGEQRALTTVINHRIRRMSAEVNPSLVNWLTSMMSMRLHVILEHNPVTEDQIQHYVIYTQSESARRTEAGSQSSQQSQNMNVEEGLSPAPATTAEEALRSTGDTDGDEAPGRPSAEETRGAVAMATTEREESTGEAEPWAATVPPEWVPIIRRDMLTQRKMKAQPPLSDAYMHGMPAKRRKTAQGEGPHLSLTEAVSRAARTAGVRPVTAPDSLQGELETPELQEAYAQQVKSDIKKRLSDDPDYNHQRFPNTHRVFSEDA
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ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. Functions as part of a cytosolic protein quality control complex, the bag6/bat3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The bag6/bat3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Similarly, the bag6/bat3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The bag6/bat3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome. Also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. Also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. May ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress. By stabilizing a large spectrum of proteins, may indirectly affect different biological processes including apoptosis. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. When nuclear, may also act as a component of some chromatin regulator complex.
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A3KQH2
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DRC9_DANRE
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Dynein regulatory complex protein 9 (IQ domain-containing protein G)
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MTSVEELRACALLQDCADQLSVLGNIIRPGAETQQRTELHLKTAQLMAGSSLSNFSGELKSQKHFKIQQTLLASDNLAKVQKDRQFVSDVINALLEELQKKNNFQSLFSAVAEERKKKAELLDIINREEEGRRQIKKLQKQLLDIRKEKTEECERLEEEVAILKDQVQDMRVRTNQQGKFVKSCAEQLVYQESKHNSYKENELEDEVKMLQEKIEEEKNVHFETEAFLKQQHANLKQKLQYWIHRYEKDMEEKEQEITALQNKRNSSQTRIQDLSKKCKDMENVVIEDRIEKEHLRAQMEKEQREKNAATKIQAWWRGTLVRKGPRSKKADKSKKKDGKKGKKKRK
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Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes (By similarity). Binds calmodulin when cellular Ca(2+) levels are low and thereby contributes to the regulation of calcium and calmodulin-dependent protein kinase IV (camk4) activity contributes to the regulation of camk4 signaling cascades. Plays a role in the regulation of definitive hematopoiesis via its effects on camk4.
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A3LSZ2
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ARO1_PICST
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Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
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MTSVEKVSILGAETIHVGYGIQDHIVQEVISHLASSTYVIVTDTNMARTTPFTKLRNKFESKLKELRPESRLLFYSVSPGENNKNRETKAAVEDFLLQQGCTRDTVILAVGGGVIGDMIGFVAATFMRGVRVVQVPTSLLAMVDSSVGGKTAIDTPLGKNFVGAFHQPEYVFADVSFLETLPTRQFINGMAEVVKTAAIWNEEEFTRLEKFSKKFLAVVSAKTPDLISIKEELVKTVLESIRVKAFVVSSDEKETGLRNLLNFGHTIGHAIEAVLTPQALHGECVSIGMIKEAELARYLGVLSPVAVARLSKCLVAYGLPVSIDEKDFLKKVGNKRHNVEIDILLKKMAIDKKNDGSKIRCVILEAIGKCYQLKAHQVSKQDLSFVLTDEVLVHPFDDKLIPKTNVVIPPGSKSISNRALVLAALGTGTVRIKNLLHSDDTKHMLEAVASLKGASISTEDNGETIVVTGNGGKLVSCDEQLYLGNAGTASRFLTSVAPLVGINPQSGEHVVLTGNARMQERPIGPLVDALRANGSEIDYLNKEGSLPLKVKAGKGLNGGRIELAATISSQYVSSILMCAPYANEPVTLSLVGGKPISQLYINMTIAMMKTFGIVVTKSETEEHTYHIPRGSYVNPKEYVIESDASSATYPLAFAALTGTSCTIPNIGSSSLQGDARFAVDVLRPMGCEVVQTATSTTVTGPSVGNLKPLPHVDMEPMTDAFLTASVVAAVAKNGTQSTSITGIANQRVKECNRIAAMVSELAKFGVVANELPDGIEIHGISPNDLVTPSTEKRGIKTFDDHRVAMSFSLLAGLCKDKVLIQERSCTGKTWPGWWDILHTKFKVAIDGYELPLQHEDSTALVEKHGNGKRSIIVIGMRGAGKSTLSKWMASFLGFKLVDLDDVLEEKIGTDIRSFVQQQGWEEFRKQEAIVAKESFIKFSEGCVLSTGGGIVEGEEARESLKSYVKSGGIVLHLHRDLDETVVLLSADTTRPAYVDEIKQVWLRRENWYRECSNYHFYSAHCSSDAEFKHLRNSFTTYIKTITGFHVAQIPKKRSFYTSLTFSDLTEVASSLEDISTGSDAIELRVDLLKETTHTFVADQTAILRKSTNLPIIYTIRTESQGGKFPDNKFEELEELLALGIKLGVQYLDLQLDLPNDLLERILESKKFTKIIASYVDVSGSLRWDNVEWKNRYNQGVSLGADLVKLVGRANSFQDNLSLEVFRGTSTLKPLIAYNVGEKGKLSRVLNPRLTPVTHAKIPAESGNEGALDVAQINKAYTDIGGLSEKHFWIVGNPVGHSRSPNLHNAGYKKLNLPYVFDRFETSDAGEAFQKLIKEDKNFGGLAVTMPLKVDIMKYTDKLSDSAQVIGAVNTVIELEGEQGKYLGENTDWVGISESFVRDGIPNLENVNVNGLVVGGGGTSRAAVYALHQLGCKKIYMLNRTVSKIQEIQKNFPAEYNIEILDSVEAVEAAQPISLIVSCIPADKPIDEQLLNKLERVLYVGGEAKIGGFTPSLLEASYKPRVTPIMKIASEKYEWNVIPGVEMLVNQGITQFQLHTGFVAPYDVVHDAVVNQ
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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A3MTK6
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CAS4_PYRCJ
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CRISPR-associated exonuclease Cas4 (EC 3.1.12.1)
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MELLSPKPLCSVVNCEDLEKLDHVSALNELRREQEIFKLLPGIYAHRYDFRRVSPSIINDFEYCPRLLWVQHKLGLKLLSEKSVVSIIRGRILHERYERLLSQYENVVAEYKVEIGDLVGVVDLVIKRGGEYIPVEIKTGFSKEAHKTQLQIYISMLKARFGYLVYRNHVEVVHRNDAALDVLKKIREILSAREAPPAKCNSCIFKPICKNLL
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CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). A ssDNA exonuclease that has 5' to 3' activity, yielding 5'-OH and 3'-phosphate groups. Has Mn(2+)-dependent endonuclease activity on circular ssDNA. Can unwind dsDNA unwinding does not require ATP.
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A3MTW6
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THIL_PYRCJ
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Thiamine-monophosphate kinase (TMP kinase) (TP kinase) (Thiamine-phosphate kinase) (EC 2.7.4.16)
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MSGFGGRGVDEKGFLRWLLGELGVEEDDVAYVDGLVVKVDGAAASTSRLPFQTWADFGWRNVAAAYSDVRVKFAEARLLLASVTAPDLGTAAEVVQGVREASQFFSLAYVGGDLNEGRDVVVDVVLVGWARARVGRAPRPGDVLVTIPQFGYTSLAYRFWQMGGAVVERGVEALKRPKPLWPLPPAECVTAAMDSSDGLGDVLWSMARGVDIVVKELPAPREVLEFAAERGLDVGEIVFNGGEEFLPVFAVRRDCPVESPYVSFAEVVPGEGRVWWRGEELKWRGWAYFRGWG
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Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1. {ECO:0000255|HAMAP-Rule:MF_02128, ECO:0000269|PubMed:26639844}.
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A3MUY9
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DHE2_PYRCJ
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NAD(+)-dependent glutamate dehydrogenase (NAD-GDH) (EC 1.4.1.2) (NAD-specific glutamate dehydrogenase)
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MSTTYIVSDFLINTLLTIKRGVELAGLPPEFYEALEKPKRILVVNIPVKMDDGKIKYFEGYRVQHNDALGPFKGGIRFHPEVTLADDIALAMLMTLKNSLAGLPYGGAKGAVRVDPRRLSRRELEELARGYARAVAPLIGEQLDIPAPDVGTDSQVMAWMVDEYSRLVGRNAPAVFTSKPPELWGNPVREYSTGFGVAVAAREVAKRLWGGIVGKTAAVQGLGNVGRWAAYWLEKMGAKVVAVSDVNGVVYRERGLDVDLIRETKAKGPQLLEMISQKNGVEIVKNPDQIFSLDVDILVPAAIENVVREDNVDGVRARLVVEGANGPTTPGAERRLYERGVVVVPDILANAGGVIMSYLEWVENLQWLFWDEEETRRRLEAIMSNNVARVYARWEKEKSWTMRDAAVVTALERIYNAMKTRGWI
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Catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate and ammonia, thereby playing a key role at the intersection of the carbon and nitrogen metabolic pathways. Is strictly specific for NAD(+)/NADH as the acceptor/donor, since it cannot use NADP(+)/NADPH. May function in vivo in the catabolic direction. Also catalyzes at low rates the oxidative deamination of L-norvaline, L-2-aminobutyrate, L-valine and L-isoleucine, and the reductive amination of 2-oxovalerate and 2-oxobutyrate.
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A3MWK6
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DHE4_PYRCJ
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NADP(+)-dependent glutamate dehydrogenase (NADP-GDH) (EC 1.4.1.4)
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MSQNGQFLEYTLQVIRRGVEMGGFPEDFYKLLSRPKRIIQVSIPVKMDNGSYEVFEGYRVQHNDALGPFKGGIRFHPEVTLADDIALAMLMTLKNSLAGLPYGGAKGAVRVDPRRLSRRELEELARGYARAVAPLIGEQLDIPAPDVGTDSQVMAWMVDEYSKLAGRNAPAVFTSKPPELWGNPVREYSTGFGVAVAAREVAKRLWGGIEGKTVAVHGAGNTGAWAAYWLEKMGAKVVAISDTRGTVVNKAGIPGEQILKVYMEKKRDKSATVLALEGEKIADSNASLYQDVDILVPAAIENVVREDNVGLVRARLVVEGANGPTTPGAERRLYERGVVVVPDILANAGGVIMSYLEWVENLQWLFWDEEETRRRLEAIMSNNVARVYARWEKEKSWTMRDAAVVTALERIYNAMKTRGWI
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Catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate and ammonia, thereby playing a key role at the intersection of the carbon and nitrogen metabolic pathways. Shows a high preference for NADP(+)/NADPH as the acceptor/donor over NAD(+)/NADH. May function in vivo in the synthetic direction. Also catalyzes at very low rates the oxidative deamination of L-2-aminobutyrate, and the reductive amination of 2-oxovalerate and 2-oxobutyrate.
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A3Q3N5
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KGD_MYCSJ
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Multifunctional 2-oxoglutarate metabolism enzyme (2-hydroxy-3-oxoadipate synthase) (HOA synthase) (HOAS) (EC 2.2.1.5) (2-oxoglutarate carboxy-lyase) (2-oxoglutarate decarboxylase) (Alpha-ketoglutarate decarboxylase) (KG decarboxylase) (KGD) (EC 4.1.1.71) (Alpha-ketoglutarate-glyoxylate carboligase) [Includes: 2-oxoglutarate dehydrogenase E1 component (ODH E1 component) (EC 1.2.4.2) (Alpha-ketoglutarate dehydrogenase E1 component) (KDH E1 component); Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex E2 component) (ODH E2 component) (OGDC-E2) (Dihydrolipoamide succinyltransferase)]
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MSSSPSPFGQNEWLVEEMYRKFREDPSSVDPSWHEFLVDYNPEPTTDSSASENGQQTRTAAPKAPPEPAPAPAPKSQDSKSQAPKQDSKPQESKPQAKAKPAESKSSTKPADAKSEKSGKSGTNGAAKPAAQPADDSDQNQVLRGAAAAVAKNMSASLDVPTATSVRAIPAKLMIDNRVVINNHLKRTRGGKISFTHLIGYAIVAAVKKFPNMNRHFAEVDGKPNAVTPAHTNLGLAIDLQGKDGNRQLVVAAIKKADTMRFGQFIAAYEDIVRRARDGKLTAEDFSGVTISLTNPGTIGTVHSVPRLMRGQGAIIGVGAMEYPAEFQGASEERIADLGIGKLITLTSTYDHRIIQGAESGDFLRTVHQLLLSDDFFDEIFRELGIPYEPVRWRTDNPDSIEDKNARVIELIAAYRNRGHLMADIDPLRLDSNRFRSHPDLDVLTHGLTLWDLDREFKVNGFAGAERKKLRDVLAVLRDAYCRHIGVEYTHILEPEQQQWLQERIEGKHEKPTVAQQKYILSRLNAAEAFETFLQTKYVGQKRFSLEGAETVIPAMDAVIDQCAEHALDEVVIGMPHRGRLNVLANIVGKPYSQIFSEFEGNLNPSQAHGSGDVKYHLGSSGTYLQMFGDNDITVSLTANPSHLEAVDPVMEGLVRAKQDLLDKGDTEDGYTVVPLMLHGDAAFAGQGVVAETLNLALLRGYRTGGTIHLIVNNQIGFTTSPAAAKSSEYCTDVAKMIGAPIFHVNGDDPEAAVWVSRLAVDFRQKFKKDVVIDLLCYRRRGHNEGDDPSMTQPSMYDVIDTKRGVRKSYTEALIGRGDISMKEAEDALRDYQGQLEQVFNEVRELEKHEIEPSESVEADQQIPAKLATAVDKSLLARIGDAHLAVPEGFTVHPRVKPVLEKRREMAYEGKVDWAFAELLALGTMISEGKLVRLSGQDTRRGTFTQRHSVVIDRKTGKEFTPLQLLATDSDGNPTGGKFLVYDSPLSEFAAVGFEYGYSVGNPDAMVLWEAQFGDFINGAQSIIDEFISSGEAKWGQLSDVVLLLPHGHEGQGPDHTSGRIERFLQLWAEGSMTIALPSTPANYFHLLRRHSLDGIQRPLIVFTPKSMLRNKAAVSDIRDFTEQKFRSVLEEPTYTDGDGDRNKVTRILLTSGKIYYELVARKNKESRDDVAIVRIEQLAPLPKRRLAETLDKYPNVDEKFWVQEEPANQGAWPTFGLTLPEMLPDHFTGIKRISRRAMSAPSSGSSKVHAVEQQEILDEAFAP
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Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle (By similarity).
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A3Q8U4
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FADB_SHELP
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MIYQSPTIQVELLEDNIARLCFNAEGSVNKFDRETLNSLNDALDALAQTQGVKGLMLTSGKDAFIVGADITEFLGLFAQDDNVLQGWLEDANKVFNKLEDLPFPTISAIKGFALGGGCETILATDLRIADTSARIGLPETKLGIIPGFGGTVRLPRVIGADNALEWITTGKDQRPEAALKVGAIDAVVAPELLETAACQMLQDAISEKIDWQARRQRKLSPLTLPKLEAMMSFATAKGMVFKVAGKHYPAPMAVVEVIEKAALSERAEALQVEHQAFIKLAKTDVAKALIGIFLNDQLVKGKAKKAAKQAQAVNSAAVLGAGIMGGGIAYQSASKGTPIVMKDINQAALDLGLNEAAKLLTAQINRGRSTPAKMAGVLNNITATLDYNALKQADVVVEAVVEHPKVKATVLAEVEQVVGEDAIITSNTSTISINLLAKSLQKPERFCGMHFFNPVHKMPLVEVIRGEHSSEETVASVVAYAAKMGKTPIVVNDCPGFFVNRVLFPYFAGFSGLLEDGADFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMAEGFPDRMAKEGKDAIDVMFEADRFGQKNGKGFYQYSVDRRGKPKKEVDPLSYELLGNAFGEQKEFSSDEIIARTMIPMIIETVRCLEEGIIATPAEADMGLVYGLGFPPFRGGVFRYLDTLGVANFVALADQYAHLGGLYQVTDKMRELAATNGSYYPA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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A3QJU3
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COQ8B_DANRE
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Atypical kinase COQ8B, mitochondrial (EC 2.7.-.-) (AarF domain-containing protein kinase 4) (Coenzyme Q protein 8B)
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MLLSEVLQVLRGAGKVGAAFTSTQGEQLRLMACNSTFGAGMKAAAEAVEGVMGTVMGGGDMTSKTDEFAGIEKWEEMDLDEAAKWSVASEMPPDFSSKDGRGETSETPVGAATGTIKGAGWPAQNTRFLHVSASQHHFRFVHDSIVARLSPEDIQRAREAKQNIARPVRQKLNERAKERKVPATRISRLANFGGLAVGLGIGAIAEVAKQSFGGKRSEVGALLDSPLLSEANAERIVNTLCKVRGAALKIGQMLSIQDNSFINPQLQKIFERVRQSADFMPAWQMHKVLEEELGSGWREKLSSIEEKPFAAASIGQVHHGVLPGGKEIAMKIQYPGVAESIHSDINNLMSVLKMSVVLPDGLFADSSLEVLQRELAWECDYEREAKCAKRFRNLLKGDPVFVVPEVFDELSARRVITMELVNGVPLDRCVDLDQETRNEICFNILQLCLRELFEFRFMQTDPNWSNFFYNSEQNKIFLLDFGACRDYPELFTDHYIEVVHAASVGDRATVLKKSKDLKFLTGFEAKAFEDAHVEAVMILGEAFASAEAFDFGTQSTTQRIQSLIPVMLRHRLTPPPEESYSLHRKMAGSFLICSKLKARFSCRNMFLDVYNAYKRQQQERRSQV
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Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Its substrate specificity is unclear: does not show any protein kinase activity. Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway. Required for podocyte migration.
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A3QM97
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CNNM1_CAEEL
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Metal transporter cnnm-1 (CNNM family homolog 1)
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MSASCLRLLTLSLFILGQCNVTAAQNGVDDEVTTVTAILDSATTAAADNSTVPTQSASNNNTSQSSKIPTIFGMRVELPADDPFGYDKHGVCSVTPEEEFKVVIYGNHLDKIHQIIWTFTNNCSEPAYVIDALNHFKVHFNHKATFHLTLKLLPEMVHAYKMCVKPKVAPGSPPLGEIYPLDDISTWLTTERPPKEYFLPLPLQIACIGFLLCLSALFSGLTLGLMSLTPQELELVIKSGAIKEQKCAAKILPVRKKGNLLLCSLLLGNVIVNSAISILMGELTTGIYALIGSTMGIVIFGEILPQSICVKKGLEVGAHTISITQLFIFLTFPIAWPVSKLLDCLLGDEYQAYDRKRLMELIKMSITDNGQVSNELKIAVGAMEIADKVVKDVMTKIEDVFMLPDTTVLNAKTVMEIVKMGYTRIPVYQYGDKNNVTDMLFVKDLALLDPDDNFTVKTVCGYHKHPVKFVMNDTPLPNLLEAFKKGEGHLAMVKRLINTDDKHDPSYVLVGVVTLEDIVEEILQAEINDEFDIVSDNVNKVKIKKEQNRDATKYFGDHEAPQTMISMQLQMVALQWLVSNERGFRQEFLDTNVLERLIRSSARRVDVSALMAMGDDAINVPRLAKVYTKDELSDKYILILEGRIQVTIGASGMMFEAGPWHHFGGEIMAKLVDGAATLGRSMSIVGTSELSARRPDLMFKPDYSAVVKEDCTYLEISVSAYINAYKASLMQRERPLNDLSDVSHNSSAHNSNLSLVEKPGPITDPSAMLVPENVRKPSVVSMDSPKILVGLGQHPVAPVAEEEEMALLDQP
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Probable metal transporter. Probably acts redundantly with the other metal transport proteins cnnm-2, cnnm-3, cnnm-4 and cnnm-5 to regulate Mg(2+) homeostasis. Promotes postembryonic gonad development by regulating Mg(2+) levels, probably via AMPK signaling.
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A3R052
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PILR1_LINPE
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Bifunctional pinoresinol-lariciresinol reductase (PLR-Lp1) ((+)-pinoresinol reductase) (EC 1.23.1.1) ((-)-lariciresinol reductase) (EC 1.23.1.4)
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MKPCSVLVVGGTGYIGKRIVSASLYLGHDTYVLKRPGTGLDIEKLQLLLSFKKRGAHLVEASFSDHDSLVRAVRLVDVVICTMSGVHFRSHNILLQLKLVEAIKEAGNVKRFIPSEFGMDPARMGQAMEPGRETFDQKMVVRKAIEEANIPHTYISANCFAGYFVGNLSQLGTLTPPSDKVIIYGDGNVKVVYVDEDDVAKYTIKAIEDDRTVNKTVYLRPPENMMSQRELVAVWEKLSGNQLEKIELPPQDFLALMEGTTVAEQAGIGHFYHIFYEGCLTNFEINAENGEEEASRLYPEVEYTRVHDYLKIYL
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Reductase involved in the lignan justicidin B biosynthesis. Catalyzes the enantioselective conversion of (+)-pinoresinol into (+)-lariciresinol and of (-)-lariciresinol into (+)-secoisolariciresinol. Low activity with the other enantiomers. Abstracts the 4R-hydride from the NADPH cofactor during catalysis.
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A3R064
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DOK3_CHICK
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Docking protein 3 (Downstream of tyrosine kinase 3)
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MERPVKDGIIYVQHCKFGKRTWRKIRAQLFAASPFGVARMEKFDARDHGTVSDISLQRCARRVIRLSDCVSVGPMGTESCPKATAAFYLTTTEKNYVLAAEQRDEWIEQLCQLAFQGKKEAEQSSSTGLQPIPMEENCLYSSWQDLTEFPVLVLRTEAAARCELHGHYVLAALPHSLTLKDAQSQQPLLTWPYPFLRKFGQDQNIFSFEAGRRSDSGEGTFTFSTPRAAELCRAVAAAIACQQQGQESPQPSAQGLSNQPWGAEAEDPQCSPTLGRAHSGSHSASYPSLNLLRFPPVEPEAPAPIVYASIARGQQPHFRPCPGQPLPEHLYENIFTAQPRPLAEEEAEEEEGRWELGCRQAPEGHSSEAAVPYPARSAPQPHTQRWAPGGSRGGAEEPSRPKPQRTLRAKLVRLLSRDGPGARDWS
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DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. Plays a role as negative regulator of the mobilization of calcium ions and of calcium signaling.
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A3R0T9
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VM3_OPHHA
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Zinc metalloproteinase-disintegrin-like ohanin (EC 3.4.24.-) (Snake venom metalloproteinase) (SVMP)
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MIQVLLVTICLVVFPYQGSSIILESGKVNDYEVVYPQKIPVLPKSKIQRREQKMYEDTMKYEFKVNGEPVVLHLERNKELFSKDYTETHYSPDGREITTSPPVEDHCYYHGYIQSDIDSTAILNACNGLKGYFRHHGEAYHIEPLKFSDSEAHAVYKYENIEKEDETPKICGVKHSTWESDEPIEKISQKKDFLEEKKYLELYIVADYVMFRKYGRNVTTIRMRVFDMVNYITVVYKALNIHVALIGFEIWSLKDKFVINASTKNNLLHFSIWRSTVLRKRNDNAQLLTGVDLNGYTLGSAYLKAMCDVLQSVGIVQDYSKSPYLVGAAMAHEIGHNLGMEHDTKTCSCMRGNCIMSPEEEGSDFPMEFSSCSLYDFQNYMLTDTPQCLINKPSNTSIIKNAVCGNYVEEEGEECDCGSPEQCENNCCEAATCKLKPGAKCAKGACCKKCQFKKAGAECRAARNECDLPEFCIGQSAECPMDRFHKNGHSCQNDQGYCFRGYCPTLAKQCITLWGSDAKVAPDECFQNNTNGNEYDYCKKTNNVIIPCKPTDVKCGRLYCTGGTENPSEGEKISSDPCKASYSEIEDIGMVDHRTKCGEKMVCSDGKCIPL
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Snake venom zinc metalloproteinase that has hemorrhagic activity. Inhibits ADP-, TMVA- and stejnulxin-induced platelet aggregation in a dose-dependent manner (on washed platelet, but not on platelet rich plasm). Also specifically degrades alpha-chain of fibrinogen (FGA).
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A3RF67
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BAGBG_DALNI
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Isoflavonoid 7-O-beta-apiosyl-glucoside beta-glycosidase (EC 3.2.1.161) (Beta-glycosidase)
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MHAMTFKAILLLGLLALVSTSASIAFAKEVRATITEVPPFNRNSFPSDFIFGTAASSYQYEGEGRVPSIWDNFTHQYPEKIADGSNGDVAVDQFHHYKEDVAIMKYMNLDAYRLSISWPRILPTGRASGGINSTGVDYYNRLINELLANDITPFVTIFHWDLPQALEDEYGGFLNHTIVNDFRDYADLCFNLFGDRVKHWITVNEPSIFTMNGYAYGIFAPGRCSPSYNPTCTGGDAGTEPDLVAHNLILSHAATVQVYKKKYQEHQNGIIGISLQIIWAVPLSNSTSDQKAAQRYLDFTGGWFLDPLTAGQYPESMQYLVGDRLPKFTTDEAKLVKGSFDFVGINYYTSSYLTSSDASTCCPPSYLTDSQVTFSSQRNGVFIGPVTPSGWMCIYPKGLRDLLLYIKEKYNNPLVYITENGMDELDDPSQSLEESLIDTYRIDSYYRHLFYVRSAIGSGANVKGFFAWSLLDNFEWNEGFTSRFGLNFVNYTTLTRYHKLSATWFKYFLARDQEIAKLDISAPKARWSSSTMIKEEKRKPKWAIQAF
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Hydrolyzes dalpatein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside and dalnigrein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside. Also has activity towards pNP-beta-D-fucoside and pNP-beta-D-glucoside, but not pNP-beta-cellobioside.
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A3RFZ7
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FCG3A_MACMU
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Low affinity immunoglobulin gamma Fc region receptor III-A (IgG Fc receptor III-A) (Fc-gamma RIII-alpha) (Fc-gamma RIII) (Fc-gamma RIIIa) (FcgammaRIIIa) (CD antigen CD16a)
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MWQLLLPTALLLLVSAGMRAEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTRWFHNESLISSQTSSYFIAAARVNNSGEYRCQTSLSTLSDPVQLEVHIGWLLLQAPRWVFKEEESIHLRCHSWKNTLLHKVTYLQNGKGRKYFHQNSDFYIPKATLKDSGSYFCRGLIGSKNVSSETVNITITQDLAVSSISSFFPPGYQVSFCLVMVLLFAVDTGLYFSVKKSVPSSTRDWEDHKFKWSKDPQDK
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Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger. Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation. Involved in the generation of memory-like adaptive NK cells capable to produce high amounts of IFNG and to efficiently eliminate virus-infected cells via ADCC. Regulates NK cell survival and proliferation, in particular by preventing NK cell progenitor apoptosis (By similarity). Fc-binding subunit that associates with CD247 and/or FCER1G adapters to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapters with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation. The ITAM-dependent signaling coupled to receptor phosphorylation by PKC mediates robust intracellular calcium flux that leads to production of pro-inflammatory cytokines, whereas in the absence of receptor phosphorylation it mainly activates phosphatidylinositol 3-kinase signaling leading to cell degranulation (By similarity). Costimulates NK cells and trigger lysis of target cells independently of IgG binding (By similarity). Mediates the antitumor activities of therapeutic antibodies. Upon ligation on monocytes triggers TNFA-dependent ADCC of IgG-coated tumor cells (By similarity). Mediates enhanced ADCC in response to afucosylated IgGs.
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A3RGC1
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VDR_PIG
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Vitamin D3 receptor (VDR) (1,25-dihydroxyvitamin D3 receptor) (Nuclear receptor subfamily 1 group I member 1)
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MEATAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKDSLRPKLSEEQQRIIAILLDAHHKTYDPTYADFGQFRPPVRGDEEEGTLPSRSSSAHAPSFSGSSSSSCSDQYTSSPDTMEPASFSHLDLSEEDSDDPSVTLDLSQLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTAEDQIVLLKSSAIEVIMLRSNQSFTMDDMSWTCGSRDYKYQVSDVAKAGHSLELIEPLIKFQVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDPTLIEAIQDRLSNTLQTYIRCRHPPPGSHLLYAKMIQKLADLRSLNEEHSKQYRCLSFQPECSMKLTPLVLEVFGNEIS
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Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells. Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR. The VDR-RXR heterodimers bind to specific response elements on DNA and activate the transcription of vitamin D3-responsive target genes (By similarity). Plays a central role in calcium homeostasis (By similarity). Also functions as a receptor for the secondary bile acid lithocholic acid (LCA) and its metabolites (By similarity).
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A3RM23
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L_RABVI
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Large structural protein (Protein L) (Replicase) (Transcriptase) [Includes: RNA-directed RNA polymerase (EC 2.7.7.48); GTP phosphohydrolase (EC 3.6.1.-); GDP polyribonucleotidyltransferase (EC 2.7.7.88) (PRNTase); mRNA cap methyltransferase (EC 2.1.1.375) (mRNA (guanine-N(7)-)-methyltransferase) (G-N7-MTase) (mRNA (nucleoside-2'-O-)-methyltransferase) (N1-2'-O-MTase)]
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MLDPGEVYDDPVDPIESDAEPRGAPTVPNILRNSDYNLNSPLIEDPARLMLEWLTTGNRPYRMTLTDNCSRSYKVLKDYFKKVDLGSLKVGGTAAQSMISLWLYGAHSESNRSRKCITELAHFYSKSSPIEKLLNCTLGNRGLRIPPEGVLSCLERVDYDKAFGRYLANTYSSYLFFHVITLYMNALDWDEEKTILALWKELTSVDIGKDLVKFKDQIWGLLIVTKDFVYSHSSNCLFDRNYTLMLKDLFLSRFNSLMILLSPPEPRYSDDLISQLCQLYIAGDQVLSMCGNSGYEVIKILEPYVVNSLVQRAERFRPLIHSLGDFPVFIKDKVSQLEGTFGPSAKRFFGVLDQFDNIHDLVFVYGCYRHWGHPYIDYRKGLSKLYDQVHIKKVIDKSYQECLASDLARRILRWGFDKYSKWYLDSRLLTRDHPLTPYIKTQTWPPKHIVDLVGDTWHKLPITQIFEIPEPMDPSEILDDKSHSFTRARLASWLSENRGGPAPSEKVIITALSKPPVNPREFLKTIDLGGLPDEDLIIGLKPKERELKIEGRFFALMSWNLRLYFVITEKLLANYILPLFDALTMTDNLNKVFKKLIDRVTGQGLLDYSRVTYAFHLDYEKWNNHQRLESTEDVFSVLDHVFGLKRVFSRTHEFFQKSWIYYSDRSDLIGLWEDQIYCLDMSNGPTCWNGQDGGLEGLRQKGWSLVSLLMIDRESQTRNTRTKILAQGDNQVLCPTYMLSPGLSREGLLYELESISRNALSIYRAIEEGASKLGLIIKKEETMCSYDFLIYGKTPLFRGNILVPESKRWARVSCISNDQIVNLANIMSTVSTNALTVAQHSQSLIKPMRDFLLMSVQAVFHYLLFSPILKGRVYKILSAEGESFLLAMSRIIYLDPSLGGVSGMSLGRFHIRQFSDPVSEGLSFWREIWLSSHESWIHALCQEAGNPDLGERTLESFTRLLEDPTTLNIKGGASPTILLKDAIRKALYDEVDKVENSEFREAILLSKTHRDNFILFLKSVEPLFPRFLSELFSSSFLGIPESIIGLIQNSRTIRRQFRRSLSRTLEESFYNSEIHGINRMTQTPQRVGRVWPCSSERADLLREISWGRKVVGTTVPHPSEMLGLLPKSSISCPCGATGGGNPRVSVSVLPSFDQSFFSRGPLKGYLGSSTSMSTQLFHAWEKVTNVHVVKRALSLKESINWFITRNSNLAQTLIRNIMSLTGPDFPLEEAPVFKRTGSALHRFKSARYSEGGYSSVCPNLLSHISVSTDTMSDLTQDGKNYDFMFQPLMLYAQTWTSELVQKDTRLRDSTFHWHLRCNRCVRPIDDITLETSQIFEFPDVSKRISRMVSGAVPHFQKLPDIRLKPGDFESLSGREKSRHIGSAQGLLYSILVAIHDSGYNDGTIFPVNIYGKVSPRDYLRGLARGVLIGSSICFLTRMTNININRPLELISGVISYILLRLDNHPSLYIMLREPSLRGEIFSIPQKIPAAYPTTMKEGNRSILCYLQHVLRYEREVITASPENDWLWIFSDFRSAKMTYLTLITYQSHLLLQRVERNLSKSMRANLRQMSSLMRQVLGGHGEDTLESDDDVQRLLKDSLRRTRWVDQEVRHAARTMTGDYSPNKKLSRKAGGSEWVCSAQQVAVSTSANPAPVLELDIRALSKRFQNPLISGLRVVQWATGAHYKLKPILDDLNVFPSLCLVVGDGSGGISRAVLNMFPDAKLVFNSLLEVNDLMASGTHPLPPSAIMSGGDDIVSRVIDFDSIWEKPSDLRNLTTWKYFQSVQKQVNMSYDLIICDAEVTDIASINRITLLMSDFALSIDGPLYLVFKTYGTMLVNPDYKAIQHLSRAFPSVTGFITQVTSSFSSELYLRFSKRGKFFRDAEYLTSSTLREMSLVLFNCSSPRSEMQRARSLNYQDLVRGFPEEIISNPYNEMIITLIDSDVESFLVHKMVDDLELQRRTLSKVAIIIAIMIVFSNRVFNVSKPLTDPLFYPPSDPKILRHFNICCSTMMYLSTALGDVPSFARLHDLYNRPITYYFRKQVIRGNIYLSWSWSDDTAVFKRVACNSSLSLSSHWIRLIYKIVKTTRLVGSIEDLSGEIERHLRGYNRWITLEDIRCRSSLLDYSCL
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RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all viral mRNAs with a decreasing efficiency. The first gene is the most transcribed, and the last the least transcribed. The viral phosphoprotein acts as a processivity factor. Capping is concommitant with initiation of mRNA transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase) adds the cap structure when the nascent RNA chain length has reached few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and facilitates subsequent guanine-N-7 methylation, both activities being carried by the viral polymerase. Polyadenylation of mRNAs occur by a stuttering mechanism at a slipery stop site present at the end viral genes. After finishing transcription of a mRNA, the polymerase can resume transcription of the downstream gene. RNA-directed RNA polymerase that catalyzes the replication of viral genomic RNA. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The replicase mode is dependent on intracellular N protein concentration. In this mode, the polymerase replicates the whole viral genome without recognizing transcriptional signals, and the replicated genome is not caped or polyadenylated.
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A4D0S4
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LAMB4_HUMAN
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Laminin subunit beta-4 (Laminin beta-1-related protein)
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MQFQLTLFLHLGWLSYSKAQDDCNRGACHPTTGDLLVGRNTQLMASSTCGLSRAQKYCILSYLEGEQKCFICDSRFPYDPYDQPNSHTIENVIVSFEPDREKKWWQSENGLDHVSIRLDLEALFRFSHLILTFKTFRPAAMLVERSTDYGHNWKVFKYFAKDCATSFPNITSGQAQGVGDIVCDSKYSDIEPSTGGEVVLKVLDPSFEIENPYSPYIQDLVTLTNLRINFTKLHTLGDALLGRRQNDSLDKYYYALYEMIVRGSCFCNGHASECRPMQKMRGDVFSPPGMVHGQCVCQHNTDGPNCERCKDFFQDAPWRPAADLQDNACRSCSCNSHSSRCHFDMTTYLASGGLSGGVCEDCQHNTEGQHCDRCRPLFYRDPLKTISDPYACIPCECDPDGTISGGICVSHSDPALGSVAGQCLCKENVEGAKCDQCKPNHYGLSATDPLGCQPCDCNPLGSLPFLTCDVDTGQCLCLSYVTGAHCEECTVGYWGLGNHLHGCSPCDCDIGGAYSNVCSPKNGQCECRPHVTGRSCSEPAPGYFFAPLNFYLYEAEEATTLQGLAPLGSETFGQSPAVHVVLGEPVPGNPVTWTGPGFARVLPGAGLRFAVNNIPFPVDFTIAIHYETQSAADWTVQIVVNPPGGSEHCIPKTLQSKPQSFALPAATRIMLLPTPICLEPDVQYSIDVYFSQPLQGESHAHSHVLVDSLGLIPQINSLENFCSKQDLDEYQLHNCVEIASAMGPQVLPGACERLIISMSAKLHDGAVACKCHPQGSVGSSCSRLGGQCQCKPLVVGRCCDRCSTGSYDLGHHGCHPCHCHPQGSKDTVCDQVTGQCPCHGEVSGRRCDRCLAGYFGFPSCHPCPCNRFAELCDPETGSCFNCGGFTTGRNCERCIDGYYGNPSSGQPCRPCLCPDDPSSNQYFAHSCYQNLWSSDVICNCLQGYTGTQCGECSTGFYGNPRISGAPCQPCACNNNIDVTDPESCSRVTGECLRCLHNTQGANCQLCKPGHYGSALNQTCRRCSCHASGVSPMECPPGGGACLCDPVTGACPCLPNVTGLACDRCADGYWNLVPGRGCQSCDCDPRTSQSSHCDQLTGQCPCKLGYGGKRCSECQENYYGDPPGRCIPCDCNRAGTQKPICDPDTGMCRCREGVSGQRCDRCARGHSQEFPTCLQCHLCFDQWDHTISSLSKAVQGLMRLAANMEDKRETLPVCEADFKDLRGNVSEIERILKHPVFPSGKFLKVKDYHDSVRRQIMQLNEQLKAVYEFQDLKDTIERAKNEADLLLEDLQEEIDLQSSVLNASIADSSENIKKYYHISSSAEKKINETSSTINTSANTRNDLLTILDTLTSKGNLSLERLKQIKIPDIQILNEKVCGDPGNVPCVPLPCGGALCTGRKGHRKCRGPGCHGSLTLSTNALQKAQEAKSIIRNLDKQVRGLKNQIESISEQAEVSKNNALQLREKLGNIRNQSDSEEENINLFIKKVKNFLLEENVPPEDIEKVANGVLDIHLPIPSQNLTDELVKIQKHMQLCEDYRTDENRLNEEADGAQKLLVKAKAAEKAANILLNLDKTLNQLQQAQITQGRANSTITQLTANITKIKKNVLQAENQTREMKSELELAKQRSGLEDGLSLLQTKLQRHQDHAVNAKVQAESAQHQAGSLEKEFVELKKQYAILQRKTSTTGLTKETLGKVKQLKDAAEKLAGDTEAKIRRITDLERKIQDLNLSRQAKADQLRILEDQVVAIKNEIVEQEKKYARCYS
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Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
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A4D126
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ISPD_HUMAN
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D-ribitol-5-phosphate cytidylyltransferase (EC 2.7.7.40) (2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase-like protein) (Isoprenoid synthase domain-containing protein) (hISPD)
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MEAGPPGSARPAEPGPCLSGQRGADHTASASLQSVAGTEPGRHPQAVAAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYQHKRISLVEAGVTRHRSIFNGLKALAEDQINSKLSKPEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSLERARHRASEMPQAFLFDVIYEAYQQCSDYDLEFGTECLQLALKYCCTKAKLVEGSPDLWKVTYKRDLYAAESIIKERISQEICVVMDTEEDNKHVGHLLEEVLKSELNHVKVTSEALGHAGRHLQQIILDQCYNFVCVNVTTSDFQETQKLLSMLEESSLCILYPVVVVSVHFLDFKLVPPSQKMENLMQIREFAKEVKERNILLYGLLISYPQDDQKLQESLRQGAIIIASLIKERNSGLIGQLLIA
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Cytidylyltransferase required for protein O-linked mannosylation. Catalyzes the formation of CDP-ribitol nucleotide sugar from D-ribitol 5-phosphate. CDP-ribitol is a substrate of FKTN during the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Shows activity toward other pentose phosphate sugars and mediates formation of CDP-ribulose or CDP-ribose using CTP and ribulose-5-phosphate or ribose-5-phosphate, respectively. Not Involved in dolichol production.
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A4D1B5
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GSAP_HUMAN
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Gamma-secretase-activating protein (GSAP) (Protein pigeon homolog) [Cleaved into: Gamma-secretase-activating protein 16 kDa C-terminal form (GSAP-16K)]
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MALRLVADFDLGKDVLPWLRAQRAVSEASGAGSGGADVLENDYESLHVLNVERNGNIIYTYKDDKGNVVFGLYDCQTRQNELLYTFEKDLQVFSCSVNSERTLLAASLVQSTKEGKRNELQPGSKCLTLLVEIHPVNNVKVLKAVDSYIWVQFLYPHIESHPLPENHLLLISEEKYIEQFRIHVAQEDGNRVVIKNSGHLPRDRIAEDFVWAQWDMSEQRLYYIDLKKSRSILKCIQFYADESYNLMFEVPLDISLSNSGFKLVNFGCDYHQYRDKFSKHLTLCVFTNHTGSLCVCYSPKCASWGQITYSVFYIHKGHSKTFTTSLENVGSHMTKGITFLNLDYYVAVYLPGHFFHLLNVQHPDLICHNLFLTGNNEMIDMLPHCPLQSLSGSLVLDCCSGKLYRALLSQSSLLQLLQNTCLDCEKMAALHCALYCGQGAQFLEAQIIQWISENVSACHSFDLIQEFIIASSYWSVYSETSNMDKLLPHSSVLTWNTEIPGITLVTEDIALPLMKVLSFKGYWEKLNSNLEYVKYAKPHFHYNNSVVRREWHNLISEEKTGKRRSAAYVRNILDNAVKVISNLEARNLGPRLTPLLQEEDSHQRLLMGLMVSELKDHFLRHLQGVEKKKIEQMVLDYISKLLDLICHIVETNWRKHNLHSWVLHFNSRGSAAEFAVFHIMTRILEATNSLFLPLPPGFHTLHTILGVQCLPLHNLLHCIDSGVLLLTETAVIRLMKDLDNTEKNEKLKFSIIVRLPPLIGQKICRLWDHPMSSNIISRNHVTRLLQNYKKQPRNSMINKSSFSVEFLPLNYFIEILTDIESSNQALYPFEGHDNVDAEFVEEAALKHTAMLLGL
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Regulator of gamma-secretase activity, which specifically activates the production of amyloid-beta protein (amyloid-beta protein 40 and amyloid-beta protein 42), without affecting the cleavage of other gamma-secretase targets such has Notch. The gamma-secretase complex is an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Specifically promotes the gamma-cleavage of APP CTF-alpha (also named APP-CTF) by the gamma-secretase complex to generate amyloid-beta, while it reduces the epsilon-cleavage of APP CTF-alpha, leading to a low production of AICD.
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A4D1E9
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GTPBA_HUMAN
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GTP-binding protein 10 (Protein obg homolog 2) (ObgH2)
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MVHCSCVLFRKYGNFIDKLRLFTRGGSGGMGYPRLGGEGGKGGDVWVVAQNRMTLKQLKDRYPRKRFVAGVGANSKISALKGSKGKDCEIPVPVGISVTDENGKIIGELNKENDRILVAQGGLGGKLLTNFLPLKGQKRIIHLDLKLIADVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFLKHIERTRQLLFVVDISGFQLSSHTQYRTAFETIILLTKELELYKEELQTKPALLAVNKMDLPDAQDKFHELMSQLQNPKDFLHLFEKNMIPERTVEFQHIIPISAVTGEGIEELKNCIRKSLDEQANQENDALHKKQLLNLWISDTMSSTEPPSKHAVTTSKMDII
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May be involved in the ribosome maturation process. Complements an ObgE(CgtA) function in E.coli ribosome maturation. Plays a role of GTPase in vitro. When missing, disorganization of the nucleolar architecture is observed.
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A4D1P6
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WDR91_HUMAN
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WD repeat-containing protein 91
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MAEAVERTDELVREYLLFRGFTHTLRQLDAEIKADKEKGFRVDKIVDQLQQLMQVYDLAALRDYWSYLERRLFSRLEDIYRPTIHKLKTSLFRFYLVYTIQTNRNDKAQEFFAKQATELQNQAEWKDWFVLPFLPSPDTNPTFATYFSRQWADTFIVSLHNFLSVLFQCMPVPVILNFDAECQRTNQVQEENEVLRQKLFALQAEIHRLKKEEQQPEEEEALVQHKLPPYVSNMDRLGDSELAMVCSQRNASLSQSPRVGFLSSLLPQSKKSPSRLSPAQGPPQPQSSAKKESFGGQGTKGKDPTSGAKDGKSLLSGLATGESGWSQHRQRRLQDHGKERKELFSTTTSQCAEKKPEASGPEAEPCPELHTEPVEPLTRASSAGPEGGGVRPEQPFIVLGQEEYGEHHSSIMHCRVDCSGRRVASLDVDGVIKVWSFNPIMQTKASSISKSPLLSLEWATKRDRLLLLGSGVGTVRLYDTEAKKNLCEININDNMPRILSLACSPNGASFVCSAAAPSLTSQVDFSAPDIGSKGMNQVPGRLLLWDTKTMKQQLQFSLDPEPIAINCTAFNHNGNLLVTGAADGVIRLFDMQQHECAMSWRAHYGEVYSVEFSYDENTVYSIGEDGKFIQWNIHKSGLKVSEYSLPSDATGPFVLSGYSGYKQVQVPRGRLFAFDSEGNYMLTCSATGGVIYKLGGDEKVLESCLSLGGHRAPVVTVDWSTAMDCGTCLTASMDGKIKLTTLLAHKA
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Functions as a negative regulator of the PI3 kinase/PI3K activity associated with endosomal membranes via BECN1, a core subunit of the PI3K complex. By modifying the phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal membranes may regulate endosome fusion, recycling, sorting and early to late endosome transport. It is for instance, required for the delivery of cargos like BST2/tetherin from early to late endosome and thereby participates indirectly to their degradation by the lysosome. May play a role in meiosis (By similarity).
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A4D1T9
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PRS37_HUMAN
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Probable inactive serine protease 37 (Probable inactive trypsin-X2)
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MKYVFYLGVLAGTFFFADSSVQKEDPAPYLVYLKSHFNPCVGVLIKPSWVLAPAHCYLPNLKVMLGNFKSRVRDGTEQTINPIQIVRYWNYSHSAPQDDLMLIKLAKPAMLNPKVQPLTLATTNVRPGTVCLLSGLDWSQENSGRHPDLRQNLEAPVMSDRECQKTEQGKSHRNSLCVKFVKVFSRIFGEVAVATVICKDKLQGIEVGHFMGGDVGIYTNVYKYVSWIENTAKDK
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Plays a role in male fertility (By similarity). May have a role in sperm migration or binding to zona-intact eggs (By similarity). Involved in the activation of the proacrosin/acrosin system.
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A4D256
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CC14C_HUMAN
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Dual specificity protein phosphatase CDC14C (EC 3.1.3.16) (EC 3.1.3.48) (CDC14 cell division cycle 14 homolog C)
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MRSSTLQDPRRRDPQDDVYVDITDRLRFAILYSRPKSASNVHYFSIDNELEYENFSEDFGPLNLAMVYRYCCKINKKLKSITMLRKKIVHFTGSDQRKQANAAFLVGCYMVIYLGRTPEAAYRILIFGDTPYIPFRDAAYGSCNFYITLLDCFHAVKKAMQYGFLNFNSFNLDEYEHYEKAENGDLNWIIPDRFIAFCGPHSRARLESGYHQHSPETYIQYFKNHNVTTIIRLNKRMYDAKRFTDAGFDHHDLFFADGSTPTDAIVKRFLDICENAEGAIAVHCKAGLGRTGTLIACYIMKHYRMTAAETIAWVRICRPGLVIGPQQQFLVMKQTSLWLEGDYFRQRLKGQENGQHRAAFSKLLSGVDDISINGVENQDQQEPKPYSDDDEINGVTQGDRSRALKRRRQSKTNDILLPSPLAVLTFTLCSVVIWWIVCDYILPILLF
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Dual-specificity phosphatase. Preferentially dephosphorylates proteins modified by proline-directed kinases (By similarity).
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A4D2B0
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MBLC1_HUMAN
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Metallo-beta-lactamase domain-containing protein 1 (EC 3.1.27.-) (Endoribonuclease MBLAC1)
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MRTEPLCGASPLLVPGDPYSVVVLLQGYAEPEGVGDAVRADGSVTLVLPQTRGPASSHRESPRGSGGAEAALEEAARGPILVDTGGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLFPGAALLVSHDFCLPGGRYLPHGLGEGQPLRLGPGLEVWATPGHGGQRDVSVVVAGTALGTVVVAGDVFERDGDEDSWQALSEDPAAQERSRKRVLVVADVVVPGHGPPFRVLREASQPETEGGGNSQQEPVVGDEEPALH
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Endoribonuclease that catalyzes the hydrolysis of histone-coding pre-mRNA 3'-end. Involved in histone pre-mRNA processing during the S-phase of the cell cycle, which is required for entering/progressing through S-phase. Cleaves histone pre-mRNA at a major and a minor cleavage site after the 5'-ACCCA-3' and the 5'-ACCCACA-3' sequence, respectively, and located downstream of the stem-loop. May require the presence of the HDE element located at the histone pre-RNA 3'-end to avoid non-specific cleavage.
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A4D7S0
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WNT2_BOVIN
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Protein Wnt-2
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MNACLVGIWLWLPLLFTWLSPEVSSSWWYMRATSGSSRVMCDNVPGLVSHQRQLCHRHPDVMRAIGLGVTEWTMECQHQFRQHRWNCNTLDRDHSLFGRVLLRSSRESAFVYAISSAGVVFAITRACSQGELKSCSCDPKKKGTAKDNKGTFDWGGCSDNIDYGIKFARAFVDAKERKGKDARALMNLHNNRAGRKAVKRFLKQECKCHGVSGSCTLRTCWLAMADFRKTGNYLWRKYNGAIQVVMNQDGTGFTVANKRFKKPTKNDLVYFENSPDYCIRDRDAGSLGTAGRVCNLTSRGMDSCEVMCCGRGYDTSHITRKTKCECKFHWCCAVRCQDCVEALDVHTCKAPKSPDWAAPT
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Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (By similarity). Functions as upstream regulator of FGF10 expression. Plays an important role in embryonic lung development. May contribute to embryonic brain development by regulating the proliferation of dopaminergic precursors and neurons (By similarity).
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A4ECA9
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HSDHB_COLAA
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7beta-hydroxysteroid dehydrogenase (7beta-HSDH) (EC 1.1.1.201) (NADP-dependent 7beta-hydroxysteroid dehydrogenase)
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MNLREKYGEWGLILGATEGVGKAFCEKIAAGGMNVVMVGRREEKLNVLAGEIRETYGVETKVVRADFSQPGAAETVFAATEGLDMGFMSYVACLHSFGKIQDTPWEKHEAMINVNVVTFLKCFHHYMRIFAAQDRGAVINVSSMTGISSSPWNGQYGAGKAFILKMTEAVACECEGTGVDVEVITLGTTLTPSLLSNLPGGPQGEAVMKIALTPEECVDEAFEKLGKELSVIAGQRNKDSVHDWKANHTEDEYIRYMGSFYRD
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7beta-hydroxysteroid dehydrogenase that catalyzes the reduction of the 7-oxo group of 7-oxo-lithocholate (7-oxo-LCA), to yield ursodeoxycholate (UDCA). As C.aerofaciens is an intestinal bacterium, this enzyme probably contributes to the formation of UDCA in the human colon. UDCA is regarded as a chemopreventive beneficial secondary bile acid due to its low hydrophobicity it protects hepatocytes and bile duct epithelial cells against necrosis and apoptosis induced by more hydrophobic secondary bile acids like deoxycholate (DCA) (Probable). This enzyme is also able to catalyze the reverse reaction, i.e. the oxidation of the 7beta-hydroxy group of UDCA to 7-oxo-LCA. To a lesser extent, is also active on the taurine- and glycine-conjugates of ursodeoxycholate. It is specific for NADPH/NADP(+) as the electron acceptor/donor since it is not active with NADH/NAD(+). In the presence of NADPH, 7beta-HSDH can also reduce dehydrocholate. And is also able to oxidize ursocholate.
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A4F2N8
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LTHAD_PSESP
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L-threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) (L-threo-3-hydroxyaspartate dehydratase) (L-THA DH)
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MQLSSYHDVIKAAERLEGFANRTPVFTSRTLDAETGAQVFIKCENLQRTGSFKFRGAFNALSRFDEAQRKAGVVAFSSGNHAQGIALAARLLQMPATIVMPTDAPAAKVAATREYGATVVFYDRITEDREQIGRTLAEQHGMTLIPSYDHPDVLAGQGTAAKELLEFTGPLDALFVGLGGGGMLSGTALATRALSPDCLLYGVEPEAGNDGQRSFQTGSIVHIDTPATIADGAQTQHLGNHTFPIIRENVNDILTVSDAELVESMRFFMQRMKMVVEPTGCLGLAALRNLKQQFRGQRVGIIVTGGNVDIEKYASLLKG
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Catalyzes the deamination of L-threo-3-hydroxyaspartate to oxaloacetate and ammonia. Shows a high specificity towards L-threo-3-hydroxyaspartate as other 3-hydroxyaminoacids, i.e. D,L-erythro- and D-threo-3-hydroxyaspartate, D-threonine, L-threonine, D,L-allothreonine, D,L-threo-3-phenylserine, D-serine, and L-serine, are not substrates for this enzyme. Exhibits no detectable serine and aspartate racemase activity. Might play a role in the detoxification of naturally occurring 3-hydroxyaspartate in Pseudomonas sp. T62 cells.
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A4F4L0
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TYOBP_PANTR
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TYRO protein tyrosine kinase-binding protein (DNAX-activation protein 12)
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MGGLEPCSRLLLLPLLLAVGGLRPVQAQAQSDCSCSTVSPGVLAGIVMGDLVLTVLIALAVYFLGRLVHRGRGAAEAATRKQRITETESPYQELQGQRSDVYSDLNMQRPYYK
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Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors (By similarity). TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the associated receptors which leads to activation of additional tyrosine kinases and subsequent cell activation (By similarity). Also has an inhibitory role in some cells (By similarity). Non-covalently associates with activating receptors of the CD300 family to mediate cell activation (By similarity). Also mediates cell activation through association with activating receptors of the CD200R family (By similarity). Required for neutrophil activation mediated by integrin (By similarity). Required for the activation of myeloid cells mediated by the CLEC5A/MDL1 receptor (By similarity). Associates with natural killer (NK) cell receptors such as the KLRD1/KLRC2 heterodimer to mediate NK cell activation (By similarity). Associates with TREM1 to mediate activation of neutrophils and monocytes (By similarity). Associates with TREM2 on monocyte-derived dendritic cells to mediate up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (By similarity). Association with TREM2 mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages (By similarity). Stabilizes the TREM2 C-terminal fragment (TREM2-CTF) produced by TREM2 ectodomain shedding which suppresses the release of pro-inflammatory cytokines (By similarity). In microglia, required with TREM2 for phagocytosis of apoptotic neurons (By similarity). Required with ITGAM/CD11B in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (By similarity). Promotes pro-inflammatory responses in microglia following nerve injury which accelerates degeneration of injured neurons (By similarity). Positively regulates the expression of the IRAK3/IRAK-M kinase and IL10 production by liver dendritic cells and inhibits their T cell allosimulatory ability (By similarity). Negatively regulates B cell proliferation (By similarity). Required for CSF1-mediated osteoclast cytoskeletal organization (By similarity). Positively regulates multinucleation during osteoclast development (By similarity).
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A4FUF0
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GLYR1_BOVIN
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Cytokine-like nuclear factor N-PAC (NPAC) (Glyoxylate reductase 1 homolog) (Nuclear protein NP60) (Putative oxidoreductase GLYR1)
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MAAVSLRLGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKKCFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINKGKRFQQAVDAVEEFLRRAKGKDQTSSHSSADDKNRRNSSEERSRPISGDEKRKLSLSEGKVKKNMGEGKKRVPSGSSERGSKSPLKRAQEQSPRKRGRPPKDEKDLSIPESSTVKGMMAGPMATFKWQPNVSEPVKDADPHFHHFLLSQTEKPAVCYQAITKKLKICEEETGSTSIQAADSTAVNGSVTPTDKKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEKCDLFIQEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVLQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLGEVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAYIH
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Cytokine-like nuclear factor with chromatin gene reader activity involved in chromatin modification and regulation of gene expression. Acts as a nucleosome-destabilizing factor that is recruited to genes during transcriptional activation. Recognizes and binds histone H3 without a preference for specific epigenetic markers and also binds DNA. Interacts with KDM1B and promotes its histone demethylase activity by facilitating the capture of H3 tails, they form a multifunctional enzyme complex that modifies transcribed chromatin and facilitates Pol II transcription through nucleosomes. Stimulates the acetylation of 'Lys-56' of nucleosomal histone H3 (H3K56ac) by EP300. With GATA4, co-binds a defined set of heart development genes and coregulates their expression during cardiomyocyte differentiation. Regulates p38 MAP kinase activity by mediating stress activation of MAPK14/p38alpha and specifically regulating MAPK14 signaling. Indirectly promotes phosphorylation of MAPK14 and activation of ATF2. The phosphorylation of MAPK14 requires upstream activity of MAP2K4 and MAP2K6.
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A4FUQ5
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FPRS4_MOUSE
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Formyl peptide receptor-related sequence 4 (N-formylpeptide receptor-like 4)
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MEVNISMPLNGSEVVFYDSTTSRVLWILSLVVLFITFVLGVLGNGLVIWVAGFQMAHTVTTVSYLNLALSDLSFMATLPLHIISMVMRGKWLFGWFLCKLVHIIANINLFVSIFLITLIAMDRCICVLCPVWSQNHRTVSLARKVVLGAWIFALLLTLPHFLFLTTVRDARGDVYCISKFESWVATSEEQLKVSVIAATASGIINFIIGFSMPMSFIAICYGLMAAKICRRGFVNSSRPLRVLTAVAVSFFVCWFPFQLIMLLGNIFNNETLSIIHMLVNPANTLASFNSCLNPILYVFLGQEFRDRLIYSLYASLERALRED
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May have an olfactory function associated with the identification of pathogens or of pathogenic states.
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A4FV08
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GNPI1_BOVIN
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Glucosamine-6-phosphate isomerase 1 (EC 3.5.99.6) (Glucosamine-6-phosphate deaminase 1) (GNPDA 1) (GlcN6P deaminase 1) (Oscillin)
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MKLIILDHYSQASEWAAKYIRNRIIQFNPGPDKYFTLGLPTGSTPLGCYKKLIEYYKNGDLSFKYVKTFNMDEYVGLPRDHPESYHSFMWNNFFKHIDIHPENTHILDGNAADLQAECDAFEEKIKAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVKTLAMDTILANARFFDGDLAKVPTMALTVGVGTVMDAREVMILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCDEDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKEKEIEKSQSSKKPYSD
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Catalyzes the reversible conversion of alpha-D-glucosamine 6-phosphate (GlcN-6P) into beta-D-fructose 6-phosphate (Fru-6P) and ammonium ion, a regulatory reaction step in de novo uridine diphosphate-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc) biosynthesis via hexosamine pathway. Deamination is coupled to aldo-keto isomerization mediating the metabolic flux from UDP-GlcNAc toward Fru-6P. At high ammonium level can drive amination and isomerization of Fru-6P toward hexosamines and UDP-GlcNAc synthesis. Has a role in fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc and their effects on hyaluronan synthesis that occur during tissue remodeling (By similarity). Seems to trigger calcium oscillations in mammalian eggs. These oscillations serve as the essential trigger for egg activation and early development of the embryo (By similarity).
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A4FV52
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VGLU1_BOVIN
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Vesicular glutamate transporter 1 (VGluT1) (Solute carrier family 17 member 7)
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MEFRQEEFRKLAGRALGKLHRLLEKRQEGAETLELSADGRPVTTQTRDPPVVDCTCFGLPRRYIIAIMSGLGFCISFGIRCNLGVAIVSMVNNSTTHRGGHVVMQKAQFNWDPETVGLIHGSFFWGYIVTQIPGGFICQKFAANRVFGFAIVATSTLNMLIPSAARVHYGCVIFVRILQGLVEGVTYPACHGIWSKWAPPLERSRLATTAFCGSYAGAVVAMPLAGVLVQYSGWSSVFYVYGSFGIFWYLFWLLVSYESPALHPSISEEERKYIEDAIGESAKLMNPVTKFNTPWRRFFTSMPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFEISKVGLVSALPHLVMTIIVPIGGQIADFLRSRRIMSTTNVRKLMNCGGFGMEATLLLVVGYSHSKGVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPIIVGAMTKHKTREEWQYVFLIASLVHYGGVIFYGVFASGEKQPWAEPEEMSEEKCGFVGHDQLAGSDESEMEDEAEPPGAPPAPPPSYGATHSTVQPPRPPPPVRDY
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Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, proton, potassium, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as an uniporter which transports preferentially L-glutamate but also phosphate from the cytoplasm into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. The L-glutamate or phosphate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane. In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane that affects the proton electrochemical gradient and promotes synaptic vesicles acidification. Moreover, may function as a K(+)/H(+) antiport allowing to maintain the electrical gradient and to decrease chemical gradient and therefore sustain vesicular glutamate uptake. The vesicular K(+)/H(+) antiport activity is electroneutral. At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation. The symporter activity is driven by an inside negative membrane potential and is electrogenic (By similarity). Is necessary for synaptic signaling of visual-evoked responses from photoreceptors (By similarity).
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A4FV54
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RAB8A_BOVIN
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Ras-related protein Rab-8A (EC 3.6.5.2)
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MAKTYDYLFKLLLIGDSGVGKTCVLFRFSEDAFNSTFISTIGIDFKIRTIELDGKRIKLQIWDTAGQERFRTITTAYYRGAMGIMLVYDITNEKSFDNIRNWIRNIEEHASADVEKMILGNKCDVNDKRQVSKERGEKLALDYGIKFMETSAKANINVENAFYTLARDIKAKMDKKLEGNSPQGSNQGVKITPDQQKRSSFFRCVLL
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The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in polarized vesicular trafficking and neurotransmitter release. Together with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Regulates the compacted morphology of the Golgi (By similarity). Together with MYO5B and RAB11A participates in epithelial cell polarization. Also involved in membrane trafficking to the cilium and ciliogenesis (By similarity). Together with MICALL2, may also regulate adherens junction assembly (By similarity). May play a role in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore play a role in glucose homeostasis (By similarity). Involved in autophagy (By similarity).
|
A4FVP2
|
TPS03_ARATH
|
Terpenoid synthase 3, chloroplastic (AtTPS03) ((E)-beta-ocimene synthase) (EC 4.2.3.106) ((E,E)-alpha-farnesene synthase) (EC 4.2.3.46)
|
MPKRQAQRRFTRKTDSKTPSQPLVSRRSANYQPSLWQHEYLLSLGNTYVKEDNVERVTLLKQEVSKMLNETEGLLEQLELIDTLQRLGVSYHFEQEIKKTLTNVHVKNVRAHKNRIDRNRWGDLYATALEFRLLRQHGFSIAQDVFDGNIGVDLDDKDIKGILSLYEASYLSTRIDTKLKESIYYTTKRLRKFVEVNKNETKSYTLRRMVIHALEMPYHRRVGRLEARWYIEVYGERHDMNPILLELAKLDFNFVQAIHQDELKSLSSWWSKTGLTKHLDFVRDRITEGYFSSVGVMYEPEFAYHRQMLTKVFMLITTIDDIYDIYGTLEELQLFTTIVEKWDVNRLEELPNYMKLCFLCLVNEINQIGYFVLRDKGFNVIPYLKESWADMCTTFLKEAKWYKSGYKPNFEEYMQNGWISSSVPTILLHLFCLLSDQTLDILGSYNHSVVRSSATILRLANDLATSSEELARGDTMKSVQCHMHETGASEAESRAYIQGIIGVAWDDLNMEKKSCRLHQGFLEAAANLGRVAQCVYQYGDGHGCPDKAKTVNHVRSLLVHPLPLN
|
Predominantly involved in sesquiterpenes (C15) biosynthesis. Using FPP as substrate, the major product is (E,E)-alpha-farnesene with minor amounts of (Z,E)-alpha-farnesene and (E,E)-beta-farnesene. Using GPP as substrate, could also be able in vitro to synthesize monoterpene (C10) with (E)-beta-ocimene as the major product and with (Z)-beta-ocimene and myrcene as minor products.
|
A4FVP6
|
NAC16_ARATH
|
NAC domain-containing protein 16 (ANAC016) (Protein NTM1-like 3)
|
MVDSSRDSCFKAGKFSAPGFRFHPTDEELVVYYLKRKICCKKLRVNAIGVVDVYKVDPSELPGLSMLKTGDRQWFFFTPRNRKYPNAARSSRGTATGYWKATGKDRVIEYNSRSVGLKKTLVFYRGRAPNGERTDWVMHEYTMDEEELGRCKNAKEYYALYKLYKKSGAGPKNGEQYGAPFQEEEWVDSDSEDADSVAVPDYPVVRYENGPCVDDTKFCNPVKLQLEDIEKLLNEIPDAPGVNQRQFDEFVGVPQGNSAEVIQSTLLNNSSGEYIDPRTNGMFLPNGQLYNRDSSFQSHLNSFEATSGMAPLLDNEKEEYIEMNDLLIPELGASSTEKSTEFLNHGEFGDVNEYDQLFNDISVFQGTSTDLSCLSNFTNNTSGQRQQLLYEQFQYQTPENQLNNYMHPSTTLNQFTDNMWFKDDQAALYVQPPQSSSGAFTSQSTGVMPESMNPTMSVNPQYKEGQNGGGTRSQFSSALWELLESIPSTPASACEGPLNQTFVRMSSFSRIRFNGTSVTSRKVTVAKKRISNRGFLLLSIMGALCAIFWVFKATVGVMGRPLLS
|
Transcriptional activator activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP) (By similarity). Transcriptional activator that promotes leaf senescence by up-regulating senescence-associated genes in response to developmental and stress-induced senescence signals. Functions in salt and oxidative stress-responsive signaling pathways. Binds to the promoter of NAC029/NAP and NAC059/ORS1 genes.
|
A4GBX8
|
M2_I77AA
|
Matrix protein 2 (Proton channel protein M2)
|
MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYRKEQQNAVDADDSHFVNIELE
|
Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
|
A4GCH6
|
M2_I83A1
|
Matrix protein 2 (Proton channel protein M2)
|
MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYREEQQNAVDADDGHFVSIELE
|
Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
|
A4GCI7
|
M2_I36A0
|
Matrix protein 2 (Proton channel protein M2)
|
MSLLTEVETPIRNEWGCRCNGSSDPLVIAANIIGILHLILWILDRLFFKCIYRLFEYGLKRGPSTEGVPESMREEYRKEQQSAVDADDGHFVSIELE
|
Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
|
A4GCJ8
|
M2_I80AA
|
Matrix protein 2 (Proton channel protein M2)
|
MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYREEQQNAVDADDGHFVSIELE
|
Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
|
A4GCK9
|
M2_I43A0
|
Matrix protein 2 (Proton channel protein M2)
|
MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVNIELE
|
Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
|
A4GCM0
|
M2_I35A3
|
Matrix protein 2 (Proton channel protein M2)
|
MSLLTEVETPIRNEWGCRCNGSSDPLVIAASIIGILHLILWILDRLLFKCIYRRFKYGLKRGPSTEGVPESMREEYRKEQQSAVDADDGHFVNIEPE
|
Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
|
A4GG66
|
CXG1_RAT
|
Gap junction gamma-1 protein (Connexin-45) (Cx45) (Gap junction alpha-7 protein)
|
MSWSFLTRLLEEIHNHSTFVGKIWLTVLIVFRIVLTAVGGESIYYDEQSKFVCNTEQPGCENVCYDAFAPLSHVRFWVFQIILVATPSVMYLGYAIHKIAKMEHGEADKKAARSKPYAMRWKQHRALEETEEDHEEDPMMYPEMELESEKENKEQSQPKPKHDGRRRIREDGLMKIYVLQLLARTVFEVGFLIGQYFLYGFQVHPFYVCSRLPCPHKIDCFISRPTEKTIFLLIMYGVTGLCLLLNIWEMLHLGFGTIRDSLNSKRRELDDPGAYNYPFTWNTPSAPPGYNIAVKPDQIQYTELSNAKIAYKQNKANIAQEQQYGSHEEHLPADLETLQREIRMAQERLDLAIQAYHHQNNPHGPREKKAKVGSKSGSNKSSISSKSGDGKTSVWI
|
One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
|
A4GNA8
|
PSD3_ARATH
|
Phosphatidylserine decarboxylase proenzyme 3 (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase 3 beta chain; Phosphatidylserine decarboxylase 3 alpha chain]
|
MGNGNSTETKESRRSKMRKKIQNFRSRRRLSRPGSGSVSGLASQRSVSADDFAGIALLTLIGAEMKFKDKWLACVSFGEQTFRSEISDSTEKPIWNSEKKLLLEKNGPSLARISVFETNRLLKNNIVGYCELDLLDFVVQEPDSTCKSFDLLDPASSNVVGSMFVSCSVEDPVETETCFAKRILSIVDYDEDGKLSFSEFSDLMNAFGNVVAANKKEELFKAADLNGDGVVTIDELAALLAVQQEQEPIINSCPVCGEALQLDKLNAMIHMTLCFDEGTGNQMTGGFLTDRQASYGWMFKLSEWTHLSTYDVGLNTGSSASHIVVIDRKTKRLVEELIDSKIVMSMRAIYQSKIGLRLMDQGAKEILQNLSEKQGKKMNSVESAQNIPSFLEFFKDQINMAEVKYPLDHFKTFNEFFVRELKPGARPIACMDQDDVAVSAADCRLMAFQSVDDSTRFWIKGRKFSIKGLLGNDVQSDAFLDGSLVIFRLAPQDYHRFHSPVSGVIEKFVNVSGSLYTVNPIAVNSKYCNVFTENKRTIVIISTAEFGKVAFVAIGATMVGSISFVRQEGDHVKKGDELGYFSFGGSTVICVFEKDSIKIDEDLLANSARSLETLVTVGMQLGVSFPKLENCVLEP
|
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. Contributes only to a minor proportion of PtdEtn production. {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000269|PubMed:17449644}.
|
A4GRC6
|
HAP2_CHLRE
|
Hapless 2 (HAP2) (Generative cell specific-1)
|
MCRAIAVALIVYLAQHYILAHAEVIASGRLEKCVVDGVTEELDCQEKVVVTLTVGNGQSLQTEALEFSLSCLNSPDGRCPCSCSAADPTCACRDLAAPLRVSLTKSPLWASYPLQYLSSFNWKPLEVILRPSNKVCKDGDWEDSPTCGWFSQGGVRVADSQGFCCECSSSQVWDDTFGSSKERTRANLDCDFWSDPLDILIGRKPVSAHCLTFDPQWYSGYELGAASLQFEIAITVEVPTAPSPTTATTSATPRTNNSSSANSTNSTNSPAPQFLSPPAPSTREVLHLGPSVPLASSASRLLSAKLLGDLAMYTQLPAISNQVLMVPQPPAAAAATGSPLDATLATNRSAWMLLDKTMLSMDGLACDKVGTGFSAFRYQPSGCGRAPQACLSGQLKDLWEADLARIADGRVPLYMITRFTGGSDTTLQSFSGGPLSFALPVTSHSQSLVTLSVAADGVRLVTNRSPGKITGAAVCRFAGTSCGGFEAVAARGYIYVNITNTGRLDSDYTLTVSNCSSNVRPIEARTLAVRAGSAASLDPPMELYVEDQAAAAARTCTVSLYDSVGAVTDSLTLSFYTNATQLVVKPSGGYNGTGDGAGVKRNGTDCSTACTNPIDVLCFVTKKCWSKFGRLLGIIGGALVGLGLLAVALKFGWLASLAASCCGGGGGAAAGGAGGGMGLGTGGGGGCFGGGQQQQQLPPAASHAMSPPQQQQRSHAEVAAGAAVAGAGAAGAAAAVLGAKHGGGGGGARGKQQHADTRHLQDRDSRAIDGGASIGSSSAGGSSSLSSYSQPREAGGRLLQPPAAAVFVPEGGGGGAAGDEGARAQSSDWDARGRSPRVADEHGSPRQRYDGVRQSPYMVSANPYDGWYDGGSGGGGGGGGGGYGREAPPPQGPPPHPVGAPPPPPRRRSLWERMWLQRPGGGGGGGGGGGGGGGGGSGGGVDQHGGRSCADAARRGGGGPGGMRGVEGLMSNGGRPNGPHPHAPPPPPPPQQQQQQQRQRRSFLESLTAMMTLPWGGGREEEAGGDRRGGGRGGAAAAHGGRGAGGGRGHPPSIGSPPPGPLQPPEYGPQGGQARRWGAGGGRGGVGGDGGGGGVGAAAYVQLSTGGRGGGGGGGRGRGGGREGPTWHNPVYDWQAPPK
|
During fertilization, required on male (minus) gametes for their fusion with female (plus) gametes. Required for membrane fusion, but not for the initial adhesion between gametes. Inserts (via its extracellular domain) into lipid membranes (in vitro). Probably initiates the fusion of gamete cell membranes by inserting its extracellular domain into the cell membrane of a female gamete.
|
A4GSN8
|
NUA_ARATH
|
Nuclear-pore anchor (Protein TRANSLOCATED PROMOTER REGION) (AtTPR)
|
MPLFMPDEELARLSSDAASVVAERADEYIRKIYAELDSVRAKADAASITAEQTCSLLEQKYLSLSQDFSSLESQNAKLQSDFDDRLAELAQSQAQKHQLHLQSIEKDGEVERMSTEMSELHKSKRQLMELLEQKDAEISEKNSTIKSYLDKIVKLTDTSSEKEARLAEATAELARSQAMCSRLSQEKELTERHAKWLDEELTAKVDSYAELRRRHSDLESEMSAKLVDVEKNYIECSSSLNWHKERLRELETKIGSLQEDLSSCKDAATTTEEQYTAELFTANKLVDLYKESSEEWSRKAGELEGVIKALEARLSQVESSYKERLDKEVSTKQLLEKENGDLKQKLEKCEAEIEKTRKTDELNLIPFSNFTRRVDNSGTSNMIEESQAVISKVPAGVSGTALAASLLRDGWSLAKIYEKYQEAVDAMRHEQLGRKEAEMILQRVLSELEEKAGFIQEERGEYERVVEAYCLVNQKLQDSVSEQSNMEKFIMELKADLRRRERENTLLQKDISDLQKQVTILLKECRDVQLRCGAARDDDEDDYPLLSDVEMEMESEADKIISEHLLKFKDINGLVEQNVKLRNLVRSLSEQIESRETELKETFEVDLKNKTDEASAKVATVLKRAEEQGQMIESLHTSVAMYKRLYEEEQKLHSSDSRSSDLSPAVVPGRKNFLHLLEDSEEATKRAQEKAFERIRILEEDFAKARSEVIAIRSERDKLAMEANFAREKLEGIMKESERKREEMNSVLARNIEFSQLIIDHQRKLRESSESLHAAEEISRKLSMEVSVLKQEKELLSNAEKRASDEVSALSQRVYRLQATLDTVQSTEEVREETRAAERRKQEEHIKQLQREWAEAKKELQEERSNARDFTSDRNQTLNNAVMQVEEMGKELANALKAVSVAESRASVAEARLSDLEKKIRSSDPKTLDMDSGGIVSLSDKEMSIELRTAKEEIEKLRGEVESSKSHMLQYKSIAQVNETALKQMESAHENFRLEAEKRQRSLEAELVSLRERVSELENDCIQKSEQLATAAAGKEDALLSASAEIASLREENLVKKSQIEAMNIQMSTLKNDLETEHEKWRVAQRNYERQVILLSETIQELTKTSQALAALQEEASELRKLADARGIENSELNAKWSEEKLMLEQQKNLAEKKYHELNEQNKLLHSRLEAKHLNSAEKNSRSGTISSGSTDSDHLEDSGLQRVVHYLRRTKEIAETEISLMRQEKLRLQSQLESALKMAESARGSLTAERASTRASLLTDDGIKSLQLQVSEMNLLRESNMQLREENKHNFEKCQEMREVAQKARMESENFENLLKTKQTELDLCMKEMEKLRMETDLHKKRVDELRETYRNIDIADYNRLKDEVRQLEEKLKAKDAHAEDCKKVLLEKQNKISLLEKELTNCKKDLSEREKRLDDAQQAQATMQSEFNKQKQELEKNKKIHYTLNMTKRKYEKEKDELSKQNQSLAKQLEEAKEEAGKRTTTDAVVEQSVKEREEKEKRIQILDKYVHQLKDEVRKKTEDLKKKDEELTKERSERKSVEKEVGDSLTKIKKEKTKVDEELAKLERYQTALTHLSEELEKLKHADGNLPEGTSAVQVLSGSILNDQAAAYVSAVEYFERVARSIASNSQVSTKPTDMVTEPSSGIPAAEPSTMTRVPSSTPLIKSPVATTQQLPKVASDNKEKRLISQKPSTEFRRPSGRRIVRPQLVKPEESPKVDVDMPEAEGTGDEGKQPAAHEPESQVTTSVRPVQTLVRKRQADSLVSEPQQDSLTQGETSSEIAPPASKKAKGSESHPDTSEGENLAKEPAIDELMDATTTTDGDNEETEAENAEEKTEEYVEAQQDNEADEPVEESPTETETIPTEEESRDQTEEENQEPLTDMESDKEEGELDLDTLEDLEEGTDVASMMRSPEKEEVQPETLATPTQSPSRMETAMEEAETTIETPVEDDKTDEGGDAAEEAADIPNNANDQQEAPETDIKPETSAATTSPVSTAPTTSSTLASAITSSGAPETEDPKRAPSPGGGSSTIVTLADRAQMKRRERIANIVVSRAPNPATRGARGRTVNLRGGGRLLPRGGRAPRGGRGQSPSPP
|
Component of the nuclear pore complex. Acts as a docking site for activities required for desumoylation and mRNA export. Required for the proper expression or localization of a subset of miRNAs. Plays a role in meristematic cell division by interacting with spindle assembly checkpoint proteins.
|
A4GTP4
|
ELK1_RAT
|
ETS domain-containing protein Elk-1
|
MDPSVTLWQFLLQLLREQGNGHIISWTSRDGGEFKLVDAEEVARLWGLRKNKTNMNYDKLSRALRYYYDKNIIRKVSGQKFVYKFVSYPEVAGCSTEDCPPQPEVSVTSAVAMAPATVHSGPGDNATGKPGTPKGAGMTGQGGLARSSRNEYMRSGLYSTFTIQSLQPQPPLHPRPASVLPNTTPAGVPAPPSGSRSTSPNPLEACLEAEEAGLPLQVILTPPEAPNQKSEELSLNPGFGRPQPPEVKVEGPKEELEVTEVGGFSPEAVKAEQEVSPSEGLLARLPAILTENTAQVCGLSTSTTEITQPQKGRKPRDLELPLSPSLLGGQGPERTPGSGTSSGLQAQGPALTPSLLPTHTLTPVLLTPSSLPPSIHFWSTLSPIAPRSPAKLSFQFPSSGSAQVHIPSISVDGLSTPVVLSPGPQKP
|
Transcription factor that binds to purine-rich DNA sequences. Forms a ternary complex with SRF and the ETS and SRF motifs of the serum response element (SRE) on the promoter region of immediate early genes such as FOS and IER2 (By similarity). Induces target gene transcription upon JNK-signaling pathway stimulation.
|
A4GXA9
|
EME2_HUMAN
|
Probable crossover junction endonuclease EME2 (EC 3.1.22.-)
|
MARVGPGRAGVSCQGRGRGRGGSGQRRPPTWEISDSDAEDSAGSEAAARARDPAGERRAAAEALRLLRPEQVLKRLAVCVDTAILEDAGADVLMEALEALGCECRIEPQRPARSLRWTRASPDPCPRSLPPEVWAAGEQELLLLLEPEEFLQGVATLTQISGPTHWVPWISPETTARPHLAVIGLDAYLWSRQHVSRGTQQPESPKVAGAEVAVSWPEVEEALVLLQLWANLDVLLVASWQELSRHVCAVTKALAQYPLKQYRESQAFSFCTAGRWAAGEPVARDGAGLQAAWRRQIRQFSRVSPAVADAVVTAFPSPRLLQQALEACSTERERMGLLADLPVPPSEGGRPRRVGPDLSRRICLFLTTANPDLLLDLGS
|
Interacts with MUS81 to form a DNA structure-specific endonuclease which cleaves substrates such as 3'-flap structures.
|
A4IFH6
|
PPLA_BOVIN
|
Cardiac phospholamban (PLB)
|
MDKVQYLTRSAIRRASTIEMPQQARQNLQNLFINFCLISICLLLICIIVMLL
|
Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN. ATP2A2 inhibition is alleviated by PLN phosphorylation. Controls intracellular Ca(2+) levels in elongated spermatids. May play a role in germ cell differentiation.
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A4IFJ5
|
PA24A_BOVIN
|
Cytosolic phospholipase A2 (cPLA2) (Phospholipase A2 group IVA) [Includes: Phospholipase A2 (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase); Lysophospholipase (EC 3.1.1.5)]
|
MSFIDPYQHIIVEHHYSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISSTPDSRKRTRHFNNDINPVWNETFEFILDPNQENILEITLMDANYVMDETLGTTTFPISSMKVGEKKQVPFIFNQVTEMILEMSLEVCSSPDLRFSMALCDQEKAFRQQRKENIKENMKKLLGPKNSEGLHSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYIAGLSGSTWYMSTLYSHPDFPEKGPEEINKELMKNVSHNPLLLLTPQKIKRYVESLWRKKSSGQPVTFTDIFGMLIGETLIHNRMNTTLSSLKEKVNTGQCPLPLFTCLHVKPDVSELMFADWVEFSPFEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSKGSTMEEELENITAKHIVSNDSSDSDDESQGPKGTEHEEAEREYQNDNQASWVQRMLMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPMSPLRDFTMQESLDEDELDAAVADPDEFEQIYEPLDVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPTIIHFVLANINFRKYKAPGVPRETNEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNNIDVIKNAIVESIEYRRQNPSRCSVSLSSVEARRFFNKEFLSKPTA
|
Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (By similarity). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific. Has calcium-independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides. Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (By similarity).
|
A4IFM7
|
MYLK2_BOVIN
|
Myosin light chain kinase 2, skeletal/cardiac muscle (MLCK2) (EC 2.7.11.18)
|
MATENGAVELEIPSSSTDTAPKAAAGEGPPAAEKDPGPPDPQKDPGPPDPEKDAGPPNPEKELESPDPKKEPDPDSTKDTEAPAPEKGDGASAQPSASSQGPEGEGGLQGEPAEGSAGQPAALPQETATAEASVKKPEAEQGTPGSQDPGEAKEQKKVAEGQAPSKKGSPAFLHSPSCPAAISSLEKPLAEKPLDETLELIFEGVPVTPGPTETEPAKVAEGEKNLPGGSQKEGEEKAAGHAGQDGVQGDTSRGIEFQAVPSERSEVGQALSPTAKEEDCFQILDDCPPPPAPFPHRIVELRPGNINSQFSLNSKEALGGGKFGAVCTCTEKATGLKLAAKVIKKQTPKDKEMVLLEIEVMNQLNHRNLIQLYAAIETPHEIVLFMEYIEGGELFERIVDEDYQLTEVDTMVFVRQICDGILFMHKMRVLHLDLKPENILCVNTTGHLVKIIDFGLARRYNPNEKLKVNFGTPEFLSPEVVNYDQISDKTDMWSLGVITYMLLSGLSPFLGDDDTETLNNVLSSNWYFDEETFEAVSDEAKDFVSNLIVKDQRARMSAAQCLAHPWLNNLAEKAKRCNRRLKSQILLKKYLMKRRWKKNFIAVSAANRFKKISSSGALMALGV
|
Implicated in the level of global muscle contraction and cardiac function. Phosphorylates a specific serine in the N-terminus of a myosin light chain (By similarity).
|
A4IG62
|
SUV3_DANRE
|
ATP-dependent RNA helicase SUPV3L1, mitochondrial (EC 3.6.4.13) (Suppressor of var1 3-like protein 1) (SUV3-like protein 1)
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MSVNRCIYLLSRSHIRYRVCASTNLSTVSTLSTTQHSTRRTFDKLSTRHSSSGSSRPLDTSLFIPLPVKTDEDAEGSVGAELTKPLDKNELLKVLNRFYKRKEMQKLASDQGLDARLFHQAFVSFRKYVLEMNSLNADLHIILNDICCGAGHIDDIFPYFMRHAKQIFPMLDCIDDLRKISDLRVPANWYPEARAIQRKIVFHAGPTNSGKTYHAIKRYLEAKSGVYCGPLKLLAHEIYEKSNAAGVPCDLVTGEERIFVDPEGKPSGHIASTIEMCSVTTPYEVAVIDEIQMIKDPARGWAWTRALLGLCAEEIHVCGEAAAVDFITELMFTTGEEVEVHNYKRLTPFSISNHAVESLDNLKPGDCIVCFSKNDIYSISRQIEIRGLECAVIYGSLPPGTKLAQAKKFNDPDDPCKILVATDAIGMGLNLSIRRIIFNSLVKHSLNEKGEKEVDTISTSQALQIAGRAGRFSSVFKEGEVTTMHRDDLPVLKEILGKPVDPIATAGLHPTAEQIEMFAYHLPQATLSNLIDIFVSLSQVDGLYFVCNIDDFKFLADMIQHIPLNLRSRYVFCTAPINKKQPFVCTSFLKFARQFSRDEPLTFNWVCRQVNWPLSPPKNIKDLVHLEAVHDVLDLYLWLSYRFMDMFPDSNQIREIQKELDENIQIGVRNITRLIRAIDSQPTDTESNSSSTVPESETSQRKGRVLRSQNQRKELPRKSSLSSRLLRDGLLTKELLSQLQKEWAREQNEDNSIPVNNGKRKKK
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Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA surveillance system in mitochondria regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. Also implicated in recombination and chromatin maintenance pathways. May protect cells from apoptosis. Associates with mitochondrial DNA (By similarity).
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A4IGL7
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PXDN_XENTR
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Peroxidasin (EC 1.11.2.-) [Cleaved into: PXDN active fragment]
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MAGAGSWLYLTAGLLVVALPQLSHSCPSRCLCFRTTVRCMHLMLESVPAVPPHTTILDLRFNRIKDIQTGAFKHLKNLNTLLLNNNQIKRIPSEAFKDLENLKYLYLYKNEIQSIDRQAFKGLASLEQLYLHFNQIETLEPESFNYLPKLERLFLHNNRITHLVPGTFSQLESMKRLRLDSNALHCDCEILWLADLLKIYSESGNAQAAATCEYPRRLQGRSVSTITPSELNCERPRITSEPQDVDVTFGNTVYFTCRAEGNPKPEIIWLRNNNELSMKDDSRLNLLNDGTLMIQNTKETDQGIYQCMAKNVAGEVKTHEVTLRYYGTPATPTFVIQPQNTEVLVGESVTLECSATGQPHPRVTWTRGDRTPLPSDPRINITPSGGLYIQNVNQDDAGEYTCFATNSVETIHSTAYIIVQAVPQFTVVPQDRNVFEGHTVDFHCEAQGNPKPVIAWTKGGNQLSVDRRHQVLSSGTLRILRVALHDQGQYECQAVNIVGSKSTAAQLIVQTRVTPVFATVPNDMTVEVGTDVQIPCSSQGDPLPIITWNKDGIQVTESGKFHISPHGYLAIRDAGLADQGRYECVARNPIGYSSVSMVLSVLVPEVSRTGDPFVATSIIEAIATVDRAINSTRTHLFDSRPRSPGDLLALFRYPRDPYTVEQARAAEIFERTLQLIQDHVQSGLMVDLNGTSYHYNDLVSPQYLNMIANLSGCATHRRINNCSNMCFHQKYRTHDGTCNNLQHPMWGASLTAFERLLKSVYENGFNLPRGISGRIYNGFPLPLPRLVSTTLIGTHTITPDEQFTHMLMQWGQFLDHDLDSTVVALSQARFSDGQDCSVVCTNDAPCFPIMVPPNDPRVRNNARCMSMVRSSPVCGSGMTSLLMNSVYPREQMNQLTSYIDASNVYGSSDHESNEIRDSASHRGLLKQGIVQRSGKPLLPFATGPPTECMRDENESPIPCFLAGDHRANEQLGLTSMHTLWFREHNRIATELLRLNPHWDGDTIYHETRKIVGAQMQHITYSHWLPKIFGDVGMKMLGEYKSYDPNVNAGILNEFATAAFRFGHTLINPILYRLDEKFEPIPQGHVPLHRAFFSPFRIVNEGGIDPLLRGLIGVAAKMRVTSQLLNTELTEKLFSMAHAVALDLAALNVQRGRDHGIPPYHDFRVFCNLSTVQTFDDLRNEIKNPDVREKLKRLYGSPLNIDLFPALMVEDLIPGSRLGPTLMCLLTTQFRNIRDGDRFWYENPGVFTAAQLTQIKQTSLARVLCDNGDNITKVQHDLFRVAEFPHGYVSCKNIAKMDLRVWQDCCEDCRTRGQFSTFSNHFRGKRSTEHSYKEDNKEPSSLLNQSVNTTCNTEQPKNLPHVNDFKEFVLDMQKTITGLRKQIKKLESRLSNTDCTDETGESHSTKEKWNKDACTKCECYNGHITCFVKSCPPVNCSRPQRIEGVCCPVCTDDKIQST
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Catalyzes the two-electron oxidation of bromide by hydrogen peroxide and generates hypobromite as a reactive intermediate which mediates the formation of sulfilimine cross-links between methionine and hydroxylysine residues within an uncross-linked collagen IV/COL4A1 NC1 hexamer and participates to the basement membrane integrity. Moreover brominates alpha2 collagen IV chain/COL4A2 and leads to bromine enrichment of the basement membranes.
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A4IGM9
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AURKB_XENTR
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Aurora kinase B (EC 2.7.11.1) (Aurora/IPL1-related kinase 2) (AIRK2) (XAIRK2) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase aurora-B) (xAurora-B)
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MSYKENLNPSSYTSKFATPSSATAAQRVLRKEPYVSTFTTPSDNLLAQRAQLARITPSASSSVPGRVAVSMDASSQNTALAELPKRKFTIDDFDIGRPLGKGKFGNVYLARDKQNKFIMALKVLFKSQLEKEGVEHQLRREIEIQSHLRHPNILRMYNYFHDRKRIYLMLEFAPRGELYKELQKHGRFDEQRSATFMEELADALQYCHERKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLRRRTMCGTLDYLPPEMIEGKTHDEKVDLWCAGVLCFEFLVGMPPFDSPSHTETHRRIVNVDLKFPPFLSDGSKDLISKLLRYHPPQRLPLKGVMEHPWVKANSRRVLPPVFQSSSK
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Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. Phosphorylates 'Ser-10' of histone H3 during mitosis.
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A4IGY6
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S39AE_XENTR
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Metal cation symporter ZIP14 (Solute carrier family 39 member 14) (Zrt- and Irt-like protein 14) (ZIP-14)
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MPLLLLSALLPFSLMAGPTPSTGKELSAASFLQDILQRYGENESLSMPQLQSLLENLEVGKGGGNQRNMSQCLSSSTLFAAHNLTSGSVVDAEGFQSFCPTILQQLETRACQESPAFQNETTPGAEGRPSPGEVWGYGFLCVTVISLCSLFGAGVVPFMKKACYKRLLLFCIALAIGTLFSNALFQLIPEAFGFNPLEDSYVFTSSVIFGGFYLFFFTEKVLKMMLKQKHEHGHSHYSADTSKRDAEEGVTEKLQNGDLDHMIPPPHGSESDLRGDEKAVQQQDLPGQQSSCYWLKGIRYSDIGTLAWMITLSDGLHNFIDGLAIGASFTVSVFQGVSTSIAILCEEFPHELGDFVILLNAGMSIPQALFFNFLSACCCYLGLAFGILAGSHFSSNWIFALAGGMFLYIALSDMFPEMNEVSKEDEEGGRAFSAFMIQNAGLLTGFAIMLLLTTFSGQIQLG
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Electroneutral transporter of the plasma membrane mediating the cellular uptake of the divalent metal cations zinc, manganese and iron that are important for tissue homeostasis, metabolism, development and immunity (By similarity). Functions as an energy-dependent symporter, transporting through the membranes an electroneutral complex composed of a divalent metal cation and two bicarbonate anions. Beside these endogenous cellular substrates, can also import cadmium a non-essential metal which is cytotoxic and carcinogenic (By similarity).
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A4IH17
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BAG6_XENTR
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Large proline-rich protein bag6 (BCL2-associated athanogene 6) (HLA-B-associated transcript 3)
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MEVTVKTLDSQTRTFTVDAEITVKEFKTHISSDVGISPEKQRLIYQGRVLQEDKKLKEYNVDGKVIHLVERAPPQTQPSTGGPSTSSSTSPSSSNAANVPGAGAPERNGNSYVMVGTFNLPHVMSGLGEASRGPRVSTVSGNDGSTLDVHINLDQQLPVQSEPRVRLVLAQQILQDIQRILDRLEGQPVNEQTAEPMDTAVSEGEASSRETLPQTTQNTDGQSNTAPTSHPSPSEYVEVLQSLSRVEERLAPFMQRYREILSSATSDAYENQEEREQSQRIINLVGESLRLLGNALVAVSDLRCNLSSASPRHLHVVRPMSHYTGPMLLQQAAIPIQINVGTTVTMTGNGTHAGQMPSDGNAAHTPTNTSEPQRSNSDNQPPSSGERPASEIPPTSVPHPHPRVVRITHQTVEPVMMMHMNIQDSGPGGPTNIPPPTAGHGGSAHIHMPGLPPEFMQAISHQITQQAVAAASGQQIPGFQAPPRFVFTRPAAPSFPPQPGVATTPPGPGGATTAVPGATVGPAGNASLAQMISGLVGQLLMHPVIVAQGGSNTPSSTSTPTSTSSSSSSSSSTVTTSTTTTSSTSFPTVSSGPSPQPPPGTDQHLSQLLGSLLGTAGSGMSNFAMGSPSITVTVPGMPAFLQGVTDILQATQTVPVSTSPPQSASQAPPPSSPSPPPAHSSPPPAAAPESLPPEFFTSVVQGVLSSMLGSLSAADQSGTESIAAFIQRLSGSHNIFQPDAEGPGGFFGDLLTLICHNFSLVDMVMLLHGHSQPLQNLQPQLRSFFLQEYLHQADPTPNNIQMASRNLTNGLEEYIRESFASVTVRDDVDITRTNLEFLQDQFNRITTHILHCADSTFGQRLLEMCNQSLFEWLALNLYCLRGDQSALTSVINERIRRLSLDVSPVLVSWVTSVLSLRLQVLLGQMPVTEGEIQRHIRRVGDVPQAPEASSQDQPMETTPVDCQNGAASPVPATTVEEVLFLPPQSSVPTICTDSEHPTQEDTGSEQWAASVPPEWVPVIRQDMQNQRKMKQQPPLSDAYLSGMPAKRRKTMQGEGPHLSLSEAVSRAMKATGAKPESSTDCVRRELDNSEAQGRYREQLCQDIQNILQDNESYSAQRFPNTQRAFRGDP
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ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. Functions as part of a cytosolic protein quality control complex, the bag6/bat3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The bag6/bat3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Similarly, the bag6/bat3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The bag6/bat3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome. Also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. Also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. May ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress. By stabilizing a large spectrum of proteins, may indirectly affect different biological processes including apoptosis. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. When nuclear, may also act as a component of some chromatin regulator complex.
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