entry
stringlengths 6
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stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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O70548
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TELT_MOUSE
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Telethonin (Titin cap protein)
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MATSELSCQVSEENQERREAFWAEWKDLTLSTRPEEGCSLHEEDTQRHETYHRQGQCQAVVQRSPWLVMRLGILGRGLQEYQLPYQRVLPLPIFTPTKVGASKEEREETPIQLRELLALETALGGQCVERQDVAEITKQLPPVVPVSKPGPLRRTLSRSMSQEAQRG
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Muscle assembly regulating factor. Mediates the antiparallel assembly of titin (TTN) molecules at the sarcomeric Z-disk (By similarity).
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O70551
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SRPK1_MOUSE
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SRSF protein kinase 1 (EC 2.7.11.1) (SFRS protein kinase 1) (Serine/arginine-rich protein-specific kinase 1) (SR-protein-specific kinase 1)
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MERKVLALQARKKRTKAKKDKAQRKPETQHRGSAPHSESDIPEQEEEILGSDDDEQEDPNDYCKGGYHLVKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKKFVAMKVVKSAEHYTETALDEIRLLKSVRNSDPNDPNGEMVVQLLDDFKISGVNGTHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIQQVLQGLDYLHTKCRIIHTDIKPENILLSVNEQYIRRLAAEATEWQRSGAPPPSGSAVSTAPQPKPADKMSKNKKKKLKKKQKRQAELLEKRMQEIEEMEKESGPGQKRPNKQEESESPVDRPLTENPPNKMTQEKLEESNSIGQDQTLTERGGEGGAPEINCNGVIGVVNYPENSNNETLRHKEDLHNANDCDVHTLKQEPSFLNSSNGDSSPSQDTDSCTPTASETMVCQSSAEQSLTRQDITQLEESIRADTPSGDEQEPNGALDSKGKFSAGNFLINPLEPKNAEKLQVKIADLGNACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYLFEPHSGEDYTRDEDHIALIIELLGKVPRKLIVAGKYSKEFFTKKGDLKHITKLKPWGLLEVLVEKYEWPQEEAAGFTDFLLPMLELMPEKRATAAECLRHPWLNS
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Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Phosphorylates SFRS2, ZRSR2, LBR and PRM1. Phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Can induce splicing of exon 10 in MAPT/TAU (By similarity). {ECO:0000250, ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:9446799}.
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O70552
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BTG4_MOUSE
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Protein BTG4 (BTG family member 4) (Protein PC3b)
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MRDEIATAVFFVTRLVKKHEKLSTQQIETFALKLMTILFEKYRGHWHPDCPSKGQAFRCIRINNNENKDPVLERACAESNVNFFHLGLPKEMTIWVDPYEVCCRYGEKKHPFTIASFKGRWENWELAQHVSCAVNRATGDCSSGTSSDEESCSREAQIIPKVNNPKSVYQVENFKQSLQPWFCLPRRKHLADGRGFLPGAACHPVPKSSKWCRPASRRVDRYHWVNAQLFSGQTAPGEPGEEALSSLKQK
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Adapter protein that bridges CNOT7, a catalytic subunit of the CCR4-NOT complex, to EIF4E, and facilitates maternal mRNAs decay during the maturation of oocytes and in the fertilized egg. It is therefore required for the maternal-zygotic transition (MZT), zygotic cleavage and initiation of embryonic development.
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O70566
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DIAP2_MOUSE
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Protein diaphanous homolog 2 (Diaphanous-related formin-2) (DRF2) (mDia3)
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MEELGAAASGAGGGGGGGEEHGGGRSNKRGAGNRAANEEETRNKPKLRDRITSFRKSATKREKPVIQHSIDYQTAVVEIPPALIVHDDRSLILSEKEVLDLFEKMMEDMNLNEEKKAPLRKKDFSIKREMVVQYISATSKSIVGSKVLGGLKNSKHEFTLSSQEYVHELRSGISDEKLLNCLESLRVSLTSHPVSWVNNFGYEGLGVLLDVLEKLLDKKQQENIDKKNQYKVIQCLKAFMNNKFGLQRILGDERSLLLLARAIDPKQQNMMTEIVKILSAICIVGEENILDKLLGGITAAAELNNRERFSPIVEGLENNEALHLQVACMQFINALVTSPYDLDFRIHLRNEFLRCGLKAMLPTLKEIENEGLDIQLRVFEENKEDDLSELSHRLNDIRAEMDDINEVYHLLYNMLKDTAAEPYLLSILQHFLLIRNDYYIRPQYYKIIEECVSQIVLHCSGMDPDFKYRQRIDFDFTHLLDACVNKAKVEENEQKAMEFSKKFDEEFTARQEAQAELQKRDEKIKELETEIQQLRGQGVPSAIPGPPPPPPLPGAGPCPPPPPPPPPPPPLPGVVPPPPPPLPGMPGIPPPPPPPLSGVPPPPPPPGGVFPLLSGPIELPYGMKQKKLYKPDIPMKRINWSKIEPKELSENCVWLKLKEEKYENADLFAKLALTFPSQMKGQRNTEAAEENRSGPPKKKVKELRILDTKTAQNLSIFLGSYRMPYEEIKNIILEVNEEMLSEALIQNLVKYLPDQNALRELAQLKSEYDDLCEPEQFGVVMSTVKMLRPRLTSILFKLTFEEHVNNIKPSIIAVTLACEELKKSESFKRLLELILLVGNYMNSGSRNAQSLGFKINFLCKIKDTKSADQKSTLLHFLAEICDEKYRDILKFPDELEHVESAGKVSAQILKSNLVAMEQSILHLEKNIKNFPPAESHHDKFVEKMMSFTQNAREQYDKLSTMHSNMLKLYESLGEYFIFDPNTVNMEEFFGDLNTFRTLFLEALKENHKRKEMEEKSRRAKLAKEKAEQEKLERQKKKKQLIDINKEGDETGVMDNLLEALQSGAAFRDRRKRIPRNPDNRRPPLERSRSRHNGAMSSK
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May be involved in oogenesis.
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O70571
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PDK4_MOUSE
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[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 4)
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MKAARFVMRSASSLSSASLVPREVELFSRYSPSPLSMKQLLDFGSENACERTSFAFLRQELPVRLANILKEIDILPDRLVNTPSVQLVKSWYIQSLMDLVEFHEKSPEDQKALSEFVDTLVKVRNRHHNVVPTMAQGILEYKDTCTVDPVTNQNLQYFLDRFYMNRISTRMLMNQHILIFSDSKTGNPSHIGSIDPNCDVVAVVQDAFECAKMLCDQYYLTSPELNLTQVNGKFPGQPIHIVYVPSHLHHMLFELFKNAMRATVEHQENRPSLTPVEATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPTPVMDNSRNAPLAGFGYGLPISRLYAKYFQGDLNLYSMSGYGTDAIIYLKALSSESVEKLPVFNKSAFKHYQMSSEADDWCIPSREPKNLAKEKLAV
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Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism in response to prolonged fasting and starvation. Plays an important role in maintaining normal blood glucose levels under starvation, and is involved in the insulin signaling cascade. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. In the fed state, mediates cellular responses to glucose levels and to a high-fat diet. Regulates both fatty acid oxidation and de novo fatty acid biosynthesis. Plays a role in the generation of reactive oxygen species. Protects detached epithelial cells against anoikis. Plays a role in cell proliferation via its role in regulating carbohydrate and fatty acid metabolism.
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O70572
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NSMA_MOUSE
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Sphingomyelin phosphodiesterase 2 (EC 3.1.4.12) (Lyso-platelet-activating factor-phospholipase C) (Lyso-PAF-PLC) (Neutral sphingomyelinase) (N-SMase) (nSMase)
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MKLNFSLRLRVFNLNCWDIPYLSKHRADRMKRLGDFLNLENFDLALLEEVWSEQDFQYLRQRLSLTYPDAHYFRSGMIGSGLCVFSKHPIQEIFQHVYSLNGYPYMFHHGDWFCGKSVGLLVLRLSGLVLNAYVTHLHAEYSRQKDIYFAHRVAQAWELAQFIHHTSKNADVVLLCGDLNMHPKDLGCCLLKEWTGLHDAFVETEDFKGSDDGCTMVPKNCYVSQQDLGPFPSGIRIDYVLYKAVSEFHVCCETLKTTTGCDPHSDKPFSDHEALMATLYVKHSPPQEDPCTACGPLERSDLISVLREARTELGLGIAKARWWAAFSGYVIVWGLSLLVLLCVLAAGEEAREVAIILCIPSVGLVLVAGAVYLFHKQEAKGLCRAQAEMLHVLTRETETQDRGSEPHLAYCLQQEGDRA
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Catalyzes, at least in vitro, the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Also hydrolyzes 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine (lyso-platelet-activating factor) in vivo (By similarity). Also acts on 1-acyl-2-lyso-sn-glycero-3-phosphocholine (lyso-PC) and sphingosylphosphocholine (By similarity).
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O70576
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STAG3_MOUSE
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Cohesin subunit SA-3 (SCC3 homolog 3) (Stromal antigen 3) (Stromalin-3)
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MPTLWSPSTQHHGSSSGSESSPLQKSVRRAQMALSPCSSSILPCDDRDSQGTAEWDSPSTNEDSDFEDSLRRNVKKRAAKQPPKAVPAAKHRKKQSRIVSSGNGKNESVPSTNYLFDAVKAARSCMQSLVDEWLDNYKQDENAGFLELINFFIRACGCKSTVTPEMFKTMSNSEIIQHLTEEFNEDSGDYPLTAPGPSWKKFQGSFCEFVKTLVYQCQYSLLYDGFPMDDLISLLIGLSDSQVRAFRHTSTLAAMKLMTSLVKVALQLSLHKDNNQRQYEAERNKGPEQRAPERLESLLEKRKEFQENQEDIEGMMNAIFRGVFVHRYRDILPEIRAICIEEIGYWMQSYSTSFLNDSYLKYIGWTLHDKHKEVRLKCVKALAGLYSNQELSLRMELFTNRFKDRMVSMVMDRECEVAVEAIRLLTLILKNMEGVLTSADCEKIYSIVYISNRAMASSAGEFVYWKIFHPECGAKAVSDRERRRSPQAQKTFIYLLLAFFMESEHHNHAAYLVDSLWDCAGSYLKDWESLTNLLLQKDQNLGDMQERMLIEILVSSARQAAEGHPPVGRITGKKSLTAKERKLQAYDKMKLAEHLIPLLPQLLAKFSADAENVAPLLQLLSYFDLSIYCTQRLEKHLELLLQQLQEVVVKHVEPEVLEAAAHALYLLCKPEFTFFSRVDFARSQLVDFLTDRFQQELDDLMQSSFLDEDEVYSLTATLKRLSAFYNAHDLTRWEISEPCSRLLRKAVDTGEVPHQVILPALTLVYFSILWTVTHISESTSHKQLMSLKKRMVAFCELCQSCLSDVDPEIQEQAFVLLSDLLLIFSPQMIVGGRDFLRPLVFFPEATLQSELASFLMDHVFLQPGELGNGQSQEDHVQIELLHQRRRLLAGFCKLLLYGVLELDAASDVFKHYNKFYEDYGDIIKETLTRARQIDRCQCSRILLLSLKQLYTELIQEQGPQGLTELPAFIEMRDLARRFALSFGPQQLHNRDLVVMLHKEGIKFSLSELPPAGSSHEPPNLAFLELLSEFSPRLFHQDKRLLLSYLEKCLQRVSKAPNHPWGPVTTYCHSLHPLEITAEASPRGPPHSKKRCVEGPCRPQEEESSSQEESLQLNSGPTTPTLTSTAVKRKQSLRTVGKKQKGRPGPGPGPGPELICSQQLLGTQRLKMSSAPCFQIRCDPSGSGLGKQLTRLSLMEEDEEEELRLLDEEWQRGDKMLHSPSSPSEHGLDLLDTTELNMEDF
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Meiosis specific component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The meiosis-specific cohesin complex probably replaces mitosis specific cohesin complex when it dissociates from chromatin during prophase I.
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O70577
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S22A2_MOUSE
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Solute carrier family 22 member 2 (Organic cation transporter 2) (mOCT2)
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MPTVDDILEHIGEFHLFQKQTFFLLALLSGAFTPIYVGIVFLGFTPNHHCRSPGVAELSQRCGWSPAEELNYTVPGLGSAGEVSFLSQCMRYEVDWNQSTLDCVDPLSSLAANRSHLPLSPCEHGWVYDTPGSSIVTEFNLVCAHSWMLDLFQSLVNVGFFIGAVGIGYLADRFGRKFCLLVTILINAISGVLMAISPNYAWMLVFRFLQGLVSKAGWLIGYILITEFVGLGYRRTVGICYQIAFTVGLLILAGVAYALPNWRWLQFAVTLPNFCFLLYFWCIPESPRWLISQNKNAKAMKIIKHIAKKNGKSVPVSLQSLTADEDTGMKLNPSFLDLVRTPQIRKHTLILMYNWFTSSVLYQGLIMHMGLAGDNIYLDFFYSALVEFPAAFIIILTIDRIGRRYPWAVSNMVAGAACLASVFIPDDLQWLKITVACLGRMGITIAYEMVCLVNAELYPTYIRNLAVLVCSSMCDIGGIVTPFLVYRLTDIWLEFPLVVFAVVGLVAGGLVLLLPETKGKALPETIEDAEKMQRPRKKKEKRIYLQVKKAELS
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Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics. Functions as a Na(+)-independent, bidirectional uniporter (By similarity). Cation cellular uptake or release is driven by the electrochemical potential, i.e. membrane potential and concentration gradient (By similarity). However, may also engage electroneutral cation exchange when saturating concentrations of cation substrates are reached (By similarity). Predominantly expressed at the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds by hepatic and renal clearance from the blood flow. Implicated in monoamine neurotransmitters uptake such as histamine, dopamine, adrenaline/epinephrine, noradrenaline/norepinephrine, serotonin and tyramine, thereby supporting a physiological role in the central nervous system by regulating interstitial concentrations of neurotransmitters. Also capable of transporting dopaminergic neuromodulators cyclo(his-pro), salsolinol and N-methyl-salsolinol, thereby involved in the maintenance of dopaminergic cell integrity in the central nervous system. Mediates the bidirectional transport of acetylcholine (ACh) at the apical membrane of ciliated cell in airway epithelium, thereby playing a role in luminal release of ACh from bronchial epithelium. Also transports guanidine and endogenous monoamines such as vitamin B1/thiamine, creatinine and N-1-methylnicotinamide (NMN). Mediates the uptake and efflux of quaternary ammonium compound choline (By similarity). Mediates the bidirectional transport of polyamine agmatine and the uptake of polyamines putrescine and spermidine. Able to transport non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha). Also involved in the uptake of xenobiotic 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP). May contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (By similarity).
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O70578
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CCG1_MOUSE
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Voltage-dependent calcium channel gamma-1 subunit (Dihydropyridine-sensitive L-type, skeletal muscle calcium channel subunit gamma)
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MSQTKTAKVRVTLFFILVGGVLAMVAVVTDHWAVLSPHLEHHNETCEAAHFGLWRICTARVAVHNKDKSCEHVTPSGEKNCSYFRHFNPGESSEIFEFTTQKEYSISAAAIAIFSLGFIIVGSICAFLSFGNKRDYLLRPASMFYAFAGLCLIVSVEVMRQSVKRMIDSEDTVWIEHYYSWSFACACAAFILLFLGGLFLLLFSLPRMPQNPWESCMDAEPEH
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Regulatory subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Regulates channel inactivation kinetics.
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O70579
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PM34_MOUSE
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Peroxisomal membrane protein PMP34 (34 kDa peroxisomal membrane protein) (Solute carrier family 25 member 17)
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MASVLSYESLVHAVAGAVGSVTAMTVFFPLDTARLRLQVDEKRKSKTTHAVLLEIIKEEGLLAPYRGWFPVISSLCCSNFVYFYTFNSLKAVWVKGQRSSTGKDLVVGFVAGVVNVLLTTPLWVVNTRLKLQGAKFRNEDIIPTNYKGIIDAFHQIIRDEGILALWNGTFPSLLLVFNPAIQFMFYEGLKRQLLKKRMKLSSLDVFIIGAIAKAIATTVTYPMQTVQSILRFGRHRLNPENRTLGSLRNVLSLLHQRVKRFGIMGLYKGLEAKLLQTVLTAALMFLVYEKLTAATFTVMGLKSTHKH
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Peroxisomal transporter for multiple cofactors like coenzyme A (CoA), flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN) and nucleotide adenosine monophosphate (AMP), and to a lesser extent for nicotinamide adenine dinucleotide (NAD(+)), adenosine diphosphate (ADP) and adenosine 3',5'-diphosphate (PAP). May catalyze the transport of free CoA, FAD and NAD(+) from the cytosol into the peroxisomal matrix by a counter-exchange mechanism.
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O70582
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LX12B_MOUSE
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Arachidonate 12-lipoxygenase, 12R-type (12R-LOX) (12R-lipoxygenase) (EC 1.13.11.-) (Epidermis-type lipoxygenase 12) (Epidermis-type lipoxygenase 2) (e-LOX 2)
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MATYKVKVATGTDFFSGTLDSISLTIVGTQGESHKQRLNHFGRDFATGAVDDYTVQCQQDLGELIIIRLHKEPHSFLAKDPWYCNYVQICAPDCRVYHFPAYQWMDGYETLALREATGKITADDTLPILLEHRQEEIRAKKDFYHWRVFVPGLPNYVDIPSYHPPPRRCRNPNRPEWDGYIPGFPILINIKATRFLNSNLRFSFVKTASFFYRLGPMALAFKLRGLVDRKRSWKRLKDIKNIFPATKSVVSEYVAEHWTEDSFFGYQYLNGINPGLIRRCTQIPDKFPVTDEMVAPFLGEGTCLQAELERGNIYLADYRILDGIPTVELNGQQQHHCAPMCLLHFGPDGNMMPIAIQLSQTPGPDCPIFLPNDSEWDWLLAKTWVRYAEFYSHEAVAHLLESHLIGEAFCLALLRNLPMCHPLYKLLIPHTRYNVQINSIGRALLLNKGGLSARAMSLGLEGFAQVMVRGLSELTYKSLCIPNDFVERGVQDLPGYYFRDDSLAVWYAMERYVTEIITYYYPNDAAVEGDPELQCWVQEIFKECLLGRESSGFPTCLRTIPELIEYVTMVMYTCSARHAAVNSGQLEYTSWMPNFPSSMRNPPMQTKGLTTLQTYMDTLPDVKTTCIVLLVLWTLCREPDDRRPLGHFPDIHFVEEGPRRSIEAFRQNLNQISHNIRQRNKCLTLPYYYLDPVLIENSISI
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Catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species. Does not convert arachidonic acid to (12R)-hydroperoxyeicosatetraenoic acid/(12R)-HPETE. In the skin, acts upstream of ALOXE3 on the lineolate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. May also play a role in the regulation of the expression of airway mucins (By similarity).
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O70583
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TRI18_MOUSE
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E3 ubiquitin-protein ligase Midline-1 (EC 2.3.2.27) (Midin) (RING finger protein Midline-1) (RING-type E3 ubiquitin transferase Midline-1) (Tripartite motif-containing protein 18)
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METLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNEPVESINAFQCPTCRHVITLSQRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSETRRERAFDANTMSSAEKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEPIPDSHIRGLMCLEHEDEKVNMYCVTDDQLICALCKLVGRHRDHQVAALSERYDKLKQNLESNLTNLIKRNTELETLLAKLIQTCQHVEVNASRQEAKLTEECDLLIEIIQQRRQIIGTKIKEGKVIRLRKLAQQIANCKQCLERSASLISQAEHSLKENDHARFLQTAKNITERVSMATASSQVLIPEINLNDTFDTFALDFSREKKLLECLDYLTAPNPPAIREELCTASYDTITVHWTSEDEFSVVSYELQYTIFTGQANVVNVACDGTCLLGSAGLCNSADSWMIVPNIKQNHYTVHGLQSGTKYIFTVKAINQAGSRSSEPGKLKTNSQPFRLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHEWIGKNAASWALCRCHNHWAVRHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCPTFTVWNKCLTIVTGLPIPDHLDCTEQRP
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Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination.
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O70584
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NKX28_MOUSE
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Homeobox protein Nkx-2.8 (Homeobox protein NK-2 homolog H) (Homeobox protein Nkx-2.9)
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MATSGRLGFTVRSLLNLPEQDAKPRVRREQQTCVPQTAAWLESECSHYLSSDESGLETSPADSSQLASLRRESPGSDPEKRRKRRVLFSKAQTLELERRFRQQRYLSAPEREQLARLLRLTPTQVKIWFQNHRYKLKRGRAPGITEPSDMAASSDLHAAPGLLRRVVVPVLVHDRPPSNNGRGEGTSAVPQDKCSARLATACPVPGYTAFGPGSALGLFPAYQHLAPPALVSWNW
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Possible role in the specification of a distinct subset of neurons.
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O70585
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DTNB_MOUSE
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Dystrobrevin beta (DTN-B) (mDTN-BDTN-B) (Beta-dystrobrevin)
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MIEEGGNKRKTMAEKRQLFIEMRAQNFDVIRLSTYRTACKLRFVQKRCNLHLVDIWNMIEAFRDNGLNTLDHSTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMVAAYDSEGRGKLTVFSVKAMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTMMADPPPQCLVWLPLMHRLAHVENVFHPVECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKEHSSWKSPAKKLSHAISKSLGCVPSREPPHPVFPEQPEKPLDLAHLVPPRPLTNMNDTVVSHMSSGVPTPTKRLQYSQDMPNLLADEHALIASYVARLQHCTRVLDSPSRLDEEHRLIARYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKAQATGSPHTSPTHGGGRPMPMPVRSTSAGSTPTHGPQDSLSGVGGDVQEAFAQGTRRNLRNDLLVAADSITNTMSSLVKELHSGAEAEEQAGTEKTREGLPPRGTFLSVFLLHTWTKLAGCQTHSTSRERSQAYGKWGGTA
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Scaffolding protein that assembles DMD and SNTA1 molecules to the basal membrane of kidney cells and liver sinusoids. May function as a repressor of the SYN1 promoter through the binding of repressor element-1 (RE-1), in turn regulates SYN1 expression and may be involved in cell proliferation regulation during the early phase of neural differentiation. May be required for proper maturation and function of a subset of inhibitory synapses.
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O70589
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CSKP_MOUSE
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Peripheral plasma membrane protein CASK (EC 2.7.11.1) (Calcium/calmodulin-dependent serine protein kinase)
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MADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTSSGLLAAERAVSQVLDSLEEIHALTDCSEKDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNPPSDAVQRAKEVLEEISCYPENNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEALRVTPPPTSPYLNGDSPESANGDMDMENVTRVRLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIVPSYRTQSSSCERDSPSTSRQSPANGHSSTNNSVSDLPSTTQPKGRQIYVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPELQEWRVACIAMEKTKQEQQASCTWFGKKKKQYKDKYLAKHNAVFDQLDLVTYEEVVKLPAFKRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITPGLNEDESLQRLQKESDVLQRTYAHYFDLTIINNEIDETIRHLEEAVELVCTAPQWVPVSWVY
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Multidomain scaffolding Mg(2+)-independent protein kinase that catalyzes the phosphotransfer from ATP to proteins such as NRXN1, and plays a role in synaptic transmembrane protein anchoring and ion channel trafficking (By similarity). Contributes to neural development and regulation of gene expression via interaction with the transcription factor TBR1. Binds to cell-surface proteins, including amyloid precursor protein, neurexins, and syndecans. May mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1. Component of the LIN-10-LIN-2-LIN-7 complex, which associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules.
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O70593
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SGTA_RAT
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Small glutamine-rich tetratricopeptide repeat-containing protein alpha (Alpha-SGT) (Small glutamine-rich protein with tetratricopeptide repeats 1)
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MDNRKRLAYAIIQFLHGQLRHGGLSSDAQESLEVAIQCLETAFGVTLEDSDLALPQTLPEIFEAATASKEMPQDPRGPDRTPPSEEDSAEAERLKTEGNEQMKLENFEAAVHLYGKAIELNPANAVYFCNRAAAYSKLGNYVGAVQDCERAIGIDPGYSKAYGRMGLALSSLNKHAEAVAYYKKALELDPDNDTYKSNLKIAELKLREAPSPTGGVGSLDIAGLLNNPHFITMASSLMNSPQLQQLMSGMISGGHNPLGTPGSSPQHSDLASLIQAGQQFAQQMQQQNPEFVEQIRSQVVRSRTPSASHEEQQE
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Co-chaperone that binds misfolded and hydrophobic patches-containing client proteins in the cytosol. Mediates their targeting to the endoplasmic reticulum but also regulates their sorting to the proteasome when targeting fails. Functions in tail-anchored/type II transmembrane proteins membrane insertion constituting with ASNA1 and the BAG6 complex a targeting module. Functions upstream of the BAG6 complex and ASNA1, binding more rapidly the transmembrane domain of newly synthesized proteins. It is also involved in the regulation of the endoplasmic reticulum-associated misfolded protein catabolic process via its interaction with BAG6: collaborates with the BAG6 complex to maintain hydrophobic substrates in non-ubiquitinated states. Competes with RNF126 for interaction with BAG6, preventing the ubiquitination of client proteins associated with the BAG6 complex (By similarity). Binds directly to HSC70 and HSP70 and regulates their ATPase activity.
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O70594
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OCTN2_RAT
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Organic cation/carnitine transporter 2 (CT1) (High-affinity sodium-dependent carnitine cotransporter) (Solute carrier family 22 member 5) (UST2r)
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MRDYDEVTAFLGEWGPFQRLIFFLLSASIIPNGFNGMSIVFLAGTPEHRCLVPHTVNLSSAWRNHSIPLETKDGRQVPQSCRRYRLATIANFSALGLEPGRDVDLEQLEQENCLDGWEYNKDVFLSTIVTEWDLVCKDDWKAPLTTSLFFVGVLMGSFISGQLSDRFGRKNVLFLTMGMQTGFSFLQLFSVNFEMFTVLFVLVGMGQISNYVAAFVLGTEILSKSIRIIFATLGVCIFYAFGFMVLPLFAYFIRDWRMLLLALTVPGVLCGALWWFIPESPRWLISQGRVKEAEVIIRKAAKFNGIVAPSTIFDPSELQDLNSKKPQSHHIYDLVRTRNIRIITIMSIILWLTISVGYFGLSLDTPNLHGDIYVNCFLLAAVEVPAYVLAWLLLQHLPRRYSISAALFLGGSVLLFIQLVPSELFYLSTALVMVGKFGITSAYSMVYVYTAELYPTVVRNMGVGVSSTASRLGSILSPYFVYLGAYDRFLPYILMGSLTILTAILTLFFPESFGAPLPDTIDQMLRVKGIKQWQIQSQTRTQKDGGESPTVLKSTAF
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Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Also relative uptake activity ratio of carnitine to TEA is 11.3. May also contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (Probable).
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O70595
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ABCB6_RAT
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ATP-binding cassette sub-family B member 6 (ABC-type heme transporter ABCB6) (EC 7.6.2.5) (Ubiquitously-expressed mammalian ABC half transporter)
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MVTVGNYCEAEGPAGPAWTQNGLSPCFFYTLVPSTLMTLGVLALVLVLPCRRREVPAGTEELSWAAGPRVAPYALQLSLAILQMALPLASLAGRVGTARGVRLPGYLLLASVLESLASACGLWLLVVERSQARQSLAMGVWMKFRHSLGLLLLWTVTFAAENLVLVSWNSPQWWWSRADLGQQVQFGLWVLRYMTSGGLFILGLWAPGLRPQSYTLHVNEEDQDGGRNQGRSTDPRSTWRDLGRKLRLLSGYLWPRGSPSLQLTVLLCMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVKDVPGAGPLRFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEMWQLQQQGQETVPEDS
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ATP-dependent transporter that catalyzes the transport of a broad-spectrum of porphyrins from the cytoplasm to the extracellular space through the plasma membrane or into the vesicle lumen (By similarity). May also function as an ATP-dependent importer of porphyrins from the cytoplasm into the mitochondria, in turn may participate in the de novo heme biosynthesis regulation and in the coordination of heme and iron homeostasis during phenylhydrazine stress (By similarity). May play a key role in the early steps of melanogenesis producing PMEL amyloid fibrils (By similarity). In vitro, it confers to cells a resistance to toxic metal such as arsenic and cadmium and against chemotherapeutics agent such as 5-fluorouracil, SN-38 and vincristin (By similarity). In addition may play a role in the transition metal homeostasis.
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O70597
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PX11A_RAT
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Peroxisomal membrane protein 11A (28 kDa peroxisomal integral membrane protein) (PMP28) (Peroxin-11A) (Peroxisomal biogenesis factor 11A) (Peroxisomal coatomer receptor) (Peroxisomal membrane protein 26) (Pmp26p) (Protein PEX11 homolog alpha) (PEX11-alpha) (RnPEX11p)
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MDAFIRVANQSQGRDRLFRATQHACMLLRYLLESKAGKEAVVTKLKNLETSVSTGRKWFRLGNVLHAIQATEQSIQATDLVPRLCLTLANLNRVVYYICDTVLWAKSVGLTSGINREKWQMRAARHYYYFLLLSLVRDLYEVLLHMGQVARDRAKREKSSGDPPKYSVANEESEWLQSFLLLLFQSLKRNPPLFLDTVKNFCDILIPLNQLGIYKSNLGVVGFGGLVSSVAGLITVVYPQLKLKAR
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May be involved in peroxisomal proliferation and may regulate peroxisomes division. May mediate binding of coatomer proteins to the peroxisomal membrane. Promotes membrane protrusion and elongation on the peroxisomal surface.
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O70600
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RSAD2_RAT
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S-adenosylmethionine-dependent nucleotide dehydratase RSAD2 (SAND) (EC 4.2.-.-) (Bone-expressed sequence tag 5 protein) (Radical S-adenosyl methionine domain-containing protein 2) (Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible) (Viperin)
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MLVPTALAARLLSLFQQQLGSLWSGLAMLFCWLRIALGWPDPGKGQPRVRGEPKETQETHEDPGSAQPTTPVSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLLLLKQAGMEKINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDYGDYLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRKWCRDYKVAFKINSVINRFNVDEDMNEHIKALSPVRWKVFQCLLIEGENSGEDALREAERFLISNEEFEAFLQRHKDVSCLVPESNQKMKDSYLILDEYMRFLNCTGGRKDPSRSILDVGVEEAIKFSGFDEKMFLKRGGKYVWSKADLKLDW
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Interferon-inducible antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon. Catalyzes the conversion of cytidine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP) via a SAM-dependent radical mechanism. In turn, ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple viruses and directly inhibits viral replication. Therefore, inhibits a wide range of DNA and RNA viruses. Promotes also TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating 'Lys-63'-linked ubiquitination of IRAK1 by TRAF6. Plays a role in CD4+ T-cells activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins.
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O70601
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LAT_RAT
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Linker for activation of T-cells family member 1 (36 kDa phosphotyrosine adapter protein) (pp36) (p36-38)
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MEADALSPVELGLLLLPFVVMLLAALCVRCRELPASYDSASTESLYPRSILIKPPQITVPRTPATSYPLVTSFPPLRQPDLLPIPRSPQPLGGSHRMPSSRQNSDDANSVASYENQEPARKNVDEDEDEDDYPEGYLVVLPDSSPAAVPVVSSAPVPSNPDLGDSAFSMESCEDYVNVPESEESAEASLDGSREYVNVSQDAQPVIRAELASVTSQEVEDEEEEDVDGEEAPDYENLQELN
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Required for TCR (T-cell antigen receptor)- and pre-TCR-mediated signaling, both in mature T-cells and during their development. Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Couples activation of these receptors and their associated kinases with distal intracellular events such as mobilization of intracellular calcium stores, PKC activation, MAPK activation or cytoskeletal reorganization through the recruitment of PLCG1, GRB2, GRAP2, and other signaling molecules (By similarity).
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O70608
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SYCP2_RAT
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Synaptonemal complex protein 2 (SCP-2) (Synaptonemal complex lateral element protein) (rnSCP2)
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MPVRPDPQQLEKCIDDALRKNDFKPLVTLLQIDICEDVKIKCSKQFLRKLDDLICRELHKKDIQTISNILISIGRCSKNIFILGQTGLQTMIKQGLVQKMVSWFENSKEIILSQRQSKDEAVMNMIEDLFDLLMVVYDVNDEGKNQVLESFIPHICALVIDSRVNFCIQQEALKKMNLMLDRIPQDANKILCNQEILTLMSNMGERILDVGDYELQVGIVEALCRMTTEKRRQELAYEWFSMDFIANAFKKIKDCEFETDCRIFLNLVNGMLGDRRRVFTFPCLSAFLGKYELQIPSDEKLEEFWIDFNLGSHTLSFYIAGDDDDHQWEAVTVPEEKVDMYNIEVRESKKLLTLTLKNIVKISKKEGKELLLYFDAALEITNVTKKLFGGNKYKEFTRKQDISVAKTSIHVLFDASGSQILVPESQPSPVKENLIHLKEKSNLQKKLTNPLEPDNSSSQRDRKNSQDEITTPSRKKMSEASMIVPDTDRYTVRSPILLINTSTPRRSRAPLQAIHSAEKAVSKTSESGVDYAVSLKSRQSDGRNRGNNRANHNKTATVQNKGHEHHESPDQTFNEIEETLSDAYAVEKVDKPVLPGVLDISKNKAHSRWACWTPVTTIKLCNNQRSCALPGDTFTQDTGVNKKCTKQKSVSDDDSEETQRVKYSKDVIKCNKSEEAEVCERNIQEQNHPKYSQKKNTANAKKNDWHIESETTYKSVLLNKTTEESLIYKKTCVLSKDVNTTICDKSPSRKSMRSHTKSRKELMSEVTSCELDEIPVRENSKGKRFTGTAESLINLINKRYNSSDDMISTRKLKEPRDGSGFSKKPELQFNKVQRKSYRKLKTVVNVTSECPLNDVYNFSLNGADEPVIKLGIQEFQATTREASMDNSIKLVDVRNRDERDLSLKTKDERILSHERKTLFSDTETECGWDDSKTDISWLRKPKSKRLMDYSRNKNTKKCKSIKSRSSTEKGQPRSTVVLSKNIAKNDYEVIVDGRTRLPRRATKTKKNYKDLSTSGSESESEKEISYLFKDKLPTKEETVHSSAQTKKLPKKQQKVFNTEALKGQPSEEQKNSSTLRNGREDSLYLSSASVSGSSSSVEVMRCTEKITERDFTQDYDYITKSLSPYPKAASPEFLNRSNRVVGHGKSPRISETSAVCVRKSCSPASGLPFSPRHTTKNNSVMNIKNTNSVINNQRTQHCNSYSDVSSNSSEKLYMEPESPDSCENHVQSKREENHAASPFSLSSEKIEKIWFDMPNDNTHVSGPSQRGSKRRMYLEEDELSNPSEAEVQEAEEREHLVSKKLCQREHFDQHTSETSLSTPEFSVPKDWQQELQGAGMFYDNINSDYKRKTDTQHKIMDDFTTKTLKLTQQHLLAMACQARGHRDENIDKFQVTLLDELEKVEKDSQTLRDLEKEFVDIEEKIVHKMRAFHQSERERFRALKTSLDKSLLVYNSVYEENVLTSEMCLMKANMKMLQDKLLKEMHEEELLNIRRGLESLFKDHEGNNA
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Major component of the axial/lateral elements of synaptonemal complexes (SCS) during meiotic prophase. Plays a role in the assembly of synaptonemal complexes. Required for normal meiotic chromosome synapsis during oocyte and spermatocyte development and for normal male and female fertility. Required for insertion of SYCP3 into synaptonemal complexes. May be involved in the organization of chromatin by temporarily binding to DNA scaffold attachment regions. Requires SYCP3, but not SYCP1, in order to be incorporated into the axial/lateral elements.
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O70622
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RTN2_MOUSE
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Reticulon-2 (Neuroendocrine-specific protein-like 1) (NSP-like protein 1) (Neuroendocrine-specific protein-like I) (NSP-like protein I) (NSPLI)
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MGQVLPVFAHCKEAPSTASSTPDSTEGGNDDSDFRELHTAREFSEDEEEETTSQDWGTPRELTFSYIAFDGVVGSGGRRDSVVRRPRPQGRSVSEPRDPPQQSGLGDSLESIPSLSQSPEPGRRGDPDPVPPAERPLEELRLRLDQLGWVVRSAGSGEDSATSSSTPLENEEPDGLEASEAGEETNLELRLAQSLHLQLEVLTPQLSPSSGTPQAHTPSPQRSQDSNSGPDDEPLLNVVEEHWRLLEQEPITAQCLDSTDQSEFMLEPLLLVADLLYWKDTRTSGAVFTGLMASLLCLLHFSIVSVAAHLALLGLCATISLRVYRKVLQAVHRGDGTNPFQAYLDMDLTLTREQTERLSQQIASHVVSTATQLRHFFLVEDLVDSLKLALLFYILTFVGAIFNGLTLVILGVVALFTVPLLYRQHQAQIDQYVGLVTNQLSHIKAKIRAKIPGTGTLAPTASVSGSKAKAE
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Inhibits amyloid precursor protein processing, probably by blocking BACE1 activity (By similarity). Enhances trafficking of the glutamate transporter SLC1A1/EAAC1 from the endoplasmic reticulum to the cell surface (By similarity). Plays a role in the translocation of SLC2A4/GLUT4 from intracellular membranes to the cell membrane which facilitates the uptake of glucose into the cell.
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O70624
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MYOC_MOUSE
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Myocilin (Trabecular meshwork-induced glucocorticoid response protein) [Cleaved into: Myocilin, N-terminal fragment (Myocilin 20 kDa N-terminal fragment); Myocilin, C-terminal fragment (Myocilin 35 kDa N-terminal fragment)]
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MPALHLLFLACLVWGMGARTAQFRKANDRSGRCQYTFTVASPNESSCPREDQAMSAIQDLQRDSSIQHADLESTKARVRSLESLLHQMTLGRVTGTQEAQEGLQGQLGALRRERDQLETQTRDLEAAYNNLLRDKSALEEEKRQLEQENEDLARRLESSSEEVTRLRRGQCPSTQYPSQDMLPGSREVSQWNLDTLAFQELKSELTEVPASQILKENPSGRPRSKEGDKGCGALVWVGEPVTLRTAETIAGKYGVWMRDPKPTHPYTQESTWRIDTVGTEIRQVFEYSQISQFEQGYPSKVHVLPRALESTGAVVYAGSLYFQGAESRTVVRYELDTETVKAEKEIPGAGYHGHFPYAWGGYTDIDLAVDESGLWVIYSTEEAKGAIVLSKLNPANLELERTWETNIRKQSVANAFVICGILYTVSSYSSAHATVNFAYDTKTGTSKTLTIPFTNRYKYSSMIDYNPLERKLFAWDNFNMVTYDIKLLEM
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Secreted glycoprotein regulating the activation of different signaling pathways in adjacent cells to control different processes including cell adhesion, cell-matrix adhesion, cytoskeleton organization and cell migration. Promotes substrate adhesion, spreading and formation of focal contacts. Negatively regulates cell-matrix adhesion and stress fiber assembly through Rho protein signal transduction. Modulates the organization of actin cytoskeleton by stimulating the formation of stress fibers through interactions with components of Wnt signaling pathways. Promotes cell migration through activation of PTK2 and the downstream phosphatidylinositol 3-kinase signaling (By similarity). Plays a role in bone formation and promotes osteoblast differentiation in a dose-dependent manner through mitogen-activated protein kinase signaling. Mediates myelination in the peripheral nervous system through ERBB2/ERBB3 signaling. Plays a role as a regulator of muscle hypertrophy through the components of dystrophin-associated protein complex. Involved in positive regulation of mitochondrial depolarization. Plays a role in neurite outgrowth. May participate in the obstruction of fluid outflow in the trabecular meshwork (By similarity).
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O70628
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PDE9A_MOUSE
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High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A (EC 3.1.4.35)
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MGAGSSSYRPKAIYLDIDGRIQKVVFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAVKQVSEREELIQGVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARNSRTNCPCKYSFLDNKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPITLRRWLLCVHDNYRNNPFHNFRHCFCVTQMMYSMVWLCGLQEKFSQMDILVLMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAIAFQILARPECNIFASVPPEGFRQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHLTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPVVEETMLRPLWESREHYEELKQLDDAMKELQKKTESLTSGAPENTTEKNRDAKDSEGHSPPN
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Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart. Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein (Probable). In brain, involved in cognitive function, such as learning and long-term memory.
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O70631
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EST2C_RAT
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Acylcarnitine hydrolase (ACH M1) (EC 3.1.1.28) (Carboxylic ester hydrolase) (EC 3.1.1.-)
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MARKQPHSWLNAVLFGLLLILIHVWGQDSPESSSIRTTHTGQVRGKLDHVRDTKAGVHTFLGIPFAKAPVGPLRFAPPEDPEPWSGVRDGTSHPAMCLQNIDMLDEVGLTDMKMILSSIPMSEDCLYLNIYTPAHAHEGSNLPVMVCIHGGALVIGMASMCDGSLLAVNEDLVVVAIQYRLGVLGFFSTGDEHARGNWGYLDQVAALRWVQQNIAHFGGNPNRVTIFGVSAGGTSVSSHVISPMSQGLFHGAIMESGVALLPDLISETSETVSTTVAKLSGCEATDSETLVRCLRAKSGAEILVINKVFKMIPAVVDGEFLPRHPKELLASEDFHPVPSIIGVNTDEYCCTIPMVMGTAQIIKELSRENLQAVLKDTAAQMMLPPECGDLLMEEYMGNTDDPQTLQIQYAEMMGDFLFVIPALQVAHFQRSHAPVYFYEFQHAPSYFKNVRPPHVKADHADEVPFVFGSFFWGIKVDFTEEEKLLSRRMMKYWANFARHGNPNSEGLPYWPVLDHDEQYLQLDTQPAVDRALKARRLQFWTKTLPQKIQELNGAQKNHAEL
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Hydrolase with high activity towards palmitoylcarnitine. Is also active with p-nitrophenylacetate and alpha-naphthylacetate (By similarity). May also hydrolyze retinyl esters.
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O70632
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M2_I97A1
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Matrix protein 2 (Proton channel protein M2)
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MSLLTEVETLTRNGWGCRCSDSSDPLVVAASIIGILHLILWILDRLFFKCIYRRFKYGLKRGPSTEGVPESMREEYRQEQQNAVDVDDGHFVNIELE
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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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O70889
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TAT_HV193
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Protein Tat (Transactivating regulatory protein)
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MELVDPNLDPWNHPGSQPTTPCTRCYCKWCCFHCYWCFTTKGLGISYGRKKRRQRPRTPQSSQIHQDFVPKQPISQARGNPTGPKESKKEVESKAKTDP
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Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs. {ECO:0000255|HAMAP-Rule:MF_04079}. Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines or cytokine receptors. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS. Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF. {ECO:0000255|HAMAP-Rule:MF_04079}.
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O70899
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TAT_HV190
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Protein Tat (Transactivating regulatory protein)
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MDPVDPKLEPWNHPGSQPQTACNNCYCKKCCYHCQMCFLKKGLGISYGRKKRSQRHRTPASLQDHQNSISKQPLSRTHGDPTGPKEQKKEVASKTETDP
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Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs. {ECO:0000255|HAMAP-Rule:MF_04079}. Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines or cytokine receptors. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS. Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF. {ECO:0000255|HAMAP-Rule:MF_04079}.
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O70902
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ENV_HV190
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Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
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METQRNYPSLWRWGTLILGMLLICSAAQNLWVTVYYGVPVWKEAKTTLFCASDAKAYETEKHNVWATHACVPTDPNPQEMVMENVTESFNMWENNMVEQMHTDIISLWDQSLKPCVKLTPLCVTLNCTNVRNNTSNSTSSMEAGGELTNCSFNVTTVLRDKQQKVHALFYRLDVVPIDNNSTQYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGLCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEQIIIRTKNISDNTKNIIVQLKTPVNITCTRPNNNTRTSIHLGPGRAFYATGDIIGDIRQAHCNISRTDWNKTLHQVVTQLGIHLNNRTISFKPNSGGDMEVRTHSFNCRGEFFYCNTSGLFNSSWEMHTNYTSNDTKGNENITLPCRIKQIVNMWQRVGRAMYAPPIQGNIMCVSNITGLILTIDEGNASAENYTFRPGGGDMRDNWRSELYKYKVVKIEPLGIAPTKTRRRVVEREKRAVGMGASFLGFLGAAGSTMGAASITLTVQARQLLSGIVQQQSNLLRAIQARQHMLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTNVPWNSSWSNKSQSEIWDNMTWMEWDKQISNYTEEIYRLLEVSQTQQEKNEQDLLALDKWASLWTWFDISHWLWYIKIFIMIVGGLIGLRIIFAVLSIVNRVRQGYSPLSFQTLVPNPRGPDRPEGTEEGGGEQDRDRSVRLVNGFLPVVWDDLRSLSLFSYRLLRDLLLIVVRTVELLGRRGREALKYLWNLLQYWGQELKNSAIDLLNTTAIAVAEGTDGIIVIVQRAWRAILHIPRRIRQGFERSLL
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[Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. {ECO:0000255|HAMAP-Rule:MF_04083}. [Surface protein gp120]: Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. {ECO:0000255|HAMAP-Rule:MF_04083}. [Transmembrane protein gp41]: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, 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. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04083}.
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O70903
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NEF_HV190
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Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
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MGGKWSKSRMGGWSTIRERMRRAEPVAEGVGAVSRDLDRRGAVTINNTASTNRDAAWLEAQEDGEEVGFPVRPQVPLRPMTYKGAFDLSHFLKEKGGLDGLIYSKQRQDILDLWVYNTQGYFPDWQNYTPGPGERFPLTFGWCFKLVPVNPQEVEQANEGENNSLLHPMSLHGMEDDGREVLMWKFDSRLALTHLARVKHPEYKDC
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Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. {ECO:0000255|HAMAP-Rule:MF_04078}. In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network-associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase-ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration. {ECO:0000255|HAMAP-Rule:MF_04078}. Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis. {ECO:0000255|HAMAP-Rule:MF_04078}. Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR-mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD. {ECO:0000255|HAMAP-Rule:MF_04078}. Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. {ECO:0000255|HAMAP-Rule:MF_04078}.
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O71189
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R1AB_GLRV3
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Replicase polyprotein 1ab [Cleaved into: Leader protease (L-Pro) (EC 3.4.22.-) (Papain-like cysteine proteinase) (PCP); Methyltransferase/helicase/RNA-directed RNA polymerase (EC 2.1.1.-) (EC 2.7.7.48) (EC 3.6.4.13)]
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MDYIRPLRVFSFPHVNNTLEYVRYNKANGDVGAFLTTMKFIGNVKLSDFTPRCAAMIYIGKLTKGVKRTFVPPPVKGFARQYAVVSGSVSALRGDGKKVLMEARTSTSATSDVSDFDVVFEAVSNALLVVHYHRVVPYAPVKREQPKPAVKQDEQKPKRQASHWAVKPTAVGVHVPLPKKQEALEPAQSVPQQSLEEKAALTFGLFFSKGGGDESDAVILRKGKLFNRALNVPIDVKNTFVWAKIWDEASRRRGYFYVKDRAVKFFPIVRGRATIEDFIVNTAPGCDVALPRIELWSMRERAFVCTTKGWCWFNNERLRGEIYRRRCFSSSFSIGFLMHLGFRSLKVIRFAGTNILHMPSLNEERTFGWKGGDVYLPNVPKTAIVAGDRTRLGGEILASVANALNQEEVYSSVVSSITNRLVLRDQSALLSHLDTKLCDMFSQRDAMIREKPSHRCDVFLKPREREKLRELFPELSIQFSDSVRSSHPFANAMRSCFNGIFSRRCGNVCFFDIGGSFTYHVKAGHVNCHVCNPVLDVKDVKRRINEILFLSTAGGDSYVSSDLLTEAASKSVSYCSRESQNCDSRADAGFMVDVYDISPQQVAEAMDKKGALVFDIALMFPVELLYGNGEVYLEELDTLVKREGDYLAYNVGQCGEMYEHSFSNVSGFFTFSYVRTSSGNVFKLEYEGYRCGYHHLTMCRAQKSPGTEVTYRSLVPSFVGKSLVFIPVVAGSSVSFKTIVLDSDFVDRIYSYALNTIGTFENRTFEYAVGAVRSQKTHVITGSRVVHSKVDISPDDMWGLVVAVMAQAIKDRAKSIRSYNFIKASEGSLAGVFKLFFQTVGDCFSNAVSVYAKAMVHDNFNVLETLMSMPRAFIRKVPGSVVVTICTSGASDRLELRGAFDISKETFGRKLKNSRLRVFSRAIVEDSIKVMKAMKTEDGKPLPITEDSVYAFIMGNVSNVHCTRAGLLGGSKATVVSSVSKGLVARGAATKAFSGITSFFSTGSLFYDRGLTEDERLDALVRTENAINSPVGILETSRVAVSKVVAGTKEFWSEVSLNDFTTFVLRNKVLIGIFVASLGAAPIAWKYRRGIAANARRYAGSSYETLSSLSSQAAGGLRGLTSSTVSGGSLVVRRGFSSAVTVTRATVAKRQVPLALLSFSTSYAISGCSMLGIWAHALPRHLMFFFGLGTLLGARASANTWKFGGFSNNWCAVPEVVWRGKSVSSLLLPITLGVSLIIRGLLNDTIPQLAYVPPVEGRNVYDETLRYYRDFDYDEGAGPSGTQHEAVPGDDNDGSTSSVSSYDVVTNVRDVGISTNGEVTGEEETHSPRSVQYTYVEEEVAPSAAVAERQGDPSGSGTADAMAFVESVKKGVDDVFHQQSSGETAREVEVDGKGLLPESVVGEAPTQERGRAADGNTAQTAVNEGDREPVQSSLVSSPQADIPKVTQSEVHAQKEVKQEVPLATVSGATPIVDEKPAPSVTTRGVKIIDKGKAVAHVAEKKQVQVEQPKQRSLTINEGKAGKQLCMFRTCSCGVQLDVYNEATIATRFSNAFTFVDNLKGRSAVFFSKLGEGYTYNGGSHVSSGWPRALEDILTAIKYPSVFDHCLVQKYKMGGGVPFHADDEECYPSDNPILTVNLVGKANFSTKCRKGGKVMVINVASGDYFLMPCGFQRTHLHSVNSIDEGRISLTFRATRRVFGVGRMLQLAGGVSDEKSPGVPNQQPQSQGATRTITPKSGGKALSEGSGREVKGRSTYSIWCEQDYVRKCEWLRADNPVMALEPDYTPMTFEVVKTGTSEDAVVEYLKYLAIGIERTYRALLMARNIAVTTAEGVLKVPNQVYESLPGFHVYKSGTDLIFHSTQDGLRVRDLPYVLIAEKGIFTKGKDVDAVVALGDNLFVCDDILVFHDAINLIGALKVARCGMVGESFKSFEYKCYNAPPGGGKTTTLVDEFVKSPNSTATITANVGSSEDINMAVKKRDPNLEGLNSATTVNSRVVNFIVRGMYKRVLVDEVHMMHQGLLQLGVFATGASEGLFFGDINQIPFINREKVFRMDCAVFVPKKESVVYTSKSYRCPLDVCYLLSSMTVRGTEKCYPEKVVSGKDKPVVRSLSKRPIGTTDDVAEINADVYLCMTQLEKSDMKRSLKGKGKETPVMTVHEAQGKTFSDVVLFRTKKADDSLFTKQPHILVGLSRHTRSLVYAALSSKLDDKVGTYISDASPQSVSDALLTRSPRLVAFEVYERMNFGPTFEGELVRKIPTSHFVAVNGFLEDLLDGCPAFDYDFFEDDFETSDQSFLIEDVRISESFSHFTSKIEDRFYSFIRSSVGLPKRNTLKCNLVTFENRNFNADRGCNVGCDDSVAHELKEIFFEEVVNKARLAEVTESHLSSNTMLLSDWLDKRAPNAYKSLKRALGSFVFHPSMLTSYTLMVKADVKPKLDNTPLSKYVTGQNIVYHDRCVTALFSCIFTACVERLKYVVDERWLFYHGMDTAELAAALRNNLGDIRQYYTYELDISKYDKSQSALMKQVEELILLTLGVDREVLSTFFCGEYDSVVRTMTKELVLSVGSQRRSGGANTWLGNSLVLCTLLSVVLRGLDYSYIVVSGDDSLIFSRQPLDIDTSVLSDNFGFDVKIFNQAAPYFCSKFLVQVEDSLFFVPDPLKLFVKFGASKTSDIDLLHEIFQSFVDLSKGFNREDVIQELAKLVTRKYKHSGWTYSALCVLHVLSANFSQFCRLYYHNSVNLDVRPIQRTESLSLLALKARILRWKASRFAFSIKRG
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RNA-dependent RNA polymerase replicates the viral genome.
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O71305
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HBSAG_WMHBV
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Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
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MGLNQSTFNPLGFFPSHQLDPLFKANAGSADWDKNPNKDPWPQAHDTAVGAFGPGLVPPHGGLLGWSSQAQGLSVTVPDTPPPPSTNRDKGRKPTPATPPLRDTHPQAMTWNTSSFQSYLQNPKVRGLYFPAGGSTSSIVNPVPTTASTTSSSFSTTGVPVSTMDITSSGFLGPLLALQAVFFLLTKILTMPQSLDSLWTSLNFLGGTPACPGLNSQSPTSSHSPTCCPPTCPGYRWMCLRRSIIFLFILLLCLIFLLVLLDYQGMLPVCPLLPTVTGTTTTTGPCRTCTPIVPGISSYPSCCCTKPTDGNCTCIPIPSSWAFAKFLWDWALARFSWLNSLLPFVQWFAGLSPTVWLLVIWMMWFWGPSLFSILSPFLPLLPLFFWLWAYI
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The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein. {ECO:0000255|HAMAP-Rule:MF_04075}. The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid. {ECO:0000255|HAMAP-Rule:MF_04075}.
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O72157
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RDRP_SBMVA
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Replicase polyprotein P2AB [Cleaved into: N-terminal protein; Serine protease (EC 3.4.21.-); VPg; RNA-directed RNA polymerase (EC 2.7.7.48) (RdRp)]
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MYHPGRSPSFLITLANVICAAILFDIHTGGYQPGSLIPIVAWMTPFVTLLWLSASFATYLYKYVRTRLLPEEKVARVYYTAQSAPYFDPALGVMMQFAPSHGGASIEVQVNPSWISLLGGSLKINGDDASNESAVLGSFYSSVKPGDEPASLVAIKSGPQTIGFGCRTKIDGDDCLFTANHVWNNSMRPTALAKRGKQVAIEDWETPLSCDHKMLDFVVVRVPKHVWSKLGVKATQLVCPSDKDAVTCYGGSSSDNLLSGTGVCSKVDFSWKLTHSCPTAAGWSGTPIYSSRGVVGMHVGFEDIGKLNRGVNAFYVSNYLLRSQETLPPELSVIEIPFEDVETRSYEFIEVEIKGRGKAKLGKREFAWIPESGKYWADDDDDSLPPPPKVVDGKMVWSSAQETVAEPLNLPAGGRVKALAALSQLAGYDFKEGEAASTRGMPLRFVGQSACKFRELCRKDTPDEVLRATRVFPELSDFSWPERGSKAELHSLLLQAGKFNPTGIPRNLEGACQNLLERYPASKSCYCLRGEAWSFDAVYEEVCKKAQSAEINEKASPGVPLSRLASTNKDLLKRHLELVALCVTERLFLLSEAEDLLDESPVDLVRRGLCDPVRLFVKQEPHASRKVREGRFRLISSVSLVDQLVERMLFGPQNQLEIAEWEHIPSKPGMGLSLRQQAKSLFDDLRVKHSRCPAAEADISGFDWSVQDWELWADVEMRIVLGGFGHKLAKAAQNRFSCFMNSVFQLSDGTLIEQQLPGIMKSGSYCTSSTNSRIRCLMAELIGSPWCIAMGDDSVEGWVDGAKDKYMRLGHTCKDYKPCATTISGRLYEVEFCSHVIREDRCWLASWPKTLFKYLSEGKWFFEDLERDVSSSPHWPRIRHYVVGNTPSPHKTNLQNQSPRYGEEVDKTTVNQGYSEHSGSPGHSIEEAQEPEAAPFCCEAASVYPGWGVHGPYCSGDYGSLT
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[Serine protease]: Responsible for cleavages of polyprotein P2A and replicase polyprotein P2AB. [VPg]: Covalently attached to the 5' extremity of the genomic and subgenomic RNAs. It may serve as a primer for the replicase. [RNA-directed RNA polymerase]: Replicates the viral genome.
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O73556
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POLG_HPE2W
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Genome polyprotein [Cleaved into: Capsid protein VP0 (P1AB) (Virion protein 0); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protein 2A H-NC (P2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); 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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METIKSIADMATGVTKTIDATINSVNEIITNTDNASGGDILTKVADDASNILGPNCYATTSEPENKDVVQATTTVNTTNLTQHPSAPTLPFTPDFSNVDTFHSMAYDTTTGSKNPNKLVRLTTHAWASTLQRGHQIDHVNLPVDFWDEQRKPAYGHAKYFAAVRCGFHFQVQVNVNQGTAGSALVVYEPKPVVDYDKDLEFGAFTNLPHVLMNLAETTQADLCIPYVADTNYVKTDSSDLGQLKVYVWTPLSIPSGSSNQVDVTILGSLLQLDFQNPRVYGQNVDIYDTAPSKPIPLRKTKYLTMSTKYKWTRNKVDIAEGPGSMNMANVLSTTAAQSVALVGERAFYDPRTAGSKSRFDDLVKISQLFSVMADSTTPSANHGIDQKGYFKWSANSDPQAIVHRNLVHLNLFPNLKVFENSYSYFRGSLIIRLSVYASTFNRGRLNGFFPNSSTDETSEIDNAIYTICDIGSDNSFEITIPYSFSTWMRKTHGKPIGLFQIEVLNRLTYNYSSPNEVYCIVQGKMGQDAKFFCPTGSLVTFQNSWGSQMDLTDPLCIEDSVEDCKQTITPTELGLTSAQDDGPLGNDKPNYFLNFKSMNVDIFTVSHTKVDNIFGRAWFAHVHDFTNDGLWRQGLEFPKEGHGALSLLFAYFTGELNIHVLFLSDRGFLRVGHTYDTETNRTNFLSSSGIITVPAGEQMTLSVPSYSNKPLRTVRSSNALGYLLCKPLLTGTSSGRIEIFLSLRCPNFFFPLPAPKPATRKYRGDLATWSDQSPYGRQGKKQLMKLAYLDRGFYKHYGIVVGDDVYQLDSDDIFKTALTGKAKFTKTRLTPDWVVEEECELDYFRIKYLESSVNSEHIFSVDNNCETIAKDIFGSHSLSQHQQIGLIGTILLTAGLMSTIKTPVNPTTIKEFFNHAIEGDEQGLSLLVQKCTTFFSSAATELLDNDLVKFIIKILVRILCYMVLYCHKPNILTTACLSTLLVMDVTSSSVLSPSCKALMQCLMDGDVKKLAEVVAESMSNTDDDEIKEQICDTVKYTKQILSNQGPFKGFNEISTAFRHIDWWIQTLLKIKDMVLSVFKPSVEKRAVEWLERNKEHVCSILDYASDIIVKSKDQTKMKTQEFYQRYNDCLSKFKPIMAMCFRSCHNSISNTVYRLFQELARIPNRMATQNDLIRVEPIGIWIQGEPGQGKSFLTHTLSKQLQKTCGLQGIYTNPTASEFMDGYDNQDIHLIDDLGQTRKERDIEMLCNCISSDPDIVPMAHLEEKGKFYTSKLVIATTNKPDFSSTVLLDSGALRRRFPYIMHIRAAKHYSKSGKLNVSQAMPHMSTGECWEVSKNGRDWETLKLKELIDKITVDYKERIANYNTWKKQLEDQTLDDLDDAVSYIKHNYPDAIPYIDEYLNIEMSTLIEQMEAFIEPKPSVFKCFASRVGDKIKEASREVVKWFSDKLKSMLNFVERNKAWLTVVSAVTSAIGILLLVTKIFKKEESKDERAYNPTLPVAKPKGTFPVSQREFKNEAPYDGQLEHIISQMAYITGSTTGHITHCAGYQHDEIILHGHSIKYLEQEEELTLHYKNKVFPIEQPSVTQVTLGGKPMDLAIVKCKLPFRFKKNSKYYTNKIGTESMLIWMTEQGIITKEVQRVHHSGGIKTREGTESTKTISYTVKSCKGMCGGLLISKVEGNFKILGMHIAGNGEMGVAIPFNFLKNDMSDQGIVTEVTPIQPMYINTKSQIHKSPVYGAVEVKMGPAVLSKSDTRLEEPVDCLVKKSASKYRVNKFQVNNELWQGVKACVKSKFREIFGVNGIVDMKTAILGTSHVNSMDLSTSAGYSFVKSGYKKKDLICLEPFSVSPMLEKLVQEKFHNLLKGNQITTIFNTCLKDELRKLDKIATGKTRCIEACEIDYCIVYRMIMMEIYDKIYQTPCYYSGLAVGINPYRDWHFMINALNDYNYEMDYSQYDGSLSSMLLWEAVQVLAYCHDSPDLVMQLHKPVIDSDHVVFNERWLIHGGMPSGSPCTTVLNSLCNLMMCIYTTNLISPGIDCLPIVYGDDVILSLDKEIEPERLQSIMAESFGAEVTGSRKDEPPSLKPRMEVEFLKRKPGYFPESTFIVGKLDTENMIQHLMWMKNFSTFKQQLQSYLMELCLHGKDTYQHYVKILNPYLKEWNIPVDDYEVVIGKLVPMVFD
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[Capsid protein VP0]: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP1 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid proteins interact with host alpha-V/beta-3 integrin heterodimer to provide virion attachment target cell (By similarity). This attachment induces virion internalization predominantly through clathrin-mediated endocytosis (By similarity). Binds packaging signals present in the viral RNA (By similarity). [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP0 and VP1 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid proteins interact with host alpha-V/beta-3 integrin heterodimer to provide virion attachment target cell (By similarity). This attachment induces virion internalization predominantly through clathrin-mediated endocytosis (By similarity). Binds packaging signals present in the viral RNA (By similarity). [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP0 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid proteins interact with host alpha-V/beta-3 integrin heterodimer to provide virion attachment target cell (By similarity). This attachment induces virion internalization predominantly through clathrin-mediated endocytosis (By similarity). Binds packaging signals present in the viral RNA (By similarity). [Protein 2B]: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication. [Protein 2C]: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. [Protein 3A]: Localizes the viral replication complex to the surface of membranous vesicles (By similarity). It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction (By similarity). This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity). Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (By similarity). [Viral protein genome-linked]: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2. During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions. [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). 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 (By similarity). [RNA-directed RNA polymerase 3D-POL]: Replicates the viral genomic RNA on the surface of intracellular membranes. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated.
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O73557
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Z_LASSJ
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RING finger protein Z (Protein Z) (Zinc-binding protein)
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MGNKQAKAPESKDSPRASLIPDATHLGPQFCKSCWFENKGLVECNNHYLCLNCLTLLLSVSNRCPICKMPLPTKLRPSAAPTAPPTGAADSIRPPPYSP
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Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087, ECO:0000269|PubMed:12970458, ECO:0000269|PubMed:14990716}.
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O73673
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GCR_PAROL
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Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
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MDQGGLKRNCNRDDSLTFGETAVGVGSDTGDTAGSLLQPAAMHLPSPSSLPQLTVAPNGGAGTKDQGEFGGLFESPRGQCEGSEMKEGKIIRLQKRKHHLDIGMFNMEDNLSLLNQNISDLNRTSTSVISTSDTSVLGKLPLPNLFPQHIKQEGGFSLEKELGTYGGHTGGGPCDLDGNSGHLIEDTEIWQDLDLPNSLPEISDFELDSEVAHLDNILHDSSGGCGPDGSLLKETKVLVGNGGNCTDVNGTDQQHPLQHHQHQQQQHRHLLQHQQHQLHHQHQQPPSLLSSVMIKEEKDHDNSFIHIRTPGVVKQEKQENGSFCQSQCLQSSMSSLHGGGPMSSTMGAGAVPGYHYKASPSSTVGLQDQKPFGIFSNLPAVAESWTRGGRFGEPSGIQRGNDGLPSAAMSPFSVSFSSSSPRTGENSSSAVPGLSKPSGPTHKICLVCSDEASGCHYGVVTCGSCKVFFKRAVEGWRARQNTDGQHNYLCAGRNDCIIDKIRRKNCPACRFRKCLQAGMNLEARKNKKLIKMKVHRPTGSAEPISNMPVPVIPRMPQLVPTMLSVLKAIEPEIIYSGYDSTLPDTSTRLMTTLNRLGGQQVISAVKWAKSLPGFRNLHLDDQMTLLQCSWLFLMSFSLGWRSYEQCNGNMLCFAPDLVINKERMKLPFMTDQCEQMLKICNEFVRLQVSYDEYLCMKVLLLLSTVPKDGLKSQAVFDEIRMTYIKELGKAIVKREENASQNWQRFYQLTKLLDSMQEMVEGLLQICFYTFVNKTLSVEFPEMLAEIITNQIPKFKDGSVKPLLFHQK
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Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling. Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth. Mediates glucocorticoid-induced apoptosis. Promotes accurate chromosome segregation during mitosis. May act as a tumor suppressor. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression.
|
O73682
|
VGFAA_DANRE
|
Vascular endothelial growth factor A-A (VEGF-A-A)
|
MNLVVYLIQLFLAALLHLSAVKAAHIPKEGGKSKNDVIPFMDVYKKSACKTRELLVDIIQEYPDEIEHTYIPSCVVLMRCAGCCNDEALECVPTETRNVTMEVLRVKQRVSQHNFQLSFTEHTKCECRPKAEVKAKKENHCEPCSERRKRLYVQDPLTCKCSCKFTQMQCKSRQLELNERTCRCEKPR
|
Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis, and induces permeabilization of blood vessels. Acts both upstream of kdr and tie1 to stimulate endothelial cell differentiation, and upstream of gata1 to stimulate hematopoietic cell differentiation.
|
O73689
|
ZIC1_XENLA
|
Zinc finger protein ZIC 1 (XZic1) (XlZic1) (ODD-paired-like) (Xopl) (ZIC-related protein 1) (ZIC-r1) (Zinc finger protein of the cerebellum 1)
|
MLLDAGAQYPAIGVTTFGSSRHHSAGDVTDREVALGINPFADGMGAFKLNPSSHDLASGQTAFTSQAPGYAAAALGHHHHPGHVSSYSSAAFNSTRDFLFRNRGFGEAASAQHSLFASAAGGFPGPHGPHADTTGHLIFPGLHEQAASHASPNVVNGQMRLGFSGDMYGRPDQYGQVTSPRSEHYASSQLHGYGPMNMNMAAHHGAGAFFRYMRQPIKQELICKWIEPEQLANPKKSCNKTFSTMHELVTHVTVEHVGGPEQSNHICVWEECPREGKPFKAKYKLINHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFKCEFEGCDRRFANSSDRKKHMHVHTSDKPYLCKMCDKSYTHPSSLRKHMKVHEASSQGSQPSPAASSGYESSTPPTIVSPSAENQSTSSLSPSSSAVHHTSNHSTLSSNFNEWYV
|
Transcriptional activator that induces expression of multiple genes including pax3, en2, snai2/slug, feb and a subset of wnt genes. Has multiple key roles in the regulation of neural induction and neurogenesis: acts as a neural competence factor, sensitizing the presumptive neuroectoderm to respond to subsequent neuralizing signals. Promotes both preplacodal cell fates and neural crest cell fates, two of the cell populations that arise from the neural plate border. Cooperates with pax3 in concert with wnt signaling to determine neural crest fate. Synergizes with the bmp-inhibitor noggin/nog and acts through the wnt pathway to induce expression of en2. May bind to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3'.
|
O73700
|
CAC1D_CHICK
|
Voltage-dependent L-type calcium channel subunit alpha-1D (CHCACHA1D) (Voltage-gated calcium channel subunit alpha Cav1.3)
|
MQHHQQQQPEQHPEEANYASSTRIPLPGDGPTTQSNSSAPSKQTVLSWQAAIDAARQAKAAQNMNTTTAQPVGSLSQRKRQQYAKSKKQGNTSNSRPPRALFCLSLNNPIRRACISLVEWKPFDIFILLSIFANCVALAVYIPFPEDDSNSTNHNLEKVEYAFLIIFTVETFLKIIAYGLLLHPNAYVRNGWNLLDFVIVVVGLFSVILEQLTKETEGGSHSGGKPGGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFIGKMHKSCFLIDSDILVEEDPAPCAFSGNGRQCVMNGTECKGGWVGPNGGITNFDNFAFAMLTVFQCITMEGWTDVLYWVNDAIGCEWPWIYFVSLIILGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENDEEADEEGKRNRVTLADLMEEKKKSRLSCFGRSSNKHASMPTSETESVNTENVSGEGENPACCGSLCQTISKSKFSRRWRRWNRFNRRKCRAAVKSVTFYWLVIVLVFLNTLTISSEHYNQPDWLTQIQDIANKVLLALFTCEMLVKMYSLGLQAYFVSLFNRFDCFVVCGGIVETILVELEIMSPLGISVFRCVRLLRIFKVTRHWASLSNLVASLLNSMKSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDETQTKRSTFDNFPQALLTVFQILTGEDWNAVMYDGIMAYGGPSSSGMIVCIYFIILFICGNYILLNVFLAIAVDNLADAESLNTAQKEEAEEKERKKNARKESLENKKSEKSEGDQKKPKDSKVTIAEYGEGEDEDKDPYPPCDVPVGEDEEDEEDEPEVPAGPRPRRISELNMKEKITPIPEGSAFFIFSSTNPIRVGCHRLINHHIFTNLILVFIMLSSVSLAAEDPIRSHSFRNNILGYADYVFTSMFTFEIILKMTAFGAFLHKGSFCRNYFNLLDLLVVGVSLVSFGIQSSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIMIVTTLLQFMFACIGVQLFKGKFYKCTDEAKQNPEECRGIYIVYKDGDVDNPMVKERVWQNSDFNFDNVLSAMMALFTVSTFEGWPALLYKAIDSNGENVGPVYNYRVEISIFFIIYIIIIAFFMMNIFVGFVIVTFQEQGEQEYKNCELDKNQRQCVEYALKARPLRRYIPKNPYQYKFWYVVNSTGFEYIMFVLIMLNTLCLAMQHYGQSKLFNDAMDIMNMVFTGVFTVEMVLKLIAFKPKIFVRKKERWLGYFSDAWNTFDSLIVIGSIVDVVLSEADPKPTETVTTDESGNSEDSARISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIAMLFFIYAVIGMQVFGKVAMRDNNQINRNNNFQTFPQAVLLLFRCATGEAWQEIMLACLPGKRCDPESDYNPGEEYTCGSNFAIIYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWSEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVAMNMPLNSDGTVMFNATLFALVRTALKIKTEGNLEQANEELRAVIKKIWKKTSMKLLDQVVPPAGDDEVTVGKFYATFLIQDYFRKFKKRKEQGLVGKYPAKNTTIALQAGLRTLHDIGPEIRRAISCDLQDDEPEENNPDEEEEVYKRNGALFGNHINHISSDRRDSFQQINTTHRPLHVQRPSIPSASDTEKNIYPHTGNSVYHNHHNHNSVGKQVPNSTNANLNNANVSKVVHGKHANFGSHEHRSENGYHSYSRADHEKRRRPSSRRTRYYETYIRSDSGDGRRPTICREERDIRDYCNDDHYLGEQEYYSGEEYYEEDSMLSGNRHVYDYHCRHHCHDSDFERPKGYHHPHGFFEEDDSQTCYDTKRSPRRRLLPPTPASNRRSSFNFECLRRQSSQDDIPLSPNFHHRTALPLHLMQQQVMAVAGLDSSKAHKHSPSRSTRSWATPPATPPNRDHTPYYTPLIQVDRAESTEHMNGSLPSLHRSSWYTDDPDISYRTFTPANLTVPNDFRHKHSDKQRSADSLVEAVLISEGLGRYAKDPKFVSATKHEIADACDMTIDEMESAASNLLNGNISNGTNGDMFPILSRQDYELQDFGPGYSDEEPEPGRYEEDLADEMICITSL
|
The isoform alpha-1D gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group.
|
O73707
|
CAC1C_CHICK
|
Voltage-dependent L-type calcium channel subunit alpha-1C (CHCACHA1C) (Voltage-gated calcium channel subunit alpha Cav1.2)
|
ALIVVGSIVDIAITEVNNAEENSRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQVFGKIALNDTTEINRNNNFQTFPQAVLLLFRCATGEAWQEIMLACLPDKKCDPDSEPANSTEADHSCGSSFAVFYFISFYMLCAFLIIDLFVAVI
|
Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm. Plays an important role in excitation-contraction coupling in the heart. Required for normal heart development and normal regulation of heart rhythm (By similarity). Required for normal contraction of smooth muscle cells in blood vessels and in the intestine. Essential for normal blood pressure regulation via its role in the contraction of arterial smooth muscle cells (By similarity). Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group (By similarity).
|
O73754
|
GREM1_XENLA
|
Gremlin-1 (Cysteine knot superfamily 1, BMP antagonist 1)
|
MNCLVYALGSLFLLSGLLLPSSEGKKKVSGSQGAIPPPDKGQPNDSEQGQAQPGDRVRGKGKGQALAAEEVLESSQEALHVTERKYLKRDWCKTQPLKQTIHEDGCNSRTIINRFCYGQCNSFYIPRHIRREEGSFQSCSFCKPKKFTTMVVTLNCPELQPPTKKKRITRVKQCRCISIDLD
|
Cytokine that has an axial patterning activity. Acts like BMP antagonist in embryonic explants. Blocks the BMP2 activity.
|
O73755
|
GREM1_CHICK
|
Gremlin-1
|
MVRTLYAIGAVFLLTGFLLPTAEGRKRNRGSQGAIPPPDKDQPNDSEQMQTQQQSGSRHRERGKGTSMPAEEVLESSQEALHITERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHVRKEEGSFQSCSFCKPKKFTTMTVTLNCPELQPPRKKKRITRVKECRCISIDLD
|
Cytokine that may play a role in the development of the medial pallium and during optic nerve and pecten development by modulating BMP signaling.
|
O73790
|
SPB10_CHICK
|
Heterochromatin-associated protein MENT (Myeloid and erythroid nuclear termination stage-specific protein) (Serpin B10)
|
MEQVSASIGNFTVDLFNKLNETNRDKNIFFSPWSISSALALTYLAAKGSTAREMAEVLHFTEAVRAESSSVARPSRGRPKRRRMDPEHEQAENIHSGFKELLTAFNKPRNNYSLRSANRIYVEKTYALLPTYLQLSKKYYKAEPQKVNFKTAPEQSRKEINTWVEKQTESKIKNLLSSDDVKATTRLILVNAIYFKAEWEVKFQAEKTSIQPFRLSKNKSKPVKMMYMRDTFPVLIMEKMNFKMIELPYVKRELSMFILLPDDIKDGTTGLEQLERELTYERLSEWADSKMMTETLVDLHLPKFSLEDRIDLRDTLRNMGMTTAFTTNADFRGMTDKKDLAISKVIHQSFVAVDEKGTEAAAATAVIISFTTSVINHVLKFKVDHPFHFFIRHNKSKTILFFGRFCCPVE
|
DNA-binding protein that promotes DNA condensation into transcriptionally inactive heterochromatin in terminally differentiated avian blood cells. Promotes tight packing of nucleosomes into spherical clusters by binding to linker DNA and subsequent oligomerization. Acts as a cysteine protease inhibitor towards CTSL (cathepsin L1) and CTSV (cathepsin L2), but does not inhibit serine proteases.
|
O73791
|
TIE2_DANRE
|
Tyrosine-protein kinase receptor Tie-2 (EC 2.7.10.1) (Tyrosine kinase with Ig and EGF homology domains-2)
|
MCLLDSCTALLLLGCWMSGSAVRISDVTLVNPDPVVSPLTAPSLLCVSSDWSSGGSVLALGQEFPRPQGSVLALGQEFPHTEPRPHPAAATVTWSSRSHAFGAFYCQIRNSTGRKIYTYKMLQEAAFLPESLTITVNQGENINISYSRRLYSPEDTVIHKNGHFEHSSPKEDISDIIHYPVTNAKAESHAGIYAIRYISAAPSSAAITRLIVRSCRAGFWGPNCTESCPRCANGGVCDDTTGECVCPPGFRGHTCDIVCGEGRFGAGCKERCVDGVCRALVFCLRDPYGCSCASGWRGLSCNDACPDGYYGAGCTQKCVCAKGRCDRFRGCVCAGRHGSRCEEADSSPVISHLRDVEINTGVELSVNCSASGRPAPLHGDITLITANRTTIAAVDTHTLNDQSTSVFRVQQVRVSSAGRWRCQVNNTHMQVEDEFTVEVKVPPRPQNPPVLQGSGPRHLLLLLNTEPYSGDGPIATTTLLYRPASAHTWSSVTAHGPLVRLDNLYPMTQYLTQVQLSRPGPGGAGQAGPAATFSTQVLELPVGVKLSAVSQTALLLSWDIAPAEQHCTYEVSCLQAGAPGTLRTFQLPSNSSAMHLSDLKPRHKYQCTVRSSCGVGQNHPSASAWTLSDQLPPPPANISIWNISDTSAVLTWAVAEGESVSRAVIRFQQVEQAQYRQQVELPVQTQQLHMRFQLLGLRPNTGYQLQLWTVNNMGESAESPPVSLMTLPQQESSALFAAHGHLLLYAILGSAGMTCCTVLLAFCIVLQLKRNTLQRRIHSILREEPAVHFSSAPPPHRRSAVVSRSLVFPALQWSDIQFQDVLGEGNFGQVLKARIRKDGLRMDAAVKRMKDYASQDDHRDFAGELEVLCRLGPHKNIIHLLGACEHRGYLYLAIEFAPHGNLLDFLRKSRVLETDPAFAIAHRTASTLSSQQLLAFSADVARGMSYLSQKQFIHRDLAARNVLVGENFVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEVVSLGGTPYCGMTCAELYEKLPLGFRLEKPLNCDDEVYELMQQCWREKPFERPSFSQILLSLGRMLEERKTYVNTTLYEKFTYAGIDCSAEEAG
|
Tyrosine-protein kinase that acts as cell-surface receptor for angiopoietins and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Can activate or inhibit angiogenesis, depending on the context. Angiopoietin signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors (By similarity).
|
O73798
|
IGF1R_XENLA
|
Insulin-like growth factor 1 receptor (xIGF-1R) (xIGFR) (EC 2.7.10.1) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
|
MKAELVPVCTAWILGLLLCLGPAAAKVCGPNMDIRNDVSELKQLRDCVVIEGYLQILLISNAKAEDFRNLRFPNLTVITDYLLLFRVSGLVSLSNLFPNLTVIRGRVLFYNYALVIFEMTDLKEIGLYNLRNITRGAVRIEKNSELCYVSTVDWSLVLDAVYNNYIVGNKPPKECVDLCPGAREKMQICEKSSINNEFADRCWSDEHCQKVCPSVCGKRACSDNNECCHPECLGSCTAPDNDTACVACHHYFYEGRCVPTCPSNTYKFEGWRCITREVCAKMHIWIHSTIPFIIHKGECVYECPSGYMLNKSQSMTCSPCEGPCPKICEEKMKTIDSVTSAQMLEGCTVLKGNLQLNIRKGQNIAAELENFLGLIETVTGYVKIRHSHALVSLSFLKSLRYILGEEQMPGNYSFYVFDNNNLQQLWDWSKHNLTIKEGKIRFAFNSKLCASEIYRMEEVTGTKGRQAEEDISLSTNGNMASCESHVLNFTSRSKIKNRIKLTWERYRPPDYRDLISFTVYYKEAPFRNVTEYDGQDACGSNSWNMVDVDLPASKESDPGILLQGLKPWTQYAIYVKAITLTMLENRHIHGAKSKIIYMRTDAAVPSIPQDMISASNSSSQLVVKWNPPSLPNGNLSYYIVRWQQQPQDRHLYQYNYCFKDKVPNRKYANGTIDTEGGTEPTKPEGSVGEKGHYCACPKTEAEEKAEKDEAEYRKVFENFLHNSIFVPRPNRRRRDVLAVGNSTVTSYEKNSTTEDFSNFSDSERDDIEYPFYETKVDYKWERTVISNLQPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAAGADDIPGIVNTKEEDDGVIFLGWPEPLRPNGLILMYEIEYKHQGEVHRECVSRQDYRKNGGIKLVRLPPGNYSAQVQAISLYGNGSWTEMVSFCVKLKPDVRNNILQMVVAIPLALSFLLVGIISIVCFVFKKRNSNRLGNGVLYASVNPEYFSAAEMYVPDKWEVPREKITMNRELGQGSFGMVYEGIAKGVVKDEAETKVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPDTESNSGQPTPSLKKMIQMAGEIADGMSYLNANKFVHRDLAARNCMVTEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTNSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEGGLLEKPDNCPDMLFELMRMCWQFNPKMRPSFLEIISSIKDELDPGFKEVSFFYSEENKPPDTEELDLEAENMESIPLDPSCALQNSEHHAGHKSENGPGVVVLRASFDERQPYAHMNGGRKNERALPLPQSSAC
|
This receptor binds insulin-like growth factor 1 (IGF1) with a high affinity and IGF2 with a lower affinity. It has a tyrosine-protein kinase activity, which is necessary for the activation of the IGF1-stimulated downstream signaling cascade. Plays a role in oocyte maturation. Promotes head development by inhibiting Wnt signaling during embryogenesis.
|
O73864
|
WNT11_DANRE
|
Protein Wnt-11
|
MTEYRNFLLLFITSLSVIYPCTGISWLGLTINGSSVGWNQTHHCKLLDGLVPDQQQLCKRNLELMHSIVRAARLTKSACTSSFSDMRWNWSSIESAPHFTPDLAKGTREAAFVVSLAAAVVSHAIARACASGDLPSCSCAAMPSEQAAPDFRWGGCGDNLRYYGLQMGSAFSDAPMRNRRSGPQDFRLMQLHNNAVGRQVLMDSLEMKCKCHGVSGSCSVKTCWKGLQDISTISADLKSKYLSATKVIPRQIGTRRQLVPREMEVRPVGENELVYLVSSPDYCTQNAKQGSLGTTDRQCNKTASGSESCGLMCCGRGYNAYTEVLVERCQCKYHWCCYVSCKTCKRTVERYVSK
|
Ligand for members of the frizzled family of seven transmembrane receptors. May play a role in the formation of dermal structure in limb buds. Is likely to signal over only few cell diameters (By similarity).
|
O73872
|
SODC_DANRE
|
Superoxide dismutase [Cu-Zn] (EC 1.15.1.1)
|
MVNKAVCVLKGTGEVTGTVYFNQEGEKKPVKVTGEITGLTPGKHGFHVHAFGDNTNGCISAGPHFNPHDKTHGGPTDSVRHVGDLGNVTADASGVAKIEIEDAMLTLSGQHSIIGRTMVIHEKEDDLGKGGNEESLKTGNAGGRLACGVIGITQ
|
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
|
O73874
|
EFNB2_DANRE
|
Ephrin-B2a
|
MGDSLWRYYFGVLVIACKVNLSRALILDSIYWNTTNTKFVPGQGLVLYPQIGDKMDIVCPRVEGGSMEGVEYYKLYMVPLEQLKSCQVTKADTPLLNCVKPDQDVKFTLKFQEFSPNLWGLEFFRGKDYYIISTSNGTMEGLDNQEGGVCKTKSMKIIMKVGQNPSDPISPKDYPTSYPPKHPDLGGKDSKSNEVLKPDASPHGEDKGDGNKSSSVIGSEVALFACIASASVIVIIIIIMLVFLLLKYRRRHRKHSPQHATTLSLSTLATPKRGGSGGNNNGSEPSDIIIPLRTADSVFCPHYEKVSGDYGHPVYIVQEMPPQSPANIYYKV
|
Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with ephb4 may play a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration (By similarity).
|
O73875
|
EPB4A_DANRE
|
Ephrin type-B receptor 4a (EC 2.7.10.1) (Eph receptor B4a) (Eph-like receptor tyrosine kinase rtk5)
|
MELFSRNVAAFWIILLEFLLGSVAEEEVLMNTKTETSDLKWTTHSRSKPEWEEVSGLDEENNSVRTYQICQADGSSSHWLRSKLIERRGASQVYVELFFTMVECSSRNTHHRSCKETFNLYYYQSDTDDATATHPAWMENPYTKVDTVAADFLLRKGGEKKVNVKTLRLGPLSKRGFYLAFQAQGACMALLSVRVFFKKCPALTRSLSVFPETVPRSLVQEAVGQCVANAAQPGPSPRPPKMFCGEDGQWVDQPTTTCTCLPGFEASHGELECRACPVGLFKMGSGTGPCSVCPENSQTGETGSAACVCRSGFYRALSDSADTPCTRPPSSPRSPVPQVNDTSLTLEWSEPLDSGGRSDLSYSVECRMCSTPGSPCTLCSDGVNYRPSQTGIQGRRVSIWGLRPHTTYSFTVMALNGVSAQSQQGPAGETINITTSPNVPVLVSGLRKSTATESSLTLYWNTPTQSHYRILQYQIRYCEKERGSEENSCHYMESNNNEVVLSDLRRATQYEVQVRARTFAGYGSFGKAILFRTLPDEDDSSSPLLVTGILIAMGMLLLIIVIGAAIYCIRKQNNYKDPELSDKNGQYLMGQGVKVYIDPFTYEDPNEAVREFAKEIDVSCVKIEEVIGAGEFGEVCRGRLRIPGKKENYVAIKTLKGGYTDKQRRDFLAEASIMGQFQHPNIIHLEGIITASCPVMILTEFMENGALDSFLRLNDGQFTPIQLVGMLRGIASGMKYLSEMSYVHRDLAARNILVNSNLVCKVSDFGLSRFLQENSSDPTYTSSLGGKIPIRWTAPEAIAFRKFTCASDVWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPPDCPTYLHQLMLDCWQKERTARPRFANIVSALDKLIRNPASLKITAQEGAGPSHPLLDQRSPLTPSSCGTVGDWLRAIKMERYEETFLQAGYTSMQLVTHINTEDLLRLGITLAGHQKKILSSIEALGIQNKAPGNVLY
|
Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with its cognate ligand/functional ligand EFNB2 is involved in the regulation of cell adhesion and cell migration, and plays a central role in heart morphogenesis, angiogenesis and blood vessel remodeling and permeability. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells (By similarity). Involved in somitogenesis.
|
O73878
|
EPB4B_DANRE
|
Ephrin type-B receptor 4b (EC 2.7.10.1) (Eph receptor B4b) (Eph-like receptor tyrosine kinase rtk8)
|
MDRVCWIMALSWFWMVSTGLVSAEEEVLMNTKLETSDLRWTIYPSGDPEWEEMSGLDEEGNSVRTFQVCPMDSSVSHWLRTRFIPRHGASQVYVEIRFTMMECSAMPASFRTCKETFNLYYYQSDEDTASATHPAWMENPYSKVDTVAADFLLRRGGERKSNVKTVRVGPLSKKGFYLAFQTQGACMALLSVRVFFKKCPAVSRAFSSFPETLPHSLVQQAEGVCVDNSAPTGQSTAPPTMFCGEDGQWVGPPSSTCACKPGYEPVDSDRCRACGLGQYKASVGGSLCRVCPDNSNTHFAGSSLCVCRPGYHRATSDLPDSACTKPPSAPRSIIYQINDTVVTLEWSEPLDRGGRSDLSYSVECMHCRGSLCVQCADSITYRPGQMGVPGRRVIIRGLLPHTTYTFTVLAQNGVSAVSHTSPASSSVNITTSRDVAVPVSGIRRIKASESSVSISWTVPPQTQHSIQDYQLRYSLKGQDDGWQYVSSRSSSVVLNDLSRASQYQVQVRARTAAGYGHFSSAVSISTLPDDEESPSRLMLTGVLVAIGLLILIAVVIVAVFCFRRSTRRRDPDPDKSGQFLMGQGIKVYIDPFTYEDPNEAVREFAKEIDVSFVKIEEVIGAGEFGEVCRGRLKVPGKKENYVAIKTLKGGYTDKQRRDFLSEASIMGQFQHPNIIHLEGVITASCPVMILTEYMENGALDSFLRLNDGQFTPIQLVGMLRGIASGMKYLSEMSFVHRDLAARNILVNSNLVCKVSDFGLSRFLTENSSDPTYTSSLGGKIPIRWTAPEAIAFRKFTSASDVWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPPECPASLHQLMLDCWQKERSSRPRFCAIVSALDRLIRNPASLKITGRIPDGPSHPLLDQRAPPPLSHCSSVADWLRAIKMERYEDAFMQAGFTAIQHITHISTEDLLRIGVTLAGHQKKILSSVQTLRIHGGSLRY
|
Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with its cognate ligand/functional ligand EFNB2 is involved in the regulation of cell adhesion and cell migration, and plays a central role in heart morphogenesis, angiogenesis and blood vessel remodeling and permeability. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells (By similarity). Involved in somitogenesis.
|
O73885
|
HSP7C_CHICK
|
Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8)
|
MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDSVVQSDMKHWPFTVVNDAGRPKVQVEYKGETKSFYPEEISSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQGTKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNLLIFDLGGGTFDVSILTIENGIFEVKSTAGDTHLGGEDFDNRLVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEKLNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLDSYAFNMKATVEDEKLPGKILDEDHQNILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD
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Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes (By similarity). Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (By similarity). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (By similarity). The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state (By similarity). In the ATP-bound form, it has a low affinity for substrate proteins (By similarity). However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins (By similarity). HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (By similarity). Substrate recognition component in chaperone-mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2 (By similarity). KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded (By similarity). May play a role in regulating apoptosis during embryonic development.
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O73888
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HPGDS_CHICK
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Hematopoietic prostaglandin D synthase (H-PGDS) (EC 5.3.99.2) (GST class-sigma) (Glutathione S-transferase) (EC 2.5.1.18) (Glutathione-dependent PGD synthase) (Glutathione-requiring prostaglandin D synthase) (Prostaglandin-H2 D-isomerase)
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MPNYKLTYFNLRGRAEICRYLFAYAGIKYEDHRLEGADWPKIKPTIPFGKVPILEVDGVIIHQSLAIARYLARESGLAGQTPVEQALADAIVDTIDDFMMLFPWAEKNQDVKEKAFNDILTNKAPELLKDLDTFLGDKKWFVGKSVTWADFYWDVCSTTLLSYKADLADKYPRLLALRDRVEALPAIAAWIQKRPKTAI
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Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides, organic isothiocyanates and alpha,beta-unsaturated carbonyls. Also exhibits low glutathione-peroxidase activity towards cumene hydroperoxide and t-butyl hydroperoxide.
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O73916
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SIX3_ORYLA
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Homeobox protein SIX3 (Sine oculis homeobox homolog 3)
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MVFRAPLDFISASRLLLPHFADAPPVLSRSRSPEHPPAGFLSLALPGLCFSATQIASVCETLEETGDIERLARFLWSLPVNTDGRDSISEHESVQRARAVVAFHTGCYRELYRILETHRFTRASHSKLQAMWLEAHYREAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRGLLREWYLQDPYPNPGKKRELAHATGLTPTQVGNWFKNRRQRDRAAAAKNRLQHHRICPDSACTLSGGDSSERADGDTFLSVTDSDSDLDV
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Transcriptional regulator which can act as both a transcriptional repressor and activator by binding a ATTA homeodomain core recognition sequence on these target genes. During forebrain development represses WNT1 expression allowing zona limitans intrathalamica formation and thereby ensuring proper anterio-posterior patterning of the diencephalon and formation of the rostral diencephalon. Acts as a direct upstream activator of SHH expression in the rostral diencephalon ventral midline and that in turn SHH maintains its expression. In addition, Six3 activity is required for the formation of the telencephalon. During postnatal stages of brain development is necessary for ependymal cell maturation by promoting the maturation of radial glia into ependymal cells through regulation of neuroblast proliferation and migration. Acts on the proliferation and differentiation of neural progenitor cells through activating transcription of CCND1 and CCND2. During early lens formation plays a role in lens induction and specification by activating directly PAX6 in the presumptive lens ectoderm. In turn PAX6 activates SIX3 resulting in activation of PDGFRA and CCND1 promoting cell proliferation. Also is required for the neuroretina development by directly suppressing WNT8B expression in the anterior neural plate territory. Its action during retina development and lens morphogenesis is AES and TLE4-dependent manner. Furthermore, during eye development regulates several genes expression. Before and during early lens development represses the CRYGF promoter by binding a SIX repressor element. Directly activates RHO transcription, or cooperates with CRX or NRL. Six3 functions also in the formation of the proximodistal axis of the optic cup, and promotes the formation of optic vesicles-like structures. During pituitary development, acts in parallel or alternatively with HESX1 to control cell proliferation through Wnt/beta-catenin pathway. Plays a role in eye development by suppressing WNT1 expression and in dorsal-ventral patterning by repressing BMP signaling pathway.
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O73925
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KCNQ1_SQUAC
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Potassium voltage-gated channel subfamily KQT member 1 (IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1) (KQT-like 1) (Voltage-gated potassium channel subunit Kv7.1)
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MSSEVKSRWSGSGSQKSGTARKPTMLEMAENAASRHYEPVPLPLQRSNSPDSSTDKNPESRAADSRAEVIINPDIPPKAIALPLSRYRGRNPFFSKVNIQGRTYNFLERPTGWKCFIYHFTVFLIVLVCLIFSVMSTIEQYHYFANRALVWMEIVLVVFFGTEYIVRLWSAGCRSKYVGFWGRLRFARKPISIIDLIVVVASVIVLCVGSNGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVDDSGSQQFGSYADALWWGVVTVTTIGYGDKVPQTWIGRTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTSWRCHAAENHESATWKMYVRQPTKFYVASPSPKTKKSVGKRKKLKTDKDNGLNSEKSLNVPNITYDHVVDKDDRKFENSNIDGYDSSVKKSLGILDVNSGALSRANSYADDLDFIEGEPVLAPITHVSQLRESHRVTVKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSLGKPTMFLSVSEKSQDRGKNTIGARLNRVEEKFVHMDQKLNTITDMLHHLVAHQQGHPHPQTQPQAQGTVVQAVASTHSSLPSYEQLTVRRKDQDNQPDL
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Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity). Associates with KCNE beta subunits that modulates current kinetics (By similarity). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity). Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity). When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (By similarity). When associated with KCNE2, forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity). When associated with KCNE4, inhibits voltage-gated potassium channel activity (By similarity). When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (By similarity).
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O73932
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IF23A_XENLA
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Insulin-like growth factor 2 mRNA-binding protein 3-A (IGF2 mRNA-binding protein 3-A) (IMP-3-A) (69 kDa RNA-binding protein A) (IGF-II mRNA-binding protein 3-A) (KH domain-containing transcription factor B3-A) (RNA-binding protein Vera-A) (Trans-acting factor B3-A) (VICKZ family member 3-A) (VLE-binding protein A) (Vg1 RNA-binding protein A) (Vg1 RBP-A) (Vg1 localization element binding protein A) (VgLE-binding and ER association protein A)
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MNKLYIGNLSENVSPTDLESLFKESKIPFTGQFLVKSGYAFVDCPDETWAMKAIDTLSGKVELHGKVIEVEHSVPKRQRSRKLQIRNIPPHLQWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYANKEHARQGLEKLNGYQLENYSLKVTYIPDEMATPQAPSQQLQQQPQQQHPQGRRGFGQRGPARQGSPGAAARPKPQTEVPLRMLVPTQFVGAIIGKEGATIRNITKQTQSKIDIHRKENAGAAEKPITIHSTPEGCSAACKIIMEIMQKEAQDTKFTEEIPLKILAHNNFVGRLIGKEGRNLKKIEQDTDTKITISPLQDLTLYNPERTITVKGSIEPCAKAEEEIMKKIRESYENDIAAMNLQAHLIPGLNLNALGLFPSSSSGMPPPSVGVPSPTSSTSYPPFGQQPESETVHLFIPALAVGAIIGKQGQHIKQLSRFAGASIKIAPAEGPDAKLRMVIITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIKVPSYAAGRVIGKGGKTVNELQNLTSAEVVVPRDQTPDENDEVVVKITGHFYASQLAQRKIQEILAQVRRQQQQQQKTVQSGQPQPRRK
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RNA-binding protein that acts as a regulator of mRNA transport and localization. Binds to the RNA sequence motif 5'-UUCAC-3'. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (By similarity). Mediates the specific association of Vg1 RNA to microtubules. Binds specifically to the vegetal localization elements (VLE or VgLE) in the 3'-UTR of Vg1 and VegT mRNAs. Binds to the Vg1 and VegT mRNAs in both the nucleus and the cytoplasm. May regulate mRNA translation (By similarity). Acts as a transcription regulator (By similarity). Binds to the 5'-[TA]GGTTACT-3' motif within element 3 of the TFIIIA gene promoter (By similarity).
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O73946
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HELS_PYRFU
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ATP-dependent DNA helicase Hel308 (EC 3.6.4.12) (ATP-dependent Holliday junction unwindase Hjm) (Holliday junction migration DNA helicase)
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MRVDELRVDERIKSTLKERGIESFYPPQAEALKSGILEGKNALISIPTASGKTLIAEIAMVHRILTQGGKAVYIVPLKALAEEKFQEFQDWEKIGLRVAMATGDYDSKDEWLGKYDIIIATAEKFDSLLRHGSSWIKDVKILVADEIHLIGSRDRGATLEVILAHMLGKAQIIGLSATIGNPEELAEWLNAELIVSDWRPVKLRRGVFYQGFVTWEDGSIDRFSSWEELVYDAIRKKKGALIFVNMRRKAERVALELSKKVKSLLTKPEIRALNELADSLEENPTNEKLAKAIRGGVAFHHAGLGRDERVLVEENFRKGIIKAVVATPTLSAGINTPAFRVIIRDIWRYSDFGMERIPIIEVHQMLGRAGRPKYDEVGEGIIVSTSDDPREVMNHYIFGKPEKLFSQLSNESNLRSQVLALIATFGYSTVEEILKFISNTFYAYQRKDTYSLEEKIRNILYFLLENEFIEISLEDKIRPLSLGIRTAKLYIDPYTAKMFKDKMEEVVKDPNPIGIFHLISLTPDITPFNYSKREFERLEEEYYEFKDRLYFDDPYISGYDPYLERKFFRAFKTALVLLAWINEVPEGEIVEKYSVEPGDIYRIVETAEWLVYSLKEIAKVLGAYEIVDYLETLRVRVKYGIREELIPLMQLPLVGRRRARALYNSGFRSIEDISQARPEELLKIEGIGVKTVEAIFKFLGKNVKISEKPRKSTLDYFLKS
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DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. Unwinds the lagging strand from forked DNA structures in a 3'-5' direction. PCNA, the DNA polymerase sliding clamp subunit, stimulates the helicase activity, and may alter substrate specificity. Unwinds branched DNA (Holliday junctions) in an ATP-dependent fashion ss- and dsDNA stimulate ATPase to the greatest extent, although it preferentially binds DNA with a single-stranded region. Processes a RecA-mediated recombination intermediate between gapped circular and homologous linear dsDNA. {ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:15677450, ECO:0000269|PubMed:16436047}.
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O74113
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CDC45_SCHPO
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Cell division control protein 45 homolog (Suppressor of nda4 protein)
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MFIKRSDYASAYLKIKEASVSGGCTVQLFVALDPDALCACKLLSTLLKGDFISHKIRPVSGYRDLEQANKTLLEQNEDIKFIILLNCGTMVDLNNYLVSMEDVSIYVIDSHRPHNLNNIYIENNIFVFDDGDIEEDMNKIHDAWYAFNSHELSDEENSDSSNEREEEVEDDNRSVESYSSSDYQARSRRRFSEETTQRRAEIKEKRKKRKEFASILSEYYEKGSWYGESITNILFAVASMLGREDNDMLWLAIVGLTCLEIHCQSSKKYFNRSYSLLKDEVNRLNPSPLENQIVGRAHGKTPHDQSIRLEDEFRFMLVRHWSLYDSMLHSAYVGSRLHIWSEEGRKRLHKLLAKMGLSLVECKQTYIHMNMDLKKTLKSSLKRFAPFYGLDDVIFHSFTRTYGFKCTLSASDVSYAISALLEMGNTGVLLQSKTVARSPDMTEEEYLEKFENAQNQEWLHNFYDAYDALDDVDSLERALKLAMHLQRAIVRTGITLLEKRAIKTLRSFRFGLINEGPDLKIFMHPLALTKMSLWIAEAINEQEREFGKLRHLPLVLAAFVEEKNRYLIVGTSTSAFTSNEDDDDDDGHGHNRFGVAFQEVANMTSATLQMDCFEASVIECQKSDLGVFLESLSFKTLL
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Required for initiation of chromosomal DNA replication. May have a role in regulating the MCM proteins nda1 and nda4.
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O74135
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CKI3_SCHPO
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Casein kinase I homolog 3 (EC 2.7.11.1)
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MSTTSSHSNVVGVHYRVGKKIGEGSFGMLFQGVNLINNQPIALKFESRKSEVPQLRDEYLTYKLLMGLPGIPSVYYYGQEGMYNLLVMDLLGPSLEDLFDYCGRRFSPKTVAMIAKQMITRIQSVHERHFIYRDIKPDNFLIGFPGSKTENVIYAVDFGMAKQYRDPKTHVHRPYNEHKSLSGTARYMSINTHLGREQSRRDDLESMGHVFMYFLRGSLPWQGLKAATNKQKYEKIGEKKQVTPLKELCEGYPKEFLQYMIYARNLGYEEAPDYDYLRSLFDSLLLRINETDDGKYDWTLLNNGKGWQYSAAKQHVVQRRHTQGTNNRRQSTIPPYARTRQNLLSSPSKQTPVNNVVDASVATQKDGIPGKAASPQVQQQQQTSSAQQQQPQRVEQPAPQTTQPTQVDTQQAAKPAPSKEKSRKKFHLRLLSCCISKQE
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Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
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O74184
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WAT1_SCHPO
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Target of rapamycin complex subunit wat1 (TORC subunit wat1) (WD repeat-containing protein pop3)
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MSVQYPPQHSVLLVSSGYDHTIRFWEALSGICSRTIQHADSQVNRLCISPDKKFLAAAGNPHVRLYDINTSSQMPLMTFEGHTNNVTAIAFHCDGKWLATSSEDGTVKVWDMRAPSVQRNYDHKSPVNDLLIHPNQGELLSCDQSGRVRAWDLGENSCTHELIPEEDVPMSSITVGSDGSMLIAGNNKGNCYVWRMLNHQGASLLQPVVKFQAHQRYITRCVLSPDVKHLATCSADATVNIWSTEDMSFMLERRLQGHQRWVWDCAFSADSTYLVTASSDHVARLWELSSGETIRQYSGHHKAAVCVALNDYQI
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component of both TORC1 and TORC2, which regulate multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls cell growth and ribosome biogenesis by regulating ribosomal protein gene expression. TORC1 negatively controls G1 cell-cycle arrest, sexual development and amino acid uptake. Represses mating, meiosis and sporulation efficiency by interfering with the functions of the transcription factor ste11 and the meiosis-promoting RNA-binding protein mei2. TORC2 is required for cell survival under various stress conditions. TORC2 positively controls G1 cell-cycle arrest, sexual development and amino acid uptake. Positively regulates amino acid uptake through the control of expression of amino acid permeases. May play a role in mRNA maturation as a coupling protein between splicing and synthesis and/or stabilization.
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O74189
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PMT1_CANAL
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Dolichyl-phosphate-mannose--protein mannosyltransferase 1 (Protein mannosyltransferase 1) (EC 2.4.1.109)
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MAKKPVTPASKVAAKQAAVRSRHQEDVFTLDPLIDPIFQKGELRSYLVTEPSPSVLKKRSIHTKEYWMLSSLLLIAFYVRMYNLSNPNSVVFDEVHFGGFARKYILGTFFMDVHPPLAKMLFGAVGAIGGFKGDFEFKSIGDKFPDSTPYIFMRQFPALLGVGTVILCYLTLRQSGVRPIIAYITTFLLIIENSNVTISRYILLDSPLIFFIAAAIYAWKKFEIQIPFTFGWYRSLLATGIALGLALSSKWVGLFTVAWVGFLCIYQLWFLIGDLSVSTKKIWGHFFARGIILLGVPIALYLGFFAIHFQLLNKEGDGGAFMSSAFRAGLQGNKIPRDITEQVGLGSVVTIRHVDTQGGYLHSHEHFYQTGSKQQQITLYPHLDSNNKWLIEPYNGTIHNETFVPLINGMKIRLKHINTGRRLHSHDEKPPVSERDWQKECSCYGYDGFAGDANDDWVVEIVNYRSQKGEAQTFVKAINTIFRLRHAMTGHYLFSSEVKLPEWGFGQQEVTSASQGKRALTHWYIETNENSILPPSEAKIINYPKLSLWQKVVESHKRMWKINQGLTSHHHWQSSPSEWPLLLRGINYWNKEHKQVYLLGNAVTWWAATLSIITFGTYVLVTVFRWHLGTPLSTNKHVFNFNVQTFSYVLGWALHYLPFFIMGRQLFLHHYLPALYFGILALGHFFEIFTGYLTSRSKYFQQVAFVLVGLFSILSLVFYVNYSSLIYGTPWTKASCELTKPFSGWDYNCGTFFDTLGEYDIQEKSLASESEIPTETVVVEAKQTPKAEPKLAKQDDHIESPAAAEPVEEKEVKEEVEQLAPPLAVDFEEETPKVEDPQVADVDASSNDEKSVEEKQQQEQQQEQEQVEDESVHQVQQ
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Protein mannosyltransferase (PMT) involved in hyphal growth and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of target proteins. Accounts for the O-glycosylation of the cell wall proteins KRE9, PIR2, RHD3, and ALS1, as well as the SEC20 t-SNARE component. O-glycosylation of SEC20 is essential for its stability. Required for filamentation and early phases of biofilm formation.
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O74201
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UBC2_CANAL
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Ubiquitin-conjugating enzyme E2 2 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 2) (Radiation sensitivity protein 6) (Ubiquitin carrier protein UBC2) (Ubiquitin-protein ligase UBC2)
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MSTPARRRLMRDFKRMQQDPPSGVSASPLPDNVMKWNAVIIGPSDTPFEDGTFRLLLSFDEQYPNKPPQVKFISEMFHPNVYASGELCLDILQNRWSPTYDVSSILTSVQSLLNDPNISSPANVEAANLYKDHRSLYVKRVRETVENSWNDDDDEEEEEEDEDEAEDEDDDDDDNIDED
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Catalyzes the covalent attachment of ubiquitin to other proteins. Plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. Also involved in postreplication repair of UV-damaged DNA, in N-end rule-dependent protein degradation and in sporulation. {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:10712706}.
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O74208
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PDH1_CANGA
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Pleiotropic ABC efflux transporter of multiple drugs PDH1 (P leiomorphic drug resistance homolog 1) (Pleiotropic drug resistance protein 2)
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MNTPDDSSVSSVDSHQPYMGFDDNVEKRIRELARSLTQQSLTSSNRSVNKEAPADGSAPLDRVSTRASSIFSADFKGVNPVFSDEEEDDYDARLDPNSDEFSSKAWVQNMAKITTGDPEFYKPYSIGCCWKDLSASGESADVSYQSTFLNLPVKLLNAVWRKARPARESDTFRILKPMDGLLKPGELLVVLGRPGSGCTTLLKSISSTTHGFQISKDSVISYNGLTPNEIKKHYRGEVVYNAEADIHLPHLTVYQTLVTVARLKTPQNRVKGVTREDFANHVTDVAMATYGLSHTRDTKVGNDLVRGVSGGERKRVSIAEVWICGSKFQCWDNATRGLDSATALEFVRALKTQAHIAKNVATVAIYQCSQDAYNLFNKVSVLYEGYQIYFGDAQHAKVYFQKMGYFCPKRQTIPDFLTSITSPAERRINKEYLDKGIKVPQTPLDMVEYWHNSEEYKQLREEIDETLAHQSEDDKEEIKEAHIAKQSKRARPSSPYVVSYMMQVKYILIRNFWRIKNSASVTLFQVFGNSAMAFILGSMFYKIQKGSSADTFYFRGAAMFFAILFNAFSSLLEIFSLYEARPITEKHRTYSLYHPSADAFASVISEIPPKIVTAILFNIIFYFLVNFRRDAGRFFFYFLINVIAVFAMSHLFRCVGSLTKTLQEAMVPASMLLLALSMYTGFAIPRTKMLGWSKWIWYINPLAYLFESLMVNEFHDRRFPCNTYIPRGGAYNDVTGTERVCASVGARPGNDYVLGDDFLKESYDYENKHKWRGFGVGMAYVIFFFFVYLILCEFNEGAKQKGEMLVFPHSVVKRMKKEGKIRDKTKMHTDKNDIENNSESITSNATNEKNMLQDTYDENADSESITSGSRGGSPQVGLSKSEAIFHWQNLCYDVPIKTEVRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERTTMGVITGDVMVNGRPRDTSFSRSIGYCQQQDLHLKTATVRESLRFSAYLRQPSSVSIEEKNEYVEAVIKILEMETYADAVVGVPGEGLNVEQRKRLTIGVELAAKPKLLVFLDEPTSGLDSQTAWATCQLMKKLANHGQAILCTIHQPSAMLMQEFDRLLFLQKGGQTVYFGDLGKGCKTMIKYFEDHGAHKCPPDANPAEWMLEVVGAAPGSHANQDYHEVWRNSEQFKQVKQELEQMEKELSQKELDNDEDANKEFATSLWYQFQLVCVRLFQQYWRTPDYLWSKYILTIFNQLFIGFTFFKADHTLQGLQNQMLSIFMYTVIFNPLLQQYLPTFVQQRDLYEARERPSRTFSWKAFILAQIVVEVPWNIVAGTLAYCIYYYSVGFYANASQAHQLHERGALFWLFSIAFYVYVGSLGLFVISFNEVAETAAHIGSLMFTMALSFCGVMATPDAMPRFWIFMYRVSPLTYLIDALLSTGVANVDIRCSNTELVTFTPPQGLTCGQYMTPYLNVAGTGYLTDPSATDECHFCQFSYTNDFLATVSSKYYRRWRNYGIFICFIVFDYVAGIFLYWLARVPKTNGKIAKNGKTAKVNFIRRLIPF
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Pleiotropic ABC efflux transporter that confers resistance to structurally and functionally unrelated compounds including caspofungin or azoles such as fluconazole, itraconazole, posaconazole, voriconazole, and isavuconazole. Does not play a role in the azole resistance in mature biofilms.
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O74213
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PGLR1_ASPAC
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Endopolygalacturonase I (EC 3.2.1.15) (Pectinase 1) (Polygalacturonase I) (PG-I)
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MHLNTTLLVSLALGAASVLASPAPPAITAPPTAEEIAKRATTCTFSGSNGASSASKSKTSCSTIVLSNVAVPSGTTLDLTKLNDGTHVIFSGETTFGYKEWSGPLISVSGSDLTITGASGHSINGDGSRWWDGEGGNGGKTKPKFFAAHSLTNSVISGLKIVNSPVQVFSVAGSDYLTLKDITIDNSDGDDNGGHNTDAFDIGTSTYVTISGATVYNQDDCVAVNSGENIYFSGGYCSGGHGLSIGSVGGRSDNTVKNVTFVDSTIINSDNGVRIKTNIDTTGSVSDVTYKDITLTSIAKYGIVVQQNYGDTSSTPTTGVPITDFVLDNVHGSVVSSGTNILISCGSGSCSDWTWTDVSVSGGKTSSKCTNVPSGASC
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Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.
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O74237
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XYL1_CANTE
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NAD(P)H-dependent D-xylose reductase (XR) (EC 1.1.1.307)
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MSASIPDIKLSSGHLMPSIGFGCWKLANATAGEQVYQAIKAGYRLFDGAEDYGNEKEVGDGVKRAIDEGLVKREEIFLTSKLWNNYHDPKNVETALNKTLADLKVDYVDLFLIHFPIAFKFVPIEEKYPPGFYCGDGNNFVYEDVPILETWKALEKLVAAGKIKSIGVSNFPGALLLDLLRGATIKPAVLQVEHHPYLQQPKLIEFAQKAGVTITAYSSFGPQSFVEMNQGRALNTPTLFAHDTIKAIAAKYNKTPAEVLLRWAAQRGIAVIPKSNLPERLVQNRSFNTFDLTKEDFEEIAKLDIGLRFNDPWDWDNIPIFV
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Reduces D-xylose into xylitol. Has a preference for NADPH, but can also utilize NADH as cosubstrate.
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O74288
|
ABFB_EMENI
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Alpha-L-arabinofuranosidase B (ABF B) (Arabinosidase B) (EC 3.2.1.55)
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MTMSRSSRSSVLALALATGSLVAAGPCDIYSSGGTPCIAAHSTTRALYSSYNGPLYQVQRASDGTTTTITPLSAGGVADASAQDAFCENTTCLITIIYDQSGNGNDLTQAPPGGFNGPDVGGYDNLAGAIGAPVTLNGKKAYGVFVSPGTGYRNNEAIGTATGDEPEGMYAVLDGTHYNDGCCFDYGNAETSSLDTGNGHMEAIYYGTNTAWGYGAGNGPWIMADLENGLFSGQSSDYNAGDPSISYRFVTAILKGGPNLWALRGGNAASGSLSTYYNGIRPTDASGYNPMSKEGAIILGIGGDNSVSAQGTFYEGAMTDGYPDDATENSVQADIVAAKYATTSLISGPALTVGDTVSLKVTTSGYDTRYIAHTGSTINTQVVSSSSSSTLKQQASWTVRTGLASTAAANGCVSFESVDTPGSYIRHSNFALLLNANDGTKLFSEDATFCPQDSFNDDGTNSIRSWNYPTRYWRHYENVLYVASNGGVNTFDAATAFTDDVSWVVADGFA
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Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan.
|
O74304
|
WIN1_SCHPO
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MAP kinase kinase kinase win1 (EC 2.7.11.25)
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MENILDPSVVNSHILENGSRRSSINPILDSELRDKTFEKAHRRSLTLLSSFTSSMLELPNNGKEENHRRPSVARSSSDRSKASAKEDLFSEAFRMAEQPPAEALTISTPVDPINIDELDRAYAVSPSDTSNLLHPPTSSSSIPIPIKNAGHSNLDHPIRPSLQSSISSNRIIKSPGIKEDDYMHRGRSISSPMIDVEHINSTAVPSKTKNLPEKPKRSHKLRNSITFAKIEDHPERKSQLRRLSSSLKCFDPEYDYNDPSLSIRRDSSTYYFSNVNETYDEEDSDLDSETSTVNWVQSVLNLPSLLSDDLMANPKNKERFEWQYMLTSVLTGDIVRSEKLRLRKIASSREGRNSDYSDNLWMEIWCWLTHRSVDSYRENLKHLRTGMVDVLLAIMNFHWDESNELTPIVAVDNMLQKLDKYERLYPSRRSILQEHSLYASESFQHKLDVLTAYSNVTHALEIQVNIIRSWVGNEEMDITKNTTNSINNVSQISNGPFVERFYRETGLIRAFEQRIMTNMNSVLSKVCNTIVTYADDLKSYGLPLIADDYMRLLSFPFRLIKEFLNLRLSCAENITSISLFTIDSLLDDLRNTMKVAVHIIQQHTVLIKPFRDDSKFVDENQSLNNILVASLKFYFNLLHRKVRNGCALLHFKETEILEGEWDFLLAVCPHIEHGFQIMSKSLSSLVGEILTNINRYLKDQLQGPDTDDSALITSFYIKVLDCVRIRFRKLMSFTRILKAHLENSCEYVIKENSLSLLIQRLEESNHVLTYTASIEHEGAYVIVPGHLVDSPNILREVLSMTFNKGDNNFESVPPYAVVLAPDSSICWNGHVTDLDIPEVSISIAPNCVRLVTLATANQLSVIEDYFISIVGDTVSLVDSAKANSSKINKQMTKIKRNSLKLALSLLDVIQTIRTRYHGMNCQNLIHYSFSYAIEFAQRLMRLSILDASSIGLIRRKMIQLAISWVGFIYEDCSPTDRNTFRWTVTALEFAMIMTYGSNILMIDKKSFEELKEKVGKCVALLLLHFDVMGTKHAGRSMDQQAGDIPARLVRNNSDRSRLSDNELASFVKEEVMHRIIELESNRRDRLYKSQLIGRVLDDTTKENRLLKELASSKSNITIRWQQGGLIGSGSFGTVYRAVNLDTGDLMAVKEVALHKPRISRPMIKRIKGEMLVLELFDHPNVVSYYGIEVHREKVNIFMELCQGSSLFEFLRYGRIEDELVIQVYVLQLLEGLAYIHSCGVSHQDVKPENILFDHNGIMKFTDFGSAKMSGSASTKIFEQLTQQEEEEFEKDSEFLQHLDQNRGYSLTGTPTYMAPELILGNPSERVGAMDIWSLGCVIVEMATGSPPWPRLDNHFSLMYHIAAHNPPIIPADDQLSPLGQNFLKRCFVSDPNQRATAAELLMDPWVYPLRAGTEFDLMNSSVVESAPSTNGAPLEL
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Involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Activates the wis1 MAP kinase kinase by phosphorylation.
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O74309
|
SLM9_SCHPO
|
Histone transcription regulator slm9
|
MHIFVPKLLENHQFSSISSSKDFVAVSAETNVYILSKDFFYPKSSEKRIIQSLNGHKTTHLSFDSPISCIRFTYDGSCLAVATEAGTFLYHSEKWDKAFQVLSGPAYEVCWSQQGHILATSWKQISIYVKDEGLRTETIVKKTEHADSNHQPAVSIEESKEAVESTSQSSEISFKLIKVIEGHHTFVGGLAFDPMGQFLASQSFDHTLKVWKLSTFGVEKSIAKPFEQMPTGNRFLRLSWSPDGAHIASVNAVNEGAYVIAIVQRDTWTYDINLVGHQGPLECATFNPYLYEDPFQKSIIASAAHDGCVSIWNTACARPMAVIHELSCSSFVDLQWSTSGFELYGVSLDGNLMLLQFEESEFGEKMDTIHYPDDLSYFNSSRSKAHVNKNAAADRTTSPTQGQPESPSKSILLRPPPSIASSPESKRRKCPKKFVARPPVPHPTSLYSQIRIGCPYLKPKLVISKSFGTLIVKNHNQLSLLKCTFSNLDGNDCSWFSYLPNAIVLANGTSVFWAVATEDSSIYIYSPAGRLLLPPVVVAATPCFLECCGDFLCCIVSTGLLYIWNIKNFEAIHSPVSTLPLFHSNFSVSKIARGPSIEQFFVTKQGHPVAIMSDGNAFAFIRDSSSWLRVSEGWWMIGSQYWGPLASESNEESPLGFLERCTDEEIIKAGRGRFLQRLVKALMLRQGYDNYEMLVSIRHLENRLMSSAKLDLEYDFRENLILYAKKIAEEGMKDKMDELCKELLGPLRIPHNGIDTVKVGNRLWSPTIAGNNKRNLLKDIIIHTAKYRDMQRITSQYSDLLRRSALL
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Probably required for replication-independent chromatin assembly (By similarity). Required for transcriptional silencing in the outer repeat (otr) centromeric repeats and the Tf2 long terminal repeat retrotransposons. May play an indirect role in the regulation of cdc2 and/or wee1 at the G2/M stage of mitosis. {ECO:0000250, ECO:0000269|PubMed:10835386, ECO:0000269|PubMed:15121850, ECO:0000269|PubMed:16428807}.
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O74312
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ATG9_SCHPO
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Autophagy-related protein 9
|
MFYQPAQNKKQYDDLADIEAQNNVPNTQEVLEAWQESLDSDEDESSPLEESNGFTISEHDDFVKSVPRKNNPTDLLYSGKLLDSDEPPSVHGNSSKVPSKHPSPSFPETTSLRNLQNGSKQKPALPNFNDPHFYNEDVTRSGHPNRSIYTQLPRNEFSNARVLWNRLSARDRVLWRWANVENLDSFLQQVYTYYTGKGLSCIIVHRLFQILTVSFVIGFTTFITSCIDWPAVTPHGSLAGVTKSQCIAQMSPITYLVLWLFLSFLLALWIYYLTDIPRLWQMREFYIHALKIATADMPTVSWQRVLYRLLKLKNVNALTAEDGRVVSLHNMKRLDAYAIANRIMRKDNYFIALINNGIINIELPLLHRRILTHTTEWNINWCIFNFVFDEQGQLRSAFRNPNSRKRLSEELRRRFIVAGFLNCLFAPIVAIYLVIHNFFRYFNEYHKNPGALSTRRYTPLALWTFREYNELQHFFDERINDSYAAASHYVSQFPDFNMIRLFKYISFILGSFTAILVIITVFDPELMVTFEITKDRSVLFYLGLFGSLIAVSRSIIPDETLVFAPEKALRRVITFTHYMPGWWSDNMHSKAVQQEFCSLYSYRIVNLLWEILGILLTPVLLFFTFPSCSQDIVDFFREHTINVEGVGYVCSYAVFQDNPPYESVASLVQSRKISPLIQNKPELSRISFYEQFNTEAPRRDLR
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Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome (By similarity). Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through atg2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion (By similarity). Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (By similarity). Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking (By similarity). Has a role in meiosis and sporulation.
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O74327
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AVT5_SCHPO
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Vacuolar amino acid transporter 5
|
MSGYSPLSSGPADVHIGKAGFFSSVINLANTILGAGILSLPNAFTKTGLLFGCLTIVFSAFASFLGLYFVSQCAARLPRGKASFAAVAKHTFPSLAVVFDASIAVKCFGVAVSYLVIVGDLMPQIAPSLGLSSPMFLRRQTWIVFALFVLTPLSFLKRLDSLRHTSVISLIALCYLVFIVLYHFIIGDTVKGEIRYFVPESGFGYLSVLPVFVFGFTCHQNAFSVINEVRNFSQGFVNFTMFTAIISSTLLYLLVAITGYLSFGSLASGNIIAMYDNTSIWIIGGKLAIVVLVLFSYPLQCHPCRNSVYQAIRRSYSAHDMSDGYHAVITLCILLFTHSLALLLSSLEMVLAFVGSTGSTFISFILPGSLYYFFSHKVASPGNSSPLQLRISRAFAAGLAIYGTVVMILCLNINIAKLSH
|
Vacuolar amino acid transporter involved in the vacuolar uptake of histidine, glutamate, tyrosine, arginine, lysine, and serine. Required for sporulation.
|
O74338
|
BLT1_SCHPO
|
Mitosis inducer protein blt1
|
MSKSAFTSKSQLKGIDGSFNDPFRQPSMNLPTPPHDDGLPSIPRSTALPNLSNRLSPYSHRNYLPIPEADSRNLEVLNSISLTTGSVVNQINKLYQRSCDNANYLQDLRSLILQTPTAEANATQVTESLNQIQKILQEASSKDREQIVQVIKELNKGNSLEVRRELGNCLAHLKKGTLNIDNALQASLQKYWKELQYFNVSKDKLLSLEESIKLLSARLEETDTPSSTHWIEINAGFKEVGDELSENFQRKQEILSGLQNNVILRTNNRKPVGSDGSNSNFNGGEEQMDSKDQEEIQDYLNSLLSVHEKDGVLLQKFHNSYVQYQKLAVALSKYENFDADKLFQQMNLAKQSNETLLQTLTEQTDQLLSFKETMDSFKFILGPSMENQALQQGILAEQQDLVAQLRDIVLRSETLAENPSNMPGSCLPGASSNTADEFTEQLNLLKNEVARLSAICPSPNSGINASVLTNADNLEKENLLLVNNNAFKVDDRSVSSVALDDHNRQLQMNVEELEGKKADLTSKINRLDKDFVKLNTTYSLLTDQVKTKQLALQEIESRVIRLEERLNMLQKLSMQPAISSSSEFVPIESHPSSSAVVPIEEPKNSIIEKKRVPHNAARNSVNLEVTLPNSKKRFSSFSGSSSKLPVRPSTALTDKRKPSWSRRLAAAIGFSSGSPEKKHVITSSDAGHQRSKSRSFSSKM
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At the onset of mitosis, forms a medial ring structure before the arrangement of the medial actin ring. Essential for the central positioning of the division septum before the cell divides.
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O74352
|
HOB1_SCHPO
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Protein hob1 (Homolog of Bin1)
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MSWKGFTKALARTPQTLRSKFNVGEITKDPIYEDAGRRFKSLETEAKKLAEDAKKYTDAINGLLNHQIGFADACIEIYKPISGRASDPESYEQEGNAEGIEAAEAYKEIVYDLQKNLASEMDVINTRIVNPTGELLKIVKDVDKLLLKRDHKQLDYDRHRSSFKKLQEKKDKSLKDEKKLYEAETAFEQSSQEYEYYNEMLKEELPKLFALAQSFIAPLFQGFYYMQLNVYYVLYEKMSHCEIQYFDFNTDILESYERRRGDVKDRAEALTITKFKTAKPTYKRPGMGPGGKDATASSSSSFSSKREEAAAEPSSSTATDIPPPYSTPSVAGASDYSTPSAGYQTVQTTTTTTEAAAAQYPQAAFPPPPVMPQPAAAAVTTPVAAPVAAAAAAVPVPPPAPAPAAAPAAEHVVALYDYAAQAAGDLSFHAGDRIEVVSRTDNQNEWWIGRLNGAQGQFPGNYVQLE
|
Has a role in DNA damage signaling as a part of stress response processes.
|
O74354
|
DNT1_SCHPO
|
Nucleolar protein dnt1
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MRTTLRLHIIKDGEQDNQFMILFDPSSSISLLKEKVQETYKSLYPFESNINIRNIKNEESYDIPNEYLVGEIFPTNSKVIVESFSSPLKKLDGTMINFKEKNIQHDLDGVENDFATVQSASNGVHAINGKRTHPDESENPRKLPKKNFVEAIDANSPGFVYRPTSIRDRAYSISSNHDNESTLTEGIALKEIESPDKDRKADGIVNLSVTQEEDDNHQSFNSSLTPSQPTTYNRANFFSINDASSDSSSDAPLRTLSSPSRLRMKDNDRKYLVEHSPAALIKESETIDGIDDKSLRSSTREVSVESPNEDSVNDDSSSDVSDEKETEAKHEIRAPAIIVRETSSHPSTAVPSENDTTESENDTLSESSTTSISSSPSENSDTSDDLTKVDSPNKSLVNDNVSAKHDKESENGKSKFPPPSQTLVTTSTISAAGNEPSDEIGSENDSDSDSDSDSSVPLSQLQKKSQQRNSVSHEIQNRGTKGSPKEPKAKPSTERPETHRTLSYSRLSELSKTFSPEIREPSLTKKTAVSMQESKEEGRSDESSESEESGSSSDESDNSEKEDRSNPIPVEKRASTVLNTKKKRKAKRNSALAGLAALV
|
Negatively regulates the septation initiation network (SIN) pathway, independently of the cdc14 phosphatase clp1. May also have a role in silencing rDNA transcription. Required for maintaining the exclusive nucleolus localization of nuc1.
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O74360
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RGA4_SCHPO
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Probable Rho-type GTPase-activating protein 4
|
MNSGTTLHLDRLSLETPSERTCFCIKCWESVPSTSQVWFGGKCWHSDCFKCVNCNKKLDPSSEDFSQDDQKQIFCKLCVDICNGCSTPICEFNAVSNSQANHPCCSNCRAFINSNAFGKFKGQHYCLPCLRKQDEENQKAVMESASGFIPLRNIAQTAENTSLTGQNQGFQNPHFIASDSPSSVLSGRMQNTSSPTNSLRPQLKVQTNGYETPGDINSAKSYKDIQKDFLLKPKNSFVKTSPSPLANGPSFRSANASPFDSCDSFHSGSSIPIEPVSSRQSSVVNNNSVQQPVAYHAFVQSPTENGTLPQLPKNESVVNPPPLRRSSTMNYKSVSTTTSPSKYGYVSGRIALSPIHLRGALRDVTNKCNLKVPRNRNSLSNLDEYYVNGLESDETPTKARFPRYPTVFNKLDDKRLSSEPNGLKKRLTNSSNYEASPRAKSLNLSQVSLHQACEPEYNRSSLVRASDVFTSNVFDATEESANELAIRISELQAEVGTLLLEATSLASIIEQQTPVSPEAFKQELVADLNYRLDYLRKSFQPELSTLLLRRDALSTTVSKLQNAYSTVMEETAYLNVKNTELVSLNNQLERELAYLREQQHKKRTSSSFGIFNNDKKSNRTISTPSPRESFSRLQMVASSLGFRPKDNKDKESGGYNKRNSKIDLKKSFSKRFHWKRDSPHMSSTPSISEEHLASEEQEDFVPAVGHCKLCGKYSNELRAHYQDCVSSTIDRQYQSKKSESPVWALNPDDFDQNRLTLLRVPTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIVALLRNEDTVLDPSEDISAVTSVFKQYLRNLPNPIITYDQYFPFITAANCASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTLIRDPDNSRDVIDMTVKNYSLAFLIDHVHEVFA
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GTPase-activating protein for Rho-type proteins.
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O74365
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SOL1_SCHPO
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SWI/SNF chromatin-remodeling complex subunit sol1 (SWI/SNF complex subunit sol1) (Switch one-like protein) (Transcription regulatory protein sol1)
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MNNQGFVPASDYPTAVSYPTQGQSYNTQEEQPAYPQRFSTSQGMYAAEYGNANMMNTSENEPNNLAHSQPFRQSPSTQRNLPNQSFDFASNGAWNGSGSVKYSSPMMPSSRIPFQQEKEAAMQQQQQQQQQQQLYQRQMQSREALLSQQIPPNQIGINAHPAVRQTPQPAPSPNTPSGNANQLTPAYAASFDKFMVSLISFMEKRGTPIKSYPQINNTPINLMMLYALVMRAGGSRQVSAHNFWPKISASLGFPSPDAISLLIQYYNSYLLPYEEAWLAAQQQQKSLQQAKANHSANVQSRPKNYPQKPVQTTPEAVHANGSMHGSLHSKSPSPAFTANRFSPAAPTTVSSERNAPPYPSAPTRPTPPTVQTSSSAAPVDSAEPVAYQPIKKPIDPMLGYPLNVAATYRLDESLLRLQMPSIVDLGTVNIQALCMSLQSTLEKEITYAMNVLLILTNDQKWMFPLSECQDVVDALIDVATQCLDNLLSVLPNEDLMEIADKRPSYRQLLYNCCVEISQFSREDFSNSLSENKTKDSINAIDVHNSEQNLLAVFVIFRNLSHFEANQNVLVQNPDFFPLLIRVVKSLNFHATSLLRSSRNTLDLHKDVLIVLCQLSQNFILPNVDVARHVLLFILSFSPFNRKKSKTILNDTLPTSIPSYTPATHPYAGPAINAYAKLLAKDANNKTNFQAIFDNNPKFLDSLFLLLASVVPKFNRHCLKICERRLPLLQQSFFCLAATVSYVKQSEQAANWCNIGEGFFVSMLRLLILLSGHPSLNPPSRVASQYPTTNPFRYVIQSGISTVRRLLSLVEAGNISLSSFPKSETLLAVLLAPTTETSFLKEISNLLDRTGDSDASLENTDDKSGI
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Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
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O74369
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CSS1_SCHPO
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Inositol phosphosphingolipids phospholipase C (IPS phospholipase C) (IPS-PLC) (EC 3.1.4.-)
|
MSVEKAPELRVLSFNCWGLRFVSKYRTERLKAVGEKLAKCDYDIVLLQEVWSIYDFQEIRNLVSCNLVYSRFFHSAAMGAGLAMFSKFPIIESSMNKYPLNGRPQAFWRGDWYVGKGVATASLQHPSGRIISLFNTHLHAPYGKGADTYLCHRLSQAWYISKLLRAAVQRGHIVIAAGDFNIQPLSVPHEIITSYGLVNDAWLSVYPDQVEHPPNRFSMNDKELVEIAGTTCDSRLNTWRENISSKDMDDFVAKRLDYVFHSPSTCEAKNAKVVFLERVPKLDCSYSDHFAIETVLSIKLQPIPVQETRVSYSIIDDTLGITYQYMARERLHMRLRIAHLLISIPLIIGVHVAIAWCDPAWLKVIILFFTVMLTIAAVVNGFCIGLLFGRWEFNGLLEFVAELKEQKLLCKQYLVDHPLPFAKS
|
Inositol phosphosphingolipids phospholipase essential for the coordination of cell wall formation. Responsible for the hydrolysis of the phosphosphingolipids (IPS), inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide (MIPC), and mannosyldiinositol phosphorylceramide (M(IP)2C).
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O74384
|
ERFB_SCHPO
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Palmitoyltransferase erf2 (EC 2.3.1.225) (DHHC cysteine-rich domain-containing protein erf2) (Meiotically up-regulated gene 142 protein) (Ras protein acyltransferase)
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MSYEKHSDAKASRYAWNQPWNPFEVTLSDPTYPMNLEEKNQIPYRFQSVPDDVPEVPHIESRYKNLPGNNIYLCCGRLQMSSQYKAFLISLFALILPGVLFFIFSAFWLWHHVSPAVPITFAYLYALAVVSMFKCSTADPGILPRNAYSLTYNPAHPWSVIPEDRKVLVGSTRSDSVFVNTVYCHTCHLYRPPRASHCHLCDNCVEYLDHHCIWLNTCIGRRNYRYYFIFLLSVVLSALYLTGLGFYTSIGSFHESTDTNFAAHLRRPWAGVSFFLGIYGALGAILPGILFCYQCYLISVGQNVHEYLRAKSTETEDVHPFHDSIWLNFLVVLCRPKNVSYVRPTRKSYV
|
The erf2-erf4 complex is a palmitoyltransferase with a major role in driving sexual development. Palmitoylates ras1. Palmitoylates isp3. Palmitoylates rho3.
|
O74420
|
WTF13_SCHPO
|
Meiotic driver wtf13
|
MKNKDYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPYSEIWKYIKTVSEDSSTGPTEIANPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPIVFIAIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAISLAQCVKVTAVFLAKCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMERPGALKRMPKFIGNGIASFLGGLGNAFGGIGNAFGGIGNAIGRIGNAFRGANDNNDIPLGEMDVESEV
|
Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system where the poison and antidote proteins are produced from the same locus the poison component is trans-acting and targets all spores within an ascus whereas the antidote component is spore-specific, leading to poisoning of all progeny that do not inherit the allele. [Isoform 1]: Localizes isoform 2 to the vacuole thereby facilitating its degradation (By similarity). In addition to suppressing isoform 2, also suppresses S.pombe strain FY29033 wtf18 isoform 2.
|
O74421
|
COQ3_SCHPO
|
Ubiquinone biosynthesis O-methyltransferase, mitochondrial (3-demethylubiquinol 3-O-methyltransferase) (EC 2.1.1.64) (Polyprenyldihydroxybenzoate methyltransferase) (EC 2.1.1.114)
|
MNSMNILNKVKNVKSYTRLVRQGFLSQQRNHSVSVNEVDHFNELAKTWWDWDGGSRLLHLMNSTRLDFMTEVFRERNCFSGKKILDIGCGGGILSESMARLGASVTAVDASPMAIEVAKKHASLDPVLNGRLEYIHGSVEGSQLPTTFDVVTCMEVLEHVEQPRDFLFSLMEKVKPNGRLVLSTISRTLLARLLTITLAEHVLRIVPVGTHTFEKFIRADELSNFLKEQNWIINDIRGVCYNPLKQQWTLDKPGSSGLGLSCNYFLSAQKPMSA
|
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. {ECO:0000255|HAMAP-Rule:MF_03190}.
|
O74423
|
ENT1_SCHPO
|
Epsin-1
|
MKAAVRSVKNFSKGYTDTQIKVRNATTNDSWGPSGTAMAEIAELTYDQNEMLEVMDIIDRRLNDKGKNWRHVFKSLSLLEYCLHNGSENVVRWAKDNIYIITTLREFVYVDDNGHDQGQNVRTKAKEITSLLEDEHALKEARGDSRERDRDRDRTRSSRFDDDDDDRAPYEESRLSRAPSRASRYDDDDRDHRSRRRSRSRRPGRSRSRRRSRRPSPSAEHNSAEENDPELQRVIEESKRQAEEDAKRRNMANDSEAELQKAIQLSKEEDEARQRHQREREQQEQAFMGNQQNAYQPVDFFGNPVQPQPTGFLQQQPTGFIRPQNTGFVQPQYTGFVQPQHTGFVQPQATGFMQPQRTGFVQPQATGFVQPQATGFVQPQATGFMQPQRTGFVQPQATGFMQPQRTGFVQPQATGFMQPQRTGFVQPQATGFIQPQRTGFVQPQQNGFFNPQPTGYMQPQRTGMMQPQRTGFSQPFESNNPFPVMQPQRTGFGQTPNAPMMAPNHTGYVHPQPTGLQRQTTGYTGNNNPYSRPLQSQSTGILQQQQQQSAPRLEPTKTGSNNPFAQFSNLPSQSTAPATKPMKPVRTGDDRFSNIAQAISTGNPMGTDSFGNIGLTRVPTQHTGSKFTNSAGQTIQAQATGNTHNPFQSQQATGYYKQPMQQQQNMQQPYYNQQNYNYQNQQPMQGMQQQSMQPQVGSLIDL
|
Binds to membranes enriched in phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin.
|
O74429
|
VIP1_SCHPO
|
Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase (EC 2.7.4.24) (Cortical actin cytoskeleton protein asp1) (InsP6 and PP-IP5 kinase)
|
MIQNASHLTSIDTESSTRTASPVSSIVTPTKRNVVGICAMDAKARSKPCRNILNRIIAEGEFEAIVFGDNMILDEAVENWPACDYLICFYSSGFPLKKAEKYVELRKPFCVNDVVFQELLWDRRLVLNILDAIRVSTPQRLICSRDGGPKINKVLEEKLRRKFGIEITEVPTPEVKMLDEDTLSVDGKIIKKPYVEKPVYGEDHNIYIYFPKSVGGGGRKLFRKVANKSSDYDPDLCAPRTEGSFIYEEFMNVDNAEDVKVYTVGPHYSHAETRKSPVVDGIVRRNPHGKEIRFITNLSEEEKNMASKISIAFEQPVCGFDLLRVSGQSYVIDVNGWSFVKDNNDYYDNAARILKQMFHVAERHRRNRVPSVQEVLNPPPRESEAWRLKSLVGVLRHADRTPKQKFKFSFTSDPFVKLLQGHTEEVILRNEQLNSVLAATNLATELKCEDINKLKQLRLALETKKDLPGTKVQLKPAYSPEGKLLKLQLIIKWGGEFTHSARYQSKDLGEQFHKDLYIMNRDCLKDVEIYTSSERRVSASAEIFAMAFLEQETIPSDLLKVRKDLLDDSNAAKDTMDKVKKHLKSLLRVGDTARKEFTWPENMPKPCEVMQQVVQLMKYHRAVMRENFIILGPEVEQVQSRWCCNENPALFRERWEKLFSEFCDSEKADPSKVSELYDTLKYDALHNRQFLERIFTPYQYLKLPQSPSLIAKEPPQRTDSNGNLVGMTGANTNHTERPLEKLYELYDLAKVLFDFVSPQEYGIEPKEKLEIGLLTSVPLLRQIIHDIKEARDSDHASTRMYFTKESHIYTLLNCILESGLPMKLPRNQIPELDYLTQICFELFERTNPSGNKEFSVRITLSPGCYAQCPLDMNLDAKHCISVSPRRSLTRHLDLQQFITKTEDLCNSVHLPKRFIPVNIN
|
Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4 (By similarity). Required for maintaining cellular integrity, normal growth and interactions with the ARP complex. Acts as a regulator of the PHO80-PHO85 cyclin/cyclin-dependent kinase (CDK) complex, thereby regulating signaling of phosphate availability (By similarity). Required for the function of the cortical actin cytoskeleton, possibly by participating in correct F-actin localization and ensuring polarized growth. Regulates polarized growth and modulates interphase microtubule cytoskeleton. Regulates microtubule dynamics without the requirement of microtubule plus-end tracking protein Mal3. Required for growth zone selection.
|
O74435
|
CDC31_SCHPO
|
Cell division control protein 31
|
MFANARAKRRSRASSPTPARLGGYAPLRVEITEEQRQDINEAFKLFDSDKDNAIDYHELRAAMRALGFNAEKSEVLKILRDFDKTGKGYLQMEDFVRVMTEKIVERDPLEEIKRAFELFDDDETGKISLRNLRRVAKELNENIDDQELEAMIEEFDLDQDGEINEQEFIAIMMDEA
|
Required for the proper coordination between exit from mitosis and the initiation of septation. Has a role in bipolar spindle formation during spindle pole body (SPB) duplication. Required for the localization of sad1 to the SPB.
|
O74441
|
CTL1_SCHPO
|
Choline transporter-like protein ctl1
|
MFSDYASRFLAQSRFSSVDQRNFKYPTSRSNLQSVSIDRNSSIDSHETDLSAGSSSLHGLNSLIDSGSIHWQLREQEQSNSHISRNENELFSKENSIYNGNFSENLGVQPNPQTISHESVNEEYTELPYDAHLPSEQKVPDRKWGLTFGFLTLALFTYSFLMVWRTNPNIPPATSPYAAIQKAFPLFHKDAIICMMLSVIWLFCLVAIPRFLYFLLASVPLTMFAFAVYLLKASRIHLETSIQPKLMLLTGIILLVAPILLSYYVWRRRIHFETSFNIIRLACRVIADIPQITLIFISFLFSFYVLIFIWVRLFARLFLRGSTLVGSVWVLPRSSWVLASFYSLHFLWLCTFFHALQCAIISSIVSQWFFYRDTKSSATKTNLVSHFFYHVVSNQYGLCAFSSFLVVITKVPLHFLPTWLRHVSRIVYYMFSKTSASYVTSPLTLAYASIYSVPYMNASKALYQIEQLNRVGLRRRSYYFSKYTLLAARSLLAIGVGVTSWNYSIHENGVFYGYIVGLLGGFLAWLIIGAIEGGLSMIVDALLICSIIDISSCQGDPNGSHCFEAWQLFESNGY
|
Required for the normal organization of the preautophagosomal structure (PAS) and for the correct subcellular location of atg9.
|
O74465
|
HRR1_SCHPO
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Helicase required for RNAi-mediated heterochromatin assembly 1 (EC 3.6.4.13)
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MEQVQDEIWKLSTLDAWEMVNKNTEVVFDEIPEPETLSEMKRHPLYSNIFNADNNTTSFTEQIETSETSKTQDSEGNKVDKNLKENKSIRRKRSIDNDYELSNVKRNDITSGKNREFENEHHPASDTSSWRELPSIPTLEELTSKSVELPSNNIYGGYKSFEDYLSIHYRLLREDAVSPLRESVLRYKVNPNYITGSSLAVYDHVRIDGYTISSSVIAAKLSFSVRAKKKIKWATSRRLISGSLVLLSNDDFQTFRIGTVCARPLSGLNKHPHEIDVKFEDISISLDPREEYVMIEATSGYWEAYKHVLRSLQRLSASTFPMKDYLVHCKSNQETAKHIQNNPRIRINSILKNNSQKIVNALEPFGPGEYILDSSQLKAYQSMLTKRLSIIQGPPGTGKSFVTLKAIETLLENTHSHVLPILVACQTNHAVDQILIRLLHQGASVMRLGSRTKDPEIAAVTIFQKAKHTKHSFKAAYNEIRHKKQRLIKQITNIMHNFNLEFVTLSYLHSKGIITTSQLESLRNNTEWISSVAENGEKTEEELISIWLGDAKVELITPSEITDGFEEELQIDPEKLEEIQKEAEDSGALMEEELRGKFINLRCKYLFSKLTTLHEKEIDTLLTIPNIWDIPEYSRGIIYCRWLESAYAAAEKELNRLYRFYLKVDRERIGFSNKRAAILLRGANVIGMTTTGLNKYRDILERINPKICFIEEAADVLEGPIIPAVFPSLEQLVLIGDHKQLRPGCSTYALRQDPFNLSISMFERLVENDMEYTRLTMQRRMHPQIRRLVSSVYEDLSDYEITKYWPSIPGMGEIRRFFLTHSRIEDNDGFASKINLFEAQMLVQFAVYLINNGVEPQKITCLTFYAAQKDLIERLLSESLNREKHFIKVATVDGYQGEENDVVLLSLVRNNDRTEVGFLSSPHRVCVSLSRARRGLFIFGNAQLVAESNPLWWDAINTLMNDETIQGLGDHLPLFTKDGTIYVNDPVELLDVNMRLTRK
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Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-directed RNA polymerase complex (RDRC) which is involved in the generation of small interfering RNAs (siRNAs) and mediate their association with the RNA-induced transcriptional silencing (RITS) complex. RITS acts as a priming complex for dsRNA synthesis at the site of non-coding centromeric RNA.
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O74469
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YQC7_SCHPO
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Exosome complex protein C1739.07
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MDPEYSELFERLNKQLDNVEDVLKPLKDAESIFELAEGKSELEQAKLYITMSYAINSTLYSFYKLNGIDASERPVMQELQRVKNYISKIQQAEKNVNPKTEAVNTSNAAISSSSSNRPKVAKDAATRIIKHHT
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Required for exosome-dependent processing of pre-rRNA and small nucleolar RNA (snRNA) precursors. Involved in processing of 35S pre-rRNA at the A0, A1 and A2 sites (By similarity).
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O74473
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CDC11_SCHPO
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Septation initiation network scaffold protein cdc11 (SIN scaffold protein cdc11) (Cell division control protein 11)
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MEQLWLEHDLSEEWIPQPQEQGSDNSSEPPTTSNVNNTQSTGRGSSGTSTEHGTFKKGRNDAPDVPQWKQVNAKNPVARDIFARLDLENMFEESSKQSPPSKSPTKNPSKKSSNNSSRRSSSSVGKLSNVSNMQSSPSKDPFVSQDYEKESISSSQFSKKYSEGSLKSQQSNTRSNSVHEKQNTDHASNASSSSSVVSSPSLKPNNTSPLKLFQGASDPFTREHLNQLTQDVKSNSFENGEKQFSLPEPRRPQKPMRTTERKASLNTKDLYQEVEEVMARLRGRMPNSGRESTIFLPRKLSGLREEEEQDEISVEVSQEDSSNAFPSLSDQLHLKSLQSMKRVTSIFNDNDDSFPSASSSPQRQAYMTDKMPLREIDVGSSQSSSKTARLNSSPKSTLKTSSVKTRRSHSAQSSRKVSDYPNMVVITPADLPEGIDTTQGSMEFDRIHNRWRRKGHDSDLGFDFETDEDASLSHPERTILFKAASTRHQANNDPNNLEKQQPHSFPLRKQNVAQSEFPKHSLRDNSENAPQILSSFHDLSLQNESFDEMFNGRYENGSPIPFISSGSGLKSKADKDAEYSFSVSRQSIIQILSDVEPYEPFWKRIIQLDISRRHLDSLIGLSELCPSIEELTLEGNEIAYLTGCPVTIRDLNAVENRLSSLTSFSNLLNLQYLDISYNQLEDLTGLSSLIHLRELKVDSNHLWSLDGIQHLDGLLKLSACNNRIKELSFTNSNLHRLEELLLGNNEIEEIEEISSLQNLMVLQLDNNKLTNLKASQPMIHLRILRISNNAIHQLEVDQFPHLRTLYMDLNRFNRPPDIRRLKRLVNFSFRTQDPEASNFVIQPSLDIRNLYLSNNTFVTLDCKHMFLGVRYLELANVQLKEVPKYIATSMPNLRVLDLSHNYISDIESLKPLQMIHRLYLVGNRIKKMRNLCDILANLKQLNVLDLRMNPLNFNIYPVIDDSIYELSAASKYQQSINQKGHHRKEDPQKQWQEKELAFSSTLSEAWRTRRKMYAEAILLACPHLEWLDGSDVSQSSRAAFTKSSN
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Essential for the onset of septum formation. Involved in the organization of astral microtubules during mitosis. Acts as a bridge between sid4 and the other SIN proteins mediating their association with the spindle pole body (SPB). The sid4-cdc11 complex organizes a signaling hub on the SPB which coordinates cell and nuclear division.
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O74475
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FKS4_SCHPO
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1,3-beta-glucan synthase component bgs4 (EC 2.4.1.34) (1,3-beta-D-glucan-UDP glucosyltransferase)
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MSGNNENVSGITGHDAVSDDQYAYDSEVYDDQNAYQRQPADAYSNEEFLDQADYDSMYGEGYNGYDYPTGVTESYGDEYTPVDTASSGINQYSTEKGKFTRPSDEYESEYSDYNAQPSDANNFYNLRGDGRYNAYDPSSDSLANVYNSVPYGSSPYDFSNSSFVGNSGSGTPLDGDSGSFYADSANLTNREPYPAWTPENELPLTKEEIEDIFIDLTNKLGFQRDSMRNMYDFFMCLLDSRASRMTPDQALLTLHADYIGSDIANYKKWYFASQMDREDAVGLANVGIYGGKVTSIKEKGKFFSRNKKAPKVVKPPRKSRFKRKKKKEQPEEAEDEYIDVNTDDSLESAEYRWRSHMRSMTQFERAQQIALWLLLWGEANNVRFMPEVIAFLFKCAYDYIISPEAQNVTEPVPEGYYLDNIVSPLYQYMHDQQFEIINGKYVRRERPHDQLIGYDDINQLFWHAEGIARLIFEDGTRLIDIPASERFHRLPEVQWNRAFYKTYYESRSWFHLITNFNRIWVIHFGMFWYFTAFNSPTLYTKPFHQRDGPKPTGASQWAAVACTSVVSCIIMAAASLCEYLFVPRRFPGSKPIWKRLCIIVLIAIINLIPIVYIFGFSSKHQQRSGRRIAVGVVAFLMSIATYVYFSLVPLQSTFGKLSVKDSRKYLANKYFTSNFAPLKFDNQALSVIIWVCVFTCKFAESYFFLTLSIRDPIIVLSTMRPYLCSIYWAGSRLCFVQPRIILGIMYFTDLILFFLDTYLWYIIFNTIFSVLRSFVLGISILTPWRNIFSRMPQRIYGKILATNDMEIKYKPKILISQIWNAIVISMYREHLLSIDHVQRLLYHQVPAEEGRRTLRTPTFFVSQDDNIVHTTFFPANSEAERRLSFFAQSLATPIPEPVPVDNMPTFTVLIPHYAEKILLSLREIIREEDQLSRVTLLEYLKQLHPVEWDCFVKDTKILVEENAPYENDSVSEKEGTYKSKVDDLPFYCIGFKSAMPEYTLRTRIWASLRSQTLYRTISGFMNYSRAIKLLYRVENPEIVQMFGGNTDRLERELDRMARRKFKLVVSMQRYAKFTKEEYENAEFLLRAYPDLQIAYLDEDPPEEEGAEPQLFAALIDGHSEIMENERRRPKYRIRLSGNPILGDGKSDNQNMSLPFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEEMETDNVNPYSESARERNKHPVAILGAREYIFSENIGILGDVAAGKEQTFGTLFSRTLAQIGGKLHYGHPDFLNGIFMTTRGGVSKAQKGLHVNEDIYAGMNAMLRGGRIKHCEYFQCGKGRDLGFGSILNFNTKVGTGMGEQMLSREYYYLGTQLQLDRFLSFYFAHPGFHLNNMFIMLSVQLFMVVLINLGAIYHVVTVCYYNGNQKLSYDTSIVPRGCYQLGPVLSWLKRCVISIFIVFWISFIPLTVHELIERGVWRATKRFFKQIGSFSPLFEVFTCQVYSQAITSDLAYGGARYIGTGRGFATARLPFSILYSRFAVPSIYIGARFLMMLLFGTMTVWVAHLIYWWVSIMALCVAPFLFNPHQFDWNDFFVDYREFIRWLSRGNSRSHANSWIGYCRLTRTRITGYKRRVLGQPSDKISMDTPRAKFTNVFFSDVLIPALLAAGAIIPYFFINSQPGNPMFITDPNNPSPYVHDTKTGTNPILRLVIISLIPIAAGFGMSGFFGGMACCLGPAFGLCCKKFPSIFAAIAHTIQIFIFIAIFEVCWFLDGWSLPKTVLAFCAVTAIHRFIFKILTLLCLSREVKQDSANISWWSGKWYGKGYGYHAFTLPAREFVCKAIELNLFATDFFLGHLLLFFMLPVICIPYIDRWHSVLLFWLRPSRQIRPPIFSTKQNRLRKRIVRRYSALYFSILVIFLILIIVPLAAGAEIRQGLTASEAVAKGAVGWNQTNSSIGSGIIQPRDTNYTANYSFWYDRYHFEFNTTY
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Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS) complex. Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall (By similarity). Required for maintaining cell integrity during cytokinesis and polarized growth.
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O74476
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IMB3_SCHPO
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Importin subunit beta-3 (Importin beta sal3)
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MSSGFPPEVLSPLLNLVQGLSSPDNTVRNDAEKSLSSDWISQRADLLLNGLAILAYQSEDPAVRSFCLVLCRRISFRTLPGDSELEVFSSISNESKQSLQSQLLACFVKESVPTVRNKLCDTIAEIARSIYDCQGEWPELINVIFNAVNSPDESFRESVFRTITSLPRLLSGQDSAVTPLFTTGLADPSIRVRISAARAYSAVILESKQSTRDQVIPLLPSLMNILPPLQQDRDSDNLADCLMAITEIAEVFPKLFKPIFESVIAFGLGIIKDKELDNSARQAALELLVCFSEGAPAMCRKSSDYTDQLVLQCLLLMTDVAGDPEDEAEELQEWLNTDDLDQDESDANHVVAEQAMDRLSRKLGGKTILPPSFTWLPRLIPSQKWSERHAALMAISSIAEGAEKLMKKELSRVLDMVLPLLADPHPRVRWAACNAVGQMSTDFAPDMQVKYPSRILEALVPVLESPESRVQAHAAAAMVNFSEEADNKVLEPYLDDILQRLLTLLQSPKRYVQEQAVTTIATVADAAAKKFEKYFDAIMPLLFNVLQQADGKEFRTLRGKTMECATLIALAVGKQRFLPVSQELIQILGNIQMGITDSDDPQASYLISAWGRICRVLGSDFVPFLSSVMPPLLVAATSKPDFTIIDDEVDESKYSEQDGWEFIPVHGQQVGIRTSTLEDKCTATEMLVCYAAELKADFDPYVNEVLTSVVLPGLKFFFHDGVRSACCKCIPQLLNARILASNRDPAKVNELWEPILRKLLDHIQNEPSVEMLADYFECFYQSLEISGLNLSPSSMEALVAAVDLQLKGFISRVQQREEEAKNGDIDIEEDEDMILAVENDQNLLNEINKTFSVVLKIHKTAFCPFWERLLPYMDGFLSGNDTVAKQWALCMMDDLIEFTGPDSWNYKDHFLPYLAEGIQSSEPEIRQAASYGIGVAAQHGGELYAEICSSALPALFKMLELPDARDEEQIYATENICVAICKICRFCSQRVQDLDKVVTYWINTLPVTHDEDDAPYAYTFLAELMEQNHVAVASQMPTIITILAETFASGVLRGRTLTRLMEASKVYLARFPADQVNSVIATLSVDNQRALSAHF
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Involved in the nuclear import of cdc25 and mcs1. Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Involved in the nuclear import of cdc25 and mcs1. Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity).
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O74499
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LSM7_SCHPO
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U6 snRNA-associated Sm-like protein LSm7
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MSSLQKRPGPGNSSQPTERPRKESILDLSRYQDQRIQATFTGGRQITGILKGFDQLMNLVLDDVEEQLRNPEDGKLTGAIRKLGLVVVRGTTLVLIAPMDGSEEIPNPFVQAE
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Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Probable component of the spliceosome.
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O74511
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EKC1_SCHPO
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Extragenic suppressor of kinetochore protein 1
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MFWRLGQGFGFQSSSAIEAILDKPEDEINLKELLEENGVLDECKSHNPKLLEYLCKPEVLSQLIDYILEVDETEIPSADGGYEEPEHTRLSYIASEILSSDVWSICEACVENKTLMVKLWSFLDSEGPLNPLQASYFAKVNEHFLDKKTEETVAFIQSIDNFVEKILRHAETSAIMDLLLKFISMDRCNTAIGIADWLYSQGLIQSLLRLLSPYVDPDVQFTVADVIKAIIAISANSNEPGVIGPNSLSRELVSRQTITTLTDYMTDSKAPHSATSLINGVSIVIELIRKNNSDYDVTPVLQMPLDTHPPTTRDPIYLGTMLRLFAEKIPVFQKILLKPSTESDLMPTSFGKIKPLGFERFRICELYAELLHCSNMSLLSDPNGEAMVMQRDHLRDYLFRHNSCARDLVMSDEDDDDSTFSDKNSKDFKETEDMNGAEDMHGRAPQITKDNLNLTTTDSPMSEAEPVSEEEYKDVMETAKALHHGDDDAASDTSYEPLPESVIEDAKKLPVIGDFLKIEFIQNNVIPTILDHFFDYPWNNFLHNVVYDVVQQVLNAPMDKDQNYALAVDMFKQGKITEKIVYGQELNDKKVAKPSGFRAGYMGHLTIIADEVVKFVEHYSSTFDQELLNLINDEKWQNFVNKTLVETRNRDNQLLGGLEPSMVGYLEDMDEGEMLDANNLPEMQFALEQELESNSSDDDVVEVHRELSHNSSSNDEDDGNDEDPLSREMSRRLSFESANDSDQDNRDHFAQYMSQQISDNNANQFSSSDEDDDDDDEVVEWVSRGNENKYPRSNFFINGSDREDFSDSEEEDGNDSSDDDRGFAEEEYSDGLVLNHGK
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Has a role in chromosome segregation. May provide a dynamic connection between kinetochore microtubules and kinetochore chromatin.
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O74518
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CID12_SCHPO
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Poly(A) RNA polymerase cid12 (PAP) (EC 2.7.7.19) (Caffeine-induced death protein 12) (Polynucleotide adenylyltransferase cid12)
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MGKVLLELHSVPWNEEGLSDNARLYSFLEFVSPKIEELKYRKLLLEKLQTHIREVVLDAELQVYGSMYIGTTLSISDVDVSLKSPRVGELEKRRVTMVLRKYLDADADFHSSARVPRINLVDVSGIGVDLTFGNDKACRTAELQKAYNEEHPIFGRLLMLLKHWLFERDLENVHHGGIASCALSYMLIGWLEMRFHKKGIDSEVQPIRALLQKFFYFWGVEWTYELFVLRPLTGQIVPKLQKGWLNEVQPNLLSIEDPIDRNNDIGKQSFQISMIKAAFVASANELLSDKTWFSTFAITEDEMFLCKQFENVINTKRSLVEGYDSDTESDELQAGG
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Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-directed RNA polymerase complex (RDRC) which is involved in the generation of small interfering RNAs (siRNAs) and mediate their association with the RNA-induced transcriptional silencing (RITS) complex. RITS acts as a priming complex for dsRNA synthesis at the site of non-coding centromeric RNA.
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O74536
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SNF1_SCHPO
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SNF1-like protein kinase ssp2 (EC 2.7.11.1)
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MQPQEVDLMENSTMRNGARVLPPEAISKRHIGPYIIRETLGEGSFGKVKLATHYKTQQKVALKFISRQLLKKSDMHMRVEREISYLKLLRHPHIIKLYDVITTPTDIVMVIEYAGGELFDYIVEKKRMTEDEGRRFFQQIICAIEYCHRHKIVHRDLKPENLLLDDNLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVINGKLYAGPEVDVWSCGIVLYVMLVGRLPFDDEFIPNLFKKVNSCVYVMPDFLSPGAQSLIRRMIVADPMQRITIQEIRRDPWFNVNLPDYLRPMEEVQGSYADSRIVSKLGEAMGFSEDYIVEALRSDENNEVKEAYNLLHENQVIQEKSHLSKSKRVDSFLSVSPPAFSEYTSELQKKSKQELIDPTLEGPRWTVSDPPTYAKQTIDSNICVLVPTAEKNKLEMRTLADAASAVDTSQSTRKKSRRNKWHFGVRCRGDAPEILLAVYRALQRAGAQFTVPKPVNGKYRSDMYTIKSRWEIPHCKREGKNTYAYIELQLYEVMPGCFMLDVKSNGYKDIYSHPERTADHGMDDLKSSFPFLDLCAMLVCKLFSA
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Serine/threonine protein kinase essential for release from glucose repression via the phosphorylation of scr1 upon glucose deprivation. Catalytic subunit of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a central regulator of cellular energy homeostasis, which, in response to a fall in intracellular ATP levels, activates energy-producing pathways and inhibits energy-consuming processes. The complex phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, leading to transcriptional activation through TBP recruitment to the promoters (By similarity). Regulates proper cell cycle exit and sexual differentiation. Regulates also ste11 levels under nitrogen deprivation.
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O74539
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MAK3_SCHPO
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Peroxide stress-activated histidine kinase mak3 (EC 2.7.13.3) (His-Asp phosphorelay kinase phk2) (Mcs4-associated kinase 3)
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MYSQHELRNKVSLALSSLLRYTFELTPFFELYEADFAYALYAGFELATNRKVVGKFSFQNVHLENEYNILTEIAKDERASKFSPTPIEFTSFPHIDLSACIAYDFGHGAELSTSYAYFRENPAEFVRFCIAICKCIEYLHSKGMVHGEIRLDSFIPISSYDNVYMLTVGSGASYFHNCLQAHNWRKYSEDSESMSRILFISPEQTGRTSYSVGYRTDIYSLGVLFFHYLSDCSPYTGSFVQRIRSILTEPLPDISKSCPKLPHLIFKIIEKMTRKNPDERYTSCSGIVNDLEACLDDIDKGLILNDHVLEKTGRTSLFYLPCSIYGREHEIKLIRKILRNSPRAINHQDKKDLETFNPYYLNAIESESSSQSLSLSQRASEVMPLVILITGCEGIGESSLIQTICDRREGYMAITKFEVSQSIVYSAIVSAVAEFIRQILAEDQLLLNNFFEELKNKLESDLYLLDSVFDLVPEIRSLLQQFSTSSGNTRKTSLLGSNHSSYSDKLGSPTILSTSFSLARPYPEPALVSPSTERPPRSSFSAALMTLLNIIASFKKVTMVIENIHLADESSLIILQKIVYSDLPLTLMITCDKENDHVINRFRLANDRIHEIELKPLSFNAVNSYVQATLHRTDDGLARFSSYVYHISKGVPLLVRNVLLSIYENKIIYFDWKKNRWEVNYDEMYTLDNDYSEPDAFMTAKKKISKLNDSSRAILGWASLLGPSFSFATVKKLCKDTDNIELNVEALQSALREGIIYATSSDDTYTFSRSIYVKAMRDLLNEAKIQIMHACLIDVCLKNRDRYNIFDIAFHINAAFDFVKGDKRSVEYCHYLHLAAEEALKIGANQEALDLYNRCIKMIPHEIPEESDDSYIRCQLIGMYVGCAEAYWVNDNFDTASEMLKLAEEKACNNSEVFPARFLYSRILFEGVHIEECTQYVLSCLKPLGYELKRHSLEDSKSIISALIPRIIDKITKSSEESQSSTDDDDRRIFEILSFLYVGSVATSYFSETAEMAIDFGIAQVEFFLSTVVNSFSAFALVYFAILANSLLEPSEDILFIGNYGEKLNREAENPIIFSRTEYLYVQSLGFIDSTTKERRLTIDYLDRNCVTCSDKHVIISLLLVSSWEKFLTSNNYSNYLADFETTHAQIMEMKPWVGDTSLITQLKRFLMCLQDNIKLDLIKSKSFLSDHNIQLSSPAAQESAKLAFSLHGWINSWYLLALVMHGEWDMAISYGENFKREFKNALLTSSRVFGIFMFTWSLVNKMLICPEFTKQKKYYEQYKENLGFFDSLCIGDNECITRVYFLLLKACGLIMNGLNFEASVMLEEVISLTEKLELFLLQAFAFETVGSIFVSMELYTSATQYLEEAIRNYAALGVKQKARHLRDKFGDLLVSNNLQVSIDEATQTDFPLVFSPERSSIDINASSMRSEKASFEIPFPEEQIDDDVSPVAQDSSLEELLISLDIIDLTSVMRSCQTIASEIELTGLLSTMTQRMLEDSSANAAVIAIRDDVGFKIAAYRTGELNEVFAPPMPITEDQTYVPSRVINYVVHTQKALFSNNINHEFDLQQERWNIENHMGRSVIAIPLYQKKEVFAILYLQGPPSAFHSRHMSVLSILGAQASFAIVNISLFHKVKEATNVNTIIIKAQREALNLVQKSEAKYRSFVDTMPCLLSKLEFDEELRIELFGSFWKEYCGELNINDPNTWKEYVHLDDHLKLQDFLLSHLHNPLPFELEIRIKRKDGVYRWNLTRCTPTTNEKNRTSFLCATIDIDDQKKARATALELARLRSNFLANISHELRTPFSGFYGMLSLLDDTNLDSEQRDIVSAARISCEMLLRVINDLLNFSKLEAGKVTLESDLEFSLESVVCDCMQSVYSACAEKGINLSYNVSPDIPFFTAGDGMKIGQMLKSILDNSVKTVNNGFIRVRAFLAGSSKKNDRDQLQIAFIVEDTREESNAIFLANMINSLNRGCNDYLPMDLSGTALGMSTCLQLCKIMGGSVSVEVSQNNPTFKICYDLKIHELGKERYDIIATPLFQNLTEFNDLIKSKVAIRVSKTSTEYDNITTYLQAARKVLHVFKGLQDLASIFDLSPDSALLRCSVVVVDVYSMDDVKAVEKILKSYPDVHVIYLCCDPSRLNIEQELQKPSGRSFACKKRWGFLQMPCTRENFLKVTLQVFKSNEDTCNFYSYVNEYGESPKPDDDMDRLNKCVGSKILIAEDNPIVRMTLKKQLEHLGMDVDAAEDGKETLQIFESHPDNYYQVCFVDYHMPVYDGLEVTRRMRKIERKHGCAPLPIFALTADMQPTMETQFQEVGITHYLSKPFKKETLIKMLLQYLVNGTDGNANTS
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Involved in the control of the SAPK-dependent transcriptional response to peroxide stress. Regulates sty1 activity.
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O74555
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BBP_SCHPO
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Branchpoint-bridging protein (Splicing factor 1) (Zinc finger protein bpb1)
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MLNSRSVGSTGSNNTPLGRRRFDEKPDSLPPLPDANGMSNGYRDSYKSNSRMDHRPDGYHDGRGRRAYRKHYWGHPTPIEEMLPSQMELETAVKSCMTMEQLELYSLNVRLEEITQKLRTGDVVPHHRERSPSPPPQYDNHGRRLNTREIRYKKKLEDERHRIIERAMKMVPGFRAPSDYRRPAKTQEKVYVPVKDYPEINFIGLLIGPRGHTLKDMEAKSGAKIAIRGKGSVKEGKGRSDPSVRGNMEEDLHCLVTADSEDKINHAIKLIDNVIQTAASVPEGQNDLKRNQLRQLATLNGTLRDDENQVCQNCGNVGHRRFDCPERINHTMNIVCRHCGSIGHIARDCPVRDQQPPMADSTADREYQSLMQELGGGSAISNGNGEPQKSIEFSESGAASPQAGHPPPWAAASTSVSSSTSSPAPWAKPASSAAPSNPAPWQQPAAPQSAPALSMNPSSLPPWQQPTQQSAVQPSNLVPSQNAPFIPGTSAPLPPTTFAPPGVPLPPIPGAPGMPNLNMSQPPMVPPGMALPPGMPAPFPGYPAVPAMPGIPGATAPPGAPGSYNTSESSNLNAPPGVSMPNGYSNR
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Necessary for the splicing of pre-mRNA. The BPB1(SF1)-u2af59-u2af23 complex has a role in the recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns.
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O74558
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MOB2_SCHPO
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Maintenance of ploidy protein mob2
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MFLLNSLSRITRGNRSKRHQNLSDASSSSGSFSKKSSTSQLVRTGSPSVEPTALYLQQPFVRTHLVKGNFSTIVSLPRFVDLDEWVALNVYELFTYLNHFYDVFATFCTVKTCPVMSAAANFDYTWLDNNRKPVHLPAPQYIEYVLAWIENRLHDQNVFPTKAGLPFPSNFLVIVKAIYKQMFRIFAHMYYAHYAEILHLSLEAHWNSFFAHFIAFGKEFQLLDKRDTAPLKDLIVVLENQGNI
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Required for coordinating polarized cell growth during interphase with the onset of mitosis.
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O74560
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RAF2_SCHPO
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Rik1-associated factor 2 (Cryptic loci regulator 7) (De-localization of swi6 protein 2)
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MPPVRAEKKRKTDLIEQVCVTNKAGELVDLEDVLEYGPYSLTGILSSEKDEQEPLFDESIVLGYSIKISPVWTYNLKDVPEKETMSIWIVTPQRRYGILSPSSEYKAIYEQISEKNRLFYLIKTKFKDDMISGTLEDYDNYIEVLKEKLELPSCFQAILLVQKHIRFLLTQMVATSSLHVWSESPFFIRIRSSYEHLILQINKNIYNARQERKKSKLSSNNPSDNNTTMKSSLNQALTLINLPEQPFSISSPTATPQLGVVKRTSPLRFPLNDIWLSGLRIVDPNIESISLWKRIQVSTSPKHQRYISLQEVCSVIAQQLQITNLEALNKLSSHGETLLQIMHTAFTWRGTKLFNDIKHAIGFRSSVQQARSQFRGYCYDYLFMHCNNGEKTSLHLLRTLICMKLDFSNAQLAAKILFHFLLFDIGSGLSGSDYTYEQYINHSAVAFSFTEEIFEKNFVTVLPDFVKLFSISFGYWPAFSFYDELLKLLRNKYPKVYSSTPNLCDQVWLDRTNLFPCNRSTRSTLPYRPTKLLDLASASSCLSKKETDFKQDTGLYSYNLEKVEALKVSPDLQTGIWSCPVQNCLYFAVCDNPYKPSQVIYDHLLGHVDSKFIFKTPSNSVRSFTNKLEHIMYNIN
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Component of the Clr4 methyltransferase complex (ClrC) which contributes to the establishment of heterochromatin by specifically methylating histone H3 to form H3K9me. ClrC preferentially ubiquitylates H3K14 and ClrC-mediated H3 ubiquitination promotes clr4 methyltransferase activity for the methylation of H3K9. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci. Has a role in both mitotic and meiotic chromosome segregation.
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O74562
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SEC8_SCHPO
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Exocyst complex component sec8
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MDTRGYSETKKGRYPVGKKSLESPNGYSNYGTSMDNELSSEYASRGMHIGDLENLVNEIEDEWKDLGREDYQPISTALELLDDSSFGRDYKSFLNVYDRISAALQTIAHTHKDDFTRGISAYGEIMEGIQKCNSRIIALKQSLEASQECIGNTNSKELQQTLARSSQYKKVISVLKELNEANQLFDNFHTLVDSKQYYHASDLIRRVWDELSRSDFDGILVVEQFKSRMTGLLSHLEDILSEELVSITFLKDAVAYPIVSYCSPNPLRETSNPYFLRDFLKNNANTSTLGQSEQLRYLEEALSLKLSDCLKMDYGRDSLRDIRIVLESLNLLGKLPNAISSLKSRTSAEMFTTVDSTSRAIVNKYSLGNNVSTVNPFSKSLYDIGLHAETDREHTMISEFLTNLFTKLRCVLMHYRGISEFMTKLETKTPKHASSSHKSSIMSVNSDPTSPKVSKFDTSDSTFPFDTLLQAFESEIRLMLKDYLISKEEYIENSGNFVVGTEMSIYNLPGENEEDKLFDVTNEIAVENKSNAFYARINELVNEKAPELILNKSNASVSTIELFSGSSKEIVRLAGHVVFVGPSVFHASSVLPQTVFFLEDSVSILKNPNIPPQFAVNFMKEFLRGSYIPQLYKFMSSHFDTIMKDVGAFQLHRDWKIYSKIPIFKCHVAIVQYFHDLQDYLPIVALNLVEFYELLHTLLVRFRNHCSDYLSDLCRTAVLKEYKHVNEDTEDVDDTVRVKLLHDDVTYPQFIKFLKQKNPSLEGLNELCRMENKRLLQYEDRAITSEVKLPVSVLSKDSDLVNSVSYLHNSMEWFLQRCFSRFMNGSRRMNVLQQNQANFGGDFLPIDNLLGNNSDLMKGAYKEVFDSLQRLQFDALLLIRMEVRLQYIHSINQSVNLPDYVVEYRGRPDASIMALNSTIVTTNLKLETCLNEWERRFVFQGLSELVDSSLYSIFYKIESMNRGSCLQMLKNMSAMIQILKTVKEIHGDVEFPKSSRVFGIYQNGAKKIIEHFIAAPKKELLPDVKQMVRIYYQRLMKDAKRNGRDDLYRQYQKKIGSVLTQFDNTVGGARKNP
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Component of the exocyst complex involved in the delivery of secretory vesicles to the plasma membrane. Also required for polarized cell growth and division septum assembly. The exocyst complex plays an important role in the targeting of rho3, as well as the two main hydrolases required for cell separation, eng1 and agn1, to the cell wall surrounding the septum before cell separation begins.
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O74563
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BRL2_SCHPO
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E3 ubiquitin-protein ligase brl2 (EC 2.3.2.27) (BRE1-like protein 2) (RING finger protein 1) (RING-type E3 ubiquitin transferase brl2)
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MYQNGKPDAPTILGQKRELEDVEIQDDDIQEVSKEDLLKDVRVRSIQFDELESKIEGLQNLAEEKLKVLATLVSWWPEILQQFSVVFQGNELKDFESEGVFSILEKFPELSYFNDAVKNNKTKALSIIQKLLSTVDSSTNSVSRDPFSVLSIDDSALTEKLNTINLDIDKILDELDTTRSQLHSIIKLPDRSSSFTLQCINESVRPQSTKVKEEATTSSKGKDEEKKVSTVEQRTQLQQLSRLQDQQNGLMESRSQSLKILDSNVNEMDKLIMERENALNNVETTNLKKYSSFLALKEAVSMTSEQLRVLEHLLSECSHEINVLSQQSKNFNGVFESSYQPLINDLDHQISVMQNDEKRINNAKTELSLSLEKKLEAKKQKEKVYKDKLDELANLETMVLEKKKAVATREAANKIRLVDLNDLELQKDLSTYLSKELASTEKAFRLVKQQTVKSSHSHYQELITKFSVEKEKAEQKYFLTMKSTDSLHAEVKLLRQKYQKTNEIISKMLNSQDTAVHRIIEFEDQLARLSSVRNNSIKQSTTFQVKKSSQKSTIQNLEEKVSYLQQFMDKNNATLTDLEFQCSDLSSSIDILSKQDEEHEKEKRKLKDTGVSTSAEELKTFRAMCKCSVCNFERWKDRIISLCGHGFCYQCIQKRIETRQRRCPICGRGFGASDVIPIHL
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E3 ubiquitin-protein ligase which belongs to the histone H2B ubiquitin ligase complex (HULC) which mediates monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation.
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O74627
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CG1C_SCHPO
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Cyclin pch1 (Pombe cyclin C homolog 1)
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MSEVIKSVPPGSQNTSQWIISKDQLVFTPSALDGIPLDQEEIQRSKGCNFIINVGLRLKLPQTALATANIYFHRFYLRFSLKNYHYYEVAATCIFLATKVEDSVRKLRDIVINCAKVAQKNSNVLVDEQTKEYWRWRDVILYTEEVLLEALCFDFTVEHPYPYVLSFIKKFVADDKNVTKVAWTYINDSTRSIACLLYSPKTIAAAAFQFALEKNEINLSTTTDGLPVWMEESQVSYEDVKGVLTLIDSLYKKINPSKQALPIDQKNGSHASSVAPGTPSSLASVSTQATPQHQNSSGRTDSFHSLNTETPSKSTVDDQILSTAAQPKKSSDTDKEMETEAS
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Essential for progression through the whole cell cycle.
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O74630
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ATM_SCHPO
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Serine/threonine-protein kinase tel1 (EC 2.7.11.1) (ATM homolog) (DNA-damage checkpoint kinase tel1) (Telomere length regulation protein 1)
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MTSLNDIVNKLSSSKIKTRSDALQNLRSYIIYSRNGNSLNQEDALIIEKAIKRAFELEWQISANHGKRQISKASQEQKLQDISYLLRTCVESYILLFREPHILALLDIILRHTFTANGSICEVVCLNFSKALRLLLSHSPHLHHLRFSDWQSLVSYCCQAIEKLSIAEETYVSDSEEEPISQKNYQEISIWKSHDVIRVKQEVVELIYVMRSLVQWYAAPINFVSEQLLKFFEFFFYAYTEETDAHLPALQCLFQLCAYAIPNCNDYSASVVLLVFKILINSDKWKRLDLRLQLIQCLAISYPLWSNSETWDPHRSIRSFNLDLLNSSFFSLKNFLNFFGKRSSLSLANFRFHTVEPKNNIAKLYDPRLHLFFSLRHNSFFESYFIYFFLAKLILLKKTVLSLASTEQANKKQKTCSQIEELLLQAELANISASSFSLQLMVIITAISDNLTNDDLLSIQKMSLNFTEKKNELQSWSFFILFNICYNKAYSSMLTTSCKKEILAAASRGLLNSVTSPVCYQILTYFNMYRPLCFASIFPFIKQQFILFNDYSPMLSYEAIDYWKSLYILLNENLFVGQSSFKSVFLKWLKWHLYHLFSKEGELPFFSFTDSSIIIFDLLMMIFYRPLSLSYITTEIRSPFERNLFHLKEAWSPVTLRFPYTTDEICKQSTEGCYPFNSNHTIDCDSLQNVIKMLESSIDEISSASYDKDELDKETPSFEAVMIFSQISFLCGFLNCFIQKKGIHNVTPNNLVIFKNLFPEVLSFVKSNHSYDPIINCISTNLQFTISDEPKHLRYEIGSDLIRSTHFRDSNPLKTLVLYIMDMASKNVFIKPQEFDHDEYFSQEEEDIYRPENLIRNHQILGLMEGSLEQIRNTDLFILQKYIDYFSSHPHDSLINILHLYPIETFCFGMSAIGAYFLDVARTSEPIFYKCLEILAQKILMNYDYERDEVYLMIFIKIFQKCVHSKLQFTDATLKLIVKITKFIEKVFIETKFSSLSGRQTFLKFIFQLSPTSHVYSKFDYQKLISLTLKDSDVCVIYNFVDDLVIFLKKCDKTLIEGFVLPILSIKIEKSLYKGFCYLYLTLKVFLSISSNRSALLYQLLKLANSYETSTIFEPLLRKLHIQSANIKQLFRIYRLEIFWSFVSKDLSNTTNDFLEFPYKPIYFSLSDFLKENSDEIILVLILTKNITLAKLITSRMSVDFSEKYTQLIPVITTYTHLSEVENKKYSLRFNSIDEALDVELLNRSKAFLFCLEMLKEVKELGSTFKSISSTSFKVYSQLTIFANRVSFNNSTAIPFFSTKSVLWYCNRLFQELEGFSSIPSVIDLVLRRLAIQLHFATDEELQVTISFRLCAFLCFSDPFITSNYLVMIVLRIARQLLSIPCTQSLGLGIARFHLKKFKPTDFDYFFQLAEFCMDFLGFCYNTIGTKMEAIQDFYTWFDGYVTALLNFEYEGYGFLRCQINFVRSVMTTKNEWIEVSNKLFERGHFLKRIAMNNYLCLYFWQVLDACPRNVLHSLSLEIWKCYKAYDITEFPDSLKLFFSDIMGWNFFKSPEIADLNHYIPKTDPRLCDTKTYEESKLIIWKLICQKACSLLFKYDILLDSFIEDCIRMFFENGNHQELRKFLNFPKDSIIYDSDFKTLVSEEGSFQWVKLQPTNFDSLSNWTKEETLKLLNMMGKSSTTHSLKLLSTYMVGFSTSIIQYIIHLILLEFDFNGNNKKQKEYVTQLILSGLLNKNTNSIRKTCMNILLYLRRQLGHHALNPFEANYWVPINYSVAASTAYDCHLYEQSLLFLTIHNTKTDELDITLLSDILSQLPCPDAYYGIKRETSFKNILLKAVHEKRSPLAISYLDAANMYRSNEDEGTKMMFSNTLNNAGFFSLNEFYIDSLKANDAIDECSNEVYASAWRMQKWDIPPLSLDNKTTKDCLVFEVLHAVHNYAIYGNYLHLEEYINKKLLLINPNEEPDSLLFYALAYDLKFLIRCNQSQFNCDILQLLKENKQMSSQLHECFQLLLEIRNVLLSLLQSHKQLDLSDDLASFRKYYILELLKISESFLIVDNLQNAFSVAMLSDALYRKFDLADENLKHDIDFLSSKILWQRDEKIDAIGMLSESLSKTNSSIFPSISYAYLGNWLYTTKSEKTELVSKNYFEKSLSHMSHLNAKEKAKIYCMFAQFCDNNYSSPDLTEDFKRMEKLYFEKKNDIQQLERSIVNASNMKEEKMLKNHHSREMSSFIIDEREYLRMSTFRSKMLTQSITHYLKCLSESDENDVLISRCCTMWLSNSHLDELNNSLQHYLQNLPCKKFIPVFYQLAARLMNENSKFQQSLTSICYNVGRNHPYHSLHVLFSLVSNVPEIENLDAGSRYRAVKKILDLLKVNQGLSNLVTKLLCSFENYVSLAEWNPRSKVDSTSFSRFPGYKWFLKDAANYGLPPITMNVKVNDTGDYSNIPTVSSFDDTIHFASGINAPKVITCLGSNGHTYKQLVKGGNDDLRQDAVMEQVFEQVNGFLRSYRKTSQRNLSMRTYKVIPLALKTGVIEWVQDTIPLGEYLDSAHKVYHPKEWSLSTCRKLIAEKQMEDLETRLKVYDLVCRHYRPVFRHFFLESYADPVQWFTTQTNYARSTAVASVLGHVLGLGDRHGQNILIDKTSGEVIHIDLGIAFEQGKKLPVPECVPFRLTRDVVDGMGITGVEGVFRRCMEFTLETLRREEDSLLSVLEVLRYDPLFSWLISPLRRMKKQKMQLENFNQPESGNITTDASRDPKIQRNNVSGESEAERAILKVRQKLSSTLSVEASVGELIRIAQDPSYLALMFCGWSAFQ
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Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, involved in the regulation of DNA damage response mechanism. Undirectly involved in the phosphorylation of rad32 which is necessary for its telomere function. Required for the control of telomere length and genome stability.
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