entry
stringlengths 6
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stringlengths 5
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stringlengths 3
2.44k
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stringlengths 2
35.2k
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O15529
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GPR42_HUMAN
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G-protein coupled receptor 42
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MDTGPDQSYFSGNHWFVFSVYLLTFLVGLPLNLLALVVFVGKLRCRPVAVDVLLLNLTASDLLLLLFLPFRMVEAANGMHWPLPFILCPLSGFIFFTTIYLTALFLAAVSIERFLSVAHPLWYKTRPRLGQAGLVSVACWLLASAHCSVVYVIEFSGDISHSQGTNGTCYLEFRKDQLAILLPVRLEMAVVLFVVPLIITSYCYSRLVWILGRGGSHRRQRRVAGLVAATLLNFLVCFGPYNVSHVVGYICGESPVWRIYVTLLSTLNSCVDPFVYYFSSSGFQADFHELLRRLCGLWGQWQQESSMELKEQKGGEEQRADRPAERKTSEHSQGCGTGGQVACAEN
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G protein-coupled receptor that is activated by short chain fatty acids (SCFAs), such as propionate. Hence may play a role in the regulation of whole-body energy homeostasis and/or in intestinal immunity.
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O15530
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PDPK1_HUMAN
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3-phosphoinositide-dependent protein kinase 1 (hPDK1) (EC 2.7.11.1)
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MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ
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Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages. Isoform 3 is catalytically inactive.
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O15533
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TPSN_HUMAN
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Tapasin (TPN) (TPSN) (NGS-17) (TAP-associated protein) (TAP-binding protein)
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MKSLSLLLAVALGLATAVSAGPAVIECWFVEDASGKGLAKRPGALLLRQGPGEPPPRPDLDPELYLSVHDPAGALQAAFRRYPRGAPAPHCEMSRFVPLPASAKWASGLTPAQNCPRALDGAWLMVSISSPVLSLSSLLRPQPEPQQEPVLITMATVVLTVLTHTPAPRVRLGQDALLDLSFAYMPPTSEAASSLAPGPPPFGLEWRRQHLGKGHLLLAATPGLNGQMPAAQEGAVAFAAWDDDEPWGPWTGNGTFWLPTVQPFQEGTYLATIHLPYLQGQVTLELAVYKPPKVSLMPATLARAAPGEAPPELLCLVSHFYPSGGLEVEWELRGGPGGRSQKAEGQRWLSALRHHSDGSVSLSGHLQPPPVTTEQHGARYACRIHHPSLPASGRSAEVTLEVAGLSGPSLEDSVGLFLSAFLLLGLFKALGWAAVYLSTCKDSKKKAE
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Involved in the association of MHC class I with transporter associated with antigen processing (TAP) and in the assembly of MHC class I with peptide (peptide loading).
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O15534
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PER1_HUMAN
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Period circadian protein homolog 1 (hPER1) (Circadian clock protein PERIOD 1) (Circadian pacemaker protein Rigui)
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MSGPLEGADGGGDPRPGESFCPGGVPSPGPPQHRPCPGPSLADDTDANSNGSSGNESNGHESRGASQRSSHSSSSGNGKDSALLETTESSKSTNSQSPSPPSSSIAYSLLSASSEQDNPSTSGCSSEQSARARTQKELMTALRELKLRLPPERRGKGRSGTLATLQYALACVKQVQANQEYYQQWSLEEGEPCSMDMSTYTLEELEHITSEYTLQNQDTFSVAVSFLTGRIVYISEQAAVLLRCKRDVFRGTRFSELLAPQDVGVFYGSTAPSRLPTWGTGASAGSGLRDFTQEKSVFCRIRGGPDRDPGPRYQPFRLTPYVTKIRVSDGAPAQPCCLLIAERIHSGYEAPRIPPDKRIFTTRHTPSCLFQDVDERAAPLLGYLPQDLLGAPVLLFLHPEDRPLMLAIHKKILQLAGQPFDHSPIRFCARNGEYVTMDTSWAGFVHPWSRKVAFVLGRHKVRTAPLNEDVFTPPAPSPAPSLDTDIQELSEQIHRLLLQPVHSPSPTGLCGVGAVTSPGPLHSPGSSSDSNGGDAEGPGPPAPVTFQQICKDVHLVKHQGQQLFIESRARPQSRPRLPATGTFKAKALPCQSPDPELEAGSAPVQAPLALVPEEAERKEASSCSYQQINCLDSILRYLESCNLPSTTKRKCASSSSYTTSSASDDDRQRTGPVSVGTKKDPPSAALSGEGATPRKEPVVGGTLSPLALANKAESVVSVTSQCSFSSTIVHVGDKKPPESDIIMMEDLPGLAPGPAPSPAPSPTVAPDPAPDAYRPVGLTKAVLSLHTQKEEQAFLSRFRDLGRLRGLDSSSTAPSALGERGCHHGPAPPSRRHHCRSKAKRSRHHQNPRAEAPCYVSHPSPVPPSTPWPTPPATTPFPAVVQPYPLPVFSPRGGPQPLPPAPTSVPPAAFPAPLVTPMVALVLPNYLFPTPSSYPYGALQTPAEGPPTPASHSPSPSLPALAPSPPHRPDSPLFNSRCSSPLQLNLLQLEELPRAEGAAVAGGPGSSAGPPPPSAEAAEPEARLAEVTESSNQDALSGSSDLLELLLQEDSRSGTGSAASGSLGSGLGSGSGSGSHEGGSTSASITRSSQSSHTSKYFGSIDSSEAEAGAARGGAEPGDQVIKYVLQDPIWLLMANADQRVMMTYQVPSRDMTSVLKQDRERLRAMQKQQPRFSEDQRRELGAVHSWVRKGQLPRALDVMACVDCGSSTQDPGHPDDPLFSELDGLGLEPMEEGGGEQGSSGGGSGEGEGCEEAQGGAKASSSQDLAMEEEEEGRSSSSPALPTAGNCTS
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Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates circadian target genes expression at post-transcriptional levels, but may not be required for the repression at transcriptional level. Controls PER2 protein decay. Represses CRY2 preventing its repression on CLOCK/BMAL1 target genes such as FXYD5 and SCNN1A in kidney and PPARA in liver. Besides its involvement in the maintenance of the circadian clock, has an important function in the regulation of several processes. Participates in the repression of glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) by BMAL1:CLOCK. Plays a role in the modulation of the neuroinflammatory state via the regulation of inflammatory mediators release, such as CCL2 and IL6. In spinal astrocytes, negatively regulates the MAPK14/p38 and MAPK8/JNK MAPK cascades as well as the subsequent activation of NFkappaB. Coordinately regulates the expression of multiple genes that are involved in the regulation of renal sodium reabsorption. Can act as gene expression activator in a gene and tissue specific manner, in kidney enhances WNK1 and SLC12A3 expression in collaboration with CLOCK. Modulates hair follicle cycling. Represses the CLOCK-BMAL1 induced transcription of BHLHE40/DEC1.
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O15535
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ZSC9_HUMAN
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Zinc finger and SCAN domain-containing protein 9 (Cell proliferation-inducing gene 12 protein) (PRD51) (Zinc finger protein 193)
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MNTNSKEVLSLGVQVPEAWEELLTMKVEAKSHLQWQESRLKRSNPLAREIFRRHFRQLCYQETPGPREALTRLQELCYQWLRPHVSTKEQILDLLVLEQFLSILPKELQGWVREHCPESGEEAVILLEDLERELDEPQHEMVAHRHRQEVLCKEMVPLAEQTPLTLQSQPKEPQLTCDSAQKCHSIGETDEVTKTEDRELVLRKDCPKIVEPHGKMFNEQTWEVSQQDPSHGEVGEHKDRIERQWGNLLGEGQHKCDECGKSFTQSSGLIRHQRIHTGERPYECNECGKAFSRSSGLFNHRGIHNIQKRYHCKECGKVFSQSAGLIQHQRIHKGEKPYQCSQCSKSYSRRSFLIEHQRSHTGERPHQCIECGKSFNRHCNLIRHQKIHTVAELV
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May be involved in transcriptional regulation.
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O15537
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XLRS1_HUMAN
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Retinoschisin (X-linked juvenile retinoschisis protein)
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MSRKIEGFLLLLLFGYEATLGLSSTEDEGEDPWYQKACKCDCQGGPNALWSAGATSLDCIPECPYHKPLGFESGEVTPDQITCSNPEQYVGWYSSWTANKARLNSQGFGCAWLSKFQDSSQWLQIDLKEIKVISGILTQGRCDIDEWMTKYSVQYRTDERLNWIYYKDQTGNNRVFYGNSDRTSTVQNLLRPPIISRFIRLIPLGWHVRIAIRMELLECVSKCA
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Binds negatively charged membrane lipids, such as phosphatidylserine and phosphoinositides (By similarity). May play a role in cell-cell adhesion processes in the retina, via homomeric interaction between octamers present on the surface of two neighboring cells. Required for normal structure and function of the retina.
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O15540
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FABP7_HUMAN
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Fatty acid-binding protein, brain (Brain lipid-binding protein) (BLBP) (Brain-type fatty acid-binding protein) (B-FABP) (Fatty acid-binding protein 7) (Mammary-derived growth inhibitor related)
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MVEAFCATWKLTNSQNFDEYMKALGVGFATRQVGNVTKPTVIISQEGDKVVIRTLSTFKNTEISFQLGEEFDETTADDRNCKSVVSLDGDKLVHIQKWDGKETNFVREIKDGKMVMTLTFGDVVAVRHYEKA
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B-FABP could be involved in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. It is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers (By similarity).
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O15541
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R113A_HUMAN
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E3 ubiquitin-protein ligase RNF113A (EC 2.3.2.27) (Cwc24 homolog) (RING finger protein 113A) (Zinc finger protein 183)
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MAEQLSPGKAVDQVCTFLFKKPGRKGAAGRRKRPACDPEPGESGSSSDEGCTVVRPEKKRVTHNPMIQKTRDSGKQKAAYGDLSSEEEEENEPESLGVVYKSTRSAKPVGPEDMGATAVYELDTEKERDAQAIFERSQKIQEELRGKEDDKIYRGINNYQKYMKPKDTSMGNASSGMVRKGPIRAPEHLRATVRWDYQPDICKDYKETGFCGFGDSCKFLHDRSDYKHGWQIERELDEGRYGVYEDENYEVGSDDEEIPFKCFICRQSFQNPVVTKCRHYFCESCALQHFRTTPRCYVCDQQTNGVFNPAKELIAKLEKHRATGEGGASDLPEDPDEDAIPIT
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Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). E3 ubiquitin-protein ligase that catalyzes the transfer of ubiquitin onto target proteins. Catalyzes polyubiquitination of SNRNP200/BRR2 with non-canonical 'Lys-63'-linked polyubiquitin chains. Plays a role in DNA repair via its role in the synthesis of 'Lys-63'-linked polyubiquitin chains that recruit ALKBH3 and the ASCC complex to sites of DNA damage by alkylating agents. Ubiquitinates CXCR4, leading to its degradation, and thereby contributes to the termination of CXCR4 signaling.
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O15547
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P2RX6_HUMAN
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P2X purinoceptor 6 (P2X6) (ATP receptor) (P2XM) (Purinergic receptor) (Purinergic receptor P2X-like 1)
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MCPQLAGAGSMGSPGATTGWGLLDYKTEKYVMTRNWRVGALQRLLQFGIVVYVVGWALLAKKGYQERDLEPQFSIITKLKGVSVTQIKELGNRLWDVADFVKPPQGENVFFLVTNFLVTPAQVQGRCPEHPSVPLANCWVDEDCPEGEGGTHSHGVKTGQCVVFNGTHRTCEIWSWCPVESGVVPSRPLLAQAQNFTLFIKNTVTFSKFNFSKSNALETWDPTYFKHCRYEPQFSPYCPVFRIGDLVAKAGGTFEDLALLGGSVGIRVHWDCDLDTGDSGCWPHYSFQLQEKSYNFRTATHWWEQPGVEARTLLKLYGIRFDILVTGQAGKFGLIPTAVTLGTGAAWLGVVTFFCDLLLLYVDREAHFYWRTKYEEAKAPKATANSVWRELALASQARLAECLRRSSAPAPTATAAGSQTQTPGWPCPSSDTHLPTHSGSL
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Receptor for ATP that acts as a ligand-gated ion channel.
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O15550
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KDM6A_HUMAN
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Lysine-specific demethylase 6A (EC 1.14.11.68) (Histone demethylase UTX) (Ubiquitously-transcribed TPR protein on the X chromosome) (Ubiquitously-transcribed X chromosome tetratricopeptide repeat protein) ([histone H3]-trimethyl-L-lysine(27) demethylase 6A)
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MKSCGVSLATAAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARTKALLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEDYPKALSAYQRYYSLQSDYWKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLSAQVKATVLQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNATRSKSCSNTSALAARIKYLQAQLCNLPQGSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQNTSDNWSGGHAVSHPPVQQQAHSWCLTPQKLQHLEQLRANRNNLNPAQKLMLEQLESQFVLMQQHQMRPTGVAQVRSTGIPNGPTADSSLPTNSVSGQQPQLALTRVPSVSQPGVRPACPGQPLANGPFSAGHVPCSTSRTLGSTDTILIGNNHITGSGSNGNVPYLQRNALTLPHNRTNLTSSAEEPWKNQLSNSTQGLHKGQSSHSAGPNGERPLSSTGPSQHLQAAGSGIQNQNGHPTLPSNSVTQGAALNHLSSHTATSGGQQGITLTKESKPSGNILTVPETSRHTGETPNSTASVEGLPNHVHQMTADAVCSPSHGDSKSPGLLSSDNPQLSALLMGKANNNVGTGTCDKVNNIHPAVHTKTDNSVASSPSSAISTATPSPKSTEQTTTNSVTSLNSPHSGLHTINGEGMEESQSPMKTDLLLVNHKPSPQIIPSMSVSIYPSSAEVLKACRNLGKNGLSNSSILLDKCPPPRPPSSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPNNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWHCESNRSHTTIAKYAQYQASSFQESLREENEKRSHHKDHSDSESTSSDNSGRRRKGPFKTIKFGTNIDLSDDKKWKLQLHELTKLPAFVRVVSAGNLLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEGYWGVLNDFCEKNNLNFLMGSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNIAWNVGPLTACQYKLAVERYEWNKLQSVKSIVPMVHLSWNMARNIKVSDPKLFEMIKYCLLRTLKQCQTLREALIAAGKEIIWHGRTKEEPAHYCSICEVEVFDLLFVTNESNSRKTYIVHCQDCARKTSGNLENFVVLEQYKMEDLMQVYDQFTLAPPLPSASS
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Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Demethylation of 'Lys-27' of histone H3 is concomitant with methylation of 'Lys-4' of histone H3, and regulates the recruitment of the PRC1 complex and monoubiquitination of histone H2A. Plays a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression (By similarity).
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O15551
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CLD3_HUMAN
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Claudin-3 (Clostridium perfringens enterotoxin receptor 2) (CPE-R 2) (CPE-receptor 2) (Rat ventral prostate.1 protein homolog) (hRVP1)
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MSMGLEITGTALAVLGWLGTIVCCALPMWRVSAFIGSNIITSQNIWEGLWMNCVVQSTGQMQCKVYDSLLALPQDLQAARALIVVAILLAAFGLLVALVGAQCTNCVQDDTAKAKITIVAGVLFLLAALLTLVPVSWSANTIIRDFYNPVVPEAQKREMGAGLYVGWAAAALQLLGGALLCCSCPPREKKYTATKVVYSAPRSTGPGASLGTGYDRKDYV
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Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
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O15552
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FFAR2_HUMAN
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Free fatty acid receptor 2 (G-protein coupled receptor 43)
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MLPDWKSSLILMAYIIIFLTGLPANLLALRAFVGRIRQPQPAPVHILLLSLTLADLLLLLLLPFKIIEAASNFRWYLPKVVCALTSFGFYSSIYCSTWLLAGISIERYLGVAFPVQYKLSRRPLYGVIAALVAWVMSFGHCTIVIIVQYLNTTEQVRSGNEITCYENFTDNQLDVVLPVRLELCLVLFFIPMAVTIFCYWRFVWIMLSQPLVGAQRRRRAVGLAVVTLLNFLVCFGPYNVSHLVGYHQRKSPWWRSIAVVFSSLNASLDPLLFYFSSSVVRRAFGRGLQVLRNQGSSLLGRRGKDTAEGTNEDRGVGQGEGMPSSDFTTE
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G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins but also to the Gq family. Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation. May play a role in glucose homeostasis by regulating the secretion of GLP-1, in response to short-chain fatty acids accumulating in the intestine. May also regulate the production of LEP/Leptin, a hormone acting on the central nervous system to inhibit food intake. Finally, may also regulate whole-body energy homeostasis through adipogenesis regulating both differentiation and lipid storage of adipocytes. In parallel to its role in energy homeostasis, may also mediate the activation of the inflammatory and immune responses by SCFA in the intestine, regulating the rapid production of chemokines and cytokines. May also play a role in the resolution of the inflammatory response and control chemotaxis in neutrophils. In addition to SCFAs, may also be activated by the extracellular lectin FCN1 in a process leading to activation of monocytes and inducing the secretion of interleukin-8/IL-8 in response to the presence of microbes. Among SCFAs, the fatty acids containing less than 6 carbons, the most potent activators are probably acetate, propionate and butyrate. Exhibits a SCFA-independent constitutive G protein-coupled receptor activity.
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O15553
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MEFV_HUMAN
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Pyrin (Marenostrin)
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MAKTPSDHLLSTLEELVPYDFEKFKFKLQNTSVQKEHSRIPRSQIQRARPVKMATLLVTYYGEEYAVQLTLQVLRAINQRLLAEELHRAAIQEYSTQENGTDDSAASSSLGENKPRSLKTPDHPEGNEGNGPRPYGGGAASLRCSQPEAGRGLSRKPLSKRREKASEGLDAQGKPRTRSPALPGGRSPGPCRALEGGQAEVRLRRNASSAGRLQGLAGGAPGQKECRPFEVYLPSGKMRPRSLEVTISTGEKAPANPEILLTLEEKTAANLDSATEPRARPTPDGGASADLKEGPGNPEHSVTGRPPDTAASPRCHAQEGDPVDGTCVRDSCSFPEAVSGHPQASGSRSPGCPRCQDSHERKSPGSLSPQPLPQCKRHLKQVQLLFCEDHDEPICLICSLSQEHQGHRVRPIEEVALEHKKKIQKQLEHLKKLRKSGEEQRSYGEEKAVSFLKQTEALKQRVQRKLEQVYYFLEQQEHFFVASLEDVGQMVGQIRKAYDTRVSQDIALLDALIGELEAKECQSEWELLQDIGDILHRAKTVPVPEKWTTPQEIKQKIQLLHQKSEFVEKSTKYFSETLRSEMEMFNVPELIGAQAHAVNVILDAETAYPNLIFSDDLKSVRLGNKWERLPDGPQRFDSCIIVLGSPSFLSGRRYWEVEVGDKTAWILGACKTSISRKGNMTLSPENGYWVVIMMKENEYQASSVPPTRLLIKEPPKRVGIFVDYRVGSISFYNVTARSHIYTFASCSFSGPLQPIFSPGTRDGGKNTAPLTICPVGGQGPD
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Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma. Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1, ATG16L1, and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy. Acts as an autophagy receptor for the degradation of several inflammasome components, including CASP1, NLRP1 and NLRP3, hence preventing excessive IL1B- and IL18-mediated inflammation. However, it can also have a positive effect in the inflammatory pathway, acting as an innate immune sensor that triggers PYCARD/ASC specks formation, caspase-1 activation, and IL1B and IL18 production. Together with AIM2, also acts as a mediator of pyroptosis, necroptosis and apoptosis (PANoptosis), an integral part of host defense against pathogens, in response to bacterial infection (By similarity). It is required for PSTPIP1-induced PYCARD/ASC oligomerization and inflammasome formation. Recruits PSTPIP1 to inflammasomes, and is required for PSTPIP1 oligomerization.
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O15554
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KCNN4_HUMAN
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Intermediate conductance calcium-activated potassium channel protein 4 (SK4) (SKCa 4) (SKCa4) (IKCa1) (IK1) (KCa3.1) (KCa4) (Putative Gardos channel)
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MGGDLVLGLGALRRRKRLLEQEKSLAGWALVLAGTGIGLMVLHAEMLWFGGCSWALYLFLVKCTISISTFLLLCLIVAFHAKEVQLFMTDNGLRDWRVALTGRQAAQIVLELVVCGLHPAPVRGPPCVQDLGAPLTSPQPWPGFLGQGEALLSLAMLLRLYLVPRAVLLRSGVLLNASYRSIGALNQVRFRHWFVAKLYMNTHPGRLLLGLTLGLWLTTAWVLSVAERQAVNATGHLSDTLWLIPITFLTIGYGDVVPGTMWGKIVCLCTGVMGVCCTALLVAVVARKLEFNKAEKHVHNFMMDIQYTKEMKESAARVLQEAWMFYKHTRRKESHAARRHQRKLLAAINAFRQVRLKHRKLREQVNSMVDISKMHMILYDLQQNLSSSHRALEKQIDTLAGKLDALTELLSTALGPRQLPEPSQQSK
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Forms a voltage-independent potassium channel that is activated by intracellular calcium. Activation is followed by membrane hyperpolarization which promotes calcium influx. Required for maximal calcium influx and proliferation during the reactivation of naive T-cells. Plays a role in the late stages of EGF-induced macropinocytosis.
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O15648
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PFKA_TRYBB
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ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase)
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MAVESRSRVTSKLVKAHRAMLNSVTQEDLKVDRLPGADYPNPSKKYSSRTEFRDKTDYIMYNPRPRDEPSSENPVSVSPLLCELAAARSRIHFNPTETTIGIVTCGGICPGLNDVIRSITLTGINVYNVKRVIGFRFGYWGLSKKGSQTAIELHRGRVTNIHHYGGTILGSSRGPQDPKEMVDTLERLGVNILFTVGGDGTQRGALVISQEAKRRGVDISVFGVPKTIDNDLSFSHRTFGFQTAVEKAVQAIRAAYAEAVSANYGVGVVKLMGRDSGFIAAQAAVASAQANICLVPENPISEQEVMSLLERRFCHSRSCVIIVAEGFGQDWGRGSGGYDASGNKKLIDIGVILTEKVKAFLKANKSRYPDSTVKYIDPSYMIRACPPSANDALFCATLATLAVHEAMAGATGCIIAMRHNNYILVPIKVATSVRRVLDLRGQLWRQVREITVDLGSDVRLARKLEIRRELEAINRNRDRLHEELAKL
|
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000255|HAMAP-Rule:MF_03186}.
|
O15726
|
KC1_PLAF4
|
Casein kinase I (PfCK1) (EC 2.7.11.1)
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MEIRVANKYALGKKLGSGSFGDIYVAKDIVTMEEFAVKLESTRSKHPQLLYESKLYKILGGGIGVPKVYWYGIEGDFTIMVLDLLGPSLEDLFTLCNRKFSLKTVRMTADQMLNRIEYVHSKNFIHRDIKPDNFLIGRGKKVTLIHIIDFGLAKKYRDSRSHTSYPYKEGKNLTGTARYASINTHLGIEQSRRDDIEALGYVLMYFLRGSLPWQGLKAISKKDKYDKIMEKKISTSVEVLCRNASFEFVTYLNYCRSLRFEDRPDYTYLRRLLKDLFIREGFTYDFLFDWTCVYASEKDKKKMLENKNRFDQTADQEGRDQRNN
|
Serine/threonine-protein kinase likely to be involved in many cellular processes. Phosphorylates rhoptry protein RON3, nucleosome assembly protein NAPL and DNA/RNA-binding protein ALBA4 in vitro (By similarity).
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O15743
|
SPNA_DICDI
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Protein spalten [Includes: Probable guanine nucleotide-binding protein spalten; Protein serine/threonine phosphatase spalten (EC 3.1.3.16)]
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MKKMLFMNKKEKKEEQSPAHSSLAQQHQLAQQQYQLQQQQLQLQYQQHQQQLQLAQQQKQNEQNLAQLSTSTSSNSSVNNTTNTNTNTTNSSSISSNNNNNNNTAVPILKAHDFCGTIMILGHTESGKTTLQRQLEFIYGVTDPTDAKHYQRLIYGNTLATLIRFIENSERLNITLSPDNLARVKRIQSQPVELARNRLPRFPLKLGWDCKCIWEDKVIQSVYNHSKICSEIRTPGRPKYYMDRMFKVFDPSYTPTEMDIISAYDQKDTIQSSAIIHKRFKVDLFGCSGKQSSPKNWVGLHQNYKPNYIFYVVALKDYFSDHLVATQNTDPTIVEMCNNHIHRNLLLESLNSFETLTKSELFDKSLAIYLIFNTSDIFYENIKQYDLKSCFSEYEGGNDPEKAVSFISNKFTKFLQNKDKPYKSHIVNLLDKNNVREEFEGIFDSLKIDAEKRGFTTPYNQSNSSPVSSIGSNSSRNSRLPNTSVSIPGLYSSDNDNTRLKNVNNNNNNNNNTTTYGSSTFPSSVISTTGSISNSIASAMDNDSSYSNESSPTSSMTLLPTTTTTTTTTTTTATTTDSTNNNNNNATVVIGKGKPPKEPKPVKPPKEPKPPKEPKPPKEPKPPKEPKPIKEPKEKPVKESKPPKEPKPIKEPKESKEPKEPKEPKPTKPPKEKKTSKVDGAAESKKNGADSCGNGGVGSKIKLESGFGSLQGRRKNMEDTHVILNNLMGAVTYNGPPKDIPISYYAVYDGHGGTETSTLLEPTVHNCLVNSQSFRDGDYEQAFRDAYAEADDIVIEKCEKSGSTGVSALLVGNKLYTANVGDSEIVLARAQPNANPKGPVTYEPVLLSYKHLASDDQEKKRVTDLGGMIIFNRLFGSLAVSRSFGDKEYKEGEKKFCVSDPYQTTTDLTARDHFFILACDGLWDKVEYDEAVQFVQRNIKLGKSATEISELLAQDSYDRGSGDNITVLVVILNWN
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Involved in cell-type differentiation and morphogenesis. Dephosphorylates casein in vitro. May also be involved as modulators or transducers in various transmembrane signaling systems.
|
O15770
|
GSHR_PLAF7
|
Glutathione reductase (GRase) (PfGR) (EC 1.8.1.7)
|
MYKHRYFHFFFFFFFFLVSTKIIRSFTFLNNNTNLSNPVYFKKKANMVYDLIVIGGGSGGMAAARRAARHNAKVALVEKSRLGGTCVNVGCVPKKIMFNAASVHDILENSRHYGFDTKFSFNLPLLVERRDKYIQRLNNIYRQNLSKDKVDLYEGTASFLSENRILIKGTKDNNNKDNGPLNEEILEGRNILIAVGNKPVFPPVKGIENTISSDEFFNIKESKKIGIVGSGYIAVELINVIKRLGIDSYIFARGNRILRKFDESVINVLENDMKKNNINIVTFADVVEIKKVSDKNLSIHLSDGRIYEHFDHVIYCVGRSPDTENLNLEKLNVETNNNYIVVDENQRTSVNNIYAVGDCCMVKKSKEIEDLNLLKLYNEETYLNKKENVTEDIFYNVQLTPVAINAGRLLADRLFLKKTRKTNYKLIPTVIFSHPPIGTIGLSEEAAIQIYGKENVKIYESKFTNLFFSVYDIEPELKEKTYLKLVCVGKDELIKGLHIIGLNADEIVQGFAVALKMNATKKDFDETIPIHPTAAEEFLTLQPWMK
|
Maintains high levels of reduced glutathione in the cytosol.
|
O15819
|
H33A_DICDI
|
Histone H3.3 type a (Histone 3, variant 3 type a)
|
MARTKQTARKSTGAKVPRKHIGSKQAHKQTPVSSSSGGVKKVHRFRPGTVALREIRKYQKSTDLLIRKLPFQRLVREIAQEFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIHLARRIRGERS
|
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
|
O15865
|
CDPK2_PLAFK
|
Calcium-dependent protein kinase 2 (EC 2.7.11.1) (PfCDPK2)
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MGNHLSVNKLKRKKKKKSFLNIYGKNTNENTSKQSNDYKYDINTSCISREGTTTLERKNLILCHSGKLEDKYIIDEKLGQGTYGCVYKGIDKVTNQLYAIKEEKKDRLKNINRFFQEIEIMKKLDHPNIVKLYETYENDNYIYLIMELCSGRELFDSIIENGSFTEKNAATIMKQIFSAIFYLHSLNIVHRDLKPENFLFQSENKDSLLKIIDFGLSKNLGTGEFTTTKAGTPYYVAPQVLDGKYDKKCDIWSSGVIMYTLLCGYPPFYGDTDNEVLKKVKKGEFCFYENDWGSISSDAKNLITKLLTYNPNERCTIEEALNHPWITQMTKSHEHVELSSTLLKNLKNFKKENELKKIALTIIAKHLCDVEINNLRNIFIALDVDNSGTLSSQEILDGLKKIGYQKIPPDIHQVLRDIDSNASGQIHYTDFLAATIDKQTYLKKEVCLIPFKFFDIDGNGKISVEELKRIFGRDDIENPLIDKAIDSLLQEVDLNGDGEIDFHEFMLMMSKKK
|
Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase. During male gametogenesis in the mosquito gut, required for male exflagellation, possibly by regulating male gamete exit from the host erythrocytes. Not required for asexual blood stage proliferation (By similarity).
|
O15909
|
RIR1_TRYBB
|
Ribonucleoside-diphosphate reductase large subunit (EC 1.17.4.1) (Ribonucleotide reductase R1 subunit)
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MLETVKLVTKRDGSVEPYDEKVVRSRIVNLMSGIDSYYVDVDDLVRVVGEGVREGMSTSMLDELLAETAAYCVTKHPDYGLLAGRLAVTALHKTTTESVLDSFRVLHEHVSQATKRHAPLISEELWDIANKHSAALQQIINYERDFDFEYFGYKTLERSYLLRVHKGRGVMEVVERPQQMFLRVALGIHGEDLERVKETYDYMSQGFFTHATPTLFNAGTPFPQMSSCFLVAMREDSIDGIYDTLKQCAIISKSAGGIGIHMHNIRAAGSYIAGTNGTSNGLVPMLRVWNNTARYVDQGGGKRKGAFAIYLEPWHADIFGFLLLKKNTGKEDQRARDLFYGLWIPDLFMERVESHGTWTLMDPNTAPFLSDCYGQEFTDLYERYEREGRGVRTIQAQELWFLILESQVETGVPFMLYKDACNFKSNQKNLGTIKCSNLCTEIVEYTSRDEVAVCNLASIALPRFVKDGAFDYVALKEVTKVVTRNLNRVIDRNHYPVCEARYSNLRHRPVGIGVQGLADAFALLSLPFAHPEAKKLNRQIFETIYIAAVEASTELAEKDGPYETFKGSPASEGKLQFDLWDEERRIRGMNEDSVHSHCGLWDWDSLKERVVKVGMRNSLLIAPMPTASTSQILGNNECIEPFTSNIYVRRVLSGEFPVVNKHLVKELIRLRLWNDDMRRKIIALNGSVSGIKEIPERIRELYKVVWEIRQKDLIDMAADRGRYIDQSQSLNLFLATPTSSQLTSMHFYSWKKGLKTGMYYLRSQPAADAIKFTLDPKAMKELPKPDKQSKEEVHGSVGRGKRKRVGEKPTANHSNAGAPNLNGPPDTDGDGGCLNCGS
|
Provides the precursors necessary for DNA synthesis. Catalyzes the rate limiting step in the de novo synthesis of deoxyribonucleotides by directly reducing ribonucleotides to the corresponding deoxyribonucleotides.
|
O15943
|
CADN_DROME
|
Neural-cadherin (Cadherin-N) (dN-cadherin)
|
MAARRCLNQLRQRYITNRFNICTCAIFLISLPFILAIEETTFAGLSAENAARMLAGSPGDVEKSSLSHHSEMSLVLPHDTYPGFSIKKFKTHPVKINGSSHSGAAAYHMLDTDYSKYFTVLEDGVVMTTADISPLVNRPVQLVVVEQTPNATNTHNLQLFVMHRNDMLRFSGSLLDASGEVRENQPAGTRVRGVPLMQAFSGSILDEELATPKKVRYTIIDGNVDDAFALQERKANKNIQISAKSLVINGDDESGVWLVTNRPLDREERAHYDLSVEASDVDGLDRTVSKIQITVLDENDNRPIFKSLDYKFAIAGQKSASMESNSSVTYQRFAIMGKVEATDADGDKIAYRLKSPSNVVIIVPQTGEIMLAGEPTSNELLIEVIAHDLRYPSLVSAKPAKVLLEFLAAEPVSFIMQHLEHDDINNHSHHREKRRVTRAVRPTKRIEFTEADGDTEGKSVFQLEKETDKETFKIRDDNPWVTVETNGAVRVKKKWDYEELGPEKTIDFWVIITNMGHNAGIKYTDNQRVIILVKDVNDEPPYFINRPLPMQAVVQLNAPPNTPVFTLQARDPDTDHNIHYFIVRDRTGGRFEVDERSGVVRTRGTDLFQLDMEYVLYVKAEDQNGKVDDRRFQSTPEERLSIVGGKRAPQFYMPSYEAEIPENQKKDSDIISIKAKSFADREIRYTLKAQGQGAGTFNIGPTSGIVKLAKELDFEDLRQPHVYSLIVTATEDSGGFSTSVDLTIRVTDVNDNAPKFELPDYQAHNVDEDIPLGTSILRVKAMDSDSGSNAEIEYLVSDDHFAVDSNGIIVNNKQLDADNNNAYYEFIVTAKDKGEPPKSGVATVRVYTKNKNDEEPKFSQQVYTPNVDENAGPNTLVTTVVASDKDGDNVRFGFVGGGTSSGQFVIEDITGVIRLHNKAISLDKDKYELNVTAMDDGSCCVNGDQTIHTSTAVVVVFITDVNDNKPVFKDCSTYYPKVEEGAPNGSPVIKVVATDEDKGVNGQVKYSIVQQPNQKGTKFTVDEETGEVSTNKVFDREGDDGKFVSVTVKATDQGDPSLEGVCSFTVEITDVNDNPPLFDRQKYVENVKQDASIGTNILRVSASDEDADNNGAIVYSLTAPFNPNDLEYFEIQAESGWIVLKKPLDRETYKLEAMAQDKGYPPLSRTVEVQIDVVDRANNPPVWDHTVYGPIYVKENMPVGGKVVSIKASSGIEGNPTVFYRLMPGSTAQTNKFHTFYLQQRPDNGDTWADIKVNHPLDYESIKEYNLTIRVENNGAQQLASEATVYIMLEDVNDEIPLFTEREQETVLEGEPIGTKVTQVNAIDKDGTFPNNQVYYYIVDSPRNEGKEFFEINLQSGEIFTKTVFDREKKGAYALEVEARDGAPSARPNSNGPNSVTKFIRIGIADKNDNPPYFDKSLYEAEVDENEDIQHTVLTVTAKDHDESSRIRYEITSGNIGGAFAVKNMTGAIYVAGALDYETRRRYELRLAASDNLKENYTTVIIHVKDVNDNPPVFERPTYRTQITEEDDRNLPKRVLQVTATDGDKDRPQNIVYFLTGQGIDPDNPANSKFDINRTTGEIFVLKPLDRDQPNGRPQWRFTVFAQDEGGEGLVGYADVQVNLKDINDNAPIFPQGVYFGNVTENGTAGMVVMTMTAVDYDDPNEGSNARLVYSIEKNVIEEETGSPIFEIEPDTGVIKTAVCCLDRERTPDYSIQVVAMDGGGLKGTGTASIRVKDINDMPPQFTKDEWFTEVDETDGTALPEMPILTVTVHDEDETNKFQYKVIDNSGYGADKFTMVRNNDGTGSLKIVQPLDYEDQLQSNGFRFRIQVNDKGEDNDNDKYHVAYSWVVVKLRDINDNKPHFERANVEVSVFEDTKVGTELEKFKATDPDQGGKSKVSYSIDRSSDRQRQFAINQNGSVTIQRSLDREVVPRHQVKILAIDDGSPPKTATATLTVIVQDINDNAPKFLKDYRPVLPEHVPPRKVVEILATDDDDRSKSNGPPFQFRLDPSADDIIRASFKVEQDQKGANGDGMAVISSLRSFDREQQKEYMIPIVIKDHGSPAMTGTSTLTVIIGDVNDNKMQPGSKDIFVYNYQGQSPDTPIGRVYVYDLDDWDLPDKKFYWEAMEHPRFKLDEDSGMVTMRAGTREGRYHLRFKVYDRKHTQTDIPANVTVTVREIPHEAVVNSGSVRLSGISDEDFIRVWNYRTQSMSRSKMDRFRDKLADLLNTERENVDIFSVQLKRKHPPLTDVRFSAHGSPYYKPVRLNGIVLMHREEIEKDVGINITMVGIDECLYENQMCEGSCTNSLEISPLPYMVNANKTALVGVRVDTIADCTCGARNFTKPESCRTTPCHNGGRCVDTRFGPHCSCPVGYTGPRCQQTTRSFRGNGWAWYPPLEMCDESHLSLEFITRKPDGLIIYNGPIVPPERDETLISDFIALELERGYPRLLIDFGSGTLELRVKTKKTLDDGEWHRIDLFWDTESIRMVVDFCKSAEIAEMEDGTPPEFDDMSCQARGQIPPFNEYLNVNAPLQVGGLYREQFDQSLYFWHYMPTAKGFDGCIRNLVHNSKLYDLAHPGLSRNSVAGCPQTEEVCAQTETTARCWEHGNCVGSLSEARCHCRPGWTGPACNIPTIPTTFKAQSYVKYALSFEPDRFSTQVQLRFRTREEYGELFRVSDQHNREYGILEIKDGHLHFRYNLNSLRTEEKDLWLNAIVVNDGQWHVVKVNRYGSAATLELDGGEGRRYNETFEFVGHQWLLVDKQEGVYAGGKAEYTGVRTFEVYADYQKSCLDDIRLEGKHLPLPPAMNGTQWGQATMARNLEKGCPSNKPCSNVICPDPFECVDLWNVYECTCGEGRIMSPDSKGCMDRNECLDMPCMNGATCINLEPRLRYRCICPDGFWGENCELVQEGQTLKLSMGALAAILVCLLIILILVLVFVVYNRRREAHIKYPGPDDDVRENIINYDDEGGGEDDMTAFDITPLQIPIGGPMPPELAPMKMPIMYPVMTLMPGQEPNVGMFIEEHKKRADGDPNAPPFDDLRNYAYEGGGSTAGSLSSLASGTDDEQQEYDYLGAWGPRFDKLANMYGPEAPNPHNTELEL
|
Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells cadherins may thus contribute to the sorting of heterogeneous cell types. May associate with arm neural isoform and participate in the transmission of developmental information.
|
O15945
|
ARNT_DROME
|
Aryl hydrocarbon receptor nuclear translocator homolog (dARNT) (Hypoxia-inducible factor 1-beta) (Protein tango)
|
MDEANIQDKERFASRENHCEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMKALRGTGNTSSDGTYKPSFLTDQELKHLILEAADGFLFVVSCDSGRVIYVSDSVTPVLNYTQSDWYGTSLYEHIHPDDREKIREQLSTQESQNAGRILDLKSGTVKKEGHQSSMRLSMGARRGFICRMRVGNVNPESMVSGHLNRLKQRNSLGPSRDGTNYAVVHCTGYIKNWPPTDMFPNMHMERDVDDMSSHCCLVAIGRLQVTSTAANDMSGSNNQSEFITRHAMDGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLKQKGQMFSLLYRARAKNSEYVWLRTQAYAFLNPYTDEVEYIVCTNSSGKTMHGAPLDAAAAHTPEQVQQQQQQEQHVYVQAAPGVDYARRELTPVGSATNDGMYQTHMLAMQAPTPQQQQQQQQRPGSAQTTPVGYTYDTTHSPYSAGGPSPLAKIPKSGTSPTPVAPNSWAALRPQQQQQQQQPVTEGYQYQQTSPARSPSGPTYTQLSAGNGNRQQAQPGAYQAGPPPPPNAPGMWDWQQAGGHPHPPHPTAHPHHPHAHPGGPAGAGQPQGQEFSDMLQMLDHTPTTFEDLNINMFSTPFE
|
Heterodimers of tgo/trh are involved in the control of breathless expression. Plays a role in the cellular or tissue response to oxygen deprivation.
|
O16000
|
STX1A_CAEEL
|
Syntaxin-1A homolog (Uncoordinated protein 64)
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MTKDRLSALKAAQSEDEQDDDMHMDTGNAQYMEEFFEQVEEIRGSVDIIANNVEEVKKKHSAILSNPVNDQKTKEELDELMAVIKRAANKVRGKLKLIENAIDHDEQGAGNADLRIRKTQHSTLSRRFVEVMTDYNKTQTDYRERCKGRIQRQLDIAGKQVGDEDLEEMIESGNPGVFTQGIITDTQQAKQTLADIEARHNDIMKLESSIRELHDMFMDMAMLVESQGEMVDRIEYNVEHAKEFVDRAVADTKKAVQYQSKARRKKICILVTGVILITGLIIFILFYAKVL
|
Plays a critical role in several secretory processes, including cuticle secretion and neurotransmitter release, and probably assists in neuronal membrane maturation or the final stages of neuronal differentiation. Plays a role in synaptic vesicle docking and tethering through its association with unc-18. Through binding to unc-18 mediates the release of the neurotransmitter acetylcholine from cholinergic motor neurons, and thereby promotes locomotory behaviors. Essential for embryonic viability and development. Has a role in dauer formation and adult life span. Required for locomotion. Probably by regulating neuronal transmission downstream of lin-3 and receptor lin-23 and phospholipase plc-3 and upstream of innexin unc-7 and egl-4/PKG in ALA neurons, involved in the decrease in pharyngeal pumping during the quiescent state that precedes each larval molt.
|
O16011
|
MBL_DROME
|
Protein muscleblind (Protein mindmelt)
|
MANVVNMNSLLNGKDSRWLQLEVCREFQRNKCSRQDTECKFAHPPANVEVQNGKVTACYDSIKGRCNRDKPPCKYFHPPQHLKDQLLINGRNHLALKNALMQQMGIAPGQPVISGQVPAVATNPYLTGIPANSYSPYYTTGHLVPALLGPDPVTSQLGPVVPQTVQVAQQKIPRSDRLETSPLAAHHHQQQQQLQHQLNNINNNNNHSTAGAAATSTTATTTTNNAAAAAAAAAAAAAAAVMGHHTLEVGKKRAADTTDMFPLVFFCSFPSPCVFAFLNCSIFGFLRLWFSLFNLRH
|
Required for terminal differentiation of photoreceptor cells. Vital for embryonic development.
|
O16025
|
AOSL_PLEHO
|
Allene oxide synthase-lipoxygenase protein [Includes: Allene oxide synthase (AOS) (EC 4.2.1.-) (Hydroperoxidehydrase); Arachidonate 8-lipoxygenase (EC 1.13.11.40)]
|
MTWKNFGFEIFGEKYGQEELEKRIKDEHTPPPDSPVFGGLKLKLKKEKFKTLFTLGTTLKGFRRATHTVGTGGIGEITIVNDPKFPEHEFFTAGRTFPARLRHANLKYPDDAGADARSFSIKFADSDSDGPLDIVMNTGEANIFWNSPSLEDFVPVEEGDAAEEYVYKNPYYYYNLVEALRRAPDTFAHLYYYSQVTMPFKAKDGKVRYCRYRALPGDVDIKEEDESGRLTEEEQRKIWIFSRHENEKRPDDYLRKEYVERLQKGPVNYRLQIQIHEASPDDTATIFHAGILWDKETHPWFDLAKVSIKTPLSPDVLEKTAFNIANQPASLGLLEAKSPEDYNSIGELRVAVYTWVQHLRKLKIGSLVPAGQNAIYNVEVETGDREHAGTDATITIRITGAKGRTDYLKLDKWFHNDFEAGSKEQYTVQGFDVGDIQLIELHSDGGGYWSGDPDWFVNRVIIISSTQDRVYSFPCFRWVIKDMVLFPGEATLPFNEVPAIVSEQRQKELEQRKLTYQWDYVSDDMPGNIKAKTHDDLPRDVQFTDEKSRSYQESRKAALVNLGIGSLFTMFENWDSYDDYHILYRNWILGGTPNMADRWHEDRWFGYQFLNGANPVILTRCDALPSNFPVTNEHVNASLDRGKNLDEEIKDGHIYIVDFKVLVGAKSYGGPVLEDIGYKVPDHLKHDEADIRYCAAPLALFYVNKLGHLMPIAIQINQEPGPENPIWTPHEENEHDWMMAKFWLGVAESNFHQLNTHLLRTHLTTESFALSTWRNLASAHPVFKLLQPHIYGVLAIDTIGRKELIGSGGIVDQSLSLGGGGHVTFMEKCFKEVNLQDYHLPNALKKRGVDDPSKLPGFYYRDDGLALWEAIETFIGEIIAIFYKNDDDVKRDNEIQSWIYDVHKNGWRVNPGHQDHGVPASFESREQLKEVLTSLVFTFSCQHAAVNFSQKDHYGFTPNAPAVLRHPPPKKKGEATLQSILSTLPSKSQAAKAIATVYILTKFSEDERYLGNYSATAWEDKDALDAINRFQDKLEDISKKIKQRNENLEVPYIYLLPERIPNGTAI
|
Bifunctional enzyme which is responsible for allene oxide biosynthesis via a two-step reaction first the lipoxygenase reaction that converts polyunsaturated fatty acids such as arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) into a (8R)-hydroperoxide intermediate ((8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate) followed by the allene oxide synthase reaction that converts the hydroperoxide intermediate ((8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate) into the allene oxide (8,9-epoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate). Shows preference for C20 or C22 highly polyunsaturated fatty acids and no activity with C18 fatty acids in vitro. Fatty acid allene oxides are intermediates in the formation of cyclopentenones or hydrolytic products in marine systems, most notably the prostanoid-related clavulones.
|
O16102
|
CHD3_DROME
|
Chromodomain-helicase-DNA-binding protein 3 (EC 3.6.4.12) (ATP-dependent helicase Chd3)
|
MSSKRGADPDWKTPGKASKDKRPKTNAKKQKFRDEEYCKVCSDGGDLLCCDSCPSVYHRTCLSPPLKSIPKGDWICPRCIPLPGKAEKILSWRWALDRSVELRTSKGEKRREYFIKWHGMSYWHCEWIPEGQMLLHHASMVASFQRRSDMEEPSLEELDDQDGNLHERFYRYGIKPEWLLVQRVINHSEEPNGGTMYLVKWRELSYNDSSWERESDSIPGLNQAIALYKKLRSSNKGRQRDRPAPTIDLNKKYEDQPVFLKEAGLKLHPFQIEGVSWLRYSWGQGIPTILADEMGLGKTIQTVVFLYSLFKEGHCRGPFLISVPLSTLTNWERELELWAPELYCVTYVGGKTARAVIRKHEISFEEVTTKTMRENQTQYKFNVMLTSYEFISVDAAFLGCIDWAALVVDEAHRLRSNQSKFFRILSKYRIGYKLLLTGTPLQNNLEELFHLLNFLSSGKFNDLQTFQAEFTDVSKEEQVKRLHEILEPHMLRRLKADVLKSMPPKSEFIVRVELSSMQKKFYKHILTKNFKALNQKGGGRVCSLLNIMMDLRKCCNHPYLFPSAAEEATISPSGLYEMSSLTKASGKLDLLSKMLKQLKADNHRVLLFSQMTKMLNVLEHFLEGEGYQYDRIDGSIKGDLRQKAIDRFNDPVSEHFVFLLSTRAGGLGINLATADTVIIFDSDWNPHNDVQAFSRAHRMGQKKKVMIYRFVTHNSVEERIMQVAKHKMMLTHLVVRPGMGGMTTNFSKDELEDILRFGTEDLFKDGKSEAIHYDDKAVADLLDRTNRGIEEKESWANEYLSSFKVASYATKEDHEEHDDYNNDAENTDPFYWENLMGKSQPKLPKKQKKQSQQSQVDVESIMGKGKRIRKEIDYSNQYPSPNRATPSSIVLM
|
Helicase which acts in nucleosome-remodeling by catalyzing ATP-dependent nucleosome mobilization. Likely to be involved in the regulation of transcription.
|
O16228
|
DJ12_CAEEL
|
Glutathione-independent glyoxalase DJR-1.2 (EC 4.2.1.130) (Protein DJ-1 homolog 2)
|
MAAQKSALILLPPEDAEEIEVIVTGDVLVRGGLQVLYAGSSTEPVKCAKGARIVPDVALKDVKNKTFDIIIIPGGPGCSKLAECPVIGELLKTQVKSGGLIGAICAGPTVLLAHGIVAERVTCHYTVKDKMTEGGYKYLDDNVVISDRVITSKGPGTAFEFALKIVETLEGPEKTNSLLKPLCLAK
|
Catalyzes the conversion of methylglyoxal (MG) or glyoxal (GO) to D-lactate or glycolic acid respectively in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against glyoxal-induced cell death. Protects dopaminergic neurons from glyoxal-dependent neuronal degeneration.
|
O16259
|
STIP1_CAEEL
|
Stress-induced-phosphoprotein 1 (CeSTI1) (STI1) (Hsc70/Hsp90-organizing protein) (CeHop) (Hop)
|
MTDAAIAEKDLGNAAYKQKDFEKAHVHYDKAIELDPSNITFYNNKAAVYFEEKKFAECVQFCEKAVEVGRETRADYKLIAKAMSRAGNAFQKQNDLSLAVQWFHRSLSEFRDPELVKKVKELEKQLKAAERLAYINPELAQEEKNKGNEYFKKGDYPTAMRHYNEAVKRDPENAILYSNRAACLTKLMEFQRALDDCDTCIRLDSKFIKGYIRKAACLVAMREWSKAQRAYEDALQVDPSNEEAREGVRNCLRSNDEDPEKAKERSLADPEVQEILRDPGMRMILEQMSNDPGAVREHLKNPEIFQKLMKLRDAGVIQMR
|
Plays a role in gonad development. Up-regulates longevity and thermotolerance. Binds daf-21/hsp90 and inhibits its ATPase activity.
|
O16299
|
FIGL1_CAEEL
|
Fidgetin-like protein 1 (EC 3.6.4.-) (Fidgetin homolog)
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MYSPKRVKLNVTSGMRKRPETGENNDDLYPPTALARNGISPYFIGKPRRKIVVETPSDSAQQQPPFKSRSQQNGLDDELDGIIIDEDEDRTVDVSFSQKQDTRKLKSRPFLGEKSSFKLGEIPKPKEEKRREEPFTMRGFDFGSDDKVTKIRDKICDIVDPTNARRTDPNFIRQMHENTLKGIEVASNPHFKKTRAPTKNRAAIQNTLGTLYPSFTTAAGQDPQNSKFQVPLDRQSSSQSIGSLAGIPPARRAPDIPKRCSNPLIRKAMGMDTEGGGKDEKMSGLRAEPTLKHFDENIISLIESEIMSVNNEIGWADVAGLEGAKKALREIVVLPFKRPDVFTGIRAPPKGVLLFGPPGTGKTMIGRCVASQCKATFFNISASSLTSKWVGEGEKLVRALFSVARLKLPSVIFIDEIDSLLSSRSESEHESSRRIKTEFLVQLDGVNTAPDERLLVLGATNRPQELDEAARRRFQKRLYIALPEPESRTQIVQNLLVGTRHDITNHNLERIRELTDGYSGADMRQLCTEAAMGPIRDIGDDIETIDKDDIRAVTVMDFAEAARVVRPTVDDSQLDAYAAWDKKFGCLPPPSISR
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Has a role in spindle assembly which acts in the progression through mitosis during embryogenesis. Required for fertility.
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O16305
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CALM_CAEEL
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Calmodulin (CaM)
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MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVTMMTTK
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Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
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O16374
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GALT1_CAEEL
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Beta-1,4-galactosyltransferase galt-1 (EC 2.4.1.-)
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MPRITASKIVLLIALSFCITVIYHFPIATRSSKEYDEYGNEYENVASIESDIKNVRRLLDEVPDPSQNRLQFLKLDEHAFAFSAYTDDRNGNMGYKYVRVLMFITSQDNFSCEINGRKSTDVSLYEFSENHKMKWQMFILNCKLPDGIDFNNVSSVKVIRSTTKQFVDVPIRYRIQDEKIITPDEYDYKMSICVPALFGNGYDAKRIVEFIELNTLQGIEKIYIYTNQKELDGSMKKTLKYYSDNHKITLIDYTLPFREDGVWYHGQLATVTDCLLRNTGITKYTFFNDFDEFFVPVIKSRTLFETISGLFEDPTIGSQRTALKYINAKIKSAPYSLKNIVSEKRIETRFTKCVVRPEMVFEQGIHHTSRVIQDNYKTVSHGGSLLRVYHYKDKKYCCEDESLLKKRHGDQLREKFDSVVGLLDL
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Catalyzes the transfer of beta-galactose from UDP-galactose to position 4 of alpha-1,6-linked fucose at the reducing end GlcNAc in N-glycan cores. Involved in susceptibility to the nematotoxic C.cinerea galectin Cgl2, likely by contributing to the synthesis of core alpha-1,6-fucosylated N-glycans to which Cgl2 binds.
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O16466
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ATG18_CAEEL
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Autophagy-related protein 18
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MSATTSEENPDSINYIGFNQDSKVICVGHKDGYMFYKTADILENNTLTYEGENLTHLGLNNCLIIERLFSSALMVVISQKDPRVLHVYHFTSRNIICDHRFNKSVLTVRLNRDRIVVCLEDCIYIYNLKDMKMMHNIMDTPTNKLGVLDLTSNPGNALIAYPGSTDTGSVHLFDAINLSSVSTFNAHEGTIACLKFNQEGNMIATASTKGTVIRVYSVPNGHRLFEFRRGVTRCVNIYSLCFSSDSKYLTSSSNTETVHVFKLEKTEGVDNKPEASTEGGGWFDAINKTFSAYMPSQVLQVGELMTTERSFATAKLPGAARSNQVSLVSHKNQQYVMAATSDGFVYAYRLDPEGGELDLIKQHNIGPKSDTSRASPTSTGSGGAAKSAEASNQSVPNMDDPDDFPPMSHTSG
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Component of the autophagy machinery that is recruited to phosphatidylinositols on preautophagosomal structures, which are early autophagic structures, to promote autophagosome formation, and the subsequent degradation and clearance of engulfed apoptotic cells and P-granules in somatic cells. In particular, binds with high affinity to phosphatidylinositols including phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 5-phosphate (PtdIns(5)P), and more weakly to phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Plays a role in mitophagy, which is the autophagic consumption of mitochondria, in response to dietary restriction. Involved in xenophagy, the autophagy-mediated degradation of pathogens and pathogen products, such as toxins. Also plays a role in membrane-pore repair. In a daf-18/PTEN- and daf-16/FOXO-dependent manner, required for the proliferation of germ stem cell progenitors in the gonad during the late phases of larval development. By regulating the release of neurotransmitters and neuropeptides, involved in the control of lifespan in response to dietary restriction and daf-2 signaling. Probably through its involvement in autophagy, required for dauer formation.
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O16785
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PARV_CAEEL
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Paralyzed arrest at two-fold protein 6 (Actopaxin homolog) (Parvin-like protein)
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MSTLGRSKTPSRDEPKKPGVFEKLSGTLSRKKKAPEDEHGNQGGAHHATDEDEVLELELEGREALDQSLVPVLARNIWLEEGEIRRYLTKETARDQKLAQVVDLLIYWLNEELADQRIVVRHLQEDLFDGQIIQKLLEKLEQIRIEVPEVSQSEEGQRQKLQIVVQTANRILGQPREQEKWSADLIHQKDFTAIIQLLVLLALHYRAPVRFPDNVVANVVVAQKEHGQVKTHRITEQITTVQTELAPKGTRDAFDTLFDYGPDKLAHVKTSLLAFCNKHLNKINLEVSDLDNQFQDGVFLVLLVGLLEGYFVPLYHFNLQVQSHEEKVKNVQFAFKLMEDTGLEKPRSRVQDIANGDVKSTLRLLHLLFTKYKHI
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Involved in the regulation of cell adhesion and cytoskeleton organization. Component of an integrin containing attachment complex, which is required for muscle development and maintenance. During embryonic development, required to recruit cpna-1, unc-89 and myofilaments to newly forming integrin attachments composed of integrins pat-2/pat-3, pat-4 and unc-112. Also required to reposition the integrin-based attachments so that they form the highly ordered array of dense body and M-line attachments that are characteristic of mature muscle cells. During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles.
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O16810
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ORC1_DROME
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Origin recognition complex subunit 1 (DmORC1)
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MVNKENARSVGQQVKWIGSQDELPPVKNLEHKNVYFYQKCIYGPLTLSVGDFILVSNADAAEPDTVSGCDVARILHMYELRELTDREPCRAIVQWYSWPKAIPHNKYDDDEVAIDFSLEVIEEHRPYDNDVALGAIYRKCIVLEGTSKTSAEEILKRHANKLKSTACPMFVSRYRFVKVKRSYRLIPLEIHLEQPEDNARPTRSSRKSLTAHRESKRSISARHDDTAGNKGSSVEKRRRASMAASSSVEFIDVNSFICENKVSPIKIVGGRSVVRLSEKKNAPEINANYLPASPLTEKNAKVETPKSRASAARRNLNLSLDRGADTTADSDCLNYSIVQQTPDPKTPSNDMKIKLRLSERRRSVRLASMDVDPLSLEEAVQEPNAQGRKRLGVANGDIYHTPTKKSKEPLESAAATEQTPSTRRKSILKSATSRLAEGTPRRSIHLSNIVEQRVFEDDEIISTPKRGRSKKTVQDNDEDYSPKKSVQKTPTRTRRSSTTTKTATTPSKGITTATATPMTPSQKMKKIRAGELSPSMQQRTDLPAKDSSKSELQLAREQLHVSVVPKSLPCREREFENIYAFLEGKIQDQCGGCMYVSGVPGTGKTATVTGVIRTLQRMAKQNELPAFEYLEINGMRLTEPRQAYVQIYKQLTGKTVSWEQAHALLEKRFTTPAPRRVTTVLLVDELDILCNRRQDVVYNLLDWPTKSAAKLVVVTIANTMDLPERLLMGKVTSRLGLTRLTFQPYSHKQLQEIVTARLGGSETFKGEAVQLVARKVAAVSGDARRALDICRRATEIADTAAVKCVTMLHVQQALAEMIASAKVQAIRNCSRMEQIFLQAIAAEVTRTGVEETTFMGVYQQVETIAAFMGVTFPPPGRALRLCSKLGAERLIISEHSRNDLFQKILLNVSADDIHYALRVEEMVN
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Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
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O16829
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CECC_DROME
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Cecropin-C
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MNFYKIFVFVALILAISIGQSEAGWLKKLGKRIERIGQHTRDATIQGLGIAQQAANVAATARG
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Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria.
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O16844
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COS_DROME
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Kinesin-like protein costa (Kinesin-like protein costal2)
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MEIPIQVAVRIFPHRELKDLLRSFGPTEPKKDAQAVDEGADSKDSEAQVPAAEKDNPSISETDPNGNAEQDSAADSKTIPDANGNDSGQKDYPDSAYCVQAIPISASALGLPSALPGGDPMDSIAAGLIQVGPHTVPVTHALPSSSSQEQVYHQTVFPLITLFLEGFDASVVTYGQRGQGKSYTLYGNVQDPTLTDSTEGVVQLCVRDIFSHISLHPERTYAINVGFVEICGGDVCDLLGMGNIHCTNVDAVFHWLQVGLSARQSLPAHTLFTLTLEQQWVSKEGLLQHRLSTASFSDLCGTERCGDQPPGRPLDAGLCMLEQVISTLTDPGLMYGVNGNIPYGQTTLTTLLKDSFGGRAQTLVILCVSPLEEHLPETLGNLQFAFKVQCVRNFVIMNTYSDDNTMIVQPAEPVPESNSSAGPLSQAGPGDNFGLQFAASQWSKLVTNAEGLFSKLIDSKLITEVEKEQIEEWLFLKQECEECLSSTEAMRQQKQLVPILEAEEPEDVNSEAANSESPNSDNENDTDNESHRPDLDDKIESLMEEFRDKTDALILEKHAEYLSKHPKAVMQSQDREIEAQPPEENGDDRKVSIGSRRRSVQPGASLSTAELAMLNRVASQQPPPPIDPESVVDPLESSSGEGIRQAALAAAAATAPIEQLQKKLRKLVAEIEGKQRQLREIEETIQVKQNIIAELVKNSDTRSHAKQRFHKKRAKLEAECDKAKKQLGKALVQGRDQSEIERWTTIIGHLERRLEDLSSMKHIAGESGQKVKKLQQSVGESRKQADDLQKKLRKECKLRCQMEAELAKLRESRETGKELVKAQGSPEQQGRQLKAVQARITHLNHILREKSDNLEEQPGPEQQETLRHEIRNLRGTRDLLLEERCHLDRKLKRDKVLTQKEERKLLECDEAIEAIDAAIEFKNEMITGHRSIDTSDRIQREKGEQMLMARLNRLSTEEMRTLLYKYFTKVIDLRDSSRKLELQLVQLERERDAWEWKERVLSNAVRQARLEGERNAVLLQRQHEMKLTLMLRHMAEETSASSASYGERALAPACVAPPVQASSDFDYDHFYKGGGNPSKALIKAPKPMPTGSALDKYKDKEQRSGRNIFAKFHVLTRYASAAAAGSSGSTAEESTALIESTTTATATTTSTTTTGAVGKVKDKALVSFRPEQLKRLMPAPTATKVTRQKNKIIIQDASRRN
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Regulates cubitus interruptus (ci) processing by recruiting multiple kinases to promote its efficient phosphorylation. Scaffolds multiple kinases and ci into proximity to promote its hyperphosphorylation, which then targets it for SCFSlimb/proteasome-mediated processing to generate its repressor form. Hh signaling inhibits ci phosphorylation by interfering with the cos-ci-kinases complex formation. Negatively regulates hh-signaling pathways during various processes, including photoreceptor differentiation. May negatively regulate a hh-signaling pathway which functions in the intestinal immune response to bacterial uracil by activating the Duox-dependent production of reactive oxygen species (ROS).
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O16850
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FOXO_CAEEL
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Forkhead box protein O (FOXO) (Abnormal dauer formation protein 16)
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MQLEQKSSLHCSKCRNFLQKFSQDMQAWNCRELDSPLPSDITLHNLEPARPDSGMSFSTDFDDDFFNLDLHQQERSASFGGVTQYSQQFLREKCSFSPYFHTSLETVDSGRTSLYGSNEQCGQLGGASSNGSTAMLHTPDGSNSHQTSFPSDFRMSESPDDTVSGKKTTTRRNAWGNMSYAELITTAIMASPEKRLTLAQVYEWMVQNVPYFRDKGDSNSSAGWKNSIRHNLSLHSRFMRIQNEGAGKSSWWVINPDAKPGRNPRRTRERSNTIETTTKAQLEKSRRGAKKRIKERALMGSLHSTLNGNSIAGSIQTISHDLYDDDSMQGAFDNVPSSFRPRTQSNLSIPGSSSRVSPAIGSDIYDDLEFPSWVGESVPAIPSDIVDRTDQMRIDATTHIGGVQIKQESKPIKTEPIAPPPSYHELNSVRGSCAQNPLLRNPIVPSTNFKPMPLPGAYGNYQNGGITPINWLSTSNSSPLPGIQSCGIVAAQHTVASSSALPIDLENLTLPDQPLMDTMDVDALIRHELSQAGGQHIHFDL
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Forkhead-type transcription factor. Binds to the promoters of genes that contain the daf-16/FOXO binding element (DBE), TTGTTTAC, in their regulatory region. Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway which affects lipogenesis, lifespan, starvation survival, heat shock and oxidative stress responses, sleep, associative memory, and dauer formation. Longevity signaling predominantly arises from expression in the intestine. Transcriptional activity of daf-16/FOXO is negatively regulated by interaction with host cell factor homolog hcf-1 and by cytoplasmic sequestration by association with ftt-2. Inhibition is required for the carbon dioxide (CO2) avoidance response. Upon loss of inhibition, daf-16 translocates to the nucleus to regulate genes that result in delayed reproduction and growth while increasing stress resistance starvation tolerance and longevity. Association with arginine methyltransferase prmt-1 prevents phosphorylation and allows for translocation to the nucleus and the subsequent transcription of longevity-related genes. Modulation of its activity by cGMP levels in sensory neurons regulates lifespan. Has a protective role against muscle dystrophy. Involved in mediating protection against aberrant protein aggregation proteotoxicity. Influences transcription of genes that code for proteins involved in immunity as part of a general stress response. Targets genes that inhibit and stimulate tumor growth. Targets kinases, phosphatases and transcription factors that are primarily involved in signaling and gene regulation. Thought to regulate ins-7 in FOXO-to-FOXO signaling, which coordinates daf-16 expression. Activity is positively regulated by shc-1-mediated inhibition of daf-2 and activation of JNK pathway. Through the regulation of its activity by shc-1-mediated inhibition of daf-2 and activation of JNK pathway, plays a role in maintaining the integrity of the gonad. Functions by indirect interaction with jnk-1 of the mitogen-activated protein kinase (MAPK) pathway. Involved in increased proteasome activity by activating expression of rpn-6.1 in response to proteotoxic stress, leading to enhanced assembly of the 26S proteasome, followed by higher proteasome activity. Also regulates proteasome activity in the intestine by preventing expression of deubiquitinase ubh-4. Represses transcription of natc-1. Involved in regulation of srh-234 expression. Binds to the promoter of the AMPK-gamma regulatory subunit, aakg-4, and activates its transcription. Also activates transcription of AMPK-gamma regulatory subunit, aakg-1. Maintains endoplasmic reticulum (ER) function by inducing protein degradation and elimination to remove misfolded secretory proteins from the ER independently of the ire-1/xbp-1 unfolded protein response pathway. Regulates epidermal innate immunity to nematophagous fungal infection and physical wounding which trigger bli-3 induced ROS release, leading to daf-16 activation independently of daf-2 signaling. May negatively regulate resistance to stress caused by oxidized cholesterol adducts by preventing the activation of daf-9 and nuclear hormone receptor daf-12, two members of the steroid signaling pathway. Promotes apoptosis during embryonic development. Probably through the regulation of the autophagy genes atg-18 and atg-16.2, plays a role in regulating stem cell number in the germline during larval development. Plays a role in learning and memory including associative memory, and aversive gustatory associated learning known as salt avoidance learning. Plays a role in regulating gene transcription in response to white light exposure. Binds to the promoter of dex-1 to positively regulate its expression in seam cells during the dauer phase. Plays a role in transgenerational lipid accumulation in response to a high-fat diet. [Isoform a]: Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway. May play a role in lifespan modulation, but less significant than that played by isoforms d and f. [Isoform d]: Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway. Transcript level in the early adult may play a role in lifespan modulation, but effect is more significant than that played by isoform a. [Isoform f]: Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway. Transcript level in the early adult may play a role in lifespan modulation, but effect is more significant than that played by isoform a.
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O17072
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NFYC1_CAEEL
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Nuclear transcription factor Y subunit nfyc-1 (CAAT box DNA-binding protein subunit nfyc-1)
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MSQFPEVLDNNLLHAENNETAEYIQNDGTNQSEVFMEHPYTPNMHPINMPSIVEGAVHPYNNLIHHNDAIPPAKYASMRQMTEDFWREKKQKMTEISEEDMLNKSKNMSVPMARVKKIMRIDDDVRNFMIASDAPIFMAQAAEFFIEEMTAMGWQYVSEARRRILQKADIASAVQKSDQFDFLIDFLPPKTVPTTSTNGPGHMSEDSFQDPNMHSDFHQRTSNSSVNRSHHN
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Component of sequence-specific heterotrimeric transcription factor (nfya-1-NF-Y and nfya-2-NF-Y) complexes which specifically recognize a 5'-CCAAT-3' box motif found in the promoters of its target genes to regulate their expression and control cellular identity in particular tissue types. In association with the components in the NF-Y complexes, represses the expression of the T-box transcription factor tbx-2 throughout larval development, which most likely restricts its expression to certain tissues. May act to repress txb-2 expression in conjunction with tbx-2 itself, which has an autoregulatory role (Probable). In association with the components in the nfya-1-NF-Y complex, negatively regulates the expression of the homeobox protein egl-5 to spatially restrict its expression in tissues such as the head. May regulate egl-5 expression in association with the mes-2-mes-3-mes-6 complex.
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O17087
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GLD2_CAEEL
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Poly(A) RNA polymerase gld-2 (EC 2.7.7.19) (Defective in germ line development protein 2)
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MVMAQQQKNAERNDEHTRRNRSPSVDSVSRVQQQSGGFAFYNQQSNHQYQQSHPRRTSFSRDGNTGYYNNHSGNKRQTYNNQRGGRSYNHRGNSNYQQNGEYSGNQGCVPKYHQRNQNYPQLQPKYSYFQPHQRPIFNSTQGYGTYSVRRSSPPSPSALSSSTANSTSNRAPTQPPILLRHAEPASDKNHQGSDHEQNHDPKIHLYRSAGTAPGGYTQCPSPYKQPPPQPPSTPSSSDKRIEQQQAEDWPTRFQHPPPQFRRGQDPMPASIELQHKTANQTMPVDIVQTNQQKTVSSYERAAQFRASASELPTDSVDAKHPCFANERMQSALIGISPQLKTQQQSPGIPIQNEAEASAVMKAMRSFQFHNWPQMSHGSYYPMPYHLENQMRPMKSGDQLPLNQQNHNLSGFPAFVGKSSLVGSSLNTRNSSEADPEEMPRIMEKLDDEVTGADHDKTIDENRRRIHKSQEPRIGTEEKALNELPRKANRRNSSCSSISSVSESSSPSALDESTLTKILPTDNFRGGRGFASPSPPTSLLSEPLSRMDVLSEKIWDYHNKVSQTDEMLQRKLHLRDMLYTAISPVFPLSGLYVVGSSLNGFGNNSSDMDLCLMITNKDLDQKNDAVVVLNLILSTLQYEKFVESQKLILAKVPILRINFAAPFDDITVDLNANNSVAIRNTHLLCYYSSYDWRVRPLVSVVKEWAKRKGINDANKSSFTSYSLVLMVIHFLQCGPTKVLPNLQQSYPNRFSNKVDVRTLNVTMALEEVADDIDQSLSEKTTLGELLIGFLDYYANEFNYDRDAISIRQGRRVERAALAVRPKIHSNSEGDKETPPPSSSASTSSIHNGGTPGIPMHHSISNPHFWRSQWRCVCIEEPFTNSNTAHSIYDEMVFEAIKKAFREAHGELQHNHDLDKLMECEPIKASTTNTGAAVFAATYEGERPLAQQPNTIACASLRVLNSIPVSSGPGHYHYQQQSNQNLSRPQRPGSNQGYQMNNNRGFNGNNQQQHQNRRSFNNQSSSNPGNGSTGPRSSRSNENVRDSSRQQNSQKGSSGVSVSKENVASTTGVPVDKKQQNSNRKDDGNRTKRSPMVQSPEPAKTKSEKTPMASSNVSQ
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Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. Acts as a regulator of mitosis/meiosis required for progression through meiotic prophase during oogenesis and spermatogenesis and for promotion of the entry into meiosis from the mitotic cell cycle. May act by regulating and activating gld-1 mRNA activity in germline. Required for polyadenylation of neg-1 mRNA during embryogenesis.
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O17185
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SUP9_CAEEL
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Two pore potassium channel protein sup-9 (Suppressor of unc-93 protein 9) (n2P38)
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MKRQNIRTLSLIVCTLTYLLVGAAVFDALETENEILQRKLVQRVREKLKTKYNMSNADYEILEATIVKSVPHKAGYQWKFSGAFYFATTVITTIGYGHSTPMTDAGKVFCMLYALAGIPLGLIMFQSIGERMNTFAAKLLRFIRRAAGKQPIVTSSDLIIFCTGWGGLLIFGGAFMFSSYENWTYFDAVYYCFVTLTTIGFGDYVALQKRGSLQTQPEYVFFSLVFILFGLTVISAAMNLLVLRFLTMNTEDERRDEQEAILAAQGLVRVGDPTADDDFGRLPLSDNVSLASCSCYQLPDEKLRHRHRKHTEPHGGPPTFSGMTTRPKY
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Potassium channel involved in coordination of muscle contraction. Activity is regulated by sup-18.
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O17286
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NFYB1_CAEEL
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Nuclear transcription factor Y subunit nfyb-1 (CAAT box DNA-binding protein subunit nfyb-1)
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MDPKPINEGMLLEDHDHGMPEEEEITEDDMNGIHNIEEDTRTISEIAMELHHPNKSQVLLDQERFLPIANVVRIMKTQMDPQAKLAKDAKECAQECVSEFISFIASEAAEICNITKRKTITADDLLTAMEATGFDNYAEPMRIFLQKYRQAHKITGPIHRTHPDYVRPPQFQMDPFVRPLFFDTEQGRRCTETQYVINGSEIVKNAPLGEEWNEQTGTLNTRADGYYMEEPMEPMPMEEVEIEEHEEIIEQDSLGAIALEQQGQMQIYVDPKTKQHFAAKETPNGMELYPLIIQDTPLQLENVSGPNQFVMNMPDGRAIPHGMGQEEPQPVSSSSVMRKIGQNPSSYAQQHHHVSHVEQHDDVEYEEEEEVDQVEEDTVPVPIAPRPAATRVQPKRTPTKRKK
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Component of sequence-specific heterotrimeric transcription factor (nfya-1-NF-Y and nfya-2-NF-Y) complexes which specifically recognize a 5'-CCAAT-3' box motif found in the promoters of its target genes to regulate their expression and control cellular identity in particular tissue types. In association with the components in the NF-Y complexes, represses the expression of the T-box transcription factor tbx-2 throughout larval development, which most likely restricts its expression to certain tissues. May act to repress txb-2 expression in conjunction with tbx-2 itself, which has an autoregulatory role. In association with the components in the nfya-1-NF-Y complex, negatively regulates the expression of the homeobox protein egl-5 to spatially restrict its expression in tissues such as the head. May regulate spatial egl-5 expression in association with the mes-2-mes-3-mes-6 complex.
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O17323
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HDA4_CAEEL
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Histone deacetylase 4 (EC 3.5.1.98) (CeHDA-7) (Histone deacetylase 7)
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MEEASSSTGSAGGAGPSVPNLPSTSEAAIGQTNLEPESIALLQSQLQEYRQKQMDLIGHFQRAQQELSVQHMHNLYAALQQQQQLQNLQTERSAVNPLLISQQHSTEDQNSGPAAPLSLANSLTNLLSSSNGNLSVPQTPTKEHHPTAPTSNRKCDLPRSNSTTISQLTKDRLKNMIANRSKGESNSQSNLMSNSVTANGNGHDNGRKLKNSNSQVNVSSPHFEPYRLPTSLANAHNLQQASEFQLRKVNSEPNLKMRIRAKLLSKGSSPVQHVQQNNSQFNFTHPQLKRSDSETSQNVPLDFMQSSSQTNLPHLMLPSPSLPNLAAAGAFHGLNLPVGQDLNAFMAVANLSPFLSLPSLLNKKLELGGLTDEGDRNGLIGSSSTSSLASNVSMGSHQYQSLLKQQIRDLVLRRKSLVREDPEGEGLAELYNGLLPQAKLQQLQALAAESGFLAKQEPTCTTGLGYDQAMVRHECCCGNNASHVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFAVSPTACLKIDANSLPLKRFLQLPCGGIGVDSDTYFNDASTQTAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMGFCFFNNVAVAVKVLQTKYPAQCAKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGNFFPGTGSVTEVGKNDAKGLTVNVPFSGDVMRDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGHPNALGGYEVTPEMFGYMTKSLLNYASGKVVLALEGGYDLKSISEAAQQCVQALIGESDDAGRLSSVALESLPNPSAVETLQKVIAIHKSYWPALHGQEAAINTTEMQWRNLKLQVQMQQQQQQQQT
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Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (By similarity). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By similarity). Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Involved in transduction of sensory signals, together with egl-4, kin-29 and mef-2 binding to transcription factor mef-2 enables negative modulation of chemoreceptor gene expression in chemosensory neurons. May be involved in muscle development (By similarity).
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O17386
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CED8_CAEEL
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Cell death abnormality protein 8
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MFLKKHKSKLLLVPRDEEQEDAGIVAVLTDRIPSVLLVRWFDLFCFGFAMCSYALDFFSDIGIAIFHFWAGRYLSGSLVLAFALLPSVIINIISMVWMLDDEMHWKRRAHPRRTGTFELNQKRFIPLSKMIVLCICQMGPLFWYYKALYYGWMFRKSSNENTDGEKRKCFSKMVEAERDATLLRFFEAFLESAPQLIIQGSIAASYFQNYYQTGTYPYWLYFQAASLLLSIISISWSVVVQNRSLRMIRDDKVNIWPHEAVLQFCWRFLTILARIITLVALVLIFGINVVPLISVHLLVTLVHVIFLQAIHIDACTHIEKLLLLINTFIHIFIPFNMVEGNTRWRYLTAYSVEFIEMMLVCWLLPLSLNTFPYIEKVQVGVPISFIAGIAIMMMYYQFFHPNRRQLIVTQSQEDLSLNVQKSVETLTPKLESSLEISGEQNTSQDLVSELLLDVEHEN
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Phospholipid scramblase that acts downstream of ced-9 and caspase ced-3 to promote phosphatidylserine exposure on apoptotic cell surface. Phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment. Regulates apoptosis kinetics during embryonic development. Not required for engulfment of germ cell corpses.
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O17389
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TYB_CAEEL
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Thymosin beta (Tetrathymosin beta)
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MAAVTELPKMNQELAGAVREGLELKKVETTEKNVLPTKEDVAEEKQHVERIHEIEHFDSTKLHSTPVKEKIVLPSADDIKQEKQHLELTDKINNFPSENLKKTETIEKNVLPSPTDVAREKTLQMAASFDKSALHHVETIVSTDVRVTEAQ
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Plays an important role in the organization of the cytoskeleton by regulating actin polymerization in two ways. Firstly, by binding to and sequestering actin monomers (G actin) inhibits actin polymerization. Secondly, by binding directly filamentous actin (F actin) promotes actin polymerization. Regulates the formation of cortical actin in oocytes conferring them enough rigidity to sustain the contractions during ovulation.
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O17468
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HIRA_DROME
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Protein HIRA homolog (Protein sesame) (dHIRA)
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MRLLKPAWVHHDDKQIFSVDIHKDCTKFATGGQGSDCGRVVIWNLLPVLSDKAEFDADVPKMLCQMDQHLACVNCVRWSQNGQNLASGSDDKLIMIWRKSAGSSGVFGTGGMQKNHESWKCFYTLRGHDGDVLDLAWSPNDVYLASCSIDNTVIIWDAQAFPHSVATLKGHTGLVKGVSWDPLGRFLASQSDDRSIKIWNTMNWSLSHTITEPFEECGGTTHILRLSWSPDGQYLVSAHAMNGGGPTAQIIEREGWKCDKDFVGHRKAVTCVRFHNSILSRQENDGSPSKPLQYCCLAVGSRDRSLSVWMTALQRPMVVIHELFNASILDLTWGPQECLLMACSVDGSIACLKFTEEELGKAISEEEQNAIIRKMYGKNYVNGLGKSAPVLEHPQRLLLPQGDKPTKFPLSNNNEANQRPISKQTETRTKDGKRRITPMFIPLHEDGPTSLSMNIVSSSGSSTTALTSCSAAIGTLPAAAPTESAATPLMPLEPLVSKIDLGRLDSRLKTQPASQRRQSLPFDPGQSNELLRTPRLEEHQSSTCSPSNLNVTATGKSEFVKAALDYRLHVSNGHLKTQHGMLAKVTASDSKEMLWEFYVGSPLVNLNLCEKYAMLCSLDGSMRLISMETGCPVFPAISLTSSAVHCAFSPDNSLVGVLTECGLLRIWDIAKKVVSLAAGCLELLNKHGTAAQFSVTNQGMPLIGFPSGNSYSYSTSLQSWLVLATKDAIMYHGIRGTLPRDMDQMQQKFPLLSMQASSQNYFSFTGSMELRHSESWQQCAKIRFIENQIKLCEALQSLDELQHWHKMLTFQLATHGSEKRMRVFLDDLLSMPEPGISQFVPKLELMQCVLDTLKPHSEWNRLHSEYTELLKECKSERQKDIFATPAPPQQKTASSAGSSPRSGEATGEEVTEKDGATAVAAAVVAGSRMAVTTGTSTTTTTTASSSLSSSGSSSSTSGSGSSSSSSSTSSLSVPQPAPSLSPEIQTLDSPTVCIDDEILSASSSLPPLDTSPVEVSPASTSGGAASTSPAASVAGSAPVSSSKTDQT
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Required for the periodic repression of histone gene transcription during the cell cycle (By similarity). Required for replication-independent chromatin assembly. Promotes remodeling of sperm chromatin following fertilization via the incorporation of histone H3.3 and histone H4. {ECO:0000250, ECO:0000269|PubMed:10837127, ECO:0000269|PubMed:11735001, ECO:0000269|PubMed:15988027, ECO:0000269|PubMed:16251970}.
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O17514
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MES2_CAEEL
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Histone-lysine N-methyltransferase mes-2 (EC 2.1.1.356) (E(z) homolog) (Maternal-effect sterile protein 2)
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MSNSEPSTSTPSGKTKKRGKKCETSMGKSKKSKNLPRFVKIQPIFSSEKIKETVCEQGIEECKRMLKGHFNAIKDDYDIRVKDELDTDIKDWLKDASSSVNEYRRRLQENLGEGRTIAKFSFKNCEKYEENDYKVSDSTVTWIKPDRTEEGDLMKKFRAPCSRIEVGDISPPMIYWVPIEQSVATPDQLRLTHMPYFGDGIDDGNIYEHLIDMFPDGIHGFSDNWSYVNDWILYKLCRAALKDYQGSPDVFYYTLYRLWPNKSSQREFSSAFPVLCENFAEKGFDPSSLEPWKKTKIAEGAQNLRNPTCYACLAYTCAIHGFKAEIPIEFPNGEFYNAMLPLPNNPENDGKMCSGNCWKSVTMKEVSEVLVPDSEEILQKEVKIYFMKSRIAKMPIEDGALIVNIYVFNTYIPFCEFVKKYVDEDDEESKIRSCRDAYHLMMSMAENVSARRLKMGQPSNRLSIKDRVNNFRRNQLSQEKAKRKLRHDSLRIQALRDGLDAEKLIREDDMRDSQRNSEKVRMTAVTPITACRHAGPCNATAENCACRENGVCSYMCKCDINCSQRFPGCNCAAGQCYTKACQCYRANWECNPMTCNMCKCDAIDSNIIKCRNFGMTRMIQKRTYCGPSKIAGNGLFLLEPAEKDEFITEYTGERISDDEAERRGAIYDRYQCSYIFNIETGGAIDSYKIGNLARFANHDSKNPTCYARTMVVAGEHRIGFYAKRRLEISEELTFDYSYSGEHQIAFRMVQTKERSEKPSRPKSQKLSKPMTSE
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Polycomb group (PcG) protein. Catalytic subunit of a the mes-2/mes-3/mes-6 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target genes. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. In association with the nfya-1-NF-Y complex, may play a role in repressing the expression of the homeobox protein egl-5 in tissues such as the head. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. The mes-2/mes-3/mes-6 complex may participate in the global inactivation of the X chromosomes in germline cells. This complex is required to exclude mes-4 from the inactivated X-chromosomes in germline cells. Required for small-RNA-induced H3K27 trimethylation. Involved in the negative regulation of lifespan in a germline-independent fashion.
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O17528
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TMED2_CAEEL
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Suppressor/enhancer of lin-12 protein 9
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MNSLTWILAVLFVTPAASYFIHVDANEEQCFFDRLTSGTKMGLMFEVAEGGFLDIDVKITGPDNKEIYKGERESSGKFTFAAHMDGVYTYCFGNKMSTMTPKAVMFTVEITEPHQQAPGAAANQDAADNAKLEEMVRELSSALMSVKHEQEYMEVRERVHRNINENTNSRVVMWAAFEAFVLVGMTVGQIFYLKRFFEVRTMV
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May have a role in the negative regulation of lin-12 and glp-1 transport to the cell surface. May also have a role in a quality control mechanism for endoplasmic reticulum-Golgi transport the budding of coatomer-coated and other species of coated vesicles, could bind cargo molecules to collect them into budding vesicles. Involved in regulating the expression of proteasomal subunits such as rpt-3 in order to confer resistance to proteasomal dysfunction.
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O17581
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SCC4_CAEEL
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Maternal uncoordinated protein 2 (Cohesin loading complex subunit SCC4 homolog)
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MNQDAVAKALLGMAEALRTQDPPKLKMAIKCARSTLSMEISDEMKAICNLQLGKLLFFYTDNFELAKNHLQCAYDKMSAMGTFYTRDKMNAISMLADLHIHYQQWPLTSIKATIRHEITTTRGFPALSNKLMFQLIELMKIDKDVEGAIEMCQLAINSSHADPKMELYFRIAKTLVTYQLMHEEPDISDVTRIGSMIKVMENSTTSDKAHLECIKDFYVCTKLAYMFYEGKSRTSRQLLRQIQKSQTSGETKIHGIRWLGEPSITLLACVMNQICALVQSNTDRVEKYYHLVIKHADEIIFKSTRSPQEPGVVRCINMIKMTTLEMMACCNVLACRPQKTLHNVRDMLEWSNRTSGPLLTRYFTPHIHYILGLQCCYFRQHENAENHFRAAMKKLHKEDITAHNTMALLNLNLAITYLNQLKMADYYEVSENLTAPKISSCSQMLKNNVKLLSAFFAYITNKLNECKLLSHEVLDDSKAEDFFRLHGLGLLLLSLVTDVDEKGVRPTVDWSKKSHDHVVILFSHSLYEKILLAAGYDPKSELMKMVVSEQLASRRMLSVENLTPLVANMPASKLLQWFDGDPFKLLPRDETVL
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Plays an important role in the loading of the cohesin complex on to DNA (By similarity). Forms a heterodimeric complex (also known as cohesin loading complex) with scc-2/SCC2 which mediates the loading of the cohesin complex onto chromatin (By similarity). Required for normal development until the fourth larval stage. Functions cell autonomously to guide migrations during the development of the nervous system. Participates in the guidance of mechanosensory neuron AVM by a slt-1-independent mechanism. Regulates chromosome segregation in early embryos.
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O17583
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LIN10_CAEEL
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Protein lin-10 (Abnormal cell lineage protein 10)
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MSSEAVAQATAATTSPEHGVPTSSATPTPPPSKGGGAGGGGGGEQQQVPFQMIPPGHFFANPFLNPYIPTAGAPAQEGEAQPQMVFSPAQYQEVMHHYFQQMMAASGAQFPIPFPMQFQPALQQPRPSSQASSSHRSEDDNGRQTAGSVVSSNVSPNHREVRPAEDSTETSGVVQNNDELLVPTSTSSDVTIGDVIEKSDSPENSQESAGGEEKSEEKRKLSGDRTDSLIRKQMSEMEKEITRRSQNKNIKTIDDDGLAELIGGSSTRTVADDFSPFVDKSGLSYTAPAPPSTEKSAPKESLNQLRSSFNLPDDSTTVGPVGPSTVPQQSQQFANNSMFMANAGNFVQNAFPIGVTMTPQATFGAAPGFQMMQPHQHNLFMQQPNPTFVNNGTNPFLQTQATLPNFVQNGTAPLVPTVSAQQFTPEQLAAAFAQQQIAQSAAPTPFDSPPPSMPSTSSGPSGALAPPPPPSHPIPRRVSGNGWPEENKENGTSTSTTNGAQSVPAAAGTDDPVWVLRDSYLKKMQREQRTSEEEEMSWQEAATAAQEAAENGGGDDQEEQETDRLLNGGTTGASTKGAERRGSVDKKKNSKETMVHEPAVLIEGVLFRARYLGSTQMLCESRGSKAARMAQAQEAVARVKAPEGDVQPSTEIDLFISTEKIMVLNTDLQRISDTDVRQDILMDHALRTISYIADIGDLVVLMARRMSTSHSDESCSDGDSSGGGVRKTPKVICHVFESDEASFIAQSIGQAFQVAYVEFLRANGIDDPSYLRQIDYQEVLNSQELLGDELEMFAKKETQKEVVVPKKAGEPLGIVVVESGWGSMLPTVVLAHMNPVGPAAHSNKLNIGDQIININGISLVGLPLSAAQTQIKNMKTATAVRMTVVSTPPVVEVRIRRPDTKYQLGFSVQNGVICSLLRGGIAERGGIRVGHRIIEINGTSVVAVAHDRIVNMLATAVGEIHMKTMPTSMFRLLTGQEQPQYI
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Required specifically for the determination of 3 vulval precursor cell fates P5.p, P6.p and P7.p during late second and early third larval stages required for basolateral localization of receptor tyrosine kinase let-23. Could have a general but redundant role in development, functioning in diverse cell lineages to control cell fates. Regulates the trafficking of the glr-1 subunit of AMPA-type glutamate receptors (AMPRs) in the ventral nerve cord. This may be partly through interacting with the small GTPase rab-6.2 in its active GTP-bound state.
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O17607
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RUVB1_CAEEL
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RuvB-like 1 (EC 3.6.4.12) (Pontin)
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MDMEVDEAISGTSSSRLAPIEEVKPTPKQIKRIAAHSHVKGLGIDTETQEAHYEAAGFVGQAPARTAASIVVDMIRLKCMAGRAVLIAGPPATGKTAIALAMSQELGDGVPFVPLVASEVFSNEVKKTEVLMRSFRRAIGLRVKETKDVYEGEVTELSPVEASDNSGMGKTISHLVLSLKTAKGSKQLKLDPSIYDSILKQRVEVGDVIYIEANSGIVKRVGRCDVYASEFDLEADEFVPMPKGDVRKSKDIVQNVSLHDLDIANARPQGRQGDVSNIVSQLMTPKKTEVTDRLRSEINKVVNEYIESGVAELMPGVLFIDEVHMLDVECFTYLYRALESPMAPVVVFATNRGTTTVRGLGDKAPHGIPPEMLDRLMIIPTMKYNEEDIRKILVHRTEAENVQFEEKAFDLLSKVGAEKSLRYALQLIAPARLCAQTCGREVIEVEDVDRCTKLFMDRGESLKKAEEEMRQPKNKK
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Possesses single-stranded DNA-stimulated ATPase and ATP dependent DNA helicase (3' to 5') activity suggesting a role in nuclear processes such as recombination and transcription (By similarity). May participate in several chromatin remodeling complexes that mediate the ATP-dependent exchange of histones and remodel chromatin by shifting nucleosomes (By similarity). Involvement in these complexes is likely required for transcriptional activation of selected genes and DNA repair in response to DNA damage (By similarity). Involved in the Ce-Tor signaling pathway whereby it is required for the accumulation and localization of box C/D snoRNP to nucleoli to regulate ribosomal maturation and thus protein synthesis. Antagonizes the transcriptional activity of transcription factor pha-4, to control postembryonic development and adult longevity. Has a role in pharyngeal development. Has a role in gonadal development.
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O17622
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KCY1_CAEEL
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UMP-CMP kinase 1 (EC 2.7.4.14) (Deoxycytidylate kinase 1) (CK 1) (dCMP kinase 1) (Uridine monophosphate/cytidine monophosphate kinase 1) (UMP/CMP kinase 1) (UMP/CMPK 1)
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MYNVVFVLGPPGSGKGTICTQIHENLGYVHLSAGDLLRAERERAGSEYGALIEGHIKNGSIVPVEITCALLENAMIASKDANGFLIDGFPRNEDNWSGWNKQMGGKVNEQFVLFLSCPVDVCIDRCLHRGQGRTDDNVESLKKRVETYNQSTFPIIEHFEKVGMVREVNSERPVTEVYEDVVKVFAAANQK
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Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:19645718}.
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O17645
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HST2_CAEEL
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Heparan sulfate 2-O-sulfotransferase hst-2 (Heparan sulfotransferase 2) (EC 2.8.2.-) (HS2ST1 homolog)
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MLWKKRKVLYFAGISVFILILLLLKLNSKPKANVWPTSSKIVIYNRIPKTGSTTFTNAIAYDLYKENGFSVLHVNMTKNRQVMSLPDQYTFVNNITTWTERLPAFYHGHVAFIDFQRFGIANPIYINIIREPLERLLSHYYFLRYGDNYRIGLKRSRAGNNETFDECYSRGGKDCDMKQMWIQIPYFCGHYHFCTEVGNPEALRVAKQNVLEKYLLVGTTSRMRDMIALLEVTVPDFFKGALGHFDSLDANRAHLRYTKKKIPPNDQTLSMIRRDEVYKMEREFYDFINNLFDAVFKKATNGISKADDLVKLPLQYHFEKIKPS
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Catalyzes the transfer of sulfate to the C2-position of selected hexuronic acid residues within the maturing heparan sulfate (HS). Involved in cell adhesion and guidance by specifically modifying proteoglycans in the extracellular matrix and on the cell surface that are essential for axon migrations.
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O17670
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EYA1_CAEEL
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Eyes absent homolog 1 (EC 3.1.3.48)
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MLPDSEGQKLKTFLLGTGTTLDPSLDPTGNSNFSMATTSDSSTIWTALPASQPGDKDIPTVDLAAISEAYGSTSSTTSLTSSVTSQYQYNSYPQYAMYTSANPANYYQQVTANLRAGTTAFPYSLTTPSYYGSYPVDYTSAAAAYQNPYYTNLRGGTAAPYYNPLNATTAAAYASVASSVLGTDAVNLGTSSDGSTGVPSTVTSFSLKEKKPKVSKKKKTGSCSPGDETYARVFIWDIDDIAVISRNYLASVTHTNEFYARAANSVSHLMERIALNNFADVNEFLEGDITNIEDAVVDETTMDSGPIDNLRGLDVMRRVAPKYSAFRQFYTENSTKNDVAGFKQEQNGFNFELLERVGFGAREATELYQSAIQLQTLPNFGQRWPCAQRCMDLVVEKSKLSAEKYANVVLSNDGLVLGAAQLMISGLNSSVPVENIYSISKQGKESVFEKIQSRFGKKCSFICITSGDTANSAKRLNIPVWPLNSNTDLDKLYSALDNFLLGG
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Tyrosine protein phosphatase (By similarity). Acts probably as a transcription regulator in the embryonic and postembryonic development of several tissues including pharynx, vulva and gonads. Required for the development of anterior tissues during late embryogenesis. Together with ceh-34, required to specify the coelomocyte fate in embryonic and postembryonic precursors. In the anterior part of the embryo, prevents apoptosis in cells that are not fated to die. Together with ceh-34 activates proapoptotic factor egl-1 expression to promote motor neuron M4 sister cell apoptosis. Also promotes apoptosis of I1 pharyngeal neuron sister cell. Plays a role in locomotion and fertility. May play a role in resistance to heat and oxidative stresses. May cooperate with the transcription factors vab-3 and ceh-32 to repress transcription factor ets-5 expression in non BAG neuronal cells.
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O17679
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SET6_CAEEL
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Histone-lysine N-methyltransferase set-6 (EC 2.1.1.-) (EC 2.1.1.366)
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MERSRTGGSSTYSMSTANVPIITISDDDDELTIWEEPRKSPISSNSYSDERNHSLSSTSNSSVERSIIITISDDESEATERNQQEVVDRAISNNLTEKRRRSVESFHRLHSKERKLEVKSRKKSRTSSSSMEASTSCTFPARQTKTKRHKRKTYSTISSFAPHHSTICAELRNVNPARIADFRHPSIFEYSDMSLNERREHWKKEMKVIKKHNDIRLMHEEAVRFDDIIELDPTLNGYYRRFMGAEQSTRALFMAVRCLATFGRNFYEEPERDHGEEEIPEELDRYFEKLIYVAPRTRIRITDDIHLSNDTHRIPVYTDAKGETLKTVKIPNPLLYDHIINNMVDKVKEPLLYEAIKIAGSSENVIRCKCCSQDPVVNCFDNKDCPCFIANQFLQSRNKTTDTNEKLKFHTFQPLMYNDGNPTYYNTVGFACSPKCACKGACTNNATYLIQKKLYSIEIYRADPQIGFGIRSTLFIPAGTPIIEYCGELVDGERLHSSLENYSYQLTDCEGDKHLYNLLREKYKNNPEYYDVLDELSKHHFHLDAKMQGSVGRFANHSCTPNMEPLRLFKEGFTPANMRMIFFTLKDIFPGEPLTLDYGSEYKVFRRQRCLCRTFACRSGPHYEKFSNLDGKLIASCFVRLHHASRIRYSVDLQLIERFYSVGKVEEVRVDPCVSFSKYNLKWRRQLSTATCERLENVIEIELSDEDS
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Histone methyltransferase that specifically di- and trimethylates 'Lys-9' of histone H3 (H3K9me2 and H3K9me3, respectively) involved in positively modulating the rate of age-related behavioral deterioration. May repress the expression of mitochondrial function-related genes by occupying their promoter regions, working in concert with probable chromatin reader protein, baz-2. Involved in modulation of the mitochondrial unfolded protein response (UPR). Regulates level of expression of bas-1, a serotonin (5-HT) and dopamine synthesizing enzyme (DOPA decarboxylase). Negatively modulates levels of endogenous 5-HT and dopamine with aging. Involved in modulating longevity, probably as a result of enhanced stress resistance via mechanisms related to dietary restriction and mitochondrial function.
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O17695
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HDA1_CAEEL
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Histone deacetylase 1 (EC 3.5.1.98)
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MNSNGPLMEHGKRRVAYYYDSNIGNYYYGQGHVMKPHRIRMTHHLVLNYGLYRNLEIFRPFPASFEDMTRFHSDEYMTFLKSANPDNLKSFNKQMLKFNVGEDCPLFDGLYEFCQLSSGGSLAAATKLNKQKVDIAINWMGGLHHAKKSEASGFCYTNDIVLGILELLKYHKRVLYVDIDVHHGDGVEEAFYTTDRVMTVSFHKYGDFFPGTGDLKDIGAGKGKLYSVNVPLRDGITDVSYQSIFKPIMTKVMERFDPCAVVLQCGADSLNGDRLGPFNLTLKGHGECARFFRSYNVPLMMVGGGGYTPRNVARCWTYETSIAVDKEVPNELPYNDYFEYFGPNYRLHIESSNAANENSSDMLAKLQTDVIANLEQLTFVPSVQMRPIPEDALSALNDDSLIADQANPDKRLPPQITDGMIQDDGDFYDGEREGDDRRNESDAKRAAQFESEGGEKRQKTE
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Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression. Plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in the endoderm determination possibly by repressing end-1 expression. Also involved in vulval development, possibly by repressing lag-2 expression. Required during mitochondrial stress for the activation of genes involved in the mitochondrial unfolded protein response (mtUPR), in concert with homeobox protein dve-1. Promotes normal hermaphrodite (XX) development, in concert with zinc finger protein tra-4 and nasp-1, perhaps as components of a complex. Plays a role in the regulation of longevity and mtUPR-associated innate immunity. In association with akir-1, plays a role in regulating the transcription of antimicrobial peptide genes in response to fungal infection.
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O17736
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ETC1_CAEEL
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E3 ubiquitin-protein ligase etc-1 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase)
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MIKSLNERDNFLNRLREMEHKREKDEKQEKAARKVQKFWRGHRVQHNQRLLFRAEFDAVSDRQRGLEETIKMAQLLVNFYETNKDEERLVMTLSELVKLKTSDKEFEKRIRETQRLLLARCCIKFLKNATENTIFFHIFRYLEDYVTCHSKLFEASSKLGLFNAEFHLLEALIGKPTGKTVERASLNPRILQLLTRIFETFVNPSRSTSVSVNVANRLLKTICVNITDLNFSNYILYYIKDHIKPTSPNFTNLFEAMKSVDILNNWKVRPEIAETASLRLQSIFVSQIVHVSNTQSEDVKQYFNSLAVFLEHHSKIMRSLNVKEDLSEFGRLRTSVNNHLKQYCEEMLISNEFRRAACIYANLPGVQVETIISLRKYFSQFLDLLAASNTFVEALYAFIARLCPNGEFDPIDAKSPKVNALELFCNCLNKRVSSVADSDFVPTDIFVDFDHTVEFLRDVSIKLIHLMFPTMARGDLYSGNLKEKMYKAETDWKDVTESVFSILGAIYQKDIRLKYFPEEFWTNHGREVLSGIGEHRRMPRRRMPNGRLQIERTMDTEFVERLAAIYEMDSDSENDDEDEDNNLPAVLRRAICVMKHIPFIVPFMDRVKLFTRLLNQDKEKHYTSTFGMGFNGPSVTVRRDQVYMDAFETFAPKMQGDKVNDLKSMVRVKMVNWAGMNESGIDGGGIFREFLSELLKTAFNVERGFFTFTESKLLYPNPTAPFLLGVDCLAHFQFIGRMIGKLIYERQLQEVRFAEFFIAQIFETDKNKDVDLQHMKSFDPIIFKHLKALQKMNNRELDELQLDFSVVTSDMGLVRNVNLKPNGSKFRVTVENVHEYVRLYVNYHLKQRIASMVDAVRKGISEIISIEWMRMFAPHELQIMIAGYEEVFTAKELRKFCELRFAAGTQDINYEEMFWDVIDKLSNDDKKALLKFVTGCSRAPVDGFKSIQPRMGVLVIPSSDDELPTSATCMNMLRIPKYSNRTKLEEKLRYAINSGAGFELA
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E3 ubiquitin-protein ligase that accepts ubiquitin from E2 ubiquitin-conjugating enzymes, such as ubc-18, in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Ubiquitinates ify-1 and cyb-1 targeting them for degradation in post-meiotic embryos.
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O17754
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CBPE_CAEEL
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Carboxypeptidase E (CPE) (EC 3.4.17.10) (Egg-laying defective protein 21)
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MLHAMRPVLLVAALLAVTAHAFLGFGSGSTHKDDAEWGHYHNQAQLEAKLGEINEKCPEITTLYEIGQSVEGRPLVVIQFSTTPGEHIPTKPEVKLIGNMHGNEPIGRELLLRFAETLCNGAINNDKEIVQLLNSTSIHILPSMNPDGFELALGTEPAQRQWLTGRSNINGVDLNRDFPDLDSIFYELQKIGVPKFDHLLSLFEDNVDRQPETIAVGQWTLSLPFVLSANFHEGDLVANYPFDAAIDENSQKTAYSASPDDGTFRWLAKSYADNHAHMSKNDHAPCDGTSQDAFARQGGITNGAKWYSVAGGMQDFNYLATNAMEITLELSCEKMPEGSQLPRFWEDNQKSIFEYVWKSHSGVKGMVVDAMTGEPIKRAVVWIRNGTETVPVKHPVTTWSEGDFYRVLPAGKYEIIVAAEGYDIAAKNVTVENKVRDSALVVNFALSPAADEPSENEQEQIAELVNEIARRR
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During FMRFamide-like peptide (FaRPs or FLP) and neuropeptide-like protein (NLP) precursor processing, catalyzes the removal of Arg or Lys residues from the C-terminus following the initial endoprotease cleavage. By processing neuropeptides, modulates basal acetylcholine release at the ventral cord neuromuscular junctions. Involved in egg-laying, defecation and locomotion. By processing FLP neuropeptides, regulates the turning step of male mating behavior. Involved in reducing pharyngeal pumping in response to high CO(2) levels.
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O17798
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FKPC1_CAEEL
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Furin-like protease kpc-1 (EC 3.4.21.-) (CelfurPC protein)
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MSNISWYRHCSVRLQLVTLALFLLLGSASLGSAHIDEEFEDDVTTTISSIASPMRRTYTNEWAVRIAGGKVEEANRLANKYGYTNLGPIIPGDEYYLFRDDRKKSRSSRKTRSLSANQLQHEEDVMWMEQQVAKRRVKRGYRRIRRHTDDNDIFEEDDDGTQISKSRNRKHPDPNDPLWTDMWYLNRGEHHSDSTTRMDHNVKEAWDLGYTGKGVVVTILDDGLERTHPDISPNYDERASYDVNDRDNDPMPRYEFSDENRHGTRCAGEVAAIFNNSLCIVGIAYNANIGGIRMLDGDVTDAVEAASVGHNADYIDIYSASWGPDDDGRTVDGPAKLTRSAFEKGITMGRKGKGSIFVWASGNGGKDADSCNCDGYTNSIYTLSISSATENGNIPWYSEACSSTLATTYSSGATGEKMILTTDLHHACTNMHTGTSASAPLAAGIVALALEANPNLTWRDLQHIVIRTAKPINLRAGDWTTNGVGRNVSHSFGYGLMDAGAMVKLAKIWKKVDEQHRCRQFYPSRYKNIPNGNRLQLQLYSDGCYGGADENKVSYVEHVQAIVTLKAPKRGDLQIYLTSPSGTKSTLLTKRARDTSRSGFTDWAFMTTHNWGEQAAGLWILEIDNDGWDDAELVKWELVLYGTDRETGDFGGQHASPLAVRSVQMEATSSGTQYSIFHVITLVILTFSQILY
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Furin-like protease which cleaves proproteins at the RX(K/R)R consensus motif. During neuronal development, regulates the formation and extension of dendrite branches and cellular positioning of various type of neurons. Together with chin-1 and cdc-42, plays a role in the development of the neuropil and is required for the guidance of axons from neurons, including SubL pioneer neurons and AIY interneurons, into the nerve ring. Its role in axon guidance in glia and pioneer neurons may be through ensuring the fmi-1 protein is correctly localized to the nerve ring. Promotes the formation, extension and self-avoidance of dendritic branches of PVD and FLP mechanosensory neurons. In PVD neurons, regulates plasma membrane levels of branching receptor dma-1 by targeting it to late endosomes and thus promotes normal dendrite branching and dendrite self-avoidance. Also controls dendrite extension in AIY and D-type motoneurons, dendrite branching in AQR sensory neurons and VC4/5 motoneurons, the normal number of dendritic branches in AVL neurons and the positioning of HSN and ALM/PLM neurons. Dispensable for maintaining dendrite branching in adults. Also regulates dauer-specific dendritic branching of IL2 neurons and dauer-specific nictation behavior. Under adverse environmental conditions, may promote dauer formation by processing insulin-like proteins ins-1 and ins-18, two daf-2/InsR antagonists.
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O17850
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ATX3_CAEEL
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Ataxin-3 homolog (EC 3.4.19.12) (Machado-Joseph disease-like protein)
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MSKDDPINSIFFEHQEAALCAQHALNMLLQDALYKWQDLRDLAIQMDKMEQQILGNANPTPGRSENMNESGYFSIQVLEKALETFSLKLTNIENPAMVDYKNNPLTARAYICNLREHWFVLRKFGNQWFELNSVNRGPKLLSDTYVSMFLHQVSSEGYSIFVVQGVLPRSDADDLISLCPVVPPKVTPKKEQKLEKVMTKFFNTVGKRLGGGSGAPPDSQEEKDLAIAFAMSMETKDGSEVSRSSAEIDEENLRKAIELSQAPGPSEPAEIPLLTRSRSSTPPGASEPFSNAEQQRRDRQKFLERFEKKKEERNDEK
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Acts as chain editing deubiquitinating enzyme that binds and cleaves 'Lys-48'-linked polyubiquitin chains, with a preference for chains containing four or more ubiquitin molecules thereby modulating protein degradation by the ubiquitin-proteasome pathway. Probably by regulating the IGF-1-insulin-like pathway, regulates lifespan. Regulates germline DNA double-strand-break repair and apoptosis in response to DNA damage by recruiting E4 ubiquitin-protein ligase ufd-2 to DNA repair foci. Interacts with key regulators of transcription and represses transcription (By similarity). Acts as a histone-binding protein that regulates transcription (By similarity).
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O17894
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HM35_CAEEL
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Homeobox protein unc-39 (Homeobox protein ceh-35) (Uncoordinated protein 39)
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MTDHPPIDTSSYFDCYQQHQLPLQYTFTSSSNSNTSNSSTSPSHISDQFSSSGGPPYELSSHILTPSSVIPTPSPSVASASISSPTIPAFGCTMSEYSMEQMEAISTSLFQARDGDRLVAFFKQLESLYGPNAVDHLRSEAIIVAYTYALYHSNEFETLFHLLSNRHFQQRHYNDLQDIWHHARYKESQLKRGKELNPVEKYRLRRKFPAPKTIWDGEEIVYSFKDSSRKFLKQFFRNVSEYPTQEQKREISRATGLKIVQISNWFKNRRQRDKSNNSAKCSPPSSSSSTNGGSDFLPIITPQSFNLAAAPFNMNMIYGTLRDSQSDNDQFTFNP
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Probable transcription factor required for differentiation and migration of neuronal cells, such as RID and CAN neurons. Specifically, plays a role in the terminal differentiation of RID peptidergic neurons. Also required for CAN neuron axon guidance.
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O17966
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TOP1_CAEEL
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DNA topoisomerase 1 (EC 5.6.2.1) (DNA topoisomerase I) (topoI)
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MSVVSNHHSNGNGNSTVYDTNGNDEIKKEVKDEPMASDSEVPFGELMKRDKKEKKQKKRKAESGSDEDDYKPEKRKSSAKNGKKKDVGSDSEDDYKPEKKKSKKNNKKKAQESSEDDDEESEGDVSEEDVKPQIHSDDELEEEDEAPTTDDEEEQKRKEKERRKKEKREKKERKEKKRLEKENRKIKEEDDEDSDDEDDEKAKKKKRKSKGAEKSKPSTSKKDAGGKKEPPKKKVKKEEDIEDIWEWWKEEKKPAGVKWNSLQHCGPLFAPPYIPLPSHVHFKYGGEKMKLTLETEEIAQFYAGVLDHEYSTKEAFNKNFMKDWRKVMTVEERERIHDLKKCDFRAIDAYQKEQREIRKAMTKEEKLKIKEEKEAEVKIYGIAIIDGHRQKVANFRIEPPGVFRGRGGHPKMGLIKKRIMPEDVIINCGKDTEIPKPPPGHKWKEVRHDNTVTWLCSWTESVLGQNKYIMLNPSSKIKGEKDFEKYETARRLKKKIGGIRERYTDDFKSKEMRVRQRATALYFIDKLALRAGNEKDVDEAADTVGCCSLRVEHIKLFDSAKLNEDDKKEKEFVVEFDFLGKDSIRYFNRVSVEKRVYKNLKIFMEGKAPSDDLFDRLDTATLNDHLRSLMDGLTVKVFRTYNASITLQEQLIKLTNPKDNVAAKILSYNRANRQVAILCNHQRAVSKGFDESMQKLEQKIKDKKKEVKEAEAALKSARGAEKEKAQKKYDRLKEQLKKLKISRTDKDENKQIALGTSKLNYIDPRITVAWCKKFEVPLEKVFTKTHREKFRWAIDMTNSSDEEYVF
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Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Required for normal spermatogenesis and oogenesis.
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O17972
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NPHP1_CAEEL
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Nephrocystin-1-like protein (Nephronophthisis homolog)
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MSIFGSILSLQDAINRFPQFEYQINRLEKEQKDTEAASRASFRKHFVRQCQELHRQLDDHRNRIEKAKTDETYKKENALEQLDKLKQRLTALSPEKEQLSFSVSVDSQSEEEKPKMAAIGRRKSTMYNDDESEDSDNDSEIIETDVQLDDPLPSQPQPPQQQHQQPQPKPRQPITITKPLESKTLNERQELDEVISRLQNPSRGDSGEVMEPVVVRGNVFVAIDSWDAEAEGDLELIKGKKYRITQTRSDGWWTALDEYGQRGLVPKTYLQHVKEKPKNVPSKVSSRLGVRDSVIGISTTTDPSRREANRQASRVDDCLGKAYDNDTHLSLVCHMAPRLSTSNIGFHDLFWSHYKDQVYKRTVHISKIIRLVRFEKMPLIEHKALVRMALVDITNPKSTQIVSNVHTLVPRVKSSTWYFEKKESQTRSCIEFSDFVLRSNYRSPTVVLVVEASHLVKTQIGIEEKSLGHTYLRLIIDDKAVPSRTNVLYLDDEVMTKMKLPEASKRRVLVQVMDVPKDKVSYVDSLPDVIVFNALYLPFFHFYRRRAGTILIRDNRNPLSAEFISDPLLSVFPFVCDQHDIMDIMLKIWKTKKKVLAKKNEAEQTAEFFQTFLHTAFFIHGIRMISYDVKDDLTLSIRQQTMQRFVDALNKGLFKQFIADQQCKPINIIDYSLDLLGNHSID
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Plays a role in the extension of dendrites from phasmid ciliated sensory neurons. May be necessary for initial assembly of the cilium.
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O18017
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BLM_CAEEL
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RecQ-like DNA helicase blm-1 (EC 3.6.4.12) (Bloom syndrome protein homolog) (High incidence of males protein 6) (RecQ helicase homolog)
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MIKNREIEVAPPRRTIQFGGYTFVEPDLNFKAPIFSCCGSIRDPSCEEREEEYIDNGHDEEPPVEVNRIQESTSFDEPVSSPPRYRPSENPGPSSSSYEPGHYSFNEYQQFPSRPQKRLVDPPIVDLDEEPPIVDLDDSFDNFHVGSTSEEVVSGDIAPEEEEEEGHDSFDDFESVPAQPPSKNTLASLQKSDSEIALNQQRHDMHGRFRGFLQDDSEEFSDEVGLLGADMNKELYDTLKSKFGFNQFRHRQKQCILSTLMGHDTFVLMPTGAGKSLCYQLPAVILPGVTVVVSPLRSLIEDQKMKMKELGIGCEALTADLGAPAQEKIYAELGSGNPSIKLLYVTPEKISASGRLNSVFFDLHRRGLLARFVIDEAHCVSQWGHDFRPDYTKLSSLREKYANPPVPIIALTATATPKIVTDARDHLKMQNSKLFISSFVRDNLKYDLIPKAARSLINVVEKMKQLYPGKSGIVYCLSRKECETVQMMLTKAGLSAEVYHAGLNDNLRVSVQRSWIANKFDVICATIAFGMGIDKPDVRFVIHYSLPKSIEGYYQETGRAGRDGMPSYCLMLYSYHDSIRLRRMIEEGNTTTGVRSMHLNNVLQVVAYCENVSVCRRKMLVEHFGEVYDEQSCRNSKTPCDICERQRKNAEAIRLFDVSTDALSILKCLPRMQKATLKYISELYRGALIKKSQEQAMRLGHTKLPFYSKGQGMSEQDALRFVRKLVIEGYIHERLYSVPNQAAAVFAYAELTEAGRDLANGKKTAKVYLHIVTCERKRKNAGLIELSNMNIVSEAQALKERHMVKHGDVFTRCLQDLTHLITAVAESSGLSGPYSIVSREGIEQIAALLPRTNSDLLRIDSMTQIKVTKYGRLIMELLATYWKQVDEREEEEMRNQLDKLKSGEIVMGGFATLQSDPGFPSVPYMKPLGGGGGCRGRGKKRAFSGFSSGRATKKPRATAPSARGKTSGRGGAKPATSLKRNMYPATSM
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Component of the BTR double Holliday Junction dissolution complex, which is involved in homologous recombination during meiotic double strand break in the germline (Probable). Stabilizes and positively regulates the localization of the BTR double Holliday Junction dissolution complex component rmh-1 at nuclear foci during meiotic recombination. Participates in DNA replication and repair (By similarity). Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction (By similarity). Negatively regulates sister chromatid exchange (SCE). ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction. Participates in DNA replication and repair. Negatively regulates sister chromatid exchange (SCE). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction.
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O18158
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OGT1_CAEEL
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UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase (EC 2.4.1.255) (O-GlcNAc) (OGT)
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MEKPNYFQSYNKVIGATGEQLAPGAVPPHPVLAPSIAPGGVAGVSAANMANIMQTPGFANLVQQAIRTQLENQAAQQLAVNQQFQLNGATAVQQQLLLTPQQSLAQPIALAPQPTVVLNGVSETLKKVTELAHRQFQSGNYVEAEKYCNLVFQSDPNNLPTLLLLSAINFQTKNLEKSMQYSMLAIKVNNQCAEAYSNLGNYYKEKGQLQDALENYKLAVKLKPEFIDAYINLAAALVSGGDLEQAVTAYFNALQINPDLYCVRSDLGNLLKAMGRLEEAKVCYLKAIETQPQFAVAWSNLGCVFNSQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVSAYLRALNLSGNHAVVHGNLACVYYEQGLIDLAIDTYKKAIDLQPHFPDAYCNLANALKEKGSVVEAEQMYMKALELCPTHADSQNNLANIKREQGKIEDATRLYLKALEIYPEFAAAHSNLASILQQQGKLNDAILHYKEAIRIAPTFADAYSNMGNTLKEMGDSSAAIACYNRAIQINPAFADAHSNLASIHKDAGNMAEAIQSYSTALKLKPDFPDAYCNLAHCHQIICDWNDYDKRVRKLVQIVEDQLCKKRLPSVHPHHSMLYPLSHAARIAIAAKHASLCFDKVHVQMLGKTPLIHADRFSVQNGQRLRIGYVSSDFGNHPTSHLMQSIPGMHDRSRVEVFCYALSVNDGTNFRSKLMNESEHFVDLSQIPCNGKAAEKIAQDGIHILINMNGYTKGARNEIFALRPAPIQVMWLGYPSTSGATFMDYIITDAVTSPLRLANAFTEKLAYMPHTFFIGDHAQMLRHLTDKVVVKDKETTERDSCLIMNTANMDPILAKSEIKEQVLDTEVVSGPNKELVRAEMVLPVLEVPTEPIKQMIMTGQMTMNVMEDMNVQNGLGQSQMHHKAATGEEIPNSVLLTSRAQYQLPDDAIVFCNFNQLYKIDPSTLDMWIKILENVPKSILWLLRFPYQGEEHIRKYCVERGLDPSRIVFSNVAAKEEHVRRGQLADVCLDTPLCNGHTTGMDILWTGTPMVTMPLESLASRVATSQLYALGVPELVAKTRQEYVSIAVRLGTDADHLANMRAKVWMARTSSTLFDVKQYCHDMEDLLGQMWKRYESGMPIDHITNNTETPHGL
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Addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine.
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O18178
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2A51_CAEEL
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Serine/threonine-protein phosphatase 2A regulatory subunit pptr-1 (Serine/threonine-protein phosphatase 2A 56kDa regulatory subunit pptr-1) (Serine/threonine-protein phosphatase 2A regulatory subunit B' pptr-1)
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MHGSGHSLTGAPHQIPPPRTQGAATGGQQLSATANQFVDKIDPFHNKRGTSRRLRINNSSRYNVDSAQELVQLALIKDTAANEQPALVIEKLVQCQHVFDFYDPVAQLKCKEIKRAALNELIDHITSTKGAIVETIYPAVIKMVAKNIFRVLPPSENCEFDPEEDEPTLEVSWPHLQLVYELFLRFLESPDFQASIGKKYIDQRFVLKLLDLFDSEDPRERDFLKTVLHRIYGKFLGLRAFIRKHINNMFLRFVYETDSFNGVGELLEILGSIINGFALPLKQEHKVFLVKVLLPLHKPKCLSLYHAQLAYCVVQFIEKDSSLTPQVFEALLKFWPRTCSSKEVMFLGEVEEILDIIEPEQFKKIIDPLFRQLAKCVSSPHFQVAERALYFWNNEYILSLIEDTSSLVMPIMFPALYRISKEHWNQTIVALVYNVLKTFMEMNGKLFDELTSTYKGERLREKQREKDRDAFWKKMEALELNPPAEGKEVTPSLFPEKLTDYLKKDGPNMTPLPVATAGGGDKSPSVVKKSSTGSETTTPAKK
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Probable regulatory subunit of serine/threonine-protein phosphatase let-92 which negatively regulates the insulin receptor signaling cascade composed of daf-2, age-1, akt-1, akt-2 and sgk-1 by promoting the dephosphorylation of akt-1 on 'Thr-350'. Negatively regulates several functions controlled by the insulin pathway including dauer formation, lifespan, fat storage and stress resistance. Plays a role in the asymmetric segregation of the P granule components during embryonic cell divisions but does not play an essential role in specifying germ cell fate. Within a PP2A phosphatase complex, acts redundantly with pptr-2, to dephosphorylate P granule components including meg-1 and meg-3 to promote the assembly and accumulation of zygotic P granules in the posterior cytoplasm during zygote polarization, and thus maintain P granule distribution and segregation in early stage embryos following meiosis. In adults, required to promote germ cell proliferation and differentiation when exposed to thermic stress.
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O18191
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APC1_CAEEL
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Anaphase-promoting complex subunit 1 (APC1) (Metaphase-to-anaphase transition protein 2)
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MRKYVLFFISGNNDSQIWATTPNTPRVIARGGLERNIHTRTLARMVNEDAPGTSTPAAQSRLQTTASPFHRTHLTQMCRRGDTNASLLRDFTRMIRDTPRNFSKNTQHGNDRDFGDLERDPDVDLLLSKVCLECVYVEPKEGAIPKANKIFISNFLSDMYINLVSVTGEVMKIIPIWKNAETTRKNLLEKGKHEPCVVDCVDAAFVMKSGITVVLGSDFTTAMFGGNERIAPIFIKEMSNQRVGRKFRLFSFAENRIFAVNEMRCIVVEIPETVTCKSATELMRTCFLHLDRDLSRKLLIKWRSVKRDVDTERLDLDRKEMIDVAIFMLDNVGVRVTNVVAQERADSPEGHGGKQMRPRMSDSEVLSMMRQFFEEMTFRPKSEVITEDGYKCHLSVELDPNGEGFVHTQDLLHAFHSQCEDWSINTMMHSILLELIPYAYLLAKVMNYRAFEEYYVQLFKHLLSQIAIEFKIPPEIHEKFVGAIHIPKPCWSLNNVIAHIICERTTPETMESIPKFISKSSVRLLTILAVGRKFIGMGTNIDMDCERWLGKDWKRRIGLSGDILKSFRRIMNGKSSNSAGRASQLIELFEIGSITIDFMVLAVKVLMLKFQTDAFAGAQSIEPKKCIYATADEMISIAHLRWKNDIRMHNVQLMLNSSRPILIATNILRKNEDDNMKELQDRFLTQTSYRTFSQPFGRAFLDFRTAVPSLLTSIYIPRLNVGGMIYPSRVTCDPPTTEIFKLCTEWGNFYNSLASALRIGSSETVRIDNEWIVMVSKNIKSTAVIGGMTLGFGLNGHLAPFNMYHAHQMLSTFDKFHSVALLIGLSASNFTTCDVQIHKILATYLSFLMGPTPLEIKLDFTIQTAAISGLGLLFADSGNMTIAKKLVNEIGRAPNRDEEPVTDRNAYKLSAGFSLGLIMLGKGNGSASTVIPFKQNIPPMSQRLIYMMNGMRRDKCVFLPQVAPPVVNDVPNLPFSNGGMMTSSQVANHVKESEYINIHQSAEPAAIALGMMFMKMNNEFIANALALPGTITELERLKPDSMYSRVLAQCLVMWDSIEPTHDFVKSLIPPVIREYATAALHFGVPIRRDEDGEEVHEAINDAEEKYWAEIVDKGTVSQTFLYAVSAACMAIALKFSSCGGPNEKNIVNTAFRIIEYYTKIVMPDGKSNKDMGSIRMCIYSGAYTRTSCLSMLITAMAILRVGTGDLEVMRYARLLRLCDKPESDWIATGKKHFEQMVAHQALGILMLGEGRYAFKKDDLSIALTIISTFPTIPQSVSDNSHYHQPLRFLWSMAVEPRLLVPFDIAESCVVEVDVTIVMKPKDGNEPIVYKEKAPYLLPPLEDLQSISIGGGNYQLVHISLQSEDQVKVMKDIMTIGQGRVMLKRYGVDSSEMKIKEATTLYDDTPSLMSMFNNEDTAVELDEYEIQCMMEKIDEGINLNSSDEYPNVQIELSCVRDVTERTTMDLAQLQKRSLKLLSESLDLWQDEVNVSNTINGLADAVQDMQI
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Probable component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins. Developmental role in early embryogenesis and the metaphase to anaphase transition in oocyte and spermatocyte meiosis and mitosis in germ cells. Required for embryonic anterior-posterior axis formation. Plays a role in regulating the abundance of glr-1 receptors in postmitotic neurons, which may in turn control animal locomotion. Involved in regulating GABA neurotransmitter release at neuromuscular junctions in GABA motor neurons.
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O18195
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WASH1_CAEEL
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WASH complex subunit homolog 1
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MYHVPLIPRDAGREETIFRINQSLQKLLRVSDEIFDRVEHRITRIHGKAEAIDRRTEVLEKKLESLQESDKVITFTLPRQLPKLPEEPPTSTSLFRINIDTEHFPGSEELPAFRRADDHVLRPCEPIDFTYELNKPDKFFLTSQVLKEYEQKGWERYKKRLLGGLRELSRSPEHIAELFYAGTSIPAFEGVSGDFSKKALDADDDGGTSRSGRTTDELAQLRLHEQLLEDTALSSTLMQEDSLDDNHPLAFRINFNEKKKKTAKMVEMPDSLPNLKGHAHDFTLRDPEIDEDRLLDILPADDQIPEASEPTEAEADAPTTFILPPPPPPMKLDPSPQPAATPVEITEIPPIISPPAPPPPPPPPPPPPPPQTPSASSSVTFSPTKSVDGGRSDLMAAIRAAGGAGNAKLSRIAEKPKRKGKFDGILESSALLGASETPRNSAPAPDGGGGGGDLMSALSKALDARRKAINGKVEAQPPAKVSSTIPAPPNFDDEEWD
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Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (By similarity). Acts as a component of the DHIC (ddl-1-containing hsf-1 inhibitory complex) which modulates lifespan by sequestering the heat shock transcription factor hsf-1 to negatively regulate its binding to DNA and its transcriptional activity.
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O18209
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PMY13_CAEEL
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Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase wee-1.3 (EC 2.7.11.1) (Lethal protein 37) (Myt1 kinase)
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MDDTEGNSSMDSIRNGQSSPLPQVTPRLPQIPMMMRETPLSTKRERQAITPRFRRPAPKMIKTMPPTRSIWSVRKESVPLLVTPQGPKPLESPKYDHTNAQSFFEQVFQIDEIIGRGSFGEVFAARCREDSQLYAVKVSLAPIRQHSISKYREAESHMIIPPHKNLVKFYRAWEETGRLYIQTELCDQSLLKYCTEKHALPEDEIWNIFVDLLQAVHHLHSNDMIHDDIKPENIFLTKDMICKLGDFGLVINLKNPNDVKSAEEGDSKYLAPEVLNGRPTKSSDIFSLGMTILEATTDLDVPSNGDSWHQIRNGQIPDRFFAGISTDLRSLIALMLDSDPRIRPTSRDLLDHPVIKKKLMKRGTYVKCISILNGFFYAFSAVLVWVMAFFSVLFHPIVRFHAAIKDRQSEICAQFVNNQQHTPIQTPETSKVYLESLTGVAVRQASQIVSPFDFSDDENPPNAQRRLFTGAVPCRLNFDNDQDDDEEQATCSSSNSSAIEPQLDEPESPPRMNDVIDKLGKRGTPRSARRNLTFNRHRQVAASVAPKSSLNHYNHHTGSGDGFSNNSLIPISDQERTEKYLRMRLTEQQLDWADQNNVIDEAPPPMSCPPRIRRSIRDLPRMPVLNFNVLDEPSNKPTVDHHTILEQSESPRRRLNRGAKPVPRNRMMSFGSSGDEV
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Acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylation of the CDK1 kinase during oocyte maturation. Required for oocyte maturation, embryonic development, germline proliferation and initiation of meiosis during spermatogenesis. Required for chromosome structure during mitosis and negative regulation of nuclear envelope breakdown.
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O18214
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MAB3_CAEEL
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Protein male abnormal 3
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MLTEDPVSEICEAKAVDELAEQEKNYYCQRCLNHGELKPRKGHKPDCRYLKCPCRECTMVEQRRQLNNLLSKKKIHCTPATQTRDGKRVRDPHCARCSAHGVLVPLRGHKRTMCQFVTCECTLCTLVEHRRNLMAAQIKLRRSQQKSRDGKEPKRNSRRKSKDMDMEMMVVTATDGQKIIGTSASPSPSSTTDTMSPSLSMSPPCSPSPLLAQYTLTLAAPIPIYPPIPMNQQLISLQQQQFLMSIIQNMAPSIGQQAPLLPGISAGSVSSAAILNEFWSMYLKNYGLQA
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Transcription factor which binds the DNA motif 5'-[CGA][TCA][TA]ACAATGT[AT][TGA]C-3', probably as a monomer. Acts partially redundantly with the transcription factor dmd-3 to coordinate tail tip cell fusion and retraction and thereby regulate male tail tip morphogenesis. Promotes male-specific development of two tissues, the peripheral nervous system and the intestine. In the peripheral nervous system, directs differentiation of sensory ray neuroblasts into peripheral sense organs. In the intestine, causes repression of vitellogenin gene transcription.
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O18276
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GBRB_CAEEL
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Gamma-aminobutyric acid receptor subunit beta (GABA(A) receptor subunit beta)
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MRRSKTRRIFHVSITLLLVSTIFCQNGTKPHNNSTSDQMSSSWSNRSQTMYSNASSLLSDLLLDYDIRLRPGFGGDALLLTMDIIIASFDSISEVDMDYTLTMYLHQYWTDERLRWSNEIPIDEMTLSGEFSQNIWVPDTFLANDKHSYLHEVTERNKMLRINVDGKVAYGMRLTSTLSCSMNLRNFPLDSQNCTVEIESYGYTTSEVLMKWNYPLAVHGVEQADVPQFTITGFHTEDSIVSTATGSYQRLSLVFQLRRSVGYFIFQTYLPCVLIVMLSWVSFWINHEATSARVALGITTVLTMTTISTGVRQSLPRISYVKSIDIYLVMCFVFVFAALLEYAAVNYSYWGRERGKGGGGNEWPVNGANKEDRESAVNVQKWVPSGLMDGVPQPQDRRVEALEEAMSTSNTAAQNNNFESTSKPKKRSSSPIPPLCRAGNTISEESESPDYPRYSTTSLKGARPHASLNHKTHHLKGRSSARAKRRMTLARMNVSMKQSISGIGRRARKVIPTIRVRDVNLIDKYSRVVFPVCFIVFNLFYWSYYMMVPS
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GABA, an inhibitory neurotransmitter, mediates neuronal inhibition by binding to the GABA receptor and opening an integral chloride channel. {ECO:0000250, ECO:0000269|PubMed:12421359}.
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O18330
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MRJP1_APIME
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Major royal jelly protein 1 (MRJP-1) (MRJP1) (56-kDa protein 4) (p56kP-4) (Apalbumin 1) (Apisin subunit MRJP1) (Bee-milk protein) (Royalactin) [Cleaved into: Jellein-1 (Jelleine-I); Jellein-2 (Jelleine-II); Jellein-4 (Jelleine-IV)]
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MTRLFMLVCLGIVCQGTTGNILRGESLNKSLPILHEWKFFDYDFGSDERRQDAILSGEYDYKNNYPSDIDQWHDKIFVTMLRYNGVPSSLNVISKKVGDGGPLLQPYPDWSFAKYDDCSGIVSASKLAIDKCDRLWVLDSGLVNNTQPMCSPKLLTFDLTTSQLLKQVEIPHDVAVNATTGKGRLSSLAVQSLDCNTNSDTMVYIADEKGEGLIVYHNSDDSFHRLTSNTFDYDPKFTKMTIDGESYTAQDGISGMALSPMTNNLYYSPVASTSLYYVNTEQFRTSDYQQNDIHYEGVQNILDTQSSAKVVSKSGVLFFGLVGDSALGCWNEHRTLERHNIRTVAQSDETLQMIASMKIKEALPHVPIFDRYINREYILVLSNKMQKMVNNDFNFDDVNFRIMNANVNELILNTRCENPDNDRTPFKISIHL
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[Major royal jelly protein 1]: Induces the differentiation of honeybee larvae into queens through an Egfr-mediated signaling pathway. Promotes body size increase by activating p70 S6 kinase, stimulates ovary development by augmenting the titer of vitellogenin (Vg) and juvenile hormone, and reduces developmental time by increasing the activity of mitogen-activated protein kinase and inducing the 20-hydroxyecdysone protein (20E). Most abundant protein found in the royal jelly which is the food of the queen honey bee larva. The royal jelly determines the development of the young larvae and is responsible for the high reproductive ability of the honeybee queen. [Jellein-1]: Has antibacterial activity against the Gram-positive bacteria S.aureus ATCC 6535, S.saprophyticus and B.subtilis CCT2471, and the Gram-negative bacteria E.coli CCT1371, E.cloacae ATCC 23355, K.pneumoniae ATCC 13883 and P.aeruginosa ATCC 27853, and antifungal activity against C.albicans. Lack cytolytic activity and does not induce rat peritoneal mast cell degranulation. [Jellein-2]: Has antibacterial activity against the Gram-positive bacteria S.aureus ATCC 6535, S.saprophyticus and B.subtilis CCT2471, and the Gram-negative bacteria E.coli CCT1371, E.cloacae ATCC 23355, K.pneumoniae ATCC 13883 and P.aeruginosa ATCC 27853, and antifungal activity against C.albicans. Lack cytolytic activity and does not induce rat peritoneal mast cell degranulation.
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O18334
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RAB6_DROME
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Ras-related protein Rab6 (Protein warthog)
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MSSGDFGNPLRKFKLVFLGEQSVGKTSLITRFMYDSFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSTVAVVVYDITNTNSFHQTSKWIDDVRTERGSDVIIMLVGNKTDLSDKRQVSTEEGERKAKELNVMFIETSAKAGYNVKQLFRRVAAALPGMDSTENKPSEDMQEVVLKDSPNETKDPEGGCAC
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Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Mediates membrane trafficking during egg chamber growth and organization, possibly upstream of exocyst component Sec5. Also during oogenesis, plays a role, together with BicD but independently of Sec5, in the polarization of the oocyte microtubule cytoskeleton, in the localization of oskar mRNA and in the anterodorsal secretion of grk. Required for anterograde opsin transport through the ER-Golgi complex. Plays a role, together with Rich, in regulating CadN transport in photoreceptor cells which is required for the formation of normal synaptic connections between axons from the inner photoreceptor cells in the eye and postsynaptic cells in the brain medulla layer M6. Necessary for proper development of bristle shafts of macrochaete and microchaete on the head, thorax and scutellum. Modulates Notch signaling. As a key regulator of vesicular traffic, plays a critical role in the regulation of actin organization and is required for normal rates of phagocytic uptake during phagocytosis involved in defense against viral and fungal infection.
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O18381
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PAX6_DROME
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Paired box protein Pax-6 (Protein eyeless)
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MRNLPCLGTAGGSGLGGIAGKPSPTMEAVEASTASHRHSTSSYFATTYYHLTDDECHSGVNQLGGVFVGGRPLPDSTRQKIVELAHSGARPCDISRILQVSNGCVSKILGRYYETGSIRPRAIGGSKPRVATAEVVSKISQYKRECPSIFAWEIRDRLLQENVCTNDNIPSVSSINRVLRNLAAQKEQQSTGSGSSSTSAGNSISAKVSVSIGGNVSNVASGSRGTLSSSTDLMQTATPLNSSESGGASNSGEGSEQEAIYEKLRLLNTQHAAGPGPLEPARAAPLVGQSPNHLGTRSSHPQLVHGNHQALQQHQQQSWPPRHYSGSWYPTSLSEIPISSAPNIASVTAYASGPSLAHSLSPPNDIESLASIGHQRNCPVATEDIHLKKELDGHQSDETGSGEGENSNGGASNIGNTEDDQARLILKRKLQRNRTSFTNDQIDSLEKEFERTHYPDVFARERLAGKIGLPEARIQVWFSNRRAKWRREEKLRNQRRTPNSTGASATSSSTSATASLTDSPNSLSACSSLLSGSAGGPSVSTINGLSSPSTLSTNVNAPTLGAGIDSSESPTPIPHIRPSCTSDNDNGRQSEDCRRVCSPCPLGVGGHQNTHHIQSNGHAQGHALVPAISPRLNFNSGSFGAMYSNMHHTALSMSDSYGAVTPIPSFNHSAVGPLAPPSPIPQQGDLTPSSLYPCHMTLRPPPMAPAHHHIVPGDGGRPAGVGLGSGQSANLGASCSGSGYEVLSAYALPPPPMASSSAADSSFSAASSASANVTPHHTIAQESCPSPCSSASHFGVAHSSGFSSDPISPAVSSYAHMSYNYASSANTMTPSSASGTSAHVAPGKQQFFASCFYSPWV
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Involved in eye morphogenesis.
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O18388
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IMB_DROME
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Importin subunit beta (Karyopherin subunit beta) (Protein ketel)
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MTSDIAMQLIAILEKTVSPDKNELLSAKNFLEQAAASNLPEFLKALSEILVNTANSAVARMAAGLQLKNHLTSKDEKVSQQYQDRWHQFPSEIRELIKNNILAALGTENTRPSCAAQCVAYVAVIELPINRWPMLIQTLVNKVVSEGSSEMHRESALEAIGYICQDIRFGVMENQSNDVLTAIIHGMRKVEPSNHVRLAATTALHNSLEFTKSNFEKDMERNFIMEVVCEATQCQDSQICVAALQCLVKIMTLYYQYMEPYMAQALFPITLAAMKSDNDAVALQGIEFWSNVCDEEIDLAIESQEATDQGRAPQRVSKHYARGALQFLTPVLVEKLTKQDECDDEDTWSPAKAASVCLMVLATCCEDEIVPHVLPFIKENIESPNWRFRDAAVMTFGSVLNGLETNTLKPLVEQAMPTLIRLMYDSSVIVRDTIAWTFGRICDIIPEAAINETYLQTLLECFVKSLKSEPRVAANVCWAFIGLSDAAWEAAVTNDGETPETYALSPYFEYIITQLLETTDRSDGAQANLRCAAYQALMDMIKNSPLDCYLVVQRTTLVILERLNQVMQMETQINNHSDRHQFNDLQSLLCATLQSVLRKVHEQDAPQISDAIMTALLTMFNSSAGKSGVVQEEAFLAVSTLVELLGAQFAKYMPAFKDFLVMGLKNFQEYQVCCAAVGLTGDIFRALKDLMVPYSNEIMTVLINNLTEPTIHRTVKPQVLSAFGDIALSIGNHFLPYLSMVLDMLRVASNLQTDANNFDMNEYINELRESILEAYTGIIQGLKGVDQTAHTDVMHMEPHLMHIISFIKRIAQEGDVSDSMLASAAGFIGDLCTSFGPRLYPLLDDAIITQFLAEGKRSKAQRTKMLCTWAVKEIKKINTQVITQ
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Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. In Drosophila, may not function as a snRNP import receptor as it does not interact with components of the snRNP complex such as snRNP U1, U2, U4/U6 and Snup.
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O18404
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HCD2_DROME
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3-hydroxyacyl-CoA dehydrogenase type-2 (EC 1.1.1.35) (17-beta-hydroxysteroid dehydrogenase 10) (17-beta-HSD 10) (EC 1.1.1.51, EC 1.1.1.62) (3-hydroxyacyl-CoA dehydrogenase type II) (Hydroxysteroid dehydrogenase) (EC 1.1.1.-, EC 1.1.1.53) (Mitochondrial ribonuclease P protein 2) (Mitochondrial RNase P protein 2) (Scully protein) (Type II HADH)
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MIKNAVSLVTGGASGLGRATAERLAKQGASVILADLPSSKGNEVAKELGDKVVFVPVDVTSEKDVSAALQTAKDKFGRLDLTVNCAGTATAVKTFNFNKNVAHRLEDFQRVININTVGTFNVIRLSAGLMGANEPNQDGQRGVIVNTASVAAFDGQIGQAAYSASKAAVVGMTLPIARDLSTQGIRICTIAPGLFNTPMLAALPEKVRTFLAKSIPFPQRLGEPSEYAHLVQAIYENPLLNGEVIRIDGALRMMP
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Versatile enzyme presenting two types of activity L-3-hydroxyacyl-CoA dehydrogenase ((3S)-3-hydroxyacyl-CoA dehydrogenase) activity and hydroxysteroid dehydrogenase (HSD) activity with a wide substrate spectrum. As a (3S)-3-hydroxyacyl-CoA dehydrogenase, it functions in the third step of the fatty acid beta-oxidation pathway, a major metabolic process in which fatty acids are oxidized to provide a significant source of energy, while also generating acyl-CoA metabolites used by many metabolic routes (Probable). As a HSD, it functions in the degradation pathways of glucocorticoids and sex steroids and epimerization of bile acids catalyzes the beta-oxidation at position 17 of androgens and estrogens, has 3-alpha-hydroxysteroid dehydrogenase activity with androsterone, and carries out oxidative conversions of 7-beta-hydroxylated bile acids like ursodeoxycholate or isoursodeoxycholate (also known as 3-beta,7-beta-dihydroxy-5-beta-cholan-24-oate or 7-beta-hydroxyisolithocholate, respectively). Also exhibits 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids. Required for cell survival during embryonic development. May play a role in germline formation.
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O18412
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FZO_DROME
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Transmembrane GTPase fzo (EC 3.6.5.-) (Protein fuzzy onions)
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MAESDSGESTSSVSSFISSSSSSRLSEFVDAKTELQDIYHDLSNYLSNFLTILEETVLLKDRQMLEHLCAFSSRVEAIAKVLSRDRMKVAFFGRTSNGKSAVINALLHEKILPSAMGHTTSCFCQVQANGSNETEHVKVEQEDEHMELSALSQLASAHSPGALKPSTLLQVNMAKNRCSILDYDVVLMDTPGVDVTAQLDDCLDSYCMDADVFILVLNAESTVSRVERQFFKDVASKLSRPNLFILNNRWDKASSLEPEMEQKVKDQHMERCVNLLVDELGVYSTAQEAWERIYHVSALEALHIRNGQITNPSGQTQQRYQEFLRFENDFSNCLAVSALKTKFGPHLLSAQKILNQLKSTLICPFIEKVSRLIDENKERRANLNAEIEDWLILMQEDREALQYCFEELTEMTQRVGRCVLNDQIKTLIPSSVLSFSQPFHPEFPAQIGQYQRSLCAHLDKLLEDRVLQCLSIPLQRKILDIEKEIGLPIAENSCDWQLIYGLDCQSYMSDFQPDLRFRFSLGFTALWHRLEGNLPLHASPFRIQKLQNGHKKCSPLPPLVNGNHWQMLESLVKSKGSLGTVLLSAMAIRSFNWPIVLILGGLVGSFYIYEYAAWTTAAQERSFKSQYARLLQQRLRSDVQQTVSGFELQLRQHLATVRNCWEAQSNETLNDLNVRTAELTKQIQSMEVLQLSLKKFRDKGQLLASRLGDFQETYLTKS
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Essential transmembrane GTPase, which mediates mitochondrial fusion during spermatogenesis. In early spermatocytes, fusion of mitochondria give rise to two organelles named Nebenkern and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission. Essential for fertility.
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O18413
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PRS8_DROME
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26S proteasome regulatory subunit 8
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MTVTNRMEIESAYHKGEGFRSYYIQKIEELQLVVAEKHQNLRRLQAQRNELNAKVRMLREELQLLQEQGSYVGEVVKPMDKKKVLVKVHPEGKFVVDLDKNIDINDVTPNCRVALRNESYTLHKILPNKVDPLVSLMMVEKVPDSTYEMVGGLDKQIKEIKEVIELPVKHPELFDALGIAQPKGVLLYGPPGTGKTLLARAVAHHTECTFIRVSGSELVQKFIGEGSRMVRELFVMAREHAPSIIFMDEIDSIGSSRIESGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDPALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVTQEDFEMAVAKVMQKDSEKNMSIKKLWK
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The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).
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O18423
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TXL_EISFE
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Lysenin (Beta-barrel pore-forming toxin) (Beta-PFT) (Invertebrate cytolysin pore) (efL1)
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MSAKAAEGYEQIEVDVVAVWKEGYVYENRGSTSVDQKITITKGMKNVNSETRTVTATHSIGSTISTGDAFEIGSVEVSYSHSHEESQVSMTETEVYESKVIEHTITIPPTSKFTRWQLNADVGGADIEYMYLIDEVTPIGGTQSIPQVITSRAKIIVGRQIILGKTEIRIKHAERKEYMTVVSRKSWPAATLGHSKLFKFVLYEDWGGFRIKTLNTMYSGYEYAYSSDQGGIYFDQGTDNPKQRWAINKSLPLRHGDVVTFMNKYFTRSGLCYDDGPATNVYCLDKREDKWILEVVG
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Pore-forming toxin that defensively acts against parasitic microorganisms by forming pores in sphingomyelin-containing membranes. Has hemolytic activity and is also cytotoxic to spermatozoa of some species of invertebrates and many species of vertebrates and to amphibian larvae, guinea pig polymorphonuclear leukocytes, chicken fibroblasts, normal spleen cells and various tumor cells. Is lethal for various species of reptiles, amphibian, birds and mammals. Induces smooth muscle contraction. It binds sphingomyelin and induces hemolysis in the same manner as lysenin-related protein 2, and is 10-fold more effective than lysenin-related protein 1.
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O18475
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DPOLQ_DROME
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DNA polymerase theta (EC 2.7.7.7) (Mutagen-sensitive protein 308)
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MAFSQSFNFGNSTLMALEKGMQADDKENAQPGNGNIQVQSAGNEVNSEIQEINSEFFRDEFSYEVNQAHKPAEQSVVNVSQVQQHMAVVSNQDSEDQSRSSALNDQICTQSSFEGEDAGADAVLDQPNLDENSFLCPAQDEEASEQLKEDILHSHSVLAKQEFYQEISQVTQNLSSMSPNQLRVSPNSSRIREAMPERPAMPLDLNTLRSISAWNLPMSIQAEYKKKGVVDMFDWQVECLSKPRLLFEHCNLVYSAPTSAGKTLVSEILMLKTVLERGKKVLLILPFISVVREKMFYMQDLLTPAGYRVEGFYGGYTPPGGFESLHVAICTIEKANSIVNKLMEQGKLETIGMVVVDEVHLISDKGRGYILELLLAKILYMSRRNGLQIQVITMSATLENVQLLQSWLDAELYITNYRPVALKEMIKVGTVIYDHRLKLVRDVAKQKVLLKGLENDSDDVALLCIETLLEGCSVIVFCPSKDWCENLAVQLATAIHVQIKSETVLGQRLRTNLNPRAIAEVKQQLRDIPTGLDGVMSKAITYACAFHHAGLTTEERDIIEASFKAGALKVLVATSTLSSGVNLPARRVLIRSPLFGGKQMSSLTYRQMIGRAGRMGKDTLGESILICNEINARMGRDLVVSELQPITSCLDMDGSTHLKRALLEVISSGVANTKEDIDFFVNCTLLSAQKAFHAKEKPPDEESDANYINDALDFLVEYEFVRLQRNEERETAVYVATRLGAACLASSMPPTDGLILFAELQKSRRSFVLESELHAVYLVTPYSVCYQLQDIDWLLYVHMWEKLSSPMKKVGELVGVRDAFLYKALRGQTKLDYKQMQIHKRFYIALALEELVNETPINVVVHKYKCHRGMLQSLQQMASTFAGIVTAFCNSLQWSTLALIVSQFKDRLFFGIHRDLIDLMRIPDLSQKRARALFDAGITSLVELAGADPVELEKVLYNSISFDSAKQHDHENADEAAKRNVVRNFYITGKAGMTVSEAAKLLIGEARQFVQHEIGLGTIKWTQTQAGVEIASRAIHDGGEVDLHMSLEEEQPPVKRKLSIEENGTANSQKNPRLETVVDTQRGYKVDKNIANQSKMNPNLKEIDAQNKARRNSTAHMDNLNPISNDPCQNNVNVKTAQPIISNLNDIQKQGSQIEKMKINPATVVCSPQLANEEKPSTSQSARRKLVNEGMAERRRVALMKIQQRTQKENQSKDQPIQASRSNQLSSPVNRTPANRWTQSENPNNEMNNSQLPRRNPRNQSPVPNANRTASRKVSNAEEDLFMADDSFMLNTGLAAALTAAESKIASCTEADVIPSSQPKEPEVIGALTPHASRLKRSDQLRSQRIQSPSPTPQREIEIDLESKNESNGVSSMEISDMSMENPLMKNPLHLNASHIMSCSKVDETASSFSSIDIIDVCGHRNAFQAAIIEINNATRLGFSVGLQAQAGKQKPLIGSNLLINQVAAAENREAAARERVLFQVDDTNFISGVSFCLADNVAYYWNMQIDERAAYQGVPTPLKVQELCNLMARKDLTLVMHDGKEQLKMLRKAIPQLKRISAKLEDAKVANWLLQPDKTVNFLNMCQTFAPECTGLANLCGSGRGYSSYGLDTSSAILPRIRTAIESCVTLHILQGQTENLSRIGNGDLLKFFHDIEMPIQLTLCQMELVGFPAQKQRLQQLYQRMVAVMKKVETKIYEQHGSRFNLGSSQAVAKVLGLHRKAKGRVTTSRQVLEKLNSPISHLILGYRKLSGLLAKSIQPLMECCQADRIHGQSITYTATGRISMTEPNLQNVAKEFSIQVGSDVVHISCRSPFMPTDESRCLLSADFCQLEMRILAHMSQDKALLEVMKSSQDLFIAIAAHWNKIEESEVTQDLRNSTKQVCYGIVYGMGMRSLAESLNCSEQEARMISDQFHQAYKGIRDYTTRVVNFARSKGFVETITGRRRYLENINSDVEHLKNQAERQAVNSTIQGSAADIAKNAILKMEKNIERYREKLALGDNSVDLVMHLHDELIFEVPTGKAKKIAKVLSLTMENCVKLSVPLKVKLRIGRSWGEFKEVSV
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Multifunctional protein with both DNA polymerase and ATPase activities. Might have 3' to 5' exonuclease activity. Plays a role in different DNA repair pathways such as DNA strand cross-link repair and microhomology-mediated end-joining (MMEJ), an alternative non-homologous end-joining (NHEJ) machinery triggered in response to double-strand breaks. MMEJ is an error-prone repair pathway that produces deletions of sequences from the strand being repaired and promotes genomic rearrangements, such as telomere fusions. Utilizes short microhomologies present in partially and fully single-stranded DNA (ssDNA) as primers for DNA synthesis. Prefers poly(dA)/oligo(dT) as a template-primer. The ATPase activity is necessary during interstrand cross-link (ICL) repair and has a critical role in generating templated insertions during MMEJ. Necessary for processing DNA damage induced by oxygen and N-ethylation. In follicle cells, contributes to double-strand break repair at physiological rereplication forks necessary for survival of fertilized eggs.
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O18497
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MAN2_SPOFR
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Alpha-mannosidase 2 (EC 3.2.1.114) (Alpha-mannosidase II) (Class II alpha-mannosidase) (Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase)
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MRTRVLRCRPFSTRILLLLLFVLAFGVYCYFYNASPQNYNKPRISYPASMEHFKSSLTHTVKSRDEPTPDQCPALKESEADIDTVAIYPTFDFQPSWLRTKEFWDKSFEDRYERIHNDTTRPRLKVIVVPHSHNDPGWLKTFEQYFEWKTKNIINNIVNKLHQYPNMTFIWTEISFLNAWWERSHPVKQKALKKLIKEGRLEITTGGWVMPDEACTHIYALIDQFIEGHHWVKTNLGVIPKTGWSIDPFGHGATVPYLLDQSGLEGTIIQRIHYAWKQWLAERQIEEFYWLASWATTKPSMIVHNQPFDIYSIKSTCGPHPSICLSFDFRKIPGEYSEYTAKHEDITEHNLHSKAKTLIEEYDRIGSLTPHNVVLVPLGDDFRYEYSVEFDAQYVNYMKMFNYINAHKEIFNADVQFGTPLDYFNAMKERHQNIPSLKGDFFVYSDIFSEGKPAYWSGYYTTRPYQKILARQFEHQLRSAEILFTLVSNYIRQMGRQGEFGASEKKLEKSYEQLIYARRNLGLFQHHDAITGTSKSSVMQDYGTKLFTSLYHCIRLQEAALTTIMLPDQSLHSQSIIQSEVEWETYGKPPKKLQVSFIDKKKVILFNPLAETRTEVVTVRSNTSNIRVYDTHKRKHVLYQIMPSITIQDNGKSIVSDTTFDIMFVATIPPLTSISYKLQEHTNTSHHCVIFCNNCEQYQKSNVFQIKKMMPGDIQLENAVLKLLVNRNTGFLRQVYRKDIRKRTVVDVQFGAYQSAQRHSGAYLFMPHYDSPEKNVLHPYTNQNNMQDDNIIIVSGPISTEITTMYLPFLVHTIRIYNVPDPVLSRAILLETDVDFEAPPKNRETELFMRLQTDIQNGDIPEFYTDQNGFQYQKRVKVNKLGIEANYYPITTMACLQDEETRLTLLTNHAQGAAAYEPGRLEVMLDRRTLYDDFRGIGEGVVDNKPTTFQNWILIESMPGVTRAKRDTSEPGFKFVNERRFGPGQKESPYQVPSQTADYLSRMFNYPVNVYLVDTSEVGEIEVKPYQSFLQSFPPGIHLVTLRTITDDVLELFPSNESYMVLHRPGYSCAVGEKPVAKSPKFSSKTRFNGLNIQNITAVSLTGLKSLRPLTGLSDIHLNAMEVKTYKIRF
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Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans the final hydrolytic step in the N-glycan maturation pathway.
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O18498
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MA1A1_SPOFR
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Mannosyl-oligosaccharide alpha-1,2-mannosidase IA (EC 3.2.1.113) (Alpha-1,2-mannosidase) (Class I alpha-1,2-mannosidase) (Man(9)-alpha-mannosidase) (SfManI)
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MTGILPTYQRFVNGVPVPSISRRSFRLREKYLIVSVLLTFGIVWLGALFYLPEFKSSNSVNDSVYNVYKRIQKAGPELLMPPPLAQNDVGDFPVIGIAHHGEGGDDPHVIEDRNRLRAKIEEDMGMKVLERPQFDVAPSVSSSRGPSKPPVDAIEEPAVGNNAANKDVSPSGPKAESSDKFVAVALAPGADPEIKHKLETVKKMMLHAWYNYKLYAWGKNELKPMSKRAHLSSVFGAGELGATIVDGLDTLYLMGLNDEFREGRDWVAEHLHINEIDSDLSVFETTIRFVGGLLSCYALTGDTMFRDKAAEVGDALLPAFDTPTGLPYALINPSTKASRQYHWAGPNSILSELGTLHLEFTYLSDVTGRDIYRQKVSRIREVLDQIDKPGDLYPNFINPRTGQWGQRHMSLGALGDSFYEYLLKAWLMSGGADEQARIMFDTAMQAALDKMLRVSPSGLAYLAELKYGRIIEEKMDHLSCFAGGMFALASTTLDNSMSERYMDVAKKLTNTCHESYARSETKLGPEAFRFSNAAEARAQKSNEKVYLLRPETFESYFIMWRLTKQQMYRDWAWEAVQALEKHCRVEGGYTGLVNVYHANPQGDDVQQSFFLAETLKYLYLIFGDDSFLPLDEWVFNTEAHPFPIRGKNPLYRAVDKPVLPEPAHAQNNRI
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Involved in the maturation of Asn-linked oligosaccharides. Converts Man(9)GlcNAc(2) to Man(5)GlcNAc(2) primarily through the Man(7)GlcNAc(2) isomer C processing intermediate.
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O18640
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GBLP_DROME
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Small ribosomal subunit protein RACK1 (Guanine nucleotide-binding protein subunit beta-like protein) (Receptor of activated protein kinase C homolog)
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MSETLQLRGTLIGHNGWVTQIATNPKDPDTIISASRDKTLIVWKLTRDEDTNYGYPQKRLYGHSHFISDVVLSSDGNYALSGSWDQTLRLWDLAAGKTTRRFEGHTKDVLSVAFSADNRQIVSGSRDKTIKLWNTLAECKFTIQEDGHTDWVSCVRFSPNHSNPIIVSCGWDRTVKVWNLANCKLKNNHHGHNGYLNTVTVSPDGSLCTSGGKDSKALLWDLNDGKNLYTLEHNDIINALCFSPNRYWLCVAYGPSIKIWDLACKKTVEELRPEVVSPTSKADQPQCLSLAWSTDGQTLFAGYSDNTIRVWQVSVSAH
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Involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes (By similarity).
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O18696
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PDE1_CAEEL
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Probable 3',5'-cyclic phosphodiesterase pde-1 (EC 3.1.4.17)
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MNRARKTSSCGCFRSAFCLLKPSTSSASEEHGDSDKKLLSVQLITPRDEEEQTSSRSIKIPPLDLNGLDCKKNAVAARRAGRRRTSEGGGVRGKGHFAEVVLDGLQRPVSLLRNQKEKSNSDDNCQEKEPTSPSSSRKKSYDNAPALESLEKLRYILHQLNSGQLPLEDLKRNIEYAALVLETAYMDETRRICDEDDDLAEVTPETVPDEVREWLAATFTRQNAGKKRDKPKFKSVANAIRTGIFFEKLFRKQQVVQCPIPPEIAELMKEVCTWSFSPFQLNEVSEGHALKYVGFELFNRYGFMDRFKVPLTALENYLSALEVGYSKHNNPYHNVVHAADVTQSSHFMLSQTGLANSLGDLELLAVLFGALIHDYEHTGHTNNFHIQSQSQFAMLYNDRSVLENHHVSSCFRLMKEDDKNILTHLTRDEYKELRNMVIEIVLATDMSTHFMQIKTMKSMLSLPEGIDKNKALCLIVHACDISHPAKPWNLHERWTEGVLEEFFRQGDLEASMGLPYSPLCDRHTVHVADSQIGFIDFIVEPTMVVCGELLVKMVEPLVSLPPTDSLFPPSVDGGDDKSPSNALSPLPDLRNSSTSPSSIRRIPLNYAGKLDIPTPWMKFLHENKAHWKERAAKEEEERKIKEAAEAEAAAKQVEENKENGVTTN
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Redundantly with pde-5, plays a role in the AFD thermosensory neurons to regulate microvilli receptive ending morphology, possibly by regulating cGMP levels.
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O18733
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MMP9_CANLF
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Matrix metalloproteinase-9 (MMP-9) (EC 3.4.24.35) (92 kDa gelatinase) (92 kDa type IV collagenase) (Gelatinase B) (GELB)
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MSPRQPLVLVFLVLGCCSAAPRPHKPTVVVFPGDLRTNLTDKQLAEEYLFRYGYTQVAELSNDKQSLSRGLRLLQRRLALPETGELDKTTLEAMRAPRCGVPDLGKFQTFEGDLKWHHNDITYWIQNYSEDLPRDVIDDAFARAFAVWSAVTPLTFTRVYGPEADIIIQFGVREHGDGYPFDGKNGLLAHAFPPGPGIQGDAHFDDEELWTLGKGVVVPTHFGNADGAPCHFPFTFEGRSYSACTTDGRSDDTPWCSTTADYDTDRRFGFCPSEKLYAQDGNGDGKPCVFPFTFEGRSYSTCTTDGRSDGYRWCSTTADYDQDKLYGFCPTRVDSAVTGGNSAGEPCVFPFIFLGKQYSTCTREGRGDGHLWCATTSNFDRDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYSFTEGPPLHEDDVRGIQHLYGPRPEPEPQPPTAPPTAPPTVCATGPPTTRPSERPTAGPTGPPAAGPTGPPTAGPSEAPTVPVDPAEDICKVNIFDAIAEIRNYLHFFKEGKYWRFSKGKGRRVQGPFLSPSTWPALPRKLDSAFEDGLTKKTFFFSGRQVWVYTGTSVVGPRRLDKLGLGPEVTQVTGALPQGGGKVLLFSRQRFWSFDVKTQTVDPRSAGSVEQMYPGVPLNTHDIFQYQEKAYFCQDRFYWRVNSRNEVNQVDEVGYVTFDILQCPED
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Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (By similarity). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (By similarity). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide (By similarity).
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O18734
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PP14A_PIG
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Protein phosphatase 1 regulatory subunit 14A (17 kDa PKC-potentiated inhibitory protein of PP1) (Protein kinase C-potentiated inhibitor protein of 17 kDa) (CPI-17)
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MAAQRLGKRVLSKLQSPSRARGPGGSPGGLQKRHARVTVKYDRRELQRRLDVEKWIDGRLEELYRGREADMPDEVNIDELLELESEEERSRKIQGLLKSCTNPTENFVQELLVKLRGLHKQPGLRQPSPSGDGSLSPRQDRARTAPP
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Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction.
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O18735
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ERBB2_CANLF
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Receptor tyrosine-protein kinase erbB-2 (EC 2.7.10.1) (Proto-oncogene c-ErbB-2) (p185erbB2) (CD antigen CD340)
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MELAAWCRWGLLLALLPSGAAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPANASLSFLQDIQEVQGYVLIAHSQVRQIPLQRLRIVRGTQLFEDNYALAVLDNGDPLEGGIPAPGAAQGGLRELQLRSLTEILKGGVLIQRSPQLCHQDTILWKDVFHKNNQLALTLIDTNRFSACPPCSPACKDAHCWGASSGDCQSLTRTVCAGGCARCKGPQPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTSCPYNYLSTDVGSCTLVCPLNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLRVFEALEEITGYLYISAWPDSLPNLSVFQNLRVIRGRVLHDGAYSLTLQGLGISWLGLRSLRELGSGLALIHRNARLCFVHTVPWDQLFRNPHQALLHSANRPEEECVGEGLACYPCAHGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVKDRYCLPCHSECQPQNGSVTCFGSEADQCVACAHYKDPPFCVARCPSGVKPDLSFMPIWKFADEEGTCQPCPINCTHSCADLDEKGCPAEQRASPVTSIIAAVVGILLAVVVGLVLGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESIPPRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVAEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPEPTPGAGGTAHRRHRSSSTRNGGGELTLGLEPSEEEPPKSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPSQDPSPLQRYSEDPTVPLPPETDGKVAPLTCSPQPEYVNQPEVWPQPPLALEGPLPPSRPAGATLERPKTLSPKTLSPGKNGVVKDVFAFGSAVENPEYLAPRGRAAPQPHPPPAFSPAFDNLYYWDQDPSERGSPPSTFEGTPTAENPEYLGLDVPV
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Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth (By similarity).
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O18738
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DAG1_BOVIN
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Dystroglycan 1 (Dystroglycan) (Dystrophin-associated glycoprotein 1) [Cleaved into: Alpha-dystroglycan (Alpha-DG); Beta-dystroglycan (Beta-DG)]
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MRMSVGSAVPLPLWGRTFLLLLSVAVTQSHWPSEPSEAVRDWENQLEASMHSALSDLHETVPTVVGIPDGTAVVGRSFRVTIPTDLIASNGEVIKVSAAGKEALPSWLHWDPQSHTLEGLPLDTDKGVHYISVSAARLGANGSHVPQTSSVFSIEVYPEDHSEPQSLRAASPDPGEVVSLVCAADEPVTVLTVILDADLTKMTPKQRIDLLRRMRGFSEVEPHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCCLNQNSVPDIRGVEVPAREGAMSAQLGYPVVGWHIANKKPSLPKRIRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPSQIRPTMTIPGYMEPSTVTTPPTTTTKKPRVSTPRPATPSTDSSTTTTRRPTKKPRTSRPVPRVTTKAPITRLETASPATRMRTTTSGVPHGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDNEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHRRPQGDKAPARFKAKLTGDPAAVTNDIHKKIALVKKLAFAFGDRNCSTITLQNITRGSIVVEWTNNTLPLEPCPKEQITALSRRIAEDDGKPRGAFVNALEPDFQAMSITVTGSGSCRHLQFVPVAPPMRVPSEAPATEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSMPETTPLNQDTVGEYAPLRDEDPSAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP
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The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization. [Alpha-dystroglycan]: Extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Also acts as a receptor for laminin LAMA5. [Beta-dystroglycan]: Transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity (By similarity).
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O18756
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GLCE_BOVIN
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D-glucuronyl C5-epimerase (EC 5.1.3.17) (Heparan sulfate C5-epimerase) (Hsepi) (Heparin/heparan sulfate:glucuronic acid C5-epimerase) (Heparosan-N-sulfate-glucuronate 5-epimerase)
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MRCLAARVNYKTLIIICALFTLVTVLLWNKCSSDKAIQVPRHLSSGFRVDALEKKAAASESNNYVNHMAKQSEEAFPQEQQKAPPVVGGFNNNGGGRVLGLKYEEIDCLINDEHTIKGRREGNEVFLPFTWVEKYFDVYGKVVQYDGYDRFEFSHSYSKVYAQRAPYHPDGVFMSFEGYNVEVRDRVKCISGVEGVPLSTQWGPQGYFYPIQIAQYGLSHYSKNLTEKPPHIEVYETAEDRDKNSKPNDWTVPKGCFMASVADKSRFTNVKQFIAPETSEGVSLQLGNTKDFIISFDLKFLTNGSVSVVLETTEKNQLFTVHYVSNTQLIAFKERDIYYGIGPRTSWSTVTRDLVTDLRKGVGLSNTKAVKPTRIMPKKVVRLIAKGKGFLDNITISTTAHMAAFFAASDWLVRNQDEKGGWPIMVTRKLGEGFKSLEPGWYSAMAQGQAISTLVRAYLLTKDHIFLNSALRATAPYKFLSEQHGVKAVFMNKHDWYEEYPTTPSSFVLNGFMYSLIGLYDLKETAGEKLGKEARSLYERGMESLKAMLPLYDTGSGTIYDLRHFMLGIAPNLARWDYHTTHINQLQLLSTIDESPIFKEFVKRWKSYLKGSRAKHN
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Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains. This is important for further modifications that determine the specificity of interactions between these glycosaminoglycans and proteins.
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O18757
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SCMC1_RABIT
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Mitochondrial adenyl nucleotide antiporter SLC25A24 (Peroxisomal Ca(2+)-dependent solute carrier) (Small calcium-binding mitochondrial carrier protein 1) (SCaMC-1) (Solute carrier family 25 member 24)
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MLRWLRGFVLPTAACQGAEPPTRYETLFQALDRNGDGVVDIRELQEGLKSLGIPLGQDAEEKIFTTGDVNKDGKLDFEEFMKYLKDHEKKMKLAFKSLDKNNDGKIEASEIVQSLQTLGLTISEQQAELILQSIDADGTMTVDWNEWRDYFLFNPVADIEEIIRFWKHSTGIDIGDSLTIPDEFTEEERKSGQWWRQLLAGGIAGAVSRTSTAPLDRLKVMMQVHGSKSMNIFGGFRQMIKEGGVRSLWRGNGTNVIKIAPETAVKFWVYEQYKKLLTEEGQKIGTFERFISGSMAGATAQTFIYPMEVMKTRLAVGKTGQYSGIYDCAKKILKYEGFGAFYKGYVPNLLGIIPYAGIDLAVYELLKSHWLDNFAKDSVNPGVLVLLGCGALSSTCGQLASYPLALVRTRMQAQAMLEGAPQLNMVGLFRRIISKEGLPGLYRGITPNFMKVLPAVGISYVVYENMKQTLGVTQK
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Electroneutral antiporter that mediates the transport of adenyl nucleotides through the inner mitochondrial membrane. Originally identified as an ATP-magnesium/inorganic phosphate antiporter, it also acts as a broad specificity adenyl nucleotide antiporter. By regulating the mitochondrial matrix adenyl nucleotide pool could adapt to changing cellular energetic demands and indirectly regulate adenyl nucleotide-dependent metabolic pathways. In vitro, a low activity is also observed with guanyl and pyrimidine nucleotides. May play a role in protecting cells against oxidative stress-induced cell death, by buffering calcium levels in the mitochondrial matrix through the formation of calcium-phosphate precipitates.
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O18766
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OPSD_PIG
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Rhodopsin
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MNGTEGPNFYVPFSNKTGVVRSPFEYPQYYLAEPWQFSMLAAYMFMLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGLALTWVMALACAAPPLVGWSRYIPEGLQCSCGIDYYTLKPEVNNESFVIYMFVVHFSIPLVIIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVVAFLICWLPYASVAFYIFTHQGSDFGPIFMTIPAFFAKSASIYNPVIYIMMNKQFRNCMLTTLCCGKNPLGDDEASTTTSKTETSQVAPA
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Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (By similarity).
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O18778
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PAHX_BOVIN
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Phytanoyl-CoA dioxygenase, peroxisomal (EC 1.14.11.18) (Phytanic acid oxidase) (Phytanoyl-CoA alpha-hydroxylase) (PhyH)
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MDRNRASARLTVLLRHLGCRSAGTIIAHHTSGVGSLASFHPQQFQYTRENNVLSLEQRKFYEENGFLVIKNLVSDADIQRFRNEFERICRKEVKPLGLSVMRDVTITKSEYVPSEKVVSKVQDFQEDEELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSNSIVCAWTAMEHIDRNNGCLVVLPGTHKGPLQPHDYPQWEGGVNIMFHGIQDYDKNNARVHLVMEKGDTVFFHPLLIHGSGRNKSQGFRKAISCHFADANCHYIDVEGTSQENIEKEVVDIVRKKYGFKDVTLKDVWTFRGRVVKGERINL
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Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono- branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon atoms) (By similarity). Does not hydroxylate long and very long straight chain acyl-CoAs or 2-methyl-and 4-methyl-branched acyl-CoAs (By similarity).
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O18793
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CCR2_MACMU
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C-C chemokine receptor type 2 (C-C CKR-2) (CC-CKR-2) (CCR-2) (CCR2) (Monocyte chemoattractant protein 1 receptor) (MCP-1-R) (CD antigen CD192)
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MLSTSRSRFIRNTNGSGEEVTTFFDYDYGAPCHKFDVKQIGAQLLPPLYSLVFIFGFVGNMLVVLILINCKKLKSLTDIYLLNLAISDLLFLITLPLWAHSAANEWVFGNAMCKLFTGLYHIGYLGGIFFIILLTIDRYLAIVHAVFALKARTVTFGVVTSVITWLVAVFASVPGIIFTKCQEEDSVYICGPYFPRGWNNFHTIMRNILGLVLPLLIMVICYSGILKTLLRCRNEKKRHRAVRLIFTIMIVYFLFWTPYNIVILLNTFQEFFGLSNCESTRQLDQATQVTETLGMTHCCINPIIYAFVGEKFRRYLSMFFRKYITKRFCKQCPVFYRETVDGVTSTNTPSTAEQEVSVGL
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Key functional receptor for CCL2 but can also bind CCL7 and CCL12 (By similarity). Its binding with CCL2 on monocytes and macrophages mediates chemotaxis and migration induction through the activation of the PI3K cascade, the small G protein Rac and lamellipodium protrusion (By similarity). Also acts as a receptor for the beta-defensin DEFB106A/DEFB106B (By similarity). Regulates the expression of T-cell inflammatory cytokines and T-cell differentiation, promoting the differentiation of T-cells into T-helper 17 cells (Th17) during inflammation (By similarity). Facilitates the export of mature thymocytes by enhancing directional movement of thymocytes to sphingosine-1-phosphate stimulation and up-regulation of S1P1R expression signals through the JAK-STAT pathway to regulate FOXO1 activity leading to an increased expression of S1P1R (By similarity). Plays an important role in mediating peripheral nerve injury-induced neuropathic pain (By similarity). Increases NMDA-mediated synaptic transmission in both dopamine D1 and D2 receptor-containing neurons, which may be caused by MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B (By similarity). Mediates the recruitment of macrophages and monocytes to the injury site following brain injury (By similarity).
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O18796
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IL6RA_PIG
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Interleukin-6 receptor subunit alpha (IL-6 receptor subunit alpha) (IL-6R subunit alpha) (IL-6R-alpha) (IL-6RA) (IL-6R 1) (CD antigen CD126) [Cleaved into: Soluble interleukin-6 receptor subunit alpha (sIL6R)]
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MLAVGCALLTALLAAPGMALAPRGCSKLEVAQDVLTSLPGASVTLTCPGGEPGDNATIHWVLRNQVTGSPDGRPAGVGRRLLLKSVQLSDSGNYSCYQDGVPAGSVRLLVDAPPEEPQLSCFRKSPLSNVGCEWRPRSPPSPTTKAVLLVRKFQNSPVEDFQEPCQYSLEAQRFFCQLAVPEGDNSFHIVTLCVANSAGSQSSTPQTFEGYGILQPDPPVNITVSAVDRNPRWLSVTWQDPPSWNSYFYRLQFELRYRAERSKTFTTWMVKELQHHCIIHDAWSGMRHVVQLRAQEEFGHGLWSEWSQEVTGIPWTESRSSPAETELPLSTQAPTTNEDDEDISSKESANATSLPVQDSASVPLPTFLVAGGSLAFGTLLCIGIILRFKKTGQLQALKEGKTNMHPPYSLGQLVPERPKSTPVLVPLISPPVSPNSLGDNTSRNSRPEARGPQSPYDVSNRDYFFPR
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Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation leads to the regulation of the immune response, acute-phase reactions and hematopoiesis. The interaction with membrane-bound IL6R and IL6ST stimulates 'classic signaling', the restricted expression of the IL6R limits classic IL6 signaling to only a few tissues such as the liver and some cells of the immune system. Whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells. [Interleukin-6 receptor subunit alpha]: Signaling via the membrane-bound IL6R is mostly regenerative and anti-inflammatory. Drives naive CD4(+) T cells to the Th17 lineage, through 'cluster signaling' by dendritic cells. [Soluble interleukin-6 receptor subunit alpha]: Soluble form of IL6 receptor (sIL6R) that acts as an agonist of IL6 activity (By similarity). The IL6:sIL6R complex (hyper-IL6) binds to IL6ST/gp130 on cell surfaces and induces signaling also on cells that do not express membrane-bound IL6R in a process called IL6 'trans-signaling'. sIL6R is causative for the pro-inflammatory properties of IL6 and an important player in the development of chronic inflammatory diseases. In complex with IL6, is required for induction of VEGF production (By similarity). Plays a protective role during liver injury, being required for maintenance of tissue regeneration. 'Trans-signaling' in central nervous system regulates energy and glucose homeostasis (By similarity).
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O18805
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DAXX_CHLAE
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Death domain-associated protein 6 (Daxx)
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MATANSIIVLDDDDENEAAAQPGPSHPLPSTASPEAEAPSSSEPHGARGSSSSGGKKCYKLENEKLFQEFLELCKTQTADHPEVVPFLCNRQQRAHSLFLASAEFCNILSRVLSRAQSRPFKLYVYINELCTVLKGHSAKKKLNLAPVATTSNEPSGNNPPTHLSLDPTNAENTASQAPRTRGSRRQIQRLEQLLALYVAEIRRLQERELDLSELDDPDSTYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIKQRIPYRGTRYPKVNRRIERLINKPGPDTFPDYGDVLRAVKKAAARHSLGLPRQQLQLMAQDAFRNVGIRLQEQRHLDLIYNFGCHLTNDYRPGVDPALSYPVLARRLRENRILALIRLDQVISFYAMLQDGGEEGKKKKRRARLHGPSSHSANPPEPSLDSGEGPIGMASQGCPSASRAETDDEDDEESDEEEEEEEEEEEEEATDFEEEEDLEQMQEGQEDDEEEEEEEEAAGKDGDGSPMSSPQISTEKNLEPGKQISRSSGEQQNKVSPLLLSEEPLAPSSIDAESNGEQPEELTLEEESPVSQLFELEIEALPLDTPSFVEMDISFFRKQSEEPFTTVLENGAGMVSSTSFNGGVSPHNWGDSGPPCKKSRKEKKQTGSGPLGNSYVERQRSVHEKNGKKICTLPSPPSPLASLAPVADSSTRVDSPSHGLVTSSLCNPSPAQLSQTPQSQPPRPSTYKTSVATQCDPEEIIVLSDSD
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Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as histone chaperone that facilitates deposition of histone H3.3. Acts as targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs) the process is independent of ATRX and facilitated by ASF1A PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX (By similarity).
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O18823
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AOAH_RABIT
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Acyloxyacyl hydrolase (EC 3.1.1.77) [Cleaved into: Acyloxyacyl hydrolase small subunit; Acyloxyacyl hydrolase large subunit]
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MKSPWRILVVSPLLLLPLHSSTSRAHDNQPGTIRSDHYTCVGCVLVVSVIEQLAQVHNSTVQASMERLCSYLPEEWVLKTACYMMVHVFGADIIKLFDKDVNADVVCHTLEFCKQEPGQPLCHLYPLPKESWKFTLEKARHIVKQSPIMKYTRSGAGICSLPFLAKICQKIKLAIKNSVPIKDVDSDKYSIFPTLRGYHWRGRDCNDSDKTVYPGRRPDNWDAHRDSNCNGIWGVDPKDGIPYEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTVSQMSVNSFLNLPTAVTNELDWPQLSGTTGFLDSASKIKENSIYLRLRKRNRCNHRDYQNISKNGASSRNVKSLIESLSRNQLLDHPAIVIYAMIGNDVCNGRKTDPVSAMTTPEQLYANVLKMLEALNSHLPTGSHVILYGLAHGAFLWDTLHSRYHPLGQLNKDVTYTQLYSFLGCLQVSPCPGWMSANETLRALTSERAQQLSETLRKIAASKKFTNFNLFYLDFAFQEVVEEWQKMGGQPWELIEAVDGFHPNEVALLLFADQLWEKVQRQWPDVLGKENPFNPQIEEVFGDQGGH
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Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses. In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria.
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O18824
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SCRB1_BOVIN
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Scavenger receptor class B member 1 (SRB1) (SR-BI)
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MGNLSRARRVTAALGFIGLLFAVLGIIMIVMVPSIIKQQVLKNVRIDPNSLSFNMWKEIPVPFYLSVYFFNIVNPEGIIQGQKPQVQEHGPYVYREFRHKSNITFNNNDTVSFLEYRSYQFQPDKSRGQESDYIVMPNILVLSASMMMENRPGLLKLMMTLAFSTLGQRAFMNRTVGEIMWGYDDPLIHLINQYFPNSLPFKGKFGLFAELNNSDSGLFTVFTGVKNFSRIHLVDKWNGVSKVNYWHSDQCNMINGTSGQMWAPFMTPESSLEFYSPEACRSMKLVYKEQGVFGGIPTFRFVAPSTLFANGSVYPPNEGFCPCRESGIQNVSTCRFNAPLFLSHPHFYNADPVLAEAVSGLHPNPKEHSLFLDIHPVTGIPMNCSVKLQLSLFVKSVKGIGQTGNIQPVVLPLMWFEESGAMEGETLETFYIQLVLMPKVLHYAQYVLLALGCVLLLIPIIYQIRSQEKCYLFWISFKKGSKDKEAVQAYSEFLMTSAPKGTVLQEARL
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Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells. Receptor for HDL, mediating selective uptake of cholesteryl ether and HDL-dependent cholesterol efflux. Also facilitates the flux of free and esterified cholesterol between the cell surface and apoB-containing lipoproteins and modified lipoproteins, although less efficiently than HDL. May be involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity.
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O18831
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GDF8_PIG
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Growth/differentiation factor 8 (GDF-8) (Myostatin)
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MQKLQIYVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACMWRQNTKSSRLEAIKIQILSKLRLETAPNISKDAIRQLLPKAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDLLMQVEGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVKTPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS
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Acts specifically as a negative regulator of skeletal muscle growth.
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O18836
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GDF8_BOVIN
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Growth/differentiation factor 8 (GDF-8) (Myostatin)
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MQKLQISVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACLWRENTTSSRLEAIKIQILSKLRLETAPNISKDAIRQLLPKAPPLLELIDQFDVQRDASSDGSLEDDDYHARTETVITMPTESDLLTQVEGKPKCCFFKFSSKIQYNKLVKAQLWIYLRPVKTPATVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPEPGEDGLTPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGEGQIIYGKIPAMVVDRCGCS
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Acts specifically as a negative regulator of skeletal muscle growth.
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O18839
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KCNJ2_PIG
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Inward rectifier potassium channel 2 (Inward rectifier K(+) channel Kir2.1) (IRK-1) (Potassium channel, inwardly rectifying subfamily J member 2)
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MGSVRTNRYSIVSSEEDGMKLATLAVANGFGNGKSKVHTRQQCRSRFVKKDGHCNVQFINVGEKGQRYLADIFTTCVDIRWRWMLVIFCLAFVLSWLFFGCVFWLIALLHGDLDASKESKACVSEVNSFTAAFLFSIETQTTIGYGFRCVTDECPIAVFMVVFQSIVGCIIDAFIIGAVMAKMAKPKKRNETLVFSHNAVIAMRDGKLCLMWRVGNLRKSHLVEAHVRAQLLKSRITSEGEYIPLDQIDINVGFDSGIDRIFLVSPITIVHEIDEDSPLYDLSKQDIDNADFEIVVILEGMVEATAMTTQCRSSYLANEILWGHRYEPVLFEEKHYYKVDYSRFHKTYEVPNTPLCSARDLAEKKYILSNANSFCYENEVALTSKEEDDSENGVPESTSTDTPPDIDLHNQASVPLEPRPLRRESEI
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Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity).
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