entry
stringlengths 6
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stringlengths 5
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| protein_name
stringlengths 3
2.44k
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stringlengths 2
35.2k
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stringlengths 7
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O60907
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TBL1X_HUMAN
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F-box-like/WD repeat-containing protein TBL1X (SMAP55) (Transducin beta-like protein 1X) (Transducin-beta-like protein 1, X-linked)
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MTELAGASSSCCHRPAGRGAMQSVLHHFQRLRGREGGSHFINTSSPRGEAKMSITSDEVNFLVYRYLQESGFSHSAFTFGIESHISQSNINGTLVPPAALISILQKGLQYVEAEISINEDGTVFDGRPIESLSLIDAVMPDVVQTRQQAFREKLAQQQASAAAAAAAATAAATAATTTSAGVSHQNPSKNREATVNGEENRAHSVNNHAKPMEIDGEVEIPSSKATVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNENSNGGSTQLVLRHCIREGGHDVPSNKDVTSLDWNTNGTLLATGSYDGFARIWTEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQNNTTFASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKWSPTGPATSNPNSNIMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGNLVHSYRGTGGIFEVCWNARGDKVGASASDGSVCVLDLRK
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F-box-like protein involved in the recruitment of the ubiquitin/19S proteasome complex to nuclear receptor-regulated transcription units. Plays an essential role in transcription activation mediated by nuclear receptors. Probably acts as integral component of corepressor complexes that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of transcription repressor complexes, thereby allowing cofactor exchange.
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O60909
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B4GT2_HUMAN
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Beta-1,4-galactosyltransferase 2 (Beta-1,4-GalTase 2) (Beta4Gal-T2) (b4Gal-T2) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2)
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MSRLLGGTLERVCKAVLLLCLLHFLVAVILYFDVYAQHLAFFSRFSARGPAHALHPAASSSSSSSNCSRPNATASSSGLPEVPSALPGPTAPTLPPCPDSPPGLVGRLLIEFTSPMPLERVQRENPGVLMGGRYTPPDCTPAQTVAVIIPFRHREHHLRYWLHYLHPILRRQRLRYGVYVINQHGEDTFNRAKLLNVGFLEALKEDAAYDCFIFSDVDLVPMDDRNLYRCGDQPRHFAIAMDKFGFRLPYAGYFGGVSGLSKAQFLRINGFPNEYWGWGGEDDDIFNRISLTGMKISRPDIRIGRYRMIKHDRDKHNEPNPQRFTKIQNTKLTMKRDGIGSVRYQVLEVSRQPLFTNITVDIGRPPSWPPRG
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Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Can produce lactose.
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O60911
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CATL2_HUMAN
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Cathepsin L2 (EC 3.4.22.43) (Cathepsin U) (Cathepsin V)
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MNLSLVLAAFCLGIASAVPKFDQNLDTKWYQWKATHRRLYGANEEGWRRAVWEKNMKMIELHNGEYSQGKHGFTMAMNAFGDMTNEEFRQMMGCFRNQKFRKGKVFREPLFLDLPKSVDWRKKGYVTPVKNQKQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDCSRPQGNQGCNGGFMARAFQYVKENGGLDSEESYPYVAVDEICKYRPENSVANDTGFTVVAPGKEKALMKAVATVGPISVAMDAGHSSFQFYKSGIYFEPDCSSKNLDHGVLVVGYGFEGANSNNSKYWLVKNSWGPEWGSNGYVKIAKDKNNHCGIATAASYPNV
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Cysteine protease. May have an important role in corneal physiology.
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O60921
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HUS1_HUMAN
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Checkpoint protein HUS1 (hHUS1)
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MKFRAKIVDGACLNHFTRISNMIAKLAKTCTLRISPDKLNFILCDKLANGGVSMWCELEQENFFNEFQMEGVSAENNEIYLELTSENLSRALKTAQNARALKIKLTNKHFPCLTVSVELLSMSSSSRIVTHDIPIKVIPRKLWKDLQEPVVPDPDVSIYLPVLKTMKSVVEKMKNISNHLVIEANLDGELNLKIETELVCVTTHFKDLGNPPLASESTHEDRNVEHMAEVHIDIRKLLQFLAGQQVNPTKALCNIVNNKMVHFDLLHEDVSLQYFIPALS
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Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase.
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O60927
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PP1RB_HUMAN
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E3 ubiquitin-protein ligase PPP1R11 (EC 2.3.2.27) (Hemochromatosis candidate gene V protein) (HCG V) (Protein phosphatase 1 regulatory subunit 11) (Protein phosphatase inhibitor 3)
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MAEAGAGLSETVTETTVTVTTEPENRSLTIKLRKRKPEKKVEWTSDTVDNEHMGRRSSKCCCIYEKPRAFGESSTESDEEEEEGCGHTHCVRGHRKGRRRATLGPTPTTPPQPPDPSQPPPGPMQH
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Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2 at 'Lys-754' leading to its degradation by the proteasome. Plays a role in regulating inflammatory cytokine release and gram-positive bacterial clearance by functioning, in part, through the ubiquitination and degradation of TLR2. Inhibitor of protein phosphatase 1.
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O60928
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KCJ13_HUMAN
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Inward rectifier potassium channel 13 (Inward rectifier K(+) channel Kir7.1) (Potassium channel, inwardly rectifying subfamily J member 13)
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MDSSNCKVIAPLLSQRYRRMVTKDGHSTLQMDGAQRGLAYLRDAWGILMDMRWRWMMLVFSASFVVHWLVFAVLWYVLAEMNGDLELDHDAPPENHTICVKYITSFTAAFSFSLETQLTIGYGTMFPSGDCPSAIALLAIQMLLGLMLEAFITGAFVAKIARPKNRAFSIRFTDTAVVAHMDGKPNLIFQVANTRPSPLTSVRVSAVLYQERENGKLYQTSVDFHLDGISSDECPFFIFPLTYYHSITPSSPLATLLQHENPSHFELVVFLSAMQEGTGEICQRRTSYLPSEIMLHHCFASLLTRGSKGEYQIKMENFDKTVPEFPTPLVSKSPNRTDLDIHINGQSIDNFQISETGLTE
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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. KCNJ13 has a very low single channel conductance, low sensitivity to block by external barium and cesium, and no dependence of its inward rectification properties on the internal blocking particle magnesium.
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O60930
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RNH1_HUMAN
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Ribonuclease H1 (RNase H1) (EC 3.1.26.4) (Ribonuclease H type II)
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MSWLLFLAHRVALAALPCRRGSRGFGMFYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAFVRKSASPEVSEGHENQHGQESEAKASKRLREPLDGDGHESAEPYAKHMKPSVEPAPPVSRDTFSYMGDFVVVYTDGCCSSNGRRRPRAGIGVYWGPGHPLNVGIRLPGRQTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGAKQSED
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Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. Plays a role in RNA polymerase II (RNAp II) transcription termination by degrading R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site and behind the elongating RNAp II.
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O60931
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CTNS_HUMAN
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Cystinosin
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MIRNWLTIFILFPLKLVEKCESSVSLTVPPVVKLENGSSTNVSLTLRPPLNATLVITFEITFRSKNITILELPDEVVVPPGVTNSSFQVTSQNVGQLTVYLHGNHSNQTGPRIRFLVIRSSAISIINQVIGWIYFVAWSISFYPQVIMNWRRKSVIGLSFDFVALNLTGFVAYSVFNIGLLWVPYIKEQFLLKYPNGVNPVNSNDVFFSLHAVVLTLIIIVQCCLYERGGQRVSWPAIGFLVLAWLFAFVTMIVAAVGVTTWLQFLFCFSYIKLAVTLVKYFPQAYMNFYYKSTEGWSIGNVLLDFTGGSFSLLQMFLQSYNNDQWTLIFGDPTKFGLGVFSIVFDVVFFIQHFCLYRKRPGYDQLN
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Cystine/H(+) symporter that mediates export of cystine, the oxidized dimer of cysteine, from lysosomes. Plays an important role in melanin synthesis by catalyzing cystine export from melanosomes, possibly by inhibiting pheomelanin synthesis. In addition to cystine export, also acts as a positive regulator of mTORC1 signaling in kidney proximal tubular cells, via interactions with components of the v-ATPase and Ragulator complexes (By similarity). Also involved in small GTPase-regulated vesicle trafficking and lysosomal localization of LAMP2A, independently of cystine transporter activity (By similarity).
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O60934
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NBN_HUMAN
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Nibrin (Cell cycle regulatory protein p95) (Nijmegen breakage syndrome protein 1)
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MWKLLPAAGPAGGEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEEKMQNGFSRTLKSGDGITFGVFGSKFRIEYEPLVACSSCLDVSGKTALNQAILQLGGFTVNNWTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEFLKAVESKKQPPQIESFYPPLDEPSIGSKNVDLSGRQERKQIFKGKTFIFLNAKQHKKLSSAVVFGGGEARLITEENEEEHNFFLAPGTCVVDTGITNSQTLIPDCQKKWIQSIMDMLQRQGLRPIPEAEIGLAVIFMTTKNYCDPQGHPSTGLKTTTPGPSLSQGVSVDEKLMPSAPVNTTTYVADTESEQADTWDLSERPKEIKVSKMEQKFRMLSQDAPTVKESCKTSSNNNSMVSNTLAKMRIPNYQLSPTKLPSINKSKDRASQQQQTNSIRNYFQPSTKKRERDEENQEMSSCKSARIETSCSLLEQTQPATPSLWKNKEQHLSENEPVDTNSDNNLFTDTDLKSIVKNSASKSHAAEKLRSNKKREMDDVAIEDEVLEQLFKDTKPELEIDVKVQKQEEDVNVRKRPRMDIETNDTFSDEAVPESSKISQENEIGKKRELKEDSLWSAKEISNNDKLQDDSEMLPKKLLLTEFRSLVIKNSTSRNPSGINDDYGQLKNFKKFKKVTYPGAGKLPHIIGGSDLIAHHARKNTELEEWLRQEMEVQNQHAKEESLADDLFRYNPYLKRRR
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Component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 may be required to bind DNA ends and hold them in close proximity. NBN modulate the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. NBN also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. NBN is a major player in the control of intra-S-phase checkpoint and there is some evidence that NBN is involved in G1 and G2 checkpoints. The roles of NBS1/MRN encompass DNA damage sensor, signal transducer, and effector, which enable cells to maintain DNA integrity and genomic stability. Forms a complex with RBBP8 to link DNA double-strand break sensing to resection. Enhances AKT1 phosphorylation possibly by association with the mTORC2 complex.
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O60936
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NOL3_HUMAN
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Nucleolar protein 3 (Apoptosis repressor with CARD) (Muscle-enriched cytoplasmic protein) (Myp) (Nucleolar protein of 30 kDa) (Nop30)
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MGNAQERPSETIDRERKRLVETLQADSGLLLDALLARGVLTGPEYEALDALPDAERRVRRLLLLVQGKGEAACQELLRCAQRTAGAPDPAWDWQHVGPGYRDRSYDPPCPGHWTPEAPGSGTTCPGLPRASDPDEAGGPEGSEAVQSGTPEEPEPELEAEASKEAEPEPEPEPELEPEAEAEPEPELEPEPDPEPEPDFEERDESEDS
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[Isoform 1]: May be involved in RNA splicing. [Isoform 2]: Functions as an apoptosis repressor that blocks multiple modes of cell death. Inhibits extrinsic apoptotic pathways through two different ways. Firstly by interacting with FAS and FADD upon FAS activation blocking death-inducing signaling complex (DISC) assembly (By similarity). Secondly by interacting with CASP8 in a mitochondria localization- and phosphorylation-dependent manner, limiting the amount of soluble CASP8 available for DISC-mediated activation (By similarity). Inhibits intrinsic apoptotic pathway in response to a wide range of stresses, through its interaction with BAX resulting in BAX inactivation, preventing mitochondrial dysfunction and release of pro-apoptotic factors. Inhibits calcium-mediated cell death by functioning as a cytosolic calcium buffer, dissociating its interaction with CASP8 and maintaining calcium homeostasis. Negatively regulates oxidative stress-induced apoptosis by phosphorylation-dependent suppression of the mitochondria-mediated intrinsic pathway, by blocking CASP2 activation and BAX translocation (By similarity). Negatively regulates hypoxia-induced apoptosis in part by inhibiting the release of cytochrome c from mitochondria in a caspase-independent manner (By similarity). Also inhibits TNF-induced necrosis by preventing TNF-signaling pathway through TNFRSF1A interaction abrogating the recruitment of RIPK1 to complex I (By similarity). Finally through its role as apoptosis repressor, promotes vascular remodeling through inhibition of apoptosis and stimulation of proliferation, in response to hypoxia (By similarity). Inhibits too myoblast differentiation through caspase inhibition (By similarity).
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O60938
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KERA_HUMAN
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Keratocan (KTN) (Keratan sulfate proteoglycan keratocan)
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MAGTICFIMWVLFITDTVWSRSVRQVYEVHDSDDWTIHDFECPMECFCPPSFPTALYCENRGLKEIPAIPSRIWYLYLQNNLIETIPEKPFENATQLRWINLNKNKITNYGIEKGALSQLKKLLFLFLEDNELEEVPSPLPRSLEQLQLARNKVSRIPQGTFSNLENLTLLDLQNNKLVDNAFQRDTFKGLKNLMQLNMAKNALRNMPPRLPANTMQLFLDNNSIEGIPENYFNVIPKVAFLRLNHNKLSDEGLPSRGFDVSSILDLQLSHNQLTKVPRISAHLQHLHLDHNKIKSVNVSVICPSPSMLPAERDSFSYGPHLRYLRLDGNEIKPPIPMALMTCFRLLQAVII
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May be important in developing and maintaining corneal transparency and for the structure of the stromal matrix.
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O60939
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SCN2B_HUMAN
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Sodium channel subunit beta-2
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MHRDAWLPRPAFSLTGLSLFFSLVPPGRSMEVTVPATLNVLNGSDARLPCTFNSCYTVNHKQFSLNWTYQECNNCSEEMFLQFRMKIINLKLERFQDRVEFSGNPSKYDVSVMLRNVQPEDEGIYNCYIMNPPDRHRGHGKIHLQVLMEEPPERDSTVAVIVGASVGGFLAVVILVLMVVKCVRRKKEQKLSTDDLKTEEEGKTDGEGNPDDGAK
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Crucial in the assembly, expression, and functional modulation of the heterotrimeric complex of the sodium channel. The subunit beta-2 causes an increase in the plasma membrane surface area and in its folding into microvilli. Interacts with TNR may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier (By similarity).
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O60941
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DTNB_HUMAN
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Dystrobrevin beta (DTN-B) (Beta-dystrobrevin)
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MIEESGNKRKTMAEKRQLFIEMRAQNFDVIRLSTYRTACKLRFVQKRCNLHLVDIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLATMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTMMADPPPQCLVWLPLMHRLAHVENVFHPVECSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKEHSSWKSPAKKLSHAISKSLGCVPTREPPHPVFPEQPEKPLDLAHIVPPRPLTNMNDTMVSHMSSGVPTPTKRLQYSQDIPSHLADEHALIASYVARLQHCARVLDSPSRLDEEHRLIARYAARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKEEEQKQAAQATGSPHTSPTHGGGRPMPMPVRSTSAGSTPTHCPQDSLSGVGGDVQEAFAQGTRRNLRNDLLVAADSITNTMSSLVKELHSAEEGAEEEEEKMQNGKDRG
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Scaffolding protein that assembles DMD and SNTA1 molecules to the basal membrane of kidney cells and liver sinusoids (By similarity). May function as a repressor of the SYN1 promoter through the binding of repressor element-1 (RE-1), in turn regulates SYN1 expression and may be involved in cell proliferation regulation during the early phase of neural differentiation. May be required for proper maturation and function of a subset of inhibitory synapses (By similarity).
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O60942
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MCE1_HUMAN
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mRNA-capping enzyme (HCAP1) (HCE) [Includes: mRNA 5'-triphosphate monophosphatase (EC 3.6.1.74) (mRNA 5'-phosphatase); mRNA guanylyltransferase (EC 2.7.7.50) (GTP--RNA guanylyltransferase) (GTase)]
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MAHNKIPPRWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMGLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKGHGECPTTENTETFIRLCERFNERNPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGDYLKELFRRYGDIEEAPPPPLLPDWCFEDDEDEDEDEDGKKESEPGSSASFGKRRKERLKLGAIFLEGVTVKGVTQVTTQPKLGEVQQKCHQFCGWEGSGFPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLEFPFRKDLRMHLSNTLLDGEMIIDRVNGQAVPRYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRNKPFFDICTSRKLLEGNFAKEVSHEMDGLIFQPTGKYKPGRCDDILKWKPPSLNSVDFRLKITRMGGEGLLPQNVGLLYVGGYERPFAQIKVTKELKQYDNKIIECKFENNSWVFMRQRTDKSFPNAYNTAMAVCNSISNPVTKEMLFEFIDRCTAASQGQKRKHHLDPDTELMPPPPPKRPRPLT
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Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphate monophosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP reaction intermediate.
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O60952
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LIME_DICDI
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LIM domain-containing protein E (DdLim)
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MSASVKCGACAKTAYPLESVVANNNSYHKGCFKCSTCNSTLNVKTFKSFEGKLYCPVHTPKVSATAVTDSVALKNALNAPKKVAEGLGNAHRGLDEKPNIGLDSMATANALNAPKKVVEGLGNVQKGIGGKPTYAVFGADGQPTGEQQEQQQYTEEQYEQPQEEQQYQEEQQQYQEEEQQYQEEEQQYQEEEQQYEEEQ
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Associates with the actin cytoskeleton and may regulate actin polymerization in lamellipodia, through a rac1-dependent signaling pathway. May play a role in cell motility. Involved in cytokinesis by regulating the microtubule system and linking it to the cortical actin network.
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O60999
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CUL1_DICDI
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Cullin-1 (CUL-1) (Cullin-A)
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MSMMTSTPTKRSVKLDDIWPELEEGIYKIITDLNKGFPKQKWIALYTHVYDYCAASQSKSSAKVGMPKQQASGANYVGEDLYNRLNLFLKKHMSQLLKLTETKMDEPLLNYYYTEWDRYTSAMKYINNIFQYMNRYWIKREIDDGKKEVYEIFILSLVIWRDCLFTPLKQRLTNSLLDIIESERNGYQINTHLIKGVINGYVSLGLNREKPKETILQVYKSGFEELFLTATENYYTNESAKFISENSVADYMKKVETRLNEEVKRVQQYLHQNTESELIAKCEKVLIEKHVEVIWNEFQTLLEKDKIPDLTRMYSLLSRIPRGLEPLRTTLEKHVQNVGLQAVSSIATNGVIEPKVYIETLLKVFKKYNELVTGAFRSDTGFVASLDKACRRFINENAVTIAAKSSSKSPELLARFTDFLLKKSPNNPEESEMEQLLNDVMIVFKYIEDKDVFQDFYSKMLAKRLIHGTSTSEDLEGTMIGKLKSTCGYEYTSKLQRMFTDMSLSRELLDRFNNHIEQVERSSLNIDFSVLVLATGSWPLQPPSTNFSIPKELQACEQLFQKFYQNQHSGRKLNWLHHLSKGELKTKYLQTSKSGYTLQCSTYQIGVLLQFNQYETLTSEEIQESTQLIDSVLKGTLTSLAKSKILLADPPLDDEEIAKTTKFSLNKQFKNKKTKIFINVPVLTQVKEEIDSIHKTVEEDRKLQIQAAIVRIMKMRKQLAHSGLMTEVISQLQTRFNPKVNIIKKCIDILIEKEYLMRVEGKKDHYSYVA
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Probable core component of cullin-based SCF-like E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit (By similarity). Required at several stages during development. CulA and fbxA regulate multicellular development by targeting regA for degradation via a pathway that requires erkB function, leading to an increase in cAMP and PKA activity. {ECO:0000250, ECO:0000269|PubMed:11390363}.
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O61122
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SVKA_DICDI
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Serine/threonine-protein kinase svkA (EC 2.7.11.1) (Severin kinase A)
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MASKKGDPEELYVRQEKIGKGSFGEVFKGINKKTNETIAIKTIDLEDAEDEIEDIQQEINVLSQCESPFVTKYFGSFLKGSKLWIIMEYLAGGSVLDLMKPGPFDEGYIAIILRELLKGLEYLHSEGKIHRDIKAANVLLSASGDVKLADFGVSGQLTDQMTKRNTFVGTPFWMAPEVIKQTGYDSKADIWSMGITALEMAKGEPPRADLHPMRALFLIPKDPPPTLEGNFSKGFKEFCALCLNKDPNQRPTAKDLLKHKFIKAAKKTSSLTDLIERRQKWLQLNGNNADDENDDLDRDAKSNEEDFGWEFPTIKQKSPVAVQEQQQTPQKPTVVSTPIKEQQQQQQPTPVTTPQQPVTTTTTTPTTETKVRSLSNSSQTTPVKTTVAATTAPATTPASNAPTSTTPNGAAVTQQQAPRASALTSVIYPVLSKLLKNTSDENVINALAQLKMAFDNAEKAKPGITHSLIAQIIETLKR
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Involved in regulation of actin cytoskeleton organization during cell motility F-actin fragmenting and capping protein allowing dynamic rearrangements of the actin cytoskeleton. Also part of a regulatory pathway from the centrosome to the midzone, thus regulating the completion of cell division.
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O61125
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STK4_DICDI
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Serine/threonine-protein kinase 4 homolog A (EC 2.7.11.1) (Kinase responsive to stress A) (STE20-like kinase krsA)
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MSTLNVPKETMSRKDPEKFFTIVEKLGEGSYGSVYKAINISTGIVVAIKKVSVDNDLEDMEKEISFMKQCKSPYIVTYYASFRKENEVWIVMEHCGAGSVCDAMKITDKTLSEDQIAVVSRDVLQGLAYLHSVRKIHRDIKAGNILMNHKGESKLADFGVSGQLSDTMAKRQTVIGTPFWMAPEVIQEIGYDYKADIWSYGITCIEMAESKPPLFNVHPMRVIFMIPNPSRPPPKLTEPEKWSPEFNDFLAKCLTRKPELRPSAEELLKHPFITKAKSHSLLVPLIDEQDIIINEKGREVALGIEQRDEEEEDEDEDSEDSDDNRGTMVRAKPRSMQNSGGEDNDEEYDTGTMVITDNKNSYDTVVFNNDDEDSGTMKLKNTMPSNKKNFVPDYMNQFKKSDDDVTNVPLSDKYSSYSLEELKKMLAELEIEREKEVQKTLEKFSINRQALLAVIDEKKSK
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Regulates both cAMP signaling during early development and the stress response. Functions as an activator of adenylylcyclase.
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O61142
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SUB1_PLAFA
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Subtilisin-like protease 1 (EC 3.4.21.62) (PfSUB-1)
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MMLNKKVVALCTLTLHLFCIFLCLGKEVRSEENGKIQDDAKKIVSELRFLEKVEDVIEKSNIGGNEVDADENSFNPDTEVPIEEIEEIKMRELKDVKEEKNKNDNHNNNNNNNNISSSSSSSSNTFGEEKEEVSKKKKKLRLIVSENHATTPSFFQESLLEPDVLSFLESKGNLSNLKNINSMIIELKEDTTDDELISYIKILEEKGALIESDKLVSADNIDISGIKDAIRRGEENIDVNDYKSMLEVENDAEDYDKMFGMFNESHAATSKRKRHSTNERGYDTFSSPSYKTYSKSDYLYDDDNNNNNYYYSHSSNGHNSSSRNSSSSRSRPGKYHFNDEFRNLQWGLDLSRLDETQELINEHQVMSTRICVIDSGIDYNHPDLKDNIELNLKELHGRKGFDDDNNGIVDDIYGANFVNNSGNPMDDNYHGTHVSGIISAIGNNNIGVVGVDVNSKLIICKALDEHKLGRLGDMFKCLDYCISRNAHMINGSFSFDEYSGIFNSSVEYLQRKGILFFVSASNCSHPKSSTPDIRKCDLSINAKYPPILSTVYDNVISVANLKKNDNNNHYSLSINSFYSNKYCQLAAPGTNIYSTAPHNSYRKLNGTSMAAPHVAAIASLIFSINPDLSYKKVIQILKDSIVYLPSLKNMVAWAGYADINKAVNLAIKSKKTYINSNISNKWKKKSRYLH
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Serine protease which plays an essential role in merozoite invasion of and egress from host erythrocytes by processing and activating various merozoite surface and parasitophorous vacuole proteins. Mediates the proteolytic maturation of serine proteases SERA4, SERA5 and SERA6 just prior to merozoite egress. Prior to merozoite egress, cleaves merozoite surface proteins MSP1, MSP6 and MSP7, which form the MSP1/6/7 complex, and thereby may prime the parasite cell surface for invasion of fresh erythrocytes. Prior to merozoite egress, cleaves MSRP2 converting it to MSRP2 p25 form, and RAP1 converting it to RAP1 p67 form.
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O61213
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DUOX1_CAEEL
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Dual oxidase 1 (DUOX1) (EC 1.11.1.-) (EC 1.6.3.1) (Blistered cuticle protein 3) (NADPH thyroid oxidase 1)
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MRSKHVLYIAILFSSIFGGKGIQQNEEFQRYDGWYNNLANSEWGSAGSRLHRDARSYYSDGVYSVNNSLPSARELSDILFKGESGIPNTRGCTTLLAFFSQVVAYEIMQSNGVSCPLETLKIQVPLCDNVFDKECEGKTEIPFTRAKYDKATGNGLNSPREQINERTSWIDGSFIYGTTQPWVSSLRSFKQGRLAEGVPGYPPLNNPHIPLNNPAPPQVHRLMSPDRLFMLGDSRVNENPGLLSFGLILFRWHNYNANQIHREHPDWTDEQIFQAARRLVIASMQKIIAYDFVPGLLGEDVRLSNYTKYMPHVPPGISHAFGAAAFRFPHSIVPPAMLLRKRGNKCEFRTEVGGYPALRLCQNWWNAQDIVKEYSVDEIILGMASQIAERDDNIVVEDLRDYIFGPMHFSRLDVVASSIMRGRDNGVPPYNELRRTFGLAPKTWETMNEDFYKKHTAKVEKLKELYGGNILYLDAYVGGMLEGGENGPGELFKEIIKDQFTRIRDGDRFWFENKLNGLFTDEEVQMIHSITLRDIIKATTDIDETMLQKDVFFFKEGDPCPQPFQVNTTGLEPCVPFMQSTYWTDNDTTYVFTLIGLACVPLICYGIGRYLVNRRIAIGHNSACDSLTTDFANDDCGAKGDIYGVNALEWLQEEYIRQVRIEIENTTLAVKKPRGGILRKIRFETGQKIELFHSMPNPSAMHGPFVLLSQKNNHHLVIRLSSDRDLSKFLDQIRQAASGINAEVIIKDEENSILLSQAITKERRQDRLDLFFREAYAKAFNDSELQDSETSFDSSNDDILNETISREELASAMGMKANNEFVKRMFAMTAKHNEDSLSFNEFLTVLREFVNAPQKQKLQTLFKMCDLEGKNKVLRKDLAELVKSLNQTAGVHITESVQLRLFNEVLHYAGVSNDAKYLTYDDFNALFSDIPDKQPVGLPFNRKNYQPSIGETSSLNSFAVVDRSINSSAPLTLIHKVSAFLETYRQHVFIVFCFVAINLVLFFERFWHYRYMAENRDLRRVMGAGIAITRGAAGALSFCMALILLTVCRNIITLLRETVIAQYIPFDSAIAFHKIVALFAAFWATLHTVGHCVNFYHVGTQSQEGLACLFQEAFFGSNFLPSISYWFFSTITGLTGIALVAVMCIIYVFALPCFIKRAYHAFRLTHLLNIAFYALTLLHGLPKLLDSPKFGYYVVGPIVLFVIDRIIGLMQYYKKLEIVNAEILPSDIIYIEYRRPREFKYKSGQWVTVSSPSISCTFNESHAFSIASSPQDENMKLYIKAVGPWTWKLRSELIRSLNTGSPFPLIHMKGPYGDGNQEWMDYEVAIMVGAGIGVTPYASTLVDLVQRTSSDSFHRVRCRKVYFLWVCSTHKNYEWFVDVLKNVEDQARSGILETHIFVTQTFHKFDLRTTMLYICEKHFRATNSGISMFTGLHAKNHFGRPNFKAFFQFIQSEHKEQSKIGVFSCGPVNLNESIAEGCADANRQRDAPSFAHRFETF
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Plays a role in cuticle biogenesis. In complex with doxa-1 and tsp-15, produces reactive oxygen species (ROS), which are probably used by mlt-7 for tyrosine cross-linking, thus stabilizing cuticular extracellular matrix. May regulate the production of ROS by playing a role in modulating proline catabolism. Required in combination with mlt-7 for correct formation of cross-links in cuticle collagens. Association with the GTPase rho-1 promotes ROS production and this interaction may be modulated by memo-1, in order to control the oxidative stress response and longevity.
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O61219
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DAF31_CAEEL
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N-alpha-acetyltransferase daf-31 (EC 2.3.1.255) (Abnormal dauer formation protein 31)
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MNIRCARVDDLMSMQNANLMCLPENYQMKYYFYHALSWPQLSYIAEDHKGNVVGYVLAKMEEDPGEEPHGHITSLAVKRSYRRLGLANKMMDQTARAMVETYNAKYVSLHVRVSNRAALNLYKNTLKFEIVDTEPKYYADGEDAYAMRRDLAKWAEERNIEPADREAYTTAKTTDDKKKNRS
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Catalytic subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity (By similarity). Plays a role in regulating larval development, metabolism and longevity. Functions downstream or alongside daf-3, daf-12 and daf-16 in the dauer formation pathway. Functions upstream of daf-15 to enable animal development.
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O61267
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LOK_DROME
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Ovarian-specific serine/threonine-protein kinase Lok (EC 2.7.11.1) (Protein loki) (dMNK)
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MARDTQGTQGTQSQASNIWTQVESQPMEKIVWGRLYGKNIKIKSLGTSSKYRIIYTHSSFSVDLNNDEFTAGRGEANDLILTLNDLPEKILTRISKVHFIIKRANCELTNPVYIQDLSRNGTFVNNEKIGTNRMRILKNDDVISLSHPTYKAFVFKDLSPNESIGLPEEINKTYYVNRKLGSGAYGLVRLVYDTRTCQQFAMKIVKKNMLSGARPSTNFSDPDRVLNEAKIMKNLSHPCVVRMHDIVDKPDSVYMVLEFMRGGDLLNRIISNKLLSEDISKLYFYQMCHAVKYLHDRGITHRDLKPDNVLLETNDEETLLKVSDFGLSKFVQKDSVMRTLCGTPLYVAPEVLITGGREAYTKKVDIWSLGVVLFTCLSGTLPFSDEYGTPAAQQIKKGRFAYGHPSWKSVSQRAKLLINQMLIVDPERRPSIDDVLQSSWLRDAPMLQKAKRLMKLDGMEIEEENFLEPPTKRSRR
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May have a role in germline establishment.
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O61307
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TENM_DROME
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Teneurin-m (Tenm) (Odd Oz protein) (Tenascin-like protein)
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MNPYEYESTLDCRDVGGGPTPAHAHPHAQGRTLPMSGHGRPTTDLGPVHGSQTLQHQNQQNLQAAQAAAQSSHYDYEYQHLAHRPPDTANNTAQRTHGRQGFLLEGVTPTAPPDVPPRNPTMSRMQNGRLTVNNPNDADFEPSCLVRTPSGNVYIPSGNLNINKGSPIDFKSGSACSTPTKDTLKGYERSTQGCMGPVLPQRSVMNGLPAHHYSAPMNFRKDLVARCSSPWFGIGSISVLFAFVVMLILLTTTGVIKWNQSPPCSVLVGNEASEVTAAKSTNTDLSKLHNSSVRAKNGQGIGLAQGQSGLGAAGVGSGGGSSAATVTTATSNSGTAQGLQSTSASAEATSSAATSSSQSSLTPSLSSSLANANNGGARTFPARSFPPDGTTFGQITLGQKLTKEIQPYSYWNMQFYQSEPAYVKFDYTIPRGASIGVYGRRNALPTHTQYHFKEVLSGFSASTRTARAAHLSITREVTRYMEPGHWFVSLYNDDGDVQELTFYAAVAEDMTQNCPNGCSGNGQCLLGHCQCNPGFGGDDCSESVCPVLCSQHGEYTNGECICNPGWKGKECSLRHDECEVADCSGHGHCVSGKCQCMRGYKGKFCEEVDCPHPNCSGHGFCADGTCICKKGWKGPDCATMDQDALQCLPDCSGHGTFDLDTQTCTCEAKWSGDDCSKELCDLDCGQHGRCEGDACACDPEWGGEYCNTRLCDVRCNEHGQCKNGTCLCVTGWNGKHCTIEGCPNSCAGHGQCRVSGEGQWECRCYEGWDGPDCGIALELNCGDSKDNDKDGLVDCEDPECCASHVCKTSQLCVSAPKPIDVLLRKQPPAITASFFERMKFLIDESSLQNYAKLETFNESRSAVIRGRVVTSLGMGLVGVRVSTTTLLEGFTLTRDDGWFDLMVNGGGAVTLQFGRAPFRPQSRIVQVPWNEVVIIDLVVMSMSEEKGLAVTTTHTCFAHDYDLMKPVVLASWKHGFQGACPDRSAILAESQVIQESLQIPGTGLNLVYHSSRAAGYLSTIKLQLTPDVIPTSLHLIHLRITIEGILFERIFEADPGIKFTYAWNRLNIYRQRVYGVTTAVVKVGYQYTDCTDIVWDIQTTKLSGHDMSISEVGGWNLDIHHRYNFHEGILQKGDGSNIYLRNKPRIILTTMGDGHQRPLECPDCDGQATKQRLLAPVALAAAPDGSLFVGDFNYIRRIMTDGSIRTVVKLNATRVSYRYHMALSPLDGTLYVSDPESHQIIRVRDTNDYSQPELNWEAVVGSGERCLPGDEAHCGDGALAKDAKLAYPKGIAISSDNILYFADGTNIRMVDRDGIVSTLIGNHMHKSHWKPIPCEGTLKLEEMHLRWPTELAVSPMDNTLHIIDDHMILRMTPDGRVRVISGRPLHCATASTAYDTDLATHATLVMPQSIAFGPLGELYVAESDSQRINRVRVIGTDGRIAPFAGAESKCNCLERGCDCFEAEHYLATSAKFNTIAALAVTPDSHVHIADQANYRIRSVMSSIPEASPSREYEIYAPDMQEIYIFNRFGQHVSTRNILTGETTYVFTYNVNTSNGKLSTVTDAAGNKVFLLRDYTSQVNSIENTKGQKCRLRMTRMKMLHELSTPDNYNVTYEYHGPTGLLRTKLDSTGRSYVYNYDEFGRLTSAVTPTGRVIELSFDLSVKGAQVKVSENAQKEMSLLIQGATVIVRNGAAESRTTVDMDGSTTSITPWGHNLQMEVAPYTILAEQSPLLGESYPVPAKQRTEIAGDLANRFEWRYFVRRQQPLQAGKQSKGPPRPVTEVGRKLRVNGDNVLTLEYDRETQSVVVMVDDKQELLNVTYDRTSRPISFRPQSGDYADVDLEYDRFGRLVSWKWGVLQEAYSFDRNGRLNEIKYGDGSTMVYAFKDMFGSLPLKVTTPRRSDYLLQYDDAGALQSLTTPRGHIHAFSLQTSLGFFKYQYYSPINRHPFEILYNDEGQILAKIHPHQSGKVAFVHDTAGRLETILAGLSSTHYTYQDTTSLVKSVEVQEPGFELRREFKYHAGILKDEKLRFGSKNSLASARYKYAYDGNARLSGIEMAIDDKELPTTRYKYSQNLGQLEVVQDLKITRNAFNRTVIQDSAKQFFAIVDYDQHGRVKSVLMNVKNIDVFRLELDYDLRNRIKSQKTTFGRSTAFDKINYNADGHVVEVLGTNNWKYLFDENGNTVGVVDQGEKFNLGYDIGDRVIKVGDVEFNNYDARGFVVKRGEQKYRYNNRGQLIHSFERERFQSWYYYDDRSRLVAWHDNKGNTTQYYYANPRTPHLVTHVHFPKISRTMKLFYDDRDMLIALEHEDQRYYVATDQNGSPLAFFDQNGSIVKEMKRTPFGRIIKDTKPEFFVPIDFHGGLIDPHTKLVYTEQRQYDPHVGQWMTPLWETLATEMSHPTDVFIYRYHNNDPINPNKPQNYMIDLDSWLQLFGYDLNNMQSSRYTKLAQYTPQASIKSNTLAPDFGVISGLECIVEKTSEKFSDFDFVPKPLLKMEPKMRNLLPRVSYRRGVFGEGVLLSRIGGRALVSVVDGSNSVVQDVVSSVFNNSYFLDLHFSIHDQDVFYFVKDNVLKLRDDNEELRRLGGMFNISTHEISDHGGSAAKELRLHGPDAVVIIKYGVDPEQERHRILKHAHKRAVERAWELEKQLVAAGFQGRGDWTEEEKEELVQHGDVDGWNGIDIHSIHKYPQLADDPGNVAFQRDAKRKRRKTGSSHRSASNRRQLKFGELSA
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Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Acts as a homophilic and heterophilic synaptic cell adhesion molecule that drives synapse assembly. Promotes bi-directional trans-synaptic signaling with Ten-a to organize neuromuscular synapses. Functions in olfactory synaptic partner matching by promoting homophilic cell adhesion between pre-synaptic olfactory receptor neurons (ORN) axons and post-synaptic projection neurons (PN) dendrites partner in the developing antennal lobe to form stable connections. Also required for peripheral axon growth cone guidance and target recognition of motor neurons.
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O61365
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NACH_DROME
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Sodium channel protein Nach (Pickpocket protein 4)
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MGHQEELKPEQVDLKVTPFVGYLRRTWSDFCATSSIHGLKYTRDEDTNKIVHLVWLLISVVMFICAVVMARTFYMDYRSSPTRMNVESDNTPVNRLYFPPVTICPDVLFNMQKSEAFLNTLRLPKGAELRGILRKLHIFYGFMLDDERYSAEDIEQMEALLFLNNLTIPEFVEHLRWNCDEILYRCRFNGEIMDCSKIFQLSKTFFGHCCSFNLRQKGWVNNKLNNLESFKVFHLNSLNFTAQRAIGGLRYGLSVVVRYKDDNYDPLQSYSYGVKLLIQEADAFPSAHSAAKFIAFNSETFAAVRPQETFCSSAVKALIIEERNCVFQNEFPMRYFSDYVYPNCELNCRVTNMVKFCGCHTYFFDFNRTSDRICTFRDIPCLVDNFANIITRKKSTQCYCPLTCEHIDYDVQLTNFPLELNMPVADKFYSGLAKNDGVLHVFINSFSYRRLRRDLLSNMVTLVSNLGSAFSLFVGMSMLSVVEIIYYFSVILRKNYKLECETRSQMLHKKPKFAWPKANDTHSKEQKSVFIIHKS
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Part of a complex that plays a role in tracheal liquid clearance. Probable role in sodium transport.
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O61394
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GALT6_CAEEL
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Probable N-acetylgalactosaminyltransferase 6 (EC 2.4.1.-) (Protein-UDP acetylgalactosaminyltransferase 6) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6) (pp-GaNTase 6)
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MIASLIRSRRRSRRCVVYSVFLFGFLALWGSFALALVFLSDMYIGEDQISTQKAIKPIARSNYHVVVGHYNGNLPEDKKRNLTSEELNANLYAPHDDWGEGGAGVSHLTPEQQKLADSTFAVNQFNLLVSDGISVRRSLPEIRKPSCRNMTYPDNLPTTSVIIVYHNEAYSTLLRTVWSVIDRSPKELLKEIILVDDFSDREFLRYPTLDTTLKPLPTDIKIIRSKERVGLIRARMMGAQEAQGDVLTFLDSHCECTKGWLEPLLTRIKLNRKAVPCPVIDIINDNTFQYQKGIEMFRGGFNWNLQFRWYGMPTAMAKQHLLDPTGPIESPTMAGGLFSINRNYFEELGEYDPGMDIWGGENLEMSFRIWQCGGRVEILPCSHVGHVFRKSSPHDFPGKSSGKVLNTNLLRVAEVWMDDWKHYFYKIAPQAHRMRSSIDVSERVELRKKLNCKSFKWYLQNVFQDHFLPTPLDRFGRMTSSSNSSVCLAWTLRSSGIKTASTADCLKIFHKTQLWLYTGDRRIRTDEHLCLSVVQLLHTTSDWKIQLKECAGFDTEYWDFKPKIGRFQNRKTGLCLASPDIFDPTKDEFNPPIVQKCRSSNDRQNWTITEMSWLPEHP
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Probable glycopeptide transferase involved in O-linked oligosaccharide biosynthesis. Glycopeptide transferases catalyze the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide (By similarity). In contrast to other members of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on peptides that have been tested. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.
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O61443
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MK38B_DROME
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Mitogen-activated protein kinase p38b (MAP kinase p38b) (MAPK p38b) (EC 2.7.11.24)
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MSRKMAKFYKLDINRTEWEIPETYQNLQPVGQGAYGQVCKAVVRGTSTKVAIKKLARPFQSAVHAKRTYRELRLLKHMDHENVIGLLDVFHPGQPADSLDQFQQVYMVTHLMDADLNNIIRTQKLSDDHVQFLVYQILRGLKYIHSAGVIHRDLKPSNIAVNEDCELRILDFGLARPAESEMTGYVATRWYRAPEIMLNWMHYNQTADIWSVGCIMAELLTGRTLFPGTDHIHQLNLIMEVLGTPADEFMSRISSESARNYIRSLPVMPRRNFRDIFRGANPLAIDLLEKMLELDADKRITAEQALAHPYMEKYHDPTDEQTAALYDQSFEENELPVEKWREMVFSEVTAFKPTAAFAELLPKEQ
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Kinase involved in dpp signal transduction pathway in the process of wing morphogenesis when the levels of dpp are enhanced or inhibited. May down-regulate insect immunity gene expression after prolonged infection.
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O61460
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VAB1_CAEEL
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Ephrin receptor 1 (EC 2.7.10.1) (Tyrosine-protein kinase Eph receptor) (Variable abnormal protein 1)
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MRLYNSRILNPHQSIFILVLQCLITIVTSHQEVLFDLSKVGSDLKWDQVSLRHDRDDVWMEETWRNPAATDEKHANQRAYVTCNYDMINPSNWLFSHFIEVKTARRIYIELLFNTRDCDAYLNPKSCKETFSVYLKQFKTSRPGSTKIEKERFSEDIDNWKNIGRLARSNSNMTTETLGMEIDSDTKTIRIAFEEQGICLSLLNVKIYYRICDEFTDQLVYFRPQVTGPKETDMVRMNGSCIPNASKKIPGVDLIGLCMSTGSGIKTSGECVCDSGYSQIADSNGARCESCPTNTYKPKGQSLCKSCPSNSISSEAASSCRCLNGYFRAEDELISMPCTQPPSRPIKLVANAITATSTRLSWNEPSSLGGRPEIWYEVKCSGRGECGTVVMTPGDKKLSTRSVQINGLRPSSDYTFLVFAKNKVSAQFPEFSEKNAVIDIRTRSEEEDVPPVSHLRVDASQSDGITIAWSVSDSDVSDFEVEVRPAIVKKRTFETRHVNMTYTTFIGLNPETVYQFRVRIRDDLRWSQPISYQLGRGLMSSPSSNEVEESQFLNQTGSALLIIIALILIVIAVALCMIVVQKKSKNRKQMSDLDVLDTYKQDSMTPDYHTTSRHHHHQGNLPATLHEQLRSTTKLNAPLIPSFGSPISQPPPYYGGVHPNSGKYKTYVDPTTYEDPYQALIEFTFDISPNDVFITQVIGGGEFGDVCLGGLSKNSPAAAKWSVSNTTMGRGGGGGGYESEPYETVAIKTLKSGSSAKAKAEFLTEATIMGQFSHPNVIRLIGVVTSAEPVMIVAEYMANGSLDQFLRNTDQRGEKVHWEKITEMLYGIASGMKYLTDMGYVHRVSFLRDLAARNVLLDMELRCKIADFGLSRGVRSEGSSVEPEYTTNGGKIPVRWTAPEAITHRKFTPSSDVWSFGVVIWEVCSFGERPYWDWTNQKVISEVMIGYRLPPPMDCPMGLYRIAQWCWKMERHERPTFTQLLATFHKYILQPTLIEHDPGELPRRVQSQSALNTYGSVNVGVVPTPPSSAAPMPSLDDFLRQIGLNHVYGQLVSNNIHSVSDLANTSHLDLLAYGLMSAECSTVRDGLNGRISGSPPGSSGTIHATTRGTRTTRPPREEGFFV
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Receptor for members of the ephrin family (By similarity). Receptor for major sperm proteins (MSPs), that functions as sperm-sensing checkpoint which inhibits oocyte meiotic maturation and ovulation when sperm are not available for fertilization. Specifically, functions to negatively regulates oocyte maturation and MAPK activation in the absence of MSPs. Required for the MSP-mediated increase in the basal sheath cell contraction rate in somatic cells. Phosphorylates phosphatase daf-18/PTEN which probably promotes daf-18 degradation. By inactivating daf-18, regulates positively insulin-like daf-2 signaling cascade. Involved in interactions between neuronal substrate cells and a migrating epithelial sheet in head epidermis morphogenesis. Also required for cell movements following gastrulation and during ventral closure of the epidermis. Might play a role in spermatheca morphogenesis. Involved in axon guidance of SDQL neurons during neurogenesis.
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O61492
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FLOT2_DROME
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Flotillin-2
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MGNIHTTGPNEALIVSGGCCGSTKKRTIVGGWAWAWWLVTDVQRLSLNVMTLNPMCENVETSQGVPLTVTGVAQCKIMKSSSYKQTDYHNDEADELLGTASEQFLGKSVKEIKQTILQTLEGHLRAILGTLTVEEVYKDRDQFAALVREVAAPDVGRMGIEILSFTIKDVYDDVQYLASLGKAQTAVVKRDADAGVAEANRDAGIREAECEKSAMDVKYSTDTKIEDNTRMYKLQKANFDQEINTAKAESQLAYELQAAKIRQRIRNEEIQIEVVERRKQIEIESQEVQRKDRELTGTVKLPAEAEAFRLQTLAQAKQCQTIEGARAEAERIRKIGSAEAHAIELVGKAEAERMRMKAHVYKQYGDAAIMNIVLESLPKIAAEVAAPLAKTDEIVLIGGNDNITNDVTRLVAQLPPSINALTGVDLSKVLSKIPGAKA
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May play a role in axon growth and regeneration. May be involved in epidermal cell adhesion and epidermal structure and function.
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O61577
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KTNA1_STRPU
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Katanin p60 ATPase-containing subunit A1 (Katanin p60 subunit A1) (EC 5.6.1.1) (p60 katanin)
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MSVDEICENTKMGREYALLGNYETSLVYYQGVLQQIQKLLTSVHEPQRKHQWQTIRQELSQEYEHVKNITKTLNGFKSEPAAPEPAPNHRAAPFSHHQHAAKPAAAEPARDPDVWPPPTPVDHRPSPPYQRAARKDPPRRSEPSKPANRAPGNDRGGRGPSDRRGDARSGGGGRGGARGSDKDKNRGGKSDKDKKAPSGEEGDEKKFDPAGYDKDLVENLERDIVQRNPNVHWADIAGLTEAKRLLEEAVVLPLWMPDYFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSASLTSKYHGESEKLVRLLFEMARFYAPSTIFIDEIDSICSKRGTGSEHEASRRVKSELLIQMDGVSGPSAGEESSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPEIDGREQLLRINLKEVPLADDIDLKSIAEKMDGYSGADITNVCRDASMMAMRRRIQGLRPEEIRHIPKEELNQPSTPADFLLALQKVSKSVGKEDLVKYMAWMEEFGSV
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Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. In mitotic spindles this could allow depolymerization of the microtubule end proximal to the centrosome, and subsequent poleward microtubule flux. {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:10531065, ECO:0000269|PubMed:8221885}.
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O61643
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INHB_DROME
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Inhibin beta chain (Activin beta chain) (dAct) (dActivin)
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MRFAFDSNHSQSGAPFKGSRCFFNCQCICCRQGCCVVVVKCCCCFNLNCCNSLGSRKSFPQPAAMRKKVADLEVLRVSRFVAVILVLARWVTAVATLLTSCILLDIFSVPGQSGVADRSQASSRTVHVSVPTTPNETPSSTSETKLKLLYGYTSYDINNDQQVKSNNLCRVLCKSRNRKRQRRRRRRRNHRRRRHRYTKRLHHLMQDNMSGFEQRLNFSDAKCQSLETNYGTNYDLVQGGKLFSQSERSLLVSPLREIEAPWPAIHGSMRNCSKIKRNRANLIWLLIGLVWFEVKLINCNGISSSNYYASNLESHKGCTLCHESGKPNIYTDKDNPHTDYNIYNKYHSNNNFNKKTNQPHNNIAPSDEVRLESIKRQILTKLGLSHKPNVSHPLPKQFIWETIYRVDGGRMIPNNAFGSSGKNLDQKTIKLRAFASPGSHLFNGRGGRTDQRSERDPSHHKYRSPFDFTFNISKNNVYGKVLRNRSLERIDKKNSFLNGWTENRQLKINSQIASMPIELKSHHNSSPKELKSGAVRKVNGINGTQMNENALKKSTYPIDINHSIDNKTHTGKNGEMSHNDYEYFNDYSVQTHDKNRYHEGRSSIGYQPAIHNIEYENQKGHHESFADDHENIDHEDFFGNTQEIITFAEEGTQYRQYRILEFSAQNRRVPSQKLSIRSAQIHIRIDKPHSLWIEKAKSLPEKHLLNTKRKWGANKPHHRIKIWVFQLSTSINITEKGIDKAIIFRASFQVDPKNLGWQKFDLTDTIREWYGHTSHEKLRLLIDCTGCGGRYSLHLFQTSKLRGNSSDYLSTNPNRPFLVLHTESSRTRRVRRRAVDCGGALNGQCCKESFYVSFKALGWDDWIIAPRGYFANYCRGDCTGSFRTPDTFQTFHAHFIEEYRKMGLMNGMRPCCAPIKFSSMSLIYYGDDGIIKRDLPKMVVDECGCP
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Controls several aspects of neuronal morphogenesis essential for optic lobe development, EcR-B1 expression in larval brains, mushroom body remodeling, dorsal neuron morphogenesis and motoneuron axon guidance. Ligands Actbeta and daw act redundantly through the Activin receptor Babo and its transcriptional mediator Smad2 (Smox), to regulate neuroblast numbers and proliferation rates in the developing larval brain.
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O61661
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CHK1_DROME
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Serine/threonine-protein kinase grp (EC 2.7.11.1) (Chk1 homolog) (Protein grapes)
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MAATLTEAGTGPAATREFVEGWTLAQTLGEGAYGEVKLLINRQTGEAVAMKMVDLKKHPDAANSVRKEVCIQKMLQDKHILRFFGKRSQGSVEYIFLEYAAGGELFDRIEPDVGMPQHEAQRYFTQLLSGLNYLHQRGIAHRDLKPENLLLDEHDNVKISDFGMATMFRCKGKERLLDKRCGTLPYVAPEVLQKAYHAQPADLWSCGVILVTMLAGELPWDQPSTNCTEFTNWRDNDHWQLQTPWSKLDTLAISLLRKLLATSPGTRLTLEKTLDHKWCNMQFADNERSYDLVDSAAALEICSPKAKRQRLQSSAHLSNGLDDSISRNYCSQPMPTMRSDDDFNVRLGSGRSKEDGGDRQTLAQEARLSYSFSQPALLDDLLLATQMNQTQNASQNYFQRLVRRMTRFFVTTRWDDTIKRLVGTIERLGGYTCKFGDDGVVTVSTVDRNKLRLVFKAHIIEMDGKILVDCRLSKGCGLEFKRRFIKIKNALEDIVLKGPTTWPIAIATNSVP
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Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. May phosphorylate the CDC25 phosphatase stg, which promotes its degradation. This results in increased inhibitory tyrosine phosphorylation of Cdk1-cyclin complexes and consequent inhibition of cell cycle progression.
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O61667
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EGL1_CAEEL
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Programmed cell death activator egl-1 (Egg-laying defective protein 1)
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MLMLTFASTSSDLLPMSNVFDVQSSVFYNEKNMFYSSSQDFSSCEDSSQFADDSGFFDDSEISSIGYEIGSKLAAMCDDFDAQMMSYSAHASDRSLFHRLLDFFAF
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Plays a major role in programmed cell death (PCD or apoptosis) by negatively regulating ced-9. Binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from a ced-9/ced-4 containing protein complex and allowing ced-4 to activate the cell-killing caspase ced-3. Required to activate programmed cell death in the sister cells of the serotonergic neurosecretory motor (NSM) neurons during embryogenesis. Required to activate programmed cell death in the sister cells of the M4 motor neuron and I1 pharyngeal neuron during embryogenesis. During larval development, required for the elimination of transient presynaptic components upstream of ced-9, ced-4 and ced-3 apoptotic pathway. Together with ain-1, a component of the miRNA-induced-silencing complex (miRISC), and probably upstream of ced-3 and ced-4, regulates temporal cell fate patterning during larval development. Has been shown in two studies to be dispensable in mitochondrial dynamics and morphology during early embryonic development. However, one study shows that during larval development, egl-1 is involved in modulating mitochondrial dynamics, perhaps acting by stabilizing the interaction between ced-9 and drp-1 in order to promote mitochondrial fission. Involved in inducing mitochondrial fragmentation during apoptosis, probably acting via ced-9 and dynamin-related protein drp-1.
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O61668
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SIX1_MESMA
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Beta-insect excitatory toxin BmKIT1 (Bm32-VI) (BmK IT1) (BmK IT) (BmKIT) (BmK-betaIT)
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MKFFLIFLVIFPIMGVLGKKNGYAVDSSGKVSECLLNNYCNNICTKVYYATSGYCCLLSCYCFGLDDDKAVLKIKDATKSYCDVQIIG
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Excitatory insect beta-toxins induce a spastic paralysis. They bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is active only on insects.
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O61705
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SCXA_MESMA
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Neurotoxin BmK-M10 (Alpha-neurotoxin TX9) (BmK AngM1) (BmK-X) (BmKX) (BmK10) (BmKalphaTx9) (Bmk M10) (BmkM10) (Neurotoxin M10)
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MNYLVMISFALLLMKGVESVRDAYIAKPENCVYECGITQDCNKLCTENGAESGYCQWGGKYGNACWCIKLPDSVPIRVPGKCQR
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Binds to voltage-dependent sodium channels (Nav) and voltage-dependent delayed rectifier potassium channels and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission. Administration to mice at a dosage of 0.8 mg/kg produces an analgesic effect.
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O61707
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TAF4_CAEEL
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Transcription initiation factor TFIID subunit 4 (TBP-associated transcription factor family member taf-4)
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MSLPRFRLVQGKAIGERSTPGVSTPEPAPPQIKQEVDYQDAHQMAPEPVEAPQAQNHQMQPPRQPIQQQMQHFQSPSPMAPQGPPGTPQNSAAAAAAASDDKNVTKCVRFLKTLINLSNNDDPEMPDKAARVKELIRGVIYLETTAEEFTRNLQQVLKSQAQPHLLPFLQNTLPALRNAVRNGTASVEGVNPPPGYVFNNGRTPGPPQPPPPQQQSQQQPPLEMRQIPNPNQIPPQMVQGGPHMVSVGARPMIRPMGPGGPSPMGLQGPVRGPMGHQMVQMHPPPPPQQIQQQHPAPPVEMEVEENLQPTAAATATRQYPEGSLKSSILKPDEVLNRITKRMMSSCSVEEEALVAISDAVESHLRELITLMAGVAEHRVESLRIPENYVAIDDVKRQLRFLEDLDRQEEELRESREKESLIRMSKNKNSGKETIEKAKEMQRQDAEAKRNRDANAAAIAALSSNKTVKNKWENTGAATTAPRPRTVRVTTRDLHLLVNQDSRFTGTFIREKMSYGGPAVDTTI
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The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (By similarity). TFIID recognizes and binds promoters via its subunit tbp-1, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (By similarity). The TFIID complex consists of tbp-1 and TBP-associated factors (TAFs), including taf-4 (By similarity). Essential for early embryonic development, probably acting via activating transcription initiation by RNA polymerase II, as part of the TFIID complex. In early embryos, but not oocytes, remains, presumably inactive, in the cytoplasm as a result of binding to oma-1. Upon degradation of oma-1, taf-4 is released and bound by taf-12, and the taf-4/12 heterodimer translocates to the nucleus and transcriptional repression is relieved. Involved in lifespan extension in a manner dependent upon mitochondrial function. Plays a role in modulating polyribosome formation.
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O61715
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INX19_CAEEL
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Innexin-19 (Neuronal symmetry protein 5) (Protein opu-19)
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MWRTPASTGPLRQDRQMFFHATLARSFINALSVRGDDDAVDRLNYYYTPLILAVCCLVISAKQYGGTPIECWVNPHSRESMEEYIESYCWIQNTYWIPMYENVPDDHTAREEKQIGYYQWVPFILIAEALMFSLPCIFWRLCSFQSGLNIQTLINAACDGQALLDASDRQKAVEAITTNFVDNLDLQSPNGRIRARGWIARIKFSRFLSGQCLSILHSFTKLLYSMNVVAQFLILNACLKSSDFLFFGFQVLNDIWAGRPWTETGHFPRVTLCDFEVRYLANLNRYTVQCALLINIINEKVFAFLWCWYMILAIITTCSFIYWIANSFIHSEKVDYVMKFIQIAESSEFKKLQKFEKDATVERLYTVIAFAPHLLDTFVSDFLKSDGVLMLRMISNHAGDMIVVQLVRNLWQEFRERNWREFEEHEEMKDVEMRRIHGGERIVISNPGQTKSFL
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Structural component of the gap junctions that specifically coordinates left-right asymmetry in the developing nervous system. Acts by forming gap junction network linking embryonic neurons and providing electrical coupling between cells, leading to promote or inhibit AWC signaling. Required for the left and right AWC olfactory neurons to establish asymmetric patterns of gene expression during embryogenesis. Acts autonomously.
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O61722
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PRL1_DROME
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PRL-1 phosphatase (EC 3.1.3.48) (Phosphatase of regenerating liver-1)
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MSITMRQKDLRPAPALIEYKGMKFLITDRPSDITINHYIMELKKNNVNTVVRVCEPSYNTDELETQGITVKDLAFEDGTFPPQQVVDEWFEVLKDKYQQNPEACVAVHCVAGLGRAPVLVALALIELGLKYEAAVEMIRDKRRGAINAKQLSFLEKYKPKARLKHKNGHKNSCSVQ
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Probable phosphatase (Probable). Inhibits growth possibly by negatively regulating Src64B-induced growth. Regulates central nervous system circuit formation and stabilization of synapse-dense terminal arbors. In dorsocentral neurons, regulates synaptogenesis in terminal arbors via modulation of the insulin receptor pathway, likely upstream of Akt1, and via reduction of PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) levels. In the nervous system, plays a protective role together with uex in response to olfactory carbon dioxide stimulation.
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O61734
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CYCL_DROME
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Protein cycle (Brain and muscle ARNT-like 1) (BMAL1) (MOP3)
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MEVQEFCENMEEIEDENYDEEKSARTSDENRKQNHSEIEKRRRDKMNTYINELSSMIPMCFAMQRKLDKLTVLRMAVQHLRGIRGSGSLHPFNGSDYRPSFLSDQELKMIILQASEGFLFVVGCDRGRILYVSDSVSSVLNSTQADLLGQSWFDVLHPKDIGKVKEQLSSLEQCPRERLIDAKTMLPVKTDVPQSLCRLCPGARRSFFCRMKLRTASNNQIKEESDTSSSSRSSTKRKSRLTTGHKYRVIQCTGYLKSWTPIKDEDQDADSDEQTTNLSCLVAIGRIPPNVRNSTVPASLDNHPNIRHVLFISRHSGEGKFLFIDQRATLVIGFLPQEILGTSFYEYFHNEDIAALMESHKMVMQVPEKVTTQVYRFRCKDNSYIQLQSEWRAFKNPWTSEIDYIIAKNSVFL
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Putative transcription factor involved in the generation of biological rhythms. Activates cycling transcription of Period (PER) and Timeless (TIM) by binding to the E-box (5'-CACGTG-3') present in their promoters.
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O61735
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CLOCK_DROME
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Circadian locomoter output cycles protein kaput (dCLOCK) (dPAS1)
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MDDESDDKDDTKSFLCRKSRNLSEKKRRDQFNSLVNDLSALISTSSRKMDKSTVLKSTIAFLKNHNEATDRSKVFEIQQDWKPAFLSNDEYTHLMLESLDGFMMVFSSMGSIFYASESITSQLGYLPQDLYNMTIYDLAYEMDHEALLNIFMNPTPVIEPRQTDISSSNQITFYTHLRRGGMEKVDANAYELVKFVGYFRNDTNTSTGSSSEVSNGSNGQPAVLPRIFQQNPNAEVDKKLVFVGTGRVQNPQLIREMSIIDPTSNEFTSKHSMEWKFLFLDHRAPPIIGYMPFEVLGTSGYDYYHFDDLDSIVACHEELRQTGEGKSCYYRFLTKGQQWIWLQTDYYVSYHQFNSKPDYVVCTHKVVSYAEVLKDSRKEGQKSGNSNSITNNGSSKVIASTGTSSKSASATTTLRDFELSSQNLDSTLLGNSLASLGTETAATSPAVDSSPMWSASAVQPSGSCQINPLKTSRPASSYGNISSTGISPKAKRKCYFYNNRGNDSDSTSMSTDSVTSRQSMMTHVSSQSQRQRSHHREHHRENHHNQSHHHMQQQQQHQNQQQQHQQHQQLQQQLQHTVGTPKMVPLLPIASTQIMAGNACQFPQPAYPLASPQLVAPTFLEPPQYLTAIPMQPVIAPFPVAPVLSPLPVQSQTDMLPDTVVMTPTQSQLQDQLQRKHDELQKLILQQQNELRIVSEQLLLSRYTYLQPMMSMGFAPGNMTAAAVGNLGASGQRGLNFTGSNAVQPQFNQYGFALNSEQMLNQQDQQMMMQQQQNLHTQHQHNLQQQHQSHSQLQQHTQQQHQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQLQLQQQNDILLREDIDDIDAFLNLSPLHSLGSQSTINPFNSSSNNNNQSYNGGSNLNNGNQNNNNRSSNPPQNNNEDSLLSCMQMATESSPSINFHMGISDDGSETQSEDNKMMHTSGSNLVQQQQQQQQQQQILQQHQQQSNSFFSSNPFLNSQNQNQNQLPNDLEILPYQMSQEQSQNLFNSPHTAPGSSQ
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Circadian regulator that acts as a transcription factor and generates a rhythmic output with a period of about 24 hours. Oscillates in antiphase to the cycling observed for period (PER) and timeless (TIM). According to PubMed:9742131, reaches peak abundance within several hours of the dark-light transition at ZT0 (zeitgeber 0), whereas PubMed:9616122 describes bimodal oscillating expression with maximum at ZT5 and ZT23. Clock-cycle heterodimers activate cycling transcription of PER and TIM by binding to the E-box (5'-CACGTG-3') present in their promoters. Once induced, Period and Timeless block Clock's ability to transactivate their promoters.
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O61789
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EGG5_CAEEL
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Inactive protein-tyrosine phosphatase egg-5 (Egg sterile protein 5) (Protein-tyrosine phosphatase-like protein egg-5)
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MALNSEVMFREQINAMRSQAGRKRATSLQSFCSGNTDDSSADSTDNMDMMVDYPQQKGVSCMRARFNSESTLSKSFRKKVKKLAQKDRRSKERLNGNSEEDAIEVPRGAPSTYAAPSKLRKSKALDCLVSEKPKDEGRSEDSGHGADIEMAKGHFNDVRMKVFAARTAMQVEPALVMKTRKALEMKNAVLENHQSPGAFSLHAAYKIAASAESRVGSITPCNKKVTKEAMANLIRSSYDDTEITQELLFSSKFDSKWKGRYTDIYMRRDENGKKPKRPVNGQGWVMPLKSICEKFGINSTFFTNHRIDLKSARDQVLLMRLLSHDQTSTWISDIHPEAVKNETLAEYLLRELDASTMQKRVQAFKANVLADRDRVRVAGQFYNNIRIGKRMFGAARKAKYLSTIIGGMERRFEILENSVNHIPFTHSASDNNQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPERCEYYWPKSPSDPAVTVPGGLRIENFGVYQAPDPLFRVTHLRLIGPDREERHVEHWQGDVNNSSNMYSPLNILRLLRNASKPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKYPVQRAVQFLRQRRPFSIETPMQYIFVHRLVAFFFRDVIGSAKELDVDYERWLQERSERMFLDDLAAPIPGYRLLSPRADPDIVRMVGRPERPNYRREAPDCVGEMPNKVAAVDGILSPAKSVFEF
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Inactive phosphatase which acts redundantly with egg-4 in the oocyte-to-zygote transition. Required for polarized cortical actin cytoskeleton rearrangement in the oocyte before and after fertilization. Together with egg-4, required for the cortical localization of kinase mbk-2 in maturing oocyte until the end of meiosis I. Also required for kinase mbk-2, pseudophosphatase egg-3 and chitin synthase chs-1 localization to cytoplasmic foci after fertilization.
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O61847
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CDK2_CAEEL
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Cyclin-dependent kinase 2 (EC 2.7.11.22) (Cell division protein kinase 2)
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MSREIRSLESIISDARENTHEKMLIRKQRDMTTDIAPERDLQGRFCSLRRIGEGTYGVVFKAIHVRDNVKCALKMIRTDRDEEGIPSTCLREISCIKDLQHDNIVTLFDIIYANSKLYMVFEFIDRDLKNLLEMLEPTNSVLPPNYVKSFMWQLLSALSYCHLRRIVHRDLKPQNILVSDSGVIKIADFGLARNFSFPSRNYTHEVVTLWYRPPEILLGSQRYSTSLDMWSLGCIFSEIASNKPLFPGECEISQLFKIFEIVGTPNIKSWPGVDSFPHYKAVFPQWPVNLKKLEETSCLTGNGLDVLREILRYPPERRLTAKGALSHRYFLQNGFTQNRPSVTDLMKDIRAQNRTPPLLNNHQEKSIF
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Serine/threonine-protein kinase which, in association with cye-1, regulates proliferation, quiescent state and cell fate during the development of several cell lineages. In the embryo, initiates the establishment of cell polarity through the recruitment of the centrosomal proteins spd-2 and spd-5 during prophase. Phosphorylation and inhibition of the translational repressor gld-1 by the cdk-2/cye-1 complex regulates the pool of germline stem cells and the size of the mitotic zone in the gonads by preventing entry into meiosis.
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O61866
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LIPL5_CAEEL
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Lipase lipl-5 (EC 3.1.1.-) (Lipase-like 5)
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MWRFAVFLAAFFVQDVVGSHGDPELHMTTPQIIERWGYPAMIYTVATDDGYILEMHRIPFGKTNVTWPNGKRPVVFMQHGLLCASSDWVVNLPDQSAGFLFADAGFDVWLGNMRGNTYSMKHKDLKPSHSAFWDWSWDEMATYDLNAMINHVLEVTGQDSVYYMGHSQGTLTMFSHLSKDDGSFAKKIKKFFALAPIGSVKHIKGFLSFFANYFSLEFDGWFDIFGAGEFLPNNWAMKLAAKDICGGLKVEADLCDNVLFLIAGPESDQWNQTRVPVYATHDPAGTSTQNIVHWMQMVHHGGVPAYDWGTKTNKKKYGQANPPEYDFTAIKGTKIYLYWSDADWLADTPDVPDYLLTRLNPAIVAQNNHLPDYNHLDFTWGLRAPDDIYRPAIKLCTDDYLGK
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Lipase involved in lipid homeostasis. Regulates mitochondrial lipid composition, in particular cardiolipins and coenzyme Q-9 levels, in response to nutrient availability. Does not affect global triglyceride levels in response to nutrient availability. However, in coelomocytes, specifically promotes triglyceride catabolism and lifespan extension in response to nutrient deprivation.
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O61931
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ERGO1_CAEEL
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Piwi-like protein ergo-1 (Endogenous RNA interference deficient argonaute protein 1)
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MSYNNGGGGGGGGYRNDRDDRYHNNDRQNYRSSDQGRSGYNDDRRDNRYDDRRGSNNDRGCYDQHDRRGSSNDDRRGYRGYNQGGGGYQQQYSQDARYGSNQRNDNYGNNRGSHGGANMYSQNGGNRGGGGGRVGGGRTAAGMSNPGDLVGGADQPIHSVSKKSLRHNAQEFAVRPKTMVQDKGLGQKTTLLTNHTLVQLPQEPITLHVFNIEVFINGKSSNKRELCGPRFWEILKENKPTFGMPNQYIFNDVNMMWSTNKLRQSEGRTNNRRMNFVWKYVKQIKFGGNIEDEETMQLLSTLIDAIATQRARLPLAPPKYTVFKRLTYLICEEAYEPELPDVSLCHKLRIGTDARVGVSIAIRTNLRAGITACFDLGHTLFTRPAYPLVRLLCDIIEHSVVLDEAFEMKYDAALRACNVSDENLRVMTQILTKMTLQLSTETGDYVGEDGEVIVRPAPTIRNPGRNFKFVGLGAPADRYYFTSDGVELTVADYYLQKYNIRLRYPNLPCVLKKAPEQCGNKHSAMPLELVSYIVVPTRYGGFTMPDMRADMINKTTYTAQQRGKLLQHIIAQKSLSGIEPPVSNNDDYMKKHKLVMKREPIRVKATILPPPTLVYGDSVFHDEHHIGEWEAVTHDPPRQVLDGAVFRRKLYKSSEQPLMKRLMGSILLIQSPRQCRDFDYNQQGYHAIMRAIEDSGQPVLWADENKHSAVIQGELQFNQNQHGIEVIEQFLQNIKSTIGEYERDGEVIVPIVFAVFQARATVYSGNNNEYNDYNVLKYLADNKYGIHTQGILEKSLGVVGPSPKNCALTRLMVEKVLGKVGTTHRKLERGGAHKTWTIFTDPAKPTLVLGIDVSHPSTRDRETGNVLQKMSAATVVGNIDLDVTEFRASSRIQDTGVECLIDFSKEIDERIGEFIDHTGKRPAHIVVYRDGLSEGDFQKYLFEERVCIEERCLKIDTSFQPSITYIVVTKRHHTQFFLEDPSQGYESQGYNVLPGTLIEDAVTTNKYYDFFLSTQIGNEGCFRPTHYYVLHDTWTGKPDSFWPTVTHALTYNFCRSTTTVALPAPVLYAHLAAKRAKETLDGINTYKSVNNIYCDLESFGDLCEVNKDMNVNEKLEGMTFV
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Argonaute protein required for gene silencing in the endogenous RNA interference (RNAi) pathway. Involved in the 26G RNAi pathway and associates with both unmethylated and methylated 26G small interfering RNAs (26G-siRNAs), which are a class of 26 nucleotide siRNAs that possess a guanine residue at the 5'-end. Associated 26G-siRNAs are methylated by the methyltransferase henn-1, which stabilizes the siRNAs. Association with 26G-siRNAs is required for the biogenesis of secondary 22G-siRNAs (a class of 22 nucleotide siRNAs that possess a triphosphorylated guanine residue at the 5'-end). May be involved in passenger strand cleavage of target 26G-siRNAs.
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O61955
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IF4E3_CAEEL
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Eukaryotic translation initiation factor 4E-3 (eIF-4E-3) (eIF4E-3) (eIF-4F 25 kDa subunit) (mRNA cap-binding protein)
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MSTSVAENKALSASGDVNASDASVPPELLTRHPLQNRWALWYLKADRNKEWEDCLKMVSLFDTVEDFWSLYNHIQSAGGLNWGSDYYLFKEGIKPMWEDVNNVQGGRWLVVVDKQKLQRRTQLLDHYWLELLMAIVGEQFDEYGDYICGAVVNVRQKGDKVSLWTRDATRDDVNLRIGQVLKQKLSIPDTEILRYEVHKDSSARTSSTVKPRICLPAKDPAPVKEKGPAATTSPSNPGTEATGTSPATPTP
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Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. All 5 eIF4E proteins bind monomethyl cap structures. Only ife-1, ife-2 and ife-5 bind trimethyl cap structures which result from trans-splicing. Translation of trimethyl cap structure mRNAs may be regulated by intracellular redox state disulfide bonds change the width and depth of the cap-binding cavity determining selectivity to mRNA caps. Ife-3 is essential for viability. Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively. Within the pid-1 variant of the PETISCO complex binds to capped 21U-RNA precursor molecules, possibly playing a role in the processing of the 5' end of the molecules to promote binding of other complex components such as pid-3. However, it is not essential for the biogenesis of 21U-RNAs by itself. Within the tost-1 variant of the PETISCO complex binds to splice leader SL1 RNA fragments to possibly play a role in their processing.
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O61967
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LAP1_CAEEL
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Protein lap1 (Lethal protein 413)
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MPAFFCLPMACQRQVDSIDRSQSNLQAIPSDIFRFRKLEDLNLTMNNIKELDHRLFSLRHLRILDVSDNELAVLPAEIGNLTQLIELNLNRNSIAKLPDTMQNCKLLTTLNLSSNPFTRLPETICECSSITILSLNETSLTLLPSNIGSLTNLRVLEARDNLLRTIPLSIVELRKLEELDLGQNELEALPAEIGKLTSLREFYVDINSLTSLPDSISGCRMLDQLDVSENQIIRLPENLGRMPNLTDLNISINEIIELPSSFGELKRLQMLKADRNSLHNLTSEIGKCQSLTELYLGQNFLTDLPDTIGDLRQLTTLNVDCNNLSDIPDTIGNCKSLTVLSLRQNILTELPMTIGKCENLTVLDVASNKLPHLPFTVKVLYKLQALWLSENQTQSILKLSETRDDRKGIKVVTCYLLPQVDAIDGEGRSGSAQHNTDRGAFLGGPKVHFHDQADTTFEENKEAEIHLGNFERHNTPHPKTPKHKKGSIDGHMLPHEIDQPRQLSLVSNHRTSTSSFGESSNSINRDLADIRAQNGVREATLSPEREERMATSLSSLSNLAAGTQNMHTIRIQKDDTGKLGLSFAGGTSNDPAPNSNGDSGLFVTKVTPGSAAYRCGLREGDKLIRANDVNMINASQDNAMEAIKKRETVELVVLRRSPSPVSRTSEPSLNGSSHQLNHFDAGSPDSTMFVTSSTPVYAS
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Critical role in assembling adherens junctions adapter protein involved in polarizing protein trafficking in epithelial cells. Necessary to maintain, not establish, the entire terminal web (organelle-depleted, intermediate filament-rich layer of cytoplasm that underlies the apical microvilli of polarized epithelial cells) or brush border assembly at the apical surface gut cells. Required for correct localization of ifb-2 intermediate filaments in the terminal web. Required for dlg-1 lateral localization. With dlg-1, cooperatively regulates ajm-1 localization to apical junctions.
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O62090
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PRY1_CAEEL
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Axin-like protein pry-1 (Protein polyray)
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METHLGWARSLEAVLSDRSALDAFQEWLIEYSSPQYLDLFFAIRAYERMALEGKPEKSQLSKSIYSKFLSSRTGNCEAIPKHFRAPIGEKLRHGTELEDRVFSHCSNFVQEFLRRQHEEFVGSEEFIEAFNKMSSTTADQLPGGSAHHSSHQNTMRRSSGTTSRKSAAQIATQLTAEALLKSKHDRHSKLGETKLEKMYPPTRQPYVCNATTSHNDSAVSSTFSGDTPEAHRMHSNRLRHIRDEQARENHGTMTLPRVEKASVDGQQWDHSSESGRRNFAMEITRKLLRHIDKVKLNDEMEKRIDDIEECRYTTIDMVNGTEPNDDLGKIDEDEELDDYLKMKMTDDSQKGSTNRSPKGPAGEPNKSGEGSKNTTLSPTNRAPAQLHNTIRVPRRKDYPRDTSASLKSHRHHQIDTNRMMSQSMCAPSYSSASSSYSRDSFAPAPTTRVNFAPGSSKSSQFYDSSGIGSMAPSAFSATSSLDYKDRRQHRKAPTPKKHSKIGKNLSNLITISYLGTDKIPVVTHVPNDGPMTLAEFKRHFALPNGAHQLFFKTECEDGSAPFQLLLIKDEHHLLPVFEGRIAAELR
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Works in parallel with axl-1 in negatively regulating bar-1 signaling in vulval precursor cells and Q neuroblasts. Inhibits Wnt signaling, which affects tissue specific expression of Hox genes, egl-5, lin-39 and mab-5. This in turn affects QR (postembryonic neuroblast) cell migration, vulval cell fate specification, and the development of sensory structures by the seam cell lineage. Has a role in alae V cell patterning, ray formation in the male tail and axon guidance. Does not affect B cell polarity.
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O62137
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ACX12_CAEEL
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Acyl-coenzyme A oxidase acox-1.2 (EC 1.3.3.-)
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MANRSIRDGDNPELLEERRMATFDTDKMAAVIYGSEEFARRRREITDAVSKIPELADIKPYPFLTREEKVTEGTRKISILTKYLNQLIDRDNEEESLHLHREVIGYEGHPFALHDALFIPTLQSQASDEQQEKWLERARRREIIGCYAQTELGHGSNLRNLETTAVYDIASQEFVLHTPTTTALKWWPGALGKSCNYALVVAELIIKRNNYGPHFFMVQLRDEKTHIPLKGVTVGDIGPKMNFNAADNGYLGLNNLRVPRTNLLMRHCKVEADGTYVKPPHAKIGYSGMVKIRSQMAMEQGLFLAHALTIAARYSAVRRQGHLDDKQVEVKVLDYQTQQHRLFPSLARAYAFIFTGFETIHLYSQLLKDVDMGNTSGMADLHALTSGLKSVVAHETGEGIEQARMACGGHGYSMASYISVVYGIAIGGCTYEGENMVMLLQLARYLVKSVELIKAGKAKKLGPVASYLADKSDETDLTSLNGYVKMFENMARRQAWKATEKFLKLMESGESREVAWNKSAVELTRASRLHTRLFIIEAFMRRVSRIEDIPVKEVLTDLLHLHVNYELLDVATYALEFMSFTQLDYVRDQLYLYLEKIRPNAVSLVDSFQISDMQLRSVLGRRDGHVYENLFKWAKSSPLNNADVLPSVEKYLKPMMEKAKL
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Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains of ascaroside pheromones, which regulates development and behavior. Specifically, shortens ascarosides with 5-carbon omega side chain (asc-omega-C5). Does not shorten indol-3-carbonyl(IC)-ascaroside with 7-carbon or 9-carbon side chains. Does not catalyze the desaturation of fatty acids or hydroxylated fatty acids.
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O62138
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ACX13_CAEEL
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Acyl-coenzyme A oxidase acox-1.3 (EC 1.3.3.-)
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MSSICKGDNSDLTEERKNATFDTDKMAAVIYGREEIASRRRQLTESISRIHELAESKPLVFMTREEKIAESCRKLEVLSRHWNQTPFNRDNEEDALHIYREVLGMEGHPLALHDTMFIPTLVAQASQEQQEKWLGRARRKEIIGCYAQTEMGHGTNLRKLETTATYSPDTQEFILNTPTITALKWWPGALGKSSNNAIVVANLLIKDQNYGPHPFMVQLRDEKTHIPLKGIVVGDIGPKMAFNGADNGYLGFNNHRIPRTNLLMRHTKVEANGTYIKPSHAKIGYSSMVKVRSRMAMDQGLFLASALVIAVRYSAVRRQGFLEDKTQKVKVLDYQTQQHRLFPSLARAYAFIFTGFETIHLYSQLLKDVDMGNTSGMADLHALTSGLKSVVTHQTGEGIEQARMACGEHGYSMASYISEIYGVAIGGCTYEGENMVMLLQLARYLVKSVELIKSGEEKKLGPMVSYLAAKGGHPDLSSLNGYVTAFEHMARRQAWKATEKFLKLMETGESREVAWNKSAVELTRASRLHTRLFIIEAFMRRVSRIEDIPVKEVLTDLLHLHVNYELLDVATYALEFMSSTQLDYIRDQLYLYLEKIRPSAVSLVDSFQISDMQLRSVLGRRDGNVYENLFKWAKSSPLNKSDVLPSVDKYLKPMMEKAKL
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Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains of ascaroside pheromones, which regulates development and behavior. Specifically, shortens ascarosides with a 7-carbon side chain (asc-C7). Does not catalyze the desaturation of fatty acids or hydroxylated fatty acids. Involved in the biosynthesis of asc-C6-MK (daumone 2) and asc-delta-C9 (daumone 3) but not asc-C7 (daumone 1) daumones are pheromones produced during unfavourable growth conditions which promote entry into the dauer stage.
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O62139
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ACX14_CAEEL
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Acyl-coenzyme A oxidase acox-1.4 (EC 1.3.3.-)
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MHLNTSICEVDNPDLTEEREKGTFDTDKMAAVIYGSEKLARRRREISEAVSKIPELADTQPFPFMDRLEKITEGSRKLEVLNNNIRDIIDYDDNGERLHIYQEVTGMEGHPLALHEVMFIPALVSQASKEQQEKWLGRARRREIIGCYAQTEMGHGTNLRKLETTATYFPDTQEFVLNTPTTTALKWWPGALGKSSNYAVVVVDMIIKGKSYGPHPFMVQLRDEKTHIPLKGIVVGDIGPKMSFNGGDNGFLGFDKFRVPRTNLLMRHVRVEADGTYVKPPHAKVNHSAMVHVRSHMATGQGALLAQALIIAVRYSAVRRQGFLENKTQEVKVLDYQTQQHRLFPSLARAYAFIFTGFETIHLYSQLLKDVDMGNTSGMADLHALTSGLKSVVTHQTGEGIEQARMACGGHGYSMASYISEIYGIAIGGCTYEGENMVMLLQLARYLVKSVELIKSGEAKKLGPMVSYLAAKGGHPDLSSLNGYVTAFEHMARRQAWKATEKFLKLMESGESREIAWNKSTVELTRASRLHTRLFIIEAFMRRVSRIEDIPVKEVLTDLLHLHVNYELLDVATYALEFMSSTQLDYIRDQLYLYLEKIRPSAVSLVDSFQISDMQLRSVLGRRDGNVYENLFKWAKSSPLNKSDVLPSVDKYLMPMMEKAKL
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Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains of ascaroside pheromones, which regulates development and behavior. Specifically, shortens ascarosides with a 9-carbon side chain (asc-C9) and, in association with acox-1.1, may contribute to the shortening of ascarosides with a 11-carbon side chain (asc-C11). May contribute to the production of indol-3-carbonyl(IC)-ascarosides in association with acox-1.1 and acox-3.
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O62140
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ACX11_CAEEL
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Acyl-coenzyme A oxidase acox-1.1 (EC 1.3.3.-) (EC 1.3.3.6)
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MVHLNKTIQEGDNPDLTAERLTATFDTHAMAAQIYGGEMRARRRREITAKLAEIPELHDSMPLPYMTREEKIMESARKLTVLTQRMSEIIDPTDAGELYHLNNEVLGIEGNPMALHGVMFIPALNAQASDEQQAKWLIRALRREIIGTYAQTEMGHGTNLQNLETTATYDIGTQEFVLHTPKITALKWWPGNLGKSSNYAVVVAHMYIKGKNFGPHTFMVPLRDEKTHKPLPGITIGDIGPKMAYNIVDNGFLGFNNYRIPRTNLLMRHTKVEADGTYIKPPHAKINYSAMVHVRSYMLTGQAIMLSYALNIATRYSAVRRQGQIDKNEPEVKVLEYQTQQHRLFPFIARAYAFQFAGAETVKLYERVLKEMKSGNVSLMADLHALTSGLKSVVTHQTGEGIEQARMACGGHGYSMASYISEIYGVAIGGCTYEGENMVMLLQLARYLVKSAALVKSGKASQLGPLVAYLGARSEPTSLIDRVPNGGITEYIKTFQHIAKRQTLKAANKFFGLMENGEKREIAWNKSSVELNRASRLHTRLFIVEAFARRVNEIGDITIKEALSDLLHLHVNYELLDVATYALEDGFMSSTQLDYVRDQLYFYLQKIRPNAVSLLDSWEFSDRELRSVLGRRDGHVYENLFKWAKESPLNKTDVLPSVDTYLKPMMEKARQSKL
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Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains. Specifically, catalyzes the desaturation of fatty acids heptanoyl-CoA (C7), nonanoyl-CoA (C9), dodecanoyl-CoA (C12) and to a lesser extent pentanoyl-CoA (C5) and hexadecanoyl-CoA (C16), and hydroxylated fatty acid hydroxynonanoyl-CoA. Also, catalyzes the desaturation fatty acid-derived side chains of ascaroside pheromones, which regulates development and behavior. Specifically, shortens ascaroside with 5-carbon omega side chain (asc-omega-C5), 7-carbon side chain (asc-C7), 9-carbon side chain (asc-C9), 11-carbon side chain (asc-C11), 13-carbon side chain (asc-C13), 15-carbon side chain (asc-C15) and to a lesser extent ascarosides with 7-omega-carbon side chain (asc-omega-C7). Also shortens indol-3-carbonyl(IC)-ascarosides with 7-carbon side chain (IC-asc-C7) and to a lesser extent (IC)-ascarosides with 9-carbon side chain (IC-asc-C9). May associate and regulate the folding and/or the catalytic activity of other acyl-coenzyme A oxidases including acox-1.2, acox-1.3, acox-1.4 and acox-3 modulating the type of ascarosides produced. In association with acox-1.3, catalyzes the desaturation of asc-C7-CoA but not of fatty acids or hydroxylated fatty acids. Involved in the biosynthesis of asc-C6-MK (daumone 2) and asc-delta-C9 (daumone 3) but not asc-C7 (daumone 1) daumones are pheromones produced during unfavourable growth conditions which promote entry into the dauer stage.
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O62247
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BLI5_CAEEL
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Kunitz-type protein bli-5 (Blistered cuticle protein 5) (Kunitz-type protease inhibitor bli-5)
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MVSIHNSFILLMLMISICFCEKCLTNEECDLKWPDAICVRGRCRCSENTIRKKSASREWVCLATNDATGNSGPPLTCPTPEGAGYQVMYRKDGEPVKCSSKKKPDTCPEGFECIQGLSILGALDGVCCPDRAKTCVHPIFDHPDDGYLSRWGFDGEQCIEFKWNPERPSSANNFKTRAHCEDYCIGSINGITNYHQSNFHLF
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Appears to lack serine protease inhibitor activity in vitro when tested with bovine pancreatic alpha-chymotrypsin and elastase. Involved in cuticle biosynthesis.
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O62255
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DCP2_CAEEL
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m7GpppN-mRNA hydrolase dcap-2 (EC 3.6.1.62) (Nudix hydrolase 5) (mRNA-decapping enzyme 2)
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MEISTENWCKKPKNRSIFSKNISFQKQNKSTEEPPSSVQKLLASLQQAQNKSDLSEQPSTSKPKKNEKRKKAVAQAPASAPAPGPEEKKKQPKRASVGARMQQQAENARISQTKRPRQVSTSKGSSRNTTAPEQQNYQQQQQQYKGPRIPTDILDELEFRFISNMVECEINDNIRVCFHLELAHWYYIDHMVEDDKISGCPNVGSRDFNFQMCQHCRVLRKYAHRADEVLAKFREYKSTVPTYGAILVDPEMDHVVLVQSYFAKGKNWGFPKGKINQAEPPRDAAIRETFEETGFDFGIYSEKEKKFQRFINDGMVRLYLVKNVPKDFNFQPQTRKEIRKIEWFKIDDLPTDKTDELPAYLQGNKFYMVMPFVKDIQIYVQKEKEKLRRRKAEAVQSTPSSSIFSQLFPAQPPPPVPEDATPTRPMYKRLTSEELFSAFKNPPAGEVARPTLPDMSPAVNGLDTLAVLGICTPLKPGASLNEFSGAPQNCPMISEEAGSPADPSAEIGFAMPMDLKQPVVTSDHPWQHHKISDSSAPPQTLESHQGWLDTQLVNTIMHSPNHPLPPTSNSPATPTAVLGHLIGKPIQPQAILPQAATPTALGSAEKPKSSRISLSDNSAFKAISSTQKQSIPKATAAPPSTEKTRSASLSGSSQVVGKPARNLFNSVVSPVSSGIQSIQGDGGAWEDVWFREQLAATTTAGTSISSLAASNQELAMINREETPIEDPYFKQQAYQKAQKAQSLIPACSQWTNSIKLDIDYVVGPLSFWMQQFSTKSPVSGTGPQLP
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Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. RNA-decapping enzyme although it does not bind the RNA cap. May contribute to gene regulation in multiple RNA pathways including monomethylguanosine- and trimethylguanosine-capped RNAs. In oocytes, may play a role in the response to stress induced by heat shock, osmotic stress and anoxia. Required for the developmental axon guidance and regrowth of PLM touch receptor neurons. Early in embryogenesis, plays a role in ciliary shape formation in sensory neurons. Promotes survival at high temperatures.
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O62305
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KCC2D_CAEEL
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Calcium/calmodulin-dependent protein kinase type II (CaM kinase II) (EC 2.7.11.17) (Uncoordinated protein 43)
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MMNASTKFSDNYDVKEELGKGAFSVVRRCVHKTTGLEFAAKIINTKKLSARDFQKLEREARICRKLQHPNIVRLHDSIQEESFHYLVFDLVTGGELFEDIVAREFYSEADASHCIQQILESIAYCHSNGIVHRDLKPENLLLASKAKGAAVKLADFGLAIEVNDSEAWHGFAGTPGYLSPEVLKKDPYSKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKSLIDSMLTVNPKKRITADQALKVPWICNRERVASAIHRQDTVDCLKKFNARRKLKAAISAVKMVTRMSGVLRTSDSTGSVASNGSTTHDASQVAGTSSQPTSPAAEVYPNVLLFNPQKFPRNCVHPFTTHPYYSPKESSKKKLFFTLLFEVCPHTSRSHILLRDNTKNIYHPYHCFTNKMSNYERAAPSSHGSSTTKKIANAIADLVIRRSSPSIRRKTEADVHNSNRNRKVSAPANLQHALVPVIDVVVATGALASSSVDNLSASTSSDLGRNLLNKKEQGPPSTIKESSESSQTIDDNDSEKGGGQLKHENTVVRADGATGIVSSSNSSTASKSSSTNLSAQKQDIVRVTQTLLDAISCKDFETYTRLCDTSMTCFEPEALGNLIEGIEFHRFYFDGNRKNQVHTTMLNPNVHIIGEDAACVAYVKLTQFLDRNGEAHTRQSQESRVWSKKQGRWVCVHVHRSTQPSTNTTVSEF
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Acts in the signaling of a variety of pathways and processes. Phosphorylates 'Ser-319' of daf-16 in response to stress signals, such as heat, starvation and oxidation, which plays a role in prolonging lifespan. Required for viability under chronic osmotic stress in which it acts downstream of osr-1. Has roles in locomotion, oocyte maturation, brood size, egg laying, defecation, meiotic maturation and neuronal cell fate specification. Required for the regulation of synaptic density and neuromuscular junction morphology. Regulates the synaptic trafficking of glr-1. Bidirectional modulator of neurotransmitter release with negative modulatory effects mainly mediated via slo-1 activation. Involved in activation of ADF neurons and increased tph-1 transcription following exposure to pathogenic bacteria which leads to learned olfactory aversion to the bacteria. Implicated in the muscle regulation of spicule protraction. In conjunction with egl-2 has a role in the suppression of mating behavior under food deprivation to encourage foraging. Involved in restricting str-2 expression to only one of the two AWC neurons. May suppress the functional response to an internal pacemaker, perhaps by modulating the activity of the IP3 receptor.
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O62415
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LYS1_CAEEL
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Lysozyme-like protein 1
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MLKLAFVTFLFALASARPQDVDSNRVVALPQDNFEVTDIGFEKIKAEPAPEVVNNDASYAYAVDISVPTTVSQMNCLKTSRYAAVFIRGFTPFGSGAFDTTSVTSIRNAYSAGLGIEVYMTPQPLSSLQGYQQLDALYNGLNGNGITIRSVWIQVTSPANWQKSATTNVNFLNSIISRAKQYGLTVGIYTNQYDWSQITGNWATLSSDVLLWYWHVLGGGVTGETPATFDDFRAFGSFKKASVKQFAQVESVCSLTVNRDVYVVGIPAAASSKNTDFFTQEDISSNNKKIVVGGVIGV
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Involved in resistance to Gram-negative bacterium S.marcescens and to bacterium Gram-positive S.aureus infection.
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O62471
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QUI1_CAEEL
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Protein qui-1 (Quinine non-avoider protein 1)
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MFRGKGQQQVSSTDNIKAMMTAAIGNKLEKRLPLVSTIFVVGNDEEEFNIERRTLWQDVLPDLQNLAFQSNFDLEFCDVPLENGELTNSVAEHVLQMWKDNPRSWIVLLLGNRYGNVSVPTSLRKEEYESIRSSIFEENGNVRVFEKAYTINRNGAVEEYRLVPSAIKDKKQLAEIIKALQAGAKAAHEEGSINQVHEQRQNRFFSSPLETFVRSILQVSPCRCLFLLRKFDQLVADPNSPNAFLETNDQNSRKIEDLKNEITLKMNDRVMTHVLRPESTDINYFFNSRDGDKYREKIARQFNEKLKNHLADINPPVRPEPPKSPMVLAANEARTHQEFLENQLALGNLKRDYDKRLDELASVKVNRGVFLIQGTDLCGKTQALCRLYHKISDKDAYKVIFFTNLTYSSNFAHEAWRTICLNICSISNIDPKEVLEHFKLGGILKSLEELVQKADKPVCIFIDDVHLLKFGHLLSQIGRRTETAPDNLSLFMTSSNVAPVNAVFAVTQTVNVDVISENEVVGMVQKMAEKVDKKLTNEQISAIRPLMAAKDGILIAKSFTHEILFNGNSSMKGGMDGRMTRIEKEFGKLAVGNAVKFIAASSHGLTRLEIHDAISADREVLEEMNMSIVYSLLTLDGIIEALGPILRKVIIDDRQIIGIAHSGLISWLRNRYLTSSQDIRSAHLQLSDLFADLLIDNEQSPRHEIAYQSFSQGIKRDNGSPNFRRLRLLWYHCLHSGNLDRLKELSLCHFEYVDYVTRYFGISHLLSLYEECATQILHHDLQVISEQVLVPALVTMARDSEQLAAEVIGRLRFTRHENSHFLNSLVDQAMSWVDLYNRQPLLVPLTCWISPPATKVCRSFTLKDWKPGNTVLTLSANHQYILISGNQSDPGVIYAYHIASEQLIGTFKGHTAAVTCLCSSNDSSLFVSTSFDKTVNVWVFSQSTPTMSLTHHTAKVTCAILTSDDQYLITASADSSAKMIKLETGEVMRSFNDHTGSVVSLQLTSNNQFLITGSGDFVVQMWDVTNGKCISRMGGLMAPVSTLAITSNDAFVVVACEDETLKVFSTVGGQELHELMGHEGKVNSLVCAQDDCQLFAATKSKVFCYDIHNGQMIDVLDTAQPFPICSLKISSDNYFLISPCGPKVTIWNVTKRNHDAHDVHADKEGFLTAVALSNDDKYAACGTNNGIVALWDLEVCQCVFTTIQNKGDPITCIRYSVDSQYCISGNQAGCILILDAQNGGVVRELFMHSSEVLSIMSLVHNKMISCDIQGKMVIWELFGDDDTPEMVATGVKPPIFVPPTGRIMVGHCSLSNKEMKIWAFPEEGPPVTRAKLSHSDEITCFATSPKGGNFIATGSRDMSLKIWQIDKGFLTQVLVGHENVVTCCCISFDERLVVSGARDEKIIVWNVQSGDMVCTVNTTAAITSLSMTGDSTVVFSTTEDGWVETWSTTKGRLLSTFNAHRPIKKLINSYESHRMLLLLENCAQLPILCLHNTPAVGVEATRRRSARAQSVSSASNEPVASTSAGEIKKDPILSSNNGGNAQSAPRATAPKPTFDMLERSKSRTSLIEKDRTTTLTQSNAPPPQKSNMCTLL
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Involved in the avoidance response to the noxious chemicals and repellents such as quinine in ASH and ADL sensory neurons. In response to the noxious chemical quinine, promotes dauer formation induced by pheromones such as the ascaroside ascr#3 in ASH nociceptive neurons.
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O62479
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SAS6_CAEEL
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Spindle assembly abnormal protein 6
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MTSKIALFDQTLIASLLQPLSLNQPDFKAYKTKVKLKISEQRNETSGEKELKFEISRSDDFEFLFSETLNNEKYQILARDHDLTVDFDAFPKVIIQHLLCKNIVKNLEEDGEVDARKKAGYHSIADPGKPTEINIILDAEKNFCSFELFSKTPISKGKIFSIKLHAVRGDHLISHLLKICSSQAVKLSTFYKSADELASLRQKCGDLEKQVEKLSGVKEEFEEMSEKFKELEDEVELVKEERENIRLLVEDKEDEVADLKQDTESLQKQLEENQEELEIVGNMLREEQGKVDQLQKRNVAHQKEIGKLRAELGTAQRNLEKADQLLKRNSQQQNQQSLDMRKLGELEADLKEKDSMVESLTETIGILRKELENEKLKAAENMDSFEKLSMENENLKEKIAHYRAQRFSPAPSGLPGLQTGLTNRLTPSFKPVLGPHTPYGANLNSRTPFRDNTTLNFQNSTIATPHAFRFNSQLIADETTGSSVTNTPPAQR
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Central scaffolding component of the centrioles ensuring their 9-fold symmetry. Required for centrosome biogenesis and duplication.
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O62589
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GD_DROME
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Serine protease gd (EC 3.4.21.-) (Protein gastrulation defective)
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MRLHLAAILILCIEHVTKAVAQGMPISPCPKVFQYRFDGSEWFGLMAVRSPDGHQPLHIRVTLSMRGKPTTYTQNYLGEIELLTRGKFTHNAPVLYKIRFPKHHFPPKLLLMSANNHVICFGSGEHSIFMTQIQLEHIRKLSFIPDKKSSLLLDPEEEEVRKTDDKPPSTPHIQFKKKPFAQAPKEICGRIDRDLDFHLSQRTESLHVAIGEPKSSDGITSPVFVDDDEDDVLEHQFVDESEAEAIESDSADSLPSITRGSWPWLAAIYVNNLTSLDFQCGGSLVSARVVISSAHCFKLFNKRYTSNEVLVFLGRHNLKNWNEEGSLAAPVDGIYIHPDFNSQLSSYDADIAVIILKDEVRFNTFIRPACLWSGSSKTEYIVGERGIVIGWSFDRTNRTRDQKLSSELPGKKSTDASAPKVVKAPIVGNAECFRANAHFRSLSSNRTFCAGIQAEERDTHQSGASIYTGISGAGLFIRRNNRWMLRGTVSAALPAVETPDAESSHKLCCKNQYIIYADVAKFLDWITAFVI
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Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo. Three proteases ndl, gd and snk process easter to create active easter. Active easter defines cell identities along the dorsal-ventral continuum by activating the spz ligand for the Tl receptor in the ventral region of the embryo.
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O62618
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MK38A_DROME
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Mitogen-activated protein kinase p38a (MAP kinase p38a) (MAPK p38a) (EC 2.7.11.24) (MAP kinase 14A) (p38 MAPK)
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MSVSITKKFYKLDINRTEWEIPDIYQDLQPVGSGAYGQVSKAVVRGTNMHVAIKKLARPFQSAVHAKRTYRELRLLKHMDHENVIGLLDIFHPHPANGSLENFQQVYLVTHLMDADLNNIIRMQHLSDDHVQFLVYQILRGLKYIHSAGVIHRDLKPSNIAVNEDCELRILDFGLARPTENEMTGYVATRWYRAPEIMLNWMHYDQTVDIWSVGCIMAELITRRTLFPGTDHIHQLNLIMEMLGTPPAEFLKKISSESARSYIQSLPPMKGRSFKNVFKNANPLAIDLLEKMLELDAEKRITAEEALSHPYLEKYAEPSVEQTSPPYDHSFEDMDLPVDKWKELIYKEVTNFKPPPSYAQVLKDVK
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Kinase involved in a signal transduction pathway. May down-regulate insect immunity gene expression after prolonged infection.
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O62643
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THY1_MACMU
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Thy-1 membrane glycoprotein (Thy-1 antigen) (CD antigen CD90)
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MNLAISIALLLTVLQVSRGQKVTSLTACLVDQSLRLDCRHENTTSSPIQYEFSLTRETKKHVLFGTVGVPEHTYRSRTNFTSKYNMKVLYLSAFTXKDEGTYTCXLHHSGHSPPISSQNVTVLRDKLVKCEGISLLAQNTSWLXLLLLSLSLLQATDFMSL
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May play a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain.
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O62651
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WT1_PIG
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Wilms tumor protein homolog
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MGSDVRDLNALLPAVPSLGGGGGCALPVSGAAEWAPVLDFAPPGASAYGSLGGPAPPPAPPPPPPPPPHSFIKQEPSWGGAEPHEEQCLSAFTVHFSGQFTGTAGACRYEPFGPPPPSQASSGQARMFPNAPYLPSCLESQPAIRNQGYSTVTFDGTPSYGHTPSHHAAQFPNHSFKHEDPMGQQGSLGEQQYSVPPPVYGCHTSTDSCTGSQALLLRTPYSSDNLYQMTSQLECMTWNQMNLGATLKGVAAGTSSSMKWTEGQSNHGAGYESDSHATPILCGAQYRIHTHGVFRGIQDVRRVPGVAPTLVRSASETSEKRPFMCAYPGCNKRYFKLSHLQMHSRKHTGEKPYQCDFKDCERRFSRSDQLKRHQRRHTGVKPFQCKTCQRKFSRSDHLKTHTRTHTGKTSEKPFSCRWPSCQKKFARSDELVRHHNMHQRNMSKLQLAL
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Transcription factor that plays an important role in cellular development and cell survival. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'. Regulates the expression of numerous target genes, including EPO. Plays an essential role for development of the urogenital system. It has a tumor suppressor as well as an oncogenic role in tumor formation. Function may be isoform-specific: isoforms lacking the KTS motif may act as transcription factors. Isoforms containing the KTS motif may bind mRNA and play a role in mRNA metabolism or splicing. Isoform 1 has lower affinity for DNA, and can bind RNA.
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O62653
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SUIS_SUNMU
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Sucrase-isomaltase, intestinal [Cleaved into: Sucrase (EC 3.2.1.48); Isomaltase (EC 3.2.1.10)]
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MARKKSSGLKITLIVLLAIVTIIAIALVAILPTKTPAVELVSTIPGKCPSAENDRLDEKINCIPDQFPTQALCAMQGCCWNPRNESPTPWCSFANNHGYEFEKISNPNINFEPNLKKNSPPTLFGDNITNLLLTTQSQTANRFRFKITDPNNQRYEVPHQFVNKDFSGPPASNPLYDVKITENPFSIKVIRKSNNKILFDTSIGPLVYSNQYLQISTKLPSKYIYGLGEHVHKRFRHDLYWKTWPIFTRDQLPGDNNNNLYGHQTFFMSIEDTSGKSFGVFLMNSNAMEVFIQPTPIVTYRVIGGILDFYIFLGDTPGQVVQQYQELTGRPAMPSYWSLGFQLSRWNYGSLDAVKEVVKRNRDARIPFDAQVTDIDYMEDKKDFTYNNKTFYGLPEFVKDLHDHGQKYIIILDPAISITSLANGNHYKTYERGNEQKVWVYQSDGTTPLIGEVWPGLTVYPDFTNPKCLDWWTNECSIFHEEIKYDGLWIDMNEVSSFVHGSTKGCSDNKLNYPPFIPDILDKLMYAKTICMDAIQHWGKQYDVHSLYGYSMAIATEKAIEKVFPNKRSFILTRSTFAGTGKHATHWLGDNTPSWEHMEWSITPMLEFGLFGMPFIGADICGFVVDTTEELCRRWMQIGAFYPYFRDHNAGGYMPQDPAYFGQDSLLVNTSRHYLDIWYTLLPYLYNLLYKAYVYGETVARPFLYEFYEDTNSWIEDLQFLWGSALLITPVLRQGADRMSAYIPDATWYDYETGGKRTWRKQRVEMYLPGDKIGLHVRGGYIIPTQQPAVNTTASRKNPLGLIIALDNNAAKGDFFWDDGESKDSIEKGKYILYTFSVLNNELDIICTHSSYQEGTTLAFETIKILGLANTVTQVQVAENNQQTIIHNSFTYHASNQSLIIDNLKLNLGKNFTVQWNQVSLDSEKIDCFPDNNPENKQNCEERGCLWEPNSAAEGPRCYFPKQYNPYLVKSTQYSSMGITVDLELNTATARIKMPSNPISVLRLEVKYHKNDMLQFKIYDPQNKRYEVPIPMDIPTTPTSTYENRLYDVNIKGNPFGIQIRRRSTGRIFWDSCLPWGLLLMNQFIQISTRLPSEYVYGFGGVGHRQFKQDLNWHKWGMFNRDQPSGYKISSYGFQPYIYMALGDGGNAHGVFLLNSNAMDVTFQPNPALTYRTIGGILDFYMFLGPNPEVATKQYHEVIGRPVKPPYWALGFHLCRYGYENTSEIRQLYEDMVSAQIPYDVQYTDIDYMERQLDFTIGKGFQDLPEFVDKIRDEGMKYIIILDPAISGNETQDYLAFQRGIEKDVFVKWPNTQDICWAKVWPDLPNITIDDSLTEDEAVNASRAHVAFPDFLKTSTAEWWATEIEDFYNTYMKFDGLWIDMNEPSSFVHGSVDNKCRNEILNYPPYMPALTKRNEGLHFRTMCMETQQTLSNGSSVLHYDVHNLYGWSQAKPTYDALQKTTGKRGIVISRSTYPSAGRWAGHWLGDNYANWDKIGKSIIGMMEFSLFGISFTGADICGFFNNSDYELCARWMQVGAFYPYSRNHNITDTRRQDPVSWNETFASMSTDILNIRYNLLPYFYTQMHDIHANGGTVIRPLLHEFFSETGTWDIYKQFLWGPAFMVTPVVEPYSESVTGYVPDGRWLDYHTGQDIGLRKRLHTLDAPLYKINLHVCGGHILPCQEPAQNTYFSRQNYMKLIVAADDNQTAQGYLFWDDGESIDTYEKGQYLLVQFNLNKATLTSTILKNGYINTREMRLGFINVWGKGNTVVQEVNITYKGNKESVKFSQEANKQILNIDLTANNIVLDEPIEISWT
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Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides (By similarity).
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O62654
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DESM_BOVIN
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Desmin
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MSQAYSSSQRVSSYRRTFGGAPSFPLGSPLSSPVFPRAGFGTKGSSSSVTSRVYQVSRTSGGAGGLGALRASRLGSTRVPSSYGAGELLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAEIYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTFSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL
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Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity. In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures. May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction. Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin.
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O62664
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PGH1_BOVIN
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Prostaglandin G/H synthase 1 (EC 1.14.99.1) (Cyclooxygenase-1) (COX-1) (Prostaglandin H2 synthase 1) (PGH synthase 1) (PGHS-1) (PHS 1) (Prostaglandin-endoperoxide synthase 1)
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MSRQGISLRFPLLLLLLSPSPVLPADPGAPAPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYYGPNCTIPEIWTWLRTTLRPSPSFVHFLLTHGRWLWDFVNATFIRDKLMRLVLTVRSNLIPSPPTYNVAHDYISWESFSNVSYYTRILPSVPRDCPTPMGTKGKKQLPDAEFLSRRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMVYATIWLREHNRVCDLLKAEHPTWGDEQLFQTARLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAMEFNQLYHWHPLMPDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPAGRIGGGRNIDHHILHVAVDVIKESRELRLQPFNEYRKRFGMKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTFGGDVGFNLVKTATLKKLVCLNTKTCPYVSFHVPDPHREDRPGVERPPTEL
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Dual cyclooxygenase and peroxidase that plays an important role in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates AA to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells. Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products.
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O62667
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S28A1_PIG
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Sodium/nucleoside cotransporter 1 (Concentrative nucleoside transporter 1) (CNT 1) (Na(+)/nucleoside cotransporter 1) (Sodium-coupled nucleoside transporter 1) (Solute carrier family 28 member 1)
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MEDNTPRQRDPISLTSVANGLENMGAELLESLEEGRAPGSDSSPAEVGGGWSKAGPEHLGRRSLQPALRVRRFCREHTQLFRWICTGLLCTAFAAFLLIACLLDFQRALALFVLFCVVLFFLAHSLLKRLLGPKLLRCVKPLRHPCLNLWFKRGLALAAFLGLVLWLVLDTAQRPEQLVSFGGICVFILLLFAGSKHHRAVSWRAVSWGLGLQFALGLFVIRTEPGFIAFQWLGDQIQIFLSYTEAGSSFVFGEALVKDVFAFQVLPIIVFFSCAMSVLYYVGLMQWVILKISWLMQATMGTTATETLSVAGNIFVSQTEAPLLIRPYLADMTLSEIHVVMTGGYATIAGSLLGAYISFGIDAASLIAASVMAAPCALALSKLVYPEVEESKFKREEGVKLTYGDAQNLLEAASSGAAMSVRVVTNIAANLIAFLAVLAFINAALSWLGDMVDVQGLSFQLICSYVLRPVAFLMGVAWEDCPVVAELLGMKLFLNEFVAYQELSGYKQRRLAGAEEWVGSRKQWISVRAEILTTYALCGFANFSSIGIMLGGLTSMVPQRKGDFSQIVLRALCTGACVSLVNACVAGILYVPRGAEVDCVSFLNTTLSSSSFEVYQCCRQFFQSTSLEFSPEALDNCCRFYNHTICV
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Sodium and pyrimidine nucleoside symporter of the plasma membrane that imports uridine, thymidine and cytidine into cells by coupling their transport to the transmembrane sodium electrochemical gradient. Also transports adenosine, an atypical substrate transported with high apparent affinity, but low maximum velocity. Therefore, exhibits the transport characteristics of the nucleoside transport system cit or N2 subtype (N2/cit). Involved in renal nucleoside (re)absorption.
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O62683
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ZO3_CANLF
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Tight junction protein ZO-3 (Tight junction protein 3) (Zona occludens protein 3) (Zonula occludens protein 3)
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MEELTIWEQHTATLCRDPRRGFGIAISGGRDRASGSVVVSDVVPGGPADGRLQTGDHVVMVNGVSMESVTSTFAIQILKTCTKLANITVKRPRKIQLPATKAGTSGRGRQGLEEEADCGQGYDGDTSSGSGRSWDKRSRRARTGRRNQAGSRGRRSPGGNSEANGLALVSGFKRLPRQDVHMRPVKSVLVRRTESEEFGVTLGSQIFIKHITDSGLAARNRGLQEGDLILQINGVSSENLSLSDTRRLIEKSEGKLTLLVLRDRGQFLVNIPPAVSDSDSDSSFLDDISALGSELSQAVPSHVPPPPPHAQRSLDSDGTDSPRDSPPLRRENSLDSRTISEPDAPRHSSYDIYRVPSSQSAEDRGYSPDSRVVRFHKGTTIGLRLAGGNDVGIFVSGVQEGSPADGQGIQEGDQILQVNDVPFRNLTREEAVQFLVALPPGEEVELVTQRNEDIFRKMVQSRVGDSFYIRTHFELEASPPSGLGFTRGDVFHVLDTLCPGPGPSGARGTHWLAVRMGRDLREQERGIIPNQSRAEQLASLESAQRAVGAGPGASVGSSARAEFWRLRGLRRGAKKSTQRSREDLSALTRQGHYPPYERVVLREASFKRPVVILGPVADIAMQKLTAEMPDQFGIADSVLRTDSPSKIIKLDTVRVIAEKNKHALLDVTPSAVERLNYVQYYPIVVFCAPESRAALKALRQWLAPASRRSARRLYAQAQKLRKHSEHLFTATIPLRGTSDTWYQELKAVVREQQTRPIWTAEDQLDNSSEDNLELPHRGLADSSADLSCDSRVNSDYETDGEGYTDGEGYTDVDEGPPAPALARSSEPVLEEEPRSPRDHGRASGARGAQVDRHPYHSQGRQDSMRTYGQEALKKKFTRARDVESSDEDGYDWGPATDL
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TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton. The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Binds and recruits PATJ to tight junctions where it connects and stabilizes apical and lateral components of tight junctions. Promotes cell-cycle progression through the sequestration of cyclin D1 (CCND1) at tight junctions during mitosis which prevents CCND1 degradation during M-phase and enables S-phase transition (By similarity). With TJP1 and TJP2, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus. Contrary to TJP2, TJP3 is dispensable for individual viability, embryonic development, epithelial differentiation, and the establishment of TJs, at least in the laboratory environment (By similarity).
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O62698
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PGH2_BOVIN
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Prostaglandin G/H synthase 2 (EC 1.14.99.1) (Cyclooxygenase-2) (COX-2) (PHS II) (Prostaglandin H2 synthase 2) (PGH synthase 2) (PGHS-2) (Prostaglandin-endoperoxide synthase 2)
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MLARALLLCAAVALSGAANPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLLKPTPNTVHYILTHFKGVWNIVNKISFLRNMIMRYVLTSRSHLIESPPTYNVHYSYKSWEAFSNLSYYTRALPPVPDDCPTPMGVKGRKELPDSKEVVKKVLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTDFERGPAFTKGKNHGVDLSHIYGESLERQHKLRLFKDGKMKYQMINGEMYPPTVKDTQVEMIYPPHVPEHLKFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDVFQIDGQEYNYQQFIYNNSVLLEHGLTQFVESFTRQRAGRVAGGRNLPVAVEKVSKASIDQSREMKYQSFNEYRKRFLVKPYESFEELTGEKEMAAELEALYGDIDAMEFYPALLVEKPRPDAIFGETMVEAGAPFSLKGLMGNPICSPEYWKPSTFGGEVGFKIINTASIQSLICSNVKGCPFTSFSVQDTHLTKTVTINASSSHSGLDDINPTVLLKERSTEL
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Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates AA to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S-RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE). Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity).
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O62699
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NOS2_CANLF
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Nitric oxide synthase, inducible (EC 1.14.13.39) (Inducible NO synthase) (Inducible NOS) (iNOS) (NOS type II) (Peptidyl-cysteine S-nitrosylase NOS2)
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MACPWKFLFRAKFHQYGMKEEKDINNNVEKPPGATPSPSTQDDLKNHKHHNDSPQPLTETVQKLPESLDKLHATPLSRPQHVRIKNWGNGMTFQDTLHHKAKGDLACKSKSCLGAIMNPKSLTREPRDKPTPPDELLPQAIEFVNQYYSSFKEAKIEEHLARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAKEMFEHICRHLRYASNNGNIRSAITVFPQRTDGKHDFRVWNAQLIRYAGYQMPDGTILGDPASVEFTQLCIDLGWKPKYGRFDVVPLVLQADGQDPEFFEIPPDLVLEVPMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDRAVIEINVAVLHSFQKQNVTIMDHHSAAESFMKYMQSEYRSRGGCPADWIWLVPPISGSITPVFHQEMLNYVLSPFYYYQVEAWKTHVWQDEKRRPQRRKIQLKVLVKAVLFASMLMRKTMASRVRVTILFATETGKSETLARDLGALFSCAFHPKVLCMDEYKLSHLEEEQLLLVVTSTFGNGDSPGNGEKLKKSLFMLKELTNKFRYAVFGLGSSMYPQFCAFAHDIDHKLSHLGASQLTPGGEGDELNGKEEAFRCWAVQTFKAACDTSDVRGKHCIQIPRLYTSNVTWDPHHYRLLQDSQPLDLNKALSKMHAKNVFTLRLKSQRNLQSPISNRTTLQVELSCEDSQELSYLPGEHLGVFPGNQLALVQGILERVVYSPAPLQPVHLETLSERGSYWVRNNRLPPCSLSQALTYFLDITTPPTHLLLRKLAQLAHQYAERHRLEILCHPSEYNKWKLTNSPTFLEVLEEFPSLRVSAGFLLSQLPILKPRYYSISSSRDCTPMEVHLTVAVLVYPTRDGQGPLHHGVCSTWLSNLKPQDPVPCFVRSAGNFKLPEDPSRPCILIGPGTGIAPFRSFWQQRLHDIKHKGLRGSRMTLVFGCRRPDEDHLYREEMLEMAQSGVLHEVHTAYSRLPGQPKVYVQDILRQQLASQVLRMLHEEQGHLYVCGDVRMARDVAHTLKHLVAAKLSLSEEQVEDYFFQLKSQKRYHEDIFGAVFPYEVKKDGAAKQPSDPRVPAAHGRS
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Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2. As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM. Involved in inflammation, enhances the synthesis of pro-inflammatory mediators such as IL6 and IL8.
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O62714
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CASR_PIG
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Extracellular calcium-sensing receptor (CaSR) (Parathyroid cell calcium-sensing receptor) (PCaR1)
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MAFSSCCWILLALTWCTSAYGPDQRAQKKGDIILGGLFPIHFGVAAKDQNLESRPESVECIRYNFRGFRWLQAMIFAIEEINSSPALLPNMTLGYRIFDTCNTVSKALEATLSFVAQNKIDSLNLDEFCNCSEHIPSTIAVVGATGSGISTAVANLLGLFYIPQVSYASSSRLLSNKNQFKSFLRTIPNDEHQATAMADIIEYFRWNWVGTIAADDDYGRPGIEKFREEAEERDICIDFSELISQYSDEEEIQQVVEVIQNSTAKVIVVFSSGPDLEPLIKEIVRRNITGKIWLASEAWASSSLIAMPEYFHVVGGTIGFALKAGQIPGFREFLQKVHPSKSVHNGFAKEFWEETFNCHLQEGAKGPLTTDTFLRGHEEGGGRISNSSTAFRPLCTGDENISSVETPYMDYTHLRISYNVYLAVYSIAHALQDIYTCIPGRGLFTNGSCADIKKVEAWQVLKHLRHLNFTSNMGEQVTFDEYGDLAGNYSIINWHLSPEDGSIVFKEVGYYNVYAKKGERLFINEEKILWSGFSREVPFSNCSRDCLAGTRKGIIEGEPTCCFECVECPDGEYSDETDASACDKCPDDFWSNENHTSCIAKEIEFLSWTEPFGIALTLFAVLGIFLTAFVLGVFIKFRNTPIVKATNRELSYLLLFSLLCCFSSSLFFIGEPQDWTCRLRQPAFGISFVLCISCILVKTNRVLLVFEAKIPTSFHRKWWGLNLQFLLVFLCTFMQIVICAIWLYTAPPSSYRNHELEDEIIFITCHEGSLMALGFLIGYTCLLAAICFFFAFKSRKLPENFNEAKFITFSMLIFFIVWISFIPAYASTYGKFVSAVEVIAILAASFGLLACIFFNKVYIILFKPSRNTIEEVRCSTAAHAFKVAARATLRRSNVSRQRSSSLGGSTGSTPSSSISSKSNSEDPFPQPERQKKQQPLALTQHVPQPQAPSTPQPQPQLQQQPRCKQKVIFGSGTVTFSLSFDEPQKSATAHRNSTHQNSLEAQKNNDALTRHQALLPLQCGEADAELTAQETGLQGSVGGDHHPEMEDPEEMSPALVMSNSRSFVISGGGSTVTENMLHS
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G-protein-coupled receptor that senses changes in the extracellular concentration of calcium ions and plays a key role in maintaining calcium homeostasis. Senses fluctuations in the circulating calcium concentration and modulates the production of parathyroid hormone (PTH) in parathyroid glands (By similarity). The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. The G-protein-coupled receptor activity is activated by a co-agonist mechanism: aromatic amino acids, such as Trp or Phe, act concertedly with divalent cations, such as calcium or magnesium, to achieve full receptor activation (By similarity).
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O62725
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PGH2_NEOVI
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Prostaglandin G/H synthase 2 (EC 1.14.99.1) (Cyclooxygenase-2) (COX-2) (PHS II) (Prostaglandin H2 synthase 2) (PGH synthase 2) (PGHS-2) (Prostaglandin-endoperoxide synthase 2)
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MLARAGLLCASLSPPHAANPCCSNPCQNQGVCMSIGFDQYMCDCSRTGFYGENCSTPEFLTRVKLLLKPTPNTVHYILTHFKGVWNIVNKIPFLADVIMKYVRTSRSHCIEPPPTYNVHYAYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGKKELPDSKEIVEKFLLRRKFIPDPQGTNMMFAFFAQHFTHQFFKTDHKRGPGFTKGLGHGVDLSHVYGETLDRQHKLRLFKDGKMKYQVIDGEVYPPTVKDTQVEMIYPPHVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEQGEWDDERLFRRSRLILIGETIKIVIEDYVRHLSGYHFSLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDTLQIDDQEYNFQQFVYNNSILLEHGLTQFGESFSRQIAGRVAGGRNVPAAVQQEQRASIDQSRQMKYQSLNEYRKRFSVKPYASFEELTGEKEMAGELKALYQDIDAMELYPALLVEKPRPDAIFGETMVEIGAPFSLKGLMGNPICSPDYWKPSHFGGEVGFKIINTASIQSLICNNVKGCPFTAFSVQDPQLTKTVTINGSSSHSGLDDINPTVLLKERSTEL
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Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates AA to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S-RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE). Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity).
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O62742
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SCP2_RABIT
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Sterol carrier protein 2 (SCP-2) (Acetyl-CoA C-myristoyltransferase) (EC 2.3.1.155) (Non-specific lipid-transfer protein) (NSL-TP) (Propanoyl-CoA C-acyltransferase) (EC 2.3.1.176) (SCP-2/3-oxoacyl-CoA thiolase) (SCP-2/thiolase) (EC 2.3.1.16) (SCP-chi) (SCPX) (Sterol carrier protein X) (SCP-X)
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MSSSARKLAPLPRVFVVGVGMTKFVKPGTEDARDYPDMAKEAGQKALADAQIPYSAVEQACIGYVYGDSTCGQRAVYHSLGLTGIPIINVNNNCSTGSTALFMGRQLIQGGMAECVLALGFEKMERGSLGAKFPDRTNPMDKHLDVLINKYGLSAHPVAPQMFGSAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQKEYSLDEVMSSRPIFDFLTVLQCCPTSDGAAAAILASEEFVKKYGLQSKAVEILAQEMVTDFPSSFEEKSIIKMVGFDMSKEAARRCYEKSGLRPSDIDVIELHDCFSANELLTYEALGLCPEGKGGALVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAAVVTLYKMGFPEAASSFRTHQIEAAPTSSAGDGFKANLVFKEIEKKLEEEGEQFVKKIGGIFAFKVKDGPGGKEATWVVDVKNGKGSVLPNSDKKADCTITIADSDLLALMTGKMNPQSAFFQGKLKITGNMGLAMKLQNLQLQPGKAKL
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[Isoform SCPx]: Plays a crucial role in the peroxisomal oxidation of branched-chain fatty acids. Catalyzes the last step of the peroxisomal beta-oxidation of branched chain fatty acids and the side chain of the bile acid intermediates di- and trihydroxycoprostanic acids (DHCA and THCA) (By similarity). Also active with medium and long straight chain 3-oxoacyl-CoAs. Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol and transfers phosphatidylcholine and 7-dehydrocholesterol between membrances, in vitro (By similarity). Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs (By similarity). [Isoform SCP2]: Mediates the transfer of all common phospholipids, cholesterol and gangliosides from the endoplasmic reticulum to the plasma membrane. May play a role in regulating steroidogenesis (By similarity). Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol (By similarity). Also binds fatty acids and fatty acyl Coenzyme A (CoA) such as phytanoyl-CoA. Involved in the regulation phospholipid synthesis in endoplasmic reticulum enhancing the incorporation of exogenous fatty acid into glycerides. Seems to stimulate the rate-limiting step in phosphatidic acid formation mediated by GPAT3. Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs (By similarity).
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O62747
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CXCR4_CERAT
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C-X-C chemokine receptor type 4 (CXC-R4) (CXCR-4) (Fusin) (Leukocyte-derived seven transmembrane domain receptor) (LESTR) (Stromal cell-derived factor 1 receptor) (SDF-1 receptor) (CD antigen CD184)
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MEGISIYTSDNYTEEMGSGDYDSIKEPCFREKNAHFNRIFLPTIYSIIFLTGIVGNGLVILVMGYQKKLRSMTDKYRLHLSVADLLFVITLPFWAVDAVANWYFGNFLCKAVHVIYTVNLYSSVLILAFISLDRYLAIVHATNSQKPRKLLAEKVVYVGVWIPALLLTIPGFIFASVSEADDRFICDRFYPNDLWVVVFQFQHIMVGLILPGIVILSCYCIIISKLSHSKGHQKRKALKTTVILILAFFACWLPYYIGISIDSFILLEIIKQGCEFENTVHKWISITEALAFFHCCLNPILYAFLGAKFKTSAQHALTSVSRGSSLKILSKGKRGGHSSVSTESESSSFHSS
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Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation. Involved in the AKT signaling cascade (By similarity). Plays a role in regulation of cell migration, e.g. during wound healing. Acts as a receptor for extracellular ubiquitin leading to enhanced intracellular calcium ions and reduced cellular cAMP levels. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (By similarity). Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival (By similarity).
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O62768
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TRXR1_BOVIN
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Thioredoxin reductase 1, cytoplasmic (TR) (EC 1.8.1.9) (Peroxidase TXNRD1) (EC 1.11.1.2) (Thioredoxin reductase TR1)
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MNGSKDLPEPYDYDLIIIGGGSGGLAAAKEAAKYDKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALRDSRNYGWNVEETVKHDWERMTEAVQNHIGSLNWGYRVALREKKVTYENAYGEFVGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMQEHGIKFIRQFVPIKVEQIEAGTPGRLRVIAKSTDSDQTIEGEYNTVLLAIGRDACTRKIGLENVGVKINEKTGKIPVTEEEQTNVPYIYAIGDILEGKLELTPVAIQAGRLLAQRLYGGSTVKCDYENVPTTVFTPLEYGSCGLSEEKAVEKFGEENVEVYHSYFWPLEWTIPSRDNNKCYAKVVCNIKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKDQLDSTIGIHPVCAEVFTTLSVTKRSGGNILQTGCUG
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Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form. Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis. Also has reductase activity on hydrogen peroxide (H2O2).
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O62786
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GTR2_PIG
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Solute carrier family 2, facilitated glucose transporter member 2 (Glucose transporter type 2, liver) (GLUT-2)
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MTEDKITGTLVFAVLTAVLGSFQFGYDIGVINAPQQVIITHYRHVLGVPLDDRKAINSYAINSTEELPTGPYPGDPTPTSWAEEETTASASLIIMLWSLSVSIFAIGGMIASFFGGMLGDRLGRIKAMLVANILSLVGALLMWFSKLGPSHILIISGRGISGLYCGLISGLVPMYIGEIAPTKFRGAIGALHQLAIVTGILVSQIIGLDFLLGNHELWHILLGLSAVPAVLQSLMLFFCPESPRYLYIKLDEEAKARKSLKKLRGSDDVTKDITEMRKEREEASSEKKVSIIQLFTNSSYRQPILVALMLHMAQQFSGINGIFYYSTSIFQTAGISQPVYATIGVGAINTIFTALSVFLVEKAGRRSLFLIGMSGMFVCAIFMSVGLVLLDKLPWMSYVSMTAIFLFVSFFEIGPGPIPWFMVAEFFSQGPRPAALAMAAFSNWTCNFIIALCFQYIADFCGPYVFFLFAGVVLVFTLFTFFKVPETKGKSFEEIAAEFQKKSGSAQSPKAAVEMEFLGATETV
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Facilitative hexose transporter that mediates the transport of glucose, fructose and galactose. Likely mediates the bidirectional transfer of glucose across the plasma membrane of hepatocytes and is responsible for uptake of glucose by the beta cells may comprise part of the glucose-sensing mechanism of the beta cell. May also participate with the Na(+)/glucose cotransporter in the transcellular transport of glucose in the small intestine and kidney. Also able to mediate the transport of dehydroascorbate.
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O62806
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MMP13_RABIT
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Collagenase 3 (EC 3.4.24.-) (Matrix metalloproteinase-13) (MMP-13)
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MQPGVLAACLLLSWTHCWSLPLLNSNEDDDLSEEDFQFAESYLRSYYHPLNPAGILKKNAAGSMVDRLREMQSFFGLEVTGKLDDNTLAIMKQPRCGVPDVGEYNVFPRTLKWSQTNLTYRIVNYTPDLTHSEVEKAFKKAFKVWSDVTPLNFTRIHNGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMIFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPARDLIFIFRGKKFWAPNGYDILEGYPQKLSELGFPREVKKISAAVHFEDTGKTLFFSGNQVWSYDDTNHTMDQDYPRLIEEEFPGIGGKVDAVYEKNGYIYFFNGPIQFEYSIWSKRIVRVMPTNSLLWC
|
Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion (By similarity).
|
O62807
|
PPARG_PIG
|
Peroxisome proliferator-activated receptor gamma (PPAR-gamma) (Nuclear receptor subfamily 1 group C member 3)
|
MGETLGDSLIDPESDAFDTLSANISQEVTMVDTEMPFWPTNFGISSVDLSVMDDHSHSFDIKPFTTVDFSSISTPHYEDIPFPRADPMVADYKYDLKLQDYQSAIKVEPVSPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKNIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY
|
Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of BMAL1 in the blood vessels.
|
O62829
|
PPM1A_BOVIN
|
Protein phosphatase 1A (EC 3.1.3.16) (Protein phosphatase 2C isoform alpha) (PP2C-alpha)
|
MGAFLDKPKMEKHNAQGQGNGLRYGLSSMQGWRVEMEDAHTAVIGLPSGLETWSFFAVYDGHAGSQVAKYCCEHLLDHITNNQDFKGSAGAPSVENVKNGIRTGFLEIDEHMRVMSEKKHGADRSGSTAVGVLISPQHTYFINCGDSRGLLCRNRKVYFFTQDHKPSNPLEKERIQNAGGSVMIQRVNGSLAVSRALGDFDYKCVHGKGPTEQLVSPEPEVHDIERSEEDDQFIILACDGIWDVMGNEELCDFVRSRLEVTDDLEKVCNEVVDTCLYKGSRDNMSVILICFPNAPKVSPEAVKKEEELDKYLESRVEEIIKKQGEGVPDLVHVMRTLASENIPSLPPGGELASKRNVIEAVYNRLNPYKNDDTDSTSTDDMW
|
Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling (By similarity). Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB (By similarity).
|
O62830
|
PPM1B_BOVIN
|
Protein phosphatase 1B (EC 3.1.3.16) (Protein phosphatase 2C isoform beta) (PP2C-beta)
|
MGAFLDKPKTEKHNAHGAGNGLRYGLSSMQGWRVEMEDAHTAVVGIPHGLEDWSFFAVYDGHAGSRVANYCSTHLLEHITNNEDFRAAGKSGSALEPSVENVKNGIRTGFLKIDEYMRNFSDLRNGMDRSGSTAVGVMISPKHIYFINCGDSRAVLYRSGQVCFSTQDHKPCNPREKERIQNAGGSVMIQRVNGSLAVSRALGDYDYKCVDGKGPTEQLVSPEPEVYEILRAEEDEFIILACDGIWDVMSNEELCEFVKSRLEVSDDLENVCNWVVDTCLHKGSRDNMSIVLVCFSNAPKVSDEAMRKDSELDKYLESRVEEIMEKSGEEGMPDLAHVMRILSAENIPNLPPGGGLAGNIIFFRRHVIEAVYSRLNPHRESDGASDEAEESGSQGKLVEALRQMRINHRGNYRQLLEEMLTSYRLAKVEGEENPAEQAATAASSNSDAGNTVAMQESHTESKSDLAELDSCTEDAGTKMSGEKL
|
Enzyme with a broad specificity. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB (By similarity).
|
O62846
|
KAPCG_MACMU
|
cAMP-dependent protein kinase catalytic subunit gamma (PKA C-gamma) (EC 2.7.11.11)
|
MGNAAAKKDTEQETVNEFLAKARGDFLYRWGNPAQNTASSDQFERLKTLGTGSYGRVMLVRHRETGNHYAMKILDKQKVVRLKQVEHTLNEKRILQAINFPFLVKLQFSFKDNSNLYLVMEYVPGGEMFSHLRRVGRFSEPQACFYAAQVVLAFQYLHSLDLIHRDLKPENLLIDQQGYLQVTDFGFAKRVKGRTWTLCGTPEYLAPEI
|
Phosphorylates a large number of substrates in the cytoplasm and the nucleus.
|
O64390
|
HXK1_SOLTU
|
Hexokinase-1 (EC 2.7.1.1) (StHK1)
|
MKKVTVGAAVVGAAAVCAVAALIVNHRMRKSSKWGRAMAILREFEEKCKTQDAKLKQVADAMTVEMHAGLASEGGQSSRCLSPMSIISQLVMKLGVFYALDLGGTNFRVLRVQLGGKDGGIIHQEFAEASIPPSLMVGTSDALFDYIAAELAKFVAAEEEKFHQPPGKQRELGFHLLIPSNADFNNSGTIMRWTKGFSIDDAVGQDVVGELTKAMKEKVLDMRVSALVNDTVGTLAGGKYTQKDVAVAVILGTGTNAAYVERVQAIPKWHGPVPKSGEMVINMEWGNFRSSHLPLTEYDHALDNESLNPAEQIFEKMTSGMYLGEILRRVLTRVAEEVLAFLAMRSLQSLKDSFVLRTPDMSAMHHDTSPDLKVVGEKLKDILEISNTSLKTRKLVLSLCNIVATRGARLDAAGVLGILKKMGRDTPKQGGSERTVIAMDGGLYEHYTEYRMCLENSLKDLLGEELATSIVFVHSNDGSGIGAALLRASHSMYLEDQA
|
Fructose and glucose phosphorylating enzyme. May be involved in the phosphorylation of glucose during the export from plastids to cytosol. Seems neither to be involved in cell sugar sensing nor in carbohydrate metabolism in tuber.
|
O64392
|
WHW1_WHEAT
|
Wheatwin-1 (Pathogenesis-related protein 4a) (Protein 0.14) (RNase) (EC 3.1.-.-)
|
MAARPMLVVALLCAAAAAATAQQATNVRATYHYYRPAQNNWDLGAPAVSAYCATWDASKPLSWRSKYGWTAFCGPAGAHGQASCGKCLQVTNPATGAQITARIVDQCANGGLDLDWDTVFTKIDTNGIGYQQGHLNVNYQFVDCRD
|
Shows antifungal activity towards B.cinerea and towards the wheat-specific pathogenic fungi F.culmorum and F.graminearum (groups 1 and 2). Has ribonuclease activity.
|
O64399
|
MYB34_ARATH
|
Transcription factor MYB34 (Myb-related protein 34) (AtMYB34) (Protein ALTERED TRYPTOPHAN REGULATION 1) (ATR1)
|
MVRTPCCKEEGIKKGAWTPEEDQKLIAYLHLHGEGGWRTLPEKAGLKRCGKSCRLRWANYLRPDIKRGEFSPEEDDTIIKLHALKGNKWAAIATSLAGRTDNEIKNYWNTNLKKRLKQKGIDAITHKPINSTGQTGFEPKVNKPVYSSGSARLLNRVASKYAVELNRDLLTGIISGNSTVAEDSQNSGDVDSPTSTLLNKMAATSVLINTTTTYSGFSDNCSFTDEFNEFFNNEEISDIYTTVDNFGFMEELKSILSYGDASAGVIENSPEVNVADAMEFIDSWNEDDNMVGVFV
|
Transcription factor involved in tryptophan gene activation and in indole-3-acetic acid (IAA) and indolic glucosinolates (IG) biosynthesis. Acts as a direct transcriptional activator of both Trp synthesis genes and Trp secondary metabolism genes.
|
O64411
|
PAO1_MAIZE
|
Polyamine oxidase 1 (EC 1.5.3.14) (EC 1.5.3.15)
|
MSSSPSFGLLAVAALLLALSLAQHGSLAATVGPRVIVVGAGMSGISAAKRLSEAGITDLLILEATDHIGGRMHKTNFAGINVELGANWVEGVNGGKMNPIWPIVNSTLKLRNFRSDFDYLAQNVYKEDGGVYDEDYVQKRIELADSVEEMGEKLSATLHASGRDDMSILAMQRLNEHQPNGPATPVDMVVDYYKFDYEFAEPPRVTSLQNTVPLATFSDFGDDVYFVADQRGYEAVVYYLAGQYLKTDDKSGKIVDPRLQLNKVVREIKYSPGGVTVKTEDNSVYSADYVMVSASLGVLQSDLIQFKPKLPTWKVRAIYQFDMAVYTKIFLKFPRKFWPEGKGREFFLYASSRRGYYGVWQEFEKQYPDANVLLVTVTDEESRRIEQQSDEQTKAEIMQVLRKMFPGKDVPDATDILVPRWWSDRFYKGTFSNWPVGVNRYEYDQLRAPVGRVYFTGEHTSEHYNGYVHGAYLSGIDSAEILINCAQKKMCKYHVQGKYD
|
Flavoenzyme involved in polyamine back-conversion (Ref.4, PubMed:16331971). Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine, spermidine and their acetyl derivatives (Ref.4, PubMed:16331971). Plays an important role in the regulation of polyamine intracellular concentration (Probable).
|
O64425
|
RMA1_ARATH
|
E3 ubiquitin-protein ligase RMA1 (EC 2.3.2.27) (Protein RING membrane-anchor 1) (RING-type E3 ubiquitin transferase RMA1)
|
MALDQSFEDAALLGELYGEGAFCFKSKKPEPITVSVPSDDTDDSNFDCNICLDSVQEPVVTLCGHLFCWPCIHKWLDVQSFSTSDEYQRHRQCPVCKSKVSHSTLVPLYGRGRCTTQEEGKNSVPKRPVGPVYRLEMPNSPYASTDLRLSQRVHFNSPQEGYYPVSGVMSSNSLSYSAVLDPVMVMVGEMVATRLFGTRVMDRFAYPDTYNLAGTSGPRMRRRIMQADKSLGRIFFFFMCCVVLCLLLF
|
E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of aquaporin PIP2-1. Forms a ubiquitin ligase complex in cooperation with the E2 enzymes UCB8/UCB10.
|
O64470
|
SHT_ARATH
|
Spermidine hydroxycinnamoyl transferase (AtSHT) (EC 2.3.1.-) (BAHD-like hydroxycinnamoyl transferase)
|
MAPITFRKSYTIVPAEPTWSGRFPLAEWDQVGTITHIPTLYFYDKPSESFQGNVVEILKTSLSRVLVHFYPMAGRLRWLPRGRFELNCNAEGVEFIEAESEGKLSDFKDFSPTPEFENLMPQVNYKNPIETIPLFLAQVTKFKCGGISLSVNVSHAIVDGQSALHLISEWGRLARGEPLETVPFLDRKILWAGEPLPPFVSPPKFDHKEFDQPPFLIGETDNVEERKKKTIVVMLPLSTSQLQKLRSKANGSKHSDPAKGFTRYETVTGHVWRCACKARGHSPEQPTALGICIDTRSRMEPPLPRGYFGNATLDVVAASTSGELISNELGFAASLISKAIKNVTNEYVMIGIEYLKNQKDLKKFQDLHALGSTEGPFYGNPNLGVVSWLTLPMYGLDFGWGKEFYTGPGTHDFDGDSLILPDQNEDGSVILATCLQVAHMEAFKKHFYEDI
|
Hydroxycinnamoyl transferase involved in the conjugation of feruloyl CoA to spermidine. Catalyzes the three conjugating steps required for the biosynthesis of N(1),N(4),N(8)-triferuloyl-spermidine. Spermidine is the only acceptor substrate while feruloyl CoA > caffeoyl CoA > coumaroyl CoA > cinnamoyl CoA >> sinapoyl CoA are efficient acyl donors. No activity with hydroxyferuloyl CoA. Required for the biosynthesis of these conjugated spermidine derivatives, specifically in anther tapetum.
|
O64471
|
MTX_ARATH
|
Mitochondrial outer membrane import complex protein METAXIN
|
MEGDQETNVYTLVARKPSFDLPTACPNCLPAYIYLKLAQLPFELAFNSTFPDSDELPYFESDTYVAYNNEDGGVIEKLKKDGIVNLDSQLQSLSDYLSLKALIVSWLEEALTYEIWVGTEGISTSKIYYSDLPWVISKVLFYKQTYLAKNRLGITKENAEQREKQIYKRASEAYEALSTRLGEQKFLFEDRPSSLDAFLLSHILFIIQALPVTSVLRCKLLEHSNLVRYAEKLKSEFLEASSSSPSPPLHSFPSSFPRKSSKPKSKPKVEKTEEEKKFKKRARFFLAAQFLAVVIYVSVMGGGSSDELEYEDEDD
|
Involved in transport of proteins into the mitochondrion.
|
O64474
|
HMA4_ARATH
|
Putative cadmium/zinc-transporting ATPase HMA4 (EC 7.2.2.12) (EC 7.2.2.21) (Protein HEAVY METAL ATPASE 4) (Putative cadmium/zinc-transporting ATPase 2)
|
MALQNKEEEKKKVKKLQKSYFDVLGICCTSEVPIIENILKSLDGVKEYSVIVPSRTVIVVHDSLLISPFQIAKALNEARLEANVRVNGETSFKNKWPSPFAVVSGLLLLLSFLKFVYSPLRWLAVAAVAAGIYPILAKAFASIKRPRIDINILVIITVIATLAMQDFMEAAAVVFLFTISDWLETRASYKATSVMQSLMSLAPQKAIIAETGEEVEVDEVKVDTVVAVKAGETIPIDGIVVDGNCEVDEKTLTGEAFPVPKQRDSTVWAGTINLNGYICVKTTSLAGDCVVAKMAKLVEEAQSSKTKSQRLIDKCSQYYTPAIILVSACVAIVPVIMKVHNLKHWFHLALVVLVSGCPCGLILSTPVATFCALTKAATSGLLIKSADYLDTLSKIKIVAFDKTGTITRGEFIVIDFKSLSRDINLRSLLYWVSSVESKSSHPMAATIVDYAKSVSVEPRPEEVEDYQNFPGEGIYGKIDGNDIFIGNKKIASRAGCSTVPEIEVDTKGGKTVGYVYVGERLAGFFNLSDACRSGVSQAMAELKSLGIKTAMLTGDNQAAAMHAQEQLGNVLDVVHGDLLPEDKSRIIQEFKKEGPTAMVGDGVNDAPALATADIGISMGISGSALATQTGNIILMSNDIRRIPQAVKLARRARRKVVENVCLSIILKAGILALAFAGHPLIWAAVLVDVGTCLLVIFNSMLLLREKKKIGNKKCYRASTSKLNGRKLEGDDDYVVDLEAGLLTKSGNGQCKSSCCGDKKNQENVVMMKPSSKTSSDHSHPGCCGDKKEEKVKPLVKDGCCSEKTRKSEGDMVSLSSCKKSSHVKHDLKMKGGSGCCASKNEKGKEVVAKSCCEKPKQQVESVGDCKSGHCEKKKQAEDIVVPVQIIGHALTHVEIELQTKETCKTSCCDSKEKVKETGLLLSSENTPYLEKGVLIKDEGNCKSGSENMGTVKQSCHEKGCSDEKQTGEITLASEEETDDQDCSSGCCVNEGTVKQSFDEKKHSVLVEKEGLDMETGFCCDAKLVCCGNTEGEVKEQCRLEIKKEEHCKSGCCGEEIQTGEITLVSEEETESTNCSTGCCVDKEEVTQTCHEKPASLVVSGLEVKKDEHCESSHRAVKVETCCKVKIPEACASKCRDRAKRHSGKSCCRSYAKELCSHRHHHHHHHHHHHVSA
|
Involved in cadmium/zinc transport.
|
O64483
|
SIRK_ARATH
|
Senescence-induced receptor-like serine/threonine-protein kinase (FLG22-induced receptor-like kinase 1)
|
MAMLKSLSSILFTSFALLFFLVHAQDQSGFISIDCGIPDDSSYNDETTGIKYVSDSAFVDSGTTKRIAAQFQSSGFDRHLLNVRSFPQSKRSCYDVPTPRGKGFKYLIRTRFMYGNYDDLGRVPEFDLYLGVNFWDSVKLDDATTILNKEIITIPLLDNVQVCVVDKNAGTPFLSVLEIRLLLNTTYETPYDALTLLRRLDYSKTGKLPSRYKDDIYDRIWTPRIVSSEYKILNTSLTVDQFLNNGYQPASTVMSTAETARNESLYLTLSFRPPDPNAKFYVYMHFAEIEVLKSNQTREFSIWLNEDVISPSFKLRYLLTDTFVTPDPVSGITINFSLLQPPGEFVLPPIINALEVYQVNEFLQIPTHPQDVDAMRKIKATYRVKKNWQGDPCVPVDYSWEGIDCIQSDNTTNPRVVSLNISFSELRGQIDPAFSNLTSIRKLDLSGNTLTGEIPAFLANLPNLTELNVEGNKLTGIVPQRLHERSKNGSLSLRFGRNPDLCLSDSCSNTKKKNKNGYIIPLVVVGIIVVLLTALALFRRFKKKQQRGTLGERNGPLKTAKRYFKYSEVVNITNNFERVIGKGGFGKVYHGVINGEQVAVKVLSEESAQGYKEFRAEVDLLMRVHHTNLTSLVGYCNEINHMVLIYEYMANENLGDYLAGKRSFILSWEERLKISLDAAQGLEYLHNGCKPPIVHRDVKPTNILLNEKLQAKMADFGLSRSFSVEGSGQISTVVAGSIGYLDPEYYSTRQMNEKSDVYSLGVVLLEVITGQPAIASSKTEKVHISDHVRSILANGDIRGIVDQRLRERYDVGSAWKMSEIALACTEHTSAQRPTMSQVVMELKQIVYGIVTDQENYDDSTKMLTVNLDTEMVPRAR
|
Involved in innate immune response of plants.
|
O64495
|
SBT12_ARATH
|
Subtilisin-like protease SBT1.2 (EC 3.4.21.-) (Cucumisin-like serine protease SDD1) (Protein STOMATAL DENSITY AND DISTRIBUTION 1) (Subtilase subfamily 1 member 2) (AtSBT1.2) (Subtilisin-like protease SDD1)
|
MEPKPFFLCIIFLLFCSSSSEILQKQTYIVQLHPNSETAKTFASKFDWHLSFLQEAVLGVEEEEEEPSSRLLYSYGSAIEGFAAQLTESEAEILRYSPEVVAVRPDHVLQVQTTYSYKFLGLDGFGNSGVWSKSRFGQGTIIGVLDTGVWPESPSFDDTGMPSIPRKWKGICQEGESFSSSSCNRKLIGARFFIRGHRVANSPEESPNMPREYISARDSTGHGTHTASTVGGSSVSMANVLGNGAGVARGMAPGAHIAVYKVCWFNGCYSSDILAAIDVAIQDKVDVLSLSLGGFPIPLYDDTIAIGTFRAMERGISVICAAGNNGPIESSVANTAPWVSTIGAGTLDRRFPAVVRLANGKLLYGESLYPGKGIKNAGREVEVIYVTGGDKGSEFCLRGSLPREEIRGKMVICDRGVNGRSEKGEAVKEAGGVAMILANTEINQEEDSIDVHLLPATLIGYTESVLLKAYVNATVKPKARIIFGGTVIGRSRAPEVAQFSARGPSLANPSILKPDMIAPGVNIIAAWPQNLGPTGLPYDSRRVNFTVMSGTSMSCPHVSGITALIRSAYPNWSPAAIKSALMTTADLYDRQGKAIKDGNKPAGVFAIGAGHVNPQKAINPGLVYNIQPVDYITYLCTLGFTRSDILAITHKNVSCNGILRKNPGFSLNYPSIAVIFKRGKTTEMITRRVTNVGSPNSIYSVNVKAPEGIKVIVNPKRLVFKHVDQTLSYRVWFVLKKKNRGGKVASFAQGQLTWVNSHNLMQRVRSPISVTLKTN
|
Serine protease involved in the negative regulation of stomatal density and distribution. Not active on EPFL6 (AC Q1PEY6). Positive regulator of water use efficiency (WUE).
|
O64503
|
UTR1_ARATH
|
UDP-galactose/UDP-glucose transporter 1 (At-UDP-Glc/GalT) (AtUTr1)
|
MEVHGSGFRRILLLALCISGIWSAYIYQGVLQETLSTKRFGPDEKRFEHLAFLNLAQSVVCLIWSYIMIKLWSNAGNGGAPWWTYWSAGITNTIGPAMGIEALKYISYPAQVLAKSSKMIPVMLMGTLVYGIRYTFPEYMCTFLVAGGVSIFALLKTSSKTISKLAHPNAPLGYALCSLNLAFDGFTNATQDSIASRYPKTEAWDIMLGMNLWGTIYNMIYMFGLPQGIGFKAIQFCKLHPEAAWDILKYCICGAVGQNFIFMTISNFGSLANTTITTTRKFVSIVVSSVMSGNPLSLKQWGCVSMVFGGLAYQIYLKWKKLQRVEKKKQKS
|
Essential sugar transporter required for the transport of UDP-galactose and UDP-glucose from the cytoplasm into the Golgi and the endoplasmic reticulum, to ensure quality control of protein folding. Essential for pollen development and involved in embryo sac progress.
|
O64517
|
MCA4_ARATH
|
Metacaspase-4 (AtMC4) (EC 3.4.22.-) (Metacaspase 2d) (AtMCP2d) (Metacaspase-7) [Cleaved into: Metacaspase-4 subunit p20; Metacaspase-4 subunit p10]
|
MTKKAVLIGINYPGTKAELRGCVNDVRRMYKCLVERYGFSEENITVLIDTDESSTQPTGKNIRRALADLVESADSGDVLVVHYSGHGTRLPAETGEDDDTGFDECIVPCDMNLITDDDFRDLVDKVPPGCRMTIISDSCHSGGLIDEAKEQIGESTKKEAEDEDESEESSSRFGFRKFLRSKVEGAIESRGFHIGGNKKDEDEAEEIETKEIELEDGETIHAKDKSLPLQTLIDILKQQTGNDNIEVGKIRPSLFDAFGDDSSPKVKKFMKVILGKLQAGNGEEGGLMGMLGKLASGFLEGKLNDEDYVKPAMQTHVGSKEEVYAGGSRGSVPLPDSGILISGCQTDQTSADATPAGKPTEAYGAMSNSIQTILEETDGEISNREMVTRARKALKKQGFTQQPGLYCHDGYANAPFIC
|
Cysteine protease that cleaves specifically after arginine or lysine residues. Does not cleave caspase-specific substrates. Plays a positive regulatory role in biotic and abiotic stress-induced programmed cell death.
|
O64530
|
STR1_ARATH
|
Thiosulfate/3-mercaptopyruvate sulfurtransferase 1, mitochondrial (EC 2.8.1.1) (EC 2.8.1.2) (AtMST1) (Rhodanese homolog protein 1) (AtRDH1) (Sulfurtransferase 1) (AtStr1)
|
MASTLFSRTFLAASHRLITPSLPQKIFNPATFLSRSLHSQLGSASTAYKSTTWARRAMASTGVETKAGYSTSSVSTSEPVVSVDWLHANLREPDLKILDASWYMPDEQRNPIQEYQVAHIPRALFFDLDGISDRKTSLPHMLPTEEAFAAGCSALGIDNKDEVVVYDGKGIFSAARVWWMFRVFGHEKVWVLDGGLPRWRASGYDVESSASGDAILKASAASEAIEKIYQGQTVSPITFQTKFQPHLVWTLDQVKNNMEDPTYQHIDARSKARFDGTAPEPRKGIRSGHIPGSKCIPFPQMFDSCNTLLPAEELKKRFDQEDISLDKPIMASCGTGVTACILAMGLHRLGKTDVPIYDGSWTEWATQPDLPIESVESSS
|
Catalyzes the transfer of a sulfur ion from a donor to cyanide or to other thiol compounds. Substrate preference is 3-mercaptopyruvate > thiosulfate. Involved in embryo and seed development.
|
O64587
|
ACD11_ARATH
|
Accelerated cell death 11 (Ceramide-1-phosphate transfer protein ACD11) (Glycolipid transfer protein domain-containing protein ACD11)
|
MADSEADKPLRKISAAFKKLAIIVNSPNPEVPVTQFSHACSLVSPLFGCLGIAFKFAEMDYVAKVDDLVRASSSISTLVVMMDKDIEADCVRKAGSHTRNLLRVKRGLDMVKVLFEQIIASEGDNSLKDPATKSYAQVFAPHHGWAIRKAVSLGMYALPTRAHLLNMLKEDEAAAKIHMQSYVNSSAPLITYLDNLFLSKQLGIDW
|
Exhibits selective intermembrane transfer of ceramide-1-phosphate (C1P) and phytoceramide-1-phosphate. Does not transport ceramide (Cer) or GalCer, suggesting a requirement for phosphate in the headgroup for functionality. Transports in vitro sphingosine, but not glycosphingolipids. Has also some in vitro activity with sphingomyelin, a lipid not detected in plant tissues. The transport function may be not directly involved in regulating cell death. Rather, perturbations in the function of ACD11 or related components could be monitored by R-proteins, which then mediate defense and programmed cell death (PCD), as proposed in the guard hypothesis (Probable). C1P transfer is stimulated by phosphatidylserine in C1P source vesicles. Regulates autophagy, inflammasome mediated IL1B and IL18 processing, and pyroptosis, but not apoptosis.
|
O64614
|
YIP4A_ARATH
|
Protein YIP4a (YPT/RAB GTPase-interacting protein 4a) (YIP4a)
|
MSQGDTVPLHPSSQSDIDEIENLINESVQSGPGTVLAARPPSPTRPSIPVSSSSSSSPFMQSNLPPLHPSSSAQKVTHVPVPPPLPAVSNSSNFQGASAFGSPPNTLTEPVWDTVKRDLSRIVSNLKLVVFPNPYREDPGKALRDWDLWGPFFFIVFLGLTLSWSASVKKSEVFAVAFALLAAGAVILTLNVLLLGGHIIFFQSLSLLGYCLFPLDVGAVICMLKDNVILKMVVVSVTLAWSSWAAYPFMSSAVNPRRKALALYPVFLMYVSVGFLIIAIN
|
Together with YIP4B, involved in the regulation of cell elongation during root and hypocotyl growth. YIP4A and YIP4B are central trafficking components in Rho-of-plant (ROPs, e.g. ARAC4/ROP2, ARAC5/ROP4 and ARAC3/ROP6) small GTPases-dependent root hair formation, thus contributing to activation and plasma membrane accumulation of ROPs during hair initiation. The ECH/YIP4 complex is involved in the modulation of the trans-Golgi network (TGN)-mediated trafficking of some proteins and cell wall components (e.g. pectin and hemicellulose) to the cell wall in dark-grown hypocotyls and in secretory cells of the seed coat.
|
O64629
|
AUR3_ARATH
|
Serine/threonine-protein kinase Aurora-3 (AtAur3) (EC 2.7.11.1) (Aurora-like kinase 3)
|
MSKKSTESDAGNTEKQWSLADFEIGRPLGKGKFGRVYLAREAKSKYIVALKVIFKEQIEKYKIHHQLRREMEIQTSLRHPNILRLFGWFHDNERIFLILEYAHGGELYGVLKQNGHLTEQQAATYIASLSQALAYCHGKCVIHRDIKPENLLLDHEGRLKIADFGWSVQSSNKRKTMCGTLDYLAPEMVENRDHDYAVDNWTLGILCYEFLYGNPPFEAESQKDTFKRILKIDLSFPLTPNVSEEAKNLISQLLVKDPSKRLSIEKIMQHPWIVKNADPKGVCASIDI
|
Phosphorylates in vitro histone H3 at 'Ser-10' (H3S10ph) and 'Ser-28' (H3S28ph), but not at 'Thr-3' (H3T3ph) or 'Thr-11' (H3T11ph). Colocalizes with phosphorylated histone H3 during mitosis. Associates with cytoskeletal structures that are necessary for cytokinesis and with the microtubule spindle.
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O64642
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URT1_ARATH
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UTP:RNA uridylyltransferase 1 (EC 2.7.7.52)
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MADGGAEPPAPPSSINAGEFLLSILHGSPSPSSQGPQHHQSFALDPAIAAIGPTVNNPFPPSNWQSNGHRPSNHNPPSWPLAFSPPHNLSPNFLGFPQFPPSPFTTNQFDGNQRVSPEDAYRLGFPGTTNPAIQSMVQQQQQQQLPPPQSETRKLVFGSFSGDATQSLNGLHNGNLKYDSNQHEQLMRHPQSTLSNSNMDPNLSHHRNHDLHEQRGGHSGRGNWGHIGNNGRGLKSTPPPPPPGFSSNQRGWDMSLGSKDDDRGMGRNHDQAMGEHSKVWNQSVDFSAEANRLRGLSIQNESKFNLSQQIDHPGPPKGASLHSVSAADAADSFSMLNKEARRGGERREELGQLSKAKREGNANSDEIEDFGEDIVKSLLLEDETGEKDANDGKKDSKTSREKESRVDNRGQRLLGQKARMVKMYMACRNDIHRYDATFIAIYKSLIPAEEELEKQRQLMAHLENLVAKEWPHAKLYLYGSCANSFGFPKSDIDVCLAIEGDDINKSEMLLKLAEILESDNLQNVQALTRARVPIVKLMDPVTGISCDICINNVLAVVNTKLLRDYAQIDVRLRQLAFIVKHWAKSRRVNETYQGTLSSYAYVLMCIHFLQQRRPPILPCLQEMEPTYSVRVDNIRCTYFDNVDRLRNFGSNNRETIAELVWGFFNYWAYAHDYAYNVVSVRTGSILGKREKDWTRRVGNDRHLICIEDPFETSHDLGRVVDKFSIRVLREEFERAARIMHQDPNPCAKLLEPYIPEDNNGQGHN
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UTP:RNA uridylyltransferase with a marked preference for uridine polymerization and a distributive activity for the first added nucleotides. Uridylates oligo(A)-tailed mRNAs to prevent 3' to 5' ribonucleotytic attacks. Reduces the accumulation of oligo(A)-tailed mRNAs. Prevents the accumulation of excessively deadenylated mRNAs to avoid siRNA biogenesis. Uridylation repairs deadenylated extremities to restore the size distribution observed for non-uridylated oligo(A) tails. Can prevent the 3' trimming of mRNAs still engaged on polysomes. Acts synergistically with HESO1 in unmethylated miRNA uridylation, leading to their degradation. URT1 and HESO1 prefer substrates with different 3' end nucleotides and act cooperatively to tail different forms of the same miRNAs. URT1 and HESO1 act sequentially, with URT1 mono-uridylating the miRNAs followed by their further uridylation by HESO1. URT1 and HESO1 are involved in the uridylation and clearance of RISC-generated 5' mRNA fragments. Has no effect on uridylation of heterochromatic siRNAs. Able to act on AGO1-bound miRNAs and the uridylated species stay associated with AGO1. Acts as post-transcriptional gene silencing (PTGS) suppressor.
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O64644
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SAP18_ARATH
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Histone deacetylase complex subunit SAP18 (18 kDa Sin3-associated polypeptide)
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MAEAARRQGGGRPLPPPPRGVNQQPPRPKPEPVDREKTCPLLLRVFTKSGGHHTSEDYAVRGKEPKDEVQIYTWKDASLRELTDLVKEVSVAARRRNARLSFAFVYPNNKGGYNVREVGETMAYPNRKQPDDSKTLSELPFEIGDYLDVAIY
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Links the histone deacetylase complex to transcriptional repressors bound to chromatin. Involved in the tethering of the SIN3 complex to core histone proteins.
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O64645
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SOC1_ARATH
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MADS-box protein SOC1 (Agamous-like MADS-box protein AGL20) (Protein SUPPRESSOR OF CONSTANS OVEREXPRESSION 1)
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MVRGKTQMKRIENATSRQVTFSKRRNGLLKKAFELSVLCDAEVSLIIFSPKGKLYEFASSNMQDTIDRYLRHTKDRVSTKPVSEENMQHLKYEAANMMKKIEQLEASKRKLLGEGIGTCSIEELQQIEQQLEKSVKCIRARKTQVFKEQIEQLKQKEKALAAENEKLSEKWGSHESEVWSNKNQESTGRGDEESSPSSEVETQLFIGLPCSSRK
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Transcription activator active in flowering time control. May integrate signals from the photoperiod, vernalization and autonomous floral induction pathways. Can modulate class B and C homeotic genes expression. When associated with AGL24, mediates effect of gibberellins on flowering under short-day conditions, and regulates the expression of LEAFY (LFY), which links floral induction and floral development.
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O64682
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PID_ARATH
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Protein kinase PINOID (EC 2.7.11.1) (Protein kinase ABRUPTUS)
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MLRESDGEMSLGTTNSPISSGTESCSSFSRLSFDAPPSTIPEEESFLSLKPHRSSDFAYAEIRRRKKQGLTFRDFRLMRRIGAGDIGTVYLCRLAGDEEESRSSYFAMKVVDKEALALKKKMHRAEMEKTILKMLDHPFLPTLYAEFEASHFSCIVMEYCSGGDLHSLRHRQPHRRFSLSSARFYAAEVLVALEYLHMLGIIYRDLKPENILVRSDGHIMLSDFDLSLCSDSIAAVESSSSSPENQQLRSPRRFTRLARLFQRVLRSKKVQTLEPTRLFVAEPVTARSGSFVGTHEYVAPEVASGGSHGNAVDWWAFGVFLYEMIYGKTPFVAPTNDVILRNIVKRQLSFPTDSPATMFELHARNLISGLLNKDPTKRLGSRRGAAEVKVHPFFKGLNFALIRTLTPPEIPSSVVKKPMKSATFSGRSSNKPAAFDYF
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Serine/threonine-protein kinase involved in the regulation of auxin signaling. Acts as a positive regulator of cellular auxin efflux and regulates organ development by enhancing polar auxin transport. Phosphorylates conserved serine residues in the PIN auxin efflux carriers. Phosphorylation of PIN proteins is required and sufficient for apical-basal PIN polarity that enables directional intercellular auxin fluxes, which mediate differential growth, tissue patterning and organogenesis. Acts in association with PIN1 to control the establishment of bilateral symmetry and promotion of cotyledon outgrowth. Regulates root gravitropism through modulation of PIN2-dependent basipetal auxin transport. Required for polarization of PIN3-dependent auxin transport for hypocotyl gravitropic response. The protein kinase activity of PID is essential for its auxin efflux regulatory function. PID kinase and PP2A phosphatase activities antagonistically regulate phosphorylation of PIN proteins, affecting PIN sorting.
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O64697
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C7101_ARATH
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Cytochrome P450 710A1 (EC 1.14.19.41) (C-22 sterol desaturase)
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MVFSVSIFASLAPYLISAFLLFLLVEQLSYLFKKRNIPGPFFVPPIIGNAVALVRDPTSFWDKQSSTANISGLSANYLIGKFIVYIRDTELSHQIFSNVRPDAFHLIGHPFGKKLFGDHNLIYMFGEDHKSVRRQLAPNFTPKALSTYSALQQLVILRHLRQWEGSTSGGSRPVSLRQLVRELNLETSQTVFVGPYLDKEAKNRFRTDYNLFNLGSMALPIDLPGFAFGEARRAVKRLGETLGICAGKSKARMAAGEEPACLIDFWMQAIVAENPQPPHSGDEEIGGLLFDFLFAAQDASTSSLLWAVTLLDSEPEVLNRVREEVAKIWSPESNALITVDQLAEMKYTRSVAREVIRYRPPATMVPHVAAIDFPLTETYTIPKGTIVFPSVFDSSFQGFTEPDRFDPDRFSETRQEDQVFKRNFLAFGWGPHQCVGQRYALNHLVLFIAMFSSLLDFKRLRSDGCDEIVYCPTISPKDGCTVFLSRRVAKYPNFS
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Required to form the C-22 double bond in the sterol side chain. Possesses in vitro C-22 desaturase activity toward beta-sitosterol and produces stigmasterol. No activity with campesterol.
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O64722
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ZHD3_ARATH
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Zinc-finger homeodomain protein 3 (AtZHD3) (Homeobox protein 21) (AtHB-21) (Zinc finger homeodomain transcription factor 4)
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MEIASQEDPIPINTSYGNSGGGHGNMNHHHHANSAPSSLNITTSNPLLVSSNSNGLGKNHDHSHHHHVGYNIMVTNIKKEKPVVIKYKECLKNHAATMGGNAIDGCGEFMPSGEEGSIEALTCSVCNCHRNFHRRETEGEEKTFFSPYLNHHQPPPQQRKLMFHHKMIKSPLPQQMIMPIGVTTAGSNSESEDLMEEEGGGSLTFRQPPPPPSPYSYGHNQKKRFRTKFTQEQKEKMISFAERVGWKIQRQEESVVQQLCQEIGIRRRVLKVWMHNNKQNLSKKSNNVSNNVDLSAGNNDITENLASTNP
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Putative transcription factor.
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