entry
stringlengths 6
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| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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F1QC45
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XRP2_DANRE
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Protein XRP2
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MGCFFSKKSRRKSPKKDAALPTGDESATGNDLAETNNTALGSNSNQEAPKQYSWDKREKVDPKDFMLTGLKNETVGRLPGKLNGQQFVIQDCENCNIFVLDHSATITIDDCVNCRIVLGPVKGSVFFRDCKDIKCVVACQQFRTRDCKKMDVFLCCATQPIIESSTGMKFGCFQYYYPELAFHFKDAGLSIFNNNWSNIHDFTPVSGETNWSLLPEDAVVLDHVPLPDPESEFKSVRIATEAGRSIVPLTKGSRRTESEESCLFVFFAGDYTTANARKLIDEATAKGFVLIQTKEVSMRPEDVSRVFQNNAESLTEWITKGPVVALELNGDGVVEACRSFANEVFNGTQLFVSESKNTSSRDVDNFFNFADMQMGL
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Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane (By similarity). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization (By similarity). In the retina, required for maintenance of rod and cone photoreceptor cells. May have a role in normal retinal localization of the transducins GNB1 and GNAT1, and the rhodopsin kinase GRK1.
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F1QCP6
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TAZ_DANRE
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Tafazzin (Taz) (EC 2.3.1.-)
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MPLEVTWPFPQCPRLGWRISSRVVMGMVGSYSYLWTKYFNSLMVHNQDVLLNLVDERPQDTPLITVCNHQSCMDDPHIWGVLKFRQLWNLNKMRWTPTASDICFTREFHSSFFSRGKCVPVVRGDGVYQKGMDFLLERLNQGEWIHIFPEGRVNMSGEFMRIKWGIGRLIAECSLHPIILPMWHIGMNDVLPNETPYIPRVGQRITVLVGKPFTVRHLVNALRAENTNPTEMRKTVTDYIQDEFRSLKAQAEALHHRLQNHT
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Acyltransferase required to remodel newly synthesized phospholipid cardiolipin (1',3'-bis-[1,2-diacyl-sn-glycero-3-phospho]-glycerol or CL), a key component of the mitochondrial inner membrane, with tissue specific acyl chains necessary for adequate mitochondrial function (By similarity). Its role in cellular physiology is to improve mitochondrial performance (By similarity). CL is critical for the coassembly of lipids and proteins in mitochondrial membranes, for instance, remodeling of the acyl groups of CL in the mitochondrial inner membrane affects the assembly and stability of respiratory chain complex IV and its supercomplex forms (By similarity). Catalyzes the transacylacion between phospholipids and lysophospholipids, with the highest rate being between phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) and CL. Catalyzes both 1-acyl-sn-glycero-3-phosphocholine (lysophosphatidylcholine or LPC) reacylation and PC-CL transacylation, that means, it exchanges acyl groups between CL and PC by a combination of forward and reverse transacylations. Also catalyzes transacylations between other phospholipids such as phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) and CL, between PC and PE, and between PC and phosphatidate (1,2-diacyl-sn-glycero-3-phosphate or PA), although at lower rate. Not regiospecific, it transfers acyl groups into any of the sn-1 and sn-2 positions of the monolysocardiolipin (MLCL), which is an important prerequisite for uniformity and symmetry in CL acyl distribution. Cannot transacylate dilysocardiolipin (DLCL), thus, the role of MLCL is limited to that of an acyl acceptor. CoA-independent, it can reshuffle molecular species within a single phospholipid class. Redistributes fatty acids between MLCL, CL, and other lipids, which prolongs the half-life of CL. Its action is completely reversible, which allows for cyclic changes, such as fission and fusion or bending and flattening of the membrane. Hence, by contributing to the flexibility of the lipid composition, it plays an important role in the dynamics of mitochondria membranes. Essential for the final stage of spermatogenesis, spermatid individualization (By similarity). Required for the initiation of mitophagy (By similarity). Required to ensure progression of spermatocytes through meiosis (By similarity).
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F1QCV2
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HDA10_DANRE
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Polyamine deacetylase HDAC10 (EC 3.5.1.48) (EC 3.5.1.62) (Histone deacetylase 10)
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MASGSALIFDEEMSRYKLLWTDPACEIEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYNDVYFHQNIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAKKNYNLNRILIVDWDVHHGQGIQYCFEEDPSVLYFSWHRYEHQSFWPNLPESDYSSVGKGKGSGFNINLPWNKVGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAGFDSAIGDPEGEMCALPEIFAHLTHLLMPLAAGKMCVVLEGGYNLTSLGQSVCQTVHSLLGDPTPRISGLGTACDSALESIQNVRNVQSSYWSSFKHLAQSETNPKRPRLDATNGGPKESSEPASESNPKKTAQDIVWPEPLKRMPASVRTVVVPPPGVELTLPKNCQHSGDISESTAKEVQRIRDKHFHDLTDQNILRSLGNIISVLDRMMRSDEVCNGCVVVSDLSVSVQCALQHALTEPAERVLVVYVGDGELPVKTNDGKVFLVQICTKETEDKCVNRLSLCLREGESLTAGFMQALLGLILPVAYEFNPALVLGIVGETAAKTGLMTVWGHMTCLIQGLARGRTLTLLQGYDKDLLELTVSALSGASISPLGPLRALKPEDVEMMEKQRQRLQERWGLLRCTVSES
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Polyamine deacetylase (PDAC), which acts preferentially on N(8)-acetylspermidine, and also on acetylcadaverine and acetylputrescine. Exhibits attenuated catalytic activity toward N(1),N(8)-diacetylspermidine and very low activity, if any, toward N(1)-acetylspermidine. Has a very weak lysine deacetylase, if any.
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F1QDF8
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FXJ1A_DANRE
|
Forkhead box protein J1-A
|
MLSMSSMDPWPEGSVGLEEEVVTAAAQAERLDTSTPLQCNTSLDSDNLDDSLTSLQWLQEFSILNASTGQHTSPSSHSHLMGSDAPSSPLAGDPASIGMPLTPGKPTAASFCRVPMFSALPSLVAHGHCPDEVDYKSNPHIKPPYSYATLICMAMQASKKTKITLSCIYKWITDNFCYFRHADPTWQNSIRHNLSLNKCFIKVPRQKDEPGKGGFWKIDPQYAERLLNGAYKKRRLPPVQINPALQHRLRMNAQATGVISRNLSVSPESQQLLKDFEEATSADQNWDPRLAEATMLSCWISGKGTNKRKQPYNHRTGKTPRRSSSPLLVMDEQEDLSSLRGNFDWDALLDSALNGELSLNEGSPLSPTPQDEELMIRGTHISPQEAPVENHVLMETQRSGDEDFDEETFLATAFLQSPWSEVDESNRSDFLGSSTVSIDQLFDLSFGGDLSSKIETLL
|
Key transcription factor required for motile ciliogenesis. Activates genes essential for motile cilia formation and function. Its activity is sufficient for ectopic development of cilia that resemble motile cilia.
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F1QEB7
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WDR11_DANRE
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WD repeat-containing protein 11
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MASTMIPYTVNIKLAARTLTGTLNLQNKTAVDWGWQGLIAQGCHSSILIIDPNTAQTIQVLERHKANVVKVKWSRENYHHSLSSPYSLRLASADAAGKIIVWDVVSGMAHCEIQEHSKPIQDMDWLWAQDASRDLLLAVHPPNYIVLWNGDTGTKLWKKSYAENILSFSFDPFEPSNLALLTSEGIVFITDFSHSKPPGSGGKKVYIASPHSSPAHSKPAAAQPTGAKKALNKVKVLITNEKPTAEAVTLNDCLQLSYLPSKRNHMLLLYPREILILDLELSQTVGVVAIERSGVPFIQVIPCAQRDALYCLHENGCITLRVCRSTTPSPNETVTDPEQNSQELVYDLRSQCDAIRVTKTVRPYRVVICPVNENKAVLVVSDGRVMLWELKAHASKSSSNLSSGLPPLYSAVNFCGTPLRQNQKCIPDLSLNSMIGHSLIPGVDSPRPLADQKEVHLKFLLTGLLSGLPLPPFSLRMCPPLTTKNINHYQPLLAVGTSNGSVLVYNLTSGLLHKELSVHSCEVRGIEWISLTSFLSFATSVPNNLGLVRNELQHVDLRTGRCFAFRGERGNDEPAIEMIKVSHLKQYLVVVFRDKPLELWDVRTGTLLREMAKNFPTVTALEWSPSHNLKSLKKKQLAAREAMARQTTLADAEQSSVESSVISLLQDAESKSESSQGISAREHFVFTDTDGQVYHITVEGNTVKDGARIPPDGSMGSIACIAWKGDTLVLGDVDGNLNFWDLKARLSRGVPTHRGWVKKIRFAPGKGNQKLLVMYTDGAEVWDTKEVQMVSSIRVGRNVNYRILDIDWCTSDKVVLASDDGCVRVLEMAMKSASYRMDEQDLTDPVWCPYLLLPRAALTLKAFLLLQPWMDTFTMDITQVDYKEKDEIKGLIQEQLNSLSNDIKSVLQDPNLSLLQRCLLVSRLFGDESDLQFWTVASHYIQAFAQSAQSNESVPEGQAAASHLDICHDILCESSFFQGFQLERVRLQEVKRSSYEHTKKCADQLLLLGQTDRAVQLLLETSADNSSYYCDSLKACLVTTITSSGPSQSTIKLVATNMIANGKLAEGVQLLCLIDKAADACRYLQTYGEWTRAAWLAKVRLNAAEGSDVLKRWAEHLCSPQVNQKSKAMLVLLSLGCFQKVGEMLHSMRYFDRAALFIEACLKYGVMETNDDINKLVGAAFVDYAKLLRSIGLKQGAVHWASRAGEAGKQLLEDLSQTEGTGTESSPADDTDNSLVNIE
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Involved in the Hedgehog (Hh) signaling pathway, is essential for normal ciliogenesis. Regulates the proteolytic processing of gli3 and cooperates with the transcription factor emx1 in the induction of downstream Hh pathway gene expression and gonadotropin-releasing hormone production. WDR11 complex facilitates the tethering of Adaptor protein-1 complex (AP-1)-derived vesicles.
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F1QFS9
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UBP13_DANRE
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Ubiquitin carboxyl-terminal hydrolase 13 (EC 3.4.19.12) (Deubiquitinating enzyme 13) (Ubiquitin thioesterase 13) (Ubiquitin-specific-processing protease 13)
|
MATDLGELLVPYMPTIRVPRTGDRVFKSECAFSYDSPESEGGLYVCMNSFLGFGREHVERHYRKTGQSVYMHLKRHVKEKATGAAGGAIPRRRNGKVFLDLELNRDFNGDDYEYEDEAKLVIFPDHYEIPLPNIEELPALVTIACDAVLNAPSPYKKQESDSWEEEIQVSRHARSLRQLDNGVRIPPSGWKCAKCEMRENLWLNLTDGSVLCGKWFFDGSGGNGHALEHYRESNFPLAVKLNTITPDGADIYSFDEEEAVLDPHISEHLLHFGIDMLQMQRTENGHHTDNHVQPRISDWEVIQEAGLKLKPVYGSGYTGIKNLGNSCYLSTTMQVLFSIPEFQRAYAGNLQRIFDYSPLDPTQDFNTQMAKLGHGLLSGQYSKPPMKSELIEQVMKEEHKQQQQRGISPKMFKALVSKGHPEFSSNRQQDAHEFLLHLINLVERNNSGSENPSDVFRFIVEERTQCCQSQKVRYTQRVDYLMQLPVPLEAASNREELIAYEGKRKEAEENMRPLPEVVRARVPFTACLQAFTEPENVPDFWSSALQAKSAGVKTSRFATFPEYMIVQLKKFTFGVDWVPKKLDMSVDVPDFLDLNRLRATGLQAGEEELPDLTPPIVIPEDTRDSSTNNSLESPEIDESSVMQLAEMGFPLEACRKAVYYTGNMGAEMAFNWIIAHMEEPDFAEPLAVPTYMESDLPSPSLPTTSALDNQPPEESISILTSMGFPRHHTIQALKASNNNLERALDWIFTHPDCEDESEAMSDTADTEPNDNSFSNANAHTDSSLSPDQDLSSPRVRDGPGRYELFAFISHMGTSTMSGHYVCHIKKEGRWLIYNDHKVCLSERPPKDLGYMYFYRRLSSC
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Deubiquitinase that mediates deubiquitination of target proteins and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD).
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F1QG30
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NSMA5_DANRE
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Sphingomyelin phosphodiesterase 5 (EC 3.1.4.12) (Mitochondrial neutral sphingomyelinase) (mtnSMase)
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MSLRESPFPNGFLEGLHAVGWGLIFPCFWFLDRLIAVCISTTLERMWRLEQECYLHPLKVVFGSILFFILFVISTPFALLGFILWAPLQAIRRPFSYHKQEQSIPMENRNARWEEMGKISFGFLTANVCLLPDGIARFNNLGHTQKRALIIGKSIVQGVTRPHIRIFVDSPSSCGTVTPSSSLIPQPNASSYGSVDASGELPDAIEVNEITPKPNCNQNSNHQKHPPRSLRTLLRDADIPMEVSALFPPSVDIVCLQEVFDKRAARKLTQALGPLYGHVLYDVGVYACHPAGSCSSFKFFNSGLFLASRFPIMEAEYRCFPNGRGEDALAAKGLLTVKVDIGLQKGEKRMVGFINCTHLHAPEGDGAIRFEQLNMLSKWTSEFQTLNRRDDELPLFDVLCGDFNFDNCSPDDRLEQSHSVFDEYTDPCRAAAGKEKPWVIGTLLEQPTLYDENMRTPDNLQRTLESEDLRKDFISPPVALDGVPLVYPEADQPWIGRRIDYLLYREKSGHRTEVEELTYVTQLAGLTDHIPVGFRLSVSLDSEQN
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Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide.
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F1QGH7
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CTNB1_DANRE
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Catenin beta-1 (Beta-catenin)
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MATQSDLMELEMAMDPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEDDDVDNQVLYEWEQGFNQSFNQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDSAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTSGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQDAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDIHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMTWNETGDLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDAMGMDPMMEHEMAGHHPGPDYPVDGLPDLGHTQDLIDGLPPGDSNQLAWFDTDL
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Key downstream component of the canonical Wnt signaling pathway (By similarity). In the absence of Wnt, forms a complex with axin1, axin2, apc, csnk1a1 and gsk3b that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of ctnnb1 and its subsequent degradation by the proteasome (By similarity). In the presence of Wnt ligand, ctnnb1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes (By similarity). Plays a key role in dorsoventral patterning: in prospective ventral blastomeres, its down-regulation by axin1 and axin2 leads to inhibit the Wnt signaling pathway, while in prospective dorsal blastomeres, degradation of axin results in stabilization and nuclear translocation of ctnnb1.
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F1QGZ6
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MELK_DANRE
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Maternal embryonic leucine zipper kinase (zMelk) (EC 2.7.11.1) (Protein kinase PK38)
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MPVDSTSELLKHYEVYETIGSGGFAKVKLGRHKLTGEKVAIKIMEKKDLGDDLPRVKIEIEAMKNLSHQHVCRLYHVIETTSKIYMVLEYCPGGELFDYIIAKDRLSEEETRVFFRQIISALAYVHSQGYAHRDLKPENLLIDEDHNLKLIDFGLCAKPKGGLGFELLTCCGSPAYAAPELIQGKAYIGSEADVWSMGVLLYALLCGFLPFDDDNCMVLYRKITRGKYSNPHWLSPSSILLLNQMMQVDPKRRLTVKHLLDHPWVMRGYSTPVEWHSKYPLGHIDEDCITEMAVTFKQSKQRTIQLVSEWKYDQITATYLLLLAKKRQGRPVRLRAECPVIDIVCSPLQDMQLKKSLRFTEDDDGVHPVVLGSMVFPPDCYDDENPWTPLTPKNTHTTNTPRMKLYPETTEKWNEMAYSPVIEHSRPCRQKPERRERTKENKENLAVPGTDGDVFALPAPRTPTSSRKVKSNRTVMTTPNHNNNKSSEVNKGAGSATKEGSRRREVEQQQNGQQGELNILAFSPERRSRSLDLAGCQVDSGQKRKGGKVFGSLERGLDKVITMLTPSKKRGPRDGPRKIKAQYNVTLTNQTNADQVLNQILSILPEKNVDFVQKGYTLKCHTQSDFGKVTMQFELEVCLLQKPEVVGIRRQRLKGDAWVYKHLVEDILSSSSQWSA
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Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation (By similarity). Also plays a role in primitive hematopoiesis, possibly by affecting the expression of genes critical for hematopoiesis. {ECO:0000250, ECO:0000269|PubMed:16024803}.
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F1QLG5
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ADN1A_DANRE
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Activity-dependent neuroprotective protein a (ADNP homeobox protein a)
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MFQLPVNNLTRLRKARKKVKRLLSDIGLDYCKEHVEDYKDVDPDDSDDSNESHLDLCTWDPTWTKSQDYRTKQFCCSDCPFASKYFSAYKNHFRNVHREDFESRILLNCSYCTYSGNKRTLETHVRLFHMPHNVMRQGVVGPHGAPVGAKDGMRVDKPMLGDRKELPVYYCKKCTYRDRLYNVVRRHIYREHFQHVATPYLGKNSEKQVNSGEAQANSHGIHCKSCHFTPRSYEALVQHVIEFHERIGHQVTAMIGHTNVIVPRLQTNPIQRGVPITSGVRPQTPQMNRFSMPKVVGLPVGNHFKQSLAGNSVPGQPVRVTLPDKAFVSSAVSHSHSGKHLGGFGVHGAAHLNAQSASFSPSLKSLPLSSSVHAATATLTSLQAKKASANALNTSQTQKWKICTICNELFPESAYSAHFEKEHQAEKVRAMAKYIMKIHNFTSKCLYCNRYLPSDSLLNHMLVHGLSCPHCHSTFHEVEKIVAHNRLAHPNEQGDQPTGSPLTFDLTLQQGNLKNVQLLVTTYNMKETPEAAAAAAAANQLSQNSAMPKPVKVSVRQPDTQSDSLVRNMSQSPVSQKKEVGKTLCPLCFTILKGPISDALAHHLRDSHQVLQTLHPVEKKLTYKCIHCLGVYTSNMTASTITLHLVHCRGVCQTPKGSKPITTGLRSPGAGSLKRELVTPDPSDPKRRKMVDQSRFYPTGFAEKPEEPIVLALDPKGYGDKSYEVRKAFLTAYFNRHPYPSQREVEKLAASLWLWKSDVASHFGNHRRLCDRDFTSRKPVVLLGFNMRLLSQIKHDMSFDDSCLFEVFDDEKSGYSRTSSFRLKSPIGFPADFIGSKQPLNTGQSSQSNCAFKTCPGSSSEPIAIDSDSDSELEVIPNENVSQHTPALRPSIVQSQTKGALLRESLRCERDVRANRSSPRVGPKVLDGSVSSSSPDEATWSGNMSSEESHYIPAGRFEVKGKKVGLLGR
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May be involved in transcriptional regulation. Positively modulates wnt-beta-catenin/ctnnb1 signaling. Required for embryonic neurogenesis. Required for progression through late erythroid differentiation.
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F1QLP1
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DHI2_DANRE
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11-beta-hydroxysteroid dehydrogenase type 2 (11-DH2) (11-beta-HSD2) (11-beta-hydroxysteroid dehydrogenase type II) (11-HSD type II) (11-beta-HSD type II) (Corticosteroid 11-beta-dehydrogenase isozyme 2) (NAD-dependent 11-beta-hydroxysteroid dehydrogenase)
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MEDFAVSFWIYIGVMSIFVGGAVKKFLAFNIGAMPSVVVWLGATLLVERLCALCMPAVLARLVLCVCCWLYFTWATPKPSLPVEDKAVFITGCDSGFGNATAKKLDAMGFEVFATVLNLEGEGAKHLRKVCSSRLTLLQVDITQPQQVQQALLDTKAKLGIRDLWGLVNNAGWCVNIGDAELSLMSNYRGCMEVNFFGTVTVTRTFLPLLRQSKGRIVTISSPSGEHPFPCLASYGASKAALNLFINTLRHELDPWGVKVSTILPSAYKTGQSSNAEYWEKQYKSLLQGLSPNLLEEYGEEYLLETKELFQNYAKTANEDLSPVIDTIVEALLSPQPQVRYYAGPGLILMYFICSYLPLSISDRFLQKLFVQKKVMPRALIKQQGLSPNDNNNSIKENMNDSSSNNSNFTKCID
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Catalyzes the conversion of biologically active 11beta-hydroxyglucocorticoids (11beta-hydroxysteroid) such as cortisol, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as cortisone, in the presence of NAD(+). Cortisol is the primary glucocorticoid in teleosts and is released to increase glucose bioavailability in order to meet the increased energy demands in response to stress. Functions as a dehydrogenase (oxidase), thereby decreasing the concentration of active glucocorticoids, regulating the hypothalamus-pituitary-interrenal (HPI) axis function in adult fish. Decreasing the excess glucocorticoids may be of relevance to brain function and neural proliferation. Plays a key role by catalyzing the oxidation of 11beta-hydroxytestosterone (11beta,17beta-dihydroxyandrost-4-ene-3-one) to 11-ketotestosterone (17beta-hydroxyandrost-4-ene-3,11-dione), the major fish androgen, that activates androgen receptor transcriptional activity. Catalyzes the conversion of 11beta-hydroxyandrostenedione (11beta-hydroxyandrost-4-ene-3,17-dione) to 11-ketoandrostenedione (androst-4-ene-3,11,17-trione), which can be further metabolized to 11-ketotestosterone. Exerts a dual role in fish by inactivating glucocorticoids and activating androgens.
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F1QLR3
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FXR1_DANRE
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RNA-binding protein FXR1 (FMR1 autosomal homolog 1)
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MEELTVEVRGSNGAYYKGFVRDVHDDSLSISFENNWQPERQVPFSDVRLPPSADTKKEIGEGEEVEIFSRANEQEPCGWWLAKVRMMKGDFYVIEYAACDATYNEIVTFERLRPVNRNKAVTESTFFRCSVPVPEDLRAACESEQAHKEFKKAVGAIRIVYSPEKSELVVLSLSEATVKRVSLLSDIHLRSIRTKLMLMSRNQEATKHLESTKQLASAFQEEFTVREDLMGLAIGSHGSNIQQARKVPGVTAIELEEETGTFRIYGESTEAVQKARNYLEFLEDSVQIPRNLVGKVIGKNGKVIQEIVDKSGVVRVRIEGDNDNKLPRQEGMVPFTFVGTKESISNVQVLLEYHIAYLNEVEQLRLERLQIDEQLRQIGMGFRSVPNRPADKEKGFGPDESSSGSIHTQRSYRGRGRRGPAHTSAYGTNSEHSYTSETDSERKAELSDWSLAADESERNPRPQRDSRRRDLRGRGRGSRGRGASNSISSVLKDPDGNPYSLLDNTETDQTADTDGSESQMNTSRRRRSRRRRTDEDTTVMDGMSESDNASLSENGLVTVADYISRAESQSRQTNPRDTRKSKKDMTRGDFISEHSAAESVSNGPNNADEPSESAKAVVNGVS
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mRNA-binding protein that acts as a regulator of mRNAs translation and/or stability, and which is required for various processes, such as heart and muscle development. Specifically binds to AU-rich elements (AREs) in the 3'-UTR of target mRNAs (By similarity). Promotes formation of some phase-separated membraneless compartment by undergoing liquid-liquid phase separation upon binding to AREs-containing mRNAs: mRNAs storage into membraneless compartments regulates their translation and/or stability (By similarity).
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F1QLY4
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RORAA_DANRE
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Nuclear receptor ROR-alpha A (Retinoid-related orphan receptor alpha 2) (Retinoid-related orphan receptor-alpha A)
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MMYFVISAMKAQIEIIPCKICGDKSSGIHYGVITCEGCKGFFRRSQQSNAAYSCPRQKNCLIDRTSRNRCQHCRLQKCLAVGMSRDAVKFGRMSKKQRDSLYAEVQKHRLQQQQRDHQQQPGEAEPLTPTYGLSTNGLTELHDDLSGYMNGHTPDGTKPDSGVSSFYLDIQPSPDQSGLDINGIKPEPICDFTPGSGFFPYCSFTNGETSPTVSMAELEHLAQNISKSHMETCQYLREELQQMTWQAFLQEEVENYQSKPREVMWQLCAIKITEAIQYVVEFAKRIDGFMELCQNDQIVLLKAGSLEVVFVRMCRAFDPQNNTVYFDGKYAGPDVFKSLGCDDLISSVFEFGKNLCSMHLSEDEIALFSAFVLMSADRSWLQEKVKVEKLQQKIQLALQHVLQKNHREDGILTKLICKVSTLRALCSRHTEKLTAFKAIYPDIVRAHFPPLYKELFGSDFEQSMPVDG
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Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) (By similarity). Required for proper cerebellum development.
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F1QN48
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FA53B_DANRE
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Protein FAM53B (Protein simplet)
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MCVAMVIIHTKTLEKKAVDDVTSEASLQPQEPLTMSQGTALFSCGIMDSGRWADVGSVCGVQQRPVGSSLESLWDSMREAGATGGISGLLRDLSLSEASPASAAPPSKRQCRSLSCSDELGCRSSWRPQGSRVWTTVEKRRCHSGGSVQRGVFNPSGFPAMQRSSSFSLPAHSSHLEPFTHGFPFQAFSECPQTPQTLYRSHEQICPAEASSPESTPELQRRSGQSGLARSRSQPCVHNHQKIGVKRRRPADSHKQRPSLDLLKMTQKLQDFHSLSCPGFSGDDKTLPSSSPALLNDTCERAQNDSSADAPIHQSESSSEDALIHQSDSSSADALIHQSESSRPAGKERECLWAGLCSRRGRDLFQLGGELDIEQIERN
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Acts as a regulator of Wnt signaling pathway by regulating beta-catenin (ctnnb1) nuclear localization. Required for appendage regeneration by regulating cell proliferation.
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F1QN54
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KIF3B_DANRE
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Kinesin-like protein KIF3B
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MSKSKSSESVKVVVRCRPMNEKERVANFNRVVSVDVKLGQVAVCNPRGASSHEHPKVFTFDSVYDWNSKQMELYDETFRPLVDSVLFGFNGTIFAYGQTGTGKTYTMEGVRNDPERRGVIPNSFEHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKDQARRLELKERPDTGVYVKDLSSFVTKSVREIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSELGPDGENHIRVGKLNLVDLAGSERQTKTGAQGERLKEATKINLSLSALGNVISALVDGRSTHIPYRDSKLTRLLQDSLGGNARTVMVANIGPASYNVEETLTTLRYANRAKNIKNKPRVNEDPKDALLREFQEEIARLKEQLEKRSGRKRRRRRRRRVGEGGEEFEDGEDEEDDDDDDEDEEEGVDADKNIADYWHEQQEKLEKERRAIMEDHSLVAEEKQRLLKEKERKMTDLHKEKEASEMLTAKVKAMESKLLVGGKNIVDHTNEQQKVLELKRQEIAEQKRREREMKQEMECRDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQSVKSEIQDAQDEHVKYRQELEQTQNELTRELKLKHLIIENFIPMEEKNKIVTRATFDEEDDLWKMTPITRIQNSDHQMMKRPVSAVGYRRPLSQHARMAMLMRPDVRYKAENILLLELDLPSRTTKDYEGPVIAPKVAAALEDALREEDEIQVDASGFHASLGSSPGLSASAAGFSKKPKSGRPKTGKKVSTPTSAHSPLSGSGSPLYPQSRGLVPK
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Microtubule-based molecular motor that transport intracellular cargos, such as vesicles, organelles and protein complexes. Uses ATP hydrolysis to generate force to bind and move along the microtubule (By similarity). Plays a role in cilia formation. Required for photoreceptor development.
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F1QNW4
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DRC4_DANRE
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Dynein regulatory complex subunit 4 (Growth arrest-specific protein 8) (GAS-8)
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MPPKRKSSPKGKTPTVVDGLSTEEMSKEQLEEHIMRLREELDREREERNYFQLERDKIHTFWEITRRHLEENKCELRNRERELEEVEERHQVEIKVYKQKVKHLLYEQQNMLSELKAESIISTKLLQDEHADLEKEQWKDMRSLKLELKQQELSSENVLKRIHLKHDEETTDLRNDFARQVQEIGSKYEKRMQKLRQEEELRRKTEIHEIEERKNTHINMLMKNHEKAFRDIRNYFSDIVYKNLDLITSLKEELKEMKKNEEKRNKEMAEVLEQNKELKESSQKAKEQVAELQKQLANYEKDKSILTRSRARLKMSDREMKELKWELEVLEQRFSKVQLERDELYMKFTKAILEVQQKSGFKNLLLECKLNTLNDTLEKKEAQLSEVLSASNLDPTTLSVVTHKLEEVLESKNHTIKDLQYEVARVCKAHNDLLKTSEAKLRAFGIPVEELCFEPLKSNGQSVGQGPAMFVSSSN
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Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays an important role in the assembly of the N-DRC linker (By similarity). Plays dual roles at both the primary (or non-motile) cilia to regulate hedgehog signaling and in motile cilia to coordinate cilia movement. Required for proper slow muscle development and positively regulates ciliary smoothened (SMO)-dependent Hedgehog (Hh) signaling pathway. Required for tether cilia motility which is essential for normal otolith formation and localization in the developing inner ear.
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F1QQA8
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ZN219_DANRE
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Zinc finger protein 219 (Zinc finger protein 219-like)
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MDSPPECMLALSCEPPLSPPSMPSLDHSPQFLPQSPQSTPSSPQTELYAPVSPCPLPEASLQDEEEEDEELSTPPSPTPAVALFPGELELGSPSSESSPPATPLAPFPSFGALEKAISSGQSTTCNDELDLQLFNNESIAVTGGTSSGPGLRFPCHVCGKRFRFQSILSLHARAHSLDRERRASAPYRTTHSKLQQNHESNSMIQNPLSGSFQKSMNEDMVPEEPLQTASSPQFLFEGTTALTPPLTEEAPISTSFSPLGHAQLEDNTPSPAAPAFRCHACKGKFRTASELARHVRILHNPYKCTMCPFSASQEERLAAHLQESHPPEDPPAEAVFPSGAIKAPPETPVPQMSVIPAFRCETCGQRFTQSWFLKGHMRKHKDSLDHKCQVCGRGFKEPWFLKNHMKVHLNKLGLKAGLGNLGPPGADQSKGPASSQVLGALYSNLLLARSMAGGGGSGSRTERSDASAGSSKSSILGYLGLPKDSSNGSCMERLQAVAQVAEMGNGGGRGGDSADGADQAAMWQLVARSLVAAQHNQQQQQQQRSHSLHQHPSSRATVAGEAKNMRAYLGGLGSREELDGSSAPWECPDCGKLFRSLQQVVAHAHVHVQKTQKGQSARGGMSREEDIINRVSGTQATGGAGQRTGENESRQEGKQLPSGVGASGSFHSVISHLSGQNGLRGSSPSSSSPRERVRGTGMKDCPYCGKAFRSSHHLKVHLRVHTGERPYKCPHCDYAGTQSGSLKYHLQRHHREQRNAMATSPNSPSPSLPSLTGSPREGAKKRRLPSMSQQSSFGRVPGEAPSSRHTQSWTIGLSEKKEGSSASAHHREGDLESQYRGLSGMMGALLPSGLEQSWIGEVTLPKVPKVSRRKPQITSRMVSANGFQDKMTSQEGGFEPLDLSRRPLQDEGGVSQSGSGPSSGSKGGNDILNQCVFCPFRTSSVELMAMHLQVNHTSKSRRKRGAPISSNNHSQKLARPDRDPLALWKFLGVEDGVASPEDWVSARAENGVSPENRETEDNLELASGAMGSFRSRKKKPQMSEHVDEEDEEIDEEENDLEANGSFANVPQNQSRRAQSVSSDLPDDDLPKEEEGVLGE
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Transcriptional regulator. Recognizes and binds to the core DNA sequence motif 5'-GGGGG-3'. Binds to the col2a1a promoter and activates col2a1a expression. Binds to the sncgb promoter and activates sncgb expression, as part of a complex with sox9a.
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F1QQC3
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LOL2A_DANRE
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Lysyl oxidase homolog 2A (EC 1.4.3.13) (Lysyl oxidase-like protein 2A)
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MAVSSALCIFSLLVLAQAQSELQQPKIELRLAGDKRKHYEGRLEVFYNNEWGTVCDDDFSIEAAHVACRQLGFLGAVAWSPSAKFGQGEGRIWLDNVHCTGRENSLAACPSNGFGVSDCRHSEDVGVICNQKRIPGHRFINIMNNNVETLEERVEEIRIRPISSHLKRIPITEGYVEVKERGKWRQICDEEWTPLNSRVACGMYGFPGEKNYNNKVYRSLSMRKKKNYWGFSVNCTGNEAHVSSCRLGKALEPKRNGTCGRGLPVVVSCVPGRAFAPSSSIGFRKAYRPEQPLVRLRGGANVGEGRVEVLKNGVWGTVCDDNWNLKAATVVCRELGFGSAKEALTGAKLGQGMGPVHMNEVECSGFEKSLTDCYFNNDALGCSHEEDAAVRCNVPAMGFQKRIRLSGGRNPFEGRVEVLAEKNGSLVWGTVCSENWGIIEAMVVCRQLGLGFASHAFQETWYWAGDANADNVVMSGVRCSGTEMSLPQCLHHGKHINCPKGGGRFAAGVSCSDTAPDLVLNAQLVEQTTYLEDRPMYALQCALEENCLSSTARKNDHSSYRRLLRFSSQIHNVGQSDFRPKLGYHAWTWHECHRHYHSMEVFTHYDLLSLNGTKVAEGHKASFCLEDTHCDEGISKRYHCANFGEQGITVGCWDTYRHDIDCQWIDVTDVKPGDYIFQVVINPNYDVAESDYTNNVMKCKCRYDGYRIWTYSCHIGGSRSSDMDEYSGMSNQLNHLR
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Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (By similarity). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation (By similarity). Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2) (By similarity). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription (By similarity). LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency (By similarity). Involved in epithelial to mesenchymal transition (EMT) and participates in repression of E-cadherin, probably by mediating deamination of histone H3 (By similarity). When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (By similarity). Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation (By similarity). Required with loxl2b for correct expression of Sox2 and for neural differentiation.
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F1QQI2
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SPXN1_DANRE
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Spexin prohormone 1 (Neuropeptide Q) (Spexin hormone) [Cleaved into: Spexin-1 (Spexin-14)]
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MKDLRTLAAYALALLLLATFVSHSWSAPKGSFQRRNWTPQAMLYLKGTQGRRFVSEDRNEGDLYDTIRLESRSQNTENLSISKAAAFLLNILQQARDEDEPY
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Plays a role in the regulation of food intake and energy metabolism. May also be involved in suppressing the anxiety response by promoting the expression of serotonin-related genes such as fev, tph2 and slc6a4a. [Spexin-1]: Acts as a ligand for galanin receptors galr2a and galr2b. Brain administration of the peptide inhibits food consumption and elevates levels of glucose, triacylglycerol and cholesterol in the serum. Likely to control food intake by regulating appetite related genes which includes the negative regulation of the orexigenic factor agrp. By controlling food intake it may act as a satiety factor in energy metabolism.
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F1QR43
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GLCEB_DANRE
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D-glucuronyl C5-epimerase B (EC 5.1.3.17)
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MMRCLAARVHYKTLIVICALLSLLTVLLWNKCTSEKALRFLPRHPQPPPSPKIDSHPQQPQPPEPPPVVGGVRYEEIDCLINDDATIKGRREGSEVYMPFSWMEKYFEVYGKVVQYDGYDRFEFSHSYSKVYAQREQYHPNGVFMSFEGYNVEVRDRVKCISGVEGVPLSTQWGPQGYFYAIQIAQYGLSHYSKNLTERPPHVEVYDTAEERDSRSSAWTVPKGCSLTRVYDKTRATSVRQFSAPENSEGVSLPLGNTKDFIISFDLKFTSNGSVSVILETTEKGPPFVIHYVTTTQLILLKDRDITYGIGPRTTWTTVTRDLLTDLRKGIGLSNTKAVKATKTMPRRVVKLVVHGTGTIDNITISTTSHMAAFYAASDWLVRNQDERGGWPIMVTRKLGEGFRALEPGWYSAMAQGQAMSTLVRAYLMTKDDTYLKAALRATGPFKLPSEQHGVKAVFMNKYDWYEEYPTIPSSFVLNGFIYSLIGLFDLAQTAGEKLGRDAGQLYSKGMESLKVMLPLYDTGSGTIYDLRHFILGTAPNLARWDYHTTHINQLQLLGTIDNSPIFRDSVKRWKSYLKGGRAKHN
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Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains. Plays a role in dorso-ventral axis specification during early development, together with glcea, where it may potentiate signaling via the BMP pathway.
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F1QSQ0
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DSC2L_DANRE
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Desmocollin 2-like protein
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MRTPPRPEGLYPSPTVRYTQFMVETGHIQLLQITYPHTHSRFRMYERAHFAACLLALVLFQRAESCDPRPVLVQVPNTVPAGYFITQVTLNGCTAIPVSFTSSDPDFTVNTDGSIVTLRSLVISTKRFSVLVQDNSGLDWRVEIILSCKNEDSQKSGSVAQKRAKRRWRPLPFSVVENASPPFPKDVEMIASDSSVNYTVHYVISGQGVTEEPIGLFQLDQKTGMVRVTGPVDREKNPEFNFIARAFDQNNREVDQFLPITVMVEDVNDNAPEFTGNRFFTVEERCRAGTRVGQVNATDRDQPKTPHSLIKYILLNATDMFSIDQSTGIITAKSNTLDREAQDKVFVGVEIRDMGGAPNGLFNRGTAVISLTDVNDNPPTFKEKLYKGTIKENLANVLVTRIPVEDKDLVNTPNWKAVYEVTKGNENGNFRMETDPKTNEGLLYVVKGLDFEKTPVMNLEVTARNEAPLVGTDAKWQSVPLQLNVEDVDEGPEFNPNIMYLKVKENLPNGTVIGTYKALDPETKNSNGIKYYKLTDPGNWITVVESTGELKVANTIDRESSLVHNDTYNITIKAVDESKKTGNGVVILQIEDVNDNIPVIQRPDLNMCNRGDAVSSVLVEAVDQDKPPYSTPFIFELGAEQEGKWKLKDITDSSVVLQQVEPMPNGMYTVPITVKDLQGTGKEQIVNVRVCSCQREDSGVGICGARSASVSLGNYGILALVLSGLLLLLLCLFLIFFCTTKRDKLQITDDTGTGGILLKSNTEAPGEEVKDGTLLLIPTADVVDGSFQSAVTESKNVNTAPGRYGQQFFQSGGVYNTTTQEFGTDQYYTSGRYDNKIYGNGTLQKFSNTGTLDTWRTNGCYLDRKLAYFGEQEDGRYADDLLKNYGNEGVGSSAGSVGCCSILGEQESMEFLNTLGPKFRPLADICYTTNKTGK
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Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. Involved in the formation and structural organization of desmosome cell-cell junctions during embryonic development. Required for embryogenesis, specifically for progression of epiboly and normal convergence-extension movements during gastrulation. Required for the development of desmosomal-rich midlines in the heart. Plays an important role in ventricular contraction and resulting heart stroke volume.
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F1QU13
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ALPK2_DANRE
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Alpha-protein kinase 2 (EC 2.7.11.1) (Heart alpha-protein kinase)
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MTAKRVDMAAPDNLLFLDSDAVNSSPASVPIEQNEPTHVLDNQTDDSLRSMPDPHTNTALESTGLMPVPCQDETLETHSQHNEGENESSLVSTQHMDHTRLTEMTINDEKSNNWDFDISGVKENDNSTNLNPDLIHHAGTDSVMERNLNDKQTDLNHKDETFGSLMSSEVLLLKENRQQEMSQDTNLHQCSSSESTGIEYSQTANDAISDAMNSEQSPDQPFSIASNDTDKTTSECSVQTCWDTVESAATSKTQPELHDDVKDVMCESFTTSQTLNIDYLSTDISVCLADLPETDSLNILTPASTLLGILGKNNNVLKTADVPINDSEMVQSINKDLASPNADISKTVFTQMDQNLLHVTDHNVKVLESNRADTVVDQYVFSENIGQEVSQASSHDEDLNSSVQSHDQQLSTANSEIEETSSEFHTQTCQDIHEGVIIAEEAMNGHNTLPEMHDIADVTTSQTPIMKDPMIDEPSYLPDLHKADTPNVITTASTLSDTLETDDSIFETADVSVSDCELIQTVTLKTVTTYETLLMMHDVGEDLTCCDFTTSAIEEPETSHPLSLDDLHESNTPNIPPHASALLDSLGMNKNFLETADVPVSDCEVIQTVTFETVTTYETFPVMHDIAEDLTCCDFTTSETPKIEEPETSHSLSLDDLNEANTPNILPHASALLESLGMNNNFLEAADMPVSDREIIHPVNKDLDSSSVEICTVVLTQTDPKEVQDSDLDEKETESNRIDDSIDGMIDTKFSLDVSKLQPVCSNDLSGTVIHSESLFSQSIPDTPQIGEKYKNDLLQVISPPTPVTNEDLGNCSEEIDDACLKFTGTERDVEGDSELWLEPSQFLAGEEDEGAIFDKWGRSCSSSPPTTHPDNTKASDYTWRENISIDHNAEDWELTFPPVERWSSSDSWASALSDWFQAVNTYPEDSFKSASTGSKLGMAIQDNILEQRTSSDNANNDEQTCLSLNLMQPDEPGQALERGLVKSDNTNGTVFKQGDKERLASCLDMDKDTTTMESQMSLLETSTPESHKADNNAVMETFNASLTHEFNAKLHGSLDISGKLLSAKREGNVLVEVTGGKVSQLGLVFEEERQSIFTSPSSSAYTRDKNLTGCVSNEERCHSSDVHLCICPSQSDSHVSSKAGHAEGNGSFLHSNIGNCTVKPYVEENIPQFIMPFAPICTGNTFLHRSFLKEDRSQADLDLPDKKIINKINLKSNKKSSSSDDSSEDNFHTCPDQSLSSSSGDSDDPSITDSGRKPAYSDTCDIGKELSKLLLLTGEHFMVSEDKRIAYVTLDLDESQHFGRFSLPNCEKQSKPDNMPHKTSKTSSDGKMRSKHKEKPDDKQQHGIQASKKQDPQPQSQVKNEGAGCEDCPVAVIETIVITEKIIPKTQGKKKKKHVQHGTPKPENDAPTDVRSESRQKNVNGKAENLELKVASNSLNKPVAQPSGKTDITKKDSAQKVMSVRPKVEPSMAKMDPAGVNATQKSSPIKLKADTFNTAKMENKTCTTDSLSTCLPSMLNDDIKRRRIADDLSRAVPIRTRPQLPAIFRQARKDGEDVTRRAYSEVVKQKNSTPKEVVVPRVVSEIQADPVPADPQNISLWCQFSPIPPEATIKWTKEAAVLSEINKVEKEDGRFTLTIIKACSKDLGFYKCSLIVANISVSTSEYHLTSEVLMELVIPSHDQPAEPRVMEGDEENIQCSPLLFKEDFLSDQYFGKNQPASILTEKVHFGEGMHRKAFRTTLTEGNLPRFRPGHPCVLKVHNSISYGTKNNEELVQKNYSLAVEECHVQNTAREYIKAYNSVAKSAESFGDLPEIIPIYLVHRPSNDIPYATLEEELLGDFVKYSVKDGKEINLMRRDSEAGQKCCAFQHWVYTQTEGNLLVTDMQGVGMKLTDVGIATCKKGYKGFRGNCATSFIDQFKALHQCNRYCELLGLVSLQPKPKRTVAPPKPKTQPVPKKKTFGPVLNAKS
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Protein kinase that recognizes phosphorylation sites in which the surrounding peptides have an alpha-helical conformation (By similarity). Regulates cardiac development and cardiomyocyte differentiation by negatively regulating Wnt/beta-catenin signaling.
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F1QVU0
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LTK_DANRE
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Tyrosine-protein kinase receptor (EC 2.7.10.1) (Anaplastic lymphoma kinase 1) (alk-1) (Protein moonstone) (mne) (Protein shady) (shd)
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MDYITRQTFVKLALFIFTVLRSSCALLEKAAEDPVHPNPLQSSPAEDSDVSFCDFESPCSWTLSSHSTGGDWFITSAQQHRSSRRDTQPIRDYSTGKSEGHFLLLKPSSSHLSAGRCSFHMTSPVVLSSGPFCHLQLARFQPEPHAGNISAFVKHTDSTDIKPIDLTIKEQESDSSQWEVLEAVIGQLNEPFQVTVQYSACSSHEVGFLAFDSLELKNCVMGDDYVDLGSDCEKYSSLQCHSGGCIEKQRVCDFHTDCPEGEDEGLICSTLPLGSYCSFELGSCGWLAADTQSSWRLVSGQQLIEDTHLLGTTLKNTQGHFLFLKVRGHGDEREALVQSPALPSTISNQDCQLQFSLYRYGDFNGTVLLSVVESGASAPALIWERSGHWKDAWQEITLPITEILNGFHLKVQAFWTSGSKADIALDDISLSAACFDTELNELLHEGLPHDLDFSPLPEPSASEASPITWWFTSCGASGPFGPTQAQCDSAYRNTNVSVVVGKEGPLRGVQMWKVPATNTYKISAYGAAGGKGAKNHNKRSHGVFISATFPLEKGDILYILIGHQGEDACPGRNPQTHKICLGESSVIEDGFDSDGSALKWAGGGGGGGGATYIYRMENGQPLPLLIAAGGGGKAYLEDPESSQDQSFREQYENDTTVSGVSGRSGAAGGGGGWSDVSSLSWAGKSLVEGGQGGSSCPEALSVLGWATFGGFGGGGGACSAGGGGGGYRGGDAPLLDDISADGQDGLSFVHPMGKIFLQPLAAMESHGEAEIVVYLNCSHCKTQSCKRDEDTKLILCLCDSDEVLAPDNVTCAGTKHSLCQFINKHLQHNSSPLVCPPLVVPMGSLADGPPSLVFIMAVIVSTVVTGVVLTCASLTLIYYRKKNHLHAVRIRLQSPEYKLSKIRSSTIMTDYNPNYGYFGKAASLSELKEVPRKNITLLRALGHGAFGEVYEGQVLGMNGENTAMQVAIKTLPEICSEQDEMDFLMEALIMSKFSHQNIVRCIGVSLQILPRFILLELMTGGDMKSFLRLNRPRTNHSSSLSMLELLHMARDIALGCRYLEENHFIHRDIAARNCLLTCPGPDRVAKIGDFGMARDIYRASYYRKGGRAMLPVKWMPPEAFLEGIFTCKTDTWSFGVLLWEIFSLGYMPYPCKTNQEVLEFVTGGGRMDPPKSCPGPVYRIMTQCWQHCPEHRPNFTTILERINYCTQDPDVINTPLPVECGPPVEEEGGTVIRPDGSGSMTPLLVARSLSQDASPRASITSVTPQALKPRLQLQRPVHLTQEVGTYRETLEPCWAEPVPASGVCPGPWLQVPEHRPCSRSSSSSGSQKLKNKTKNLWNPTYGSWVLESFGRGKSALCHTQSMPLSCNPTSVSAPSSTSEHTDPVVEVNANVSASPPPSAAPSQTTLTPTAAPSRKSPTGAAGVSLATVMDLAKLQSFPCGNVNYAYDEQSYETESLPVVVSKSLEPSTSSAATSSLVALSQPGSFTHKPLVKRHASYGHEDVRRYTQPEKPTRDRDSGFSLSEDLSVTPV
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Receptor tyrosine kinase required for the establishment and proliferation of iridophores and their progenitors from multipotent neural crest cells. Iridophores are the blue-tinted cells that reflect light to give fish their metallic shine and which, together with yellow xanthophore and black melanophores, generate the zebrafish's stripes. Following activation by alkal ligands (alkal1, alkal2a or alkal2b) at the cell surface, transduces an extracellular signal into an intracellular response. Ligand-binding to the extracellular domain induces tyrosine kinase activation, resulting in the activation of the mitogen-activated protein kinase (MAPK) pathway (By similarity). Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif (By similarity).
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F1QWA8
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SARM1_DANRE
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NAD(+) hydrolase SARM1 (NADase SARM1) (EC 3.2.2.6) (NADP(+) hydrolase SARM1) (EC 3.2.2.-) (Sterile alpha and TIR motif-containing protein 1)
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MFLSLVVYLSKICRYLSMFSSDRLTVPEYVSSRLHNRRTAPDPRAVSPGISTDVQAVLDGSLPALRSAIRTLRSSKDTGDLEETRRAIAETFQLVEEAWVLPTVGRRVAEEICNRIRLDGGLELLLQLMQTPAVEITYESAKLLEQILVSENRDYVARMGLGVILNLTREQEDAQLARSVSGILEHMFKHTEETSAQLITNGALDTILYWCRGTDPTVLRHCAVALSNCAMYGGHRCQRLMIEKQAAEWLFPLAFSKEDELIRFHACLAVAVLAANREMEKEVVKSGTLELVEPFIASLDPDEFARNMLDSADSMQGRTAADLQHLLPLLDGTRLEGKCIAAFYLCVETSIKSRQRNTKIFQEIGAVQSLKRIVMYSSNATVCSLAKRALKMMSEEVPRRILSSVPNWKSGEVQTWLQQIGFSAFSERFQELQVDGDLLLNITEQDLIQDLGMTSGLTRKRFLRDLRVLKTYANYSTCDPNNLADWLADADPRFRQYTYGLVQSGVDRNNIVHITDQQLLTDCHVENGIHRAKILSAARRPSKPCLTDSQPKGPDVFISYRRTTGSQLASLLKVHLQLRGFSVFIDVEKLEAGRFEEKLITSVQRARNFILVLSANALDKCMGDVAMKDWVHKEIVTALNGKKNIVPVTDNFVWPDPTSLPEDMSTILKFNGIKWSHEYQEATIEKILRFLEGCPSQEKPDGAKTDKKEPQKK
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NAD(+) hydrolase, which plays a key role in axonal degeneration following injury by regulating NAD(+) metabolism. Acts as a negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway by promoting Wallerian degeneration, an injury-induced form of programmed subcellular death which involves degeneration of an axon distal to the injury site (By similarity). Wallerian degeneration is triggerred by NAD(+) depletion: in response to injury, SARM1 is activated and catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR), cyclic ADPR (cADPR) and nicotinamide NAD(+) cleavage promoting cytoskeletal degradation and axon destruction. Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules (By similarity). Can activate neuronal cell death in response to stress (By similarity).
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F1QXD3
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ZH15B_DANRE
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Palmitoyltransferase ZDHHC15B (EC 2.3.1.225) (Acyltransferase ZDHHC15B) (EC 2.3.1.-) (Zinc finger DHHC domain-containing protein 15B)
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MALSRALRCCQRIFSWIPVIIISSVVLWSYYAYVFELCFVTLSNNLERVTYLLIFHVCFIMFCWTYWKAIFTPPSTPTKKFHLSYTDKERYEMEERPEVQKQILVDIAKKLPIFTRAQSGAIRFCDRCQVIKPDRCHHCSVCETCVLKMDHHCPWVNNCVGFSNYKFFLLFLSYSMIYCVFIASTVFQYFLKFWVGDLPNGPAKFHVLFLLFVALMFFVSLMFLFGYHCWLVAKNRSTLEAFSPPVFQNGPDRNGFNVGLSKNLRQVFGEHKKLWFIPVFTSQGDGHYFPLRTLRESENPLLANEEKWVEDGGSDEESADENGSSLLIRTES
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Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates. Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By similarity). May thereby regulate target proteins association and localization to membranes (By similarity). In the nervous system, probably catalyzes the palmitoylation of synaptic proteins and is involved in the differentiation of dopaminergic neurons and the development of the diencephalon.
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F1QZ88
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E2F8_DANRE
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Transcription factor E2F8 (E2F-8)
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MSSTLSEGQTLIKKSLSPSKATSTNNKGHVFVEPQTPLKNSNKASTSEAALPETLKIMGPLTTPTKVLDAPSSDPWTPTSNLKMLISAASPEIRNREKERAVDSSESENSQETEQGEEVEKLHISRKDKSLGLLCYKFLARYPNYPNPALNNGISLDDVAAELHVERRRIYDIMNVLESLNMVSRLAKNRYTWHGRVKLAQTLAVLKRAGKENRYEQLMQQIRQRSQEREEREFDLDGEEKENEEMSSFEVDGDSGLADLPGADSKAASANSRKDKSLRVMSQKFVMLFLVSSPPVVSLDVAAKILIGEDHVVDQDKNKFKTKIRRLYDIANVLSSLELIKKVHVTEDKGRKPAFKWTGPEDIPSPKDLEISTTSSAPKPLESRSSVENCAKNLFSSPGTKRGFTRHHSLVKLVKSIQDDRRKINSAPSSPIKMTGDSADSDFYTTKMAHLAAICKKHLDEQSADGRPNNAVTDSSQSSKQPESTSASNHGPPGMQIPVLPAGAISYLPTKCSPIIPLLIPQHQTGGPYAVYMHPTSLRPQPTSLAVRSMTFESPVGANAKTSPATLTSNNQTNQSSSYGKEQTSPVNLKRASGEKSSVGSPSKMQRTEPKSVSPKLCEILQARLKARRGALTSNRPSARALHLEFSKPSESQPTVQTGTASLEHSLETFLEKEEKSQTSDNEAGLTPVRQPHSQPQKLSAPFQDMVLPSGPIHTETLIPAGYLIPISQQSIVNFREPQCSNESSKASTPTYNIYHTPTAGSRPAFPQEVTPTRLPLHRIPPISPFPSHGHRLHSPSPAILNFTLQNLGLIPGSVTPNPHTPEQSSSLQSPHPGLPHQGMIFVKPMSPARALQQTSIHGQPVTLISIPQALVTTPKGGQAFQQSFFHTPVSFPTVNTTAPKKIYIPQRKLDVSPEEI
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Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as e2f1. Acts as a regulator of S-phase by recognizing and binding the E2-related site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes (By similarity). Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator and promoting expression of vegfa. {ECO:0000250, ECO:0000269|PubMed:22903062}.
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F1R237
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TDRD6_DANRE
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Tudor domain-containing 6
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MCSIPGLPSKGSNVPVLITRVNLNPSCVLVEFWGNFDEDRKFAYQQLKKEIQYPRECFSESDGNPGDLCLVQVYETWYRARIVSRDSDEYSVFLIDEGRTLRAAVNTLAWGKSDFFYLPPEVEFCILANALPLSPENNWSSMALEFMKTFCGRRVNATVQDVLVAHRTFLLDIPCLSRQMFEMGFAKKLYSDQFMEFVVRSLQASTGTSDLKRISSIRTKPVEIIEQKEKQQAYMFPELQTDTVETVVITEVTSPFRIFCQLKVFSQELKKLTEQITQYYEGRVGSYFARAENLGSPCASRGSDGKWYRSVLQQVMSANNVVEVLHVDYGKKQFVQVENVKPLASEFFRMPVVTYVCSLHGIVDKGVGWTASQIDYLKSLLLNRTVIAKFQYQSLSEGVHYVTLYGEENTNINKLFELKPKCSLDSDMTLADFAVQKSPSSQKSKISRTTESTHINETYSDLKVNKPVFFTETLTPNSTHMAVVQHVDSPGKFWIQTQRYADEFDLLMNGLGNLYSDPTSTESLIRKPVVGLICAAKAQDGVFYRAAVYKVIDKTAEVYFLDYGNTEVVDSFNLRQLPLRFQQLPAVAVKCSLHGVKPRLKLWEERATLFFSKLVRDRIIDLHVQDKQQDTHIVQLVDPSLDGEKDVSKLLCNAGFAVSEKSIVDYSATRSCGLKTTHASGVFLTGTQPQTPCSSSVVMDSASAFKEYLFPIGSSLEVTVSYIENPNDFWCQKARNAACLEVLMQDIQRFYSHSEFEPLLEAACVARHPETGIWYRALVIQKHQTPHVDVLFIDYGQTKKVAIEDLRKITPAFLKMKGQAFRCSLYNLIHPVLHSSSDWSTEATLEFQEFVDAAASMNVPLKCTIFAVMYDSQKVVFNVVDLETPFQSICNLLVQRRLADRAPSKRSPLPPFRLDTYYYSTHGVKTGCDEKVSITCVKGVNQFFCHLARNSDEVEKLAEKVNFLCHQLEATKCPQTFGTVCFAKYTDGLWYRGQIKSTKPSVVINFVDYGDTLEVDKSDLLPVPIEAGDIMSVPVQAIECGLSDMPEELPCEVDNWFRKFADSHCFTALIVAKEPAGKLILELYDGKTQVNALIKQKFHNEIHKNDASTFKIYGLKSRAAESVEASACKKESSTGPKRDAIDQVPKSRESHAIQRSNDVASKQPQSRWGFSTNGRPEPTRDSGTINNCQKQPELRTSQGNLRHPCTSSKPEVVKPKPQALLKESALPIKSIKPGLEAEVFISHCNSPCSFFVQFATDEDDIYSLVEKLNADQSRCRNIDSSDIHEGDLVCAMFPDDSSWYRAVVRKNTNEKIDVEFVDFGNTAVISSKNVCHLGQSFASFPRYSIHCSVHKLNVDSKDQELAPNFKQVLEQNIEKVICTFVKMSGTMWEVRLDVNGVVLGSVCKDHVKPEIAIPDLKDAASEIKVCTYYKNPDISIGQVITGYTSYIKGPQLFWCQYVAMDKLQEISDMLQNIGNASETTLREDCMPVGSACIALFTEDNLWYRAKVTSKDLDTLSITFVDYGNESKVKIGDVKALPPKLSDVPPHAFDCQLEGFDVSEGFWDETADDAFYELVHDKPLNITIEKMGNSEMPHIVKLDCDGVDINTTMKSHWKTRNPETPPAELFNGAEMASDDDYVASKVNIDSVVTFDTDTDPADNETCTSALEMELSEQENLLSSTGVENEAQIDPLKMATENVTLPITESTVLSETHKKLETITEDEPVLGFTGLSDTNQHAVSKETDVGLPQHSEGASSVTIDSFLMNNTDSQLCIVEEPEAPSYEIIQSNLGCLRRATEKKPVGSECVIWSQVRRSWCTARVLKVSEEATLVLLEKYDSEVVVDPINIFEIMPEKPLQIACIEAAIANDDATKETDATLENSASKLYQTEVSDANGIAVALESEDLNGKEETFIDQMAPNDELAGQPQEEESVSCSAFLEDSKAKHMLVEGAQVHDLVQGLCPDDVESKDPQDDLNTSFEEQNDGAKMSTAVDLLLDFLDTAPRDKVQDVSETDALLEEFNIHVTEDLIVLTSDDGAESDTASDGTLHGDAVAMEVGPDTEESSCFQERSNASDCTSAEDSQVTHLTLKVEDASDDVIFVGVLQESQAVVHEPESEKEKRD
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Tudor domain-containing protein involved in germ cell development, more specifically the formation of chromatoid body (during spermiogenesis), Balbiani body (during oogenesis), germ plasm (upon fertilization), and for proper miRNA expression and spliceosome maturation (By similarity). Required for Balbiani body and germ plasm formation and mobility through interaction with dimethylated arginines in the prion-like protein Bucky ball (buc). Coordinates transcript deposition into future primordial germ cells. Interacts with known germ plasm mRNAs such as vasa, dazl, nanos3 and hook2.
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F1R2J1
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PNX_DANRE
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Homeobox protein pnx (Posterior neuron-specific homeobox)
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MHEETSNSTLQGKTSFSIADILDPAKFNGTRETREISNNRESPKTTSPTQDPSAPNIANASAAKVKSKRIRTAFTLDQLRILERSFQSSHYLSVFERHCIASALGLSETQVKIWFQNRRTKWKKELDGHGGEEQSHCAPTALTQNPIMYALPGHHANHHVHYYPQQTHYLNTSFHPQTLMMY
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Transcriptional repressor. Activity as a repressor is enhanced by binding to the corepressor tle3a.
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F1R345
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DDX11_DANRE
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ATP-dependent DNA helicase DDX11 (EC 3.6.4.12) (DEAD/H-box protein 11)
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MESKSGRFPFPFQPYPIQESFMEALYTALDQRKVGIFESPTGTGKSLSLICGALTWLRDYEEQRKQEAARLLEGQKDSDVVKEKNSNSGPPEPDWVSEFVQKKAERDMVNKLKDEELKRKKREERLEMIRHNAQLRYAMKRKADEDDEAVKLLQLSREGAEPETHSPEEEGLIVAEYESDDEATPKSRLCDDDNDDDDDLEEEHVTKIYYCSRTHSQLAQFVHEVQKSPYGDAVRLVNLGSRQNLCINPEVVRLGNVQMMNERCLEMQKNKHEKRQKASDSESKRSRGLAKATCVFSRFENLMAMKDEVLVKVRDVEQLIQHGRETHTCPYYSTRMSIPAAQVVVLPYQSLLHASTRKASGIKLKDQIVIIDEAHNLMDTISAIHSAEISGGQLCRAHSQLSQYCERYRSRLKAKNLMYIKQILFVLEGLVRTLGGKVGQNPNTQSCQTGSELLTINDFLFKAQVDNINLFKVQKYFEKSMISRKLCGFAEKYEGSGINTHSSSKNKENRRTEGLGRFLQTLQSKPTDVSEQQMAVEDKPIMASPMMLAESFLFALTNANKDGRVVIQRQACVAQSSLKFLLLNAAVHFAQILQECRAVIIAGGTMQPVADFKEQLLFSAGVTEERILEFSCGHVIPPENILPIVLCAGPSGQQLEFTFQTRDSPQMMEETGRVLSNLCNIVPGGVVCFFPSYEYEKRILGHWESTGILQRLQSKKKIFQEPKKASQVEQVLSEYSKCIQRCSNIGGGQTGALLFSVVGGKMSEGINFSDDLGRCIVMVGMPYPNIKSPELQEKMAYLDKHMPHVAGKSPGKALVESLCMKAVNQSIGRAIRHRGDYACIVLCDHRYARTGTLQKLPEWIRSSTHTHATFGPAFASARRFFLEKRQKATL
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DNA-dependent ATPase and ATP-dependent DNA helicase that participates in various functions in genomic stability, including DNA replication, DNA repair and heterochromatin organization as well as in ribosomal RNA synthesis. Plays a role in DNA double-strand break (DSB) repair at the DNA replication fork during DNA replication recovery from DNA damage. Plays a role in the regulation of sister chromatid cohesion and mitotic chromosome segregation. Stimulates 5'-single-stranded DNA flap endonuclease activity of FEN1 in an ATP- and helicase-independent manner. Also plays a role in heterochromatin organization (By similarity). Involved in rRNA transcription activation through binding to active hypomethylated rDNA gene loci by recruiting UBTF and the RNA polymerase Pol I transcriptional machinery. Plays a role in embryonic development. Associates with chromatin at DNA replication fork regions. Binds to single- and double-stranded DNAs (By similarity).
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F1R4C4
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PIS4A_DANRE
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E3 SUMO-protein ligase PIAS4-A (EC 2.3.2.27) (Protein inhibitor of activated STAT protein 4)
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MAAELVEAMNMVKSFRVSDLQTLLASMGRSKSGLKQDLVGRALRLVQTEYSPELLKNVRQLYETRFPKASAWLAARRPETVAVNYPALNSSPRGTGQGTDYLNGIPKPAPPPAAEVKLVPLPFYHNLETLLPPTELVAQNSEKLQESQCVFDLTPNQVDQIRNSSELRPGMKSVQVVLRICYTDSIGVQEDQYPPNIAVKVNQSYCHVPGYYPSNKPGVEPRRPCRPVNITPWLHLSTVTNRVTITWGNFGKRYSVAVYLVRVFTSGELFNQLKHCSVENPDRCRERIQDKLRFDPESEIATTGLRVSLICPLVKMRLGVPCRVLTCAHLQCFDAVFFLQMNEKKPTWTCPVCDKPAPFELLTIDGLLSEILKETPEDVEEIEYLTDGSWRPIRDDKEKERERENSRTPDYPVVDICVPEANGHSPAHSGTNQTGKSGSGGASAGTGSTSGGSGGGTVVDLTLDDSSEEEGGGGAEDSEETDDSQDSPAPKRGRYDYDKDLVTAY
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Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase (By similarity). May play a role as a transcriptional coregulator in various cellular pathways (By similarity). Catalyzes conjugation of SUMO2 to KAT5 in response to DNA damage, facilitating repair of DNA double-strand breaks (DSBs) via homologous recombination (HR) (By similarity). Mediates sumoylation of PARP1 in response to PARP1 trapping to chromatin (By similarity). Negatively regulates induction of interferon phi 1 (ifnphi1) mediated by mavs and ticam1/trif. Also inhibits ifnphi1-mediated activation of the interferon-stimulated genes (ISGs) pkz and cd40, and to a lesser extent rsad2 and isg15. May inhibit ticam1/trif-mediated activation of NF-kappa-B.
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F1R4U0
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TXTPB_DANRE
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Tricarboxylate transport protein B, mitochondrial (Citrate transport protein B) (Solute carrier family 25 member 1b)
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MSGSPKFVSPFHRPHCLSAAAPAGQAKLTHPGKAILAGGIAGGIEICITFPTEYVKTQLQLDEKANPPRYKGIVDCVKQTVQGHGVKGLYRGLSSLLYGSIPKAAVRFGVFEFLSNQMRDESGKLDSTRGLICGLGAGVAEAVVVVCPMETVKVKFIHDQTSANPKYRGFFHGVREIVRTQGLKGTYQGLTATVLKQGSNQAIRFYVMTALRNWYKGDNPNKSINPVVTGLFGAVAGAASVFGNTPLDVIKTRMQGLEAHKYKSTVDCAIKIMKYEGPAAFYKGTVPRLGRVCMDVAIVFIIYEEVVKVLNKVWKTD
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Mitochondrial electroneutral antiporter that exports citrate from the mitochondria into the cytosol in exchange for malate. Also able to mediate the exchange of citrate for isocitrate, phosphoenolpyruvate, cis-aconitate and to a lesser extend cis-aconitate, maleate and succinate (By similarity). Required for proper neuromuscular junction formation.
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F1R520
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CSTN1_DANRE
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calsyntenin-1
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MRIRGVKPFASAVGLLLGLLYAVDAAKVNKHKPWIETTYHGIVTENDDKVLLDPPLIALDKDAPLRYAGEICGFRIHGQNVPFEAVVLDKSTGEGVIRAKDKLDCELQKEHTFTIQAYDCGEGPDGGNMKKSHKATVHIQVNDVNEYSPVFKEKSYKATVIEGKKYDSIMKVEAVDADCSFQFSQICSYEIVTPDVPFTIDKDGNIKNTEKLNYGKERMYKLTVTAYDCGKNRASEDVLVKINIKPTCKPSWQGFNKRIEYEPGTGSLALFPSMHLETCEEPITSIQASIMLETNHIGKGCDRDTYSEKSLHKLCGASSGTVELLPAPSNSANWTVGLPTDNGHDSDQVFEFNGTQAIKVPEGVVSTTLKEPFTISVWMRHGPGGREKETILCNSDKTEMNRHHYSLYVHNCRLVLLLRQEPTESESYKPAEFHWKLDQVCDKEWHHYVLNIEFPAVTLFVDGGTFEPFLVTEDYPLHTSKIETQLTIGACWQGGSARMTQFFRGNLAGLMIRSGKLENKKVIDCLYTCKEGLDVQLPEEVASAVKVEFNPNQSSLSLEGDDIESFEKVMQHISYLNSRQFPTPGIRHLRVSTTVKCFNEETCISVPDSEGYVMVLQPEEPKISLSGIDHFARGAAEFESVEGVTLFPELRIVSTITREVEVEAEAETEAEGEDDPTVQETVVSEEIMHNLDTCEVTVVGEDLNGDHESLEVDLAQIQQRALEMSSSNVGMVITGVNTMANYEQVLHLIRYRNWHTEALFDRKFKLVCSELNGRYISNEFKVEVNVIHTANPMDHANNAMVQPQFISQVQHASVDLSGHNLVNTHQASVVPSAATIVIVVCVSFLVFMIILGVFRIRAAHQRTMRDQENGKENEMDWDDSALTITVNPMETYEDQHSSEEEGDEEEEESEDGEEEDDITSAESDSSEDEAGEQEDQQGSSRQQQLEWDDSTLTY
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Postsynaptic adhesion molecule involved in vesicle trafficking required for branching of peripheral but not central axons of sensory neurons. Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with presynaptic neurexins (By similarity).
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F1R5H6
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BRD4_DANRE
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Bromodomain-containing protein 4
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MGDGLDAVQMSGSSSSQGQPSSQAPSSFNPNPPETSNPTRPKRQTNQLQYLLKVVLKSLWKHQFAWPFHAPVDAVKLNLPDYYKIIKNPMDMGTIKKRLESAFYTSAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKVFLTKISEMPQQEVEISTTAGKGRGRGRRDPDMNMKVGPVLEPLTASPQTRGLSNLTPGPQTRGPPQGPPTLPPQPIVQIQALPPRVPPSLPTIPLHAPQLGPPFSLGPTDCNPPAPIITAVPPPTQTALPPVHIQQSAAPPILQTPISIPNKRKSQKRKADTTTPTANDQLNESSPAESKSGKTLPRRDNTRPSKLPKKEAPDSQHHWTAAPGTPSPKQQEQLRYCSGIVKDMFAKKHAAYAWPFYKPVDVDTLGLHDYHDIIKHPMDLSTIKDKLETRQYREAQEFAADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPEEMLAPAPAPVLHPAPVKTQPVMATASSSDTSSDSSSESESSTDDSEEERAQRLAELQEQLKAVHEQLAALSQPQASKPKKKEKEKKEKKKDKHKKKAGVMPALEEILEPPPALKPQGKPKNKDPLPKKSKKLSKKEGGKSNRSMAPPGAAPPTLQPVPGLDTEEDLGLTGGAAMAGMAAGEKCKPMSYEEKRQLSLDINKLPGDKLGRVVHIIQSREPSLKNSNPDEIEIDFETLKPSTLRELERYVSSCLRKKKKPAVPEKSMEAISAVKTKGTSSDSGSSSESSSSESEDSETGMASKPKKRGRGEGKKAHHQTTAPGMPLPQVPLQPQTPALQPSIQLKQQQPQHPSPAAYMPPPVTALEPSQLLENPFDPLAHFMHLPHHANDSSSPAPPHLNAHPPGGPVSPETHPFLNQHPILPSPALHNALPQQPSRPSNRAAPLPPKPLQQSTSQQQPPPQQTLVPPQQLQPQQQQPAPPQQQHLPHHPLHAPQQMRPRPLSPPTLTPQGLLSSQPPQMLLEDDEEPVPSMSLPMYLQHLQPNRLQATPTSLMQSLQSRPQPPGQPSLLQSVQVQSHLPPPQLPVQTQVQPQQPAPHQPSPQLSQHQARHMQQLGFPQGPLQTAQTQPGQHKVSMPSTKAQQIIQQQQATQHHSPRQHKADSYNSAHLRDNPSPLMMHSPQIPQYSLVHQSPSQDKKEPQRGPSALGGIKEEKLPPSPVMRGEPFSPAMRPESHKHPDSKPTMPGHSQQRADMKPLEMSRPVIRSSEQSGPPPSMQDKEKFKQEPKTPSAPKKVQDVKFKNMGSWASLAQKSSTTPSSGLKSSSDSFEQFRRAAREKEEREKALKAQVEQAEKDRLRKEQEKLRGRDEEDSIEPPRRPLEEPRRRQEPQQVQPPPQQHQTQAQAQTLNPAQSPSASQPTQAPPQSPASSQSALDQQREMARRREQERRRREAMAATIDMNFQSDLMAIFEENLF
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Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters (By similarity).
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F1R777
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MTA70_DANRE
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N6-adenosine-methyltransferase subunit METTL3 (EC 2.1.1.348) (N6-adenosine-methyltransferase 70 kDa subunit) (MT-A70)
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MSDTWSHIQAHKKQLDSLRERLQRRRKDPTQLGTEVGSVESGSARSDSPGPAIQSPPQVEVEHPPDPELEKRLLGYLSELSLSLPTDSLTITNQLNTSESPVSHSCIQSLLLKFSAQELIEVRQPSITSSSSSTLVTSVDHTKLWAMIGSAGQSQRTAVKRKADDITHQKRALGSSPSIQAPPSPPRKSSVSLATASISQLTASSGGGGGGADKKGRSNKVQASHLDMEIESLLSQQSTKEQQSKKVSQEILELLNTSSAKEQSIVEKFRSRGRAQVQEFCDYGTKEECVQSGDTPQPCTKLHFRRIINKHTDESLGDCSFLNTCFHMDTCKYVHYEIDSPPEAEGDALGPQAGAAELGLHSTVGDSNVGKLFPSQWICCDIRYLDVSILGKFAVVMADPPWDIHMELPYGTLTDDEMRKLNIPILQDDGFLFLWVTGRAMELGRECLSLWGYDRVDEIIWVKTNQLQRIIRTGRTGHWLNHGKEHCLVGVKGNPQGFNRGLDCDVIVAEVRSTSHKPDEIYGMIERLSPGTRKIELFGRPHNVQPNWITLGNQLDGIHLLDPEVVARFKKRYPDGVISKPKNM
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The METTL3-METTL14 heterodimer forms a N6-methyltransferase complex that methylates adenosine residues at the N(6) position of some RNAs and regulates various processes such as the circadian clock, differentiation of embryonic and hematopoietic stem cells, cortical neurogenesis, response to DNA damage, differentiation of T-cells and primary miRNA processing. In the heterodimer formed with mettl14, mettl3 constitutes the catalytic core (By similarity). N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in mRNA stability, processing and translation efficiency (By similarity). M6A is also involved in hematopoietic stem cells specification: m6A methylation and subsequent destabilization of mRNAs, such as notch1a, leads to decreased Notch signaling, promoting endothelial to hematopoietic transition. M6A also takes place in other RNA molecules, such as primary miRNA (pri-miRNAs) (By similarity). Mediates methylation of pri-miRNAs (By similarity).
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F1RA39
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MCA2B_DANRE
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[F-actin]-monooxygenase mical2b (EC 1.14.13.225) (Molecule interacting with CasL protein 2B) (MICAL-2)
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MGETEEERTSQAGQLFENFIQATTCKGTLQAFSVLCRQLELNPSDHRGFYSSLKTAVTFWKAKGLWGKLDKRAGHKEYSKGRACADTRCLIIGGGPCGFRTAIELALLGAKVVVIEKRDTFSRNNVLHLWPYTIHDLRNLGAKKFYGKFCAGSIDHISIRQLQLMLLKIALIVGVEVHVNVEFVKLLEPPEDQSTDGQGWRAEIRPADNPVSDYEFDVIIGADGRRSTLDGFRRKEFRGKLAIAITANFVNRNTTAEAKVEEISGVAFIFNQKFFLELKEETGIDLENIVYYKDNTHYFVMTAKKQSLLDKGVIINDYIETERLLAFDNVNQEALLSYAREAADFGTNYQLPSLDYAINHYGQPDVAMFDFTCMYASENAALVREKSHRQLLVALVGDSLLEPFWPMGTGCARGFLAAFDTAWMIKGWAQGKEPLDLLSERESIYRLLPQTTAENISKNFEQYTIDPATRYPNLNSSCVRPHQVRHLFISGEQDLSSLERSGQTRRSVSISRRESEVRPGRLLLWCQNQTQDYRGVNVTDLNTSWRSGLALCALIHRQRPELIDFDSLNEADCAKNNQLAFDVAEREFGIQPVTTGKEMDAERGPDKLIMVLYLSKFYEMFHKSTQSVTGLPKEIDANNGDCSSKTANSLYNSINHARKRIPKLDKKLEESDVNRKRKKASSHHEELMSCQTAPPAGEREEQKENKVRSMATQLLARFEENAPSCALRRQSDSESDSDADRPVSLDLTENPRFARPKIEPTHPSTTPDKAKWQPSPYLRLLESNTRSETLHTEHYVESQSSHRLTEIQSECQYSSVSSAYKSSERRPRSPLIPFTPTLSPMMHCLQQLEEQVIQQRKREPLNRKSIKERAQKLSSLFTGNPAQPQTDESSPAVSPSSPPQTIPESSTLSCLLSPAPSLTHKQCSEASETHLKADKHTEIRRVERLDPSKQRTVGKVSSAIGVKAATLAILYETDHRPNNPITLSLTEARRCAESGLVSVRKEFSASLGGSDTCVFCQKRVYIMERLSAEGFFFHRECFRCHICGCSLRLGAHTFDSQQGTFYCKMHFSQRKTSTRHRRGEIQDGGIRSSSITISNHTSTDGTRGQPSGGEFDSSTQQDLQTLPDSKEIISVSEVKDSSKKADPADSAPACPDSPLQKVKRSTAKGEITNKNILWKKKIRSTLPLVLMKKFHRGKPEDKTEVLAEEDGNSDFEEIHESLSSKKPSNPSTDSNCLPTKDNSSTPLDEIPKIPLYRTHVLPEYPKPSSSSPEPIVTSISSDPISFSPKKKLTLSLSEKEKLLNWDLTNPGKSGAEEQQQQHVKPSISLQHDHPEPTHPQPEPAPPLFGFQQWANNLRKSFSKGSNPVVLRRNRPMKARPLSEGSFNVGAVFQDEERCGSLVDEGEARPRTESEIASLLEQVALGSKTSRGTKDDMASLPPRKLNFFSSLRIKRVEGAEQSRGEGQKDILSILSRFRNKASAQQQQQQKSNSSSEDEQEPKLTHSGALQKKKEKIAIRQTKSDELKRLHRAQVIQRQLEEVEEKQRSLEEKGVALEKVLRGENGDDGSTDEAALLQTWFKLVLEKNKLSRYESELMIFAQELELEDTQSRLQQDLRRRMATEDCEKSASELVEEQNILVEIMKVVEKRDKLVSLLEEQRLKEKAEDRDLESLILSRGYQFHWT
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Nuclear monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin and regulates the srf signaling. Acts by modifying nuclear actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization (By similarity). Acts as a key regulator of the srf signaling pathway elicited by nerve growth factor and serum: mediates oxidation and subsequent depolymerization of nuclear actin, leading to increase mkl1/mrtf-a presence in the nucleus and promote srf:mkl1/mrtf-a-dependent gene transcription.
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F1RAX4
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STRA6_DANRE
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Receptor for retinol uptake stra6 (Stimulated by retinoic acid gene 6 protein homolog)
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MSAETVNNYDYSDWYENAAPTKAPVEVIPPCDPTADEGLFHICIAAISLVVMLVLAILARRQKLSDNQRGLTGLLSPVNFLDHTQHKGLAVAVYGVLFCKLVGMVLSHHPLPFTKEVANKEFWMILALLYYPALYYPLLACGTLHNKVGYVLGSLLSWTHFGILVWQKVDCPKTPQIYKYYALFGSLPQIACLAFLSFQYPLLLFKGLQNTETANASEDLSSSYYRDYVKKILKKKKPTKISSSTSKPKLFDRLRDAVKSYIYTPEDVFRFPLKLAISVVVAFIALYQMALLLISGVLPTLHIVRRGVDENIAFLLAGFNIILSNDRQEVVRIVVYYLWCVEICYVSAVTLSCLVNLLMLMRSMVLHRSNLKGLYRGDSLNVFNCHRSIRPSRPALVCWMGFTSYQAAFLCLGMAIQTLVFFICILFAVFLIIIPILWGTNLMLFHIIGNLWPFWLTLVLAALIQHVASRFLFIRKDGGTRDLNNRGSLFLLSYILFLVNVMIGVVLGIWRVVITALFNIVHLGRLDISLLNRNVEAFDPGYRCYSHYLKIEVSQSHPVMKAFCGLLLQSSGQDGLSAQRIRDAEEGIQLVQQEKKQNKVSNAKRARAHWQLLYTLVNNPSLVGSRKHFQCQSSESFINGALSRTSKEGSKKDGSVNEPSKEAESAAASN
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Retinol transporter. Accepts retinol from the extracellular retinol-binding protein rbp4, mediates retinol transport across the cell membrane, and then transmits retinol to the cytoplasmic retinol-binding protein rbp1. Required for normal vitamin A homeostasis.
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F1RBC8
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ABCD1_DANRE
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ATP-binding cassette sub-family D member 1 (EC 3.1.2.-) (EC 7.6.2.-) (Adrenoleukodystrophy protein) (ALDP)
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MSVYSKLPSQLKKPLVKKAVVLLIALYGVKKLSPYFFGKLKGRTSKQVKGADPLTSNGEPLVEAARKRKRSPAVNREFFDRLIRLLKILFPRLFCKELGLLGFHSLALISRTFLSIYVANLDGQIVKTIVKKDPRAFVVELTKWLLIAIPATFVNSAIRYLEGQLTLAFRTRLVTHAYMLYFSDQTYYRVSNMDGRLANPDQSLTEDVVMFAASVAHLYSNLTKPILDVVVTCYTLIKTAESKGANTTWPSVIAGIVVALTAKVLRAFSPRFGKLVAEEARRKGDLRYMHSRIIANSEEIAFYGGHKIEMLQLQRSYNSLSRQINLILFKRLWYVMLEQFLMKYLWSASGLVMVAVPIITATGYSKYDSEDVKQAALDMKEEDLVSERTQAFTTARSLLNAAADAVERIMVSYKEVTELAGYTARVYEMFEVFEDVRDGVYRRSATEVKPEETGAPQNVTHGMRVEGPLQIRGQVIDVEQGIKCENLPIITPTGDVVVSSLNMQVDEGMHLLITGPNGCGKSSLFRILSGLWPVYSGVLYKPSPDHMFYIPQRPYMSVGTLRDQVIYPHSVQEMQEKGITDRQLEEILQTVSLRYILEREGGWDAVSDWKDVLSGGEKQRMGMARMFYHKPQYALLDECTSAVSIDVEGKIFEAAKDAGISLLSITHRPSLWKYHSHLLQFDGEGGWRFEKLDASTRISLQDEKIRLETQLSGIPKMQQRLTELCRILGEDSSLPTPGDEEEDEEEDEKQTERDVQSAGKEKDLME
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ATP-dependent transporter of the ATP-binding cassette (ABC) family involved in the transport of very long chain fatty acid (VLCFA)-CoA from the cytosol to the peroxisome lumen. Coupled to the ATP-dependent transporter activity has also a fatty acyl-CoA thioesterase activity (ACOT) and hydrolyzes VLCFA-CoA into VLCFA prior their ATP-dependent transport into peroxisomes, the ACOT activity is essential during this transport process. Thus, plays a role in regulation of VLCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation, mitochondrial function and microsomal fatty acid elongation (By similarity). Involved in oligodendrocyte patterning and myelination.
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F1RCP1
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BECN1_DANRE
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Beclin-1
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METLRFSSNTMQVSFVCQRCNQPLKLDTSFNVLDRMTIHELTAPLVMVTANKQQDSGESSSFPEETFLENKQDGVARKFIPPARMMSAESTNSFTLIGEASDGGTMENLSRRLKVTSNLFDIMSGQTDIDHPLCEECTDTLLDHLDTQLNITENECQNYKSCLELLSQLPEEEEASLLNALQQLKQEEESLIQELESIETKREAVAKELDEGRNHSQLMDTEELRYQKEYCEFKRQQLELDDDLKSVDNQMRYCQIQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALASKMGLCFQRYQLVPYGNHSYLESLSDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKDDTGFCLPYRMDVDKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNR
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Plays a central role in autophagy. Acts as core subunit of different PI3K complex forms that mediate formation of phosphatidylinositol 3-phosphate and are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis (By similarity). Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 (By similarity). Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms (By similarity). Involved in endocytosis including endosome formation in neuronal cells (By similarity).
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F1RCY6
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RENT1_DANRE
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Regulator of nonsense transcripts 1 (EC 3.6.4.-) (ATP-dependent helicase RENT1) (Nonsense mRNA reducing factor 1) (NORF1) (Up-frameshift suppressor 1 homolog)
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MSVEAYGPSSQTLTFLDTEEAELLGADTQGSEFEFTDFTLPSQTQTQGQTQSQLDNQVNGPDGVLPNGEDAVGKTSQLLAELNFEEDEEDTYYTKDLPVHACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAKADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLSWLVKIPSEQEQLRARQITAQQINKLEELWKENPTATLEDLEKPGVDEEPQHVLLRYEDAYQYQNIFGPLVKLEADYDKKLKESQTQDNITVRWDLGLNKKRIAYFTLPKTDSGDMRLMQGDEICLRYKGDMAPLWKGIGHVIKVPDNYGDEIAIELRSSAGAPVEVPHNFQVDFVWKSTSFDRMQSALKTFAVDETSVSGYIYHKLLGHEVEDVIIKCQLPKRFTAQGLPDLNHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSREAIDSPVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSSDEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQFRSILIDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGVTAADRLKKGFDFQWPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEKITTRLLKAGAKPDQIGIITPYEGQRSYLVQYMQFSGSLHTKLYQEVEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVGNPKALSKQPLWNHLLNYYKEQKVLVEGPLNNLRESLMQFSKPRKLVNTINPGARFMSTAMYDAREAMIPGSVYDRSSTGRPSNMYFQTHDQVGMIGTGPNPMGSLNIPIPFNLVMPPMPPPGYLGQVNGPAAGRGAPKGKTGGRGGRQRNRGTGNHGSGQPNMPNSQASQDLVSQPFSQGPLTQGYITMSQPSQMSQPGLSQPELSQDSYLGDEFKSQMDVALSQDSTYQGERAYQHGGVTGLSQY
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RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation its phosphorylation appears to be a key step in NMD. The formation of an upf1-upf2-upf3 surveillance complex is believed to activate NMD.
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F1RD40
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MYCB2_DANRE
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E3 ubiquitin-protein ligase MYCBP2 (EC 2.3.2.33) (Myc-binding protein 2) (Protein Esrom)
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MMCAAAAAGAGGSGILSSSSHSMGLGVRVIPGAGNDFAPIGSGMGSCPVVGARSDCRSRYQLLLSGRALAERYRRIYTTAINDKEQGLNLGRGKKALSKKKLKRRQKVKSKVKTRTKTDTLDGAFPVPDIKLHSNPSAFNVYCNVRHCVLDWQQKEAALALASRNSVQSGDSDSEEEEEYREPFVKLPKIIGIGLCGVFELIKETRFSHPSLCLRSLQALLDMLQGQQPESFQTEPPDVLESLFHLLLETTVRSTGMNDPTGQTLTALSCACLFSLVVAWGDTGKTLQAVSAILTNNGSHACQTIQVPTILNALQRSVQAVLVGKIQIQEWFGNGIKRAALMNKWVLKEVNIDDDEHCLLQTDGSFLYLLCKDGLYKVGSGYSGTVRGHVYNSTSRIRNRKEKRSWLGFAQGCLLYRDMNSHNMAAIKINPETLEQEGTITVPGLQADGQNIIFTDGEYINQIAACKDDGFVVRIYATSSDPALQQELQLKLARKCLHACGISLFDLEKDLHIISTGFDEEAALIGAGREFALMKTASGKIYYTGKYQSLGIKQGGPSSGKWVELPVTKSPKIVQFSVGHDGSHALLVAEDGSVFFTGSASKGEDGESTKSRRQPKPYKPKKMIKLETKMAVYTACNNGSSSIVTKDGELYMFGKDAIYSDSTCQVSDLKGHFVTQVAMGKAHTCVLTKSGEVWTFGVNNKGQCGRDTGAMSQAGKAFGVENMATAMDEDLEDELDEKEEKSMMCQPGMHKWKLDQCMVCTVCGDCTGYGASCVSSGRPDRVPGGICGCGSGESGCSSCGCCKACARELDGQEARQRGIFDAVKEMIPLDLLLGVNIEEHIQIRQEEKRQRINRRHRLEEGRGPLVFPGPLFMNQREQVLARLRPLQAVKLMREKLKDGSSERGDKDASKITTYPPGAVRFDCELRAVQVSCGFHHSVVLMENGDVYTFGYGQHGQLGHGDVNSRGSPTLVQALPGPSTQVTAGSNHTAVLLMDGQVFTFGSFSKGQLGRPILDMPYWNAKPSPMPNIGAKYGRKATWIGASGDQTFLRIDEALINSHVLATSEIFANKHIIGLVPTSISEPPPFKCLLINKLDGSCRTFNDSEQEDLQGFGLCLDPVYDVIWRFLPVTREMCCYNAVIADARVPTASDIQALCSILSPELALPSGSHASTTRSHGALHILGCLDTLAAMQELKMGVASAEEETQAVMKVYSKEDYSVVNRFESHGGGWGYSAHSVEAIRFCADADILLGGLGLFGGRGEYTAKIKLFELGPDGGDHETDGDLLAETDVLAYDCAAREKYAMMFDEPVLLQLGWWYVAWARVSGPSSDCGSHGQATITTDDGVVFQFKSSKKSNNGTDVNAGQIPQLLYRLPSNDGNASKGKQQTSEPVHILKRTFARTVSVDCFESLLSILHWSWTTLVLGVEELRGLKGFQFTATLLDLERLRFVGTCCLRLLRVYICDIFPISASTKAIVEESSKLAECVGKTRSLLKKILSEGMDNCLTKLDNDPQGYLSQPLTLLEAVLQECHNTFTACFHSFYPTPALQWACLCDLLNCLDQDIQEANFRTSSSRLLAAVMSALCNTSVKLTSILPIAYDGEVLLRSLVKQVSTENDSALAHRFPLLVAHMEKLSHTEENLMGMTTFREVLEKMLVIVVLPVRKSLRKEVELFSPHLVSNTCGLLASIVSELTASALGSEVDGLNSLHSVKATPNRFTKTSQGRSWNTGNGSPDAICFTVDKPGVVLVGFCVYGGGGIHEYELEVLADDAQTEHPGDSAHSHRWTSLELVKGTYCTDDSPSDIAEIRLDKAVPLKENVKYAVRLRNYGSRTANGDGGITTVQCSDGVAFTFSTCSLSSNGTNQTRGQIPQILYYRSEYDGDLQSQLLSKANEEDKNCSRALSVVSVVVRAAKDLLHRAFAVDVEDIPELLSSSSLFSMLLPLILAYIGPVAASVPKAAVEVFGLVQELLPAVSALNQKYAPPTFNPNQSTDSTTGNQPEQGLSACTTSNHYAVLESDHPYKQAGVTQYKVSFPDCVRWMTVEFDPQCGTAQPEDVLRLLIPSRSLHFSGLSSKALAHETINSWTELKKFSGSSGWPTAVLVLPGNEALFSLETASDYVKDEKASFYGFKCVAVGYEFNPGLDEGIIQLEKELAYLGSVCAAALMKKDLALPIGNELEEDLEILEEASLQVCKSHSGLLGKGLALSHSPTILEALEGNLPLHLQTNEHSFLEDFITCVQSSSGGRLARWLQPDSYADPQKTSLILNKDDIRCGWPTTVVVQTKDQYGDVVHVPNMKVEVKAVPVSQKKSIQQENMKKLQRLPGTSSNSATGTDLTFGGHPAPKLEATYEPMIIKEARYIAITMMKAYENYSFEELRFASPTPKRPSENMLIRANTDGTYSANWTPGAVGLYTIHVTIDGIEIDAGLEVEVKDPPKGMIPPGTQMVKPKAEPQPSKVRKFVAKDSAGLRVRSHPSLQSEQIGIVQVNGTITFIDEIHNDDGVWLRLNDETVKKYVPNMNGYTEAWCLSFNQHLGRSLLVPVDVINSEGTWVQLDKNSVVEFCESDEGEAWSLARDRGGNQYLRHVEEQAVLEHGAQTPPPSPFSVQAFNRGMASSGAQGFDYGISNNKGDRDNMASWSVSPGSKHRQESRSSKTDSHSNRSVDQVKSKNNESLSASEALILKSDTGKLRSDSHSRSHSPNHNTLQALKADGRTSGLRAESPNPGSRSSSPKQKTFTSGRSSPSSTSSPRSSSPHDKNLPAKVSPSKVHLDPPRERSKSDSYTLDPDTLRKKKVPLMEPLRGRSTSPKPKLPPKESKGGSSNAENRAPSPHVVQENLHSEVVEVCRSSALLSNDEGNDENSELHNAEEGSSKVHFSIGKAPVKEELESRSSPKVSRKTSSRHVRPKKDKSGPLFKGENVRPTEPAKQAMSPSVAECARAVFAAFLWHEGIVHDAMACSSFLKFNPELTKEHAPIRNSLSCQQGFDEKESKLKNRHSLEISSALNMFNISPHGPDISKMGSINKNKVLSMLKEPPLPEKCEDGKESVSYEMTSHSSMRSKSILPLTLQHLVAFWEDISMATIKAATQNMIFPSPGSSAILKKKENEKDSKKTKKEKKKKEKAEVRPRGNLFGEMAQLAMGGPEKDTICELCGESHPYPVTYHMRQAHPGCGRYAGGQGYNSIGHFCGGWAGNCGDGGIGGSTWYLVCDRCREKYLREKQTAAREKVKQSRKKPLQVKTPRALPTMEAHQVIRANALFLLSLSSAAEPSLLCHHPPKPFHSHLPSLKEGVSEELPNKMGCLYLQTLARQHTENFGVYQDDNLFQDEMRYLRSTSVPAPYISVTPDACPNVFEEPGSNMKSMPPSLETSPITDSDTAKRTVFQRSYSVVASEYDKQHSASPARVKAVPRRRVHSGDAEVGSSLLRHPSPELSRLISAHGSLSKGERNFQWPVLAFVIQHHDLEGLEVAMKHALRKSACRVFAMEAFNWLLCNVTQTTSLHDILWHFVASLTPSPFETEEEEDEENKGNKENLEQEKDLGVCEHPLSDIIIAGEAAHPLPHTFHCLLQTISDLMMSLPSGSSLQQMALRCWSLKFKQSDHQFLHQSNVFHHINNILSKSDDGDSEESFNISVQSGYEAISQELCVVTCLKDLTSVVDIKTSSRPAMIGSLTDGSTETFWESGDEDKNKTKSITISCVKGINASYVSVHVDNSRDIGNKVTSMIFLCGKAVEDLCRIKQIDLDSRHMGWVTSELPGGDHHVIKIELKGPENTLRVRQVKVLGWKEGESIKIAGQISASVAQQKNCEAETLRVFRLITSQVFGKLICGDAEPTPEQEEKNLLSSPEGEDKAPSDADLKEHMVGIIFSRSKLTNLQKQVCAHIVQAIRMEATRVREEWEHAISSKENANSQPSDDDASSDAYCFELLSMVLALSGSNVGRQYLAQQLTLLQDLFSLLHTASPRVQRQVTSLLRRVLPEVTPMRLASVIGVKALPPADISDIIHSTEKGDWTKLGILDMFLGCIAKALTVQLKAKGTTIVGTAGMAAGKGVTTVTLPMIFNSSYIRRGESHWWMKGSTPPQIAEIIIKLVKDMAAGHLSDAWSRVTKNAIAETIIALTKMEEEHRSPVRCIATTRLWLALASLCVLDQDHVDRLSSGRWMGKDGQQKQMPMCDNHDDGETAAIILCNACGNLCTDCDRFLHLHRRTRTHQRQVFKEEEEAIKVDLHEGCGRTKLFWLMALADSKTMKAMVEFREHTGKPASSSSDACRFCGTRHGTELSAVGSVCSDQDCQEYAKLACSKTHPCGHPCGGVKNEDLCLPCLHGCDKTATCLKQDADDMCMICFTEALSAAPAIQLDCSHVFHLQCTRRVLENRWLGPRITFGFMSCPICKNKINHLVLKDLLDPIKELYEDVRRKALMRLEYEGLHKSEAITMSGARFFNNPAGFAMNRYAYYVCFKCKKAYFGGEARCDAEAGQGDDYDPRELICGACSDVSRAQMCSKHGTDFLEYKCRYCCSVAVFFCFGTTHFCNACHDDFQRMTSVPKEELPHCPAGPKGKQLEGSECPLHVVHPPTGEEFALGCGVCRNAHTF
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Atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues (By similarity). Shows esterification activity towards both threonine and serine, with a preference for threonine, and acts via two essential catalytic cysteine residues that relay ubiquitin to its substrate via thioester intermediates (By similarity). Interacts with the E2 enzymes UBE2D1, UBE2D3, UBE2E1 and UBE2L3 (By similarity). Plays a key role in neural development, probably by mediating ubiquitination of threonine residues on target proteins (By similarity). Involved in different processes such as regulation of neurite outgrowth, synaptic growth, synaptogenesis and axon degeneration (By similarity). Required in the visual system for correct fasciculation, targeting and mapping of retinal axons. Acts as a regulator of pteridine synthesis. May play a role in the regulation of the circadian clock gene expression (By similarity).
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F1RD85
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LOX3A_DANRE
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Lysyl oxidase homolog 3A (EC 1.4.3.-) (EC 1.4.3.13) (Lysyl oxidase-like protein 3A)
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MLRSELRDMVVAMVLWGILLPFCLSQTTSPSQDGKIKFRLAGYPRKHNEGRIEVFYNREWGTICDDDFTLANAHVLCRQLGFVEALSWSHSAKYGPGSGKIWLDNVICGGSENSIEKCVSRGWGNSDCTHQEDAGVICKDERLPGFAESNIIEMQVDEKRMEKIRLRPLKGAHAGRLPVTEGVVEVKFKEGWGHICNTGWTIKNSRVVCGMMGFPSQRSVGKKPNSLKSAYRIHSVTCSGNEAHLSACTMEFSRANSSAPCPGGGAAVVSCVPGLQFTQGRVRKAKLNPVPQMRLKGGARAGEGRVEVLKGSEWGTVCDDHWNLQSASVVCRELGFGTAKEALTGARMGQGMGPIYMNEVQCGGDEKSLWDCPHQSITAEDCKHTEDASVICNIPYMGFEKLMRLTGGRTRLEGRVELLLPAGGGVRDWGLICGDGWTSREAMVVCRQLGLGHASSGLRETWYWDSSNVTEMVMSGVKCKGDEMTLTDCQHHSVVSCKRAGAQFSAGVICSDMASDLVLNAPLVEQTVYIEDRPLHLLYCAAEENCLAKSAAQASWPYGHRRLLRFSSEIHNIGKADFRPRLGRHSWVWHECHRHYHSMDIFTYYDLLSLNGTKVADGHKASFCLEDTECHEGVSKRYECANFGEQGITVGCWDLYRHDIDCQWIDITDVSPGNYILQVIINPNFEVAESDFTNNAMRCNCKYDGHRVWLHKCHLGDSFSEEAEKEFEHYPGQLNNKIS
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Protein-lysine 6-oxidase that mediates the oxidation of peptidyl lysine residues to allysine in target proteins. Catalyzes the post-translational oxidative deamination of peptidyl lysine residues in precursors of elastin and different types of collagens, a prerequisite in the formation of cross-links between collagens and elastin. Can mediate oxidation of lysine residues that are acetylated. Also able to catalyze deacetylation of lysine residues (By similarity).
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F1RDG9
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FYNB_DANRE
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Tyrosine-protein kinase fynb (EC 2.7.10.2) (Proto-oncogene c-Fynb)
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MGCVQCKDKEAAKLTDDRDTSLSQSGVGYRYGVDPTPQHYPAFSGTGTAVAAIPNYNNFHGAAVSQGMTVFGGISTSTHQGTLRTRGGTGVTLFVALYDYEARTEDDLSFRKGEKFQIINSTEGDWWDARSLTTGGTGYIPSNYVAPVDSIQAEDWYFGKLGRKDAERQLLSTGNPRGTFLIRESETTKGAFSLSIRDWDDVKGDHVKHYKIRKLDSGGYYITTRAQFETLQQLVQHYTERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLRHDKLVQLYAVVSEEPIYIVTEYMGKGSLLDFLKDGEGRALKLPNLVDMAAQVAGGMAYIERMNYIHRDLRSANILVGDSLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGKFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMQCPQDCPSSLHELMVQCWKKDAEERPTFEYLQAFLEDYFTATEPQYQPGDNL
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Tyrosine-protein kinase implicated in the control of cell growth. Plays a role in the regulation of intracellular calcium levels. Required in brain development and mature brain function with important roles in the regulation of axon growth, axon guidance, and neurite extension. Role in CNTN1-mediated signaling (By similarity).
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F1RE08
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PTGIS_DANRE
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Prostacyclin synthase (EC 5.3.99.4) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) (Prostaglandin I2 synthase) (PGIS)
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MMWTALLLVGLSILVIVLYGRRTRRRNEPPLDKGMIPWLGHALEFGKDAAKFLTRMKEKHGDIFTVRAAGLYITVLLDSNCYDAVLSDVASLDQTSYAQVLMKRIFNMILPSHNPESEKKRAEMHFQGASLTQLSNSMQNNLRLLMTPSEMGLKTSEWKKDGLFNLCYSLLFKTGYLTVFGAENNDSAALTQIYEEFRRFDKLLPKLARTTINKEEKQIASAAREKLWKWLTPSGLDRKPREQSWLGSYVKQLQDEGIDAEMQRRAMLLQLWVTQGNAGPAAFWVMGYLLTHPEALRAVREEIQGGKHLRLEERQKNTPVFDSVLWETLRLTAAALITRDVTQDKKIRLSNGQEYHLRRGDRLCVFPFISPQMDPQIHQQPEMFQFDRFLNADRTEKKDFFKNGARVKYPSVPWGTEDNLCPGRHFAVHAIKELVFTILTRFDVELCDKNATVPLVDPSRYGFGILQPAGDLEIRYRIRF
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Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2). Catalyzes the biosynthesis and metabolism of eicosanoids. Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2), a potent mediator of vasodilation and inhibitor of platelet aggregation. Additionally, displays dehydratase activity, toward hydroperoxyeicosatetraenoates (HPETEs), especially toward (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate (15(S)-HPETE) (By similarity).
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F1RE57
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DHC3A_DANRE
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Palmitoyltransferase ZDHHC3-A (EC 2.3.1.225) (Acyltransferase ZDHHC3A) (EC 2.3.1.-) (Zinc finger DHHC domain-containing protein 3)
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MRSPVPRFRDVERQASGLQPPQCLPSCHERQSSMWFIKDACGIVCAIITWFLVFFAEFVVLFVMLIPSKNLTYSLVNGTLFNSLAFLALASHFRAMCTDPGAVPKGNATKEYIESLQLKPGQVVYKCPKCCSIKPDRAHHCSVCKRCIRKMDHHCPWVNNCVGENNQKYFVLFTMYICLISLHSLVMVVFHFLNCFEDDWTKCSTFSPPATVILLILLCFEGLLFLIFTSVMFGTQVHSICTDETGIEKLKREDPTWEKTQCWEGMKSAFGGPLSVTWFSPFTDLSCQKDDSSPVPMFPQGEIIEEDVIEIPLEPH
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Golgi-localized palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and regulates their association with membranes (Probable). Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (Probable).
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F1RET2
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SMYD5_DANRE
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Histone-lysine N-trimethyltransferase SMYD5 (EC 2.1.1.372) (SET and MYND domain-containing protein 5) ([histone H4]-lysine20 N-trimethyltransferase SMYD5)
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MAAPVDDMFSRCVDSAKASNCVDVRFINNVKGKGLFAKKPFKKGDTIFIERPLVSSQFLWNALYKYRACEYCLRALETAEENARRLSGLPALILPHPELCKVRPDRHQACPQCQVMYCSSECRQAAMDQYHKILCLGPSNDDPDHPVNKLQDAWRSVHFPPETSSVMILAKMVATIKQTQDKERWQRLFTNFCSRTANEEEEIVHKLLGEKFQGQLGLLRNLFTTALYEDRLSQWFTPEGFRSLFSLVGTNGQGIGTSSLSQWVHACDALELPRQQREQLDAFIDQLYKDIDKETGDFLNCEGSGLFLLQSSCNHSCVPNAEASFPENNFLLHLTALGDIGPGEEICISYLDCCQRDRSRHSRHKILRENYLFICSCQKCLSQMDDADMTSEDEEEVEGEGETEGEDMEDEMTDV
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Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 to form trimethylated histone H4 lysine 20 (H4K20me3) which represents a specific tag for epigenetic transcriptional repression (By similarity). Plays a crucial role in hematopoiesis during embryogenesis by negatively regulating expression of genes related to both primitive and definitive hematopoiesis.
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F1REV3
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KRIT1_DANRE
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Krev interaction trapped protein 1 (Krev interaction trapped 1) (Cerebral cavernous malformations 1 protein homolog) (Santa)
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MGNQELEEVFVAVIRPKNTTSLNSKEYRAKSYEILLIEVPLEGKEKKRKKVLLGTKIHADSDRTKSILEFVDETTKPISNNQGIIGKRVVHMRKFLLDGDSGGKEASLFIVPINVKDNSKSVHHPGSPSFYCLQDIMRVCSETSAHFSSSTSKMLLALDKWLAEQHTVPHAIPALFRPAPVDRVKTNVSNPAYAVEKQTDGTLHMGYTALEIKSKLMSLEKADLCIQNPLYGSDLQYTNRVDKVIINPYFGLGAPDYSKIQIPKRDKWQHSMTSVTEDKERQWVDDFPLHRSACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGNCNPNLLNGQLSSPLHFAAIGGHAEIVQLLLQHPEIDRHIEDQQKRSPLQVCEENKQNNWEETVNLLQQASNKPYEKVRIYRMDGSYRSVELKHGNNTTVQQIMEGMRLSQETQQYFTIWICSENLSLQLKPYHKPLQHLRMWSEIVTDLTALDPQRESPQLFLRRDVRLPLEVEKKVEDPLSILILFDEARHCLLKGFLSTSDNKLITLASLLLQIIYGNYDSKKHKQGFLNEENLKSIVPISKVKSKAHHWTNRILHEYKSLSTSEGVSKEMHHLQRLFLQNCWDIPTYGAAFFTGQVFTKASSSTHKVIRVYVGVNTKGLHLMNMETKVLHLSLEYGTFMWQLGQADQYVQIHSLENKKNFVVHTKQAGLIVKLLMKLSGQIAPNDRAVSDKYAYG
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Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Plays a role in integrin signaling. Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS. Probable microtubule-associated protein that may bind to phosphatidylinositol 4,5-bisphosphate (PIP2)-containing membranes (By similarity). Required for correct endothelial cell polarity and cell junction stabilization in cardiovascular development. May play a role in the regulation of macroautophagy through the down-regulation of the mTOR pathway (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O00522, ECO:0000269|PubMed:21633110, ECO:0000269|PubMed:23007647}.
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F1RKQ4
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TKFC_PIG
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Triokinase/FMN cyclase (Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)) [Includes: ATP-dependent dihydroxyacetone kinase (DHA kinase) (EC 2.7.1.28) (EC 2.7.1.29) (Glycerone kinase) (Triokinase) (Triose kinase); FAD-AMP lyase (cyclizing) (EC 4.6.1.15) (FAD-AMP lyase (cyclic FMN forming)) (FMN cyclase)]
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MTSKKLVNSVAGCADDALAGLVACNPSLQLLQGHRVALRSDLDSLKGRVALLSGGGSGHEPAHAGFIGKGMLTGVIAGAVFTSPAVGSILAAIRAVAQAGTVGTLLIVKNYTGDRLNFGLAREQARAEGIPVEMVVVGDDSAFTVLKKAGRRGLCGTVLIHKVAGALAEAGVGLEEITNRVSVVAKAMGTLGVSLSSCSVPGSRPTFELSADEVELGLGIHGEAGVLRIKMATADEIVAHMLNHMTDSSNVSHVPVQSGSSVVLMVNNLGGLSYLELGIIADAAVRFLEGRGVKIARALVGTFMSALEMPGVSLTLLLVDEPLLKLIDAETTAAAWPNVAKVSVTGRKRSRAAPAEPPEAPDATAAGGATSKQMVRVLERVCTTLLGLEDQLNALDRAAGDGDCGTTHSRAARAIQGWLKESPPPASPAQLLSKLSLLLLEKMGGSSGALYGLFLTAAAQPLKAKTDLAAWSAAMDAGLEAMQKYGKAAPGDRTMLDSLWAAGQELQAWKSPGANLLPVLTKALLENAEAAAEATKNMEAGAGRASYISSARLDQPDPGAVAAAAILRAILEVLQSQGA
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Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. Represses IFIH1-mediated cellular antiviral response (By similarity).
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F1RQM2
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AGM1_PIG
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Phosphoacetylglucosamine mutase (PAGM) (PGlcNAc mutase) (EC 5.4.2.3) (Acetylglucosamine phosphomutase) (N-acetylglucosamine-phosphate mutase) (Phosphoglucomutase-3) (PGM 3)
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MDLDAITKHSASHAKPDGLILQYGTAGFRTKADRLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEDDNGVKLVDPLGEMLAPSWEEHATHLANAEEQDLARALVAISEEAAVNLHQDAFVVIGRDTRPSSEKLSESVIDGVTVLGGQFHDYGLLTTPQLHYMVCCRNTGGQYGEATIDGYYHKLSTAFVELSKQASCSGDDHRTLKVDCANGIGALKLKEMKHYLPQGLSVQLFNDGTKGKLNHFCGADFVKSHQKPPEGIEMKANERCCSFDGDADRIIYYYCDVDGHFHLIDGDKIATLISSFLKELLLEIGESLTVGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDLGVYFEANGHGTVLFSKAAEAKIRQLAKELEDKKGKAAKMLENVIDLFNQATGDAISDMLVIEAILALKGLTIQQWDALYTDLPNRQLKVKVADRQVISTTDAERQVVKPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQENADSLAYEVSLAVFQQAGGVGERPQPGF
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Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation.
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F1RRV3
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THYG_PIG
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Thyroglobulin
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MALALWVFALLGSACLVSANIFEYQVDAQPLRPCELQRERAFLKRADYVPQCAEDGSFQTVQCKKDGGSCWCVDADGREVPGSRQPGRPVACLSFCQLQKQQILLSSYINSTATSYLPQCQDSGAYAPVQCDVRREQCWCVDAEGMEVYGTRRLGRPARCPGSCEIRNRRLLHGVGDKSPPQCSADGTFLPVQCKFVNTTDMMFFDLVHSYNRFPDAFVTFSSFRSRFPEVSGYCHCADSQGRELAGTGLELLLDEIYDTVFAGLDLASSFTETTLYRILQRRFLAVQLVTSGRFRCPTKCEVERFAATSFGHPYVPSCGRDGEYQAGQCQQEGLCWCVDAQGQEIPGTRRPSEPLSCAEGQSCPSERRRALSRLHLGPSGYSGQRGSFLAAERGPVSQTVPSFAASCPLPLKELFVESGILQPVVQGQKKEVTAATESLLKEGLRGIFPSRELARLALQFTANPKRLQQNLFGGRFLANVGQFNLSGALGTRGTFNFSHFFQQLGLPGFQKRQALADPAKSLSVGLDSNPATEAPEALKMGVAMNKTVVGSFGFEVNLQENRNALTFLSSLLELPEFLLFLQHAISVPEDIARDLGDVMEMALSSQGCEQTPGSLFVPSCTAEGSYEDVQCFAGECWCVDARGRELAGSRARGGRPRCPTACEKQRERMQSLLGRQPAGSSVFVPSCTREGHFLPVQCFSSDCYCVDADGQPIPGTRTAPGEPKQCPTPCQLQAEQAFLGTVRGLISNPSEPPVLSSIYIPQCSASGQWRRVQCDGPPEQAFEWYERWGAQSRSGQELTPAELLMKIMSYREAASGSFRLFIQNLYEAGQQGIFPGLARYSSLQDVPLAVLEGNLTQATGNILLEPYLFWQILNGQLPRYPGPYSDFSAPLAHLDLRSCWCVDEAGRKLEGTQTEPSKVPACPGSCEEVKLRVLQFIKEAEEIVMVSNSSQFPLGESFLAAKGIRLTDEELALPPLSPSRETFLEKFLSGSDYAIRLAAQSTFSFYQRRRVALSDAPRTSGPLQPYPYVPQCDALGSWEPVQCHAATGHCWCVDGEGAYLPASLAARSPQVLQCPTPCETSRVRGLLSAWKQAGSQVRPSPKDLFIPACTETGEFARLQASEASTWCVDPASGEAMPPGTNSSAPCPGLCEVLQRGVPSRRASPGTTPACRAEDGGFAPVQCDPAQGSCWCVLGSGEEVPGTRVAGSQPACERPQLWQTIQTRGQFQLQLPPGKVCSADYAGLLPTFQVVILDELTARGFCRIQVTTARTPVSIPVCDDSTVRVGCLSLDRLGVNVTWTLRLEDAPPASLPDLRDIEEALAGKDLVGRFADLIQSGTFQLHLDSRTFPADPSIHFLQGNSLGTSPRTRFGCVEGSRQVPATSNTSQDPLGCVRCPEGSYFQEEQCIPCPAGFYQEQTGSLACAPCPAGTTTTSVGAFSQTHCVTACQRDEAGLQCDQDGQYRASQRDRASGKAFCVDSEGRRLPWSETQAPLVDAQCLMMRKFEKLPESKVIFTADVAVLGSIVPDSESSLMQCLADCARDEACSFLTVSLEGSEGSCDFYAWTSDNIACTSSGQEEDALGTSKATSLGSLTCQVKVRPGDGVAPAVYLKKGQEFATIGQKRFEQTGFQNALSGLYSPVVFSASGASLTEAHLFCLLACDRDSCCDGFILTQVQGGPIICGLLSSPDVLLCHVRDWRDPSEAQADATCPGVTYDQDSRQGTLRLGGQEFKSLTPREGARDTFTSFQQVYLWKDSDMGSRSESMGCRRDMQPRPESPEETDLTAELFSPVDLNQVIVSENRSLPSQQHRLFKHLFSLQQAHLWCLSRCVQEPSFCQLAEITDSSPLYLTCTLYPEAQVCDDVMEASPRGCRRILPRRPNALFQRRVVLQDRVKNFYTRLPFQKLTGLSIRHKVPMADKAISSGFFECERLCDVDPCCTGFGFLNVSQLKGGEVTCLTLNSLGLQTCSEENGGSWRLLACGSPDTEVRTYPFGWYQKPAVQNDAPSFCPSAALPPVPEKVALDSWQPLPPSSVVVDPSIRNFDVAHISTAAVGDFSAARERCLLECSRHQACLVTTLQTRPGAVRCMFYADTQSCTHSLQAQNCQLLLREEATHIYRKPDIPLPGLGSSAPTVTIATHGQLLGTSQAIQLGASWKQVDQFLGVPYAAPPLAESRFRAPEPLNWTGTWDATKPRASCWQPGIRPATAPGVSEDCLYLSVFVPQSLTPNSSVLVFFHNGAEGPLAMAVDGSFLAAVGNLIVVTASYRTGVFGFLSSGSSEVSGNWGLLDQVAALTWVQTHIGVFGGDPRRVALAADRGGADVAGIHLLTSRATNSRLFRRAVLMGGSVLSPAAVIRPDRAQQQAAALAKEVGCPPRPSQKWYPASAGACQPPNDAQMQLLAVSGPFHYWGPVVDGQLLREAPARALQRPPRAKLDLLIGSSQDDGLIDRAKAVKRFEESQGRTSSKTAFYQALQNSLGGEAGDPGVQAAATWYYSLEHDTDDYASFSRALEAATRDYFIICPVIDMASHWARTARGNVFMYHAPESYSHGSLELLADVRYAFGLPFYPAYEGQFTQEEKSLSLKIMQYFSNFVRSGNPNYPHEFSRKAPEFAAPWPDFVPGDGAESYKELSVLLPNRQGLKKADCSFWSKYILSLKASADEAEDGPLAESEEEDRPGLTEDLLGLPELASKSYSK
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Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3). The synthesis of T3 and T4 involves iodination of selected tyrosine residues of TG/thyroglobulin followed by their oxidative coupling. Following TG re-internalization and lysosomal-mediated proteolysis, T3 and T4 are released from the polypeptide backbone leading to their secretion into the bloodstream (By similarity). One dimer produces 7 thyroid hormone molecules (By similarity).
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F1RRW5
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ACE_PIG
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Angiotensin-converting enzyme (ACE) (EC 3.4.15.1) (Dipeptidyl carboxypeptidase I) (Kininase II) [Cleaved into: Angiotensin-converting enzyme, soluble form]
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MGAASGCRWPWPPLLPLLLMLLLPPPPLPVALALDSALQPGNFTADEAGAEDFAQSFNSSSEQVLFQSTAASWAHDTNITEENARRQEEAALISQEFSEVWGQKAKALYDPIWQNFTSRTLRRIIGVVRTLGSANLSPAKRQQYNSLLSNMTRIYSTAKVCFPNKTATCWSLDPELTNILATSRSYTLLLYAWEGWHNAAGIPLKPLYQDFTALSNEAYKQDGFSDTGAYWRSLYDSPTFTEDLERLYHQLEPLYLNLHAYVRRALHRQYGDRFINLRGPIPAHLLGNMWAQSWNNIYDMVVPFPGKPSLDVTSAMVQKGWNVTHMFRVAEEFFTSLGLLPMPPEFWAESMLEKPSDGREVVCHASAWDFYNRKDFRIKQCTQVTMDQLSTVHHEMGHVQYYLQYKDQHVSLRRGANPGFHEAIGDVLALSVSTPAHLHKIGLLDHVTSDWESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPLYNYDWWYLRTKYQGVCPPVVRNETHFDAGAKYHVPNVTPYIRYFVSFILQFQFHQALCKEAGHQGPLHQCDIYQSTRAGAKLRAVLQAGSSRPWQEVLKDMVGSGALDAQPLLDYFQPVTQWLEEQNQRSGDILGWPEYQWRPPMPDNYPEGIDLVSDEAEASKFVEEYDRRSQVVLNEYAEANWDYNTNITAEGSKRVLEKSTQMANHTVKYGIWARKFDVANIQNFTLKRMIKKIQDLERAALPFKELEEYNQILLDMETAYSVASVCHANSTCLQLEPDLTNLMATSRSYEELLWAWKGWRDKVGRAILPYFPKYVELTNKAARLNGYEDGGDAWRAAYEMPFLEQELEQLFQELQPLYLNLHAYVRRALHHHYGPEHINLEGPIPAHLLGNMWAQTWSNIYDLVVPFPSASKMDASEAMINQGWTPQRMFKEADNFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHASAWDFFNGKDFRIKQCTTVNMEDLVVAHHEMGHIQYFMQYKDLPVTFREGANPGFHEAIGDVLALSVSTPKHLRSINLLKSEDDGYEEDINFLMKMALDKVAFVPFSYLVDQWRWRVFDRSITKENYNQEWWSLRLKYQGLCPPVARSQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCQAAGHKGPLHKCDIYQSKEAGRRLADAMKLGLSKPWPEAMQLITGQPNVSASAMMTYFKPLLDWLVTENGRHGEKLGWPQYNWTPNSARLEGSFAGTGRVNFLGLNLEEQQARVGQWVLLFLGVTLLVATMGLTQRLFSIRHQILRRTHRGPQFGSEVELRHS
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Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity (By similarity). Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates (By similarity). Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin (By similarity). Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response. Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins (By similarity). Catalyzes degradation of different enkephalin neuropeptides (Met-enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met-enkephalin-Arg-Gly-Leu) (By similarity). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin (By similarity). Met-enkephalin-Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long-term synaptic potentiation of glutamate release (By similarity). Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) (By similarity). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1 (By similarity). Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation (By similarity). Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones (By similarity). Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region (By similarity). [Angiotensin-converting enzyme, soluble form]: Soluble form that is released in blood plasma and other body fluids following proteolytic cleavage in the juxtamembrane stalk region.
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F1RT67
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IMPA3_PIG
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Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase (Golgi-resident PAP phosphatase) (gPAPP) (EC 3.1.3.7) (3'(2'), 5'-bisphosphate nucleotidase 2) (Inositol monophosphatase domain-containing protein 1) (Myo-inositol monophosphatase A3) (Phosphoadenosine phosphate 3'-nucleotidase)
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MAPMGIRLSPLGVAVFCLLGLGVLYHLYSGFLAGRFSLFGMGGEPGGGAAGPGAAADGGTVDLREMLAVSVLAAVRGGDEVRRVRESNVLHEKSKGKTREGADDKMTSGDVLSNRKMFYLLKTAFPNVQINTEEHVDATDQEVILWDRKIPEDILKEIATPQEVPAESVTVWIDPLDATQEYTEDLRKYVTTMVCVAVNGKPVLGVIHKPFSEYTAWAMVDGGSNVKARTSYNEKTPRIVVSRSHSGMVKQVALQTFGNQTTIIPAGGAGYKVLALLDVPDKSQEKADLYIHVTYIKKWDICAGNAILKALGGHMTTLSGEEISYTGSDGIEGGLLASVRVDHQALVRKLPDLEKTGHK
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Exhibits 3'-nucleotidase activity toward adenosine 3',5'-bisphosphate (PAP), namely hydrolyzes adenosine 3',5'-bisphosphate into adenosine 5'-monophosphate (AMP) and a phosphate. May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',5'-bisphosphate produced by Golgi sulfotransferases during glycosaminoglycan sulfation. Has no activity toward 3'-phosphoadenosine 5'-phosphosulfate (PAPS) or inositol phosphate (IP) substrates including I(1)P, I(1,4)P2, I(1,3,4)P3, I(1,4,5)P3 and I(1,3,4,5)P4.
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F1RWC3
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CUBN_PIG
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Cubilin (Intrinsic factor-cobalamin receptor)
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MVNNMSLLFLWSLVIFLTFAESYGEAGGPELQRHKRNTELQQPRMAAERGNLVFFTGLAQNIEFRTGSQGKIKLNDEDVGECLRQIQKNKFDIMNLKRGIIGLPQNVSSQIHQLESKLVDLERRFQSLQLTVDGKVCSSNPCQNGATCLNLHDSFFCICPSQWKGPLCSDDVNECEIYSGTPLGCQNGATCINTPGSYSCLCSPETHGPQCASKYDDCEGGSEMRCVHGICEDLTRVQAGEPRFRCICHAGWTSPSNSTACTLDRDECSSWPAPCSALVPCFNTLGSFYCGACPTGWQGNGYICEDINECEINNGGCSVAPPVECVNTPGSYYCPSCPPGYQGDGRMCTLIDLCSVNNGGCHPHAACSLILGSLPLCTCLPGYTGNGYGLHGCVPLSNVCLTRPCLHGQCMETASGYVCNCDSGWAGMNCTENINECLSNPCLNGGTCVDGINAFSCECTRFWTGSLCHLPQQVCGGTMSDVSGSFSYMSPDVGYVHDVDCFWVLRTEEGKVLRITFTFFQLESVDNCPHEFLQIHDGDSPAAFPLGRFCGSSPPHELLSSDNALYFHFFSEHLRNERGFTIRWETRQPECGGVLTGTYGSLKSPGYPGKYPPGRDCVWKVIASPDLLITFTFGTLSLEHHDDCRKDYLEIRDGPLHQDPVLGKFCTSLSVPPLQTTGPFARIHFHSDNQINDQGFHITYLTTPSDLHCGGNFTDPEGLLSPDLSGPFTHSRQCIYVITQPLGEQIQVNFTHVELEGQSGCSQSYIEVRDDQTLLGKVCGNETPSHIKSITNSIWIRLKIDASVVRASFGAAYQVACGGELTGEGVIRSPFYPNVYPGERICRWTIHQPQSQVVLLNFTAFEMGSSAHCDTDYIEIGSSPVLGSPENKKYCGTDIPSFITSVYNSLHVVFVKSSSTENHGFMAKFSTEALACGEILTESSGIIQSPGHPNIYPHGVNCTWHILVQPGHLIHLEIRQFHLEFHYNCTRDYLEIYDTVSDTSLGRYCGKSIPPSLTSNTNSLKLIFVADADLAYEGFVINYEATDASAGNTTALLYRRIWIFTSPNFPSNYPNNMECIYRITVETSQQIALHFTDFSLEEPIGGACAADYVEITNGGYASSPPLGKYCGSNPPPRIISHSNKLWLKFKSDFFGSGPGFSAYWDGSLTGCGGNLTTPTGTFTSPNYPMPYYHSSECFWWLKSSHGSPFELEFNDFHLEYHPNCTLDYLDVYDGLSTSSHLLTRLCGNEKPPLIRSTGDSMSLKLRTDEGQQGGGFLVKYQQTCDNVVIVNRTYGILESIHYPKPYSVNQRCNWTIQATAGNTVNYTFLAFELESHANCSTDYLELYDGPQRMGRFCGAVIPPSGSTTGSRLQVLFHTDGVGQGERGFQMQWLVHGCGGELSGDTGTFSSPGYPVGYPANKECIWYIHSSPGSSIQLTIHDFDVEYHATCNFDVLEIYGGPDFHSPRIAQLCVQRSAENPMQVSSTGNELALRFKTDSSVNGRGFNVSWRAVPGGCGGIFQAPSGEIHSPNYPSPYRSNTECTWLIQVEKNHRVLLNFTDFDLEPQDSCIMAFDGLSSATARLVGVCGRQQLSNPIISTGSSLFVRFQSGPSRQSRGFRAQFRQACGGHILTDSFDTISSPRFPASYPNNQNCSWIIQAQPPFNHITLSFSHFGLESSSTCTRDFVEILDGSHSDAPLRGRYCGSSMPHPITSFGNALMLRFVSDSSVNFDGFHATYVASTSACGGIFHMAEGIFNSPGYPEVYPSNVECVWNIASSPGNQLQLSFITFQLEDSRDCSRDFVEIREGNATGRLVGRYCGNVLPLNYSSIIGHDLWIKFVSDGSGSGVGFQAAFNNIFGNDHIVGTHGKVASPLWPRNYPHNSNYQWIVNVNESQVIHGRILEMDVEGTFNCYYDKLRIYDGADIHSRLIGTYCGAQTESFSSTGSSLTFQFSSDSSISGRGFLLEWFAMDASDGPLPTIATGACGGFLRTGDAPVFLYSPGWPGSYSNGADCMWLIQAPDSTVELNILSLDIESHRTCDYDKLVIRDGDNNMAQELAVLCGREIPGPIRSTGEYMTIRFTSDFSVTRAGFNASFHKSCGGYLHADRGIITSPGYPEAYTSNLNCSWHVQVQQGLSIAVHFEQPFQVSNRDAFCNQGDYLVLKNGPDIYSPPLGPHGGNGRFCGSRPSSTLFTSDNELFVQFISDNSNEGQGFKITYEAKSLACGGNIYIHDADSSGYVASPNHPDNYPQHADCIWVIAAPSGRPIRLEFEDQFSIEITPNCTSSYLELRDGADSNAPVLAKFCGTSLPPSQLSSGEVMYLRFRSDNSPTHAGFKAKYSIAQCGGTVTGQSGVIESSGYPALPYANNLFCEWRLQGLSGHYLTIHFEDFNLQNSSGCERDFVEIWENHTSGNLLGRYCGNTVPDSIDTSGNVALVRFVTDGFLTASGFRLRFDSSMEGCGGDLQGPTGTFTAPNYLNPNPHGWMCEWRITVQEGRRVTLTLNDLRLEAHPFCNSEHVAVFNGIRSNSPQLEKRCSSVNGSNEIRSSGNTMKVVYFTDGSRPYGGFTASYTSSEDAVCGGSLTNSPEGNFTSPGYDGTRNYSRNLNCEWTLSNSNQGNSSIYIDFEDFYLESHQDCQFDVLEFRVDNADGLLIWRLCGSSKPTMPLVIPYPQVWIHFVTNERVEHIGFRARYSFTDCGGIQIGDHGVISSPNYPASYDSLTHCSWLLEAPQGHTITLTFSDFDIEAHASCAWDSVTVRNGGSPGSPIIGHYCGSSNPRTIQSGSNQLVVIFNTDSSVQNGGFYATWNTETSGCGGILHSDTGTIRSPHWPQNFPENSRCSWTVITHPSKHLEISFDNNFLIPSGDSQCLNSFVKVWAGTQEADKDLLATSCGNVSPGRIITPRNAFTAVFQSQETPAQGFSASFLSRCGRNFTNPSGYIVSPNYPKQYDNNMNCTYIIEASPLSVILLKVVSFHLEARSTVSGSCDSDGVHIIRGHSLSSTPLVTLCGDEALSPVTISGPVLLNFYSNAHTTDFGFKFSYRITPCGGTFNLSFGIIKSPSYSYSNYPNDMHCLYTVTVRDDRVIQLKFNDFDLVPSTFCSQDYLEIYDGSNISDPLLGKFCGSTLPPNVKSSNNTMFLVFKTDSVHTARGWKISFRETLGPQQGCGGYLTGSTHTFGSPDSDSNGRYDKNLNCIWFITAPVNKLIKLTFSTFALEAATSLQRCIYDYVKLYDGDSENANLAGTFCGSTVPAPFISSGNFLTVQFVSDSSLEREGFNATYTLLDMPCGGTYNATWTSQSIWSPSSSDPDVPLTTCTWVIEAPLHQQVEITVWTFQLHSQDCDQNYLEFRDPPERNGNPGIRFCGRNASAVPTFYSSLSTAIIIFKSEVFNTDSRVGFTYRIAGCSREYQKAFGRLRSPGWPAGYASDADCAVVLRAPQNHTISLFFHAFGLEDSGGCTRDFLEVRNGSESTSPLLGKYCGTLLPNPIFSQSRDLYLRFKSDSATSGRGYEIIWTSSPSGCGGTLYGDSGLVTSPGYPGTYPNHTHCEWVIIAPGGRPVTVSFSFISIDDPGECVQNYLMLYDGPDANSPSSGPYCGADTDVAPFAASSHRVFIRFHAEAAARPSALRLTWAS
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Endocytic receptor which plays a role in lipoprotein, vitamin and iron metabolism by facilitating their uptake. Acts together with LRP2 to mediate endocytosis of high-density lipoproteins, GC, hemoglobin, ALB, TF and SCGB1A1. Acts together with AMN to mediate endocytosis of the CBLIF-cobalamin complex. Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the CBLIF-cobalamin complex. Ligand binding requires calcium. Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. May play an important role in the development of the peri-implantation embryo through internalization of APOA1 and cholesterol. Binds to LGALS3 at the maternal-fetal interface.
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F1S5L4
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GPAT1_PIG
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Glycerol-3-phosphate acyltransferase 1, mitochondrial (GPAT-1) (EC 2.3.1.15)
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MDESALTLGTIDVSYLPNSSEYSIGRCKHASEEWGECGFRPPVFRSATLKWKESLMSRKRPFVGRCCYSCTPQSWDRFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDVHKGMFATNVTENVLNSSRVQEAIAEVAAELNPDGSAQQQSKAVNKVKKKAKKILQEMVATVSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATEMNLPLIFLPVHRSHIDYLLLTFILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGQKDILYRALLHGHIVELLRQQQFLEIFLEGTRSRSGKTSCARAGLLSVVVDTLSTNTIPDILIIPVGISYDRIIEGHYNGEQLGKPKKNESLWSVARGVIRMLRKNYGCVRVDFAQPFSLKEYLESQSQKPVSAPLSLEQALLPAILPSRPSDAVDEGTDMSINESRNAADESFRRRLIANLAEHILFTASKSCAIMSTHIVACLLLYRHRQGIDLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLLGNCITITHTSRNDEFFITPSTTVPSVFELNFYSNGVLHVFIMEAIIACSLYAVLKKRGSGGPASPSLISQEQLVRKAASLCYLLSNEGTISLPCQTFYQICHETVGRFIQYGILTVAEQDDQEDISPSLAEQHWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITFLQRLLGPLLEAYSSAAIFIHNFSGPVPEPEYLQKLHKYLINRTERRVAVYAESATYCLVKNAVKMFKDIGVFKETKQKKVSVLELSSTFLPQCNRQKLLEYILSFVVL
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Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipids biosynthesis such as triglycerides, phosphatidic acids and lysophosphatidic acids.
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F1SPM8
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AAK1_PIG
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AP2-associated protein kinase 1 (EC 2.7.11.1) (Adaptor-associated kinase 1)
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MKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTESEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSFFSFKLLKKECPVPNVQNSPIPAKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRAMVQPPPQVAGSSNQPGLLASVPQPKTQAPPSQPLPQSQAKQPQAPPAPQQPPSAPAQGLPAQAQATPQHQQQLFLKQQPQPPQPQPQAQAPPVKSLKFYPFYPMCKGRQTVSSQFQAVHPAAQQPAIAQFPAVSQGSSQQQLIQNFYQQQQQQQQQQQLATTLHQQQLLTQQAALQQKTTVAAIQPPQAQPATASQPPPAQEPAQIQAPVRQQPKVQTTPPPAIQGQKLGSLTPPSSPKAQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRASQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKHPEKLGGSAESLIPGFQPTQGDAFAASSFAAGTAEKRKGGQAVDSSLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADVAVESLIPGLEPPVPQRLPSQTESVASNRTDSLTGEDALIDCSLLSNPTTDLLEEFAPIAISAPAHKAAEDSNLISGFDVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL
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Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Preferentially, may phosphorylate substrates on threonine residues (By similarity). Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes (By similarity). Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes (By similarity). Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity (By similarity).
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F1SR90
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SELS_PIG
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Selenoprotein S (SelS)
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MEQDGDQLSARPALETEGLRFLHVTVGSLLATYGWYIVFCCILLYVVFQKLSTRLRALRQRHLDGAAAALEPDVVVKRQEALAAARLKMQEELNAQVEKHKEKLRQLEEEKRRQKIERWDSVQEGRSYRGDARKRQEEDSPGPSTSSVIPKRKSDKKPLRGGGYNPLSGEGGGACSWRPGRRGPSSGGUG
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Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination (By similarity).
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F1SVH7
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FPOB_METMA
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F(420)H(2) dehydrogenase subunit B (EC 1.12.98.3) (F(420)H(2)-dependent phenazine dehydrogenase subunit B) (F(420)H(2)-dependent phenazine oxidoreductase subunit B) (FPO subunit B) (Methanophenazine hydrogenase subunit B) (Methanosarcina-phenazine hydrogenase subunit B)
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MGEVKETKTNNSKENPEEEVPGVITTTTSAIHNFLKKTKAQDIINWGRKNSLWFMTQPMGCCGVEMIATGCAHYDTDRFGIIPRNSPRHADVMIISGYVTKKYLPALKRLWDQMPAPKWVIAMGDCAISGGPFYESYSTVQNIDEIFPIDVYIPGCPPRPEALIQGFVELQEKIKARKDRGTEY
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Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methanol or methylamines. Catalyzes the oxidation of methanophenazine to dihydromethanophenazine. It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) centers, to methanophenazine (an electron carrier in the membrane). It couples the redox reaction to proton translocation (for every two electrons transferred, two hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. It also catalyzes the oxidation of F(420)H(2) with quinones such as 2,3-dimethyl-1,4-naphthoquinone, 2-methyl-1,4-naphthoquinone and tetramethyl-p-benzoquinone.
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F1T160
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BBLA_TOBAC
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Berberine bridge enzyme-like A (NtBBLa) (EC 1.1.1.-)
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MFPLIILISFSLASLSETATGAVTNLSACLINHNVHNFSIYPTSRNYFNLLHFSLQNLRFAAPFMPKPTFIILPSSKEELVSTIFCCRKASYEIRVRCGGHSYEGTSYVSFDASPFVIVDLMKLDDVSVDLDSETAWAQGGATIGQIYYAIAKVSDVHAFSAGSGPTVGSGGHISGGGFGLLSRKFGLAADNVVDALLIDADGRLLDRKAMGEDVFWAIRGGGGGNWGIVYAWKIRLLKVPKIVTTCMIYRPGSKQYVAQILEKWQIVTPNLVDDFTLGVLLRPADLPADMKYGNTTPIEIFPQFNALYLGPKTEVLSISNETFPELGVKNDECKEMTWVESALFFSELADVNGNSTGDISRLKERYMDGKGFFKGKTDYVKKPVSMDGMLTFLVELEKNPKGYLVFDPYGGAMDKISDQAIAFPHRKGNLFAIQYLAQWNEEDDYMSDVYMEWIRGFYNTMTPFVSSSPRGAYINYLDMDLGVNMVDDYLLRNASSSSPSSSVDAVERARAWGEMYFLHNYDRLVKAKTQIDPLNVFRHEQSIPPMLGSTQEHKYSSE
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Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins) nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN). Catalyzes a late oxidation step subsequent to the pyridine ring condensation reaction in the biosynthesis of alkaloids.
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F1T161
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BBLC1_TOBAC
|
Berberine bridge enzyme-like C-1 (NtBBLc) (EC 1.1.1.-)
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MFPLIILISFSFTFLSASATSGAGEGVANLSTCLINHNVHNFSMYPTSRNYFNLLDFSLQNLRFAASNMPKPTVIILPNSKEELVSTILCCRQTSYEIRVRCGGHSYEGTSSVSFDGSPFVIIDLMKLDDVSVDLDSETAWAQGGATIGQIYYAIAKASDVHAFSAGSGPTVGSGGHISGGGFGLLSRKFGVAADSVVDALLIDADGRLLDRKAMGEDVFWAIRGGGGGNWGIIYAWKIRLVKVPKIVTTFKISKPGSKQYVAPLLYKWQIVAPNLADDFTLGVQMIPIDLPADMKYGNPTPIEICPQFNGLYLGPKTEAVSILNEAFPELNVKNDDAKEMTWIESALFFSDLDNIFGNSSDDISHLKERYLGVKICFKGKSDYVKTPFSMDGIMTALVEHEKNPNAFLVFDPYGGAMDKISAQAIAFPHRKGNLFAIQYYAQWNEEDDAKSNEHIEWIRGFYNKMAPFVSSSPRGAYVNYLDMDLGMNMDDDYLLRNASSRYSSSVDAVERARAWGEKYFLNNYDRLVKAKTKIDPLNVFRHEQSIPPTLGSTQEHNYSSE
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Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins) nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN). Catalyzes a late oxidation step subsequent to the pyridine ring condensation reaction in the biosynthesis of alkaloids.
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F2JXJ3
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LODA_MARM1
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L-lysine 6-oxidase (EC 1.4.3.20) (L-lysine-epsilon-oxidase) (Marinocine)
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MALSVHPSIGVARLGNANTDNFVLNPMEIGGLPYEHDVDLKPTTTVVNFKDEAGCIRRQGQVFKVFGASNEELTLDSPNVKNIEWTVHLANKKAAWYEFRELNGNLLYGRDNSYSARGVPWRNASKTASSERQSLIIDLGPRSVSGVMATVEISINNIPETYLHPSYPSGELLQGSKHFESLGTLRTDSQGRLIVLGGYGFAGGNTDLSGYGGGDDWYDDISDGSVTCVVTYSDDSSETSTAWMVVGSPDFAPEIVNISTLSDTCFDVGVRNFDLVPDMYDSATGHYKSDYVANFDRDILPIIQRISQYQWVSNVQSMSGFFSFQFDYRDGSAANKANRMKYYNYFRQLDNKVIGDYDQPQQVLMSSEVEGDILPLMPMNSGSNSVSSSNFYDLTDNVVEKFLALDATQLFLLGQWAEGEFTAGPADDYPVSDMDTASIGNCVGLPMCPGIEMTWSLQNPVIYKDAYQIKHYQDKAYFDVNGLTPERDECEEETGCEPGDLTKRMACPWQADFFNCTIQTVNFSEPSVNKASQTETVTSRTHYEWGNLPAGVSVPDQSSVSATKNVDEKVPLPPAYYSYWWPPQSPWDVLTGELDTEGQLHSHLPAGQQINYARGINSYSQMVEHWSALAFIRDRNQNNDGFPFFTETERNHELFDFKEVLVGQVTGNSEDNETSLPVFFINANKESLEGKGTKKGKLMASYFEERAFSKVRSSNIRPRSGTRMRG
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Has antibacterial activity against a wide spectrum of Gram-positive and Gram-negative bacteria including nosocomial isolates of S.aureus and Pseudomonas sp. The antimicrobial activity is due to hydrogen peroxide generated by its lysine oxidase activity. Also has autotoxic activity. Involved in biofilm differentiation responsible for cell death within microcolonies during biofilm development which is linked to the generation of a phenotypically diverse dispersal population and thus may play a role in colonization.
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F2SG60
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MDR3_TRIRC
|
ABC multidrug transporter MDR3 (Multidrug resistance protein 3)
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MAPTEEANVTKPTGELRPDEKLNYEEDVKCSGSSSTTVGKTAYDTDDISQSQAAELQDLARQLSRASRQGGLDVENEPQQVINPFLDSESDPELNPDSKSFNVAKWLKTILQITSRDPERFPKRTAGVSFRNMNVHGYGTAADYQSDVGNLPLKAWSGIMSMLGLRKKVRIDILRDFEGLVKSGEMLVVLGRPGSGCSTLLRTLSGETHGLYLDEGNDIQYQGISWEQMHKNFRGEVIYQAETETHFPQMTVGDTLYFAARARAPANRLPGVSREQYAIHMRSMVMSMLSLSHTINTQVGNEYIRGVSGGERKRISIAETTLSGSPLQCWDNSTRGLDSANALEFVKSLRLSTKYSGTTAIVAIYQAGQAIYDIFDKAVVLYEGHQIYFGNAVRAKEYFIEMGFDCPSRQTTADFLTSVTSPSERRVRPGYESRVPQTPAEFAQRWKESEDRRILMQEIDEYNKTYPLHGEQLQKFQASRLAEKSRSTSKSSPYTLSYPMEIKLCMWRGFQRLKGDMSMTLTSIIGNIAMSLIIASVFYNQQETTDSFFSRGSLLFFAILMNAFASSLEILTLWHQRPIVEKHDKYALYHPSSEAISSILVDMPAKLAVAIVFNLIIYFMTNLRRTPGHFFIFFLFSFTTTLTMSNVFRSIAAVSRTLSQALVPTSIFMLALVIYTGFTIPVRDMRPWFKWISYINPIQYAFESLMINEFHDREFKCAVYIPSGPGYSNVSGTSKICAAKGAMAGKPTVSGDVFLRETYSYYASHMWRNYGIIVAFFLFFLFVYITATELVSAKPSKGEILVFPKGKVPAFLKQSKKKQDPEAASTQEKQPVETSGHDQTAAIVKQTSVFHWESVCYDIKIKKESRRILDNVDGWVKPGTLTALMGVSGAGKTTLLDVLANRVTMGVVTGEMLVDGRLRDDSFQRKTGYVQQQDLHLEISTVREALTFSALLRQPNTTPYEEKVAYVEEVIKMLGMEEYANAVVGVLGEGLNVEQRKRLTIGVEIAAKPDLLLFFDEPTSGLDSQTAWSICTLMRKLADHGQAVLCTIHQPSAMLMQEFDRLLFLASGGRTVYFGELGKHMSTLIEYFESKGAPKCPPDANPAEWMLEVIGAAPGSKTDIDWPAVWRDSAERVEVRRHLAELKSELSQKPQTPRLTGYGEFAMPLWKQYLIVQHRMFQQYWRSPDYIYSKACLAIVPTLFIGFTFYKEQVSLQGIQNQMFAIFMFMILFPNLVQQMMPYFVIQRSLYEVRERPSKTYSWIAFMISSVVVEIPWNALLTVPAFFCWYYPIGFYKNAIPTDAVTERSGTMFLLILIFLMFSSTFSSMVIAGIEQAETGGNIAQLCFSLTLVFCGVLVSPTAMPGFWIFMYRLSPFTYFVSAVLSTGVGRTDIVCAANEILRLTPAAGQTCMEYLGPYTKFAGGRILTPDATDMCEFCAVADTDTFLKGVNIIFDERWRNIGILFGYIAFNMVGAIGLYWLLRVPKRKSGVKQGQQPQKQANETKA
|
Pleiotropic ABC efflux transporter involved in the modulation susceptibility to azoles, including fluconazole, itraconazole, ketoconazole, miconazole and voriconazole.
|
F2WP51
|
LPAKS_PSESP
|
Linear primary-alkylsulfatase (EC 3.1.6.21) (Primary type-III alkylsulfatase) (Type III linear primary-alkylsulfatase)
|
MKLNALSTATHGSRSSPVKLWKFSTSFLLAASIIVSGQSWAAETAKPATDATKAANDALLKELPFDDKTSFDLAHKGFIAPLPAEPIKGEKGNMIWDPSKYGFIKEGEAAPDTTNPSLWRQSQLINISGLFEVTDGIYQVRNYDLSNMTIVEGKDGITIFDPLISQETAKAALDLYYKHRPKKPVVAVIYTHSHVDHYGGVRGVVDEADVKAGKVKIYAPLGFLEHAVAENVMAGTAMSRRASYMYGNLLPPDAKGQLGAGLGTTTSAGTVTLIPPTDIIKETGETHVIDGLTYEFMYAPGSEAPAEMLYYIKEKKALNAAEDSTHTLHNTYSLRGAKIRDPLAWSKYLNEALKLWGDDVQVMYAMHHWPVWGNKEVREQLSLQRDMYRYINDETLRLANKGYTMTEIAEQVKLPKKIATKFSNRGYYGSLNHNVKATYVLYLGWFIGNPATLWELPPADKAKRYVEMMGGADAVLKKAKEYYDKGDFRWVAEVVNHVVFAEPNNQAAKNMQADALEQLGYQAESGPWRNFYLTGAQELRNGVQQLPTPDTASPDTVKAMDLDLFFDFLAMRLKGPDVADKHITLNLDFTDLKQKYTLEMVNGVLNHTEGMQAKNADATVTLTRETLNNVMLKQTTLKDAESSGDIKIEGDKGKLEELMSYMDNFDFWFNIVTP
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Alkylsulfatase that cleaves primary alkyl sulfates such as sodium octyl sulfate and the widely used detergent sodium dodecyl sulfate (SDS).
|
F2XF95
|
PINS1_PICGL
|
(-)-alpha-pinene synthase 1, chloroplastic (EC 4.2.3.119) ((-)-beta-pinene synthase 1) (EC 4.2.3.120) (Terpene synthase TPS-Pin-1) (PgTPS-Pin-1)
|
MALVSIAPLASKSCLHKSLSSSAHELKTICRTIPTLGMSRRGKSATPSMSMSLTTTVSDDGVQRRMGDFHSNLWNDDFIQSLSTSYGEPSYREQAERLIGEVKKMFNSMSSEDGELINPHNDLIQRVWMVDSVERLGIERHFKNEIKSALDYVYSYWSEKGIGCGRESVVADLNSTALGLRTLRLHGYAVSADVLNLFKDQNGQFACSPSQTEEEIRSVLSLYRASLIAFPGEKVMEEAEIFSAKYLEEALQKISVSSLSQEIRDVLEYGWHTYLPRMEARNHIDVFGQDTQNSKSCINTEKLLELAKLEFNIFHSLQKRELEYLVRWWKDSGSPQMTFGRHRHVEYYTLASCIAFEPQHSGFRLGFAKTCHIITILDDMYDTFGTVDELELFTAAMKRWNPSAADCLPEYMKGMYMIVYDTVNEICQEAEKAQGRNTLDYARQAWDEYLDSYMQEAKWIVTGYLPTFAEYYENGKVSSGHRTAALQPILTMDIPFPPHILKEVDFPSKLNDLACAILRLRGDTRCYKADRARGEEASSISCYMKDNPGVTEEDALDHINAMISDVIRGLNWELLNPNSSVPISSKKHVFDISRAFHYEYKYRDGYSVANIETKSLVKRTVIDPVTL
|
Terpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (1S,5S)-beta-pinene.
|
F2XF96
|
PINS2_PICGL
|
(-)-alpha-pinene synthase 2, chloroplastic (EC 4.2.3.119) ((-)-beta-pinene synthase 2) (EC 4.2.3.120) (Terpene synthase TPS-Pin-2) (PgTPS-Pin-2)
|
MALVSIAPLASKSCLHKSLSSSAHELKTICRTIPTLGMSRRGKSATPSMSMSLTTTVSDDGVQRRMGDFHSNLWNDDFIQSLSTSYGEPSYRERAERLIGEVKKMFNSMSSEDGELINPHNDLIQRVWMVDSVERLGIERHFKNEIKSALDYVYSYWSEKGIGCGRESVVADLNSTALGLRTLRLHGYAVSADVLNLFKDQNGQFACSPSQTEEEIGSVLNLYRASLIAFPGEKVMEEAEIFSAKYLEEALQKISVSSLSQEIRDVLEYGWHTYLPRMEARNHIDVFGQDTQNSKSCINTEKLLELAKLEFNIFHSLQKRELEYLVRWWKDSGSPQMTFGRHRHVEYYTLASCIAFEPQHSGFRLGFAKTCHIITILDDMYDTFGTVDELELFTAAMKRWNPSAADCLPEYMKGMYMIVYDTVNEICQEAEKAQGRNTLDYARQAWDEYLDSYMQEAKWIVTGYLPTFAEYYENGKVSSGHRTAALQPILTMDIPFPPHILKEVDFPSKLNDLACAILRLRGDTRCYKADRARGEEASSISCYMKDNPGVTEEDALDHINAMISDVIRGLNWELLNPNSSVPISSKKHVFDISRAFHYGYKYRDGYSVANIETKSLVKRTVIDPVTL
|
Terpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (1S,5S)-beta-pinene.
|
F2XF99
|
FARNS_PICXS
|
(E,E)-alpha-farnesene synthase (EC 4.2.3.46) ((E)-beta-ocimene synthase) (EC 4.2.3.106) (Terpene synthase TPS-Far/Oci) (PgxeTPS-Far/Oci)
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MASVDQSQLCSKSVSMSLSVDDGVQRRTGDYHSNLWDDDFIQSLSTPYGAPCYRERAERLIGEVKEMFNSVRLSPLNDLLQGLSMVDSVERLGIDRHFKNEIKSALDYVYSYWSEKGIGCGRESVVTDLNSSALGFRALRLHGYPVSSDVFKDQNGQFACSANTQTEGEMRGVLNLFRASLVAFPGEKVMEDAERFSAIYLKEALKTVPICSGSLSGEIEYVLEYGWLTNFPRLEARNYIDIFGKDTSPCLQTEKLLELAKLEFNIFHSLQQRELKQVSRWWKDSGFSQLTFTRHRHVEFYTLASCIAIEPKHSAFRLGFAKLCYLGIVLDDIYDTFGTMDELELFTAAIKRWDPSATECLPEYMKGVYMVFYECVNQMAREAEKTQGRDTLSYARNTWEAVFDAFLEEAKWISSGYIPTFEEYLENGKVSFGYRAATLQPILTLDVPLPLHILQEIDFPSRFNDLAASILRLRGDVCGYKAERSRGEEASSISCYMKDNPGATEEDALNQIDTMIKEKIKELNWEFLKPDSNVPISSKKHAFDILRAFYHLYKYRDGFSIANNETKSLVMRTLLETVPF
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Terpene synthase (TPS) involved in the biosynthesis of sesquiterpene and monoterpene natural products included in conifer oleoresin secretions and volatile emissions these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to (3E,6E)-alpha-farnesene and of (2E)-geranyl diphosphate (GPP) to (E)-beta-ocimene.
|
F2XFA8
|
PINS1_PICSI
|
(-)-alpha-pinene synthase 1, chloroplastic (EC 4.2.3.119) ((-)-beta-pinene synthase 1) (EC 4.2.3.120) (Terpene synthase TPS-Pin) (PsTPS-Pin)
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MALVSIAPLASKSCLHKSLSSSAHELKTICRTIPTLGMSRRGKSATPSMSMSLTTTVSDDGVQRRMGDFHSNLWNDDFIQSLSTSYGEPSYRERAERLIGEVKKMFNSMSSEDGELISPHNDLIQRVWMVDSVERLGIERHFKNEIKSALDYVYSYWSEKGIGCGRESVVADLNSTALGFRTLRLHGYAVSADVLNLFKDQNGQFACSPSQTEEEIRSVLNLYRASLIAFPGEKVMEEAEIFSAKYLEESLQKISVSSLSQEIRDVLEYGWHTYLPRMEARNHIDVFGQDTQNSKSCINTEKLLELAKLEFNIFHSLQKRELEYLVRWWKDSGSPQMTFCRHRHVEYYTLASCIAFEPQHSGFRLGFAKACHIITILDDMYDTFGTVDELELFTAAMKRWDPSAADCLPEYMKGVYLILYDTVNEMSREAEKAQGRDTLDYARRAWDDYLDSYMQEAKWIATGYLPTFAEYYENGKVSSGHRTSALQPILTMDIPFPPHILKEVDFPSKLNDLACAILRLRGDTRCYKADRARGEEASSISCYMKDNPGATEEDALDHINAMISDVIRGLNWELLNPNSSVPISSKKHVFDISRAFHYGYKYRDGYSVANIETKSLVKRTVIDPVTL
|
Terpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (1S,5S)-beta-pinene.
|
F2XFB2
|
LEVOS_PICSI
|
Bifunctional levopimaradiene synthase, chloroplastic (Abietadiene synthase) (EC 4.2.3.18) (Levopimaradiene synthase) (EC 4.2.3.32) (Terpene synthase TPS-LAS) (PsTPS-LAS) (PsTPS-LASl)
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MALLSSSLSSHIPTGAHHLTLNAYANTQCIPHFFSTLNAGTSAGKRSSLYLRWGKGSNKIIACVGEDSVSAPTLLKREFPPGFWKDHVIDSLTSSHKVAASDEKRIETLISEIKNMFRSMGYGETNPSAYDTAWVARIPAVDGSEQPEFPETLEWILQNQLKDGSWGEGFYFLAYDRILATLACIITLTLWRTGEIQVQKGIEFFKTQAVKIEDEADSHRPSGFEIVFPAMLKEAKVLGLDLPYELPFIKKIIEKREAKLERLPTNILYALPTTLLYSLEGLQEIVDWQKIIKLQSKDGSFLTSPASTAAVFMRTGNKKCLEFLNFVLKKFGNHVPCHYPLDLFERLWAVDTVERLGIDRHFKEEIKDALDYVYSHWDERGIGWARENLVPDIDDTAMGLRILRLHGYNVSSDVLKTFRDENGEFFCFLGQTQRGVTDMLNVNRCSHVAFPGETIMEEAKTCTERYLRNALEDVGAFDKWALKKNIRGEVEYALKYPWHRSMPRLEARSYIEHYGPNDVWLGKTMYMMPYISNEKYLELAKLDFNHVQSLHQKELRDLRRWWTSSGFTELKFTRERVTEIYFSPASFMFEPEFATCRAVYTKTSNFTVILDDLYDAHGTLDDLKLFSDSVKKWDLSLVDRMPEDMKICFMGFYNTFNEIAEEGRKRQGRDVLGYIRNVWEIQLEAYTKEAEWSAARYVPSFDEYIENASVSIALGTVVLISALFTGEILTDDVLSKIGRGSRFLQLMGLTGRLVNDTKTYEAERGQGEVASAVQCYMKDHPEISEEEALKHVYTVMENALDELNREFVNNREVPDSCRRLVFETARIMQLFYMDGDGLTLSHETEIKEHVKNCLFHPVA
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Terpene synthase (di-TPS) involved in the biosynthesis of diterpene natural products included in conifer oleoresin secretions and volatile emissions these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (+)-copalyl diphosphate ((+)-CPP) to isopimaradiene.
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F2XG53
|
CAS3_STRTR
|
CRISPR-associated nuclease/helicase Cas3 (EC 3.1.-.-) (EC 3.6.4.-)
|
MKHINDYFWAKKTEENSRLLWLPLTQHLEDTKNIAGLLWEHWLSEGQKVLIENSINVKSNIENQGKRLAQFLGAVHDIGKATPAFQTQKGYANSVDLDIQLLEKLERAGFSGISSLQLASPKKSHHSIAGQYLLSHYGVDEDIATIIGGHHGRPVDDLDGLNSQKSYPSNYYQDEKKDSLVYQKWKSNQEAFLNWALTETGFNSVSQLPKIKQPAQVILSGLLIMSDWIASNEHFFPLLSLDETDVKNKSQRIETGFKKWKKSNLWQPETFVDLVTLYQERFGFSPRNFQLILSQTIEKTTNPGIVILEAPMGIGKTEAALAVSEQLSSKKGCSGLFFGLPTQATSNGIFKRIEQWTENIKGNNSDHFSIQLVHGKAALNTDFIELLKGNTINMDDSENGSIFVNEWFSGRKTSALDDFVVGTVDQFLMVALKQKHLALRHLGFSKKVIVIDEVHAYDAYMSQYLLEAIRWMGAYGVPVIILSATLPAQQREKLIKSYMAGMGVKWRDIENIDQIKIDAYPLITYNDGPDIHQVKMFEKQEQKNIYIHRLPEEQLFDIVKEGLDNGGVVGIIVNTVRKSQELARNFSDIFGDDMVDLLHSNFIATERIRKEKDLLQEIGKKAIRPPKKIIIGTQVLEQSLDIDFDVLISDLAPMDLLIQRIGRLHRHKIKRPQKHEVARFYVLGTFEEFDFDEGTRLVYGDYLLARTQYFLPDKIRLPDDISPLVQKVYNSDLTITFPKPELHKKYLDAKIEHDDKIKNKETKAKSYRIANPVLKKSRVRTNSLIGWLKNLHPNDSEEKAYAQVRDIEDTVEVIALKKISDGYGLFIENKDISQNITDPIIAKKVAQNTLRLPMSLSKAYNIDQTINELERYNNSHLSQWQNSSWLKGSLGIIFDKNNEFILNGFKLLYDEKYGVTIERLDKNESV
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CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Functions as a ssDNA-dependent ATPase dsDNA, ssRNA do not stimulate ATPase activity, while other nucleotides (aside from dATP) are not hydrolyzed. Functions as a ssDNA nuclease activity does not require ATP. Functions as an ATP-dependent helicase helicase activity requires hydrolysable ATP. Unwinds both DNA/DNA hybrids and RNA/DNA hybrids, moving mostly in a 3' to 5' direction.
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F2Y4A3
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SPHK2_ARATH
|
Sphingosine kinase 2 (EC 2.7.1.91)
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MENDQFMCPTDIITGIVFIDGELAMLTLTADGELRWTEYGLRQYLSMKKDVLGFIVEGKQIRVKAVVEKEAGGICCGQFGGDFVRKDFVFEPLIDQNGWCYKLRQYLDSLGRPKRLLVFVNPFGGKKSAREIFVKEVKPLFEDADVQLEIQETKYQLHAKEFVKSMDVSKYDGIVCVSGDGILVEVVNGLLERADWRNALKLPIGMVPAGTGNGMIKSLLDTVGLRCCANSATISIIRGHKRSVDVATIAQGNTKFFSVLMLAWGLIADIDIESEKFRWMGSARIDFYALQRIICLRRYNGRILFLPAPGFEGYGQPASCSLYQEPHVSDKEVGYQGPETKFEDLEWREMKGPFVTIWLHNVPWGSENTLTAPAAKFSDGYLDLIVLKNCPKLVLLSLMRQTSSGTHVESPYIVYIKVKAFVLEPGALVDEPDKEGIIDSDGEVLARGKRTYKCDQKALMSYDKLQVTVDQGLATLFSPEY
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Involved in the production of sphingolipid metabolites. Phosphorylates sphingosine and various l sphingoid long-chain base (LCB) products, such as phytosphingosine (PHS, 4-hydroxysphinganine), 4-hydroxy-8-sphingenine, 4,8-sphingadienine and D-erythro-dihydrosphingosine, but has a very few activity toward D,L-threo- dihydrosphingosine. Is required for abscisic acid (ABA) signaling that mediates stomatal closure, inhibition of seed germination and root elongation. May function upstream of PLDALPHA1 and phosphatidic acid (PA) in an amplification response to ABA that mediates stomatal closure.
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F2YMG0
|
PRS56_MOUSE
|
Serine protease 56 (EC 3.4.21.-)
|
MPLAMLLLLLLLLSPDSQTAHGHPLYTRLSPGALQVLSAQGTQALQAAQRSAQWAIKRVLMEIQHRLHECQGPGRPRPQAPLLQDPPEPVQCGERHQGVANTTRAHGRIVGGSTAPSGAWPWLVRLQLGGLPLCGGVLVAASWVLTAAHCFAGASNELLWTVMLAEGPQGEQAEEVQVNRILPHPKFDPQTFHNDLALVQLWTPVSPEGPARPICLPQGSREPPAGTPCAIAGWGALFEDGPESEAVREARVPLLSADTCQKVLGPGLRPSTMLCAGYLAGGIDSCQGDSGGPLTCSEPGPRPREVLFGVTSWGDGCGEPGKPGVYTRVTVFKDWLQEQMSAGPSTREPSCRELLNWNAREEEPFTDAPGLCAFYARQCLGSESSCARLALQQCLQRRRRCELRSLAHTLLGLLRGAQELLGPRPGLRRGVSAPARSAPSLQELPGHNPREQRLYSGSRIAGTWLQKPKPERRPETKGCPGLEPLQQKLAAIQRAHAWILQIPAEHLAMNFHEVLADLGSKTLTGLFRAWVRAGLGDQRVVFSGLVGLEPSTLAHSLPRLLVQALKAFRSASLTEGEPQAPWIGADQGQRLGKERQGQLQPPVP
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Serine protease required during eye development.
|
F2YTN4
|
MOMT1_SOLHA
|
Myricetin 3'/5'-O-methyltransferase 1 (ShMOMT1) (3'-methyl myricetin 5'-O-methyltransferase) (Syringetin synthase) (EC 2.1.1.267) (3-methyl quercetin 3'-O-methyltransferase) (EC 2.1.1.-) (7-methyl quercetin 3'-O-methyltransferase) (Rhamnetin 3'-O-methyltransferase) (EC 2.1.1.-) (Myricetin 3'-O-methyltransferase) (Laricitrin synthase) (EC 2.1.1.267) (Quercetin 3'-O-methyltransferase) (Isorhamnetin synthase) (EC 2.1.1.267)
|
MALSMDNIVISNEEEICMMKAMHLPCGLYLNMVLKAAIELDLFEIIAKSTTQKLSSYEIASQIPTKNPNASSLVLERILRFLASQSLLTCNITKNDDGNVHTTYNLTPLSQSLISDKDGTSIAPFLLLATDPVGVHACFHLKDAILEGEIPFNKAHGVHAFEYHGKDSRMNGLFNKAMQNLTCIEMKRIVECYNGFQGVKEIIDVGGGLGISLASIISKYPNIKGINFDLPHVIKDAPTYEGIEHVGGDMWDSIPQGELIILKAVLHSLDDEDCVKILKNCWRALPNDGKVVVIEQIQPKYPETNLLSKRSFSFDISMMIMFHGGKERTKQQFEDLAKQAGFTYIKVVARAYYSWLIELYKY
|
Flavonoid 3'/5'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as myricetin derivatives, aroma compounds possessing antioxidant properties and exhibiting pharmacological activities such as anti-carcinogen, anti-viral, anti-thrombotic, anti-diabetic, anti-atherosclerotic, and anti-inflammatory effects. Catalyzes S-adenosylmethionine-dependent regioselective 3'/5'-O-methylation of flavonoids active on various hydroxylated flavonoid substrates, including myricetin and quercetin, but inactive toward kaempferol. Mediates the formation of 3'-methyl derivatives from quercetin, myricetin, 3-methyl quercetin and 7-methyl quercetin (rhamnetin), producing 3'-methyl quercetin (isorhamnetin), 3'-methyl myricetin (laricitrin), 3,3'-dimethyl quercetin (3-O-methylisorhamnetin) and 7,3'-dimethyl quercetin (7-O-methylisorhamnetin), respectively. Triggers the 5'-O-methylation of 3'-methyl myricetin (laricitrin), thus leading to production of 3',5'-dimethyl myricetin (syringetin).
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F2YTN5
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MOMT2_SOLHA
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Myricetin 7/4'-O-methyltransferase 2 (ShMOMT2) (3',4',5'-trimethyl myricetin 7-O-methyltransferase) (EC 2.1.1.-) (3',5'-dimethyl myricetin 7-O-methyltransferase) (7-O-methyl syringetin synthase) (Syringetin 7-O-methyltransferase) (EC 2.1.1.-) (3'-methyl quercetin 4'-O-methyltransferase) (4'-O-methyl isorhamnetin synthase) (Isorhamnetin 4'-O-methyltransferase) (EC 2.1.1.-) (3-methyl quercetin 7-O-methyltransferase) (EC 2.1.1.82) (4'-methyl kaempferol 7-O-methyltransferase) (7-O-methyl kaempferide synthase) (Kaempferide 7-O-methyltransferase) (EC 2.1.1.-) (7-methyl quercetin 4'-O-methyltransferase) (Rhamnacene synthase) (Rhamnetin 4'-O-methyltransferase) (EC 2.1.1.-) (Kaempferol 4'-O-methyltransferase) (Kaempferide synthase) (EC 2.1.1.155) (Myricetin 7-O-methyltransferase) (EC 2.1.1.-) (Quercetin 7-O-methyltransferase) (Rhamnetin synthase) (EC 2.1.1.-)
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MASNNNCAYELIEAEAQSWDYILSYLRPSCIKCAIQLGIPDILHKNADPIMSLSDLIAALPNLNPSKTTFIPILMRVLVDFGLFNYHQQQGDGYSLTTVGRLLVENHHFGNRSFFLFAQHPVVLNTAASVGDWLKDDLRTAFETADGKSHWDYCGADPEFNGVFNDAMAGDSRLMSNLLISDCCAGVFEGLTSLVDIGGGTGAVAMAIAGAFPSLKCIVLDLPHVIADRKGSGNLEFVAGSMFDKIPHANAILLKWILHNWDDEDCVKLLKKCKESISSRENGGKVIIIDMIMEDNYNNKQLVQSQHLMDLIMRITYASKERTEKEWEKLFLEAGFSGYKIITSLGLRSLIEIYP
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Flavonoid 7/4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as myricetin derivatives, aroma compounds possessing antioxidant properties and exhibiting pharmacological activities such as anti-carcinogen, anti-viral, anti-thrombotic, anti-diabetic, anti-atherosclerotic, and anti-inflammatory effects. Catalyzes S-adenosylmethionine-dependent regioselective 7/4'-O-methylation of flavonoids active on various hydroxylated flavonoid substrates, including myricetin, quercetin and kaempferol. Mediates the formation of 4'-methyl derivatives from kaempferol, 3'-methyl quercetin (isorhamnetin), 7-methyl quercetin (rhamnetin) and 3'-methyl myricetin, producing 4'-methyl kaempferol (kaempferide), 3',4'-dimethyl quercetin (4'-O-methyl isorhamnetin), 7,4'-dimethyl quercetin (4'-O-methyl rhamnetin, rhamnacene) and 3',4'-dimethyl myricetin, respectively. Triggers the 7-O-methylation of quercetin, myricetin, 4'-methyl kaempferol (kaempferide), 3-methyl quercetin, 3',5'-dimethyl myricetin (syringetin) and 3',4',5'-trimethyl myricetin, thus leading to production of 7-methyl quercetin (rhamnetin), 7-methyl myricetin, 7,4'-dimethyl kaempferol (7-O-methyl kaempferide), 3,7-dimethyl quercetin, 7,3',5'-trimethyl myricetin (7-O-methyl syringetin) and 7,3',4',5'-tetramethyl myricetin, respectively.
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F2Z472
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SVS3A_MOUSE
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Seminal vesicle secretory protein 3A (Seminal vesicle secretory protein III) (SVS III)
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MKSIFFSLSLLLLLEKKAAGIELYAGGTKGHFLVKTSPLMFIGKNQFLYGHKEEQEEAPEESIFVQTKHHEYGQDADADMGGALSSQELTSLKEDIVCEEEDELAQQKSQLPSQSQIKSQTQVKSYAAQLKSQPGQLKTIGQVKSQTMLKSHGAPLKSFKARLNLREDIPQQVKGRGYGLAEDLAQVRQQPAKVHRLKGKHRQSRKTAAFYPQFRRRSRPYPRYFVQFQEQLQGSVHHTKSFYPGPGMCYCPRGGVILYQDAFTD
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Component of the copulatory plug.
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F3Y5P4
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GRDN_CAEEL
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Girdin homolog (Coiled-coil domain-containing protein grdn-1)
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MKEKHENWSHPLAFWLCDCAAIIPNPATQNFAKNDFLDGLLMLNLMKFINPHFSENEKNGQSLYEELLNQISQFYEKNLDQVIVCKMPEISILESSGEIDEITFEELKKLLLLLLGCAIQSDHKKVFVDRITGFDQTIQAELAACIQKLTESDEIVQNLEDFERRKMKETDEVGGGGGSIEDVDSDDMESSTTSSSNGEIAIKQQDQSFLMSRSTSPTSELRHQTLQIANLQHEMRQMRTQAENRDEECQKLELDNEEKAQKIKILENERLKLVDFKKKWKSVNDDLQEANCKIEKLQNLVGIEKKYREARDGKELYKSKYDIVVKKNLEMEETITTLEKNLKTLQMEMKEKFGVEDNLQRMRNTIDDLEAEISKKNLEIEDFLDEKHRMDREIKELKEIVHQMEVPSTTTTPRIMDSLADQLENAKQDEFEMMKAEIRKLRAQTEGATPETTIIQCNQDLDTLRSQLSTEQHQTAQLHLEIQKMQVEKEQIDGNMERIGIELEEMSAQVENLNLERDEAVKQLLEARRKFGEFQMGQSRDLEEKWSKEVEKSNKISKKCEILEEKLQESDFLLAKSRDEAKKLQFELDEALEETSHVTRSLSSEKNTLKAKLLELQDQVEAQTLELLNQKNCGKRLEDRDQMISNLHNLKNELENDLKTCQTQLELESKKLQRLREDLVLEKSRRADLIGRIHSLCTTLSLNGANFEKINNDDELIDNIDDIMMNALVAVKRERDDLRIQGNQQIQELHDLKRDIEKLRRSESESLNESDDRVRELTRENMHTKEQVFMLQEKLRELNLELSTKNDEIDMVKASIEELNRNSTASCTSNAEIARLQVSIRNSQIQEDLVKQENTKLRDELQEMQKMSKKRSQNLDELENMHKTLLVDHSRLQQLHNLLTRDYDEAKKESMELRQKVQNIPRQQAVFMNANIRELEAKLSEEISRREQLEKEHKMCRIHCENLRRDITELVQTRDELSLELRRAHDTCHNKNNQIDELKKQLNQKISEVNKLSSKIEALSQLNRTYNEENRNLSRQLEILLTQNKELLQRALHDKDQYHLEMKDFQDQLSALRRHKEKLEDKIMDQYRTMENKKSTPERKQPLVKRAAKALINRRRATSNGGSTTEDSSVYSADERSSPPLAGTNEDVDHLPPTCSSSDDHDVISPDFSAKNPLLRSRNDFMGGSVRSPRRYGNDHDGHIYTSPFLPPRVPIRNSPMTSSLRSRPPPPPYNRSPAHKIEQNSSFFEPIAHSTPNSSILEERRVVGEGEKRELVRDKEERIDKTLSYYENVNLPQNPPDLPENSDLKPNESTIWHEYGCV
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Scaffolding protein that plays a role in ciliogenesis, cilium positioning and dendrite anchoring in sensory amphid neurons including AWB, AWA, AWC, ADL and ASI, the phasmid neurons PHA and PHB and the gas sensing neurons AQR, PQR, URX and BAG. Its role in cilium positioning may be through regulation of the localization of cell adhesion proteins such as the apical junction protein ajm-1, and the ciliary scaffolding protein Rootletin/che-10. Plays a more prominent role in regulating dendrite morphogenesis in AQR than in PQR neurons. Regulates localization of hmr-1 to the distal AQR dendrite. During embryonic elongation, required for the anchoring of URX and BAG dendrites to the presumptive nose.
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F3YDF1
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YMEL1_DROME
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ATP-dependent zinc metalloprotease YME1L (EC 3.4.24.-) (YME1-like ATPase)
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MFSTTTHSVPYLYLGNFSRKPHYYSVNRTKLHGSAGAARLSKSTSTSSRSHDLVLDLRNLLSRSSASIQGMVERAARLNGILDRRLVDDVLAKVTSMLPSMRDVRVTLEESATQIGRVQLQNYQFEVSLTGAAGSVPTGANVKVIPTITPGLLRPLFSQQQLNQIRGFKTDRSIEAEQKRNPTMTSRLKNALANSPQRLDGDTPLQAEKLRRLLAKSEEHGFNKAESLKIAFAEGYLAAANSEDSPKSGKTMKYLKTLQTIVVIVVFLGIFLSFFTTSNGSVFRSIQLGNQVEVDPEEINVTFEDVKGCDEAKQELKEVVEFLKSPEKFSNLGGKLPKGVLLVGPPGTGKTLLARAVAGEAKVPFFHAAGPEFDEVLVGQGARRVRDLFKAAKARAPCVIFIDEIDSVGAKRTNSVLHPYANQTINQLLSEMDGFHQNAGVIVLGATNRRDDLDQALLRPGRFDVEVMVSTPDFTGRKEILSLYLTKILHDEIDLDMLARGTSGFTGADLENMINQAALRAAIDGAETVSMKHLETARDKVLMGPERKARLPDEEANTITAYHEGGHAIVAFYTKESHPLHKVTIMPRGPSLGHTAYIPEKERYHVTKAQLLAMMDTMMGGRAAEELVFGTDKITSGASSDLKQATSIATHMVRDWGMSDKVGLRTIEASKGLGTGDTLGPNTIEAVDAEIKRILSDSYERAKAILRKHTREHKALAEALLKYETLDADDIKAILNESQT
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ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region. Plays an important role in regulating mitochondrial morphology and function by cleaving Opa1, giving rise to a form of Opa1 that promotes maintenance of normal mitochondrial structure and mitochondrial protein metabolism. Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins. Required to control the accumulation of nonassembled respiratory chain subunits such as ND-30.
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F4HPR5
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DRP5A_ARATH
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Dynamin-related protein 5A (Protein ARC5-like)
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MANSNTYLTTPTKTPSSRRNQQSQSKMQSHSKDPINAESRSRFEAYNRLQAAAVAFGEKLPIPEIVAIGGQSDGKSSLLEALLGFRFNVREVEMGTRRPLILQMVHDLSALEPRCRFQDEDSEEYGSPIVSATAVADVIRSRTEALLKKTKTAVSPKPIVMRAEYAHCPNLTIIDTPGFVLKAKKGEPETTPDEILSMVKSLASPPHRILLFLQQSSVEWCSSLWLDAVREIDSSFRRTIVVVSKFDNRLKEFSDRGEVDRYLSASGYLGENTRPYFVALPKDRSTISNDEFRRQISQVDTEVIRHLREGVKGGFDEEKFRSCIGFGSLRDFLESELQKRYKEAAPATLALLEERCSEVTDDMLRMDMKIQATSDVAHLRKAAMLYTASISNHVGALIDGAANPAPEQWGKTTEEERGESGIGSWPGVSVDIKPPNAVLKLYGGAAFERVIHEFRCAAYSIECPPVSREKVANILLAHAGRGGGRGVTEASAEIARTAARSWLAPLLDTACDRLAFVLGSLFEIALERNLNQNSEYEKKTENMDGYVGFHAAVRNCYSRFVKNLAKQCKQLVRHHLDSVTSPYSMACYENNYHQGGAFGAYNKFNQASPNSFCFELSDTSRDEPMKDQENIPPEKNNGQETTPGKGGESHITVPETPSPDQPCEIVYGLVKKEIGNGPDGVGARKRMARMVGNRNIEPFRVQNGGLMFANADNGMKSSSAYSEICSSAAQHFARIREVLVERSVTSTLNSGFLTPCRDRLVVALGLDLFAVNDDKFMDMFVAPGAIVVLQNERQQLQKRQKILQSCLTEFKTVARSL
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Probable microtubule-associated force-producing protein that is targeted to the forming cell plate during cytokinesis. May play a role in cell division.
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F4HPZ9
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LIG6_ARATH
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DNA ligase 6 (AtLIG6) (DNA ligase VI) (EC 6.5.1.1) (Ligase 1)
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MASDSAGATISGNFSNSDNSETLNLNTTKLYSSAISSISPQFPSPKPTSSCPSIPNSKRIPNTNFIVDLFRLPHQSSSVAFFLSHFHSDHYSGLSSSWSKGIIYCSHKTARLVAEILQVPSQFVFALPMNQMVKIDGSEVVLIEANHCPGAVQFLFKVKLESSGFEKYVHTGDFRFCDEMRFDPFLNGFVGCDGVFLDTTYCNPKFVFPSQEESVGYVVSVIDKISEEKVLFLVATYVVGKEKILVEIARRCKRKIVVDARKMSMLSVLGCGEEGMFTEDENESDVHVVGWNVLGETWPYFRPNFVKMNEIMVEKGYDKVVGFVPTGWTYEVKRNKFAVRFKDSMEIHLVPYSEHSNYDELREFIKFLKPKRVIPTVGVDIEKFDCKEVNKMQKHFSGLVDEMANKKDFLLGFYRQSYQKNEKSDVDVVSHSAEVYEEEEKNACEDGGENVPSSRGPILHDTTPSSDSRLLIKLRDSLPAWVTEEQMLDLIKKHAGNPVDIVSNFYEYEAELYKQASLPTPSLNNQAVLFDDDVTDLQPNPVKGICPDVQAIQKGFDLPRKMNLTKGTISPGKRGKSSGSKSNKKAKKDPKSKPVGPGQPTLFKFFNKVLDGGSNSVSVGSETEECNTDKKMVHIDASEAYKEVTDQFIDIVNGSESLRDYAASIIDEAKGDISRALNIYYSKPREIPGDHAGERGLSSKTIQYPKCSEACSSQEDKKASENSGHAVNICVQTSAEESVDKNYVSLPPEKYQPKEHACWREGQPAPYIHLVRTFASVESEKGKIKAMSMLCNMFRSLFALSPEDVLPAVYLCTNKIAADHENIELNIGGSLISSALEEACGISRSTVRDMYNSLGDLGDVAQLCRQTQKLLVPPPPLLVRDVFSTLRKISVQTGTGSTRLKKNLIVKLMRSCREKEIKFLVRTLARNLRIGAMLRTVLPALGRAIVMNSFWNDHNKELSESCFREKLEGVSAAVVEAYNILPSLDVVVPSLMDKDIEFSTSTLSMVPGIPIKPMLAKIAKGVQEFFNLSQEKAFTCEYKYDGQRAQIHKLLDGTVCIFSRNGDETTSRFPDLVDVIKQFSCPAAETFMLDAEVVATDRINGNKLMSFQELSTRERGSKDALITTESIKVEVCVFVFDIMFVNGEQLLALPLRERRRRLKEVFPETRPGYLEYAKEITVGAEEASLNNHDTLSRINAFLEEAFQSSCEGIMVKSLDVNAGYCPTKRSDSWLKVKRDYVDGLGDTLDLVPIGAWYGNGRKAGWYSPFLMACFNPETEEFQSVCRVMSGFSDAFYIEMKEFYSEDKILAKKPPYYRTGETPDMWFSAEVVWEIRGADFTVSPVHSASLGLVHPSRGISVRFPRFISKVTDRNPEECSTATDIAEMFHAQTRKMNITSQH
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DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair (Probable). Required to maintain seed viability (e.g. longevity and storability) and during seed germination, probably by repairing DNA damage accumulated during seed development, storage and/or imbibition. Facilitates seed germination in cold conditions (2 degrees Celsius) and under oxidative stress (e.g. menadione, a genotoxic agent). Involved in repair of X-ray-induced damage.
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F4HQ84
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COG3_ARATH
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Conserved oligomeric Golgi complex subunit 3 (COG complex subunit 3) (Component of oligomeric Golgi complex 3)
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MATKAASSSSLPKSGAISKGYNFASTWEQSAPLTEQQQAAIVSLSHAVAERPFPANLVHEHVHRPENGLSVSVEDTHLGDSGAIEAVLVNTNQFYKWFTDLESAMKSETEEKYRHYVSTLTERIQTCDNILHQVDETLDLFNELQLQHQGVTTKTKTLHDACDRLLMEKQKLMEFAEALRSKLNYFDELENVSSNFYSPNMNVSNSNFLPLLKRLDECISYIEDNPQYAESSVYLLKFRQLQSRALGMIRTYILAVLKTAASQVQAAFRGTGGNKTSVSEGVEASVIYVRFKAAANELKPVLEEIESRSARKEYVQILAECHRLYCEQRLSLVKGIVHQRVSDFAKKEALPSLTRSGCAYLMQVCHMEHQLFTHFFPASSEEVSSLAPLVDPLSTYLYDILRPKLIHEANIDLLCELVHILKVEVLGDQSARQSEPLAGLRPTLQRILADVNERLTFRARTYIRDEIANYTPSDEDLDYPAKLEGSPNTTSETDLRDDENADVFKTWYPPLEKTLSCLSKLYRCLEQAVFTGLAQEAVEVCSLSIQKASKLIIKRSTTMDGQLFLIKHLLILREQIAPFDIEFSVTHKELDFSHLLEHLRRILRGQASLFDWSRSTSLARTLSPRVLESQIDAKKELEKCLKTTCEEFIMSVTKLVVDPMLSFVTKVTAIKVALSSGTQNHKVDSVMAKPLKEQAFATPDKVVELVQKVYAAIQQELLPILAKMKLYLQNPSTRTILFKPIKTNIVEAHTQVESLLKAEYSAEEQANINMISIQDLQTQLDNFL
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Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. Involved in pollen tube growth by modulating Golgi morphology and vesicle trafficking homeostasis leading to the deposition of cell wall components and proteins at the pollen tube tip. Required for sporophytic development.
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F4HQA1
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PAF1_ARATH
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Protein PAF1 homolog (Protein EARLY FLOWERING 7) (Protein VERNALIZATION INDEPENDENCE 2)
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MASYRPPYPPLPQPPSQNSLAPPPPPPSLPPPVPPPPPSHQPYSYPPPPPPPPHAYYQQGPHYPQFNQLQAPPPPPPPSAPPPLVPDPPRHQGPNDHEKGASKQVGRRERAKPDPSKHHHRSHLPHSKKIETEEERRLRKKRELEKQRQDEKHRQQMKNSHKSQMPKGHTEEKKPTPLLTTDRVENRLKKPTTFICKLKFRNELPDPSAQLKLMTIKRDKDQFTKYTITSLEKLWKPKIFVEPDLGIPLDLLDLSVYNPPKVKAPLAPEDEELLRDDDAVTPIKKDGIRRKERPTDKGMSWLVKTQYISSINNESARQSLTEKQAKELREMKGGINILHNLNNRERQIKDIEASFEACKSRPVHATNKNLQPVEVLPLLPYFDRYDEQFVVANFDGAPIADSEFFGKLDPSIRDAHESRAILKSYVVAGSDTANPEKFLAYMVPSLDELSKDIHDENEEISYTWVREYLWDVQPNANDPGTYLVSFDNGTASYLPLPMRLNLRKKRAREGRSSDEIEHFPVPSRVTVRRRSTVSVIEHKDSGVYSSRVGASSSKMRRLEDEGGLGRSWKHEPEQDANQYSDGNEDDYSE
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Component of the PAF1 complex (PAF1C) which is involved in histone modifications such as methylation on histone H3 'Lys-4' (H3K4me3). Involved in regulation of flowering time. Required for the expression of the flowering repressors and MAD-box genes FLC, AGL27/FLM and AGL31/MAF2. Required for histone H3 trimethylation on 'Lys-4' H3K4me3 at the FLC and AGL27/FLM loci. Involved in the control of seed dormancy and germination.
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F4HQE2
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RTEL1_ARATH
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Regulator of telomere elongation helicase 1 homolog (EC 3.6.4.12)
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MGFTVVSRSGSPTRRENQKRRVCFRLLLRLLRRGFVVLSAESDPKMPNYSIRGINVEFPFEAYQSQIIYMDRVIESLQNKCHALLESPTGTGKTLCLLCATLAWRKSLGSFSTRKDRKNSAIPWSDSDEPLSQSGGGGGGAFPTIVYASRTHSQLRQVIKELKRSSYRPKMVVLGSREQLCVNEEVNSLRGKALTNACQYLCKKRGKRQCNHFNRLPDYLKHNPHIGDEPVDIEDLVNIGKDSGPCPYYITRELHKDVDIIFAPYNYLISNGYRKFLKVNWTNSVLIFDEAHNLESLCADSASFDLPSVLLSACISEAQECVQLAAARRDSLNDVSINPENFAILKGLLLKLQELISKVPIPKRDEGFTKPGPYIYEMLKSLNITHETAPKLIGTVEEAAVFLEEEKQRTATNAGSKLEIIADMLKLIFRENGSNHADVYRVHVQELEQNSTDVMKGKVSRTLSWWCFSPGITMLDIAQKGVGSIILTSGTLSPMDSLAQELKLDFPIRLENPHVISSNQLWAGVVSTGPSGYVLNSSYRNRDVPEYKQELGNAIVNFSRVVPEGLLIFFPSYYLMDSCITFWKNGCYRNSMTVWERICKLKKPVIEPKDSSLFPAAMRDFSEKLQDRATSGVVFFAVCRGKVSEGLDFADGAGRAVVITGLPYARVTDPRVKLKREFLDEQSQLADVKLPRSTLLSGSMWYSQEAARAVNQAIGRVIRHRHDYGAIIFCDDRFEQPSQQSKISLWIRPNVKCYSRYGEVISDLARFFRTERSNFPARLVTEQENNIVSTLLPVESIEDNPTPAFGNSNLKNVGVAQNELSRLEAFPPANRASPLERDGNNVKRNGLTILKHTGKIPRIVKGDVMQGCSSRKAKLVELSDDEETPVERRCEVVDLESDNCETQTCVTEVLASSTCLNTMGLKKKRKVPESQGSASSSVLTAKGNGGGDKKEASASAFLSQVKEKLNTEEYKKFIGYMQALKKKEIKLANVMQSIVQLFCGSERDHLLMGFKDFVPVKYRPAYEECIKTRKRQSIIFGNSN
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ATP-dependent DNA helicase implicated in DNA replication, DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates. Also plays a role in preserving the stability of 45S rDNA repeats.
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F4HQM3
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NCER1_ARATH
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Neutral ceramidase 1 (AtNCER1) (N-CDase 1) (NCDase 1) (EC 3.5.1.23) (Acylsphingosine deacylase 1) (N-acylsphingosine amidohydrolase 1)
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MELSLVRLWNTCFPSFFYISTVLFLLTGGGVYSHSEYLIGLGSYDITGPAADVNMMGYANMEQVASGIHFRLRARTFIVSEPQGKRVVFVNLDACMASQIVKLKVIERLKARYGDLYTEQNVGISGIHTHAGPGGYLQYVVYIVTSLGFVRQSFDALVDGIENSIIQAHENLRPGSIFLNNGELLDAGVNRSPSAYLNNPSKERSKHKYNVDKEMTLLKFVDDQWGPVGSFNWFATHGTSMSRTNSLISGDNKGAASRFMEDWYEQNTAERSYSEEFISDEIPRRVSSLIENHQDSHHELLELASYFESQPGKPVTRISSSARRVRSALRKADKPGFVSAFCQTNCGDVSPNVLGAFCLDTGLPCDFNHSTCGGKNEMCYGRGPGYPDEFESTRIIGERQFKMALELFNKASEQLQGKVDYRHVYVDFSQLNVTLPKKDGKSEVVKTCPAAMGFAFAAGTTDGPGAFDFTQGDDKGNPFWRLVRNVLKTPDKKQIDCHYPKPILLDTGEMTKPYDWAPSILSLQVLRIGQLFILSVPGEFTTMAGRRLRYAVKTQLKNSGNKDLSGEIHVVIAGLANGYSQYVTTFEEYQVQRYEGASTLYGPHTLSGYIQEFKKLSKSLVLDMPVQPGPQPPDLLDKQLSFLTPVMMDTTPSGDSFGDVISDVPKNLSLKRGNGQVTVVFRSACPRNDLLTEGTFTLVERLEQKDKTWTPVYDDDDLCLRFKWSRHKKLSSRSQATVEWRIPESASPGVYRITHFGAAKKLFGSVHHFTGSSSAFVVT
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Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid. Regulates sphingolipid homeostasis. Promotes oxidative stress resistance.
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F4HRI2
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HEI10_ARATH
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E3 ubiquitin-protein ligase CCNB1IP1 homolog (EC 2.3.2.27) (RING finger-containing protein HEI10) (RING-type E3 ubiquitin transferase HEI10)
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MRCNACWRDLEGRAISTTCGHLLCTEDASKILSNDGACPICDQVLSKSLMKPVDINPNEEWINMAMAGISPQILMKSAYRSVMFYIAQRDLEMQYKMNRVVAQCRQKCEGMQAKFSEKMEQVHTAYQKMGKRCQMMEQEVENLTKDKQELQEKFSEKSRQKRKLDEMYDQLRSEYESVKRTAIQPANNFYPRHQEPDFFSNPAVNMMENRETIRKDRSFFSPATPGPKDEIWPARQNSSNSGPFDISTDSPAIPSDLGNRRAGRGHPVYGGGGTANPQSTLRNLILSPIKRSQLSRSRPQLFTL
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Ubiquitin E3 ligase required for class I crossover (CO) formation during meiosis.
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F4HRT5
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CRWN1_ARATH
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Protein CROWDED NUCLEI 1 (Protein KAKU2) (Protein LITTLE NUCLEI 1)
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MSTPLKVWQRWSTPTKATNPDSNGSSHGTGLDMVTPVSGRVSEIQFDDPRILPEKISELEKELFEYQHSMGLLLIEKKEWSSQYEALQQAFEEVNECLKQERNAHLIAIADVEKREEGLRKALGIEKQCALDLEKALKELRAENAEIKFTADSKLTEANALVRSVEEKSLEVEAKLRAVDAKLAEVSRKSSDVERKAKEVEARESSLQRERFSYIAEREADEATLSKQREDLREWERKLQEGEERVAKSQMIVKQREDRANESDKIIKQKGKELEEAQKKIDAANLAVKKLEDDVSSRIKDLALREQETDVLKKSIETKARELQALQEKLEAREKMAVQQLVDEHQAKLDSTQREFELEMEQKRKSIDDSLKSKVAEVEKREAEWKHMEEKVAKREQALDRKLEKHKEKENDFDLRLKGISGREKALKSEEKALETEKKKLLEDKEIILNLKALVEKVSGENQAQLSEINKEKDELRVTEEERSEYLRLQTELKEQIEKCRSQQELLQKEAEDLKAQRESFEKEWEELDERKAKIGNELKNITDQKEKLERHIHLEEERLKKEKQAANENMERELETLEVAKASFAETMEYERSMLSKKAESERSQLLHDIEMRKRKLESDMQTILEEKERELQAKKKLFEEEREKELSNINYLRDVARREMMDMQNERQRIEKEKLEVDSSKNHLEEQQTEIRKDVDDLVALTKKLKEQREQFISERSRFLSSMESNRNCSRCGELLSELVLPEIDNLEMPNMSKLANILDNEAPRQEMRDISPTAAGLGLPVTGGKVSWFRKCTSKMLKLSPIKMTEPSVTWNLADQEPQSTEQANVGGPSTTVQAATTYSFDVQKAESETGTKEVEVTNVNSDGDQSDINSKAQEVAADSLSNLDVDGQSRMKGKGKARTRRTRSVKDVVDDAKALYGESINLYEPNDSTENVDDSTKASTGETGRSDKAISKNGRKRGRVGSLRTCTTEQDGNESDGKSDSVTGGAHQRKRRQKVASEQQGEVVGQRYNLRRPRRVTGEPALSKKNEDIGGVQQEEGIHCTQATATASVGVAVSDNGVSTNVVQHEATADSEDTDAGSPKRTDESEAMSEDVNKTPLRADSDGEDDESDAEHPGKVSIGKKLWTFLTT
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Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (By similarity). Required for nucleus structure organization (e.g. size and shape).
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F4HRV8
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ASY1_ARATH
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Meiosis-specific protein ASY1 (Protein ASYNAPTIC 1) (AtASY1)
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MVMAQKLKEAEITEQDSLLLTRNLLRIAIFNISYIRGLFPEKYFNDKSVPALDMKIKKLMPMDAESRRLIDWMEKGVYDALQRKYLKTLMFSICETVDGPMIEEYSFSFSYSDSDSQDVMMNINRTGNKKNGGIFNSTADITPNQMRSSACKMVRTLVQLMRTLDKMPDERTIVMKLLYYDDVTPPDYEPPFFRGCTEDEAQYVWTKNPLRMEIGNVNSKHLVLTLKVKSVLDPCEDENDDMQDDGKSIGPDSVHDDQPSDSDSEISQTQENQFIVAPVEKQDDDDGEVDEDDNTQDPAENEQQLARVKDWINSRHLDTLELTDILANFPDISIVLSEEIMDQLVTEGVLSKTGKDMYIKKRDKTPESEFTFVKEEADGQISPGKSVAPEDYLYMKALYHSLPMKYVTITKLHNMLDGEANQTAVRKLMDRMTQEGYVEASSNRRLGKRVIHSSLTEKKLNEVRKVLATDDMDVDVTETINKTNGPDAKVTADVSTCGGIHSIGSDFTRTKGRSGGMQQNGSVLSEQTISKAGNTPISNKAQPAASRESFAVHGGAVKEAETVNCSQASQDRRGRKTSMVREPILQYSKRQKSQAN
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Required for normal meiosis in male and female gametophytes. Plays a crucial role in coordinating the activity of DMC1, a key member of the homologous recombination machinery. Acts at the interface between the developing chromosome axes and the recombination machinery to ensure DMC1-mediated interhomolog recombination.
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F4HS99
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REC1_ARATH
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Protein REDUCED CHLOROPLAST COVERAGE 1
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MAPKNNRGKTKGDKKKKEEKVLPVIVDVIVNLPDETEAILKGISTDRIIDVRRLLSVNFDTCHVTNYSLSHEIRGSRLKDTVDVSALKPCVLTLTEEDYNEGTAVAHVRRLLDIVACTTCFGPSPEKSDSVKSAQVKGGGKNSKQSDTSPPPSPASKDTVVDEAGETSHSFPKLGSFYEFFSLAHLTPPLQYIRLATKRETEDIAKEDHLLSIDVKLCNGKLVHIEGCRKGFYSIGKQRIICHNLVDLLRQISRAFDNAYSDLLKAFSERNKFGNLPYGFRANTWLIPPTAAQSPAAFPPLPVEDERWGGDGGGQGRDGSYDLVPWSNEFAFIASMPCKTAEERQVRDRKVFLLHNLFVDVATFRAIKAVQKVMAEPVLAEEDSEVLYSETVRDLTVTVTRDTSNASSKVDTKIDGIQATGLDKKKLMERNLLKGLTADENTAAHDVATLGTISLKYCGYIAVVKLEKESEELSPPSQIVDLLEQPEGGANALNINSLRFLLHKSSPEQNKKTPQQHDDELTSSREFVSKMLEESIAKLEGEEIDRDSIMRWELGACWIQHLQDQKNTEKDKKQTGEKSKNELKVEGLGKPLKSLNSSKKKTDVSSPKTPQTALSSQVDAVSSEADTAASLQSDAEKNAQENVLILKNLLSDAAFTRLKESDTGLHHKSLQELVDLAQNYYTEVAIPKLVADFGSLELSPVDGRTLTDFMHTRGLRMRSLGYVVKLSDKLSHVQSLCVHEMIVRALKHILQAVISAVATDTDKIAIKVAAALNMMLGIPENVAATPHNPWNVHPLIFRWLEKFLKKRYDYDLNAFSYKDLRKFAILRGLCHKVGIELIPRDFDMDSPAPFRKTDVVSLVPVHKTFYFKSMQQAACSSADGRQLLESSKTALDKGKLEDAVTYGTKALAKLVAVCGPYHRMTAGAYSLLAVVLYHTGDFNQATIYQQKALDINERELGLDHPDTMKSYGDLAVFYYRLQHTELALKYVKRALYLLHLTCGPSHPNTAATYINVAMMEEGLGNVHVALRYLHKALKCNQRLLGPDHIQTAASYHAIAIALSLMEAYHLSVQHEQTTLRILRAKLGPDDLRTQDAAAWLEYFESKAFEQQEAARNGTPKPDASIASKGHLSVSDLLDYINPSHNAKGKESVAAKRKNYILKLKEKSKQSNVSEHLVEIPREKQKEMSEEDTEETGSEEGKSSEENHETILAPVEEPPSPPVIEDATMDNSNPITSSDVSTEPQHPDGSEDGWQPVQRPRSAGSYGRRMKQRRASIGKVYTYQKKNVEADIDNPLFQNATQQNDKYYILKKRTASYSSYADHHSPGLTTQGTKFGRKIVKTLAYRVKSTQPSSGNAKTAGETSEEDGLKTDASSVEPPTLSSTVQSEAYHTKNSVVSLGKSPSYKEVALAPPGSIAKYQVWVPQAEVSDKQEDDEMEKKTEQGTSMELTRDEQMITGLEEEVKKEISADPESNITQGEEEIKVELQPSEGVLGGSHINENDESGGGIQVEEQVEVELINDGVTDMIHSTREQQVIDQLAADSEDLKAKLSISTTDSGDASRGLLPNKKLSASAAPFNPSSPPSIIRPTPIGMNIGPSWPVNMTLHHGPPPPYPSPPTTPNLMQPMSFVYPPPYSQSVPTSTYPVTSGPFHPNQFPWQLNVSDFVPRTVWPGCHPVEFPPPHMITEPIAATVLEPTVILPTDIDTSGVEETKEGTQDVAVADEVMDSVNHVNNAVARSETENGNRKSEEGEKTFSILLRGRRNRKQTLRMPISLLNRPYDSQPFKLGYSRVIRDSEAPKSVA
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May act as the scaffold of a protein complex, which sequesters key factors that are required for the G2 to M transition in meristematic tissues (By similarity). Together with REC2, REC3 and FMT/CLU, contributes to the establishment of the cellular volume devoted to the chloroplast compartment.
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F4HT77
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RBA1_ARATH
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Disease resistance protein RBA1 (NAD(+) hydrolase RBA1) (EC 3.2.2.6) (NADP(+) hydrolase RBA1) (EC 3.2.2.-) (Response to HopBA1 protein) (RBA1)
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MTSVSPRYRNVPVPKVFLSFRGEEIRHGFISHLADALERYGIMFIIDKDEQRGNDLTSLLLRIKESKVALVIFSSRFAESRFCMDEIVKMKECVDERKLLVIPIFYKVRARDVSGRTGDFGKKFWALAQKSRGCQIKEWMEALECISNKMGLSLGDGRSEADFIKEIVKEVERVLATFTSEDTEDHHCQTVKLLKGLVVGCLAHQELPLVLVFTQVYYYVKFSIFFIEEIFSSCFRKGFVLKPCKEDLQINSISIPGIDLENFKNMMQQAMYELNQMLLQSLGNIDPHRDVAFENQPQDQPDSPIALPEERRVALEATKFCGHAAYWWNQTKTTRARIGKVLIHFWEKLKKKFKDTYDRTVRI
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Disease resistance (R) protein that specifically recognizes the HopBA1 type III effector protein from P.syringae, and triggers cell death. Acts as a NAD(+) hydrolase (NADase): in response to pathogen-recognition, catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide NAD(+) cleavage triggering a defense system that promotes cell death. In addition to ADPR, also generates a cyclization variant of cyclic ADPR (cADPR), termed v-cADPR, for which the cyclizing bond is unknown. Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules.
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F4HTH8
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KTN82_ARATH
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Katanin p80 WD40 repeat-containing subunit B1 homolog KTN80.2 (DDB1 binding WD40 hypersensitive to ABA 3) (DWD hypersensitive to ABA 3)
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MAKRGYKLQEFLAHSANVNCLSIGKKTSRLFITGGDDYKVNLWAIGKPTSLMSLCGHTSAVDSVAFDSAEVLVLAGASSGVIKLWDVEEAKMVRAFTGHRSNCSAVEFHPFGEFLASGSSDANLKIWDIRKKGCIQTYKGHSRGISTIRFTPDGRWVVSGGLDNVVKVWDLTAGKLLHEFKFHEGPIRSLDFHPLEFLLATGSADRTVKFWDLETFELIGSTRPEATGVRSIKFHPDGRTLFCGLDDSLKVYSWEPVVCHDGVDMGWSTLGDLCISEGKLLGCSYYQNSVGIWVSDISQIEPYGIGSADKKECVEKILSALDDQSFDRIKSTPRRSSSPDYETKEIKNIYIDSTGGNSAVAHKSGSLSTPATSTGQAGDNKSLVVHSVVPRDSDIGKDSSDSGKESITFSKTKPGMLLRPAYVRKTPTKFDETKKQSVAVGYLKKSGLDGEKKLDTETAFDSEMSGRNPYDADDSIIKSITNKFEQALLPESPTDEAKCMLLKPPRVQRSPSTKYNEARWATSTDSGALDSKKNGLESSRDMDLPTGLRDDRGSNPCEEDIENKSISSRSERVLSPEKAGDELKSLESPGGSKESKSVKVVRGVKVVSGRTRSLVERFERGEKITHSEDKAASATVVHSSNSVEEEPLTASVQTVSMMPTQVMPVKLDQATNSTTVDVPVLSTRRTKSTPVRVMPVVLGRDTSMATDTPPVTSTRPDRTSATNLTSDVSGVTSKRQTRTSPAPVMPMILNQTTKMKSDEPSITSTWPDRTSATDLTSDVSGVISSRQTRTSPAPVMPMKLNQKTKIKSDEPPITSTRPDRPSATNLTSDESPVTSTRQAKTSPAPVTPVILNQRQTTNMKSDEPPVISTRPLRTSSARVMPVILNQASTTYDERPLSSSRSARTSPARIMPMKLNQADNMPSYEPPVALTRSARNSPARVIPVKLNQATNVTADASHIRSRQRFSPTQTLATPAVFDQVTDMTLDETTKTQQSSDILTQKEEPQISGREDDGDIWEILMRTHSEVLNTLQSRLTKLQIVRHFWERSDIKGAIAALRKLSDHSVQADVINILTDKTEILTLDLFSQLAPVLTGLLGSKTERPVNVSLEMLLKLVAVFGTVIQSTVSARRVVGVDLHAEERLQICQSCSAELQKVQKILPLLTRRGGLIARKAQELNLVLQTP
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May participate in a complex which severs microtubules in an ATP-dependent manner (By similarity). Microtubule severing may promote rapid reorganization of cellular microtubule arrays (By similarity). Confers precision to microtubule (MT) severing by specific targeting of KTN1 to MT cleavage sites such as crossover or branching nucleation sites. Together with other KTN80s, regulates cell elongation by modulating MT organization. Negative regulator of abscisic acid (ABA) responses. May function as a substrate receptor for cullin-RING ubiquitin ligase 4 complexes (CRL4), a family of E3 ligases involved in protein degradation. {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:21421380, ECO:0000269|PubMed:28978669}.
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F4HTM3
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GCS1_ARATH
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Mannosyl-oligosaccharide glucosidase GCS1 (EC 3.2.1.106) (Alpha-glucosidase 1) (Glucosidase 1) (Protein KNOPF) (Protein MUNCHKIN)
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MTGASRRSARGRIKSSSLSPGSDEGSAYPPSIRRGKGKELVSIGAFKTNLKILVGLIILGIIVIYFVINRLVRHGLLFDESQKPRVITPFPAPKVMDLSMFQGEHKESLYWGTYRPHVYFGVRARTPLSLVAGLMWLGVKDEMYVMRHFCENSDDLSTFGWREHNGRDYGRQELVENDMVIETSFVKSKGDGLGYGGDWAVRIDVKNKGLNDDVKRSAHLFFYLADEGGNVLNLGQDGLDFQGSSLLVSGSREDVGDWQIHLKSQNQLETHYSGFKTPHIYNLSDLVQQNLALQARKFGRLQLSDTSEDSSNIYIFQISGRLPFTIDIPFISGIKGESSNVEKRLTSLTGLPLSDLLKKKHQEFDAKFNECFKLSEKHDSETLGVGRTAIANMLGGIGYFYGQSKIYVPKSTQPGSRDNFLLYWPAELYTAVPSRPFFPRGFLWDEGFHQLLIWRWDIRITLDIVGHWLDLLNIDGWIPREQILGAEALSKVPEEFVVQYPSNGNPPTLFLVIRDLIDAIRMEKFVASEKDEVLSFLERASVRLDAWFQWFNTSQKGKEIGSYFWHGRDNTTTQELNPKTLSSGLDDYPRASHPSEDERHVDLRCWMYLAADCMHSITELLGKEDKLSKENYNSTVKLLSNFNLLNQMHYDSDYGAYFDFGNHTEKVKLIWKEVIQENGQLSRQLVRKTFGKPKLKLVPHLGYVSFFPFMSRIIPPDSPILEKQLDLISNRSILWSDYGLVSLAKTSSMYMKRNTEHDAPYWRGPIWMNMNYMILSSLYHYSIVDGPYREKSKAIYTELRSNLIRNVVRNYYETGYIWEQYDQVKGTGKGTRLFTGWSALTLLIMSEDYPIF
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Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor. Required for the accumulation of seed storage proteins, the formation of protein bodies, cell differentiation, cellulose biosynthesis and organization (in cell walls), cell shape determination and organization (e.g. epidermal cells), and embryo development. Involved in root development.
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F4HU51
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ACH2_ARATH
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Acyl-CoA hydrolase 2 (AtACH2) (EC 3.1.2.20) (Acyl-CoA thioesterase II) (ACT-II) (Hexadecanoyl-CoA hydrolase ACH2) (EC 3.1.2.2)
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MNTESVVEFLGNVPLLQKLPSSSLKKIAQVVVPKRYGKGDYVVREDQTWDGCYFILQGEAQVSGPDEEDNRSEFLLKQYDYFGVGLSGNVHSADIVAMSQLTCLVLPRDHCHLLETNSIWQSDTSLDKCSLVERILQLDPLELNIFRGITLPDAPIFGKVFGGQFVGQALAAASKTVDFLKVVHSLHSYFLLVGDIDIPIIYQVHRIRDGNNFATRRVDAVQKGNIIFILLASFQKEQQGFEHQESTMPSVPDPDTLLSLEELRESRITDPHLPRSYRNKVATRNFVPWPIEIRFCEPSNSTNQTKSPPRLNYWFRAKGRLSDDQALHRCVVAFASDLIFCGVGLNPHRRKGVKSAALSLDHAMWFHRPLRADEWLLYVIVSPTAHETRGFVTGQMFNRKGELVVSLTQEALLREARPPKPSGTSKL
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Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Active with both medium chain and long chain acyl-CoAs (e.g. 12:0-CoA, 14:0-CoA, 16:0-CoA, 18:0-CoA, 16:1-CoA, 18:1-CoA, 18:2-CoA and 20:4-CoA) as substrates, palmitoleoyl-CoA (16:1-CoA) being the favorite substrate.
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F4HU55
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BSK4_ARATH
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Serine/threonine-protein kinase BSK4 (EC 2.7.11.1) (Brassinosteroid-signaling kinase 4)
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MGGQSSKIGTCCSHKTTALEAPDVENKENGEVNGVHSFREYSLEQLKIATSCFALENVVSEHGETAPNVVYQGKLENHMKIAIKRFSGTAWPDPRQFLEEARLVGQLRSKRMANLLGYCCEGGERLLVAEFMPNETLAKHLFHWDTEPMKWAMRLRVALYISEALEYCSNNGHTLYHDLNAYRVLFDEECNPRLSTFGLMKNSRDGKSYSTNLAFTPPEYLRTGRITAESVIYSFGTLLLDLLTGKHIPPSHALDLIRDRNLQTLTDSCLEGQFSDSDGTELVRLTSCCLQYEARERPNIKSLVTALISLQKDTEVLSHVLMGLPQSGTFASPPSPFAEACSGKDLTSMVEILEKIGYKDDEDLSFMWTEQMQEAINSKKKGDIAFRRKDFSEAIEFYTQFLDLGMISATVLVRRSQSYLMSNMAKEALDDAMKAQGISPVWYVALYLQSAALSVLGMEKESQIALTEGSILEARKISASTQN
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Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1. Functions redundantly with BSK3, BSK6, BSK7 and BSK8.
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F4HU58
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TAD1_ARATH
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tRNA-specific adenosine deaminase TAD1 (AtTAD1) (EC 3.5.4.34) (tRNA-specific adenosine-37 deaminase TAD1)
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MEEDWGKTVSEKVISAYMSLPKKGKPQGREVTVLSAFLVSSPSQDPKVIALGTGTKCVSGSLLSPRGDIVNDSHAEVVARRALIRFFYSEIQRMQLTSGKSNEAKRQRIDSETSSILESADSSCPGEVKYKLKSGCLLHLYISQLPCGYASTSSPLYALKKIPSTQVDDSLLVQASDICSSRHSDVPEIGSNSNKGNGSQVADMVQRKPGRGETTLSVSCSDKIARWNVLGVQGALLYQVLQPVYISTITVGQSLHSPDNFSLADHLRRSLYERILPLSDELLTSFRLNKPLFFVAPVPPSEFQHSETAQATLTCGYSLCWNYSGLHEVILGTTGRKQGTSAKGALYPSTQSSICKQRLLELFLKETHGHKRESSKSKKSYRELKNKATEYYLMSKIFKGKYPFNNWLRKPLNCEDFLIN
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Involved in RNA editing. Catalyzes the specific deamination of adenosine-37 in the cytosolic tRNA-Ala. Generates inosine at the position 3'-adjacent to the anticodon tRNA-Ala.
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F4HVA6
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TAF6B_ARATH
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Transcription initiation factor TFIID subunit 6b (TBP-associated factor 6b) (AtTAF6b)
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MVTKESIEVIAQSIGLSTLSPDVSAALAPDVEYRVREVMQVYHQLQLYFCPLISSLTCRRNLQEAIKCMRHARRTTLMAHDVDSALHFRNLEPTSGSKSMRFKRAPENRDLYFFDDKDVELKNVIEAPLPNAPPDASVFLHWLAIDGIQPSIPQNSPLQAISDLKRSEYKDDGLAARQVLSKDLQIYFDKVTEWALTQSGSTLFRQALASLEIDPGLHPLVPFFTSFIAEEIVKNMDNYPILLALMRLARSLLHNPHVHIEPYLHQLMPSIITCLIAKRLGRRSSDNHWDLRNFTASTVASTCKRFGHVYHNLLPRVTRSLLHTFLDPTKALPQHYGAIQGMVALGLNMVRFLVLPNLGPYLLLLLPEMGLEKQKEEAKRHGAWLVYGALMVAAGRCLYERLKTSETLLSPPTSSVWKTNGKLTSPRQSKRKASSDNLTHQPPLKKIAVGGIIQMSSTQMQMRGTTTVPQQSHTDADARHHNSPSTIAPKTSAAAGTDVDNYLFPLFEYFGESMLMFTPTHELSFFL
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TAFs are components of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. Not redundant with TAF6.
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F4HVG8
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CSK_ARATH
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Chloroplast sensor kinase, chloroplastic (EC 2.7.10.2)
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MLLSAIASQTLLSSNPNLHFSNSIPNPRPSNPSLKLLNASSSSSSSSSSSIFTRGLRYVNHTVSNEESEPGGGETMVASASAIASAIRGASTTPVEFTQMIEKDHLKTKIILPSPDFQRLCLEQLDLFRQIVDPNAVLSIYVRPAGSYVMDRLELRRVTCYPSVNAGDVVILVGNFGIPAGLRAAEASLSSQQVELVSKHRAAVFPMVKHPFVVGFLVAELPVEAEEEEEEEEEEKPHGVNQFLSPEEAYALPASANTKSPRVKLPSVKVFTEEQRSYAINISRTLAMAYVMDQKTMLLQQSSWQNNVRMSKLVEQIRGPLSTMRTLSKMLSTHTKRNQISHDIVEDLIVQGDQIKDTLEELQDAVHLTKANIVRHNEEALKKINKTHNETRRSKYEHKDPIDGSQISSTRLSLGSGLDDSEMPMPPLALAPLQMHSIRPCDISNVLLDMVETVRPLALTQQRVVELGENSASLQVAVEEPALRQALSNLIEGALLRTHVGGKVEILSTRAPAGGSLVVIDDDGPDMRYMTQMHSLTPFGAELLSENMVEDNMTWNFVAGLTVAREILESYGCVIRVISPRSSDAALGAGGTRVELWLPAFPAAVSEANEA
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Sensor kinase that senses the plastoquinone (PQ) redox state involved in stoichiometry adjustment of both photosystems (e.g. long-term adaptation via transcriptional regulation of reaction center genes of photosystems I and II) and state transitions (e.g. short-term adaptation involving reversible post-translational phosphorylation of light-harvesting complex II, LHC II), thus linking photosynthesis with gene expression in chloroplasts. Autophosphorylates, probably on a tyrosine residue. Probably phosphorylates SIGA/SIG1 in response to plastoquinone redox state modification. Reduced PQ suppresses its autophosphorylation activity. Represses expression of a number of chloroplast-encoded genes.
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F4HVJ3
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POD1_ARATH
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Protein POLLEN DEFECTIVE IN GUIDANCE 1
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MAIRSSGRKLSFEILSQNSSFENDDTSIRRSSSDPITGNVASESPRDYGKRKRSKKKKKKVNQVETILENGDSHSTIITGSSGDFGETTTMFENRLNYYGGGGSGSSGGGCVVTLLDGQTVHHNGFNFGELRQRNVNGSVDGSNDERWSDTLSSDKKLYMEETSVELSPSENPPFQEVQHQFPRSEINGNVVRRLDTEASLDWKQLVADDPDFLSAETRSPMKYFMEEIYGGISLRSTTTPGNDIERERIYDTIFRLPWRCEVLIDTGFFVCVNSFLSLLTVMPIRVLLIFMDAFKNRQFRRPSASELSDLACFLVLATGTILLGRTDISLIYHMIRGQSTIKLYVVYNILEIFDRLCQSFCGDVFGALFSSAKGLSISPPEKLRFSTWRFVSDLALTMAASILHSFILLAQAITLSTCIVAHNNALLALLVSNNFAEIKSSVFKRFSKDNIHGLVYADSIERFHISAFLVSVLAQNILESEGAWFGNFIYNATTVFFCEMMIDIIKHSFLAKFNDIKPIAYSEFLQALCEQTLNIRPEDRKTNLTFVPLAPACVVIRVLTPVYAAHLPYSPLPWRMLWMVILFVITYIMLTSLKVLIGMGLRKHATWYINRCRRRNSSHLHND
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Probable component of the calreticulin 3 (CRT3) complex, acting probably as a co-chaperone involved in protein retention in the endoplasmic reticulum lumen. Required for micropylar pollen tube guidance. Plays an essential role in cell plate orientation or positioning in early embryo patterning.
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F4HVS0
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BTSL2_ARATH
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Zinc finger protein BRUTUS-like At1g74770
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MGGGNLHSLPPENASVSASYAVTVGNTKLSDAPVLFFVYCHKAFRAQLVELRRFATDAAEADSFSGDLAVELSRKFEFLKLVYKYHSAAEDEVIFLALDKRVKNIVSNYSLEHAGTDDLFTSIFHWLHVLEEEIGSRSDVLREVILCIGTIQSSICQHMLKEERQVFPLLIEKFSFREQASLVWQFICSVPVMVLEDFLPWMISHLSHEEKIEVENCIKDVAPNEDSLQQVISSWLLDDSQSSCGTPTEIMKGVQYVNVSKSLKKSPESHPSSGCFQRFWEWSKKSLSIPNVGRSPIHGLRLFQNAIEKDLRDIQEGLCQAKFQTLILDLDVLMARLNFLADVLVSYSNAFKKFFHPVLEEMTARRSSTAKQFNIDDCLENFQRLLYKSADDKTKTDNFLLQLQEELESLIIQVTKQFAIQRTEVFPIISKNCNHEMQKQLLYTSIHVLPLGLLKCVILWFSAHLSEEESQSILHFLSLEDSSPKKSFPRLLLQWLRFGYSGKTSVERFWKQLDVMFKVRCSCQKEHTEEASGSFSNQTQLQLCKVSKDVYPRKKDKSSTCFMSMDLAVGDMYETPYSSRMNQQMTFSGKLKPPLHLPDFFGEKNMDDPMIMDVKPIDLLFFFHKAMKMDLDYLVCGSTRLAADFRFLAEFQQRFHMIKFLYQIHSDAEDEIAFPALEAKGQLKNISHSFSIDHELETKHFDKVSFILNEMSELNMLVSTINTTAADHDRKMKYERLCLSLREICKSMHKLLSEHIQHEETELWGLFRNCFSIEEQEKIIGCMLGRISGEILQDMIPWLMESLTSDEQLAAMSLWRQATRKTMFVEWLTEWYNGHVLQEEAGEANNDPFGDSDPLEIVWKYLFEASADGEKGSMRSSLLKLPKTNFTGIMNQPPPNYKVEVGKKEEKDLERSESKKICRGSNQEGDKEQTDKMSQKVSQFGPSKKYEQLLTMSEEELVVVIKKISCDSSLDPQKKDYIKQNLLMSRWNISQRTYNLEPSSLSSNMETVHGQHPSYRDPHSLIFGCNHYKRNCKLLAPCCDKLFTCIRCHDEEADHSVDRKQITKMMCMKCLLIQPIGANCSNTSCKSSMGKYFCKICKLYDDERKIYHCPYCNLCRVGKGLGIDYFHCMKCNACMSRTLVEHVCREKCLEDNCPICHEYIFTSSSPVKALPCGHLMHSTCFQEYTCSHYTCPVCSKSLGDMQVYFKMLDALLAEEKMPDEYSNKTQVILCNDCGRKGNAPYHWLYHKCTTCGSYNSRLL
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Probable E3 ubiquitin-protein ligase that may regulate the response to iron deficiency and thus contributes to iron homeostasis.
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F4HVW5
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VAD1_ARATH
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Protein VASCULAR ASSOCIATED DEATH 1, chloroplastic
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MAMLSTASVSGSVDLPRGTMKVDSSASPEVVSDLPPSSPKGSPDRHDPSTSSPSPSRGGDNQSEVISKSEEYRQLFRLPADEILVQDFNCACQESILMQGHMYLFIHYICFYSNIFGYETKKIIPFAEISCVKRAKTAGIFPNAIEILAGGKKYFFASFLSRDEAFKLIHDGWLEYGSAVKSEGEILVTEPQVSDGVVKRARSSMDLANELDIPVRDETLHLSSSSSLPVISQNGVPPSSVQRHAEPDVDVVAANTFNWKPEDTDAPKLSSDFTKVAEAKFSIPVEEFFRLFFSDGAVSFVESFHKNCGDKEFRCTSWQPHEKLGHTRNVSFQHPIKIYFGAKFGGCQESQKFRMYRNSHLVIETSQEISDVPYADYFTVEGVWDLKRDCRDSVEGCILDVYVNVAFSKRTVWKGKIVQSTLEECREAYAHWIRMAHELLKQKKLENQEGNKLIEDGEPLAAREERVSECDEEGKVEMVGEGVVKKSLKEAWVNLTSFVKRQSGTRQVIVLAFAVILLMQVTIVVLLKKGGGGQVEYHERYDEYSVNGETLGWLEKRMHFLREEMMMVEDRLQRMRQDHAALKAQFHHLERLLRRNKQ
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Involved in ethylene- and salicylic acid-dependent cell death control associated with cells in the vicinity of vascular bundles.
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F4HVY0
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CER1_ARATH
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Very-long-chain aldehyde decarbonylase CER1 (EC 4.1.99.5) (Protein ECERIFERUM 1)
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MATKPGVLTDWPWTPLGSFKYIVIAPWAVHSTYRFVTDDPEKRDLGYFLVFPFLLFRILHNQVWISLSRYYTSSGKRRIVDKGIDFNQVDRETNWDDQILFNGVLFYIGINLLPEAKQLPWWRTDGVLMAALIHTGPVEFLYYWLHKALHHHFLYSRYHSHHHSSIVTEPITSVIHPFAEHIAYFILFAIPLLTTLLTKTASIISFAGYIIYIDFMNNMGHCNFELIPKRLFHLFPPLKFLCYTPSYHSLHHTQFRTNYSLFMPLYDYIYGTMDESTDTLYEKTLERGDDIVDVVHLTHLTTPESIYHLRIGLASFASYPFAYRWFMRLLWPFTSLSMIFTLFYARLFVAERNSFNKLNLQSWVIPRYNLQYLLKWRKEAINNMIEKAILEADKKGVKVLSLGLMNQGEELNRNGEVYIHNHPDMKVRLVDGSRLAAAVVINSVPKATTSVVMTGNLTKVAYTIASALCQRGVQVSTLRLDEYEKIRSCVPQECRDHLVYLTSEALSSNKVWLVGEGTTREEQEKATKGTLFIPFSQFPLKQLRRDCIYHTTPALIVPKSLVNVHSCENWLPRKAMSATRVAGILHALEGWEMHECGTSLLLSDLDQVWEACLSHGFQPLLLPHH
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Aldehyde decarbonylase involved in the conversion of aldehydes to alkanes. Core component of a very-long-chain alkane synthesis complex. Involved in epicuticular wax biosynthesis and pollen fertility.
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F4HW04
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DPOE1_ARATH
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DNA polymerase epsilon catalytic subunit A (EC 2.7.7.7) (DNA polymerase 2 a) (AtPOL2a) (DNA polymerase II subunit a) (Protein ABA OVERLY SENSITIVE a) (Protein EARLY IN SHORT DAYS 7) (Protein EMBRYO DEFECTIVE 142) (Protein EMBRYO DEFECTIVE 2284) (Protein EMBRYO DEFECTIVE 529) (Protein TILTED 1)
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MSGDNRRRDRKDTRWSKKPKVVNTAEDELESKLGFGLFSEGETRLGWLLTFSSSSWEDRDTGKVYSCVDLYFVTQDGFSFKTKYKFRPYFYAATKDKMELELEAYLRRRYERQVADIEIVEKEDLDLKNHLSGLQKKYLKISFDTVQQLMEVKRDLLHIVERNQAKFDALEAYESILAGKREQRPQDCLDSIVDLREYDVPYHVRFAIDNDVRSGQWYNVSISSTDVILEKRTDLLQRAEVRVCAFDIETTKLPLKFPDAEYDQIMMISYMVDGQGFLIINRECVGEDVEDLEYTPKPEFEGYFKVTNVKNEVELLQRWFYHMQELKPGIYVTYNGDFFDWPFIERRASHHGIKMNEELGFRCDQNQGECRAKFACHLDCFAWVKRDSYLPQGSHGLKAVTKAKLGYDPLEVNPEDMVRFAMEKPQTMASYSVSDAVATYYLYMTYVNPFIFSLATIIPMVPDEVLRKGSGTLCEMLLMVEAYKANVVCPNKNQADPEKFYQNQLLESETYIGGHVECLESGVFRSDIPTSFKLDSSAYQQLIDNLGRDLEYAITVEGKMRMDSISNYDEVKDEIKEKLEKLRDDPIREEGPLIYHLDVAAMYPNIILTNRLQPPSIVTDEICTACDFNRPGKTCLRKLEWVWRGVTFMGKKSDYYHLKKQIESEFVDAGANIMSSKSFLDLPKVDQQSKLKERLKKYCQKAYKRVLDKPITEVREAGICMRENPFYVDTVRSFRDRRYEYKTLNKVWKGKLSEAKASGNSIKIQEAQDMVVVYDSLQLAHKCILNSFYGYVMRKGARWYSMEMAGVVTYTGAKIIQNARLLIERIGKPLELDTDGIWCCLPGSFPENFTFKTIDMKKLTISYPCVMLNVDVAKNNTNDQYQTLVDPVRKTYKSHSECSIEFEVDGPYKAMIIPASKEEGILIKKRYAVFNHDGTLAELKGFEIKRRGELKLIKVFQAELFDKFLHGSTLEECYSAVAAVADRWLDLLDNQGKDIADSELLDYISESSTMSKSLADYGEQKSCAVTTAKRLAEFLGVTMVKDKGLRCQYIVACEPKGTPVSERAVPVAIFTTNPEVMKFHLRKWCKTSSDVGIRLIIDWSYYKQRLSSAIQKVITIPAAMQKVANPVPRVLHPDWLHKKVREKDDKFRQRKLVDMFSSANKDVVLDTDLPVTKDNVEDIEDFCKENRPSVKGPKPIARSYEVNKKQSECEQQESWDTEFHDISFQNIDKSVNYQGWLELKKRKWKVTLEKKKKRRLGDLRSSNQVDTHEINQKVGQGRGGVGSYFRRPEEALTSSHWQIIQLVPSPQSGQFFAWVVVEGLMLKIPLSIPRVFYINSKVPIDEYFQGKCVNKILPHGRPCYSLTEVKIQEDQFKKESKKRAALLADPGVEGIYETKVPLEFSAICQIGCVCKIDNKAKHRNTQDGWEVGELHMKTTTECHYLKRSIPLVYLYNSTSTGRAIYVLYCHVSKLMSAVVVDPFNGNELLPSALERQFRDSCLELSLDSLSWDGIRFQVHYVDHPEAAKKIIQRAISEYREENCGPTVAVIECPDFTFMKEGIKALDDFPCVRIPFNDDDNSYQPVSWQRPAAKIAMFRCAAAFQWLDRRITQSRYAHVPLGNFGLDWLTFTIDIFLSRALRDQQQVLWVSDNGVPDLGGINNEEAFFADEVQQTSLVFPGAYRKVSVELKIHNLAVNALLKSNLVNEMEGGGFMGFEQDVNPRGINSNDNTSFDETTGCAQAFRVLKQLIHSCLTDVRKSKNIYADSILQRLSWWLCSPSSKLHDPALHLMLHKVMQKVFALLLTDLRRLGAIIIYADFSKVIIDTVKFDLSAAKAYCESLLSTVRNSDIFEWILLEPVHYWHSLLFMDQYNYAGIRADDEISLDEVTIEPKWSVARHLPEYIERDFIIIIAKFIFDPWKFAIENKKGSSESLEAQMIEYLREQIGSTFINMLVKKVDDIMSHMKEINVSDASRVSGQAPKGDYSLEFIQVISAVLALDQNVQQDVLVMRKSLLKYIKVKECAAEAEFLDPGPSFILPNVACSNCDAYRDLDICRDPALLTEKEWSCADTQCGKIYDREQMESSLLEMVRQRERMYHMQDVVCIRCNQVKAAHLTEQCECSGSFRCKESGSEFSKRMEIFMDIAKRQKFRLLEEYISWIIYGPSY
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DNA polymerase II, which participates in chromosomal DNA replication. Required for the timing and determination of cell fate during plant embryogenesis and root pole development, by promoting cell cycle and cell type patterning. Necessary for proper shoot (SAM) and root apical meristem (RAM) functions. Involved in maintaining epigenetic states, controlling hypersensitive response (HR), and mediating abscisic acid (ABA) signaling. Required for flowering repression through a mechanism involving epigenetic gene silencing. May participate in processes involved in chromatin-mediated cellular memory.
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F4HW51
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CHR20_ARATH
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Protein CHROMATIN REMODELING 20 (AtCHR20) (EC 3.6.4.-) (ATP-dependent helicase ATRX) (Transcriptional regulator ATRX) (X-linked helicase II)
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MEANEESLKGKIEKLEGKEVIVESKEDEMDIIIEENREAEQEVMEVKARDGRGEQNDVLMEENNNQGEQKDEEMQDASSRSESSDFNSDEDEQILSRRDDELDLEKPLSEEEIDELISDLLAVESKAAEAQEALEKESLSKVESEVREELAQALRGDELDEAVAAEMMTFKDEWEATLDELETESATLLEQLDGAGIELPKLYEMIESQAPNGCYTEAWKQRAHWVGTQVTKETVESLANAERFLHTHRPVRKRHGKLLEEGASGFLEKKLADGAVKESLAGTSELDWSSLNKVFSEKRDESVSFGSKQWASVYLASTPHQAAAMGLEFPGVNEVEEIEEIDASLADPFLADAIDNERELALTEEQKTNYIRVKEEDDITCDRVLQLRLKRKRRKKRSKQVIRCAAENMDDDSVYLDGNNTTPNFAKDQVKSPETSTQVHNSEVNIEENGNFSNSDVDKMTPSTHINVDAKRDDSQNPANNFRCTACNKVAVEVHSHPLLEVIVCMDCKRSIEDRVSKVDDSLERHCEWCGHIADLIDCRTCEKLFCASCIKRNIGEEYMSEAQSSGWDCCCCSPIPLQRLTLELEKAMRDKKSIELSSDSSSDSSSDNNSVDTDADVNVTISSKKKSKKKIRRIIDDAELGKDTRTKIAIEKARQERLRSLQFSARYKTISSMGDVKSIPEGAEVEVLGDAHSGYIVNVVREIGEEAVRVPRSISAKLKVHQVTGIRFMWENIIQSISRVKSGDKGLGCILAHTMGLGKTFQVIAFLYTAMRCVDLGLKTALIVTPVNVLHNWRSEFEKWMPSEVKPLRIFMLGDVSRERRFDLLTKWRKKGGVFLMGYTNFRNLSLGRGVKDLNAARGICNALRDGPDILVCDEAHIIKNTKADTTQALKQVKCQRRIALTGSPLQNNLMEYYCMVDFVREGFLGSSPEFRNRFQNPIENGQHMNSTAEDVKIMNQRSHILYEQLKGFVQRMDMNVVKKDLPPKTVFVISVKLSPLQRILYQRFLELYGFSDGRTDERMRKNFFAAYQVLAQILNHPGIPQLRSEDSKNGRRGSIVDIPDDCSSDENIDYNMVTGEKQRTMNDLQDKVDGYLQKDWWVDLLQKNNYKVSDFSGKMILLLDILSMSADVGDKALVFSQSIPTLDLIELYLSRVPRHGKQGKFWKKGKDWYRIDGKTESSERQKLVDRFNEPDNKRVKCTLISTRAGSLGINLYAANRVIIVDGSWNPTYDLQAIFRAWRYGQKKPVFAYRLMARGTIEEKIYKRQVTKEGLAARVVDRQQVHRTISKEEMLHLFEFDDDDEKSEAVTEISKQNEAGHSNLVEQAILWTKKATLSRVGGDKLMENLLQRHGPNWISSFHEHETLLQENEEERLTKEEKDMAWEVYRRALEWEEVQRVPFSESPVVPKPSPSTQTEPLPQPKGFNRSRFVNRNCTRIAHQLTLISQGLKVGSSTVCGECGRVIRWEDVIPASKLSAVIVN
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Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3-containing nucleosomes (By similarity). Involved in DNA repair of gamma-irradiation-mediated damages.
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F4HWY6
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MYO11_ARATH
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Myosin-11 (Myosin XI E) (AtXIE)
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MRNSGTPVNIIVGSHVWIEDSDVAWIDGLVEKINGQDVEVQATNGKKITAKLSKIYPKDMEAPAGGVDDMTKLSYLHEPGVLQNLKIRYELNEIYTYTGNILIAINPFQRLPHIYDAHMMQQYKGAPFGELSPHVFAVADVAYRAMINEGKSNSILVSGESGAGKTETTKMLMRYLAYLGGRAVTEGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKQGRISGAAVRTYLLERSRVCQISDPERNYHCFYLLCAAPQEELEKYKLGHPKTFHYLNQSKCFELVGISDAHDYIATRRAMDIVGMSEKEQEAIFRVVAAILHLGNVEFTKGKEVDSSVPKDDKSKFHLNTVAELLMCDVKALEDALCKRVMVTPEEVIKRSLDPQSALISRDGLAKTIYSRLFDWLVEKINVSIGQDATSRSLIGVLDIYGFESFKTNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEAIDWSYIEFVDNQDVLDLIEKKPGGIVALLDEACMFPKSTHETFANKLYQTFKTHKRFIKPKLSRTDFAVAHYAGEVQYQSDLFLDKNKDYVIPEHQDLLGASKCPFVVGLFPPLPEETSKSSKFSSIGSRFKLQLQQLMETLNSTEPHYIRCVKPNNLLKPAVFENVNIMQQLRCGGVLEAIRISCAGYPTRKPFFEFINRFGLLYPRALEGNYEEKAAAQKILDNIGLKGYQVGKTKVFLRAGQMAELDARRTMVLSAAAKKIQRRIRTHQAQRRFILLRKATISLQALCRGRLSSKIFDNLRRQAAAVKIQKNARRLHSRKSYKNLHVAALVVQTGLRAMAAHKQFRFRKQTKAATTIQAQFRCHRATLYFKKLKKGVILSQTRWRGKLARRELRQLKMASRETGALKEAKDMLEKKVEELTYRAQLEKRSRVDLEEEKNQEIKKLQSSLEEMRKKVDETNGLLVKEREAAKKAIEEAPPVVTETQVLVEDTQKIEALTEEVEGLKANLEQEKQRADDATRKFDEAQESSEDRKKKLEDTEKKAQQLQESVTRLEEKCNNLESENKVLRQQAVSIAPNKFLSGRSRSILQRGSESGHLSVDARPSLDLHSHSINRRDLSEVDDKPQKSLNEKQQENQELLIRCIVQHLGFQGKRPVTACIIYKCLLQWRSFEVERTSVFDRIIQTIGQAIETQDNNNILAYWLSNASTLLLLLQRTLKASGAAGMAPQRRRSSSATLFGRMTQSFRGTPQGVNLAMINGGVDTLRQVEAKYPALLFKQQLTAYVEKIYGMIRDNLKKEISPLLGLCIQAPRTSRASLVKGASRSVGNTAAQQALIAHWQGIVKSLTNFLNNLKSNHVPPFLVRKVFTQIFSFINVQLFNSLLLRRECCSFSNGEYVKAGLAELEHWCYNATDEYAGSSWDELKHIRQAIGFLVIHQKPKKTLDEISHELCPVLSIQQLYRISTMYWDDKYGTHSVSPDVIANMRVLMTEDSNNAVSNSFLLDDDSSIPFSVDDLSKSMERIEIGDVEPPPLIRENSGFSFLLPCSD
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Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Involved in trafficking of Golgi stacks, mitochondria and peroxisomes.
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F4HX15
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LPAI_ARATH
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Phospholipase A I (AtPLA1) (EC 3.1.1.-)
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MSSTCSSPSAVEDPELGFRIDLDWTAGDSEDQVALRLESQLMVALPAPHDTVVVELKGIGDDDEGGLENVGLEMRVEKRREPLRAVTLMKAVGSGQQYDGVGVLTRLMRSDMMPAAIPAPAIDVASSCGVHWKTVTSLSLSGCGLLVMPVEVTELPLLEKLCLEHNKLSVLPPEIGKLKNLKILRVDNNMLISVPVELRQCVGLVELSLEHNKLVRPLLDFRAMAGLRILRLFGNPLEFLPEILPLHQLRHLSLVNIRIVSDENLRSVNVQIETENTSYFGASRHKLSAFSPLIFRSSSCHHPLLASTLVKIMQDEGNRSVIGKDENAVRQLISMITSDNQHVVEQACVALSSLARDVGVAMQLMKCDIMKPTETVLKSSSPDEVISVLQVVVTLAFVSDSVSQKMLTKDMLKALKSLCAHKNPEVQRQALLAVGNLAFCLENRRILITSESLRELLMRLIVTPEPRVNKAAARALAILGENEILRRSIKGRQVPKQGLRILTMDGGGMKGLATVQILKEIEKGSGKPIHELFDLICGTSTGGMLAIALGVKLMTLEQCEEIYKNLGKLVFAESVPKDNEAASWREKLDQLYKSSSQSFRVVIHGSKHSANEFERLLKEMCADEDGDLLIESAVKNVPKVFVVSTLVSVMPAQPFIFRNYQYPVGTPEMSYAFSDHSGGSTLTSSTASDQAGYYKQSAFMGSCKHQVWQAIRASSAAPYYLDDFSVDSYRWQDGAIVANNPTIFAIREAQLLWPDTKIDCLVSIGSGSVPTRVRKGGWRYLDTGQVLIESACSVERVEEALSTLLPMLPEIQYFRFNPVDDRCGMELDETDPAIWLKLEAAIEEFIQSNPQVFKNVCERLTLPFLNDEKWCDNLKPRFMNGKLPNSRVESSPSLGWRRNVLLMEAQHSPDSGRVKYHARALESFCSNNGIKLSSLHTTATPGCQKPSPGTAFPTPFTSPLITGSLPPSPLLFTPELGPQKFNRIDMVPPLSLDGGHVGKTVMSPPSSPPRQRQLYLPLRQMHEKLQNLPQVGILHLSLQNDSNGSILSWQNDVFVVAEPGDLADKFLQSVKVSILSVMQSNRRKAASVLSNICSISDLVRSKKCFQVGNIIHRYIGRQTLVMEDDQEIASFMFRRTVPSAHLTPDDIRWMVGAWRDRIIVFSGTFGPTQAVVKAFLDSGAKAVIGPSNEPQETPLITSQGSSEYNIGDQNGKFEIGEEEDEDEEVNEETEREEMEPPTPTSDWEDSDHEKTNRDGKYCGLWEDDEEEVSEFVCQLYDQLFRENSRVDVALQKALASHRKLRYTCHLPNV
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Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG), and less efficiently the phoshpolipids phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylglycerol (PG), phosphatidylserine (PS) and phosphatidylinositol (PI). Hydrolyzes phospholipids at both the sn-1 and sn-2 positions. Involved in basal jasmonic acid production and promotes resistance to the necrotrophic fungal pathogen Botrytis cinerea.
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