entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
|
|---|---|---|---|---|
O75951
|
LYZL6_HUMAN
|
Lysozyme-like protein 6 (EC 3.2.1.17)
|
MTKALLIYLVSSFLALNQASLISRCDLAQVLQLEDLDGFEGYSLSDWLCLAFVESKFNISKINENADGSFDYGLFQINSHYWCNDYKSYSENLCHVDCQDLLNPNLLAGIHCAKRIVSGARGMNNWVEWRLHCSGRPLFYWLTGCRLR
|
May be involved sperm-egg plasma membrane adhesion and fusion during fertilization. Exhibits bacteriolytic activity in vitro against Micrococcus luteus and Staphylococcus aureus. Shows weak bacteriolytic activity against Gram-positive bacteria at physiological pH. Bacteriolytic activity is pH-dependent, with a maximum at around pH 5.6.
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O75952
|
CABYR_HUMAN
|
Calcium-binding tyrosine phosphorylation-regulated protein (Calcium-binding protein 86) (Cancer/testis antigen 88) (CT88) (Fibrousheathin II) (Fibrousheathin-2) (FSP-2) (Testis-specific calcium-binding protein CBP86)
|
MISSKPRLVVPYGLKTLLEGISRAVLKTNPSNINQFAAAYFQELTMYRGNTTMDIKDLVKQFHQIKVEKWSEGTTPQKKLECLKEPGKTSVESKVPTQMEKSTDTDEDNVTRTEYSDKTTQFPSVYAVPGTEQTEAVGGLSSKPATPKTTTPPSSPPPTAVSPEFAYVPADPAQLAAQMLGKVSSIHSDQSDVLMVDVATSMPVVIKEVPSSEAAEDVMVAAPLVCSGKVLEVQVVNQTSVHVDLGSQPKENEAEPSTASSVPLQDEQEPPAYDQAPEVTLQADIEVMSTVHISSVYNDVPVTEGVVYIEQLPEQIVIPFTDQVACLKENEQSKENEQSPRVSPKSVVEKTTSGMSKKSVESVKLAQLEENAKYSSVYMEAEATALLSDTSLKGQPEVPAQLLDAEGAIKIGSEKSLHLEVEITSIVSDNTGQEESGENSVPQEMEGKPVLSGEAAEAVHSGTSVKSSSGPFPPAPEGLTAPEIEPEGESTAE
|
May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction. Isoform 1 binds calcium in vitro. Isoform 2 and isoform 6 probably bind calcium. Isoform 3 and isoform 5 do not bind calcium in vitro. Isoform 4 probably does not bind calcium.
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O75955
|
FLOT1_HUMAN
|
Flotillin-1
|
MFFTCGPNEAMVVSGFCRSPPVMVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVTGEVLDILTRLPESVERLTGVSISQVNHKPLRTA
|
May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.
|
O75956
|
CDKA2_HUMAN
|
Cyclin-dependent kinase 2-associated protein 2 (CDK2-associated protein 2) (DOC-1-related protein) (DOC-1R)
|
MSYKPIAPAPSSTPGSSTPGPGTPVPTGSVPSPSGSVPGAGAPFRPLFNDFGPPSMGYVQAMKPPGAQGSQSTYTDLLSVIEEMGKEIRPTYAGSKSAMERLKRGIIHARALVRECLAETERNART
|
Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Inhibits cell cycle G1/S phase transition by repressing CDK2 expression and activation represses CDK2 activation by inhibiting its interaction with cyclin E and A. Plays a role in regulating the self-renewal of embryonic stem cells (ESCs) and in maintaining cell survival during terminal differentiation of ESCs (By similarity). Regulates microtubule organization of metaphase II oocytes (By similarity).
|
O75962
|
TRIO_HUMAN
|
Triple functional domain protein (EC 2.7.11.1) (PTPRF-interacting protein)
|
MSGSSGGAAAPAASSGPAAAASAAGSGCGGGAGEGAEEAAKDLADIAAFFRSGFRKNDEMKAMDVLPILKEKVAYLSGGRDKRGGPILTFPARSNHDRIRQEDLRRLISYLACIPSEEVCKRGFTVIVDMRGSKWDSIKPLLKILQESFPCCIHVALIIKPDNFWQKQRTNFGSSKFEFETNMVSLEGLTKVVDPSQLTPEFDGCLEYNHEEWIEIRVAFEDYISNATHMLSRLEELQDILAKKELPQDLEGARNMIEEHSQLKKKVIKAPIEDLDLEGQKLLQRIQSSESFPKKNSGSGNADLQNLLPKVSTMLDRLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWITHNKGLFLNSYTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIRQIASQLEQEWKAFAAALDERSTLLDMSSIFHQKAEKYMSNVDSWCKACGEVDLPSELQDLEDAIHHHQGIYEHITLAYSEVSQDGKSLLDKLQRPLTPGSSDSLTASANYSKAVHHVLDVIHEVLHHQRQLENIWQHRKVRLHQRLQLCVFQQDVQQVLDWIENHGEAFLSKHTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAHQLEDRIQDFVRRVEQRKILLDMSVSFHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFGQQQQTTLQVTVNVIKEGEDLIQQLRDSAISSNKTPHNSSINHIETVLQQLDEAQSQMEELFQERKIKLELFLQLRIFERDAIDIISDLESWNDELSQQMNDFDTEDLTIAEQRLQHHADKALTMNNLTFDVIHQGQDLLQYVNEVQASGVELLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCVQLRHLQAEVKQVLGWIRNGESMLNAGLITASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRDCAEKVASHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVLESLEQEYKREEDWCGGADKLGPNSETDHVTPMISKHLEQKEAFLKACTLARRNADVFLKYLHRNSVNMPGMVTHIKAPEQQVKNILNELFQRENRVLHYWTMRKRRLDQCQQYVVFERSAKQALEWIHDNGEFYLSTHTSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVTAVDKRYRDFSLRMEKYRTSLEKALGISSDSNKSSKSLQLDIIPASIPGSEVKLRDAAHELNEEKRKSARRKEFIMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPGIVNKELIIFGNMQEIYEFHNNIFLKELEKYEQLPEDVGHCFVTWADKFQMYVTYCKNKPDSTQLILEHAGSYFDEIQQRHGLANSISSYLIKPVQRITKYQLLLKELLTCCEEGKGEIKDGLEVMLSVPKRANDAMHLSMLEGFDENIESQGELILQESFQVWDPKTLIRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHVEGDPCKFALWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQERTIHLKGALKEPIHIPKTAPATRQKGRRDGEDLDSQGDGSSQPDTISIASRTSQNTLDSDKLSGGCELTVVIHDFTACNSNELTIRRGQTVEVLERPHDKPDWCLVRTTDRSPAAEGLVPCGSLCIAHSRSSMEMEGIFNHKDSLSVSSNDASPPASVASLQPHMIGAQSSPGPKRPGNTLRKWLTSPVRRLSSGKADGHVKKLAHKHKKSREVRKSADAGSQKDSDDSAATPQDETVEERGRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADAVPLPPPMAIQQHSLLQPDSQDDKASSRLLVRPTSSETPSAAELVSAIEELVKSKMALEDRPSSLLVDQGDSSSPSFNPSDNSLLSSSSPIDEMEERKSSSLKRRHYVLQELVETERDYVRDLGYVVEGYMALMKEDGVPDDMKGKDKIVFGNIHQIYDWHRDFFLGELEKCLEDPEKLGSLFVKHERRLHMYIAYCQNKPKSEHIVSEYIDTFFEDLKQRLGHRLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKASLDTSELERAVEVMCIVPRRCNDMMNVGRLQGFDGKIVAQGKLLLQDTFLVTDQDAGLLPRCRERRIFLFEQIVIFSEPLDKKKGFSMPGFLFKNSIKVSCLCLEENVENDPCKFALTSRTGDVVETFILHSSSPSVRQTWIHEINQILENQRNFLNALTSPIEYQRNHSGGGGGGGSGGSGGGGGSGGGGAPSGGSGHSGGPSSCGGAPSTSRSRPSRIPQPVRHHPPVLVSSAASSQAEADKMSGTSTPGPSLPPPGAAPEAGPSAPSRRPPGADAEGSEREAEPIPKMKVLESPRKGAANASGSSPDAPAKDARASLGTLPLGKPRAGAASPLNSPLSSAVPSLGKEPFPPSSPLQKGGSFWSSIPASPASRPGSFTFPGDSDSLQRQTPRHAAPGKDTDRMSTCSSASEQSVQSTQSNGSESSSSSNISTMLVTHDYTAVKEDEINVYQGEVVQILASNQQNMFLVFRAATDQCPAAEGWIPGFVLGHTSAVIVENPDGTLKKSTSWHTALRLRKKSEKKDKDGKREGKLENGYRKSREGLSNKVSVKLLNPNYIYDVPPEFVIPLSEVTCETGETVVLRCRVCGRPKASITWKGPEHNTLNNDGHYSISYSDLGEATLKIVGVTTEDDGIYTCIAVNDMGSASSSASLRVLGPGMDGIMVTWKDNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQAGNGRSTGVLDTSRLTSFIERRKHQNDVRPIRSIKNFLQSRLLPRV
|
Guanine nucleotide exchange factor (GEF) for RHOA and RAC1 GTPases. Involved in coordinating actin remodeling, which is necessary for cell migration and growth. Plays a key role in the regulation of neurite outgrowth and lamellipodia formation. In developing hippocampal neurons, limits dendrite formation, without affecting the establishment of axon polarity. Once dendrites are formed, involved in the control of synaptic function by regulating the endocytosis of AMPA-selective glutamate receptors (AMPARs) at CA1 excitatory synapses (By similarity). May act as a regulator of adipogenesis (By similarity).
|
O75969
|
AKAP3_HUMAN
|
A-kinase anchor protein 3 (AKAP-3) (A-kinase anchor protein 110 kDa) (AKAP 110) (Cancer/testis antigen 82) (CT82) (Fibrous sheath protein of 95 kDa) (FSP95) (Fibrousheathin I) (Fibrousheathin-1) (Protein kinase A-anchoring protein 3) (PRKA3) (Sperm oocyte-binding protein)
|
MSEKVDWLQSQNGVCKVDVYSPGDNQAQDWKMDTSTDPVRVLSWLRRDLEKSTAEFQDVRFKPGESFGGETSNSGDPHKGFSVDYYNTTTKGTPERLHFEMTHKEIPCQGPRAQLGNGSSVDEVSFYANRLTNLVIAMARKEINEKIDGSENKCVYQSLYMGNEPTPTKSLSKIASELVNETVSACSRNAAPDKAPGSGDRVSGSSQSPPNLKYKSTLKIKESTKERQGPDDKPPSKKSFFYKEVFESRNGDYAREGGRFFPRERKRFRGQERPDDFTASVSEGIMTYANSVVSDMMVSIMKTLKIQVKDTTIATILLKKVLLKHAKEVVSDLIDSFLRNLHSVTGTLMTDTQFVSAVKRTVFSHGSQKATDIMDAMLRKLYNVMFAKKVPEHVRKAQDKAESYSLISMKGMGDPKNRNVNFAMKSETKLREKMYSEPKSEEETCAKTLGEHIIKEGLTLWHKTQQKECKSLGFQHAAFEAPNTQRKPASDISFEYPEDIGNLSLPPYPPEKPENFMYDSDSWAEDLIVSALLLIQYHLAQGGRRDARSFVEAAGTTNFPANEPPVAPDESCLKSAPIVGDQEQAEKKDLRSVFFNFIRNLLSETIFKRDQSPEPKVPEQPVKEDRKLCERPLASSPPRLYEDDETPGALSGLTKMAVSQIDGHMSGQMVEHLMNSVMKLCVIIAKSCDASLAELGDDKSGDASRLTSAFPDSLYECLPAKGTGSAEAVLQNAYQAIHNEMRGTSGQPPEGCAAPTVIVSNHNLTDTVQNKQLQAVLQWVAASELNVPILYFAGDDEGIQEKLLQLSAAAVDKGCSVGEVLQSVLRYEKERQLNEAVGNVTPLQLLDWLMVNL
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May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction.
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O75970
|
MPDZ_HUMAN
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Multiple PDZ domain protein (Multi-PDZ domain protein 1)
|
MLEAIDKNRALHAAERLQTKLRERGDVANEDKLSLLKSVLQSPLFSQILSLQTSVQQLKDQVNIATSATSNIEYAHVPHLSPAVIPTLQNESFLLSPNNGNLEALTGPGIPHINGKPACDEFDQLIKNMAQGRHVEVFELLKPPSGGLGFSVVGLRSENRGELGIFVQEIQEGSVAHRDGRLKETDQILAINGQALDQTITHQQAISILQKAKDTVQLVIARGSLPQLVSPIVSRSPSAASTISAHSNPVHWQHMETIELVNDGSGLGFGIIGGKATGVIVKTILPGGVADQHGRLCSGDHILKIGDTDLAGMSSEQVAQVLRQCGNRVKLMIARGAIEERTAPTALGITLSSSPTSTPELRVDASTQKGEESETFDVELTKNVQGLGITIAGYIGDKKLEPSGIFVKSITKSSAVEHDGRIQIGDQIIAVDGTNLQGFTNQQAVEVLRHTGQTVLLTLMRRGMKQEAELMSREDVTKDADLSPVNASIIKENYEKDEDFLSSTRNTNILPTEEEGYPLLSAEIEEIEDAQKQEAALLTKWQRIMGINYEIVVAHVSKFSENSGLGISLEATVGHHFIRSVLPEGPVGHSGKLFSGDELLEVNGITLLGENHQDVVNILKELPIEVTMVCCRRTVPPTTQSELDSLDLCDIELTEKPHVDLGEFIGSSETEDPVLAMTDAGQSTEEVQAPLAMWEAGIQHIELEKGSKGLGFSILDYQDPIDPASTVIIIRSLVPGGIAEKDGRLLPGDRLMFVNDVNLENSSLEEAVEALKGAPSGTVRIGVAKPLPLSPEEGYVSAKEDSFLYPPHSCEEAGLADKPLFRADLALVGTNDADLVDESTFESPYSPENDSIYSTQASILSLHGSSCGDGLNYGSSLPSSPPKDVIENSCDPVLDLHMSLEELYTQNLLQRQDENTPSVDISMGPASGFTINDYTPANAIEQQYECENTIVWTESHLPSEVISSAELPSVLPDSAGKGSEYLLEQSSLACNAECVMLQNVSKESFERTINIAKGNSSLGMTVSANKDGLGMIVRSIIHGGAISRDGRIAIGDCILSINEESTISVTNAQARAMLRRHSLIGPDIKITYVPAEHLEEFKISLGQQSGRVMALDIFSSYTGRDIPELPEREEGEGEESELQNTAYSNWNQPRRVELWREPSKSLGISIVGGRGMGSRLSNGEVMRGIFIKHVLEDSPAGKNGTLKPGDRIVEVDGMDLRDASHEQAVEAIRKAGNPVVFMVQSIINRPRKSPLPSLLHNLYPKYNFSSTNPFADSLQINADKAPSQSESEPEKAPLCSVPPPPPSAFAEMGSDHTQSSASKISQDVDKEDEFGYSWKNIRERYGTLTGELHMIELEKGHSGLGLSLAGNKDRSRMSVFIVGIDPNGAAGKDGRLQIADELLEINGQILYGRSHQNASSIIKCAPSKVKIIFIRNKDAVNQMAVCPGNAVEPLPSNSENLQNKETEPTVTTSDAAVDLSSFKNVQHLELPKDQGGLGIAISEEDTLSGVIIKSLTEHGVAATDGRLKVGDQILAVDDEIVVGYPIEKFISLLKTAKMTVKLTIHAENPDSQAVPSAAGAASGEKKNSSQSLMVPQSGSPEPESIRNTSRSSTPAIFASDPATCPIIPGCETTIEISKGRTGLGLSIVGGSDTLLGAIIIHEVYEEGAACKDGRLWAGDQILEVNGIDLRKATHDEAINVLRQTPQRVRLTLYRDEAPYKEEEVCDTLTIELQKKPGKGLGLSIVGKRNDTGVFVSDIVKGGIADADGRLMQGDQILMVNGEDVRNATQEAVAALLKCSLGTVTLEVGRIKAGPFHSERRPSQSSQVSEGSLSSFTFPLSGSSTSESLESSSKKNALASEIQGLRTVEMKKGPTDSLGISIAGGVGSPLGDVPIFIAMMHPTGVAAQTQKLRVGDRIVTICGTSTEGMTHTQAVNLLKNASGSIEMQVVAGGDVSVVTGHQQEPASSSLSFTGLTSSSIFQDDLGPPQCKSITLERGPDGLGFSIVGGYGSPHGDLPIYVKTVFAKGAASEDGRLKRGDQIIAVNGQSLEGVTHEEAVAILKRTKGTVTLMVLS
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Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses. Promotes clustering of HT2RC at the cell surface (By similarity).
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O75971
|
SNPC5_HUMAN
|
snRNA-activating protein complex subunit 5 (SNAPc subunit 5) (Small nuclear RNA-activating complex polypeptide 5) (snRNA-activating protein complex 19 kDa subunit) (SNAPc 19 kDa subunit)
|
MLSRLQELRKEEETLLRLKAALHDQLNRLKVEELALQSMISSRRGDEMLSSHTVPEQSHDMLVHVDNEASINQTTLELSTKSHVTEEEEEEEEEESDS
|
Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box.
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O75995
|
SASH3_HUMAN
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SAM and SH3 domain-containing protein 3 (SH3 protein expressed in lymphocytes homolog)
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MLRRKPSNASEKEPTQKKKLSLQRSSSFKDFAKSKPSSPVVSEKEFNLDDNIPEDDSGVPTPEDAGKSGKKLGKKWRAVISRTMNRKMGKMMVKALSEEMADTLEEGSASPTSPDYSLDSPGPEKMALAFSEQEEHELPVLSRQASTGSELCSPSPGSGSFGEEPPAPQYTGPFCGRARVHTDFTPSPYDHDSLKLQKGDVIQIIEKPPVGTWLGLLNGKVGSFKFIYVDVLPEEAVGHARPSRRQSKGKRPKPKTLHELLERIGLEEHTSTLLLNGYQTLEDFKELRETHLNELNIMDPQHRAKLLTAAELLLDYDTGSEEAEEGAESSQEPVAHTVSEPKVDIPRDSGCFEGSESGRDDAELAGTEEQLQGLSLAGAP
|
May function as a signaling adapter protein in lymphocytes.
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O76003
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GLRX3_HUMAN
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Glutaredoxin-3 (PKC-interacting cousin of thioredoxin) (PICOT) (PKC-theta-interacting protein) (PKCq-interacting protein) (Thioredoxin-like protein 2)
|
MAAGAAEAAVAAVEEVGSAGQFEELLRLKAKSLLVVHFWAPWAPQCAQMNEVMAELAKELPQVSFVKLEAEGVPEVSEKYEISSVPTFLFFKNSQKIDRLDGAHAPELTKKVQRHASSGSFLPSANEHLKEDLNLRLKKLTHAAPCMLFMKGTPQEPRCGFSKQMVEILHKHNIQFSSFDIFSDEEVRQGLKAYSSWPTYPQLYVSGELIGGLDIIKELEASEELDTICPKAPKLEERLKVLTNKASVMLFMKGNKQEAKCGFSKQILEILNSTGVEYETFDILEDEEVRQGLKAYSNWPTYPQLYVKGELVGGLDIVKELKENGELLPILRGEN
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Together with BOLA2, acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins. Acts as a critical negative regulator of cardiac hypertrophy and a positive inotropic regulator (By similarity). Required for hemoglobin maturation. Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity.
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O76021
|
RL1D1_HUMAN
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Ribosomal L1 domain-containing protein 1 (CATX-11) (Cellular senescence-inhibited gene protein) (Protein PBK1)
|
MEDSASASLSSAAATGTSTSTPAAPTARKQLDKEQVRKAVDALLTHCKSRKNNYGLLLNENESLFLMVVLWKIPSKELRVRLTLPHSIRSDSEDICLFTKDEPNSTPEKTEQFYRKLLNKHGIKTVSQIISLQTLKKEYKSYEAKLRLLSSFDFFLTDARIRRLLPSLIGRHFYQRKKVPVSVNLLSKNLSREINDCIGGTVLNISKSGSCSAIRIGHVGMQIEHIIENIVAVTKGLSEKLPEKWESVKLLFVKTEKSAALPIFSSFVSNWDEATKRSLLNKKKKEARRKRRERNFEKQKERKKKRQQARKTASVLSKDDVAPESGDTTVKKPESKKEQTPEHGKKKRGRGKAQVKATNESEDEIPQLVPIGKKTPANEKVEIQKHATGKKSPAKSPNPSTPRGKKRKALPASETPKAAESETPGKSPEKKPKIKEEAVKEKSPSLGKKDARQTPKKPEAKFFTTPSKSVRKASHTPKKWPKKPKVPQST
|
Regulates cellular senescence through inhibition of PTEN translation. Acts as a pro-apoptotic regulator in response to DNA damage.
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O76024
|
WFS1_HUMAN
|
Wolframin
|
MDSNTAPLGPSCPQPPPAPQPQARSRLNATASLEQERSERPRAPGPQAGPGPGVRDAAAPAEPQAQHTRSRERADGTGPTKGDMEIPFEEVLERAKAGDPKAQTEVGKHYLQLAGDTDEELNSCTAVDWLVLAAKQGRREAVKLLRRCLADRRGITSENEREVRQLSSETDLERAVRKAALVMYWKLNPKKKKQVAVAELLENVGQVNEHDGGAQPGPVPKSLQKQRRMLERLVSSESKNYIALDDFVEITKKYAKGVIPSSLFLQDDEDDDELAGKSPEDLPLRLKVVKYPLHAIMEIKEYLIDMASRAGMHWLSTIIPTHHINALIFFFIVSNLTIDFFAFFIPLVIFYLSFISMVICTLKVFQDSKAWENFRTLTDLLLRFEPNLDVEQAEVNFGWNHLEPYAHFLLSVFFVIFSFPIASKDCIPCSELAVITGFFTVTSYLSLSTHAEPYTRRALATEVTAGLLSLLPSMPLNWPYLKVLGQTFITVPVGHLVVLNVSVPCLLYVYLLYLFFRMAQLRNFKGTYCYLVPYLVCFMWCELSVVILLESTGLGLLRASIGYFLFLFALPILVAGLALVGVLQFARWFTSLELTKIAVTVAVCSVPLLLRWWTKASFSVVGMVKSLTRSSMVKLILVWLTAIVLFCWFYVYRSEGMKVYNSTLTWQQYGALCGPRAWKETNMARTQILCSHLEGHRVTWTGRFKYVRVTDIDNSAESAINMLPFFIGDWMRCLYGEAYPACSPGNTSTAEEELCRLKLLAKHPCHIKKFDRYKFEITVGMPFSSGADGSRSREEDDVTKDIVLRASSEFKSVLLSLRQGSLIEFSTILEGRLGSKWPVFELKAISCLNCMAQLSPTRRHVKIEHDWRSTVHGAVKFAFDFFFFPFLSAA
|
Participates in the regulation of cellular Ca(2+) homeostasis, at least partly, by modulating the filling state of the endoplasmic reticulum Ca(2+) store. Negatively regulates the ER stress response and positively regulates the stability of V-ATPase subunits ATP6V1A and ATP1B1 by preventing their degradation through an unknown proteasome-independent mechanism.
|
O76027
|
ANXA9_HUMAN
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Annexin A9 (Annexin XXXI) (Annexin-31) (Annexin-9) (Pemphaxin)
|
MSVTGGKMAPSLTQEILSHLGLASKTAAWGTLGTLRTFLNFSVDKDAQRLLRAITGQGVDRSAIVDVLTNRSREQRQLISRNFQERTQQDLMKSLQAALSGNLERIVMALLQPTAQFDAQELRTALKASDSAVDVAIEILATRTPPQLQECLAVYKHNFQVEAVDDITSETSGILQDLLLALAKGGRDSYSGIIDYNLAEQDVQALQRAEGPSREETWVPVFTQRNPEHLIRVFDQYQRSTGQELEEAVQNRFHGDAQVALLGLASVIKNTPLYFADKLHQALQETEPNYQVLIRILISRCETDLLSIRAEFRKKFGKSLYSSLQDAVKGDCQSALLALCRAEDM
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Low affinity receptor for acetylcholine known to be targeted by disease-causing pemphigus vulgaris antibodies in keratinocytes.
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O76031
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CLPX_HUMAN
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ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial
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MPSCGACTCGAAAVRLITSSLASAQRGISGGRIHMSVLGRLGTFETQILQRAPLRSFTETPAYFASKDGISKDGSGDGNKKSASEGSSKKSGSGNSGKGGNQLRCPKCGDLCTHVETFVSSTRFVKCEKCHHFFVVLSEADSKKSIIKEPESAAEAVKLAFQQKPPPPPKKIYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNIPANLRQQAEVEKQTSLTPRELEIRRREDEYRFTKLLQIAGISPHGNALGASMQQQVNQQIPQEKRGGEVLDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANYNVEKAQQGIVFLDEVDKIGSVPGIHQLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRKLRGETVQVDTTNILFVASGAFNGLDRIISRRKNEKYLGFGTPSNLGKGRRAAAAADLANRSGESNTHQDIEEKDRLLRHVEARDLIEFGMIPEFVGRLPVVVPLHSLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPNSDIVCVEVDKEVVEGKKEPGYIRAPTKESSEEEYDSGVEEEGWPRQADAANS
|
ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex. Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure. ATP-dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis. Important for efficient erythropoiesis through up-regulation of heme biosynthesis.
|
O76036
|
NCTR1_HUMAN
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Natural cytotoxicity triggering receptor 1 (Lymphocyte antigen 94 homolog) (NK cell-activating receptor) (Natural killer cell p46-related protein) (NK-p46) (NKp46) (hNKp46) (CD antigen CD335)
|
MSSTLPALLCVGLCLSQRISAQQQTLPKPFIWAEPHFMVPKEKQVTICCQGNYGAVEYQLHFEGSLFAVDRPKPPERINKVKFYIPDMNSRMAGQYSCIYRVGELWSEPSNLLDLVVTEMYDTPTLSVHPGPEVISGEKVTFYCRLDTATSMFLLLKEGRSSHVQRGYGKVQAEFPLGPVTTAHRGTYRCFGSYNNHAWSFPSEPVKLLVTGDIENTSLAPEDPTFPADTWGTYLLTTETGLQKDHALWDHTAQNLLRMGLAFLVLVALVWFLVEDWLSRKRTRERASRASTWEGRRRLNTQTL
|
Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis.
|
O76039
|
CDKL5_HUMAN
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Cyclin-dependent kinase-like 5 (EC 2.7.11.22) (Serine/threonine-protein kinase 9)
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MKIPNIGNVMNKFEILGVVGEGAYGVVLKCRHKETHEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNMLELLEEMPNGVPPEKVKSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGNNANYTEYVATRWYRSPELLLGAPYGKSVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPSEQMKLFYSNPRFHGLRFPAVNHPQSLERRYLGILNSVLLDLMKNLLKLDPADRYLTEQCLNHPTFQTQRLLDRSPSRSAKRKPYHVESSTLSNRNQAGKSTALQSHHRSNSKDIQNLSVGLPRADEGLPANESFLNGNLAGASLSPLHTKTYQASSQPGSTSKDLTNNNIPHLLSPKEAKSKTEFDFNIDPKPSEGPGTKYLKSNSRSQQNRHSFMESSQSKAGTLQPNEKQSRHSYIDTIPQSSRSPSYRTKAKSHGALSDSKSVSNLSEARAQIAEPSTSRYFPSSCLDLNSPTSPTPTRHSDTRTLLSPSGRNNRNEGTLDSRRTTTRHSKTMEELKLPEHMDSSHSHSLSAPHESFSYGLGYTSPFSSQQRPHRHSMYVTRDKVRAKGLDGSLSIGQGMAARANSLQLLSPQPGEQLPPEMTVARSSVKETSREGTSSFHTRQKSEGGVYHDPHSDDGTAPKENRHLYNDPVPRRVGSFYRVPSPRPDNSFHENNVSTRVSSLPSESSSGTNHSKRQPAFDPWKSPENISHSEQLKEKEKQGFFRSMKKKKKKSQTVPNSDSPDLLTLQKSIHSASTPSSRPKEWRPEKISDLQTQSQPLKSLRKLLHLSSASNHPASSDPRFQPLTAQQTKNSFSEIRIHPLSQASGGSSNIRQEPAPKGRPALQLPGQMDPGWHVSSVTRSATEGPSYSEQLGAKSGPNGHPYNRTNRSRMPNLNDLKETAL
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Mediates phosphorylation of MECP2. May regulate ciliogenesis.
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O76041
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NEBL_HUMAN
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Nebulette (Actin-binding Z-disk protein)
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MRVPVFEDIKDETEEEKIGEEENEEDQVFYKPVIEDLSMELARKCTELISDIRYKEEFKKSKDKCTFVTDSPMLNHVKNIGAFISEAKYKGTIKADLSNSLYKRMPATIDSVFAGEVTQLQSEVAYKQKHDAAKGFSDYAHMKEPPEVKHAMEVNKHQSNISYRKDVQDTHTYSAELDRPDIKMATQISKIISNAEYKKGQGIMNKEPAVIGRPDFEHAVEASKLSSQIKYKEKFDNEMKDKKHHYNPLESASFRQNQLAATLASNVKYKKDIQNMHDPVSDLPNLLFLDHVLKASKMLSGREYKKLFEENKGMYHFDADAVEHLHHKGNAVLQSQVKYKEEYEKNKGKPMLEFVETPSYQASKEAQKMQSEKVYKEDFEKEIKGRSSLDLDKTPEFLHVKYITNLLREKEYKKDLENEIKGKGMELNSEVLDIQRAKRASEMASEKEYKKDLESIIKGKGMQAGTDTLEMQHAKKAAEIASEKDYKRDLETEIKGKGMQVSTDTLDVQRAKKASEMASQKQYKKDLENEIKGKGMQVSMDIPDILRAKRTSEIYSQRKYKDEAEKMLSNYSTIADTPEIQRIKTTQQNISAVFYKKEVGAGTAVKDSPEIERVKKNQQNISSVKYKEEIKHATAISDPPELKRVKENQKNISNLQYKEQNYKATPVSMTPEIERVRRNQEQLSAVKYKGELQRGTAISDPPELKRAKENQKNISNVYYRGQLGRATTLSVTPEMERVKKNQENISSVKYTQDHKQMKGRPSLILDTPAMRHVKEAQNHISMVKYHEDFEKTKGRGFTPVVDDPVTERVRKNTQVVSDAAYKGVHPHIVEMDRRPGIIVDLKVWRTDPGSIFDLDPLEDNIQSRSLHMLSEKASHYRRHWSRSHSSSTFGTGLGDDRSEISEIYPSFSCCSEVTRPSDEGAPVLPGAYQQSHSQGYGYMHQTSVSSMRSMQHSPNLRTYRAMYDYSAQDEDEVSFRDGDYIVNVQPIDDGWMYGTVQRTGRTGMLPANYIEFVN
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Binds to actin and plays an important role in the assembly of the Z-disk. May functionally link sarcomeric actin to the desmin intermediate filaments in the heart muscle sarcomeres. Isoform 2 might play a role in the assembly of focal adhesion.
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O76050
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NEUL1_HUMAN
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E3 ubiquitin-protein ligase NEURL1 (EC 2.3.2.27) (Neuralized-like protein 1A) (h-neu) (h-neuralized 1) (RING finger protein 67) (RING-type E3 ubiquitin transferase NEURL1)
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MGNNFSSIPSLPRGNPSRAPRGHPQNLKDSIGGPFPVTSHRCHHKQKHCPAVLPSGGLPATPLLFHPHTKGSQILMDLSHKAVKRQASFCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIHPDSLPKYACPDLVSQSGFWAKALPEEFANEGNIIAFWVDKKGRVFHRINDSAVMLFFSGVRTADPLWALVDVYGLTRGVQLLDSELVLPDCLRPRSFTALRRPSLRREADDARLSVSLCDLNVPGADGDEAAPAAGCPIPQNSLNSQHSRALPAQLDGDLRFHALRAGAHVRILDEQTVARVEHGRDERALVFTSRPVRVAETIFVKVTRSGGARPGALSFGVTTCDPGTLRPADLPFSPEALVDRKEFWAVCRVPGPLHSGDILGLVVNADGELHLSHNGAAAGMQLCVDASQPLWMLFGLHGTITQIRILGSTILAERGIPSLPCSPASTPTSPSALGSRLSDPLLSTCSSGPLGSSAGGTAPNSPVSLPESPVTPGLGQWSDECTICYEHAVDTVIYTCGHMCLCYACGLRLKKALHACCPICRRPIKDIIKTYRSS
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Plays a role in hippocampal-dependent synaptic plasticity, learning and memory. Involved in the formation of spines and functional synaptic contacts by modulating the translational activity of the cytoplasmic polyadenylation element-binding protein CPEB3. Promotes ubiquitination of CPEB3, and hence induces CPEB3-dependent mRNA translation activation of glutamate receptor GRIA1 and GRIA2. Can function as an E3 ubiquitin-protein ligase to activate monoubiquitination of JAG1 (in vitro), thereby regulating the Notch pathway. Acts as a tumor suppressor inhibits malignant cell transformation of medulloblastoma (MB) cells by inhibiting the Notch signaling pathway.
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O76054
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S14L2_HUMAN
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SEC14-like protein 2 (Alpha-tocopherol-associated protein) (TAP) (hTAP) (Squalene transfer protein) (Supernatant protein factor) (SPF)
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MSGRVGDLSPRQKEALAKFRENVQDVLPALPNPDDYFLLRWLRARSFDLQKSEAMLRKHVEFRKQKDIDNIISWQPPEVIQQYLSGGMCGYDLDGCPVWYDIIGPLDAKGLLFSASKQDLLRTKMRECELLLQECAHQTTKLGRKVETITIIYDCEGLGLKHLWKPAVEAYGEFLCMFEENYPETLKRLFVVKAPKLFPVAYNLIKPFLSEDTRKKIMVLGANWKEVLLKHISPDQVPVEYGGTMTDPDGNPKCKSKINYGGDIPRKYYVRDQVKQQYEHSVQISRGSSHQVEYEILFPGCVLRWQFMSDGADVGFGIFLKTKMGERQRAGEMTEVLPNQRYNSHLVPEDGTLTCSDPGIYVLRFDNTYSFIHAKKVNFTVEVLLPDKASEEKMKQLGAGTPK
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Carrier protein. Binds to some hydrophobic molecules and promotes their transfer between the different cellular sites. Binds with high affinity to alpha-tocopherol. Also binds with a weaker affinity to other tocopherols and to tocotrienols. May have a transcriptional activatory activity via its association with alpha-tocopherol. Probably recognizes and binds some squalene structure, suggesting that it may regulate cholesterol biosynthesis by increasing the transfer of squalene to a metabolic active pool in the cell.
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O76061
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STC2_HUMAN
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Stanniocalcin-2 (STC-2) (Stanniocalcin-related protein) (STC-related protein) (STCRP)
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MCAERLGQFMTLALVLATFDPARGTDATNPPEGPQDRSSQQKGRLSLQNTAEIQHCLVNAGDVGCGVFECFENNSCEIRGLHGICMTFLHNAGKFDAQGKSFIKDALKCKAHALRHRFGCISRKCPAIREMVSQLQRECYLKHDLCAAAQENTRVIVEMIHFKDLLLHEPYVDLVNLLLTCGEEVKEAITHSVQVQCEQNWGSLCSILSFCTSAIQKPPTAPPERQPQVDRTKLSRAHHGEAGHHLPEPSSRETGRGAKGERGSKSHPNAHARGRVGGLGAQGPSGSSEWEDEQSEYSDIRR
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Has an anti-hypocalcemic action on calcium and phosphate homeostasis.
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O76062
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ERG24_HUMAN
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Delta(14)-sterol reductase TM7SF2 (Delta-14-SR) (EC 1.3.1.70) (3-beta-hydroxysterol Delta (14)-reductase) (Another new gene 1 protein) (C-14 sterol reductase) (C14SR) (Putative sterol reductase SR-1) (Sterol C14-reductase) (Transmembrane 7 superfamily member 2)
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MAPTQGPRAPLEFGGPLGAAALLLLLPATMFHLLLAARSGPARLLGPPASLPGLEVLWSPRALLLWLAWLGLQAALYLLPARKVAEGQELKDKSRLRYPINGFQALVLTALLVGLGMSAGLPLGALPEMLLPLAFVATLTAFIFSLFLYMKAQVAPVSALAPGGNSGNPIYDFFLGRELNPRICFFDFKYFCELRPGLIGWVLINLALLMKEAELRGSPSLAMWLVNGFQLLYVGDALWHEEAVLTTMDITHDGFGFMLAFGDMAWVPFTYSLQAQFLLHHPQPLGLPMASVICLINATGYYIFRGANSQKNTFRKNPSDPRVAGLETISTATGRKLLVSGWWGMVRHPNYLGDLIMALAWSLPCGVSHLLPYFYLLYFTALLVHREARDERQCLQKYGLAWQEYCRRVPYRIMPYIY
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Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis.
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O76064
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RNF8_HUMAN
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E3 ubiquitin-protein ligase RNF8 (hRNF8) (EC 2.3.2.27) (RING finger protein 8) (RING-type E3 ubiquitin transferase RNF8)
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MGEPGFFVTGDRAGGRSWCLRRVGMSAGWLLLEDGCEVTVGRGFGVTYQLVSKICPLMISRNHCVLKQNPEGQWTIMDNKSLNGVWLNRARLEPLRVYSIHQGDYIQLGVPLENKENAEYEYEVTEEDWETIYPCLSPKNDQMIEKNKELRTKRKFSLDELAGPGAEGPSNLKSKINKVSCESGQPVKSQGKGEVASTPSDNLDPKLTALEPSKTTGAPIYPGFPKVTEVHHEQKASNSSASQRSLQMFKVTMSRILRLKIQMQEKHEAVMNVKKQTQKGNSKKVVQMEQELQDLQSQLCAEQAQQQARVEQLEKTFQEEEQHLQGLEIAQGEKDLKQQLAQALQEHWALMEELNRSKKDFEAIIQAKNKELEQTKEEKEKMQAQKEEVLSHMNDVLENELQCIICSEYFIEAVTLNCAHSFCSYCINEWMKRKIECPICRKDIKSKTYSLVLDNCINKMVNNLSSEVKERRIVLIRERKAKRLF
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E3 ubiquitin-protein ligase that plays a key role in DNA damage signaling via 2 distinct roles: by mediating the 'Lys-63'-linked ubiquitination of histones H2A and H2AX and promoting the recruitment of DNA repair proteins at double-strand breaks (DSBs) sites, and by catalyzing 'Lys-48'-linked ubiquitination to remove target proteins from DNA damage sites. Following DNA DSBs, it is recruited to the sites of damage by ATM-phosphorylated MDC1 and catalyzes the 'Lys-63'-linked ubiquitination of histones H2A and H2AX, thereby promoting the formation of TP53BP1 and BRCA1 ionizing radiation-induced foci (IRIF). Also controls the recruitment of UIMC1-BRCC3 (RAP80-BRCC36) and PAXIP1/PTIP to DNA damage sites. Also recruited at DNA interstrand cross-links (ICLs) sites and catalyzes 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Promotes the formation of 'Lys-63'-linked polyubiquitin chains via interactions with the specific ubiquitin-conjugating UBE2N/UBC13 and ubiquitinates non-histone substrates such as PCNA. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation. Also catalyzes the formation of 'Lys-48'-linked polyubiquitin chains via interaction with the ubiquitin-conjugating UBE2L6/UBCH8, leading to degradation of substrate proteins such as CHEK2, JMJD2A/KDM4A and KU80/XRCC5: it is still unclear how the preference toward 'Lys-48'- versus 'Lys-63'-linked ubiquitination is regulated but it could be due to RNF8 ability to interact with specific E2 specific ligases. For instance, interaction with phosphorylated HERC2 promotes the association between RNF8 and UBE2N/UBC13 and favors the specific formation of 'Lys-63'-linked ubiquitin chains. Promotes non-homologous end joining (NHEJ) by promoting the 'Lys-48'-linked ubiquitination and degradation the of KU80/XRCC5. Following DNA damage, mediates the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF168, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. Following DNA damage, mediates the ubiquitination and degradation of POLD4/p12, a subunit of DNA polymerase delta. In the absence of POLD4, DNA polymerase delta complex exhibits higher proofreading activity. In addition to its function in damage signaling, also plays a role in higher-order chromatin structure by mediating extensive chromatin decondensation. Involved in the activation of ATM by promoting histone H2B ubiquitination, which indirectly triggers histone H4 'Lys-16' acetylation (H4K16ac), establishing a chromatin environment that promotes efficient activation of ATM kinase. Required in the testis, where it plays a role in the replacement of histones during spermatogenesis. At uncapped telomeres, promotes the joining of deprotected chromosome ends by inducing H2A ubiquitination and TP53BP1 recruitment, suggesting that it may enhance cancer development by aggravating telomere-induced genome instability in case of telomeric crisis. Promotes the assembly of RAD51 at DNA DSBs in the absence of BRCA1 and TP53BP1 Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. May be required for proper exit from mitosis after spindle checkpoint activation and may regulate cytokinesis. May play a role in the regulation of RXRA-mediated transcriptional activity. Not involved in RXRA ubiquitination by UBE2E2.
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O76070
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SYUG_HUMAN
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Gamma-synuclein (Breast cancer-specific gene 1 protein) (Persyn) (Synoretin) (SR)
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MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGAKTKENVVQSVTSVAEKTKEQANAVSEAVVSSVNTVATKTVEEAENIAVTSGVVRKEDLRPSAPQQEGEASKEKEEVAEEAQSGGD
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Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases (By similarity). May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity).
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O76071
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CIAO1_HUMAN
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Probable cytosolic iron-sulfur protein assembly protein CIAO1 (WD repeat-containing protein 39)
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MKDSLVLLGRVPAHPDSRCWFLAWNPAGTLLASCGGDRRIRIWGTEGDSWICKSVLSEGHQRTVRKVAWSPCGNYLASASFDATTCIWKKNQDDFECVTTLEGHENEVKSVAWAPSGNLLATCSRDKSVWVWEVDEEDEYECVSVLNSHTQDVKHVVWHPSQELLASASYDDTVKLYREEEDDWVCCATLEGHESTVWSLAFDPSGQRLASCSDDRTVRIWRQYLPGNEQGVACSGSDPSWKCICTLSGFHSRTIYDIAWCQLTGALATACGDDAIRVFQEDPNSDPQQPTFSLTAHLHQAHSQDVNCVAWNPKEPGLLASCSDDGEVAFWKYQRPEGL
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Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. As a CIA complex component, interacts specifically with CIAO2A or CIAO2B and MMS19 to assist different branches of iron-sulfur protein assembly, depending of its interactors. The complex CIAO1:CIAO2B:MMS19 binds to and facilitates the assembly of most cytosolic-nuclear Fe/S proteins. CIAO1:CIAO2A specifically matures ACO1 and stabilizes IREB2. Seems to specifically modulate the transactivation activity of WT1. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation. {ECO:0000255|HAMAP-Rule:MF_03037, ECO:0000269|PubMed:17937914, ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:23891004, ECO:0000269|PubMed:9556563}.
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O76074
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PDE5A_HUMAN
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cGMP-specific 3',5'-cyclic phosphodiesterase (EC 3.1.4.35) (cGMP-binding cGMP-specific phosphodiesterase) (CGB-PDE)
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MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAERVHTIPVCKEGIRGHTESCSCPLQQSPRADNSAPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTMEPLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRN
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Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. Specifically regulates nitric-oxide-generated cGMP.
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O76075
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DFFB_HUMAN
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DNA fragmentation factor subunit beta (EC 3.-.-.-) (Caspase-activated deoxyribonuclease) (CAD) (Caspase-activated DNase) (Caspase-activated nuclease) (CPAN) (DNA fragmentation factor 40 kDa subunit) (DFF-40)
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MLQKPKSVKLRALRSPRKFGVAGRSCQEVLRKGCLRFQLPERGSRLCLYEDGTELTEDYFPSVPDNAELVLLTLGQAWQGYVSDIRRFLSAFHEPQVGLIQAAQQLLCDEQAPQRQRLLADLLHNVSQNIAAETRAEDPPWFEGLESRFQSKSGYLRYSCESRIRSYLREVSSYPSTVGAEAQEEFLRVLGSMCQRLRSMQYNGSYFDRGAKGGSRLCTPEGWFSCQGPFDMDSCLSRHSINPYSNRESRILFSTWNLDHIIEKKRTIIPTLVEAIKEQDGREVDWEYFYGLLFTSENLKLVHIVCHKKTTHKLNCDPSRIYKPQTRLKRKQPVRKRQ
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Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology.
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O76076
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CCN5_HUMAN
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CCN family member 5 (Connective tissue growth factor-like protein) (CTGF-L) (Connective tissue growth factor-related protein 58) (WNT1-inducible-signaling pathway protein 2) (WISP-2)
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MRGTPKTHLLAFSLLCLLSKVRTQLCPTPCTCPWPPPRCPLGVPLVLDGCGCCRVCARRLGEPCDQLHVCDASQGLVCQPGAGPGGRGALCLLAEDDSSCEVNGRLYREGETFQPHCSIRCRCEDGGFTCVPLCSEDVRLPSWDCPHPRRVEVLGKCCPEWVCGQGGGLGTQPLPAQGPQFSGLVSSLPPGVPCPEWSTAWGPCSTTCGLGMATRVSNQNRFCRLETQRRLCLSRPCPPSRGRSPQNSAF
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May play an important role in modulating bone turnover. Promotes the adhesion of osteoblast cells and inhibits the binding of fibrinogen to integrin receptors. In addition, inhibits osteocalcin production.
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O76080
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ZFAN5_HUMAN
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AN1-type zinc finger protein 5 (Zinc finger A20 domain-containing protein 2) (Zinc finger protein 216)
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MAQETNQTPGPMLCSTGCGFYGNPRTNGMCSVCYKEHLQRQQNSGRMSPMGTASGSNSPTSDSASVQRADTSLNNCEGAAGSTSEKSRNVPVAALPVTQQMTEMSISREDKITTPKTEVSEPVVTQPSPSVSQPSTSQSEEKAPELPKPKKNRCFMCRKKVGLTGFDCRCGNLFCGLHRYSDKHNCPYDYKAEAAAKIRKENPVVVAEKIQRI
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Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation.
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O76081
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RGS20_HUMAN
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Regulator of G-protein signaling 20 (RGS20) (Gz-selective GTPase-activating protein) (G(z)GAP) (Gz-GAP) (Regulator of G-protein signaling Z1) (Regulator of Gz-selective protein signaling 1)
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MPQLSQDNQECLQKHFSRPSIWTQFLPLFRAQRYNTDIHQITENEGDLRAVPDIKSFPPAQLPDSPAAPKLFGLLSSPLSSLARFFSHLLRRPPPEAPRRRLDFSPLLPALPAARLSRGHEELPGRLSLLLGAALALPGRPSGGRPLRPPHPVAKPREEDATAGQSSPMPQMGSERMEMRKRQMPAAQDTPGAAPGQPGAGSRGSNACCFCWCCCCSCSCLTVRNQEDQRPTIASHELRADLPTWEESPAPTLEEVNAWAQSFDKLMVTPAGRNAFREFLRTEFSEENMLFWMACEELKKEANKNIIEEKARIIYEDYISILSPKEVSLDSRVREVINRNMVEPSQHIFDDAQLQIYTLMHRDSYPRFMNSAVYKDLLQSLSEKSIEA
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Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is inhibited by the phosphorylation and palmitoylation of the G-protein. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:12379657}.
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O76082
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OCTN2_HUMAN
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Organic cation/carnitine transporter 2 (High-affinity sodium-dependent carnitine cotransporter) (Solute carrier family 22 member 5)
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MRDYDEVTAFLGEWGPFQRLIFFLLSASIIPNGFTGLSSVFLIATPEHRCRVPDAANLSSAWRNHTVPLRLRDGREVPHSCRRYRLATIANFSALGLEPGRDVDLGQLEQESCLDGWEFSQDVYLSTIVTEWNLVCEDDWKAPLTISLFFVGVLLGSFISGQLSDRFGRKNVLFVTMGMQTGFSFLQIFSKNFEMFVVLFVLVGMGQISNYVAAFVLGTEILGKSVRIIFSTLGVCIFYAFGYMVLPLFAYFIRDWRMLLVALTMPGVLCVALWWFIPESPRWLISQGRFEEAEVIIRKAAKANGIVVPSTIFDPSELQDLSSKKQQSHNILDLLRTWNIRMVTIMSIMLWMTISVGYFGLSLDTPNLHGDIFVNCFLSAMVEVPAYVLAWLLLQYLPRRYSMATALFLGGSVLLFMQLVPPDLYYLATVLVMVGKFGVTAAFSMVYVYTAELYPTVVRNMGVGVSSTASRLGSILSPYFVYLGAYDRFLPYILMGSLTILTAILTLFLPESFGTPLPDTIDQMLRVKGMKHRKTPSHTRMLKDGQERPTILKSTAF
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Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Relative uptake activity ratio of carnitine to TEA is 11.3. In intestinal epithelia, transports the quorum-sensing pentapeptide CSF (competence and sporulation factor) from Bacillus Subtilis wich induces cytoprotective heat shock proteins contributing to intestinal homeostasis. May also contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (Probable). [Isoform 3]: Retained in the ER, unable to perform carnitine uptake.
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O76083
|
PDE9A_HUMAN
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High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A (EC 3.1.4.35)
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MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLFCVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIMLQPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA
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Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart. Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein (Probable). In brain, involved in cognitive function, such as learning and long-term memory (By similarity).
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O76090
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BEST1_HUMAN
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Bestrophin-1 (TU15B) (Vitelliform macular dystrophy protein 2)
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MTITYTSQVANARLGSFSRLLLCWRGSIYKLLYGEFLIFLLCYYIIRFIYRLALTEEQQLMFEKLTLYCDSYIQLIPISFVLGFYVTLVVTRWWNQYENLPWPDRLMSLVSGFVEGKDEQGRLLRRTLIRYANLGNVLILRSVSTAVYKRFPSAQHLVQAGFMTPAEHKQLEKLSLPHNMFWVPWVWFANLSMKAWLGGRIRDPILLQSLLNEMNTLRTQCGHLYAYDWISIPLVYTQVVTVAVYSFFLTCLVGRQFLNPAKAYPGHELDLVVPVFTFLQFFFYVGWLKVAEQLINPFGEDDDDFETNWIVDRNLQVSLLAVDEMHQDLPRMEPDMYWNKPEPQPPYTAASAQFRRASFMGSTFNISLNKEEMEFQPNQEDEEDAHAGIIGRFLGLQSHDHHPPRANSRTKLLWPKRESLLHEGLPKNHKAAKQNVRGQEDNKAWKLKAVDAFKSAPLYQRPGYYSAPQTPLSPTPMFFPLEPSAPSKLHSVTGIDTKDKSLKTVSSGAKKSFELLSESDGALMEHPEVSQVRRKTVEFNLTDMPEIPENHLKEPLEQSPTNIHTTLKDHMDPYWALENRDEAHS
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Forms calcium-sensitive chloride channels. Highly permeable to bicarbonate.
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O76093
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FGF18_HUMAN
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Fibroblast growth factor 18 (FGF-18) (zFGF5)
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MYSAPSACTCLCLHFLLLCFQVQVLVAEENVDFRIHVENQTRARDDVSRKQLRLYQLYSRTSGKHIQVLGRRISARGEDGDKYAQLLVETDTFGSQVRIKGKETEFYLCMNRKGKLVGKPDGTSKECVFIEKVLENNYTALMSAKYSGWYVGFTKKGRPRKGPKTRENQQDVHFMKRYPKGQPELQKPFKYTTVTKRSRRIRPTHPA
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Plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. Required for normal ossification and bone development. Stimulates hepatic and intestinal proliferation.
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O76094
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SRP72_HUMAN
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Signal recognition particle subunit SRP72 (SRP72) (Signal recognition particle 72 kDa protein)
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MASGGSGGVSVPALWSEVNRYGQNGDFTRALKTVNKILQINKDDVTALHCKVVCLIQNGSFKEALNVINTHTKVLANNSLSFEKAYCEYRLNRIENALKTIESANQQTDKLKELYGQVLYRLERYDECLAVYRDLVRNSQDDYDEERKTNLSAVVAAQSNWEKVVPENLGLQEGTHELCYNTACALIGQGQLNQAMKILQKAEDLCRRSLSEDTDGTEEDPQAELAIIHGQMAYILQLQGRTEEALQLYNQIIKLKPTDVGLLAVIANNIITINKDQNVFDSKKKVKLTNAEGVEFKLSKKQLQAIEFNKALLAMYTNQAEQCRKISASLQSQSPEHLLPVLIQAAQLCREKQHTKAIELLQEFSDQHPENAAEIKLTMAQLKISQGNISKACLILRSIEELKHKPGMVSALVTMYSHEEDIDSAIEVFTQAIQWYQNHQPKSPAHLSLIREAANFKLKYGRKKEAISDLQQLWKQNPKDIHTLAQLISAYSLVDPEKAKALSKHLPSSDSMSLKVDVEALENSAGATYIRKKGGKVTGDSQPKEQGQGDLKKKKKKKKGKLPKNYDPKVTPDPERWLPMRERSYYRGRKKGKKKDQIGKGTQGATAGASSELDASKTVSSPPTSPRPGSAATVSASTSNIIPPRHQKPAGAPATKKKQQQKKKKGGKGGW
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Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER. The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER. Binds the signal recognition particle RNA (7SL RNA) in presence of SRP68. Can bind 7SL RNA with low affinity. The SRP complex possibly participates in the elongation arrest function (By similarity).
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O76095
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JTB_HUMAN
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Protein JTB (Jumping translocation breakpoint protein) (Prostate androgen-regulated protein) (PAR protein)
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MLAGAGRPGLPQGRHLCWLLCAFTLKLCQAEAPVQEEKLSASTSNLPCWLVEEFVVAEECSPCSNFRAKTTPECGPTGYVEKITCSSSKRNEFKSCRSALMEQRLFWKFEGAVVCVALIFACLVIIRQRQLDRKALEKVRKQIESI
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Required for normal cytokinesis during mitosis. Plays a role in the regulation of cell proliferation. May be a component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Increases AURKB activity. Inhibits apoptosis induced by TGFB1 (By similarity). Overexpression induces swelling of mitochondria and reduces mitochondrial membrane potential (By similarity). {ECO:0000250, ECO:0000269|PubMed:21225229}.
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O76096
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CYTF_HUMAN
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Cystatin-F (Cystatin-7) (Cystatin-like metastasis-associated protein) (CMAP) (Leukocystatin)
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MRAAGTLLAFCCLVLSTTGGPSPDTCSQDLNSRVKPGFPKTIKTNDPGVLQAARYSVEKFNNCTNDMFLFKESRITRALVQIVKGLKYMLEVEIGRTTCKKNQHLRLDDCDFQTNHTLKQTLSCYSEVWVVPWLQHFEVPVLRCH
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Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system.
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O76324
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DCO_DROME
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Discs overgrown protein kinase (EC 2.7.11.1) (Protein double-time)
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MELRVGNKYRLGRKIGSGSFGDIYLGTTINTGEEVAIKLECIRTKHPQLHIESKFYKTMQGGIGIPRIIWCGSEGDYNVMVMELLGPSLEDLFNFCSRRFSLKTVLLLADQMISRIDYIHSRDFIHRDIKPDNFLMGLGKKGNLVYIIDFGLAKKFRDARSLKHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGALPWQGLKAANKRQKYERISEKKLSTSIVVLCKGFPSEFVNYLNFCRQMHFDQRPDYCHLRKLFRNLFHRLGFTYDYVFDWNLLKFGGPRNPQAIQQAQDGADGQAGHDAVAAAAAVAAAAAASSHQQQQHKVNAALGGGGGSAAQQQLQGGQTLAMLGGNGGGNGSQLIGGNGLNMDDSMAATNSSRPPYDTPERRPSIRMRQGGGGGGGGVGVGGMPSGGGGGGVGNAK
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Involved in circadian rhythms, viability and molecular oscillations of the clock genes period (per) and timeless (tim). Dbt reduces the stability and thus the accumulation of monomeric per proteins, probably through phosphorylation. No evident circadian oscillation is detected in head. Together with CkIalpha, regulates processing of ci by phosphorylating it, which promotes its binding to slmb, the F-box recognition component of the SCF(slmb) E3 ubiquitin-protein ligase.
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O76329
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ACTNB_DICDI
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Interaptin (Actin-binding protein D) (Alpha-actinin B)
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MEHSTPLNEEIVHKKNDENWVIAQKKVFTNWCNIFLNQRSQKIEDLETDLYDGILLGSLLEILSGKNVILSKCKQLKTRLHYINNLNFSLKFIGDEGLRLVGVASEDITDGNLKLILGLVWTLILRYQIQSMQNSKSSQQNLHSSTKPSELMLNWVKSQISDYGHHIKDLTTSFQNGLLFCALVHKLVPEKLDYKSLSESDSLGNLTLAFEVANKELGIPSILDPHDIITTPDELSILTYISLFPKVYQQTLEPLNNNNNISPSLSSSSSSLLNTPNKRNSIQLSKSTSFEQQNQQQQQQNLLSPNSYRNSISFSKSPSFEGSQSTGSSRSISPISSPIKNSTTGNSNLSKSTSFEKIEASNTTNNNTIIIAEESRVIEKIVEKIIEVEKIVEVEKIVEVEKIVEVEKIVEVEKIVKVDDIEKLTNLQDQLTEQQQQYQEKSLKLVNLELELQEKSNQLVDKSNQLSTMQATNSELMEKIGGLMNDLTDIPTQDIKEKDEIIANLKIESEKNLKCFQDDFNALQSRYSLTIEQTSQLQDRIKQLINELQERDDKFIEFTNSSNQSLADNQRVIDQLTNEKQSITLQLQDQQDIKEKEFQFEKQQLLSQIDSITTNIQEYQDKFNNLQQEFNTQQTLNQQETHRLTQQLYQINTDYNEKQTQLQSEIKDNQTINEQLNKQLSEKDKEIEKLSNQQEQQQDEKINNLLLEIKEKDCLIERINQQLLENIDLNSKYQQLLLEFENFKLNSSKEKENQLNELQSKQDERFNQLNDEKLEKEKQLQSIEDEFNQYKQQQLSSNSNIDQQLQSTIIELSELKEQKELNDSKLIEKEKQLQQLQQEFDQLNEKNQKDHQDQLELLEKQLKQLQQEYDQLNETNQSIENQLNQQNLINKENLNEKEQELLKLQNQLNQQIEKIQFDQQEFSKQNSINIELVNEKNEKLIQLQQDYDQLKQQNRSNDEKDENDLIEKENQLKSIQNELNQLIEKNESDHKEQQLKQQSIENDLIEKENQIQQLQSQLNEQRQQQSNQLSEKDQQLNQLIEKNQFDQKEQQLKQQSIENDLFEKENQIQQLQSQLNEQRQQQSNQLSEKDQQLNQLIEKNESDQKEQQLKQQSIENDLIEKENQIQQLQLQLNEQRQLQSEVSIDNDKILELEKQLKQCQSDLLKLNDEKQQQDKQLQDKQIEFDQLQLTFNQFKNDKDSQFIQLQDDQKQQLQSIQQDLNQLKQENQEKEKQLSEKDEKLQSIQFENQEKEKQLSEKDEKLQSIQQNLNQLNDENQEKVKQFSEKDEKLQSIQQDLNQLKQENQEKEKQLSEKDEKLQSIQQDLNQLNDDQIKKNEKLKEKEEQLLKLQQDFNDQQSQQLKQLEEKLSEKENQLQQLKQENEINQLNQQQQSNEIIQQLKDQLLKQQQQEQQENNNEKEIERLIQEIEQLKQQQEIDQSELSNKEIKIQTTQQEFDQLSHNRSKDQLHLQQLQQELDQLKQSFDDQDHQFKKVIDERYNLQLQLEQSTLSNNQLDQLLKEKLKPLELDSNEKQKTIDDLLSNISNLQISLQNDKDLISERNNSIKTLESRITQQLSLLDEKDNLIKDLQQQKQQQQQPPTASSSPSSSPSLLSSTPTPKPQRPNQIEIDRLVNEIVNRNQDLIRKNKTKFYKLENGDYIVNSIIYRLSLDDDNDSDLIAQEYENGNSTTFEKSLRIFPSKNTRPIFDWRALFFIGAAVLAISTLFSSSRPIKYEKPT
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May function as linker between cellular membranes and the actin cytoskeleton. Required for normal development of fruiting bodies.
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O76337
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CED6_CAEEL
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Cell death protein 6 (Candidate adapter protein ced-6)
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MAKDIYKTFKRSVSGIVGGNNINGEGSSSPSTSAPQVKYRGGTGRTWIHPPDYLINGHVEYVARFLGCVETPKANGSDVAREAIHAIRFQRDLKRSEQTRETAKLQKVEIRISIDNVIIADIKTKAPMYTFPLGRISFCADDKDDKRMFSFIARAEGASGKPSCYAFTSEKLAEDITLTIGEAFDLAYKRFLDKNRTSLENQKQIYILKKKIVELETENQVLIERLAEALRANSKADYENTGPPIYPGLGPPALPLSPMPQGPPPNIPPSSIYSMPRANDLPPTEMAPTLPQISTSSNGASPSVSPASTSPSGPAPSIPPPRPPALAPPPPVAPRRNPVVSPKNSTAGLLDGLELGSAEPAKKAPSNIFDDSFDPRAGEKKSTAAEYNPFGADFLSGIQNGKEAPPSASAELLASEAIARLPKPESSSVPPKKTAAEYDAMINEVEKKLAAMSSGSFEFGQLQTGDLGGIEGESDYGTPSDRLNPKMMNLKQ
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May function as an adapter protein in a pathway that mediates recognition and phagocytosis of apoptotic cells during normal development. Promotes engulfment of cells at both early and late stages of apoptosis. Required for actin reorganization around apoptotic cells. Plays a role in protecting dopaminergic neurons from oxidative stress-induced degeneration. Mediates recruitment of E3 ubiquitin-protein ligase trim-21 to the apoptotic cell surface which promotes ubiquitination and degradation of ced-1.
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O76357
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ILYS3_CAEEL
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Invertebrate-type lysozyme 3 (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase)
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MFVKSLVFLTIAVAYASADCLHCICMRESGCKPIGCNMDVGSLSCGYYQIKLPYYEDCGQPTKKSGETTEAAWKRCANDLSCATTCVENYYNRYKSQCAGTGQGACEVMARNHNGGPQGCKHSGTLGYWNGIKSCCGCS
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Has bacteriolytic activity against Gram-positive bacteria. Plays a role in defense against bacterial pathogens. Involved in pharyngeal grinder function by enabling proper lysis of ingested bacteria.
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O76360
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EGL4_CAEEL
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cGMP-dependent protein kinase egl-4 (EC 2.7.11.12) (Egg-laying defective protein 4)
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MSSGSRPSSGGGGGGGGASGGAGGGAPGGGGGGIRGFFSKLRKPSDQPNGNQVQVGTRTFEAHELQKLIPQLEEAISRKDAQLRQQQTIVEGHIKRISELEGEVTTLQRECDKLRSVLEQKAQSAASPGGQPPSPSPRTDQLGNDLQQKAVLPADGVQRAKKIAVSAEPTNFENKPATLQHYNKTVGAKQMIRDAVQKNDFLKQLAKEQIIELVNCMYEMRARAGQWVIQEGEPGDRLFVVAEGELQVSREGALLGKMRAGTVMGELAILYNCTRTASVQALTDVQLWVLDRSVFQMITQRLGMERHSQLMNFLTKVSIFQNLSEDRISKMADVMDQDYYDGGHYIIRQGEKGDAFFVINSGQVKVTQQIEGETEPREIRVLNQGDFFGERALLGEEVRTANIIAQAPGVEVLTLDRESFGKLIGDLESLKKDYGDKERLAQVVREPPSPVKIVDDFREEFAQVTLKNVKRLATLGVGGFGRVELVCVNGDKAKTFALKALKKKHIVDTRQQEHIFAERNIMMETSTDWIVKLYKTFRDQKFVYMLLEVCLGGELWTTLRDRGHFDDYTARFYVACVLEGLEYLHRKNIVYRDLKPENCLLANTGYLKLVDFGFAKKLASGRKTWTFCGTPEYVSPEIILNKGHDQAADYWALGIYICELMLGRPPFQASDPMKTYTLILKGVDALEIPNRRIGKTATALVKKLCRDNPGERLGSGSGGVNDIRKHRWFMGFDWEGLRSRTLKPPILPKVSNPADVTNFDNYPPDNDVPPDEFSGWDEGF
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Promotes chemoreceptor gene expression in response to increased cGMP levels by antagonizing the gene repression functions of the class II HDAC hda-4 and the mef-2 transcription factor. Regulates gene expression via recruitment of a histone deacetylase complex containing hda-2, saeg-1 and saeg-2. Represses body size and lifespan through the dbl-1 and insulin pathways, respectively. May also signal through daf-3 and/or daf-5. Role in egg-laying, dauer formation and motility. Regulates behavioral responses to various chemosensory stimuli in sensory neurons. Required for the initiation of long term adaptation to prolonged odor exposure which results in a decrease in odor seeking behavior. May regulate this process by phosphorylating tax-2, a subunit of cyclic nucleotide-gated channel tax-2/tax-4. In ASH sensory neurons, negatively regulates avoidance behavior to some bitter tastants, such as quinine, probably by phosphorylating rgs-2 and rgs-3 which are 2 regulator of G-protein signaling proteins. In AWB sensory neurons, involved in avoidance behavior to some repellent odors. In ASE left (ASEL) sensory neuron, involved in the sensing of environmental alkalinity downstream of receptor-type guanylate cyclase gcy-14. In sensory neurons, involved in the signaling pathway downstream of insulin, TGF-beta and receptor-type guanylate cyclase responsible for inducing quiescence after food intake. Might play a role in aversive olfactory learning in AWC neurons when an odor is associated with food deprivation, depending on the ins-1/age-1 signal from the AIA to the AWC neurons. Probably by regulating neuronal transmission downstream of lin-3 and receptor lin-23 and phospholipase plc-3 in ALA neurons, involved in the decrease in locomotion during the quiescent state that precedes each larval molt.
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O76365
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CTU1_CAEEL
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Cytoplasmic tRNA 2-thiolation protein 1 (EC 2.7.7.-) (Cytoplasmic tRNA adenylyltransferase 1) (Thiolation of uridine in tRNA protein 1)
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MEKRRGPPPCQSGSGCSNPAKIRKAKDGAQLCGPCFSRNFEDDVHEAIVNNKLFKRGERVAIGASGGKDSTVLAYVMKTLNDRHDYGLDLQLLSIDEGIKGYRDDSLLAVEKNRVEYGLPLTILSYRDLYGWTMDDIVAKIGKKNNCTFCGVFRRQALDRGAFKIGATKLVTGHNADDMAETLLMNVLRGDIARLERCTNIVTGEEGDLPRAKPLKYCFERDIVMYARTNQLEYFYTECIYAPNAYRGYARKYVRDLEKVHPRAILDLIRSGEKVSVKKEVEMPTLKICERCGYMTSQKLCKACLLIEGLNTGNTDLGVRKSKKSKKVTVEADELNKEGGCGSGGGGGGCGCAGAEDAAENEETRQRLKDLQF
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Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. {ECO:0000255|HAMAP-Rule:MF_03053, ECO:0000269|PubMed:18391219}.
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O76373
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CBPC1_CAEEL
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Cytosolic carboxypeptidase 1 (EC 3.4.17.-)
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MPSDSDDVAAVKQPWSQLIVDISNFLSEHPQSKTSQALLPSCNGVWSDEEKLELIEAFGHKKQSHLTKSGVKAVLAAFEGDRTQPDVIFLCRLLHLIFSHFSSENDRKKEKYIVKCDVIATLTRITRKRIIMTLDVTDESSIDHNLDEVLWKLLHKIGLKDPRVSLKVRMGGLISPMCKLFIQKDTLPELFLPFFIKISRSPRNGQAIGRYEGFMTRLLVKIKALDASDQTSQVLLLDKHLQLLFFTMKNKRTRTQLLRENICKYLLEVLRRHLASSSNSRPTRLLSSLFGTFDKSLSAAHTEVVIGTIAILRLLSNFKKARDELKNLQVLDICSRELKEFWSDEWKTGPKSRIVDSLSALCLRCMSPLPYPLETRRFPIDFPLPTATPSTPGGHGRIRNSSSINISFDNGRSSDEDGMDEEDEAFVRDDDDEGKDDRGSDDDDGKDDDEINGALPKTTRLNPQQLAKYAPFFVENEQGTLQPTFSMIYQTNQESWRSICEKTRHVMPIHHHLPIEMFNTPTRIREKTAKTSNNMKKMIIEELDKPERSATSNQVIYDLDTAAFDGLPSPELPFVTGGGKLDTSKDLQFDSRFESGNLRMVIQVAPTHYELFLSPDVNQLRDHYQWFFFQVSNMRKSVKYTFEIVNCLKSTSLYSQGMQPVMYSMMESANGWRRVGENVCYFRNLYINENEEKKNVEEQKKKKYYYSIRFNVTFQNTGDICYIAYHYPYTYSFLNSSLSMLKKRKQENVYCREDVIGHSLAGNPIKMLTITTPASAAEIAAREVIVLSARVHPGETNASWIMQGILENLLCRQSNEMYRLRESFIFKIVPMINPDGVTNGSHRCSLAGIDLNRMWDRPNEALHPEVFATKAIIQYLCEVANKKPFAYVDIHGHSKKWDYFVYGNNASESWRADDVLDVGAAQLEEELHLALPKALEATCPSRFNASECRFNITRAKESSARVNVWRQFGVSTAYTLESTFCGFHKGQNSGYQINTSDLKEIGRDLLHSFLEMTKT
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Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation of proteins such as tubulins (Probable). Via the deglutamylation of tubulin, regulates the localization and velocity of kinesin motors and the structural integrity of microtubules in sensory cilia. In male CEM sensory neurons, regulates the cilia release of bioactive extracellular vesicles. Also regulates microtubule dynamics in uterine muscle cells.
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O76411
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SCD2_CAEEL
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ALK tyrosine kinase receptor homolog scd-2 (EC 2.7.10.1) (Suppressor of constitutive dauer formation protein 2)
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MRKRRLWWFVVLFRVTLVGAILPNETFDVRRYYADRFLIEDEENGSSRSYYISAESKAKAAEQFALLAPNCSLTSDIQENTCNETSSFCDHRVDSTYKTYHYEQEKCNCFIETCDEETNSTELMVLYPDCYCGKREKHCDLSKEKCHWTPDSDHDDLKFEVFESSNKVLFDYMLQAGSEKANLKMNKVSMVSKFFRQSGFNCSLRFMHHFTHQSSTSRLVVRSILQSGEKKNLYEHWLKPASVFWVPVQVAIGSYAEPFKISIDCETGFPPKKKKNKPFTCSIADIYFENCGEIRDPIEQCSRGDQFLCSISANTRCLQNAQCDSRIDCDDESDEMDCGNINGTMCDFNGQDYCNSWYQVTNVTDYHERLSEPTTVAPLNKLNEVPLHLFRLQSPSAKIKEAMRGSGNMLVFDHKPNPLTRRTSALVSPELPRTNPEAYDEKSPLFKSCKLRFYLCSRTYSKVWQISVISKGINPMESGRTIIYEAGYTLIPKENCTWERVFVNIPRQNAGFRIGIFVTNYFPGSEEYVAIDNLSFSPTCFERDINQSTWDIPDLFINTCGASGFEQPQNCDHNRELDGQTGHFLKEDGTQQWTVPVTGFYRMEICGAGGGSNSKASGDTGDCVTLQVHLIENLSLRMLIGQMGESPCFTEHDDELRPSSCSKISHNYVYDGKRGAAGGGATLLTVEKDLWNVVAGGGAGASWDGFDMEVGYGASAIHVKPDQRCNETCKAVSHTDFIVERRDNRCPGEKGESTVFGGFGGGGNSCGMLGGSGAGYQAGNPFGKSRARSGSSNVSIDFSKSPIYYQSERLDEGYIKIAFCRKRCEPPTVCRFRKDYFEEEYCGCPDGSNVTDTEEACAFPLVCPSSSTNQYRNFTYEPFCLCNNGKEIYDVYNDTCEEIQIWTLYNITFLIFAALTIIGALFVVYHYRNREKQMKQEILDLTQMKSPDYLYDDIYFGRTTRKAALDSLPSISRDSIERGRVLGRGNFGEVYYGEYSGVKLAVKMISRTFSASQASQSDFCNEALCMGTFVDENVVRLIGIDFEKVPYMIALEYMEGGDLLSFVKECRPNQVSLNPFQLAMSDLIKICCDVAAGCKCLETFGYVHRDIAARNILLTTRGPQRVAKIADFGMAKEITYGTEYYRINGRTMMPIKWTPPEAFIDGVFTTKSDIWSFGVLCWEVFSLGVVPYPNRRNEEVMLMLTEGARLEYPYGIPTRVYQLMRDCWKTAAADRPKFVDVVEIFQDIQDDPASVGMPFPIHPAVRATFAHSQSTPVSVETPMTAMTEISLNSTFTDASTVKVSAQQDMQDRIQLHELMLTREHPYTSELTSYVVNSIRKDLARVQYENGLTSVPQPEYLSPENNDESVQLIPQSNTVTDQTPPTSLIDLNRLGVQNTGPTLHRPDSLNFNDPYSSVPLLECQTR
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Probable tyrosine-protein kinase receptor which regulates the dauer/non-dauer developmental decision probably by controlling daf-3 transcriptional activity in parallel or together with the TGF-beta pathway. Regulates integration of conflicting sensory cues in AIA interneurons. May act as a receptor for hen-1. In AWA neurons, together with hen-1, plays a role in regulating olfactory adaptation by controlling the forgetting sensory responses to odorants such as diacetyl.
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O76460
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RAD54_DROME
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DNA repair and recombination protein RAD54-like (DmRAD54) (EC 3.6.4.-) (Protein okra) (RAD54 DNA repair protein)
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MRRSLAPSQRGPLRPESRHSFTPPLLKKNKRSCQQELEREQELDRRRLGALRDASNTSELPLPIRFTANSEYELAIAKVLARKFKVPMDNYVPDYGGKRVLGVRRCISRRPLHDPMACNALVLFHPPAYTEHERMGMDPTKVLVHVVVDPLLSNILRPHQREGVRFMYECVEGKRGNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPECKPTINKAIVVSPSSLVKNWEKEFTKWLHGRLLCLPMEGGTKENTIRALEQFSMTSARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSTEQERQRAIEKTQELIGLVDQCIIRRTNQILTKYLPVKFEMVICAKLTAIQLELYTNFLKSDQVRRSLADCNEKASLTALADITTLKKICSHPDLIYEKLTAREKGFENSQNVLPSNYKPKDLNPELSGKFMLLDFMLAAIRAEGNDKVVLISNYTQTLDLFEQLARKRKYGFVRLDGTMSIKKRSKVVDRFNDPESDSFLFMLSSKAGGCGLNLIGANRLFMFDPDWNPANDEQAMARVWRDGQKKPCYIYRLVASGSIEEKILQRQTHKKSLSSTIIDNNESAEKHFTRDDLKDLFTFDANILSDTHDKLKCKRCVQNIQMKPPPEDTDCTSHLSQWYHCSNNRGLPDNILAQAWMDCKCVSFVFHHRSQAQEIVPSAEEEATDQPEEKPESRKRSSTPASDDSADEDFRGF
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Involved in mitotic DNA repair and meiotic recombination. Functions in the recombinational DNA repair pathway. Essential for interhomolog gene conversion (GC), but may have a less important role in intersister GC than spn-A/Rad51. In the presence of DNA, spn-A/Rad51 enhances the ATPase activity of okr/Rad54.
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O76512
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RENT1_CAEEL
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Regulator of nonsense transcripts 1 (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent helicase smg-2) (Nonsense mRNA reducing factor 1) (Up-frameshift suppressor 1 homolog)
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MDDSDDEYSRSHGETLTFVDPEDDGVSIGNTQDSQFAYEQFSVPTQSSQATDLLPGGTDGTTNDLPFHDVEDDESDSEKSLTEEQHEQKLPEHACRYCGISDPLCVAKCTVCRKWFCNSNDGTSGGHIVHHMVRSQHKEAYTHKDSPCGDTQLECYRCGSKNVFNLGFIPGKKDQVVVIICRTPCASIAFQNDDNWSPEDWKSVIAEKQLLSWIVNVPSEEQVARARKITATQAVRMEELWRDHPEATVDDLNKPGLDREPDHVQLRYVDAHHYSKVFRPLVAIEAEYDRRVKESASQAVGTVRWEQGLRQSVLAFFHLPQFADGVMKLAKGDELRLKHSQTVDGSEWTKIGSVFKIPDNHGDEVGIEIRGAVDKSVMESRIMFTVDVVWNATTFERQYKALAALLNDSKAISPYLYQKLLGHPAEEMMLKFDLPRRLSVAGLPELNSSQMQAVKQVLTRPLSLIQGPPGTGKTVVSATIVYHLVQKTEGNVLVCSPSNIAVDHLAEKIHKTGLKVVRLCARSREHSETTVPYLTLQHQLKVMGGAELQKLIQLKDEAGELEFKDDLRYMQLKRVKEHELLAAADVICCTCSSAADARLSKIRTRTVLIDESTQATEPEILVSIMRGVRQLVLVGDHCQLGPVVICKKAAIAGLSQSLFERLVLLGIRPFRLQVQYRMHPVLSEFPSNVFYDGSLQNGVTENDRHMTGVDWHWPKPNKPAFFWHCSGSEELSASGTSFLNRTEAANVEKLVSKLIKAGVQPHQIGVITSYEGQRSFIVNYMHTQGTLNSKLYENVEIASVDAFQGREKDYIIVTCVRSNDILGIGFLSDPRRLNVAITRAKYGLVLVGNAKVLARHDLWHELINHYKSKEMLYEGPINALKPLNLALPKATIRTKNNIAGNANRFGIKRMQYTFNEYKSNDPSQPRLPPTYSNSQNLLSMSKLAQTFNKNVPIPAHMMDPNVYAAARNQKDRRRGDQRRPPPQAEAAMDLSQGMMSQQSQQYPPQGASSQSQYLLDGASSLSGWSQSQTTTTTTRHHHHRQNRNSQQQMSQDMDDIQQKMDDLLFSQDC
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RNA-dependent helicase required for nonsense-mediated decay (NMD) of aberrant mRNAs containing premature stop codons and modulates the expression level of normal mRNAs. 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 smg-2-3-4 surveillance complex is believed to activate NMD (By similarity).
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O76584
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GPA11_CAEEL
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Guanine nucleotide-binding protein alpha-11 subunit
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MSAADMARKNSLINRQLEKEKIDSKKMLKILLLGGPECGKSTIFKQMKIIHMNGFSDLDYVNFRYLIYSNIMQSMDQLLEAAEFFHFPPDDSPSIRRALNHYKSYKVRYSTSEVELNRELADSLSKLYNAEFIKSVLNRKNELKLLDSAVYFLDDIDRISAHEYKPTEMDVLRARVPTTGITEIEFPFKQASLRMVDVGGQRSEQRKWIHCFDNVNGVLFIAAISGYNLYDEDEENRKDDGTPTKTNRLRYSMELFKRIANHQCFSKKTAMILFLNKIDIFKEKIGKYPLTTCFKNYKGVNAFEPACKYVTDRFSRLVSGDIQHEKPLYTHITNATDTRNIDRVFDSCMDVIFKISMEKVGFM
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Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Mediates the transduction of food and serotonin signals, which modulates the avoidance response to the odorant octanol. Has a role in lifespan to promote longevity.
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O76616
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PID3_CAEEL
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Protein pid-3 (piRNA biogenesis and chromosome segregation protein 1) (piRNA-induced silencing defective protein 3)
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MVAHQKADFKSKWAMVVTVNNLNDKKRADLREFSEWFIETLRLEGAFIGHYFNYEAAPVTIVETLPGNFDSCTNAYQKIHKEHPQVVLVVHILPQSQSNEYEWMKVLASRYGFVRQGLLYDNCANRFQNVETDQNSVFRNMCQWIYRSGTAIVRNEGNACGILHGKDPKPTFDKVLFNSEDIKDSVFKVLHAEEEPRGADQENMLKISGYPGMLNTFGIAQLLTPYRVNGITITGAQSAVVALENKFQVYQAVQDFNGKKLDRNHKLQVSSLVVSSPAVPLEWPSLKKSKKLVEQVGKPIRLSKVSS
|
Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively. Within the pid-1 variant of the PETISCO complex may stabilize 21U-RNA precursor molecules. Promotes the biogenesis of 21U-RNAs. Required for chromosome segregation and cell division in early embryos.
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O76689
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SNF6_CAEEL
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Sodium-dependent acetylcholine transporter (Sodium:neurotransmitter symporter family protein 6)
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MSVSSNDPEQRNGRGMASGNNVDMSLYPPFIKQLDAKLPDYTREGDIEYPFEEITGVGDENRIRGNWSNKSDYLLAVIGFTAGVGSFWKFPFLVFQHGGAAFLVPYLCMLCLASLPMFFMEMVLGQFSSSAAISVWKVVPLFKGIGFAQVTISGFFAVFFNIISAWTLFYLINSFSFSIPWSNCANSWSGENCTLGTRIQCKEMNGTLLVNGSCIVEHASSNETTVIPLHDLGSIPSLKYFHNDVLMLSKGVDDFGTLNWYLGLCVLACWIAVFLCLFQGVKSSGKVVYVAVIVPFIILTVLLTRLLTLDGSLAAVFYFLTPKWEILMDLHVWGEAAVQAFYSVSCCSGGLFTIASYSRFHNNIYKDIWLVLIVDVIVSLVGCLLTFSAIGFTCYEFAISLDKFHIRDGFHLVFVFLAEALAGVSVAPLYAGLFFIMILLVVHATQMFVVETIVSSICDEYPERLRRNRRHVLTTVCALFILLSIPFCLSSGLFWMELLTQFVLTWPLVVIAFLECMAINWVYGVDNMLDNAKWIVGYWPPCYIFWKILFKFICPMVYLAILCFLWLDWNSIQYESYQFPYWSILTAWCIASFPLILIPIVGIWQFCIAKGTITQKWWRVLYPDDAWGPAMAIHRAEKFPLQIPEARRLLLPPEVEIASSRGVLQEEMPMSYDYNTSSAADVRSNRSTGHGATDVRSVAATNNTIPKFERETAI
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Mediates sodium-dependent uptake of acetylcholine at neuromuscular junctions during periods of increased synaptic activity, may also prevent spillover to adjacent synaptic sites. Not involved in the uptake of other neurotransmitters (GABA, glycine, proline and glutamate) and there was also no inhibition of uptake by adding an excess of other candidate substrates (GABA, glycine, taurine, creatine, proline, alanine, carnitine, glutamate and betaine). Required for muscle integrity altered transport of acetylcholine due to loss of dystrophin-glycoprotein complex (DGC) function results in muscle degeneration.
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O76743
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GLH4_CAEEL
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ATP-dependent RNA helicase glh-4 (EC 3.6.4.13) (Germline helicase 4)
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MSFSDDGWGAEAEVKVAEDVPEKNVPPPVEPPRAPQSTAIKTEPERNSDEPSAGFGIDPITTSKTFGSQTTPKTEFGGAPSLSGFGGNAAAAAANKTSFDQQGNGFGGAAKHGFGGVGGAPSSFGANVIPVNKPSLGHKTTGFGGEPKHVSGGAFSSANNFDQQDKGFGGAASSGFGNGSMLTNQKVGLENQTTGVGASEVPTSKPSSFGQQPAVVSGFGGAAKMGFGGSSSSGFGGQKAGATESSGFPTKETSTSQPGFGGDSSTGFGSGLKAGFGGHGAGAAENSGLPTETTGFGGKLPSAGFGASSSNESAFGQQSKGFGGATKNGFGGDSSSSFGSGSKAGFGGTSSSGIGGQKPGATESSGFPTKETSTSGGTFGSGFGGKPTSTGFGAPSTTDSSSGQQTAGFGGASKPGFGGDSSTGFGSGLKAGFGGHRASTAENSGLPTETTGFGGKLPPAGFGASSSNESAFGQQSKGFGGATKNGFGGDSSNSFGKRDSGFGGPQDQGFGDTDAPSKSGLGSFNTGGGAVKSAFGAAGFGSSSNFGNGNTFGEPSDNQRGNWDGGERPRGCHNCGEEGHISKECDKPKVPRFPCRNCEQLGHFASDCDQPRVPRGPCRNCGIEGHFAVDCDQPKVPRGPCRNCGQEGHFAKDCQNERVRMEPTEPCRRCAEEGHWGYECPTRPKDLQGNFLESYDFVFTPDDKMFEDAVNNDDKIDFDQKVVASTGKVEIPDMASFDGFKILPQDLHDNLKRMKMNRPTPIQRASFFPIMHGNDVVACAHTGSGKTLAFLIPFVIKLMEEFEKDRDVTDEKPSPRLLIVAPTRELVNQTFTTARQLTYETGLKCGLAFGGYSRNANVQHLRSFSQLNILVATMGRLQDFVNAGEVSLSKMKYIVLDEADRMVDSNDFGEEVSKIIGSPGERTQQTVLFSASFSEDLQSDDLPKFVKEGYTMLQVDKFGTANEKIDQKILPVPRTEKRDAIYKLLGIDENTVTLLPDAPIEKQKTLIFVNSVKFCDTLAALISSAGVSTISMHSYQNQEQRDRTLDDFRRGKYQCMVASNVCARGLNIAGLDHVVNYDMPDKNGFDEYVNRIGRTGRAGFTGTSTAFVDVENDTDIIPCLVSILNEAKKEVPEWLTEGAGHQEEGGDDWNEQEQEW
|
Probable ATP-binding RNA helicase. May act redundantly with the P-granule component glh-1 to regulate the formation of the granular structure of P-granules in embryos. May protect somatic cells from excessive apoptosis during normal development.
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O76745
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NP_CIMLE
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Nitrophorin Cim l NP (NP) (Salivary nitrophorin) (cNP) (allergen Cim l NP)
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MKLLLSAGAALAFVLGLCAAGSPPAQLSVHTVSWNSGHERAPTNLEELLGLNSGETPDVIAVAVQGFGFQTDKPQQGPACVKNFQSLLTSKGYTKLKNTITETMGLTVYCLEKHLDQNTLKNETIIVTVDDQKKSGGIVTSFTIYNKRFSFTTSRMSDEDVTSTNTKYAYDTRLDYSKKDDPSDFLFWIGDLNVRVETNATHAKSLVDQNNIDGLMAFDQLKKAKEQKLFDGWTEPQVTFKPTYKFKPNTDEYDLSATPSWTDRALYKSGTGKTIQPLSYNSLTNYKQTEHRPVLAKFRVTL
|
Heme-based protein that delivers nitric oxide gas (NO) to the victim while feeding, resulting in vasodilation (Probable). In place of heme, the heme-binding cysteine can also reversibly bind NO when it is present in high concentrations.
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O76818
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PBAN_AGRIP
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PBAN-type neuropeptides (Pheromone/pyrokinin biosynthesis-activating neuropeptide) [Cleaved into: Diapause hormone (DH); PBAN precursor-related peptide 1 (PBAN-PP-1); PBAN precursor-related peptide 2 (PBAN-PP-2); Alpha-subesophageal ganglion neuropeptide (Alpha-SG neuropeptide) (Alpha-SGNP); Beta-subesophageal ganglion neuropeptide (Beta-SG neuropeptide) (Beta-SGNP) (Pyrokinin-1); Pheromone biosynthesis-activating neuropeptide (Agi-PBAN) (Pyrokinin-2); Gamma-subesophageal ganglion neuropeptide (Gamma-SG neuropeptide) (Gamma-SGNP) (Pyrokinin-3); PBAN precursor-related peptide 3 (PBAN-PP-3)]
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MYGAVLPGLFFIFISCVVASSNDVKDGGADRGAHSDRGGMWFGPRIGKRSLRMATEDNRQAFFKLLEAADALKYYYDQLPYEMQADEPEARVTKKVIFTPKLGRSLSYEDKMFDNVEFTPRLGRRLADDTPATPADQEMYRPDPEQIDSRTKYFSPRLGRTMNFSPRLGRELAYEMLPSKVRVVRSTNKTQST
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[Pheromone biosynthesis-activating neuropeptide]: A hormone that controls sex pheromone production in female moths and pheromone responsiveness in male.
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O76840
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PPN1_CAEEL
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Papilin (Abnormal cell migration protein 6)
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MRLLLFSAALLLCSVPTWAFSLSSFFGSDVAQKPYLHPNSPPERDPASSRMKRQAYQVYVDGDVSVTVDKSGQKETGNWGPWVPENECSRSCGGGVQLEKRQCSGDCTGASVRYISCNLNACESGTDFRAEQCSKFNDEALDGNYHKWTPYKGKNKCELVCKPESGNFYYKWADKVVDGTKCDSKSNDICVDGECLPVGCDGKLGSSLKFDKCGKCDGDGSTCKTIEGRFDERNLSPGYHDIIKLPEGATNIKIQEARKSTNNLALKNGSDHFYLNGNGLIQVEKEVEVGGTIFVYDDAEPETLSAQGPLSEELTVALLFRKGSRDTAIKYEFSIPLEEEVDYMYKFDNWTPCSVSCGKGVQTRNLYCIDGKNKGRVEDDLCEENNATKPEFEKSCETVDCEAEWFTGDWESCSSTCGDQGQQYRVVYCHQVFANGRRVTVEDGNCTVERPPVKQTCNRFACPEWQAGPWSACSEKCGDAFQYRSVTCRSEKEGEEGKLLAADACPADEQEKFDTERTCNLGPCEGLTFVTGEWNLCTRCNDTEETREVTCKDSQGRAYPLEKCLVDNSTEIPTDTRSCATQPPCEYEWTVSEWSKCTTECGHGHKTRRVICAIHQNGGLEVVDEGHCQAEKPEGKTNCTNEEKCTGTWYTSSWSECTAECGGGSQDRVAVCLNYDKKPVPEWCDEAVKPSEKQDCNVDDCPTCVDSEFGCCPDNSTFATGEFNFGCSNCSETEFGCCADNVTVATGPNSKGCEEFVESPLNLEADVANADAEASGDAPELCSVTNENGEAVDVECATIAPITALLGDGELIGNDTDASNETIHCSKTEFGCCPDWYTAASGKGNEGCPSFTLGGCNETQFGCCHDDVTLARGANLEGCGEPSCAASLYGCCKDRKTIAFGPHYSGCERSSFPCELSDFGCCPDGETAALGKNGTGCGENCLTTKFGCCPDGKTTAKGSHNEGCGCEFAQYGCCPDGKSVAKGAGFYGCPESCAQSQFGCCPDGKTRARGENKEGCPCQYTRYGCCPDGETTALGPRNDGCDNCRYAKHGCCPDGETKALGPDGAGCPPTTTPPFLMGGTVAPHKIAACNQTQESGTVCGAGYKLAWHYDTTEGRCNQFWYGGCGGNDNNFASQDMCETICVEPPGKGRCYLPRVDGPLRCDQLQPRYYYDHSKKHCVAFWWRGCLGNANNFNSFEECSMFCKDVGPYDAPTTAAPPPPPQQNAQQYLPTPEVQQIEIQSAEQPQPQQPQQQQQQQQQQPQQPRQSMEDICRSRQDAGPCETYSDQWFYNAFSQECETFTYGGCGGNLNRFRSKDECEQRCFFVHGAQPSAARQEQAQPAAQPAQPAQPSNIVSPPQQSASPVVVPSNSKQRDACHLNVDQGRCKGAFDSWYYEVATGSCVTFKYTGCGGNANRFASKDQCESLCVKPASEAASAGIDGAAGINSVCDEAKDTGPCTNFVTKWYYNKADGTCNRFHYGGCQGTNNRFDNEQQCKAACQNHKDACQLPKVQGPCSGKHSYYYYNTASHQCETFTYGGCLGNTNRFATIEECQARCPKDDQTTTTSQPEELPSLPLVQEDPQPRPAFSLKQSFAHSRRRDAPFARSVSARHHTPDSEEERVDCYAVPDPGSCGDYRLVWHYSATSNSCRQFYYGGCAGNTNRFETRDKCETSCVAKIEERVESVSEASKSLEEVRLTDPRMDSHFGYHDPEVDQIEEEAEYVIVDTGALPELCMLPEQRGSCYDNILRWRFDSEKSQCVTFMYSGCNPNANHFTSQETCERACGKWRNVAVCELPAEHGDCQLAIPRWYHDPKTSQCQMMMWTGCGGNGNAFSSKADCESLCRVETLWSNNTDFCTLERSAGPCTDSISMWYFDSTHLDCKPFTYGGCRGNQNRFVSKEQCQQSCRPGDTKSEDICTLRPEPGPCRLGLEKYFYDPVIQSCHMFHYGGCEGNANRFDSELDCFRRCSSVKVEASESERVGQLTSASTPVIYIVNKTAIFVGNTFRIRCNSYGVLPITWYKNGGLLQFGSRITEENDDTLEIVDALTADAGVYTCIAGQDSTMSEGVEVVIKRLPGHRTTSRPMLTPSKNFSLGTPPTPSPSTVSTTPFRIYTPGSAPSDARVSRPTSNSCMDVGNASTCDLIVKNGLCGKKRYGTFCCHTCTRVHNFKF
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Involved in pharynx morphogenesis probably by remodeling the basement membrane. [Isoform a]: Plays a role in embryogenesis, the second phase of distal cell tip migration and is required for distribution of the metalloproteinase, mig-17, during organogenesis.
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O76856
|
CATD_DICDI
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Cathepsin D (EC 3.4.23.5) (Ddp44)
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MKLLILTLFLATIVLAQALTVPLNFHQASRESRRRVPQKWSNRLSALNAGTTIPISDFEDAQYYGAITIGTPGQAFKVVFDTGSSNLWIPSKKCPITVVACDLHNKYNSGASSTYVANGTDFTIQYGSGAMSGFVSQDSVTVGSLTVKDQLFAEATAEPGIAFDFAKFDGILGLAFQSISVNSIPPVFYNMLSQGLVSSTLFSFWLSRTPGANGGELSFGSIDNTKYTGDITYVPLTNETYWEFVMDDFAIDGQSAGFCGTTCHAICDSGTSLIAGPMADITALNEKLGAVILNGEGVFSDCSVINTLPNVTITVAGREFVLTPKEYVLEVTEFGKTECLSGFMGIELNMGNFWILGDVFISAYYTVFDFGNKQVGFATAIQG
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Protease that may act during cell growth and/or development.
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O76902
|
PKHF1_DROME
|
Pleckstrin homology domain-containing family F member 1 homolog (PH domain-containing family F member 1 homolog) (Protein rush hour)
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MVDRLVNSEANTRRIASVENCFGSSGVPLAMQGRVLVGEGVLTKMCRKRPKSRQFFLFNDILVYGNIVIGKKKYNKQHIMPLEEVSLESIADNQTYRNGWYIRTTTKSFVVFAATSTEKQEWMAHINKCVEDLLRKSGKKPVENHAAVWVPDTDASVCMHCKKTQFTFIQRRHHCRNCGAVVCAGCSAKKFLLPQQSTKALRVCDACYERLKHVPSSLGSGEDSAAATGAASGNKLNTTAGDSSNDEDSDEETASPGGESHDEPRFYGDNSVLSAVEDSSTITSPSSATTGSLEAPQVTPSVQSSPAAVATTGSHC
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Functions in the regulation of endosome morphology and late endosome formation. Has a role in controlling trafficking from early to late endosomes and from late endosomes to lysosomes. Important for localization of Gdi to the endosomal membranes. May function in controlling the activity of multiple regulators in the endocytic pathway, perhaps by positively controlling those involved in the early steps of endocytosis such as Rab5 and hrs, and negative regulating those involved in the late stages of endocytosis like car and VhaSFD.
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O76906
|
CRM_DROME
|
Protein cramped
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MEELSKQPPPPPLTQPPPPSSSVSIEEPLPNGKGGGAVVVNSIAKLPEEELLGSVTMHNCPGTRASARVIQKMKQDQTRPMTPPPSEREPNKKEEKAAQKTPSQLKTGSGKTTWTNVERNCFFDALNEFGKDFEAVANCINAKLKRRNANSDYSFKTKDQVRQHYYQTHHKICKYVRFSEELKKPAQELYTLINYGEMRRKLQFLTEKHFMKLKQLVYQGQITVRCKGKNIRIKTPSCKALRRLNQLDDSLEDIRLPSKVEVLVTPANMEAFGRVQSLAQNPRGRIIVPLHKKLISFIKTFEYKWRSANQRLHEEKSAYFSSSLPSAASNNNNNNNETEPLQPSVASLDPSMCFQPRPGVAIHRPLLSITAYLSSISICLTAYEERMGFKVRSETLGNLAGMSVAANKRLRTESGSEKRSPETKKPKSSASPPLEKSLDDGPLEGNLMKMENSSGDELGEEIHEFLGDILEAMQHPQAATIPALSATTGDTTNVAVALETSHDPVQQAYPANADLSNAMATSVLQTSCAAAPAPSTPVTGSLAAPSVARSKRKEAKEAAAAAQARNFKPLLSDDILKRIRKGWTQANAADITIGDLYVVFGQDSKLELEYYWCEVDSSTAMASSILTINTVTPSSSSVGTQTGSAASNANQTGASSNCYVSASSNSSTSSTSLPYNPNDCDSVERVRAVTTSSVSNKLKHLLLVANLSERVRKRQCNCGHTCDRKRDLMTKAQQLAEATATGGVGGMVEGNFRTPMLPVRRPISNIDPVRQLSALTRQKISRQVLVQRRLLPPTSAGDRPYDLLSVRQLHSGLFEPIDRVDGTSSAGISTSGSKPDCSMNAMTASQDQEPGDQGALEFLNDEATQVSARDMPNLDICVATNRTDVSSSLNEAAQDGSTTQSFFQGSMSPMHLLRDSTSNARWLEDNINDFSLTSLLGHLDEIDATRDILDPSSSMSVISESSVDFRHKFQEIAALLQQQEKD
|
Polycomb group (Pc-G) genes are needed to maintain expression patterns of the homeotic selector genes of the Antennapedia (Antp-C) and Bithorax (Bx-C) complexes, and hence for the maintenance of segmental determination. Can act as a modifier of position effect variegation (PEV).
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O76908
|
VILYA_DROME
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RING finger protein vilya
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MAKSQAGQTVEPEASKLWIHCNSCCALFCDKKHTFFLLACHHVFCERCVKVSAGRTPSDAPIFECSTCRRSVRGRQLTNSMPNHFKQLFHPEPFTIGNDFVETFQRGNHRHFDKYKERKELEMDKLFKDIEVAKSVCQKRFLEAQMLRVERKKLMQRSRYIKAEVANRKAEMHRMAQAYRSRSLTSQSSSSAQRSARGRPRGRGTATQSSSRRRSTESAKRQQITSFIHPPNNSFDL
|
Required for the formation of DNA double-strand breaks during meiosis together with narya and nenya.
|
O76922
|
AUB_DROME
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Protein aubergine (Protein sting)
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MNLPPNPVIARGRGRGRKPNNVEANRGFAPSLGQKSDPSHSEGNQASGGNGGGGDAQVGPSIEKSSLSAVQMHKSEGDPRGSVRGRRLITDLVYSRPPGMTSKKGVVGTHITVQANYFKVLKRPNWTIYQYRVDFTPDVEATRLRRSFLYEHKGILGGYIFDGTNMFCINQFKAVQDSPYVLELVTKSRAGENIEIKIKAVGSVQSTDAEQFQVLNLILRRAMEGLDLKLVSRYYYDPQAKINLENFRMQLWPGYQTSIRQHENDILLCSEICHKVMRTETLYNILSDAIRDSDDYQSTFKRAVMGMVILTDYNNKTYRIDDVDFQSTPLCKFKTNDGEISYVDYYKKRYNIIIRDLKQPLVMSRPTDKNIRGGNDQAIMIIPELARATGMTDAMRADFRTLRAMSEHTRLNPDRRIERLRMFNKRLKSCKQSVETLKSWNIELDSALVEIPARVLPPEKILFGNQKIFVCDARADWTNEFRTCSMFKNVHINRWYVITPSRNLRETQEFVQMCIRTASSMKMNICNPIYEEIPDDRNGTYSQAIDNAAANDPQIVMVVMRSPNEEKYSCIKKRTCVDRPVPSQVVTLKVIAPRQQKPTGLMSIATKVVIQMNAKLMGAPWQVVIPLHGLMTVGFDVCHSPKNKNKSYGAFVATMDQKESFRYFSTVNEHIKGQELSEQMSVNMACALRSYQEQHRSLPERILFFRDGVGDGQLYQVVNSEVNTLKDRLDEIYKSAGKQEGCRMTFIIVSKRINSRYFTGHRNPVPGTVVDDVITLPERYDFFLVSQAVRIGTVSPTSYNVISDNMGLNADKLQMLSYKMTHMYYNYSGTIRVPAVCHYAHKLAFLVAESINRAPSAGLQNQLYFL
|
Acts via the piwi-interacting RNA (piRNA) metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. In ovary, associates predominantly with antisense piRNAs that contain uridine at their 5' end. In testis, associates with Su(Ste) antisense piRNAs (most abundant class of piRNAs found in complex with aub in testes) and negatively regulates Ste expression, most likely by cleaving its transcripts. Also in testis, may repress translation of vas when associated with a piRNA derived from chromosome X, termed AT-chX-1, whose sequence shows strong complementarity to vas mRNA. Aub-piRNA complexes from ovary and testis possess RNA cleavage activity. Involved in telomere regulation by repressing specialized telomeric retroelements HeT-A and TART Drosophila telomeres being maintained by transposition of specialized telomeric retroelements. Also involved in telomeric trans-silencing, a repression mechanism by which a transposon or a transgene inserted in subtelomeric heterochromatin has the capacity to repress in trans, in the female germline, a homologous transposon, or transgene located in euchromatin. Involved in the suppression of meiotic drive of sex chromosomes and autosomes. Involved in transposon silencing in the adult brain. Required for dorsal-ventral as well as anterior-posterior patterning of the egg. Required during oogenesis for primordial germ cell formation and activation of RNA interference. During early oogenesis, required for osk mRNA silencing and polarization of the microtubule cytoskeleton. During mid-oogenesis, required for osk mRNA localization to the posterior pole and efficient translation of osk and grk. During embryogenesis, required for posterior localization of nanos (nos) mRNA, independently of osk, and pole cell formation. Essential for the formation and/or structural integrity of perinuclear nuage particles. Required for the localization of Mael to the meiotic nuage. Forms a complex with smg, twin, AGO3 and specific piRNAs that targets nanos mRNA (and probably other maternal mRNAS) for deadenylation promoting its decay during early embryogenesis.
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O76924
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ARI2_DROME
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Potential E3 ubiquitin-protein ligase ariadne-2 (EC 2.3.2.31) (Protein ariadne-2) (RING-type E3 ubiquitin transferase ariadne-2)
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MDSDIEMDMESDNDGEYDDDYDYYNTGEDCDVERLDPKRADPEYFEYECLTVEDIEKLLNERVEKLNTILQITPSLAKVLLLEHQWNNVAVVEKYRQDANALLVTARIKPPSVAVTDTASTSAAAASAQLLRLGSSGYKTTASATPQYRSQMCPVCASSQLGDKFYSLACGHSFCKDCWTIYFETQIFQGISTQIGCMAQMCNVRVPEDLVLTLVTRPVMRDKYQQFAFKDYVKSHPELRFCPGPNCQIIVQSSEISAKRAICKACHTGFCFRCGMDYHAPTDCQVIKKWLTKCADDSETANYISAHTKDCPKCHICIEKNGGCNHMQCFNCKHDFCWMCLGDWKTHGSEYYECSRYKDNPNIANESVHVQAREALKKYLHYYERWENHSKSLKLEQQTIDRLRQRINSKVMNGSGTWIDWQYLFNAAALLAKCRYTLQYTYPYAYYMEAGSRKNLFEYQQAQLEAEIENLSWKIERAETTDLGDLENQMDIAEKRRTTLLKDFFPVDA
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Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
|
O76927
|
RS21_DROME
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Small ribosomal subunit protein eS21 (40S ribosomal protein S21) (Overgrown hematopoietic organs at 23B)
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MENDAGENVDLYVPRKCSASNRIIHAKDHASVQLSIVDVDPETGRQTDGSKTYAICGEIRRMGESDDCIVRLAKKDGIITKNF
|
May be an associated component of the ribosome rather than a core structural subunit. May act as a translation initiation factor. Has a role in regulation of cell proliferation in the hematopoietic organs and the imaginal disks of larva.
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O76932
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PP4C_DROME
|
Serine/threonine-protein phosphatase 4 catalytic subunit (PP4C) (EC 3.1.3.16)
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MSDYSDLDRQIEQLKRCEIIKENEVKALCAKAREILVEEGNVQRVDSPVTVCGDIHGQFYDLKELFKVGGDVPEKNYLFMGDFVDRGYYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSTAVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQYLDQIRSIDRKQEVPHDGPMCDLLWSDPEDQTGWGVSPRGAGYLFGSDVVSQFNRTNDIDMICRAHQLVMEGFKWHFNETVLTVWSAPNYCYRCGNVAAILELNEYLHRDFVIFEAAPQESRGIPSKKPQADYFL
|
Protein phosphatase that regulates many processes such as microtubule organization at centrosomes. The probable PP4 complex Pp4-19C-PPP4R2r-flfl (PPP4C-PPP4R2-PPP4R3) is required to prevent caspase-induced cell death (in vitro).
|
O77051
|
E2F2_DROME
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Transcription factor E2F2 (dE2F2) (E2F transcription factor 2) (E2F-like transcription factor E2F2)
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MYKRKTASIVKRDSSAAGTTSSAMMMKVDSAETSVRSQSYESTPVSMDTSPDPPTPIKSPSNSQSQSQPGQQRSVGSLVLLTQKFVDLVKANEGSIDLKAATKILDVQKRRIYDITNVLEGIGLIDKGRHCSLVRWRGGGFNNAKDQENYDLARSRTNHLKMLEDDLDRQLEYAQRNLRYVMQDPSNRSYAYVTRDDLLDIFGDDSVFTIPNYDEEVDIKRNHYELAVSLDNGSAIDIRLVTNQGKSTTNPHDVDGFFDYHRLDTPSPSTSSHSSEDGNAPACAGNVITDEHGYSCNPGMKDEMKLLENELTAKIIFQNYLSGHSLRRFYPDDPNLENPPLLQLNPPQEDFNFALKSDEGICELFDVQCS
|
Transcriptional repressor that binds to E2f sites and represses E2f-regulated target genes. Binding to E2f sites requires transcription factor Dp. Acts synergistically with Rbf2 to antagonize E2f1-mediated transcriptional activation. Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. The DREAM complex is required for recruiting E2f2 at differentiation-specific promoters and for stabilizing E2f2-Rbf complexes during S phase. During development, the complex represses transcription of developmentally controlled E2f target genes. During oogenesis, plays a role in restricting DNA synthesis to sites of chorion gene amplification in late stage ovarian follicle cells. Plays an inhibitory role in ionizing radiation (IR)-induced p53-independent apoptosis. May be involved in cell cycle exit by temporarily limiting CycE-dependent activation of E2f-regulated transcription.
|
O77059
|
CRY1_DROME
|
Cryptochrome-1 (DmCRY1) (dcry) (Blue light photoreceptor)
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MATRGANVIWFRHGLRLHDNPALLAALADKDQGIALIPVFIFDGESAGTKNVGYNRMRFLLDSLQDIDDQLQAATDGRGRLLVFEGEPAYIFRRLHEQVRLHRICIEQDCEPIWNERDESIRSLCRELNIDFVEKVSHTLWDPQLVIETNGGIPPLTYQMFLHTVQIIGLPPRPTADARLEDATFVELDPEFCRSLKLFEQLPTPEHFNVYGDNMGFLAKINWRGGETQALLLLDERLKVEQHAFERGFYLPNQALPNIHDSPKSMSAHLRFGCLSVRRFYWSVHDLFKNVQLRACVRGVQMTGGAHITGQLIWREYFYTMSVNNPNYDRMEGNDICLSIPWAKPNENLLQSWRLGQTGFPLIDGAMRQLLAEGWLHHTLRNTVATFLTRGGLWQSWEHGLQHFLKYLLDADWSVCAGNWMWVSSSAFERLLDSSLVTCPVALAKRLDPDGTYIKQYVPELMNVPKEFVHEPWRMSAEQQEQYECLIGVHYPERIIDLSMAVKRNMLAMKSLRNSLITPPPHCRPSNEEEVRQFFWLADVVV
|
Blue light-dependent regulator that is the input of the circadian feedback loop. Has no photolyase activity for cyclobutane pyrimidine dimers or 6-4 photoproducts. Regulation of expression by light suggests a role in photoreception for locomotor activity rhythms. Functions, together with per, as a transcriptional repressor required for the oscillation of peripheral circadian clocks and for the correct specification of clock cells. Genes directly activated by the transcription factors Clock (Clk) and cycle (cyc) are repressed by cry. Necessary for light-dependent magnetosensitivity, an intact circadian system is not required for the magnetoreception mechanism to operate. Required for both the naive and trained responses to magnetic field, consistent with the notion that cry is in the input pathway of magnetic sensing.
|
O77081
|
TPSTA_CAEEL
|
Protein-tyrosine sulfotransferase A (EC 2.8.2.20) (Tyrosylprotein sulfotransferase A) (TPST-A)
|
MRKNRELLLVLFLVVFILFYFITARTADDPYYSNHREKFNGAAADDGDESLPFHQLTSVRSDDGYNRTSPFIFIGGVPRSGTTLMRAMLDAHPEVRCGEETRVIPRILNLRSQWKKSEKEWNRLQQAGVTGEVINNAISSFIMEIMVGHGDRAPRLCNKDPFTMKSAVYLKELFPNAKYLLMIRDGRATVNSIISRKVTITGFDLNDFRQCMTKWNAAIQIMVDQCESVGEKNCLKVYYEQLVLHPEAQMRRITEFLDIPWDDKVLHHEQLIGKDISLSNVERSSDQVVKPVNLDALIKWVGTIPEDVVADMDSVAPMLRRLGYDPNANPPNYGKPDELVAKKTEDVHKNGAEWYKKAVQVVNDPGRVDKPIVDNEVSKL
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Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.
|
O77086
|
C3G_DROME
|
Guanine nucleotide-releasing factor 2 (CRK SH3-binding GNRP) (DC3G)
|
MPQFDESFLSDCALADRWHFYSYTVKQLPPHPSPKPNRNRNPYPSGASHDDHQHQLHHHHHQQHHHNHHRLWKTQRQSWSPRDTNNNHSLTSNNCNCNSSNTCNSISATGNTLHSIKFHRRRKYKKLARLALSTPAIPLQMDVDVDVNVTVDREFDMEMDTPVPLKNAVCHGSISSPSTPGTCSSGIGVGGGGCSSSSNNSINSGSYSTACTPPPPTHQHHSQHQQLQGTPGGSSRVGGAGAGGGGGVPPAPPSAGSSGHKNSLKGTKLARRARSFKDDLIEKISLMRTTNNTLGRSHSPHSPRTKHGTKAPPTTEEVLRSTQTLETHVKDISNALKHFRDVILKKKLEVLPGNGTVILETIASMYSVIQTYTLNENSAIMSSATLQVYQSLGKLIKLCDEVMLSEDSGECASLSNENVREVIDLLEDAVRNLVTLAQGKLKEQDQCAFRYSGSGLGGIGAAAEIMGAVTASPGASVPGTGVMRVSAAESAAQRTSLPDIALTPKERDILEQHNVNPMRGSHSTESILRDTSPPPKPPLPNRASNPPPLPPKRRSQPSASAGTVGVGCSSSTSTSNQASPLPYAQSHNISLNSDLDCSSNISLLNYGVDRLSVRSRSPDENSQCSFDSALNHSREEEDQQQQHQHLRSFPKLAAMMDEDMDKMVSYSAAIDDKTQTPLSTGGGIAGVAGGTGGAGEGVAAAASGDGETNSNRHSNESGFVSMREFRTSTQTTDYSVQSSTKSSSSNSEIAFSISESTAVGSSSEYQQISQLVSHSQRHISSSSSSCTTTTTSSSTTTGYGSSEVEQLQQQQQQQTTTTPADLAPALPPKSIQRSSLTRHDSPGVGDELDEVQSSSGWASHRSSQSEVAELRQLSPLHHLNHHPHTASAGQLQQWHSKHHSLIEGPRLQLAGSGSCSAFDQRHLDQEPPPLPIKKKHILAYMEICSASTRSIEQHRHTMHACNISRNISHSQTMNIMPMSKELSPELEMPPALPPKNYKQRKATSMVASPTLQPVIVTTPPPSPKPTLGENGSTGRPDSRMATVCEELNDAVASEDAMPEPRSPVLDSNENVSAVDDGQTFYCHSHQLPAAEMEMSEDASSADNQPITTPQVLEEQEEPTAESRPLVAVHESVKPANVDEDEEAERADMLINMLEEVNITRYLILKKREEDGPEVKGGYIDALIVHASRVQKVADNAFCEAFITTFRTFIQPIDVIEKLTHRYTYFFCQVQDNKQKAAKETFALLVRVVNDLTSTDLTSQLLSLLVEFVYQLVCSGQLYLAKLLRNKFVEKVTLYKEPKVYGFVGELGGAGSVGGAGIAGSGGCSGTAGGGNQPSLLDLKSLEIAEQMTLLDAELFTKIEIPEVLLFAKDQCEEKSPNLNKFTEHFNKMSYWARSKILRLQDAKEREKHVNKFIKIMKHLRKMNNYNSYLALLSALDSGPIRRLEWQKGITEEVRSFCALIDSSSSFRAYRQALAETNPPCIPYIGLILQDLTFVHVGNQDYLSKGVINFSKRWQQYNIIDNMKRFKKCAYPFRRNERIIRFFDNFKDFMGEEEMWQISEKIKPRGRRPVNY
|
Guanine nucleotide-releasing protein that binds to SH3 domain of Crk. Transduces signals from Crk to activate RAS. Also involved in MAPK activation.
|
O77150
|
BM02_DROME
|
Bomanin Short 2 (Bomanin-2) (Immune-induced peptide 2) (DIM-2)
|
MKFFSVVTVFVFGLLALANAVPLSPDPGNVVINGDCKYCNVHGGK
|
Secreted immune-induced peptide induced by Toll signaling. Has a role in resistance to bacterial and fungal infections.
|
O77203
|
PIAA_DICDI
|
Protein pianissimo A (Developmental gene 1117 protein) (Protein pianissimo) (Target of rapamycin complex 2 subunit piaA) (TORC2 subunit piaA)
|
MTSSDSSVNTTSSSFGNISISSPNHSSSTPPLNNGNGNNVSASETELKKHVLYSLQCLDEKTLTLKVKLDHLNKLVELKKSIPDLNKLGISPTQLYKSVRPFIALPPKTIRTAGLRVMRYYLSNSNNVKELLDLKVQYFITRSLERDKHSEPERIQALKIIRTIMEIDCSLMPHCFVKGLVSIAENQEDNFCRVCLECLTEISIRNPQISSHCGGIRTVFDAVLDPFYQGIQESLLICILYLLSDKDTRIYIRPKSDLEIILAPLTNSFNIGVKLKGASKEKEKEKEKEDEVAMKKWTASSKAVLTLIKSWIGIISLNSDDQGLKSVVDTLRMPQIELQEKALDSIFEIFRVQLPKSIQETFGPQKATQTFNFGSETLQDLPSRTRSLRHNLLNNYLSVLLIAFIDNGLIEGLVYLGNYVANRDGMSEQEKECSKNISLKSTVLLAELLHMSNALLPPSQCAKLQTLPSLVNSAISFRLDPRLRSSSNTMVTNLHSYSHNKSSTTLMDSTLAIGLTGANKWRRIKGQDRRLDKVDDVKMKMEWHMDDNQFQQKIKDTQVLVTKDYQKWSWELMFELLEGPLNNPQHLSNTLKTKFIKRILSFLRPNKKLFSTMAWTTENLKYVRTACVALEVLISHEIGFDFLKDNKTIIQIADMLKVELDYNIKPPPSSSSSSENKKDNVRLLNPEKVLKTMSREYFTMLGTLSSNLLGLEILARNNIFDYIKPLAELPGRDDLSHLIMTSLDYNVNGASRTILQKILTSSSRVVRYLATKYLRFLLRSGVQDFSNWGVELLVQQLNDVDAKVSALSLNVLDEACDDPSCLEVLIDLKPNLLKLGKPGKSLLLRFLSSPKGLENLLQNNGFVEQEEQLWITSENATYVNAIESAVSESLSPSVWRFKEAPDGSSTSGVYLPPHFFGELAKTEKGCQLIRKSNNYQRFLKIIQDPTAKQLDKRASLIAIGHIGSSVDGYSFVKESDTIKLLIGIAEKSQCLALRSTCFYALGMISCIEEAQPIFNSFGWESPSDLNSRILLPKDLKNSTFLSVPQYQYQGSWADHSFETLPSNHFSDPIKNEIISFVGNLSSHITAEGASKNLKRLKIKYPDHFATSEILNAVFILLNTFKYRLGARRFIYDLFDVAIFSSDPYHDLN
|
Regulates cell growth, chemotaxis, signal relay and the actin cytoskeleton. Required for chemoattractant receptor and G protein-mediated activation of the 12 transmembrane domain adenylyl cyclase. Functions as a part of protein complex TORC2. TORC2, is presumed to be indirectly negatively modulated by rapamycin and regulates actin polarization. TORC2, but not TORC1, negatively regulates phagocytosis. This protein and dagA protein CRAC, a cytosolic regulator, are both essential for activation of the enzyme adenylyl cyclase. This protein and CRAC do not function redundantly. Both proteins are integral components of the adenylyl cyclase activation pathway.
|
O77229
|
CATA_DICDI
|
Catalase-A (EC 1.11.1.6)
|
MSAPVLTTSSGSPIDNNLNSMTAGVNGPILIQDFTLIDKLAHFDRERIPERVVHAKGAGAHGYFEVPSSDVPKWCKAKFLNKVGKRTPIFTRFSTVGGEKGSSDSERDPRGFAVKFYTEEGNFDMVGNNTPVFFIRDPSKFPDFIHTQKRNPQTNCKDPNMFWDFLGQTPESTHQVSILFSDRGTPKSYRHMHGFSSHTLKFVNAQGKPYWVKLHFTSETGIQNYTAEEAAKMSMNDPDSATRDLFETIAKGGEPAWKVSIQLMEFEDALKYRFNPFDVTKIWSHKDYPLIQIGRMVLNRNPENYFAEVEQAAFSPSHMVPGIEPSPDKMLQGRLFSYPDTHRHRLGVNYQQIPVNCPFAVKGGVKNYQRDGFMAVNGNGGKGPNYQPNSFGGPEPHPEFAQHKFDVSGFAARQPYNHPNDDFVQPGDLYRLMSEDAKSRFVSNLVGHMSGVTIKEIQVRAVSNFYKADKDLGARLCKGLGIDVNDVIKFAARSNL
|
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
|
O77237
|
PELI_DROME
|
Protein pellino
|
MVKRTDGTESPILAEDGGDGHDKPRLRYGELVILGYNGYLPQGDRGRRRSKFVLHKRTEASGVKRSKHYIVQSPQTSKAILDANQHSISYTLSRNQAVIVEYKEDTETDMFQVGRSSESPIDFVVMDTLPGDKKDAKVMQSTISRFACRILVNRCEPAKARIFAAGFDSSRNIFLGEKATKWQDNVEIDGLTTNGVLIMHPKGSFCGGNAKCGLWRECSVGGDVFSLRESRSAQQKGQPIYDECNILQDGTLIDLCGATLLWRSAEGLQHSPTKHDLEKLIDAINAGRPQCPVGLNTLVIPRKVNIGDQVNQPYVYLNCGHVQGHHDWGQDENTGARRCPMCLELGPVVTLCMGLEPAFYVDVGAPTYAFNPCGHMATEKTVKYWANVEIPHGTNGFQAVCPFCATPLDGATGYIKLIFQDNLD
|
Scaffold protein involved in the Toll signaling pathway via its interaction with pelle/pll kinase.
|
O77277
|
TORS_DROME
|
Torsin-like protein
|
MMSFPRMLSLCLSVLVILPLPLQSVDPLTIGAVGAVALGAYFKEHTYCRFAECCDDRNIPARIDELERSLERTLIGQHIVRQHIVPALKAHIASGNKSRKPLVISFHGQPGTGKNFVAEQIADAMYLKGSRSNYVTKYLGQADFPKESEVSNYRVKINNAVRDTLRSCPRSLFIFDEVDKMPSGVFDQLTSLVDYNAFVDGTDNTKAIFIFLSNTAGSHIASHLGSVMKNGRLREDTRLSDFEPLLRKAAYNMDGGMKKTTMIESHVIDHFIPFLPMEKAHVIKCLEAELLRWRRDPKQANNQKIIEDIINSSISYDRTHSLFAISGCKTLEKKVAMAIY
|
May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins.
|
O77334
|
YVH1_PLAF7
|
Dual specificity protein phosphatase YVH1 (PfYVH1) (EC 3.1.3.16) (EC 3.1.3.48)
|
MIVKVFDYIYISNVYNANDIYELIKLNIGGVLTCFDCTCIEWCHHNDTNVTNKIFYKDIFVNTKKDLIKCDVPIITNKSVNSDIIGGTHQINNYYNEQNNNYHDNTYKEFTQTHKTNIDPSQIKSDHINEERKEHYDYIIFPSDIINNTQCNNNNLKDYIKSMLILKEDAYIDFDVIHMDQLKNKHNNNNNNNNNNNNNNNNNNNNNNCCTFKNPDISNTSQHHVEHIQIHKSNSHSNIPSDNINFCNKKYDKNLSRSVEISEKDKHPENSLLYEFVNKDKLNYKINQEEDTVSSEKNKLCDNNNNNNMVHTRHIYNVCELNKCLRENKLIPYNNIYKMKHLYLNILDTFDENILKHVNKAHLFIDSVIQKKKNILIHCMAGISRCSSIILSYVSKKNKKGIEYNFNLLKSKYPFAHPNENFYRQLLLYEKMNYTLDGCTDYHNIYKKIKMNRENLEELKILNLKNDKQPIYNFRCKHCNYVLFNDNEIIKHDFKISKIKKNYGNSCTSIFIEKKEWILTENKMKGVLNCPNVNCNIKLGKWSWTGICCSCGYLQIPAFMINSSNVDRMNISKTV
|
Dual specificity protein phosphatase which dephosphorylates both phosphotyrosine and phosphoserine residues.
|
O77410
|
EIF3E_DROME
|
Eukaryotic translation initiation factor 3 subunit E (eIF3e) (Eukaryotic translation initiation factor 3 subunit 6)
|
MANFDLTRINCQFLDRHLTFPLLEFLCGKEIYNQQELLEYILETVNKTNMIDYTMDTRKRLNLSQEMPEELVQRKAEVLATLKQLQNEVAPIMKATDILKNGESMKDSKTFVNALQKDYNFKVEHLESAYKLAKYLYECGNYQESTSYLYFCLIVMSPNDKNYLNVLWGKLAAEILTLNWNTALEDLTRLRDYIDNANFSTIQALQQRTWLIHWSVLVFFNHPKGRDLIIEMFLYKPLYLNAIQTMCPHIMRYLATAVVINRTRRNALKDLIKVIQQESYTYRDPITEFLECLYVNFDFEGARLKLHECQTVILNDFFIVACLNEFVEDARLMIFETFCRIHQCITISMLADKLNMKPNEAECWIVNLIRNARLNAKIDSKLGHVVMGTQPLSPYQQLVEKIDSLSMRSEHLAGLIERKSKQKQNQESADSWKYY
|
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In addition to its role in the eIF-3 complex, also functions in protein ubiquitination and degradation. During mitosis required for regulating mitotic microtubule growth and kinetochore formation, and consequently is required for satisfying the spindle assembly checkpoint (SAC) during metaphase to prevent delays in mitotic progression. This is likely by promoting the ubiquitination and degradation of Klp67A, a kinesin-like protein that suppresses microtubule polymerization at plus ends. Acts in the COP9 signalosome (CSN) mediated regulation of cullin neddylation by promoting Cul1 and Cul3 neddylation and negatively regulating the CSN complex subunit CSN5. {ECO:0000255|HAMAP-Rule:MF_03004, ECO:0000269|PubMed:18493598, ECO:0000269|PubMed:28505193}.
|
O77448
|
TERT_TETTS
|
Telomerase reverse transcriptase (EC 2.7.7.49) (Telomerase catalytic subunit) (Telomerase subunit P133)
|
MQKINNINNNKQMLTRKEDLLTVLKQISALKYVSNLYEFLLATEKIVQTSELDTQFQEFLTTTIIASEQNLVENYKQKYNQPNFSQLTIKQVIDDSIILLGNKQNYVQQIGTTTIGFYVEYENINLSRQTLYSSNFRNLLNIFGEEDFKYFLIDFLVFTKVEQNGYLQVAGVCLNQYFSVQVKQKKWYKNNFNMNGKATSNNNQNNANLSNEKKQENQYIYPEIQRSQIFYCNHMGREPGVFKSSFFNYSEIKKGFQFKVIQEKLQGRQFINSDKIKPDHPQTIIKKTLLKEYQSKNFSCQEERDLFLEFTEKIVQNFHNINFNYLLKKFCKLPENYQSLKSQVKQIVQSENKANQQSCENLFNSLYDTEISYKQITNFLRQIIQNCVPNQLLGKKNFKVFLEKLYEFVQMKRFENQKVLDYICFMDVFDVEWFVDLKNQKFTQKRKYISDKRKILGDLIVFIINKIVIPVLRYNFYITEKHKEGSQIFYYRKPIWKLVSKLTIVKLEEENLEKVEEKLIPEDSFQKYPQGKLRIIPKKGSFRPIMTFLRKDKQKNIKLNLNQILMDSQLVFRNLKDMLGQKIGYSVFDNKQISEKFAQFIEKWKNKGRPQLYYVTLDIKKCYDSIDQMKLLNFFNQSDLIQDTYFINKYLLFQRNKRPLLQIQQTNNLNSAMEIEEEKINKKPFKMDNINFPYYFNLKERQIAYSLYDDDDQILQKGFKEIQSDDRPFIVINQDKPRCITKDIIHNHLKHISQYNVISFNKVKFRQKRGIPQGLNISGVLCSFYFGKLEEEYTQFLKNAEQVNGSINLLMRLTDDYLFISDSQQNALNLIVQLQNCANNNGFMFNDQKITTNFQFPQEDYNLEHFKISVQNECQWIGKSIDMNTLEIKSIQKQTQQEINQTINVAISIKNLKSQLKNKLRSLFLNQLIDYFNPNINSFEGLCRQLYHHSKATVMKFYPFMTKLFQIDLKKSKQYSVQYGKENTNENFLKDILYYTVEDVCKILCYLQFEDEINSNIKEIFKNLYSWIMWDIIVSYLKKKKQFKGYLNKLLQKIRKSRFFYLKEGCKSLQLILSQQKYQLNKKELEAIEFIDLNNLIQDIKTLIPKISAKSNQQNTN
|
Catalytic component of telomerase, an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER. TERT is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
|
O77459
|
KEN_DROME
|
Transcription factor Ken (Protein Ken and Barbie)
|
MKEFQRMLMLQYSKHGECILKEIGAAFRGEHPADLTIVCENKVKLHAHKLVLAAASPLIRNLLEDTHLSDCSTTVYFPDVNATYFKFLLDFLYSGQTCITSRDVNYLHDLLLLLQIKSDSWKTTDSAYLSSKCGGLRDRADRRKQQYTSPQNLEPDQTLKYEVDSVDESRNAADFSSAFNSNDNCESAAECERSGGHNNKEEDEDDCTHKDNKSDKDTDEIVNLSNAPPSGTSGSNSNISTSSNHQQQQHHHHHHHNHNNNNNNNNNNSSSSTINPVNLSLDLRTKSENSASRTLGSGSDHSGIDLAVTASESTKRKGLFFDSHKDVMKPLSDGSDINSSPENYVVTPHRKRRPGFHNTQSDNQPFTSYPHSLLEELRLAKSTTSPISGFGSEKNMLAHLEDGALNGDTLTPDRKHLLEAQRNRAQSPEIPMHLGPQFVYQWQSNQNAAMSAMPNLQSRLSSLSHISLNLDHPEGRSGSASGSGANLAGSNTHASSVREYRCEYCGKQFGMSWNLKTHLRVHTGEKPFACRLCVAMFKQKAHLLKHLCSVHRNVITTTNGADTENRYSCCFCSMCFESVQELVRHLSGHHNNLLLTKNLRE
|
Transcription factor required for terminalia development. Negative regulator of the JAK/STAT pathway: represses JAK/STAT-dependent expression of ventral veins lacking (vvl) in the posterior spiracles.
|
O77460
|
IPYR_DROME
|
Inorganic pyrophosphatase (EC 3.6.1.1) (Nucleosome-remodeling factor 38 kDa subunit) (Pyrophosphate phospho-hydrolase) (PPase)
|
MLAKITRSSFYASRAVGRLSGSIPTSPAALASNCRYIQIERKRTKSHEMALYETVEKGAKNSPSYSLYFKNKCGNVISPMHDIPLYANEEKTIYNMVVEVPRWTNAKMEISLKTPMNPIKQDIKKGKLRFVANCFPHKGYIWNYGALPQTWENPDHIEPSTGCKGDNDPIDVIEIGYRVAKRGDVLKVKVLGTIALIDEGETDWKIIAIDVNDPLASKVNDIADVDQYFPGLLRATVEWFKIYKIPDGKPENQFAFNGDAKNADFANTIIAETHKFWQNLVHQSPASGSISTTNITNRNSEHVIPKEEAEKILAEAPDGGQVEEVSDTVDTWHFIHLK
|
Component of NURF (nucleosome remodeling factor), a complex which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin. NURF is required for homeotic gene expression, proper larval blood cell development, normal male X chromosome morphology, ecdysteroid signaling and metamorphosis. Inorganic pyrophosphatase (PPase), hydrolyzes inorganic pyrophosphate to inorganic phosphate, essential for driving critical biosynthetic reactions including transcription, replication, and DNA repair.
|
O77469
|
FBLN1_CAEEL
|
Fibulin-1
|
MRICFLLLAFLVAETFANELTRCCAGGTRHFKNSNTCSSIKSEGTSMTCQRAASICCLRSLLDNACDSGTDIAKEEESCPSNINILGGGLKKECCDCCLLAKDLLNRNEPCVAPVGFSAGCLRSFNKCCNGDIEITHASEIITGRPLNDPHVLHLGDRCASSHCEHLCHDRGGEKVECSCRSGFDLAPDGMACVDRNECLTRQSPCTQSEDCVNTIGGYICQRRISRLVPHRHRANRIGNAPRRMRDDPYSRAGEYREASQANTEFGCPMGWLFQHGHCVDVDECNLGSHDCGPLYQCRNTQGSYRCDAKKCGDGELQNPMTGECTSITCPNGYYPKNGMCNDIDECVTGHNCGAGEECVNTPGSFRCQQKGNLCAHGYEVNGATGFCEDVNECQQGVCGSMECINLPGTYKCKCGPGYEFNDAKKRCEDVDECIKFAGHVCDLSAECINTIGSFECKCKPGFQLASDGRRCEDVNECTTGIAACEQKCVNIPGSYQCICDRGFALGPDGTKCEDIDECSIWAGSGNDLCMGGCINTKGSYLCQCPPGYKIQPDGRTCVDVDECAMGECAGSDKVCVNTLGSFKCHSIDCPTNYIHDSLNKNQIADGYSCIKVCSTEDTECLGNHTREVLYQFRAVPSLKTIISPIEVSRIVTHMGVPFSVDYNLDYVGQRHFRIVQERNIGIVQLVKPISGPTVETIKVNIHTKSRTGVILAFNEAIIEISVSKYPF
|
Incorporated into fibronectin-containing matrix fibers. Plays a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Important for certain developmental processes and contributes to the supramolecular organization of ECM architecture, in particular to those of basement membranes. [Isoform a]: Involved in regulating the shape and adhesion of cells in the developing pharynx, intestine, body-wall muscle and gonadal tissue. During gonadogenesis, regulates the width of gonads and the migration of distal tip cells (DTC). Together with type IV collagen let-2 and downstream of metalloprotease mig-17, recruits nidogen nid-1 to the gonad basement membrane thereby inducing basement membrane remodeling required for the directional migration of DTCs. Acts antagonistically with metalloprotease gon-1 to maintain optimal levels of type IV collagen emb-9 in the gonad basement membrane during gonadogenesis. Required for larval development.
|
O77485
|
FUT2_PANTR
|
Galactoside alpha-(1,2)-fucosyltransferase 2 (Alpha(1,2)FT 2) (Fucosyltransferase 2) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 2) (Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT2) (EC 2.4.1.69) (Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT2) (EC 2.4.1.344)
|
MLVVQMPFSFPVAHFILFVFTVSTIFHVQQRLAKIQAMWELPVQIPVLASTSKALGPSQLRGMWTINAIGRLGNQMGEYATLYALAKMNGRPAFIPAQMHSTLAPIFRITLPVLHSATASRIPWQNYHLNDWMEEEYRHIPGEYVRFTGYPCSWTFYHHLRQEILQEFTLHDHVREEAQKFLRGLQVNGSRPGTFVGVHVRRGDYVHVMPKVWKGVVADRRYLQQALDWFRARYSSPIFVVTSNGMAWCRENIDTSHGDVVFAGDGIEGSPAKDFALLTQCNHTIMTIGTFGIWAAYLTGGDTIYLANYTLPDSPFLKIFKPEAAFLPEWMGIAADLSPLLKH
|
Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose on both O- and N-linked glycans chains of cell surface glycoproteins and glycolipids and the resulting epitope regulates several processes such as cell-cell interaction including host-microbe interaction, cell surface expression and cell proliferation. Preferentially fucosylates gangliosides GA1 and GM1 in the antrum, cecum and colon and in the female reproductive organs. Fucosylated host glycoproteins or glycolipids mediate interaction with intestinal microbiota influencing its composition. Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble ABO blood group antigen synthesis pathway.
|
O77486
|
FUT2_GORGO
|
Galactoside alpha-(1,2)-fucosyltransferase 2 (Alpha(1,2)FT 2) (Fucosyltransferase 2) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 2) (Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT2) (EC 2.4.1.69) (Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT2) (EC 2.4.1.344)
|
MLVVQMPFSFPMAHFILFVFTVSTIFHVQQRLAKIQAMWELPVQIPVLASTSKALGPSQLRGMWTINAIGRLGNQMGEYATLYALAKMNGRPAFIPAQMHSTLAPIFRITLPVLHSATASRIPWQNYHLNDWMEEEYRHIPGEYVRFTGYPCSWTFYHHLRQEILQEFTLHDHVREEAQKFLRGLQVNGSQPGTFVGVHVRRGDYVHVMPKVWKGVVADRRYLQQALDWFRARYSSPIFVVTSNGMAWCRENIDTSHGDVVFAGDGIEGSPAKDFALLTQCNHTIMTIGTFGIWAAYLTGGDTIYLANYTLPDSPFLKIFKPEAAFLPEWTGIAADLSPLLKH
|
Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose on both O- and N-linked glycans chains of cell surface glycoproteins and glycolipids and the resulting epitope regulates several processes such as cell-cell interaction including host-microbe interaction, cell surface expression and cell proliferation. Preferentially fucosylates gangliosides GA1 and GM1 in the antrum, cecum and colon and in the female reproductive organs. Fucosylated host glycoproteins or glycolipids mediate interaction with intestinal microbiota influencing its composition. Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble ABO blood group antigen synthesis pathway.
|
O77487
|
FUT2_PONPY
|
Galactoside alpha-(1,2)-fucosyltransferase 2 (Alpha(1,2)FT 2) (Fucosyltransferase 2) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 2) (Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT2) (EC 2.4.1.69) (Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT2) (EC 2.4.1.344)
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MLVVQMPFSFPVAHFILFVFTVSTIFHIQQRLAKIQAMWELPEQIPVLASTSKALGPSQLRGIWTINAIGRLGNQMGEYATLYALAKMNGRPAFIPAQMHSTLAPIFRITLPVLHSTTASRIPWQNYHLNDWMEEKYRHIPGEYVRLTGYPCSWTFYHHLRHEILQEFTLHDHVREEAQKFLRGLQVNGSQPSTFVGVHVRRGDYVHVMPKVWKGVVADRRYLQQALDWFRARYSSPIFVVTSNGMAWCQENIDTSHSDVVFAGDGIEGSPAKDFALLTQCNHTIMTIGTFGIWAAYLAGGDTIYLANYTLPDSPFLKIFKPEAAFLPEWTGIAADLSPLLKH
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Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose on both O- and N-linked glycans chains of cell surface glycoproteins and glycolipids and the resulting epitope regulates several processes such as cell-cell interaction including host-microbe interaction, cell surface expression and cell proliferation. Preferentially fucosylates gangliosides GA1 and GM1 in the antrum, cecum and colon and in the female reproductive organs. Fucosylated host glycoproteins or glycolipids mediate interaction with intestinal microbiota influencing its composition. Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble ABO blood group antigen synthesis pathway.
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O77503
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AGO2_RABIT
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Protein argonaute-2 (Argonaute2) (EC 3.1.26.n2) (Argonaute RISC catalytic component 2) (Eukaryotic translation initiation factor 2C 2) (eIF-2C 2) (eIF2C 2) (Protein slicer)
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GYAFKPPPRPDFGTSGRTIKLQANFFEMDIPKIDIYHYELDIKPEKCPRRVNREIVEHMVQHFKAQIFGDRKPVFDGRKNLYTAMPLPIGREKVELEVTLPGEGKDRIFKVSIKWVSCVSLQALHDALSGRLPSVPFETIQALDVVMRHLPSMRYTPVGRSFFTASEGCSNPLGGGREVWFGFHQSVRPSLWKMMLNIDVSATAFYKAQPVIEFVCEVLDFKSIEEQQKPLTDSQRVKFTKEIKGLKVEITHCGQMKRKYRVCNVTRRPASHQTFPLQQESGQTVECTVAQYFKDRHKLVLRYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIRATARSAPDRQEEISKLMRSASFNTDPYVREFGIMVKDEMTDVTGRVLQPPSILYGGRNKAIATPVQGVWDMRNKQFHTGIEIKVWAIACFAPQRQCTEVHLKSFTEQLRKISRDAGMPIQGQPCFCKYAQGADSVGPMFRHLKNTYAGLQLVVVILPGKTPVYAEVKRVGDTVLGMATQCVQMKNVQRTTPQTLSNLCLKINVKLGGVNNILLPQGRPPVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDAHPNRYCATVRVQQHRQEIIQDLAAMVRELLIQFYKSTRFKPTRIIFYRDGVSEGQFQQVLHHELLAIREACIKLEKDYQPGITFIVVQKRHHTRLFCTDKNERVGKSGNIPAGTTVDTKITHPTEFDFYLCSHAGIQGTSRPSHYHVLWDDNRFSSDELQILTYQLCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLVDKEHDSAEGSHTSGQSNGRDHQALAKAVQVHQDTLRTMYFA
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Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. May inhibit translation initiation by binding to the 7-methylguanosine cap, thereby preventing the recruitment of the translation initiation factor eIF4-E. May also inhibit translation initiation via interaction with EIF6, which itself binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur. In some cases RISC-mediated translational repression is also observed for miRNAs that perfectly match the 3' untranslated region (3'-UTR). Can also up-regulate the translation of specific mRNAs under certain growth conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF-alpha) mRNA and up-regulates translation under conditions of serum starvation. Also required for transcriptional gene silencing (TGS), in which short RNAs known as antigene RNAs or agRNAs direct the transcriptional repression of complementary promoter regions. {ECO:0000255|HAMAP-Rule:MF_03031}.
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O77504
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S22A1_RABIT
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Solute carrier family 22 member 1 (Organic cation transporter 1) (rbOCT1)
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MPTVDDVLEQVGEFGWFQKRTFLFLCLISAILAPIYLGIVFLGFTPDHRCRSPGVDELSQRCGWSPEEELNYTVPGLGATDGAFVRQCMRYEVDWNQSSLGCVDPLASLAPNRSHLPLGPCQHGWVYDTPGSSIVTEFNLVCADAWKVDLFQSCVNLGFFLGSLGVGYIADRFGRKLCLLLTTLINAVSGVLTAVAPDYTSMLLFRLLQGLVSKGSWMSGYTLITEFVGSGYRRTVAILYQVAFSVGLVALSGVAYAIPNWRWLQLTVSLPTFLCLFYYWCVPESPRWLLSQKRNTDAVKIMDNIAQKNGKLPPADLKMLSLDEDVTEKLSPSLADLFRTPNLRKHTFILMFLWFTCSVLYQGLILHMGATGGNVYLDFFYSSLVEFPAAFVILVTIDRVGRIYPMAASNLAAGVASVILIFVPQDLHWLTIVLSCVGRMGATIVLQMICLVNAELYPTFVRNLGVMVCSALCDVGGIITPFMVFRLMEVWQPLPLIVFGVLGLLAGGMTLLLPETKGVALPETIEDAENLRRKAKPKESKIYLQVQTSELKGP
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Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics. Functions as a pH- and Na(+)-independent, bidirectional transporter (By similarity). Cation cellular uptake or release is driven by the electrochemical potential (i.e. membrane potential and concentration gradient) and substrate selectivity (By similarity). Hydrophobicity is a major requirement for recognition in polyvalent substrates and inhibitors (By similarity). Primarily expressed in the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds from the blood by hepatic and renal clearance (By similarity). Most likely functions as an uptake carrier in enterocytes contributing to the intestinal elimination of organic cations from the systemic circulation. Transports endogenous monoamines such as N-1-methylnicotinamide (NMN), guanidine, neurotransmitters dopamine, serotonin, noradrenaline, adrenaline and histamine, and quaternary ammonium compound such as choline. Also transports natural polyamines such as spermidine, agmatine and putrescine at low affinity, but relatively high turnover. Involved in the hepatic and intestinal uptake of the vitamin B1/thiamine, hence regulating hepatic lipid and energy metabolism. Contributes to the influx and efflux of fatty acid carriers carnitines and acylcarnitines across the basolateral membrane of hepatocytes, from the liver to the systemic circulation and inversely and may be involved in regulating the systemic availability of hepatic acylcarnitines (By similarity). Also capable of transporting non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) (By similarity). May contribute to the transport of cationic compounds in testes across the blood-testis-barrier (By similarity). Also mediates the uptake of xenobiotics tributylmethylammonium (TBuMA), quinidine, N-methyl-quinine (NMQ), N-methyl-quinidine (NMQD) N-(4,4-azo-n-pentyl)-quinuclidine (APQ), azidoprocainamide methoiodide (AMP), N-(4,4-azo-n-pentyl)-21-deoxyajmalinium (APDA) and 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP).
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O77507
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RAD51_RABIT
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DNA repair protein RAD51 homolog 1
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MAMQMQLEANADTSVEEESFGPQPVSRLEQCGINANDVKKLEEAGFHTEEAVAYAPKKELINIKGISEAKADKILTEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARGFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVTVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD
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Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Recruited to resolve stalled replication forks during replication stress. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross-link repair.
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O77510
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TNFA_PAPHU
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Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
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MSTESMIRDVELAEEALPRKTAGPQGSRRCWFLSLFSFLLVAGATTLFCLLHFGVIGPQREEFPKDPSLISPLAQAVRSSSRTPSDKPVVHVVANPQAEGQLQWLNRRANALLANGVELTDNQLVVPSEGLYLIYSQVLFKGQGCPSNHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINLPDYLDFAESGQVYFGIIAL
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Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation (By similarity). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (By similarity). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (By similarity). Promotes osteoclastogenesis and therefore mediates bone resorption (By similarity).
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O77564
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FOLH1_PIG
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Glutamate carboxypeptidase 2 (EC 3.4.17.21) (Folate hydrolase 1) (Folylpoly-gamma-glutamate carboxypeptidase) (FGCP) (Glutamate carboxypeptidase II) (GCPII) (Membrane glutamate carboxypeptidase) (mGCP) (N-acetylated-alpha-linked acidic dipeptidase I) (NAALADase I) (Prostate-specific membrane antigen homolog) (Pteroylpoly-gamma-glutamate carboxypeptidase)
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MWNPLHETDSTSVAWRRPRWLCAGALVLAAGLFVLGFLFGWFIKSPNEAANISPQHNVKKAFLDELKAENIKTFLYNFTRIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTRPNYISIIDEDGNEIFNTSLFEPPPPGYENVSDVVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKILIARYGKIFRGNKVKNAQLAGAKGIILYSDPADYFAPGVQSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRLQIAEAVGLPRIPVHPIGYSDAQKLLEKMGGSAPPDDSWKGSLHVPYNVGPGFTGNFSTQKVKMHIHSDNKVKRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGKLKKEGWRPRRTVLFASWDAEEYGLFGSTEWAEENSRILQERGVAYINADSSIEGNYTLRVDCTPLMYSLVYNLTKELQSPDEGFEGKSLFESWNEKSPSPEFSGLPRISKLGSGNDFEVFFQRLGIASGRARYTKDWVTNKFSSYPLYHSVYETYELVEKFYDPTFKYHLAVAQVRGGIVFELANSVVRPFDCRDYAVVLRNYADKLYNISMNHPQEMKAYSVSFDSLFSAVKNFTEIASNFSERVQDLDKNNPILLRIMNDQLMFLERAFIVPLGLPDRAFYRHVIYAPSSHNKYMGESFPGIYDALFDIENKVDPSKAWGEVKRQISIAAFTVQAAAGTLREVA
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Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides (By similarity). In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.
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O77620
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IL2_RABIT
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Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
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MYKVQLLSCIALTLALLTSSAPTSSSTKETQEQLDQLLLDLQVLLKGVNDYKNSKLSRMLTFKFYMPKKVTELKHLQCLEEELKPLEEVLNLAQGKNSHGGNTRESISNINVTVLKLKGSETFMCEYDETVTIVEFLNRWITFCQSIISASSS
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Cytokine produced by activated CD4-positive helper T-cells and to a lesser extend activated CD8-positive T-cells and natural killer (NK) cells that plays pivotal roles in the immune response and tolerance. Binds to a receptor complex composed of either the high-affinity trimeric IL-2R (IL2RA/CD25, IL2RB/CD122 and IL2RG/CD132) or the low-affinity dimeric IL-2R (IL2RB and IL2RG). Interaction with the receptor leads to oligomerization and conformation changes in the IL-2R subunits resulting in downstream signaling starting with phosphorylation of JAK1 and JAK3. In turn, JAK1 and JAK3 phosphorylate the receptor to form a docking site leading to the phosphorylation of several substrates including STAT5. This process leads to activation of several pathways including STAT, phosphoinositide-3-kinase/PI3K and mitogen-activated protein kinase/MAPK pathways. Functions as a T-cell growth factor and can increase NK-cell cytolytic activity as well. Promotes strong proliferation of activated B-cells and subsequently immunoglobulin production. Plays a pivotal role in regulating the adaptive immune system by controlling the survival and proliferation of regulatory T-cells, which are required for the maintenance of immune tolerance. Moreover, participates in the differentiation and homeostasis of effector T-cell subsets, including Th1, Th2, Th17 as well as memory CD8-positive T-cells.
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O77628
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FOS_BOVIN
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Protein c-Fos (Cellular oncogene fos) (Transcription factor AP-1 subunit c-Fos)
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MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDYCTDLAVSSANFIPTVTAISTSPDLQWLVQPTLVSSVAPSQTRAPHPYGVPTPSAGAYSRAGVMKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLSGGLPEAATPESEEAFTLPLLNDPEPKPSVEPVKSVGSMELKAEPFDDYMFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHGGSLGMGPMATELEPLCTPVVTCTPSCTTYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL
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Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex, at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation (By similarity). In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum (By similarity).
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O77633
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ADA10_PIG
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Disintegrin and metalloproteinase domain-containing protein 10 (ADAM 10) (EC 3.4.24.81) (Kuzbanian protein homolog) (Mammalian disintegrin-metalloprotease) (CD antigen CD156c)
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MVLLRVLILLLSWAAGLGGQYGNPLNKYIRHYEGLSYDVDSLHQKHQRAKRAVSHEDQFLRLNFHAHGRHFNLRMKRDTSLFSDEFRVETSNKVLDYDTSHIYTGHIYGEEGSFSHGSVIDGRFEGFIQTHGGTFYIEPAERYIKDRTLPFHSVIYHEDDINYPHKYGPQGGCADHSVFERMRKYQMTGVEEVTQTPQEKHANNGPELLRKKRTTSAEKNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTADEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEQCDCGYSDQCKDECCYDANQPEGKKCRLKPEKECSPSQGPCCTAQCKFKSKTEKCRDDSDCAKEGICNGITALCPASDPKPNFTDCNRHTQVCINGQCAGSICEKYGLEECTCASSDGKDDKELCHVCCMKKMEPLTCASTGSEKWKKHFLGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKKAIFSPELYENIAEWIVAYWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQTIQPPQRQRPRESYQMGHMRR
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Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B. Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3. Mediates the proteolytic cleavage of IL6R and IL11RA, leading to the release of secreted forms of IL6R and IL11RA (By similarity). Enhances the cleavage of CHL1 by BACE1 (By similarity). Cleaves NRCAM (By similarity). Cleaves TREM2, resulting in shedding of the TREM2 ectodomain (By similarity). Involved in the development and maturation of glomerular and coronary vasculature (By similarity). During development of the cochlear organ of Corti, promotes pillar cell separation by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions (By similarity). May regulate the EFNA5-EPHA3 signaling (By similarity).
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O77636
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ADA17_PIG
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Disintegrin and metalloproteinase domain-containing protein 17 (ADAM 17) (EC 3.4.24.86) (TNF-alpha convertase) (TNF-alpha-converting enzyme) (CD antigen CD156b)
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MLREQFSFDIAEEASKVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPIGKKNIYLNSGLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGLAECAPNE
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Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called Notch extracellular truncation (NEXT). Plays a role in the proteolytic processing of ACE2. Plays a role in hemostasis through shedding of GP1BA, the platelet glycoprotein Ib alpha chain. Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R, leading to the release of secreted form of IL6R (By similarity). Mediates the proteolytic cleavage and shedding of FCGR3A upon NK cell stimulation, a mechanism that allows for increased NK cell motility and detachment from opsonized target cells.
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O77642
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1433S_SHEEP
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14-3-3 protein sigma (Stratifin)
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MERASLIQKAKLAEQAERYEDMAAFMKSAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEESSEEKGPEVQEYREKVETELRGVCDTVLGLLDTHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADNAGEEGGEAPEEPQS
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Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53 (By similarity).
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O77656
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MMP13_BOVIN
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Collagenase 3 (EC 3.4.24.-) (Matrix metalloproteinase-13) (MMP-13)
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MHPRVLAGFLFFSWTACWSLPLPSDGDSEDLSEEDFQFAESYLKSYYYPQNPAGILKKTAASSVIDRLREMQSFFGLEVTGRLDDNTLDIMKKPRCGVPDVGEYNVFPRTLKWSKMNLTYRIVNYTPDLTHSEVEKAFRKAFKVWSDVTPLNFTRIHNGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPYSKHPKTPDKCDPSLSLDAITSLRGETLIFKDRFFWRLHPQQVEAELFLTKSFGPELPNRIDAAYEHPSHDLIFIFRGRKFWALSGYDILEDYPKKISELGFPKHVKKISAALHFEDSGKTLFFSENQVWSYDDTNHVMDKDYPRLIEEVFPGIGDKVDAVYQKNGYIYFFNGPIQFEYSIWSNRIVRVMTTNSLLWC
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Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion (By similarity).
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O77667
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DHI2_BOVIN
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11-beta-hydroxysteroid dehydrogenase type 2 (11-DH2) (11-beta-HSD2) (EC 1.1.1.-) (Corticosteroid 11-beta-dehydrogenase isozyme 2) (NAD-dependent 11-beta-hydroxysteroid dehydrogenase)
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MESWPWPSGGAWLLVPARALLQLLRADLRLGRPLLAALALLAALDWLCQRLLPPLAALAVLAATGWIVLSRLARPQRLPVATRAVLITGCDSGFGNATAKKLDTMGFTVLATVLDLNSPGALELRACCSSRLKLLQMDLTKPGDISRVLEFTKVHTPSTGLWGLVNNAGQNIFVADAELCPVATFRTCMEVNFFGALEMTKGLLPLLRRSSGRIVTVSSPAGDMPFPCLAAYGTSKAALALLMGNFSCELLPWGVKVSIIQPACFKTESVKDVHQWEERKQQLLATLPQELLQAYGEDYIEHLNGQFLHSLSQALPDLSPVVDAITDALLAAQPLRRYYPGHGLGLIYFIHYYLPEGLRQRFLQSFFISPYVPRALQAGQPGLTSARDIAQDQGPRPDPSPTAQ
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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(+). Functions as a dehydrogenase (oxidase), thereby decreasing the concentration of active glucocorticoids, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids. Affinity towards corticosterone is higher than cortisol or dexamethasone. Plays an important role in maintaining glucocorticoids balance during preimplantation and protects the fetus from excessive maternal corticosterone exposure (By similarity). Catalyzes the oxidation of 11beta-hydroxytestosterone (11beta,17beta-dihydroxyandrost-4-ene-3-one) to 11-ketotestosterone (17beta-hydroxyandrost-4-ene-3,11-dione), a major bioactive androgen. 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. Converts 7-beta-25-dihydroxycholesterol to 7-oxo-25-hydroxycholesterol in vitro. 7-beta-25-dihydroxycholesterol (not 7-oxo-25-hydroxycholesterol) acts as ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration (By similarity). May protect ovulating oocytes and fertilizing spermatozoa from the adverse effects of cortisol.
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O77668
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OREX_PIG
|
Hypocretin neuropeptide precursor (Hypocretin) (Hcrt) (Orexin precursor) (Prepro-orexin) (Preprohypocretin) [Cleaved into: Orexin-A (Hypocretin-1) (Hcrt1); Orexin-B (Hypocretin-2) (Hcrt2)]
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MNPPFAKVSWATVTLLLLLLLLPPAVLSPGAAAQPLPDCCRQKTCSCRLYELLHGAGNHAAGILTLGKRRPGPPGLQGRLQRLLQASGNHAAGILTMGRRAGAEPAPRLCPGRRCLAAAASSVAPGGRSGI
|
Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested.
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O77676
|
KGP1_RABIT
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cGMP-dependent protein kinase 1 (cGK 1) (cGK1) (EC 2.7.11.12)
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MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFRKFTKFERSKDLIKEAILDNDFMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLAYVMEDGKVEVTKEGVKLCTMGPGKVFGELAILYNCTRTATVKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEYMEFLKSVPTFQSLPEEILSKLADVLEETHYENEEYSIRQGARGDTFFIISKGKVNVTREDSPSEDPIFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAEAKAKYEAEAAFFANLKLSDFNIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDFIVRLYRTFKDSKYLYMLMEACLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGIIYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEIILNKGHDISADYWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPSERLGNLKNGVKDIQKHKWFEGFNWEGLRKGTLTPPIIPSVASPTDTSNFDGFPEDNDEPPPDDNSGWDIDF
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Serine/threonine protein kinase that acts as key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates IRAG1 and inhibits IP3-induced Ca(2+) release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca(2+) levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation decreasing contraction controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle (By similarity). {ECO:0000250, ECO:0000269|PubMed:16885398}.
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O77698
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TRFL_BUBBU
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Lactotransferrin (Lactoferrin) (EC 3.4.21.-)
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MKLFVPALLSLGALGLCLAAPRKNVRWCTISQPEWLKCHRWQWRMKKLGAPSITCVRRAFVLECIRAITEKKADAVTLDGGMVFEAGLDPYKLRPVAAEIYGTKESPQTHYYAVAVVKKGSNFQLDQLQGRNSCHTGLGRSAGWNIPMGILRPYLSWTESLEPFQGAVAKFFSASCVPCVDRQAYPNLCQLCKGEGENQCACSPREPYFGYSGAFKCLQDGAGDVAFVKETTVFENLPEKADRDQYELLCLNNTRAPVDAFKECHLAQVPSHAVVARSVDGKEDLIWKLLSKAQEKFGKNKSGSFQLFGSPPGQRDLLFKDCALGFLRIPSKVDSALYLGSRYLTALKNLRETAEEVQARRARVVWCAVGPEEQKKCQQWSQQSGQIVTCATASTTDDCIALVLKGEADALSLDGGYIYTAGKCGLVPVLAENRKSSKHSSLDCVLRPTEGYLAVAVVKKANEGLTWNSLKGKKSCHTAVDRTAGWNIPMGLIANQTGSCAFDEFFSQSCAPGADPKSRLCALCAGDDQGLDKCVPNSKEKYYGYTGAFRCLAEDVGDVAFVKNDTVWENTNGESTADWAKNLNREDFRLLCLDGTRKPVTEAQSCHLAVAPNHAVVSLSERAAHVEQVLLHQQALFGENGKNCPDKFCLFKSETKNLLFNDNTECLAKLGGRPTYEEYLGTEYVTAIANLKKCSTSPLLEACAFLTR
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Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. Lactotransferrin is a major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity. Antimicrobial properties may include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. The most effective inhibitory activity is seen against E.coli and P.aeruginosa. Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. Interferes with the lipopolysaccharide (LPS)-stimulated TLR4 signaling, but cannot directly stimulate the TLR4 signaling pathway and subsequent NF-kappa-B activation (By similarity). The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites.
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O77708
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KCC2D_RABIT
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Calcium/calmodulin-dependent protein kinase type II subunit delta (CaM kinase II subunit delta) (CaMK-II subunit delta) (EC 2.7.11.17)
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MASTTTCTRFTDEYQLFEELGKGAFSVVRRCMKIPTGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILESVNHCHLNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDMWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPAKRITASEALKHPWISHRATVASMMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSAAKSLLKKPDGVKINNKANVVTSPKENIPTPALEPQTTVIHNPDGNKESTESSNTTIEDEDVKARKQEIIKVTEQLIEAINNGDFEAYTKICDPGLTAFEPEALGNLVEGMDFHRFYFENALSKSNKPIHTIILNPHVHLVGEDAACIAYIRLTQYMDGSGMPKTMQSEETRVWHRRDGKWQNVHFHRSGSPTVPIKPPCIPNGKENYSGGTSLWQNI
|
Calcium/calmodulin-dependent protein kinase involved in the regulation of Ca(2+) homeostatis and excitation-contraction coupling (ECC) in heart by targeting ion channels, transporters and accessory proteins involved in Ca(2+) influx into the myocyte, Ca(2+) release from the sarcoplasmic reticulum (SR), SR Ca(2+) uptake and Na(+) and K(+) channel transport. Targets also transcription factors and signaling molecules to regulate heart function. In its activated form, is involved in the pathogenesis of dilated cardiomyopathy and heart failure. Contributes to cardiac decompensation and heart failure by regulating SR Ca(2+) release via direct phosphorylation of RYR2 Ca(2+) channel on 'Ser-2808'. In the nucleus, phosphorylates the MEF2 repressor HDAC4, promoting its nuclear export and binding to 14-3-3 protein, and expression of MEF2 and genes involved in the hypertrophic program. Is essential for left ventricular remodeling responses to myocardial infarction. In pathological myocardial remodeling acts downstream of the beta adrenergic receptor signaling cascade to regulate key proteins involved in ECC. Regulates Ca(2+) influx to myocytes by binding and phosphorylating the L-type Ca(2+) channel subunit beta-2 CACNB2. In addition to Ca(2+) channels, can target and regulate the cardiac sarcolemmal Na(+) channel Nav1.5/SCN5A and the K+ channel Kv4.3/KCND3, which contribute to arrhythmogenesis in heart failure. Phosphorylates phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2, contributing to the enhancement of SR Ca(2+) uptake that may be important in frequency-dependent acceleration of relaxation (FDAR) and maintenance of contractile function during acidosis. May participate in the modulation of skeletal muscle function in response to exercise, by regulating SR Ca(2+) transport through phosphorylation of PLN/PLB and triadin, a ryanodine receptor-coupling factor. In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (By similarity).
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O77726
|
ZP2_MACRA
|
Zona pellucida sperm-binding protein 2 (Zona pellucida glycoprotein 2) (Zp-2) (Zona pellucida protein A) [Cleaved into: Processed zona pellucida sperm-binding protein 2]
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MACGQRGGSWRPSGWFNAGWSTYRSISLFFALVTSVNSIDVFQLVNPAFPGTVICDERGITVEFPSSPGTKKWHASVVDPLGLNVPNCTYILNPEKFTLRVTYENCTRRVHGGYQMTIRVMNDSAALRHGAVMYQFFCPAMQVEETQGLSASTICKKDFMSFSLPRVFSGLADDNKVTKLKMGWSIEVGDGARVKTLTLPEAMKEGFSLLIDNHRMIFHVPFNATGVTHYVQGNSHLYMVSLKLTFISPGQKVIFSSQAICAPDPVNCNATHMTLTIPEFPGKLKSVSFENQNIDVSQLHDNGIDLEATNGTKLHFSKTLLKTKLSEKCLLHQFYLASLRLTFLLQSETVSMVIYPECVCESPVSIVTGELCTQDGFMDFEVYSYQTQPALDLDTLRVGNSSCQPVFKAQSQGLVRFHIPLNGCGTRYKFEDDKVIYENEIHALWTDLPPSKISRDSEFRMTVKCSYSRNDMLLNINVESLTPPVASVKLGPFTLILQSYPDNSYQQPYGENEYPLVRFLRQPIYMEVRVINRDDPNIKLVLDDCWATSTMDPDSFPQWNIVVDGCAYELDNYQTTFHPVGSSVTHPDHYQRFDMKAFAFVSEAHVLSSLVYFHCSALICNRLSPDSPLCSVTCPVSSRHRRATEATEAEKMTVSLPGPILLLSDDSSFRGVGSSDLKASGSSGENSRSETGEEVGSRDVMDTKGHRTAGDVGSKAVAAVAALAGVVATLGFICYLYKKRTVSNH
|
Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP2 may act as a secondary sperm receptor.
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O77736
|
TNR6_PIG
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Tumor necrosis factor receptor superfamily member 6 (Apo-1 antigen) (Apoptosis-mediating surface antigen FAS) (FASLG receptor) (CD antigen CD95)
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MSGIWVLLSLVFTCIAGPLSKGDDAQVTDPDSEMVKLNITKRESECPEGQHREGQFCCQPCPPGKRKHADCTSPGGAPQCVPCSEGEDYTDKNHHSSKCRRCRVCDGEHGLEVEKNCTRTQNTKCRCKPNFFCHTSQCEHCNPCTTCEHGVIENCTPTSNTKCREVFQSAGSRSNLHWLWALLILIPVPALVYREVKRRCRRKENGYQKPITSNAEEVPMIKDVDLGKYITRIAEQMKITEVKDFVRKNGIEETKIDEIMHDNPKDTAEQKVQLLRNWYLYHGKKDAYCTLIQGLRKAKLSALADKINDIVQKDVTSEQENANSQNENESLT
|
Receptor for TNFSF6/FASLG. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both (By similarity).
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O77737
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B2CL1_PIG
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Bcl-2-like protein 1 (Bcl2-L-1) (Apoptosis regulator Bcl-X)
|
MSQSNRELVVDFLSYKLSQKGYSWSQFTDVEENRTEAPEGTESEAETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVLNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIATWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTLAGVVLLGSLFSRK
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Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. Regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q07817}.
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O77742
|
OMD_BOVIN
|
Osteomodulin (Keratan sulfate proteoglycan osteomodulin) (KSPG osteomodulin) (Osteoadherin) (OSAD)
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MGFSSLVCVLFFFLGVKVYCQYESYQWDEDYDQEPDDVYQTEFQFQQNINYEAPFHQHTLGCASECFCPPNFPSSMYCDNRKLKTIPNIPAHIQQVYLQFNEIEAVTADSFINATHLKEINLSHNKIKSQKIDHGVFATLPNLLQLHLQHNNLEDFPFPLPKSLERIFLGYNEISRLQTNAVNGLVNLTMLDLCFNKIDDSVLQEKVLAKMEKLMQLNLCNNRLESMPPGLPSSLMYLSLENNSISSIPENYFNKLPKLHALRISHNKLQDIPYNIFNLSNLIELNVGHNKLKQAFYIPRNLEHLYLENNEIENVNVTVMCPSVDPLHYHHLTHIRIDQNKLKAPISSYIFLCFPHIHTIYYGEQQSTNGQTIQLKTQVFRRFQDDGDSEDHDDHHEGPEEEGTEENIDAHYYGSQEWQETI
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May be implicated in biomineralization processes. Has a function in binding of osteoblasts via the alpha(V)beta(3)-integrin.
|
O77746
|
PDE5A_CANLF
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cGMP-specific 3',5'-cyclic phosphodiesterase (EC 3.1.4.35) (cGMP-binding cGMP-specific phosphodiesterase) (CGB-PDE)
|
MERGSPGAGAARLPRDQDSVEAWLDDHRDFTFSYFVKKATREMVNAWFAERVHTIPVCKEGIRGHAESCSCSSQQSSRADSSAPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLADSEKKEQMPLTPPRFDNDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEASNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKLPDTLTRERDANRINYMYAQYVKNTMEPLNIPDVSKDKRFPWTNENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETKELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPADLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAEQQEKTLINGESSQAKRN
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Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. Specifically regulates nitric-oxide-generated cGMP.
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