entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
|
|---|---|---|---|---|
G4NEB8
|
MST7_MAGO7
|
Mitogen-activated protein kinase kinae MST7 (MAPKK MST7) (EC 2.7.11.24) (MEK MST7)
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MADPFAPRTMKRRNVKGLALTPAAPKPPPTAENAPIHRDSDQHAQLEIGIEFNLDLRPEDLEVIKDLGSGNGGTVSKVRHIPTNTVMARKVIHVEAKREMRKRIVRELQIMHSCNSEYIVTFYGAFLNENNDVIMCMEYADVGSLDRVSRVFGPIRVDVLGKIAEATLGGLTYLYAKHHIMHRDIKPSNILVNSRGSIKLCDFGVSGELINSIADTFVGTSTYMAPERIQGEKYTVKSDVWSFGLSIMELAIGKFPFAASEQLSDAESAPAGILDLLQQIVHEPAPKLPKSDAFPQILEDMIQKCLYKNPDDRPTPEELFERDPFVQAAKRTPVDLREWAFGLMERDNRKSHLAPQLSPATADLLRSSDSPTATYHGDDRPLETPTSAYRVDPRRGPAEGSAGLADQVDRLYIRD
|
Mitogen-activated protein kinase kinase part of the MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for appressorium formation, penetration and invasive growth. The MST11-MST7-PMK1 MAP kinase cascade transduces signals from the cell surface sensors MDB2 and SHO1 that recognize various surface signals such as surface hydrophobicity, cutin monomers, and rice leaf waxes. MST7 acts as the upstream MAPKK that directly phosphorylates MAP kinase PMK1.
|
G4RK16
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PFP_THETK
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Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent) (PPi-dependent phosphofructokinase) (PPi-PFK) (Pyrophosphate-dependent 6-phosphofructose-1-kinase)
|
MKIGVLTGGGDAPGLNIAVYTFVKLAERKHEVYAIYHGWRGLLNKEVKRVSSRDLLDFAFSGGTYIRTSRTNPFKDEERARLLESNVKELGLDVVVAIGGDDTLGAAGEAQRRGILDAVGIPKTIDNDVYGTDYTIGFDSAVNAAIEATESFKTTLISHERIGVVEVMGREAGWIALFTGLSTMADAVLIPERPASWDSVAKRVKEAYNERRWALVVVSEGIKEYGGPKDEYGHSRLGGVGNELAEYIERSTGIEARAVVLGHTIRGVPPTAFDRILAVRYATAAYEAVENGRYGVMVAYSNGDIAYVPIVDVVGKNRLVSGYWMRLYETYWPDLAG
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Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. {ECO:0000255|HAMAP-Rule:MF_01976, ECO:0000269|PubMed:9555897}.
|
G4SLH0
|
TTN1_CAEEL
|
Titin homolog (EC 2.7.11.1)
|
MEGNEKKGGGLPPTQQRHLNIDTTVGGSISQPVSPSMSYSTDRETVMRSASGHATVAETHLIRSIGSQSQSYTEEHWSSEITSFVALAPPKFIQVIKAYRVHSTDTISLVVEVASDPPAIFEWFYNEKSVLQDRDRFQVGHGINISRLKVSRPEQGVYKCVTRNPAGVSTSYGYITVNADREHLSSSKEDMRLQRQHSVTYHQAPRFLTQVPNLFVTAGSNVIIDVEVDANPPARFSWFVNGKEYRDSIHGVEMFSPDVNRSVVRFSIPVAGEYKVVASNVHGSAMSCGHVDIQKVIELEESTLTTSTTAFDPMTTSMRALGNNGRNSRQAVNMFELNYTQRSSSVPRGVRHLESHIEVSNMTGEEKKTQQQTRTDAASIVESRFHPQPPKPPRAGTSRRFLPEPPKFVTTLPSVITVNAEEKLVLSVDVQAIPAAEFAWHVNGFEVKKSQSVVLLDEHNKSTLVLHPPVKQGKYKVTARNDVGSDSVTTQVTRIGEVKDGAGSEPPDIVESAVTVTCSHEEDVGSHSSLQTVRRIQEMQEEDEVDPIKPFIEATSPKVKESVEHPFANILNPKKREERLSPSGKGKHLLFAPRITAHPSESVFKILDGSPLKLRVMASSLPPATFLWMLNNFELRSNQNVTIRNDEENSSEIEFQKAPNGNVTVSAKNHLGEDRWTGKVILQYESPPPGQKITTIEKVTESWTLEEAVITQVVPTAADPGDRIVIIVRFDENKTSNCQFNWTINGVNIEKLEENLVAVESTEFESSLIVEKLEEQLCGEVVCVVKNQHGEVFSSSAHLRIRDDDSSFEIVPPNLPEECAPKIVEPLHSASFLDGQAMSLRCKITANPSAAVVWSKDDVNVEDWVLNKDVTTTVLDGGVCELLNPECFAEDAGLYKCTATNPHGTAETAAFINVEGAEYIKDHEEAEISESVLTDDVHIILPPKFIETLTAETDNFQQLGYVRMVATVRSVAPITVSWQKDGMDIYENEKYEVMQFADGAQILTIRAPTNLDSGVYTCTAESEHGVSNSSCQVELTISAESSPESFEKVEITPPEEVKETGIDDDIEVILKEEVSGTAQIEKREEEFKLLVKVADQVASTLVANVFLEAVHEAVKKIVETEDEEEDNQIEATQEPRFETSTDEYHVKENGTIKMAATISGHPTPFLEWYFGEEKLQVSQNVSMYYEAGTSAIILKNVQKRQGGNYFLRAHNCHGESILPMKLTVDPIEAVTHVLETSIPKVVVEQDAKEEEVRRAAEIISEQFAQLWVQDAQTEAVSAQAHQTPVVAEQASEEPTLPEVVAALQEQKPSVEKAPQPQFEVLETEDQDVVEQMQKQLPPVQKSMSVQEEKASSQRTPSPMNYEDKVKTIQSNLLRVNSHEAMEPIEATNLLLNTALQLKNEHVCDETTTVIVTQQPQKYDQLVTVVESNIEYHALRLSTSSSSPLKFIDLETIIQKPSTSCESIDRMFVEKSKRTANAQHRIVVLQGMSNTFHNAITWSLKKVKKLVGDAEAKAYADVEVVKQDETNEQVMTIIDNDTIVPQLLQVAAAANKLKLENVSVALIKEGDRAHQELVIEYESSIDEPMFEPVHNTSHLTFHQQQPTGPDQHVWSRRSKFEEDEAHVVAVFVEVDANCPDQSVEIVATVNAAYEGDNRQGIEDEPFTEVSQSLATESSAAPQAPKFLRKLVNCFGRIGEPVQLKCLIAGMPQPEIEWTVDGDPIVPNDEYSIVYEDGVCILRIESTLIEDEGEYCCTASNVAGTTFSKCYLKLSEADDDAVDLLRQLSEIKIIDPTLSTGYPMSMISDEENTSHQLLSNVLLTDKEVPITATYNEDLSRAESFRRFFESAETTVKVTELYQGESVEAQFQQPEKREQVSTSNTDVMFVNQKVDVMESTVSTVGNAVRQSVSSSTNSWDYMFNDPFPESQEINVIENELYEPRVPLLPQKLSYKGQEIFANTNTVERNSKAGAKAKGEVENLKKCVETLLLFDAEMDMKDIKESSPKKEIISKKDQQSLDDQIKVTQQILKDVERDLNKMERTSPGKSLSPNKRTFAPKDVEDIEAAIFSISDQLADRQSSEEALREALQEMILSNSSPMKELSRNNETSKPEVLKSEIQKIPEVETKISEVYPIVKLKQAISAIENSLLEDTEVTEIMKRKGSDKDKRKATRIKRVPSAHSARITPITSNLRDRLNQLHQLTVSEDSGSLKQNEEAKEIQELFVKIEKEINTIAELCKEKMTKKGADTVTHVLNSVLQHVASIINVILVAQDHQPIEVHAETTKTAEVSVWYSFDVHPESEDIIGIVDEEPTNRRPSSTPRGSTRSSNLTTSQDSQATTKMTVSSEDTIEAPIAPPRKGRSLSRDAERLLEIQPRAPPRRSRQSGDTLSPEPTPVLTLVKSDETPAPVRPPRSRSRHSGDELAETSPEAQPIRPPRSHSRHSGDELEEVQPVRPPRSKSKTADANCLQIESMDESQYSLSCIHIQKTNFAFTNSTHETSNASVVVDLRNMAQLECTVQSLDDLASIQMLCEESDYPSDTDRSLLLAGTVRYFNRASPSLHEVSPSLNMESVSMDLKPETEPEEIVQDVYVNVELHSVPSLSSLVEVNPNTLMQTLASEKSSLKAAEEDEKEGEEEGEEEVTADVSFIGRSVLSTETLDVVLEEKDMSQMNSTLPLDYERAFSSNTIRETDILSDESITVDSSYHKSPEPTVDFARSQVKSEEVTENFSLIHKPARRRVTGIVVNSLIYTIAANIAEDNTFDVDVVQEPQRYNISIKVIEDIVDFTSLTIMSDCEDDPPADVLVLKQDTSKLQALSYDDISVATTRTGITVSIVARSLNDGIYASLEEIAWGEVEMTVPDIMQMSTEEKSSLQFNVTVSESNLEEAKSLKSQVSFRSSQNSVSEMDNTISSTATISIPSYVVKLESTATITCELNNYLPKNCTIDWYCGKTKIIIDHEQFDRISHDLLEVLIIRSVEAINGNLYSLKINEDLFPVAYLIVENTNLTTSANILTRPETQFVMEGQPTVITVELDDPNVIVNWLKDRRPLHENERIRLETDGQGNHRVIIPNTCVGDQGTYLALTSSESVAITLVVEERIEEKEVMVIASGTESEEDDVQEYLVPPGSTATIACELEECELKRSIRWLRDGKDIRFEQGKTEHVQNGLKHYLVVHDATSLDSGLYKTERSEEQCEETIIPRGVVATIQCQTSEPQESIQWSKDGNIIPSDISRFEFRSLDNNQSHEMVISNISWSDAGVYSVLINGKSSFVSKIVVVESELITQSVEEEPEAEPEIDVSLHIVESEQIIELNVPQSPKLGASHETLVPIGQDDIEVIDKQEAAPVVESIEETSSIGSEEFEIIEKFTEEEVPKVAEPSEPTQADVPKIAAPLEQSQIQQEVPTVAAPSEPTQADVPKEAAPSEPSQADVPKVAAPLEQTQIQQEVPMVAAPLEPTQADVPKVAAPLEQSQIQQEVPTVAAPSEPTQADVPKEAAPSEPSQADVPKVAAPLEQTQIQQEVPMVAAPLEPIQEEVPKEAAPSEPTQEDVPKGAAPLEPTQEDVPKEAAPSGPTQEDVPKEEAPSEPTQEDVPKEAAPSEPTQENVPKEAAPSEPTKDVPKEAAPSEPIQEEVPKEATLSEPTQEQSEVSKRSEPVEPTQIQQAASEEETPLEETNETVVQTNEDVKEAEVPENAEAQKVVDSSDLQVAASEIAHLAIDEAVLETSNQPSQFDSLQEQKPSVVHENEHVRSVCVDLTFSRDSEQIVSDVIVAEVGYDEDECSTIADTITSLSSSPLYTAPVFTERLPSSACFANSKLTLEVMFSGVPQPTISWLIDDHELVSDGERISIKCENGVSAIRFFNVDRNAGGFLKCRATNCAGQVETSCEIVAADEISVISDSSITSSTRPHFVVPLPERVTHTVNDHITIKCKFSGQPLPAAMWEKDGVLLDLQKYQVTTEDGTSILKIESASLDDKAVYTCTIANEAGCESTSCTIDVVDDHLGLQQTGLHVMCERDQNDVELDILVQSPNHLGVTFNFPPVNRTLARQPPYFLLPLSDKVVIDEKCTLKCVVMGIPLVIVKWIVDGVVVTEDDNHEIHFEDGIALLRMKNIKKDKSVVQCEAINCKGKVTTSCVLTKCGVEESEAGDLQKPSFVLSLKDTCTTTDHATLKCIVVGTPLPDVSCSFNGVTDNSKIRSEDGIVLIQVNDVTEEGIVVECTISNETGSSTSNCVVKIIKQEEKNYQRPIIVFNQAGSVNNERELSVKVGVIASPEPTLFWKHNGKSIEEGGDYYLIFEDGIGILKVFNIQDGSHEFTCIAKNEYGQTTVEIPVEIGLKTENKLTLVKTLNDIAVVDDIVQLKIVAEGDLPIEFKWFEDGQILEDDSSHKITVDKCISTLQLKLEETGTRIITCEVSNSSSKVNASCNVERVHNTVSDFVMTNDNSTRFLAVGRKCTRERNNTILKAVVVARENIGDICEIDGEKIPDAYIEGNSLSIKVDTLSKKLSNVSFKVSASEGKVFETRKIEIAQEDTDEENFEINYSLRIDEQSGNTTYTFENSELYQGNQSRELDNTERNFTVNKEKDESKKPSEVQPAEIVEQKDVPVQETSAPTVEKLAPVESKETPEVQAAEIVEQKDVPVPETRAPTVEPTVEKHTPVDSKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKHTPVESKEKSEVQPAEIVEQKDVTCEEEIKELLTEVEVELFFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPSVEPTVEKLAPVESKETSEVQQAEIVEQKDVPVPETSAPSVEPTVEKLAPAESKETSEVQPAEIVEQKDVTCEEEIKELLTEVEVELFFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKLKPVESKETSEVQQVEIIEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKLKPVESKETSEVQQVEIIEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKLKPVESKETSEVQQVEIIEQKDVPVPETSAPTVEPTVEKHAPVESKETSEVQPAEIVEQKVVPVPETSAPTVEPTVEKLAPVESKETPEVQPAEILEQKDVTCEEEIKELLTEVEVELFFSKAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLKSVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKLAPVDSKETSEVEPAEIVEQKDVTCEEEIKELLTEVEVELLFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLKSVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKHAPVESKETSEVQPAEIVEQKVVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEQKDVSVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTIEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVQPAEIVEQKDVTCEEEIKELLTEVEVELFFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAHEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDLPVPETSAPTVEPTVEKLAPVESKKTSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETTATTFEPTKEKLAPVDSKETSEVQTAEIVEQKDVPVPETSATTVEPTKEKLAPGESKETSEVQQAAIVEQKDVAVPETSATTVEPTKEKLAPVESKETSEIQTAEIVEQKDVPVPETSTSYVEPTKEKLAPGESKETSEVQQAAIVEQKDVPVPETSATTVEPTKEKLAPVESKETSEIQQAAVVEQKDVPVPETSATTVEPTKEKLAPVESKETSEVQQAAIVEQKDVPVPEANAPTFEPTVEKLAPVESKETSEVQQAAIVEQKDVPVPEANAPTVEPTVEKLAPVESKETSVESKETQADAKLKKEKDDKHKQEADAKLQKENDDKLKQEADAKLKKENDDKLKQEADAKLKKENDDKLKQEADAKLKKENDDKLKQEAAAKLKKENDDKLKQEADAKLKKENDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLKKENDDKLKQEADAKLKKEKHDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQDADAKLQKEKDDKLKQEADAKLKKEKDDKLKHEADAKLQKEKDDKLKQEADAKLKKEKDDRLKKDADAKLQKEKDDKLKQEADAKLKKEKDDKLKHEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQDADAKLQKEKDDKLKQEADAKLKKEKDDKLKHEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQDADAKLKKEKDDKLKHEADAKLQKEKDDNFKQEANAKLQKEKDDKLKQEKDDNFKQEANAKLQKEKDDKLKQEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEKNDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQETDAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADGKLKKEKDNKLKQEADGKLKKEKDNKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEANAKLQKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDNFKQEANAKLQKEKDDKLKQEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQETDAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADGKLKKEKDNKLKQEADGKLKKEKDNKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKGDKLKLEDQTNQSRIFEETSIEVTSLLKCKQQAIIVSKSFALCERVVLNAEEPFTLEVFCNAVFVKQRTDKIGIGIIFERSGASKKDESRPDRLDDNCVLTDVTDGLSILSPPPKAKKHLKKKKKHHKKEKIAVKETEQDEKTVSHLKPEISGMERKRSNSGSSDIFVDVDIEAGEESIHTDALVDLNFYDYDQMELSIFEDYDSDDDSASIDCDVSLSNVAADDGIDVFPSDGDTQEVEQKVTLPKKHQSDEDVISKEEENLETSVSYGSIEETVSFTIGTGQSIIEHPKSHAVGQMNSEVIIKCKTSQPISDAKWFCNGMVLLPDEQVNMTVTGCEAVLRLVKFLPQNKGNYHVLIDGSIGSQPAILSGPVPPVILNKLTKPITHQAGKSFTYKFNFMGAPAPRLRVLSNGEPVSFDVKYEIYDNIASLYIPKMSKRDGGEYTVVLENKYGKDESDLHITMVDTPLKPRKAQLVALTDTSATFKWLPPHTGESDILHYIVMRRSTESRRWRNIGHVQEKTFTAIELVPNEFYAFRIVAVNGFGEGAPSEIIEVNTLDYDQEESFDFAGEEELKLDDVQVNNEVVTEITIEESEVTIEEHRKLKKKSKKSKKTTDEPELDSEIALEVSSDITSSLEITTESTIPDTAPESQETLNVEIAVTETTVQKITNPSDESAKKDVNEDTAVSSIVKKDDKDVNKKSLPESGLTTKKEIQGKPEKKIMKKKTEKADSSISETSETLTKDLTQTKQSEPEPAKRTTETSVQDEVKRKTETTSKSKQTTEEHPQPGGKSDSSISSTSDASEVKQVQQSESEAQKVTEKPETAKLESKSKMTEDTTKESDNKETVDEKPKKKVLKKKTEKSDSTISETSETSAVESAGPSESETQNVAAVDKEKKQKETDEKQKLEAEIAGKKSTEQKSKLEAEAKLKRAAEEDAAKKQKEKTEAASKKAAAEKLELEKQAQINKAAEADAVKKQNELDEQNKLEATKKLAAEKLKLEEQSAAKSKQAAEEQAKLDAQTKAKAAEKQTGLEKDEKSNKDSGSNETVEEKPKKKVLKKKTEKSDSSISQKSDTSKTVAESAGSSESETQKVADATSKQKETDKKQKLEAEITAKKSADEKSKLETESKLIKAAEDAAKKQKEKEDKLKLEADVASKKAAAEKLELEKQAQIKKAAEADAVKKQKELAEKQKLESEAATKKAAAEKLKLEEQAQINKAAEADAVKKQKELDEKNKLEANKKSAAEKLKLEEESAAKSKQTVEEQAKLDAQTKEKTAEKQTGLEKDDKSTKDSESKETVDEKPKKKVLKKKTEKSDSSISQKSVTSKTVVESGGPSESETQKVADAARKQKETDEKQKLEAEITAKKSADEKSKLEAESKLKKAAEVEAAKKQKEKDEQLKLDTEAASKKAAAEKLELEKQAQIKKAAEADAVKKEKELAEKQKLESEAATKKAAAEKLKLEEQKKKDAETASIEKQKEQEKLAQEQSKLEVDAKKSAEKQKLESETKSKKTEEAPKESVDEKPKKKVLKKKTEKSDSSISQKSDTAKTVAESAGQSDSETQKVSEADKAHKQKESDEKQKLESEIAAKKSAEQKSKLETEAKTKKVIEDESAKKQKEQEDKKKGDDSAKKQKDQKEKQKLESEATSKKPTSEKQKDEKTPQEKAKSENETVMTTEPQQLEVKSEPKKSDKTETVEKEVASSTEKSDDSKTKEPKEKKKIIKKKKDTTKPQEASKELSSDESRIDLESDISLSLDTVTESDDLSTASTIKLQKESDESGIDSRMGQTSEAEDSPFISQPVSATVTEMAGEAKFTVKFSRKPIYVKWMRDDREIRVAYGKASVETTDDSSVLVIKNIDGKDVGNIYAVFDSEYRSAMARLDLRVPCKITLESSSNAPEIVAGKNLDLSFKISGYPLPTNIELLHNNENLRTRSDVTDFDDSISIRMKRLKLEDSGEIKIIGKNDSSEDQLRIPINVIEVTSKPTSLQVTSTERETVTLTWSLPTELNGSNVNEYLVERKTVDGGRWRHACTVTDSRAVVDGLFSGTEYVFRVVAVNGAGQSAPSDTIEATTQAEEEIDETVPTSPVEKVKEPVSKKPENTKESEGHKKRDRKESEDHDENNLGKSGKDEFATSGESGTSNQNEESAQLNTSFTSTEQHGQTEKQVRKGTRKSLTRSLNIRESDIDADVVEVEYDEQGDDIPSDPTTSGTYAFDKIEEEPARTSGEMAMAEKDSDAMEVRGLNKKLSKKGGKEGTSTEKSSSKTKKQEKSALSVQEMNKSLKKKGEKGEAETAASDFIENADQTGMSIQDLNKSMKKKVESGEATGQINDASNNKDADELSIQDSQQSLKKKSENESVTGEQLDKSQEVEDDKMTIQSLKKSIKKKPESREVSGGKSEKSKEKESDEMSIQQLNKSVKKKPENEAVTQGKSGKSQEQESDKMSIQALNKSMKKKDGVDGVEGNINIGRSDGDQLSVNDIDAELSTSEQVENASQNLGATADSDGDSLSLQTLKKRISKKGIHGEAESKLGEKQSGSDSFTLQDLYEELKAKEDAVEAGAETSNADQSAEKTSLEVRDMKKKMKKKQVSGTAENLIGESNRDETSMEIRDLNTQHSNQTGEDESSTFNFGQKDQEQYSMVMKDVSKKLARQNAEEIQSGKLIPTTNEEKTGLALTGKNKNLKKGEENEKTKFEAKHLGSSSASDSLAESTLRSKKTKKGEVEKSELSIDMKNQDKTTLATTLLEDDLAKTTSAEESEAEHLVALQNKEKTSLAMRRKRVSFDSSTKSESIEDVIPDKNRDSDKMSITGIKKKMSQKSESAEAQKNESPEVKEISSFEEKTLKSKKKSKADRNQGTEANLGDKTIDKDYLSVTDKNQSLEKSEASGQAEKSIKAPNKSKVTTSFADESLTSELDRLMADEEMAEMMFAEEEKAADLLNVMNKNKGLNKSEQEESQEISLKSQSKVKDSDSLSSTDKKIGLKKSDKDQKLGTSKIFGSKDQESVGYEEKTSNFSKQRRGVSDLGSDAMTDQKNVQESQYAEISADDHMSKTGADGEISATRTIVDGSDAAQGSEYAEISKKRKFKRAEQIGEAETSLCDSRENTHDSLSISDVNPELRRSNVEISAFGQIDLTAEEVTSLTDINKDAQLTKKQDENDAKKSVSKNLKAGAKKDSDTLSITSKKDKFGKRQDSREASATVEQQGEEKVTKNLKGSRGKKEKLGDAGIDVNFENQEEFASTTGDIESIVSEKGHDTYSEKTVKSSKKKSPQTAGAEYGGSESLNASSALSTTDVDAQLKNQEKDGVAESSIGKSNQKDSYSEQELNVNKKKKQAVGAAMNQGSGSTKESDNLAVASVESNLAKDSANQEASLHGLVDNDATSLSQLDSEHRLKKRDDELSAHTKLGKHTQSENIALTETDDSLVKGDSEESAELNIKQQGETAEDKYVESRKKTTLKKKPEQKQVTDTLSAVDGRHDTTSLSVADSGISFDKSMENELAGSGDGTASASVSAKVRGADGNAKTNLISSFEKPGQESKTSKTLSGKQKKQEKSSFAEKNAGFDLSMGEGKNDESVESSLQKNRDADSLALQGTDLAFSKPSDSSANAHLDMPQRELTLRICQAETVDWSDDSEVEEGTRTSAPGEVKKKKKFIISAISQDGEFSDAESITFDENGVRVEKRRRKKRDPKEYMGAGELAMRIPAFAKKMQYIGCIEGDVVVFTIKVVSDDVPLIRMYRNDFPVANFDKMAFEGFTKGSEHSFNVTINDIRKLDGGKLVFEAKNDYGVDKCTILLDVRDSGSFIEDYSEIHRSAEIQNSVGDVQVKEGETAKLTGRVDGFPLPELIWIKNGKEIDMMVPSTKYQLDYHSDGEFEARIANCTFEDDDDYSLLVENLAGVDSCNFQVFVDCNEYPDDEHFNRRRRLQRGRRVMEASSDSELDDAKKRKKRRIKRVVERRNPNAPRLTQLIPPRFDKILSDHDAIEGENVVMMVETLGEPEPQVRFYRDGKLIDDGSGDRMEVRHEDEMRKHWLILKDICKDEEAEYACQAINVAGEAWCFSDVVVHMSEESRDDDKSVDEVDDSTVLEEKKDDGDDKSKPKTKKKIIKKKETPESEQVTAAEPEQQKISEVDVQSVAETEVGAKKKPDAEKPTDLSKAKKDSKSKKSDEPEASTEEKSTTEKPTNDKTSKKSAEKKTVKPKKEVTGKPLEAKKPVEDKKDASQPSSSKESSPPTDGKKKKQIPKALFIPDEISSRFGDPSTMHSETNITTTIRGREGSADAKTPLVEPLSASVSMKVESAKEKAEFSFKRRSETPDDKSRKKEGLPPAKKSEKKDEVTAEKQSTEALIESKKKEVDESKISEQQPSDKNKSEVVGVPEKAAGPETKKDVSEIEEVPKKKTIKKKTEKSDSSISQKSNVLKPADDDKSKSDDVTDKSKKTTEDQTKVATDSKLEKAADTTKQIETETVVDDKSKKKVLKKKTEKSDSFISQKSETPPVVEPTKPAESEAQKIAEVNKAKKQKEVDDNLKREAEVAAKKIADEKLKIEAEANIKKTAEVEAAKKQKEKDEQLKLETEVVSKKSAAEKLELEKQAQIKKAAEADAVKKQKELNEKNKLEAAKKSAADKLKLEEESAAKSKKVSEESVKFGEEKKTKAGEKTVQVESEPTSKKTIDTKDVGATEPADETPKKKIIKKKTEKSDSSISQKSATDSEKVSKQKEQDEPTKPAVSETQMVTEADKSKKQKETDEKLKLDAEIAAKTKQEADEKSKLDAQEKIKKVSEDDAARKEKELNDKLKLESEIATKKASADKLKLEEQAQAKKAAEVEAAKKQKEKDEQLKLDTEAASKKAAAEKLELEKQAQIKKAAGADAVKKQKELDEKNKLEANKKSAAGKLKIEEESAAKSKQTVEEQAKLDAQTKAKTAEKQTKLEKDEKSTKESESKETVDEKPKKKVLKKKTEKSDSSISQKSETSKTVVESAGPSESETQKVADAARKQKETDEKQKLEAEITAKKSADEKSKLEAESKLKKAAEVEAAKKQKEKDEQLKLDTEAASKKAAAEKLELEKQSHIKKAAEVDAVKKQKELEEKQRLESEAATKKADAEKLKLEEQKKKAAEIALIEIQKEQEKLAQEQSRLEDEAKKSAEKQKLESETKSKQTEEAPKESVDEKPKKKVLKKKTEKSDSSISQKSKSAKSTVDAAETLESDFNLVEKKTVQKVEQSPDESTSATIKRDPAQKTEEISKQDDGDEKKTTTDGKPPKPEDSEATPKKRVVKKKTQKSDSVASDASLADVSKLSDDVEEKPKKKVLKKKTEKSDSVISETSSVDTIKPESVEIPTEKAEQMILHNRFSTDSAVESEPKNAHKDDTEKTTDDMMTRRKSSAIFSDDEQSISSKTSSEGRRRRRRTGFASKFASDTLALRGDNVEIEAELLAEDDTVTWKVNGKDADLNSRCHEMSHTFFRTLIIDEVEPTDSGMEITATCGTESHTTILKVEELPVDFVKYLPRKTSGKEGQEVTISVTLNHPIDISKVVWLKDGKPLEINKDYSIDTVGCSVSLTLRRAKYEDSGKYKVVCDGVDCSTHLSIQGKPVLKNVSETKPVITVDKDDQFSLLVAYDSNPEASFSMTVDGKDLEFDGRSRIDVVDDGLKLTKRGVSKTDAGEYEVKLKNEFGEVAQKFDVKVNDTPSAPGDVSVVKAESDCLHIEWTAPTEDNGAEVTSYVIEKKESGRRKFHKVATVNGKKTSYVVDDLEIETPYIVRIAAVNKFGTGEFIETKPVQTGSPFQVPTVEFPPTIDNVTSTSCSLSWPKPIEDGGSPVYGYDVYKRENEGEWQKMNGEELVFTESFNVRALSSGKEYEFKIEACNEAGLRSNSNVVSKKLTVEGLVPEIILDMPMVKVLDNDKVEVTWKSDGEKEFVVQYKSDGSSIWASVDIGGPRSESAATSKCIIDGLREGIPYVFRVAARNQHGTGEFSEPTIPVVVLADDAPRVLKAIKPVKIPKKGELRLECHAAGHPAPEYIWYKDGKEIIPTDENTEIVNEGSMSALIIHELAGEDVGLYKVLVENIHGTAESEAEVGISDVRAHFNSSFSELTEIEEGHDIELTCEVSDEEAVVNWYKDGKKLVASDRVQFYAMARKRTLRIKGSTDADSGVYKCETTDGRSRTEGEVIVNEQEPHILVGPQDAIVKDFGETMVLFCETSKPVRKVKWFKNGVEIWPQMNKAIMENDGKRATLEIKNFDKHDIGAYTASVSEKETSAPAKLVFEVAPNLIIPTEIRDGVTVHAGNEFDFAVEFSGFPIPTIHLTNNGTPLKAIAVVTEYDDSVSVRMKDVTLDNSGTVRVIAESPLGQCIKEIPLKIIDKPSAPCDLQFKEVTEDSVFLSWQPPLETNGAPLTGYVIERKAVDNNRWRPCGQVKPTKLTFVAEDLFCNQVYGFRILAVNEVGESEPCDTVDVLTLESSEPVSESSELFVPKIAILRTPQVTVAVDETKVTLRWEECPETSLYKVERKKVGDSDWLEIANTDRNKFKDRSLTESGEYVYQVTATGIHAVSSPSEETNPVKILVPGSEMPASKTEKKTDAAKSESEQKSAEEIVAEKQVDQSQASESTTEAVEEKKTKKVVKKKVAENKGEETLQEVKEKLKKGKAVEKVQDESRRGSLQASSDNESVTTTSEKRSEAELEKNSEKSAEKKSTSADLEAADKAETEKSETGKETTEKKKKVVKKVAKKGLVKADKSKIELTAGKEGEISAQVAETGVSVEWKKDGKALDASYTVTSTGGVSTVKIPIVDVNTSGVFTCKVKSSEGDEEEVSIAVTVKLPEVPKVEAEQSIVEVKVGDVAKLSAKISEPASSVNWTKDDKPIKEDGNVKAQLSPDGTAQLTISKTDSAHSGIYKLNVENDAGKGKVEIALRIKGAAKGAPGIPTGPIVFDDVTESSAEFSWKAPENNGGCEITGYNVERKESKNKGWKQCGKTKELKFKADGLEEGTDYDVKVSAVNTMGTGSALEGKITTLKKKEETGKQKSEKSESDEKKSESDKVSELKQIGKPEYVSSTATSIALKWTSDNDEVTYTVQMKEANSKRPWAVVAKEISECSATIAQLKEGTSYLFRVIAQNKTGQTVTSEQSESIECKDTTESKKPAFTNAPTDLTAVKNGKTKITAEFTGHPAPEIHWFKNKKEIFSGKRQWIENIAGATSLTIGEMREDDEGEYKIVVKNTAGSVEHSCKLTMDQLPEINRVDRYASTLVFDKGETVKLRLSFSGRPQPEVIWIDNNGKVIEESRKMKIEKTVLNTVLTINSIDSQDQGEFALKIKNRCGEDKYAIGIQVTDRPAAPGKPAVEDQNVDSVRLRWAAPTNDGGSPVRNYTVEMCTEKGKTWTKAEVTKQAFITLFNLVPGESYRFRVRADNTFGQSEPSDESELVVVKNVSRVVEEPKKKEVKVKEQESVDYERVAKDSEPSEYKTIDIHRLPNDLQAKYIIHEELGKGAYGTVYRATEKATGKTWAAKMVQVRPGVKKENVIHEISMMNQLHHEKLLNLHEAFDMGNEMWLIEEFVSGGELFEKILEDDSLMSEEEVRDYMHQILLGVSHMHKNQIVHLDLKPENILLKAKNSNELKIIDFGLARKLDPKKSVKLLFGTPEFCAPEVVNYQPVGLSTDMWTVGVISYVLLSGLSPFLGDSDEDTLANVSASDWDFDDPSWDDVSDLAKDFICRLMIKDKRKRMSVQDALRHPWITGPLLSAFNDLSEYVKKMQPKLDKSGVPARQKRNFLSLKRWSDDLLPIGRLAKRGAIFRRLTMDGVFERNIAFDTDAAPSVKKQLEDIVANVGDLIATLSCDVDGVPSPKVQWYKDDKELTVPSMKYDSFYNEGLAELTVKNIVESDAGKYTCRATNDLGSIMTHAKLSVKADEKKKKKSKTSPAVIEKKKDRKTSKVVVIEEMIDMPPNFHHLLQDDEAKIGEPKILVVTNTTLPEPTVDWYHNGEHISINDSNYLRKHDKGRYELHILSVDSTDEGKWKAVGKNAFGECESEAKLTVVIPDGQYAPSFGKQLSDVKCSESDILKLEVNIQANPAPEINWFRNESEIEHSQHHRLQFDDGSGNYSLTIIDAYAEDSGEYKCVAKNKIGKAHTVCCVRIEELLSKRSKKIDGSKAPRFRMQLPTPREVPQGADLTLVCSVSGTPHPNIKWTKDDKPIDMSNKQVRHENGVCTLHIIGARDDDQGRYVCEAENIHGVAQSFSVVEIKEAVDKDHVRPKFLEPLVNCSTCEGNEMVLECCVTGKPIPTITWYKDGLKLIIENRMLQYTDRKGVSRLNIMNVVMNDDGEYTCEAVNSLGKDFTHCTVKVVDMGLSKTRLTPVRSRSRSRSRSPSVVGGEIQRPPVVTRPLADATVTEGNRELLEVEVDGFPTPTIEWYHDGKLVAESRTLRTYFDGRVAFLKIYEAHEEHNGQYVCKVSNKLGAVETRAIVVVEAPDAAEHVTQMPTFVKKLQDVVLKTAGETATFTCQSYANPAAQVVWLHNGKALQQTKSNYKTRLFDDNTATLVIENVTDELCGTYTAVANNQFGDVHTSAQLTISGSEAKKIAASLPYFIIELKPKINVVEGATLSIQADLNGSPIPEVVWLKDNSELVESDRIQMKCDGVNYQLLVRDVGLEDEGTYTITAENEKGKIRQNTEVSVTKSKEVKEKKEKKKVEKKDEGKKKPGRPGLPRPSGASKTEQVTMAFDAPSEGPADSYEVERRCPDQREWVSCGSTKSLELEIKGLTPNTEYIFRVAGKNKQGLGEWSEMTSTLKTASVGQAPQFTISPQSKIIANRDDEFEIAVEFSGTPTPSVKWYKENLQIVPDEKIDVATTSTSSILNLKSQEENGTFNCLIENELGQASASCQVTIFNKPASLQSTPDHSLERNLVPTLQKALNNESAQAGQQIMLTCRISSRSESTVAWFKDDERIESAGRYELSSDKKSNHKLVCHAVQSQDTGKYRCVVTNKYGYAESECNVAVEDVTKFIAPSFSATLSDSTAILGHNITLECKVEGSPAPEVSWTKDGERISTTRRIRQTQDENGNCKLSISKAESDDMGVYVCSATSVAGVDSTSSMVMIAKTTGTDSHLVIAQTADEKHEKPRFTRAPPSLIEVNESGQFTLIAKAVGEPKPTVTWLKDGREILRTNRIYHHFVTGDGESHLIAECVVSKTSGIFSCKAENPNGTVIAETQVIVQRMKPANQLANVAPKFTIPLTDMGIVNGHPTTLSCNVTGSPEPTLEWIYIDDSGHKINLTSSTTDWTECRFGKVAELKSERVLREQRGTYQCIATNSSGQATTQCYLLVGELSDEPAGPPRFVKCLQDTWTPLKESIEFSVELAGFPTPDLTWYHNEKKINEGKDVKITFPSDTTSVLSIKNVSLASLGMYFVEASNIHGVLRTAGRLNVSDERRKAEPPQFKHVLEPVLAVQPKVAFSEEHPRASSSAATARVKKGAAPMFLQGLEDMDLKAGASAAVAGKLGRKLRPHRSTTNDADKLAKALAQSLRLDEPRASIDSRPESAANAALDEVRAAINSRNKRVCRPKFMVKPKPRKVLEEYKSLRLKTAISGNPMPQVHWDKEGIILETGNKYSIYNDGDFYYLEVHHVSTFDKGFYNCTAANNEGIITCTSEIDVLPNKEDSAAQVAKRKSRKEAKAPNFIEVLPGRSQANLNESLCVECSVSAYPCASIIWTRNSVRLLPQADRYTMSYDGECASLKFISVTPGDEGTYACEAVNELGSAVTNMNLQVSGVDPNAAEGIPPLFRFEKIKSVRKVVDGSRVELAAELVQASEPLQIRWLRNKVTIVDSPSFSYSRSENMVFLTIADVFPEDGGEYTVEAKNQSGIARCTMQLDVRNNERSVADEAPRVFDFEPTTRSDPGVSVELRAKVIGHPDPVISWTKAGQKLNNEEKYMMRNEGDKFILRIANVTRADAGKYELTAINPSGQANAELELTVVQSTKTVGAKPKFNESPISVQTCEKNRAELRASFSGTPAPACRWFYNGNELIDGLDGYTITSSDTNSSLLINSVDKKHFGEYLCTIRNQNGEELANAMILSEVLSMFYSSLFLVVFVDIVAQCHVARLLHFLNEERFVGRNIFA
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Serine/threonine-protein kinase. Key component in the assembly and functioning of muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase (By similarity).
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G4STG9
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PFP_META2
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Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent) (PPi-dependent phosphofructokinase) (PPi-PFK) (Pyrophosphate-dependent 6-phosphofructose-1-kinase)
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MNKPKKVAILTAGGLAPCLSSAIGSLIERYTEIDPSIEIICYRSGYKGLLLGDSYAVTPKIRENAALLHKFGGSPIGNSRVKLTNVKDCIKRGLVQEGQDPQKVAADQLVKDGVDVLHTIGGDDTNTAAADLAAFLAKNDYGLTVIGLPKTIDNDVFPIKQSLGAWTAAEQGAQYFQNVVAEYNANPRMLIVHEVMGRNCGWLTAATAMEYRKLLDRSEWLPEIGLDRAAYEVHGVFVPEMEIDLAAEAKRLREVMDKVDCVNIFVSEGAGVDAIVAEMQAKGQEVPRDAFGHIKLDAVNPGKWFGEQFAEMIGAEKTLIQKSGYFARASASNVDDIRLIKSCADLAVECAFRRESGVIGHDEDNGNVLRAIEFPRIKGGKPFDIDTPWFVQMLAGIGQSKGARVEVSH
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Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. {ECO:0000255|HAMAP-Rule:MF_01977, ECO:0000269|PubMed:20868748}.
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G4SW86
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ERG_META2
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Delta(14)-sterol reductase (EC 1.3.1.70) (C-14 sterol reductase) (C14SR) (MaSR1) (Sterol C14-reductase)
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MSEQESRDNAAVDAVRQKYGFGFSWLVLMIALPPLVYYLWICVTYYQGELVFTSDAAAWRRFWSHVAPPTWHAAGLYAAWFLGQAALQVWAPGPTVQGMKLPDGSRLDYRMNGIFSFLFTLAVVFGLVTMGWLDATVLYDQLGPLLTVVNIFTFVFAGFLYFWGLNGKQWERPTGRPFYDYFMGTALNPRIGSLDLKLFCEARPGMIFWLLMNLSMAAKQYELHGTVTVPMLLVVGFQSFYLIDYFIHEEAVLTTWDIKHEKFGWMLCWGDLVWLPFTYTLQAQYLVHHTHDLPVWGIIAIVALNLAGYAIFRGANIQKHHFRRDPNRIVWGKPAKYIKTKQGSLLLTSGWWGIARHMNYFGDLMIALSWCLPAAFGSPIPYFHIVYFTILLLHREKRDDAMCLAKYGEDWLQYRKKVPWRIVPKIY
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Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. Complements the deletion of the Delta(14)-sterol reductase gene ERG24 in yeast.
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G4T4R7
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AGASK_RUMGN
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Bifunctional alpha-galactosidase/sucrose kinase AgaSK [Includes: Alpha-galactosidase (EC 3.2.1.22) (Melibiase); Sucrose kinase (EC 2.7.-.-)]
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MAIIYNPNKKIFTLHTAHTTYQMQVDPLGYLLHLYYGEKTNSSMDYVLTYADRGFSGNPYAAGMDRTYSLDALPQEYPSLGTGDYRNIALNIKNEKGVESADLLFKSYEIRNGKYRLQGLPAVWADEKEAQTLEIVLADENAQVEVHLLYGVLEENDVITRSVRIKNTGTGQITIEKAAAACLDFVQGEFDVLRFYGKHAMERNLERTPLGHGTIAFGSRRGTSSHQYNPAVILAEKGTTETAGSCYGMLFVYSGNFSCEAEKDQFNQTRLLLGLNEELFSYPLASGETFTVPEVILSYSAEGLSALSQQYHNCIRNHVCRSKYVHMQRPVLINSWEAAYFDFTGDTIVDLAKEAASLGIDMVVMDDGWFGKRNDDNSSLGDWQVNETKLGGSLAELITRVHEQGMKFGIWIEPEMINEDSDLYRAHPDWAIRIQGKKPVRSRNQLLLDFSRKEVRDCVFDQICVVLDQGKIDYVKWDMNRSMADVYAGNLSYDYVLGVYDFMERLCSRYPDLLLEGCSGGGGRFDAGMLYYSPQIWCSDNTDAINRTRIQYGTSFFYPVSAMGAHVSAVPNHQTGRVTSFHTRGVTAMAGTFGYELNPALLSDEEKQQIREQIKTYKKYETLINEGTYWRLSDPFTDEIAAWMSVSEEQDHALVSVVRLMAEANQATVYVRLRGLKPDAVYLEEQSGRQYSGAALMHAGIPLPPFTEEYEAYQFAFTELKEAGRLYEKVQKWCDGNAENRVVISIYGGSGSGKTTLATALQQYFLNDGTECYLLSGDDYPHRIPKRNDEERMRVYKEAGEDGLRGYLGTKKEIDFDRINEVLAAFHEGKDSITLRHMGREDGEISLEETDFSGISVLLLEWTHGGSDDLHGVDLPVFLESSPGETRERRIRRNRDENAASPFICRVVELEQEKLEVQRKNAGLIVGKDGSVYEQ
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Bifunctional enzyme with alpha-galactosidase and sucrose kinase activities. Produces sucrose-6-phosphate directly from raffinose. Binds ATP. Phosphorylates sucrose specifically on the C6 position of glucose in the presence of ATP. Hydrolyzes melibiose, raffinose, stachyose and synthetic substrate p-nitrophenyl-alpha-D-galactopyranoside with high activity. Low activity against locust bean gum, guar gum and synthetic substrates xylose alpha-D-4-nitrophenol, glucose alpha-D-4-nitrophenol and o-nitrophenyl-alpha-D-galactopyranoside.
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G4V4G2
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SDHE_SERS3
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FAD assembly factor SdhE (Antitoxin CptB) (DUF339 protein)
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MDIDNKPRIHWACRRGMRELDISIMPFFEHDYDTLSDDDKRNFIRLLQCDDPDLFNWLMNHGEPTDQGLKHMVSLIQTRNKNRGPVAM
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An FAD assembly protein, which accelerates covalent attachment of the cofactor into other proteins. Plays an essential role in the assembly of succinate dehydrogenase (SDH, respiratory complex II), an enzyme complex that is a component of both the tricarboxylic acid cycle and the electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SdhA of SDH. Required for flavinylation of the flavoprotein subunit FdrA of fumarate reductase (FDR). Flavinylation of SDH and FDR occurs in a similar but not identical manner, as site-specific mutations display subtle differences between them. Flavinylates SdhA in vivo in the absence of the other SDH subunits SdhE mutants that do not flavinylate also interfere with wild-type activity in a possible dominant-negative fashion. Weakly binds to FAD and facilitates its binding to SdhA. Required for production of prodigiosin antibiotic (Pig) overproduction of SdhE in a deletion mutant leads to decreased synthesis of Pig compared to wild-type. Capable of flavinylating A.pasteurianus SdhA when the SDH operon and this gene are expressed in G.oxydans flavinylation of SdhA is detected only in the presence of sdhE.
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G4WJD4
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COLD_YERPU
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GDP-4-keto-6-deoxy-D-mannose 3-dehydratase (EC 4.2.1.168)
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MRKIMINFPLASSTWDEKELNAIQRIIDSNMFTMGESVKQYEKDFAEYFGSKYSVMVSSGSTANLLMIAALFFTKKPKFKRGDEVIVPAVSWSTTYFPLQQYGLNVRFVDIDKKTLNIDLDKLKSAITEKTKAILAVNLLGNPNDFDAITKITEGKDIFILEDNCESMGARLNGKQAGTYGLMGTFSSFFSHHIATMEGGCVITDDEELYHILLCIRAHGWTRNLPEFNHITGQKSIDPFEESFKFVLPGYNVRPLEMSGAIGIEQLKKLPSFIEMRRKNATIFKELFSSHPYIDIQQETGESSWFGFALILKESSPITRAELVKKLIEAGIECRPIVTGNFLKNKEVLKFFDYTIAGEVTDAEYIDKHGLFVGNHQIDLSEQIKNLFNILKK
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Involved in the biosynthesis of L-colitose, a 3,6-dideoxyhexose present in the O-antigen region of lipopolysaccharides (LPS), where it serves as an antigenic determinant and is vital for bacterial defense and survival. Catalyzes the removal of the C3'-hydroxyl group from GDP-4-keto-6-deoxy-D-mannose via a combined transamination-deoxygenation reaction. The catalysis is initiated by a transamination step in which pyridoxal 5'-phosphate (PLP) is converted to pyridoxamine 5'-phosphate (PMP) in the presence of L-glutamate. This coenzyme then forms a Schiff base with GDP-4-keto-6-deoxy-D-mannose and the resulting adduct undergoes a PMP-mediated beta-dehydration reaction to give a sugar enamine intermediate, which after tautomerization and hydrolysis to release ammonia yields GDP-4-keto-3,6-dideoxy-D-mannose as a product.
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G4YRX5
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PSR1_PHYSP
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RxLR effector protein PSR1 (Avirulence homolog protein 18) (Suppressor of RNA silencing protein 1)
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MRLTYVLLVAVTTLLVSCDATKPSTEATAVSKRLLRFVEAADEEERRIDFSPEKLRKMLGDETYRLKKFGKWDSDGHTFDGLKHYLLLSDSSMVKLRNMYKAWLEQ
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Secreted effector that possesses RNA silencing suppression activity by inhibiting the biogenesis of small RNAs in the host plant to promote enhanced susceptibility of host to the pathogen during infection. Interferes with secondary siRNA production by associating with host nuclear protein PINP1 that acts as a regulator of the accumulation of both microRNAs and endogenous small interfering RNAs.
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G4ZHR2
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XEG1_PHYSP
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Xyloglucan-specific endo-beta-1,4-glucanase 1 (EC 3.2.1.151) (Glycoside hydrolase family 12 protein XEG1) (GH12 protein XEG1)
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MKGFFAGVVAAATLAVASAGDYCGQWDWAKSTNYIVYNNLWNKNAAASGSQCTGVDKISGSTIAWHTSYTWTGGAATEVKSYSNAALVFSKKQIKNIKSIPTKMKYSYSHSSGTFVADVSYDLFTSSTASGSNEYEIMIWLAAYGGAGPISSTGKAIATVTIGSNSFKLYKGPNGSTTVFSFVATKTITNFSADLQKFLSYLTKNQGLPSSQYLITLEAGTEPFVGTNAKMTVSSFSAAVN
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Glycoside hydrolase that exhibits xyloglucanase activity. Acts as an important virulence factor during P.sojae infection but also acts as a pathogen-associated molecular pattern (PAMP) in soybean and solanaceous species, where it can trigger defense responses including cell death. XEG1-induced cell death can be suppressed by P.sojae RxLR effectors. The PAMP activity is independent of its xyloglucanase activity. XEG1 induces plant defense responses in a RLP kinase Serk3/Bak1-dependent manner in Nicotiana benthamiana. Moreover, the perception of XEG1 occurs independently of the perception of ethylene-inducing xylanase Eix2 in Tomato. With truncated paralog XLP1, is required to elevate apoplastic sugar during P.sojae infection.
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G4ZHR3
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XLP1_PHYSP
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Inactive glycoside hydrolase XLP1 (Glycoside hydrolase family 12 protein XLP1) (GH12 protein XLP1) (XEG1-like protein 1)
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MKSFLQLVVVVAALLSVSTADFCSQWRLSKAGKYVIYNNLWNKNAAASGSQCTGVDKISGSTIAWHTSYTWTGGAATEVKSYSNAALVFSKKQIKNIKSIPTKMKYSYSHSSGTFVADVSYDLFTSSTASGSNEYEIMIWLAAYGGAGPISSTGKAIATVTIGSNSFKLYKGPNGSTTVYQPPGLPLST
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Secreted XEG1-like protein that has lost enzyme activity but binds to host soybean apoplastic glucanase inhibitor protein GIP1 more tightly than does XEG1, thus it outcompetes XEG1 for GIP1 binding and frees functional XEG1 to support P.sojae infection. With XEG1, is required to elevate apoplastic sugar during P.sojae infection.
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G4ZJX4
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AVH23_PHYSP
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RxLR effector protein Avh23 (Avirulence homolog protein 23)
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MRLTYFLTVIVVATLHAGGTALATAEAPNHAAIVNVASADNVHSLDTTAEIGGRMLRKVKEDTVSKKDHEERGPGAILERQTAFVKKLFSRQNAIVNRAQGAFQRQNAFVNRDQGAFQRQNAFVKRAIQRQNHFKLSDNA
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Effector that suppresses plant defense responses during the early stages of pathogen infection. Suppresses cell death induced by effectors and PAMPs in plant hosts. Acts as a modulator of histone acetyltransferase (HAT) in plants. Avh23 binds to the ADA2 subunit of the HAT complex SAGA and disrupts its assembly by interfering with the association of ADA2 with the catalytic subunit GCN5. As such, Avh23 suppresses H3K9 acetylation mediated by the ADA2/GCN5 module and increases plant susceptibility.
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G4ZSG0
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AVH52_PHYSP
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RxLR effector protein Avh52 (Avirulence homolog protein 52)
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MRLTSILVLVIAATFHTTGTALTLTKDSKAGIANGDSPASGDFIDANSARLLRRVEKDKVDYEQDEQRSFGALKDAVKKLNPVTAVKKFFKQRAKRKKVIQTARDADNNLAWAMKEVYKAAN
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Effector that suppresses plant defense responses during the early stages of pathogen infection. Suppresses cell death induced by effectors and PAMPs in plant hosts. Interacts with host acetyltransferase TAP1 and causes TAP1 relocation into the nucleus where it acetylates histones H2A and H3 during early infection, thereby promoting susceptibility of host plant to P.sojae.
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G5AY81
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HYAS2_HETGA
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Hyaluronan synthase 2 (EC 2.4.1.212) (Hyaluronate synthase 2) (Hyaluronic acid synthase 2)
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MHCERFLCILRIIGTTLFGVSLLLGITAAYIVGYQFIQTDNYYFSFGLYGAFLASHLIIQSLFAFLEHRKMKKSLETPIKLNKTVALCIAAYQEDPDYLRKCLQSVKRLTYPGIKVVMVIDGNSDDDLYMMDIFSEVMGRDKSATYIWKNNFHEKGPGETDESHKESSQHVTQLVLSSKSVCIMQKWGGKREVMYTAFRALGRSVDYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGGDVQILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFVEDWYSQEFMGNQCSFGDDRHLTNRVLSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFREWLYNAMWFHKHHLWMTYEAVITGFFPFFLIATVIQLFYRGKIWNILLFLLTVQLVGLIKSSFASCLRGNIVMVFMSLYSVLYMSSLLPAKMFAIATINKAGWGTSGRKTIVVNFIGLIPVSVWFTILLGGVIFTIYKESKKPFSESKQTVLIVGTLLYACYWVMLLTLYVVLINKCGRRKKGQQYDMVLDV
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Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation (By similarity). This is one of three isoenzymes responsible for cellular hyaluronan synthesis and it is particularly responsible for the synthesis of high molecular mass hyaluronan (By similarity).
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G5BQH4
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APOC3_HETGA
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Apolipoprotein C-III (Apo-CIII) (ApoC-III) (Apolipoprotein C3)
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MQPRVFLAVTLLALLASARALETEDASLLGYMQDYMQGYMEHASKTAQDALTRVQDSQMAQQARGWMSDSLSSLQDYWSSFKGKWSGFGFWDATPEEASPTPAPEGI
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Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors. Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners.
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G5BQH5
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APOA1_HETGA
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Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I); Truncated apolipoprotein A-I]
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MKAVVLAVAVLFLTGSQARHFWQGDEPQTSWDRMKDFAALYVDAIQESGKDCAAQLDASALGKQLNLNLLANWNTLTSTFNNLREQLGSVTKEFWDNLGEDTVWLRQQMNKDLEEVKQKVQSYLDNFQKKVNEEVERYRDKVQPLGKELHKDAQQKLKELQEKLAPLGQDIRQRAREYVDALRTHLGSYTQGMRQGLAKRLEALKESAPVSEYQVKASKHLKTFSEKAKPALEDLRQGLMPVMESLKASFLSSIDQASKQLSAQ
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Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility (By similarity).
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G5BWH8
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APOA2_HETGA
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Apolipoprotein A-II (Apo-AII) (ApoA-II) (Apolipoprotein A2) [Cleaved into: Proapolipoprotein A-II (ProapoA-II); Truncated apolipoprotein A-II]
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MKLLAMTVLLVTICSLDGALVRRQAEEPDLQGLFSQYFQTVTSYGKDLLQKTKPQDLQAQVQSYFEKTQEQLVPLVKKAGTELFNMLSNMIELKKTQPATA
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May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism.
|
G5CV52
|
TPS17_SOLLC
|
Terpene synthase 17 (SlTPS17) ((+)-valencene synthase TPS17) (EC 4.2.3.73) ((E)-beta-farnesene synthase TPS17) (EC 4.2.3.47) ((E)-beta-ocimene synthase TPS17) (EC 4.2.3.106) ((E)-gamma-bisabolene synthase TPS17) (EC 4.2.3.-) ((Z)-beta-ocimene synthase TPS17) (EC 4.2.3.-) ((Z)-gamma-bisabolene synthase TPS17) (EC 4.2.3.-) (Alpha-bergamotene synthase TPS17) (EC 4.2.3.54, EC 4.2.3.81) (Beta-bisabolene synthase TPS17) (EC 4.2.3.-) (Beta-myrcene synthase TPS17) (EC 4.2.3.15) (Gamma-gurjunene synthase TPS17) (EC 4.2.3.-) (Gamma-terpinene synthase TPS17) (EC 4.2.3.114) (Limonene synthase TPS17) (EC 4.2.3.-) (Terpinolene synthase TPS17) (EC 4.2.3.113)
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MELCTQTVAADHEVIITRRSGSHHPTLWGDHFLAYADLRGANEGEEKQNEDLKEEVRKMLVMAPSKSLEKLELINTIQCLGLGYHFQSEIDESLSYMYTHYEEYSIGDLHAIALCFRLLRQQGYYVSCDAFKKFTNDQGNFKEELVKDVEGMLSLYEAAQFRVHGEQILDEALNFTIAQLKQILPKLSNSQLAQQITNALKYPIKDGIVRVETRKYISFYQQNQNHNEVLLNFAKLDFNILQTLHKKELSDMTRWWKKMELVNTLPYARDRLVECYFWCLGTYFEPQYSVARKMLTKISFYISIIDDTYDIYGKLDELTLFTQAIERWNIDASEQLPLYMKIIYRDLLDVYDEIEKELANENKSFLVNYSINEMKKVVRGYFQEAKWYYGKKVPTMEQYMKNGISTSAYILLTTTSWLAMGNVATKDAFDWVATEPPIVVASCYIIRLLNDLVSHEEEQKRGNAASAVECYMNEYSVTKEEAHIKIRDIIENYWKDLNEEYFKVDMIIIPRVLLMCIINLTRVAEFIYKDEDAYTFSKNNLKDVISDILVDPII
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Sesquiterpene synthase involved in the biosynthesis of volatile compounds. Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into gamma-gurjunene, (E)-beta-farnesene and (+)-valencene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into (E)-alpha-bergamotene and (Z)-gamma-bisabolene as well as beta-bisabolene, (Z)-alpha-bergamotene and (E)-gamma-bisabolene to a lower extent. Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene, (E)-beta-ocimene, limonene, terpinolene, gamma-terpinene and (Z)-beta-ocimene.
|
G5CV54
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TPS14_SOLLC
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Sesquiterpene synthase 14 (SlTPS14) (Terpene synthase 14) ((E)-gamma-bisabolene synthase TPS14) (EC 4.2.3.59) ((Z)-gamma-bisabolene synthase TPS14) (EC 4.2.3.40) (Alpha-bisabolene synthase TPS14) (EC 4.2.3.-) (Beta-bisabolene synthase TPS14) (EC 4.2.3.-)
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MATNLTLETDKEIKNMNQLSMIDTTITRPLANYHSSVWKNYFLSYTPQLTEISSQEKLELEELKEKVRQMLVETSDKSTQKLVLIDTIQRLGVAYHFDNEIKISIQNIFDEFEQNKNEDDNDLYIVALRFRLVRGQRHYMSSDVFKKFTNDDGKFKETLTKDVQGLLNLYEATHLRVHGEQILEEALSFTVTHLKSMSPKLDSSLKAQVSEALIQPIYTNVPRVVAPKYIRIYENIESHDDLLLKFVKLDFHILQKMHQRELSELTRWWKDLDHSNKYPYARDKLVECYFWATGVYFGPQYKRARRMITKLIVIITITDDLYDAYATYDELVPYTNAVERCEISAMDSISPYMRPLYQVFLDYFDEMEEELTKDGKAHYVYYAKVEMNKLIKSYLKEAEWLKNDIIPKCEEYKRNATITVANQMILITCLIVAGEFISKETFEWMINESLIAPASSLINRLKDDIIGHEHEQQREHGASFVECYVKEYRASKQEAYVEARRQIANAWKDINTDYLHATQVPTFVLQPALNLSRLVDILQEDDFTDSQNFLKDTIKLLFVDSVNSTSCG
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Sesquiterpene synthase involved in the biosynthesis of volatile compounds. Mediates the conversion of (2E,6E)-farnesyl diphosphate ((EE)-FPP) into beta-bisabolene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into alpha-bisabolene, but also smaller amounts of (Z)-gamma-bisabolene, (E)-gamma-bisabolene and nerolidol.
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G5DAC6
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XTH1_DIOKA
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Xyloglucan endotransglucosylase protein 1 (XET protein 1) (EC 2.4.1.207) (DkXTH1) (Xyloglucan endotransglucosylase/hydrolase protein 1) (XTH protein 1)
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MAFMSFINGFSTLFLVALLASSMMAAKGGNFYQDFDVTWGDHRAKIFNGGQLLSLSLDKTSGSGFRSKKEYLFGRIDMQLKLVAGNSAGTVTAYYLSSQGPTHDEIDFEFLGNLSGDPYIVHTNVFTQGKGNREQQFYLWFDPTRNFHTYSVVWNPRQIIFLIDNTPIRVFKNAESIGVPFPKNQPMRIYSSLWNADDWATRGGLVKTDWTKAPFTAYYRNFNAKTCSGACTESFGDGAWQSQELDAHSRRRLRWVQKNFMIYNYCTDLKRFPEGLPKECQRRSRFL
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Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Overexpression in Arabidopsis transgenic plants results in elevated tolerance to abiotic stress, such as salt, ABA (abscisic acid) and drought stresses, and in the production of wider leaves. Overexpression in transgenic tomato plants slows down fruit ripening and softening, and the plants produce larger fruits. Both transgenic plants have larger and more irregular cells. Moreover, the fruits of the transgenic tomato have higher density of cell wall and intercellular spaces. May provide cells with more strength and thickness to maintain structural integrity. Probably involved in cell wall assembly and synthesis in fast growing tissues and in the maintenance of firmness in mature fruits.
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G5DAC7
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XTH2_DIOKA
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Xyloglucan endotransglucosylase protein 2 (XET protein 2) (EC 2.4.1.207) (DkXTH2) (Xyloglucan endotransglucosylase/hydrolase protein 2) (XTH protein 2)
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MAMGTHFGGLWLALLCMVSATMGAVPRKPVDVPFGRNYVPTWAFDHIKYFNGGSQIQLSLDKYTGTGFQSKGSYLFGHFSMQIKMVPGDSAGTVTAFYLSSQNSEHDEIDFEFLGNRTGQPYILQTNVFTGGKGDREQRIFLWFDPTKEYHSYSVLWNLFLIIFFVDDVPIRVFKNSKDLGVRFPFDQPMKIYSSLWNADDWATRGGLEKTDWSKAPFVASYRSFHVDGCEASVNAKFCDTQGKRWWDQKEFQDLDSFQYRRLRWVRSKYTIYNYCTDRKRYPVMPPECKRDRDI
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Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Probably involved in cell wall restructuring during fruit ripening and postharvest fruit softening.
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G5DBJ0
|
CPP1_NICBE
|
Protein CHAPERONE-LIKE PROTEIN OF POR1, chloroplastic (NbCPP1)
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MATTLISKLTLSSAFLGQQFSSRGNSMRSAPAGLFLRGPRCAATDTPYGGNIPQFPRVNVWDPYKRLGISRDASEEEVWSSRNFLLNQYYNHERSAESIEAAFEKILMASFINRKKTKINLKTRLKKKVEESPPWVQNLLSFVELPPPVIILRRLFLFGFMACWSVMNSTEAGPAFQVAISFGACVYFLNDKTKSLGRAALIGFGALVAGWFCGSLLVPMIPPNLLHPTWSLELLTSLFIYVSLFLGCTFLK
|
Exhibits holdase chaperone activity involved in the stabilization of POR proteins against photooxidative stress in chloroplasts. Required for chloroplast development.
|
G5DDC2
|
ADH1B_MAIZE
|
Aminoaldehyde dehydrogenase 1b (ZmAMADH1b) (EC 1.2.1.-) (4-trimethylammoniobutyraldehyde dehydrogenase AMADH1b) (EC 1.2.1.47) (Aminobutyraldehyde dehydrogenase AMADH1b) (EC 1.2.1.19) (Betaine aldehyde dehydrogenase AMADH1b) (EC 1.2.1.8) (Gamma-guanidinobutyraldehyde dehydrogenase AMADH1b) (EC 1.2.1.54)
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MMASQAMVPLRQLFVDGEWRPPAQGRRLPVVNPTTEAHIGEIPAGTAEDVDAAVAAARAALKRNRGRDWARAPGAVRAKYLRAIAAKVIERKQELAKLEALDCGKPYDEAAWDMDDVAGCFEYFADQAEALDKRQNSPVSLPMETFKCHLRREPIGVVGLITPWNYPLLMATWKVAPALAAGCAAVLKPSELASVTCLELADICKEVGLPPGVLNIVTGLGPDAGAPLSAHPDVDKVAFTGSFETGKKIMAAAAPMVKPVTLELGGKSPIVVFDDVDIDKAVEWTLFGCFWTNGQICSATSRLLVHTKIAKEFNEKMVAWAKNIKVSDPLEEGCRLGPVVSEGQYEKIKKFILNAKSEGATILTGGVRPAHLEKGFFIEPTIITDITTSMEIWREEVFGPVLCVKEFSTEDEAIELANDTQYGLAGAVISGDRERCQRLSEEIDAGIIWVNCSQPCFCQAPWGGNKRSGFGRELGEGGIDNYLSVKQVTEYISDEPWGWYRSPSKL
|
Dehydrogenase that catalyzes the oxidation of several aminoaldehydes. Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively. Catalyzes the oxidation of 4-(trimethylamino)butanal and 4-guanidinobutanal to 4-trimethylammoniobutanoate and 4-guanidinobutanoate, respectively. Catalyzes the oxidation of betaine aldehyde to glycine betaine.
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G5E5X0
|
LIMD1_BOVIN
|
LIM domain-containing protein 1
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MDKYDDLGLEASKFIEDLNMYEASKDGLFRVDKGAGNNPEFEETRRVFATKMAKIHLQQQQQQQLLQEETLPRASRGPINGGARLGPPAHREAGGGSKLAADGAAKPPLAASTVAPGTTITVAPGQPSYPPQEQRAKLYVRGSRQGSQDCGSKESMVNSEMSAFHRPGPCEDPSCLTHGDYYDNLSLAGPKWADDPGVSPGIRLGVGSGWSGTPGSDPLLSKPSRDPHLYHQQLSAGSGRSLQSGQDGGPGGGNSEKPAGVWTTASSQRVSPGLPSAGPENGALPRSAQPRTPSFSAPLALNRPSQGSLPRTNSGVGSEVSGTMPKPTVDPQPWFQDGPKSYLSSSAPSSSPASMDHMQAGALPGLGPKPGSTDPGIGPKLSPNSLVHPVMSTLPELSCKEGASSWASDGSLGPVLPETPSSPRVRLPCQTLIPGPELGPTAAELKLEALTQRLEREMDAHPKADYFGACVKCSKGVFGAGQACQAMGNLYHDACFTCAACSRKLRGKAFYFVNGKVFCEEDFLYSGFQQSADRCFLCGHLIMDMILQALGKSYHPGCFRCVICNECLDGVPFTVDSENKIYCVRDYHKVLAPKCAACGLPILPPEGSDETIRVVSMDRDYHVECYHCEDCGLELNDEDGHRCYPLEDHLFCHSCHVKRLEKGPSPAALRQHHF
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Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation (By similarity).
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G5E829
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AT2B1_MOUSE
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Plasma membrane calcium-transporting ATPase 1 (EC 7.2.2.10) (Plasma membrane calcium ATPase isoform 1) (PMCA1) (Plasma membrane calcium pump isoform 1)
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MGDMANNSVAYSGVKNSLKEANHDGDFGITLTELRALMELRSTDALRKIQESYGDVYGICTKLKTSPNEGLSGNPADLERREAVFGKNFIPPKKPKTFLQLVWEALQDVTLIILEIAAIVSLGLSFYQPPEGDNALCGEVSVGEEEGEGETGWIEGAAILLSVVCVVLVTAFNDWSKEKQFRGLQSRIEQEQKFTVIRGGQVIQIPVADITVGDIAQVKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKSLDKDPLLLSGTHVMEGSGRMVVTAVGVNSQTGIIFTLLGAGGEEEEKKDEKKKEKKNKKQDGAIENRNKAKAQDGAAMEMQPLKSEEGGDGDEKDKKKANLPKKEKSVLQGKLTKLAVQIGKAGLLMSAITVIILVLYFVIDTFWVQKRPWLAECTPIYIQYFVKFFIIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTMNRMTVVQAYINEKHYKKVPEPEAIPPNILSYLVTGISVNCAYTSKILPPEKEGGLPRHVGNKTECALLGFLLDLKRDYQDVRNEIPEEALYKVYTFNSVRKSMSTVLKNSDGSFRIFSKGASEIILKKCFKILSANGEAKVFRPRDRDDIVKTVIEPMASEGLRTICLAFRDFPAGEPEPEWDNENDVVTGLTCIAVVGIEDPVRPEVPEAIKKCQRAGITVRMVTGDNINTARAIATKCGILHPGEDFLCLEGKDFNRRIRNEKGEIEQERIDKIWPKLRVLARSSPTDKHTLVKGIIDSTVSEQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTLASLALATEPPTESLLLRKPYGRNKPLISRTMMKNILGHAFYQLVVVFTLLFAGEKFFDIDSGRNAPLHAPPSEHYTIVFNTFVLMQLFNEINARKIHGERNVFEGIFNNAIFCTIVLGTFVVQIIIVQFGGKPFSCSELSIEQWLWSIFLGMGTLLWGQLISTIPTSRLKFLKEAGHGTQKEEIPEEELAEDVEEIDHAERELRRGQILWFRGLNRIQTQIRVVNAFRSSLYEGLEKPESRSSIHNFMTHPEFRIEDSEPHIPLIDDTDAEDDAPTKRNSSPPPSPNKNNNAVDSGIHLTIEMNKSATSSSPGSPLHSLETSL
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Catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytoplasm to the extracellular space thereby maintaining intracellular calcium homeostasis. Plays a role in blood pressure regulation through regulation of intracellular calcium concentration and nitric oxide production leading to regulation of vascular smooth muscle cells vasoconstriction. Positively regulates bone mineralization through absorption of calcium from the intestine. Plays dual roles in osteoclast differentiation and survival by regulating RANKL-induced calcium oscillations in preosteoclasts and mediating calcium extrusion in mature osteoclasts. Regulates insulin sensitivity through calcium/calmodulin signaling pathway by regulating AKT1 activation and NOS3 activation in endothelial cells (By similarity). May play a role in synaptic transmission by modulating calcium and proton dynamics at the synaptic vesicles.
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G5E870
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TRIPC_MOUSE
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E3 ubiquitin-protein ligase TRIP12 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase TRIP12) (Thyroid receptor-interacting protein 12) (TR-interacting protein 12) (TRIP-12)
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MSNRPNNNPGGSLRRSQRNTAGAQPQDDSIGGRSCSSSSAVIVPQPEDPDRANTSERQKTGQVPKKDNSRGVKRSASPDYNRTNSPSSAKKPRAFQHIESFSETNKPHSKSKKRHLDQEQQLKSAQLPSTSKAHTRKSVAAGSSRNQKRKRTESSCVKSGSGSESTGAEERSAKPIKLASKSATSAKAGCSTITDSSSAASTSSSSSAIASASSTVPAGARVKQGKDQNKARRSRSASSPSPRRSSREKEQSKTGGSSKFDWAARFSPKVSLPKTKLSLPGSSKSETSKPGPSGLQAKLASLRKSTKKRSESPPAELPSLRRSTRQKTTGSCASTSRRGSGLGKRGAAEARRQEKMADPESNQETVNSSAARTDEAPQGAAASSSVAGAVGMTTSGESESDDSEMGRLQALLEARGLPPHLFGPLGPRMSQLFHRTIGSGASSKAQQLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQMEHNFDIMNHACRALTYMMEALPRSSAVVVDAIPVFLEKLQVIQCIDVAEQALTALEMLSRRHSKAILQAGGLADCLLYLEFFSINAQRNALAIAANCCQSITPDEFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASKDLLTNVQQLLVVTPPILSSGMFIMVVRMFSLMCSNCPTLAVQLMKQNIAETLHFLLCGASNGSCQEQIDLVPRSPQELYELTSLICELMPCLPKEGIFAVDTMLKKGNAQNTDGAIWQWRDDRGLWHPYNRIDSRIIEAAHQVGEDEISLSTLGRVYTIDFNSMQQINEDTGTARAIQRKPNPLANSNTSGYSELKKDDARAQLMKEDPELAKSFIKTLFGVLYEVYSSSAGPAVRHKCLRAILRIIYFADAELLKDVLKNHAVSSHIASMLSSQDLKIVVGALQMAEILMQKLPDIFSVYFRREGVMHQVKHLAESESLLTSPPKACTNGSGSLGSTTPASSGTATAATNASADLGSPSLQHSRDDSLDLSPQGRLSDVLKRKRLPKRGPRRPKYSPPRDDDKVDNQAKSPTTTQSPKSSFLASLNPKTWGRLSAQSNSNNIEPARTAGVSGLARAASKDTISNNREKIKGWIKEQAHKFVERYFSSENMDGSNPALNVLQRLCAATEQLNLQVDGGAECLVEIRSIVSESDVSSFEIQHSGFVKQLLLYLTSKNEKDAVGREIRLKRFLHVFFSSPLPGEEPVGRVEPVGHAPLLALVHKMNNCLSQMEQFPVKVHDFPSGNGAGGSFSLNRGSQALKFFNTHQLKCQLQRHPDCANVKQWKGGPVKIDPLALVQAIERYLVVRGYGRVREDDEDSDDDGSDEEIDESLAAQFLNSGNVRHRLQFYIGEHLLPYNMTVYQAVRQFSVQAEDERESTDDESNPLGRAGIWTKTHTIWYKPVREDEESTKDCVGGKRGRAQTAPTKTSPRNAKKHDELWHDGVCPSVANPLEVYLIPTPPENITFEDPSLDVILLLRVLHAISRYWYYLYDNAMCKEIIPTSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGKTCPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPEINQSDSQDSRVAPRLDRKKRTVNREELLKQAESVMQDLGSSRAMLEIQYENEVGTGLGPTLEFYALVSQELQRADLCLWRGEEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQETSLTSHDLFDIDPVVARSVYHLEDIVRQKKRLEQDKSQTKESLQYALETLTMNGCSVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFESVFPLCHLQYFYPEELDQLLCGSKADTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDYSSIDIMRDKLLIAAREGQQSFHLS
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E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardless of the presence of lysine residues in target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Mediates ubiquitination of ASXL1: following binding to N(6)-methyladenosine methylated DNA, ASXL1 is ubiquitinated by TRIP12, leading to its degradation and subsequent inactivation of the PR-DUB complex.
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G5E8I7
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U17LC_MOUSE
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Ubiquitin carboxyl-terminal hydrolase 17-like protein C (EC 3.4.19.12) (Deubiquitinating enzyme 2)
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MVVSLSFPEADPALSSPGAQQLHQDEAQVVVELTANDKPSLSWECPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCKMCAMEAHVTQSLLHSHSGDVMKPSQILTSAFHKHQQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSAQSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSAFMGNKLDRKVSYPEFLDLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFSYVKARHGAWYKMDDTKVTSCDVTSVLNENAYVLFYVQQTDLKQVSIDMPEGRVHEVLDPEYQLKKSRRKKHKKKSPCTEDAGEPCKNREKRATKETSLGEGKVLQEKNHKKAGQKHENTKLVPQEQNHQKLGQKHRINEILPQEQNHQKAGQSLRNTEGELDLPADAIVIHLLRSTENWGRDAPDKENQPWHNADRLLTSQDPVNTGQLCRQEGRRRSKKGKNKNKQGQRLLLVC
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Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. Important for preimplantation stage embryonic development.
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G5E8K5
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ANK3_MOUSE
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Ankyrin-3 (ANK-3) (Ankyrin-G)
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MSEEPKEKPAKPAHRKRKGKKSDANASYLRAARAGHLEKALDYIKNGVDVNICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDTNADVESKSGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSAPILSKTKNGLSPLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKASPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTALHQAAQQGHTHIINVLLQNNASPNELTVNGNTALAIARRLGYISVVDTLKVVTEEIMTTTTITEKHKMNVPETMNEVLDMSDDEVRKASAPEKLSDGEYISDGEEGDKCTWFKIPKVQEVLVKSEDAITGDTDKYLGPQDLKELGDDSLPAEGYVGFSLGARSASLRSFSSDRSYTLNRSSYARDSMMIEELLVPSKEQHLTFTREFDSDSLRHYSWAADTLDNVNLVSSPVHSGFLVSFMVDARGGSMRGSRHHGMRIIIPPRKCTAPTRITCRLVKRHKLANPPPMVEGEGLASRLVEMGPAGAQFLGPVIVEIPHFGSMRGKERELIVLRSENGETWKEHQFDSKNEDLAELLNGMDEELDSPEELGTKRICRIITKDFPQYFAVVSRIKQESNQIGPEGGILSSTTVPLVQASFPEGALTKRIRVGLQAQPVPEETVKKILGNKATFSPIVTVEPRRRKFHKPITMTIPVPPPSGEGVSNGYKGDATPNLRLLCSITGGTSPAQWEDITGTTPLTFIKDCVSFTTNVSARFWLADCHQVLETVGLASQLYRELICVPYMAKFVVFAKTNDPVESSLRCFCMTDDRVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNFYSFKENRLPFSIKIRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLPAHKKAEKADRRQSFASLALRKRYSYLTEPSMSPQSPCERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLEGPIFDYGNISGTRSFADENNVFHDPVDGHPSFQVELETPMGLYCTPPNPFQQDDHFSDISSIESPFRTPSRLSDGLVPSQGNIEHPTGGPPVVTAEDTSLEDSKMDDSVTVTDPADPLDVDESQLKDLCQSECAQCWASVPGIPNDGRQAEPLRPQTRKVGMSSEQQEKGKSGPDEEVTEDKVKSLFEDIQLEEVEAEEMTEDQGQAMLNRVQRAELAMSSLAGWQNETPSGSLESPAQARRLTGGLLDRLDDSSDQARDSITSYLTGEPGKIEANGNHTAEVIPEAKAKPYFPESQNDIGKQSIKENLKPKTHGCGRTEEPVSPLTAYQKSLEETSKLVIEDAPKPCVPVGMKKMTRTTADGKARLNLQEEEGSTRSEPKQGEGYKVKTKKEIRNVEKKTH
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Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments (By similarity). In skeletal muscle, required for costamere localization of DMD and betaDAG1. Regulates KCNA1 channel activity in function of dietary Mg(2+) levels, and thereby contributes to the regulation of renal Mg(2+) reabsorption. {ECO:0000250, ECO:0000269|PubMed:19109891, ECO:0000269|PubMed:23903368}.
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G5E8P1
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BRD1_MOUSE
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Bromodomain-containing protein 1 (Bromodomain and PHD finger-containing protein 2)
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MRRKGRCHRGSAARHPSSPCSIKHSPTRETLTYAQAQRMVEIEIEGRLHRISIFDPLEIILEDDLTAQEMSECNSNKENSERPPVCLRTKRHKNNRVKKKNEVLPSTHGTPASASALPEPKVRIVEYSPPSAPRRPPVYYKFIEKSAEELDNEVEYDMDEEDYAWLEIINEKRKGDCVSAVSQNMFEFLMDRFEKESYCENQKQGEQQSLIDEDAVCCICMDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRHCLQSRARPADCVLCPNKGGAFKKTDDDRWGHVVCALWIPEVGFANTVFIEPIDGVRNIPPARWKLTCYLCKQKGVGACIQCHKANCYTAFHVTCAQKAGLYMKMEPVKELTGGSATFSVRKTAYCDVHTPPGCTRRPLNIYGDVEMKNGVCRKESSVKTVRSTSKVRKKAKKAKKTLAEPCAVLPTVCAPYIPPQRLNRIANQVAIQRKKQFVERAHSYWLLKRLSRNGAPLLRRLQSSLQSQRNTQQRENDEEMKAAKEKLKYWQRLRHDLERARLLIELLRKREKLKREQVKVEQMAMELRLTPLTVLLRSVLEQLQEKDPAKIFAQPVSLKEVPDYLDHIKHPMDFATMRKRLEAQGYKNLHAFEEDFNLIVDNCMKYNAKDTVFYRAAVRLRDQGGVVLRQARREVESIGLEEASGMHLPERPIAAPRRPFSWEEVDRLLDPANRAHMSLEEQLRELLDKLDLTCSMKSSGSRSKRAKLLKKEIALLRNKLSQQHSQAPPTGAGTGGFEDEAAPLAPDTAEEVLPRLETLLQPRKRSRSTCGDSEVEEESPGKRLDTGLTNGFGGARSEQEPGGGPGRKAAPRRRCASESSICSSNSPLCDSSFSTPKCGRGKPALVRRHTLEDRSELISCIENGNYAKAARIAAEVGQSNMWISTDAAASVLEPLKVVWAKCSGYPSYPALIIDPKMPRVPGHHNGVTIPAPPLDVLKIGEHMQTKSEEKLFLVLFFDNKRSWQWLPKSKMVPLGVDETIDKLKMMEGRNSSIRKAVRIAFDRAMNHLSRVHGEPASDLSDID
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Scaffold subunit of various histone acetyltransferase (HAT) complexes, such as the MOZ/MORF and HBO1 complexes, that acts as a regulator of hematopoiesis. Plays a key role in HBO1 complex by directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation (H3K14ac), thereby promoting erythroid differentiation.
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G5E8Q8
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AGRF5_MOUSE
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Adhesion G protein-coupled receptor F5 (G-protein coupled receptor 116)
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MRSPRTFTFYFLLLVICSSEAALSTPTEPIVQPSILQEHELAGEELLRPKRAAAAGDRVAEEYMVDIEISFENVSFLESIRAHLNNLSFPIRGTEADILNIAMTTVCTPAGNDLLCFCEKGYQWSEERCLHSLTCQDYDSALPGGYCSCLKGLPPQGPFCQLPEAFITLKLKVRLNIGFQEDLKNTSSALYRSYKTDLERAFRAGYRTLPGFRSVTVTQFTKGSVVVNYVVRVTSAPLPGSIHKANEQVIQNLNHTYKMDYNSFQGTPSNETKFTVIPEFIFEGDNVTLECETEFVTSNTSWYYGEKRSDIQNSDKYSIHTTVINNISLITRLTIYNFTQHDAGMYGCNVTLDIFEYGTVRKLDVTPIRILAKEERKVVCDNHPISLNCCSENIANWSSIEWKQEGKISILGNPESDLESSCSTYTLKADGTQCPSGSSGTTVIYTCEFVSAYGARGSKNIAVTFTSVANLTITRDPISVSEGQSFSITCLSDVSSFDEVYWNTSAGIKIHPRFYTMRRYQDGAESVLMVKTSTREWNGTYHCIFRYKNSYSIATKDVTVHPLPLVSDIMMDPLEASGLCTSSHQFKCCVEEDAGEEYAVTFHVDSSSFPAEREVIGKQACYTYSLPANLPRCPKDIAVFCHFTNAANSSVRSPSMKLKLIPRENVTCQDPIIGIGDPGKVIQKLCQFSGVYGSPGQAIGGTVTYKCVGTQWKEESRACISAPINGLLQVAKALIKSPTQDQKLPTYLRDLSVSAGKEEQDIRSSPGSLGAIISILDLLSTVPTQVNSEMMRDILATINVILDKSALNSWEKLLQQQSNQSSQFLHSVERFSQALQLGDSTPPFLAHPNVQMKSMVIKRGHPQIYQQQFIFKDSDLWGDVAIDECQLGNLQPDSSIVTVAFPTLKAILAQDVQRKTSSNSLVMTTTVSHNIVKPFRISMTFKNNHRSGGKPQCVFWNFSLANNTGGWDSSGCSVEDDGRDNRDRVFCKCNHLTSFSILMSPDSPDPGSLLKILLDIISYIGLGFSIVSLAACLVVEAMVWKSVTKNRTSYMRHICIVNIAFCLLIADIWFIVAGAIHDGRYPLNETACVAATFFIHFFYLSVFFWMLTLGLMLFYRLIFILHDASKSTQKAIAFSLGYGCPLIISSITVGVTQPQEVYMRKNACWLNWEDTRALLAFAIPALIIVVVNVSITVVVITKILRPSIGDKPGKQEKSSLFQISKSIGVLTPLLGLTWGFGLATVIQGSNAVFHIIFTLLNAFQGLFILLFGCLWDQKVQEALLHKFSLSRWSSQHSKSTSIGSSTPVFSMSSPISRRFNNLFGKTGTYNVSTPETTSSSLENSSSAYSLLN
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Receptor that plays a critical role in lung surfactant homeostasis. May play a role in controlling adipocyte function.
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G5E8Z2
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TAF4B_MOUSE
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Transcription initiation factor TFIID subunit 4B (Transcription initiation factor TFIID 105 kDa subunit) (TAF(II)105) (TAFII-105) (TAFII105)
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MPAGLTEPAGAAAPVVSSASGAVTMAPVAALPVRVEGTPVALGPVTKAPVSVCVESVAPQPLPAPVGTLVTKVVPVTALPKLGSPRLPAPQIVTVKTPGTTTIQLPANLQLPPGTVLIKSNSGQLMLVSPQQAVTGAKTTSNITPRPAVPANTQTVKICTVPNSSSQLMKKVTVAPVKNLTQIGTTVATTASSTSSGQPVALPSSVITVTPAKLVNTVSTLKSSSLGVLSTPSNDARLKAETSVAAQTALPPTVLENVKKCKNFLSMLIKLACSGSQSPEMGQNVKRLVEQLLDAEIEAEEFTRKLYIELKSAPQPHLVPFLKKSVVALRQLLPNSQSFIENCVKEVSGDVVISSCTMTTATSPVVTSTVSPVLVSGATAPRTLSVQQTLNPLAGPGVANTGVVTLHSVAPAAATGGTTAATVLLQTSKPLTTSVPNTVAAVSLQPENPVVSGAAVTLAIPSATFGEASATPLCLPSAKPAITSAGTKADKPAIGTPVQIVTQPSTLLPQAAGIPQTAKVKQLVVQQPSGSSVNHVTSISHSSPLSTQNCGQKTPVNAVMPTSSIIKQITLPGNKLLSLQAQRSSIQSNKIKENGPTCFRGEDDINDVTFMAEVNLDEENACILAAHSDFVGTLIQSCKEEPFLVIGALQKRILDIGKKHDITELNSDAVNLISHATQERLRGLLEKLTTIAQHRMTIYKGSENYILSTDTRSQLKFLEKLDQLEKQRKDLEEREMLLKAAKSRSNKEDPEQLRLKQKAKELQQLELAQIQYRDANLTALAAIGPRKKRPLESGNESFKDNPSTSGTSSLTATKPFRPRITRICLRDLIFCMEQEREMKYSRALYLALLK
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Cell type-specific subunit of the general transcription factor TFIID that may function as a gene-selective coactivator in certain cells. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators asond repressors. TAF4B is a transcriptional coactivator of the p65/RELA NF-kappa-B subunit. Involved in the activation of a subset of antiapoptotic genes including TNFAIP3. Through interaction with OCBA/POU2AF1, acts as a coactivator of B-cell-specific transcription. Plays a role in spermiogenesis and oogenesis.
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G5EB19
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PPOA_EMENI
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Psi-producing oxygenase A (Fatty acid oxygenase ppoA) [Includes: Linoleate 8R-lipoxygenase (EC 1.13.11.60); 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase (EC 5.4.4.5)]
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MGEDKETNILAGLGNTISQVENVVAASLRPLPTATGDGTYVAESTQTGLAKDLSHVDLKDVRTLAEVVKSAATGEPVDDKQYIMERVIQLAAGLPSTSRNAAELTKSFLNMLWNDLEHPPVSYLGADSMHRKADGSGNNRFWPQLGAAGSAYARSVRPKTMQSPSLPDPETIFDCLLRRKEYREHPNKISSVLFYLASIIIHDLFQTDPKDNSVSKTSSYLDLSPLYGNNQDEQNLVRTFKDGKLKPDCFATKRVLGFPPGVGVLLIMFNRFHNYVVDQLAAINECGRFTKPDESNVDEYAKYDNNLFQTGRLVTCGLYANIILKDYVRTILNINRTDSTWSLDPRMEMKDGLLGEAAAMATGNQVSAEFNVVYRWHACISKRDEKWTEDFHREIMPGVDPSTLSMQDFVAGLGRWQAGLPQEPLERPFSGLQRKPDGAFNDDDLVNLFEKSVEDCAGAFGASHVPAIFKSVEALGIMQARRWNLGTLNEFRQYFNLAPHKTFEDINSDPYIADQLKRLYDHPDLVEIYPGVVVEEAKDSMVPGSGLCTNFTISRAILSDAVALVRGDRFYTVDYTPKHLTNWAYNEIQPNNAVDQGQVFYKLVLRAFPNHFDGNSIYAHFPLVVPSENEKILKSLGVAEKYSWEKPSRISHPIFISSHAACMSILENQETFKVTWGRKIEFLMQRDKHQYGKDFMLSGDRPPNAASRKMMGSALYRDEWEAEVKNFYEQTTLKLLHKNSYKLAGVNQVDIVRDVANLAQVHFCSSVFSLPLKTDSNPRGIFAESELYKIMAAVFTAIFYDADIGKSFELNQAARTVTQQLGQLTMANVEIIAKTGLIANLVNRLHRRDVLSEYGIHMIQRLLDSGLPATEIVWTHILPTAGGMVANQAQLFSQCLDYYLSEEGSGHLPEINRLAKENTPEADELLTRYFMEGARLRSSVALPRVAAQPTVVEDNGEKLTIKAGQVVMCNLVSACMDPTAFPDPEKVKLDRDMNLYAHFGFGPHKCLGLDLCKTGLSTMLKVLGRLDNLRRAPGAQGQLKKLSGPGGIAKYMNEDQSGFTPFPSTMKIQWDGELPQLKEDF
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Bifunctional heme-containing enzyme that oxidizes linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (within the N-terminal heme peroxidase domain), which is subsequently isomerized to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (within the C-terminal P450 heme thiolate domain). Oxidized unsaturated fatty acids, so-called oxylipins, derived from endogenous fatty acids, influence the development of the asexual conidiophores and sexual cleistothecia and regulate the secondary metabolism. These substances were collectively named psi factors and are primarily a mixture of hydroxylated oleic, linoleic and alpha-linolenic acids. They are termed psi-beta, psi-alpha, and psi-gamma, respectively (By similarity).
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G5EB30
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CHIA1_EMENI
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Endochitinase A (EC 3.2.1.14) (Chitinase A)
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MAPKLFTFVSALSGLASLASAFHAEAKSNIAVYYGQGVNQPRLAEFCAETSYDIINIGFINSFPEQNPLTGLPGSDFGNQCWADTFVVDGIASQLYSHCPNIAEDIPKCQAAGKKVFLSLGGATPTYWFDTIDASTKLADFLWGAFGPVTDAWTVADKPRPFGNAVVDGFDFDIEFFGSKGYANMIKRFRRRFGEVPDQTFYISAAPQCSIPDEQLSVAIKNAVIDFVWVQFYNTPGCSARDFVLGTKNGFNYDSWVEVIKAGANPNAKLYVGLPASGAAANLGYYLTPEEVKPLVKKYMDKYPETFGGVMLWEATQARNNQIDGVGYNEKIREILYDLDPNHPPPTTSPTPTPTPSTTTTSTTSTTSTTSATSTTSTTSTTSTTSTTPTTSTTSTTSTTTPTPSPSPSTASSSTTETVTPSPKPSPSESSTTSETSSLPSTSTPVVSETPSETKTPTSSSAPPLSSSSPVGGSSSTASSSTSTPSETPSASSTRAVSETSTHISTSTSSGPETSLTGSSTSVPATSSSVPSSAISPSSTPVISETPRPPVTSSSSSTFVSSTSTSTDCSESSTAIGTHSSSSISETPSASTPAASPSTSPETTKTLTVFPTPGSSVSTGTTSASTLSSSVPATSGGHTETSTVSTSSANQTPSASTSKPLIPTNSASSTSTGSVTSTPSAPGVPSSSAGSDETATTSTTDSEPTSTSSGSVTAKPTTTEPATTTTIIVTSYTSICPTGFTTITTTITSTYCPGTASATATAIAPTTDVPGSGSGSSPAQPTITADIPEGWTTTVTVCTVCAATPTTVTLTLPPATTTEESTSAQPTGEVPSSDGSGSGEVSTTTVVVVPAPTGNAGDGVPAPGANVGEEYTAAPGSATTSKPLIGGGASGAHTAYPYASSTFHIIPSASAHVPVPSGSGSSPSGTQGGASPTFTGAGSRYDVVKGVPALVALALSLLAVL
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GPI-anchored chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation.
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G5EB37
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CHMU_EMENI
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Chorismate mutase (CM) (EC 5.4.99.5) (AnCM)
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MDTAIDLSDASKALDLANIRFQLIRLEDTITFHLIERVQFPLNKTIYIPGGVKIPNEQISLMDYLLRETERLQSRVRRYQSPDEYPFFPSALEKPILQPLDYPKILHDNDVNVNETIKTRYVQDILPAICPQFGGREDRGETQENYGSAATCDVSCLQALSRRIHFGKFVAESKFQKETEKFVALIKAGDRKEIDEAITDAKVEQKVLERLALKAKTYGTDPGFPEQSGPKIDVQAVQDMYKEYVIPLTKVVEVEYLMQRLKGTQWE
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Catalyzes the Claisen rearrangement of chorismate to prephenate. Acts at the first branch point in the aromatic amino acid pathway where it steers biosynthesis towards phenylalanine and tyrosine, and away from tryptophan (By similarity).
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G5EB89
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KAPA_EMENI
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Importin subunit alpha (Karyopherin alpha)
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MAERYIPEHRRTQYKARNQFRPDELRRRREEQQVEIRKQKREENLAKRRGIQTRDGGIGVGGGMAAAESDDEASAIESELNVELPEMVKGVFSDQIEAQIQATTKFRKLLSKERNPPIERVIETGVVSRFVEFLRSPHTLVQFEAAWALTNIASGSAQQTQVVIEAGAVPIFVELLSSPEPDVREQAVWALGNIAGDSPQCRDFVLNAGALRPLLTLINDGRKISMLRNATWTLSNFCRGKTPQPDWNTIAPALPVLAKLIYMLDDEVLIDACWAISYLSDGPNEKIQAVIEAGIPRRLVELLMHASTSVQTPALRSVGNIVTGDDVQTQVIINCGALPALLSLLSSTKDGIRKEACWTISNITAGNSSQIQSVIDAGIIPPLVHLLANGDFKTRKEACWAISNATSGGLQKPDQIRYLVTQGCIKPLCDLLACPDNKIIQVALDGLENILKVGEMDKEAGQGDAHVNRYALFIEEAGGMEKIHDCQNNANEEIYMKAYNIIEKYFSDEDEAAGDIDELAPQQTQTGFTLGATQQQPGGFSFGGANGGDSMDM
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Import of proteins with classical NLS composed of one or two clusters of basic residues is initiated by binding to the importin alpha/beta heterodimer, where importin alpha acts as an adapter subunit to bridge NLS cargos to importin beta, which transports the whole complex through the nuclear envelope. Involved in the nuclear accumulation of the light-dependent developmental regulator veA. Participates at different regulatory stages of asexual and sexual development, being required for the completion of both reproductive cycles with the formation of conidiospores and ascospores, respectively. Mediates secondary metabolite gene expression with positive regulation of penicillin production and negative regulation of mycotoxin biosynthesis.
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G5EBF1
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SAX3_CAEEL
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Protein sax-3 (Sensory axon guidance 3)
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MFNRKTLLCTILLVLQAVIRSFCEDASNLAPVIIEHPIDVVVSRGSPATLNCGAKPSTAKITWYKDGQPVITNKEQVNSHRIVLDTGSLFLLKVNSGKNGKDSDAGAYYCVASNEHGEVKSNEGSLKLAMLREDFRVRPRTVQALGGEMAVLECSPPRGFPEPVVSWRKDDKELRIQDMPRYTLHSDGNLIIDPVDRSDSGTYQCVANNMVGERVSNPARLSVFEKPKFEQEPKDMTVDVGAAVLFDCRVTGDPQPQITWKRKNEPMPVTRAYIAKDNRGLRIERVQPSDEGEYVCYARNPAGTLEASAHLRVQAPPSFQTKPADQSVPAGGTATFECTLVGQPSPAYFWSKEGQQDLLFPSYVSADGRTKVSPTGTLTIEEVRQVDEGAYVCAGMNSAGSSLSKAALKVTTKAVTGNTPAKPPPTIEHGHQNQTLMVGSSAILPCQASGKPTPGISWLRDGLPIDITDSRISQHSTGSLHIADLKKPDTGVYTCIAKNEDGESTWSASLTVEDHTSNAQFVRMPDPSNFPSSPTQPIIVNVTDTEVELHWNAPSTSGAGPITGYIIQYYSPDLGQTWFNIPDYVASTEYRIKGLKPSHSYMFVIRAENEKGIGTPSVSSALVTTSKPAAQVALSDKNKMDMAIAEKRLTSEQLIKLEEVKTINSTAVRLFWKKRKLEELIDGYYIKWRGPPRTNDNQYVNVTSPSTENYVVSNLMPFTNYEFFVIPYHSGVHSIHGAPSNSMDVLTAEAPPSLPPEDVRIRMLNLTTLRISWKAPKADGINGILKGFQIVIVGQAPNNNRNITTNERAASVTLFHLVTGMTYKIRVAARSNGGVGVSHGTSEVIMNQDTLEKHLAAQQENESFLYGLINKSHVPVIVIVAILIIFVVIIIAYCYWRNSRNSDGKDRSFIKINDGSVHMASNNLWDVAQNPNQNPMYNTAGRMTMNNRNGQALYSLTPNAQDFFNNCDDYSGTMHRPGSEHHYHYAQLTGGPGNAMSTFYGNQYHDDPSPYATTTLVLSNQQPAWLNDKMLRAPAMPTNPVPPEPPARYADHTAGRRSRSSRASDGRGTLNGGLHHRTSGSQRSDSPPHTDVSYVQLHSSDGTGSSKERTGERRTPPNKTLMDFIPPPPSNPPPPGGHVYDDIFQTATRRQLNRGSTPREDTYDSVSDGAFARVDVNARPTSRNRNLGGRPLKGKRDDDSQRSSLMMDDDGGSSEADGENSEGDVPRGGVRKAVPRMGISASTLAHSCYGTNGTAQRFRSIPRNNGIVTQEQT
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Required to confine migrating sex myoblasts to the ventral muscle quadrants during their migration through the body and for multiple aspects of sensory, motor, and interneuron axon guidance.
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G5EBH0
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PLCB_CAEEL
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1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta egl-8 (EC 3.1.4.11) (Egg-laying defective protein 8) (Phosphoinositide phospholipase C-beta egl-8) (Phospholipase C-beta egl-8) (PLC-beta egl-8)
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MAKEFQFNWKPTIIPELLHGSVFDRYDDESTCLELNAQVRIDENGFFLRWLIEGKDAVVLDMGQIWEARTGGLPKDGRIMFELEQRGASETIAERTIWITHGQDLVNVQSFFLVAESVELAKTCRAGINDILKSSRIRHVCPTTQLMKYHTWLTMNVNERRKIPIKLIIKTFSSGKPEKMVQKCLNDLGLGGDKYTPARVINRSMGKKFRNFYKCSRGRKRKEREELDVDILTFEKFQRLYNKICPRTEVQELFVKLSGQKEYLTKERLINFLNEEQRDPRLNEILFPFFDSQRIVALLKKHENDIKYQEDGKMSGDGFLRFLMSDENPPVFLDRIEMFMDMDQPLCHYYINSSHNTYLTGRQYGGKSSSEIYRQVLLSGCRCIELDCWDGTGENKGEPIITHGKAMCTDVFFKDVLVQIRDTAFARSDFPVVLSFENHCSKSNQLKMAKYCMDIFGDMLLSKPFEDAPLDPGVSLPSPNRLRKKILIKNKRLKTDIERHQLDQFLREGKLDEEDELNETPEVVGEDSVSPRSGGSGGTGAPEEVDDDTSDDDDDPSVQTSLNVMRTIPTVNTTSNNGSNRSARSSLDTPSPSGGSLMVPDRATSTATSIKNAVLARSPNFSSLRQKLSFKRRQSPLAGDQRAHPEVEQPVSSSSPATPSISGPPPCATSSGSTSSITITTTGCSTSSSGPSKHILGGEMPAKENDEAHPELKQNFIAKNLKGFGFSKKQPVLTKEEEERIFAEYHYTGATTNIHPLLSSLVNYTHPVKFSGFDVAEANNLHFHMSSFSESTGLGYLKQSAPEFVNYNKRQSSRIYPKGARVDSSNFLPQIFWNAGCQMVSLNFQTPDVYMQLNMGKFEYNGGSGYLLKPDFLRRPDRTFDPFSESPVDGVIAAHCSVRVISGQFLSDRKIGTYVEVEMYGLPTDTIRKEHKTKVIPGNGLNPVYNEDPFVFRKVVLPELAVLRFAVYDENGKQLGQRILPLDGLQAGYRHISLRSDTNQSFILSPVLFVQIVIKTYVPDELSGLVDALADPRAFLSEQKKRQEALAHMGVDDSDIPDVPNTRNMALRHVKQPPRQNGSSADLLANNGQTGSARGDQTSSMASSTIRSPNEQPQPVAVDKFKVDPIEVDDLRRDKAFAKLLKRFQKELDDLRKKHQKQRDSIQKQQPARRRNSSIAWIQTNVDKLITNNRRSTKKEKGSRRSLTASVSSGCGSASGTVTVSVCSPSGASCSGYSTGGPSTPVACNSDGTGSPATIGSPVPQDLVNNDRVRSLVNTQTGEWSAMVRRHDEEEFELKKVQLKEQFDLLRKLMSEAQKNQMLALKLRLEAEGKDLKQTQTKKSMEDAKVIQLDKGIKTKAERDRRVKELNEKNLKMFVEERKRLAMKAQKHEEQLTKRHLDQLEQLDKDFHKALDAEVGNYKEEQLAAQPTSVV
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Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) which plays an important role in the regulation of intracellular signaling cascades (By similarity). Required in the nervous system to modulate neuronal activity. Facilitates synaptic transmission at neuromuscular junctions by regulating the release of acetylcholine from the motor neurons and thus affecting locomotion. Plays a role in efficient egg laying and defecation. Involved in axon regeneration after injury. Plays a role in male mating behavior by regulating spicule insertion and sperm transfer. By triggering Ca(2+) transient via IP3-mediated activation of IPR3 receptor itr-1 in ASH sensory neurons, regulates avoidance behavior in response to nose touch. By activating tpa-1 via DAG production, required for the expression of antimicrobial peptide nlp-29 in response to fungal infection. During embryogenesis, may play a role in epidermal morphogenesis together with plc-1.
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G5EBH1
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TAT5_CAEEL
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Probable phospholipid-transporting ATPase tat-5 (EC 7.6.2.1)
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MGKRKKNDESSSSSSQKPCVSSSSDDFSVSFVRAEEDDVATTIRDKTASLKSNATHFSAASAAKGGMFDFRCCRSLFSRRRVLHSRTVRVGYGPVGHDANVTFTPNTVCNQKYNIFSFVPIVLFQQFKFFLNLYFLLMACSQFIPAIQIGAPITYWGPLGFVLTITLIREAFDDFVRYLRDRDLNSEKYEKLTRDGTRIEIRSADIEVGDVIIMHKDRRVPADVVLLRTTDKSGACFIRTDQLDGETDWKLRIPVPHTQHLPNEADIMELNCEVYAEKPQKDIHAFVGTLKITDDDNVQDGSLNVENVLWANTVVASGTAVGIVVYTGRETRSVMNTTLPESKVGLLDLEVNNLTKLLFCFVLVLSSVMVAMKGLDNLWYRYLMRFILLFSYIIPISLRVNLDMAKLFYSWQIGRDKHIPETVIRSSTIPEELGRISFLLSDKTGTLTKNEMHFKKIHLGTVAFSSDAFEEVGQHVRSAYAGRLAKHSFSAKLQNAVEAIALCHNVTPIFENGEISYQAASPDEVALVKWTETVGVRLASRDLHAMSLSVQLPNGQTLMKQFQILYVFPFTSETKRMGIIVKDETTDEVTLLMKGADTVMSGMVQYNDWLDEECSNMAREGLRTLVVARKPLSQAELEAFDRAYHAAKMSISDRSQNMANVVNRMLERDLQLLCLTGVEDRLQDQVTTSLELLRNAGIKIWMLTGDKLETAICIAKSSGLFSRSDNIHVFGNVHNRTDAHNELNNLRRKTDVALVMPGSALNVCLQYYEAEVAELVCACTAVVCCRCSPEQKAQIVQLLRKYRAPLRVAAIGDGGNDVSMIQAAHAGIGIDANEGKQASLAADFSITQFSHVCRLLLVHGRFCYKRSCALSQFVMHRGLIISTMQAIFSCVFYFASVSLYQGVLMVAYSTCYTMLPVFSLVVDRDVTATNALTYPELYKELGKGRSLSYKTFCIWVLISLYQGAVIMYGALLVFDADFIHVVSISFSALIVTELIMVAMTVHTWHWAMLLAQALSLGLYMISLILFDQYFDRQFVLSWVFISKTTAITAVSCLPLYIVKALRRKFSPPSYAKVN
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Plays a role in regulating membrane trafficking of cargo proteins during embryogenesis. Regulates snx-3 retromer-mediated endosomal sorting of mig-14, a transporter of Wnt egl-20 morphogen. Together with mon-2 and pad-1, may participate in the formation of endosomal carriers that direct mig-14 trafficking back to Golgi, away from lysosomal degradation. Required for Wnt egl-20 gradient formation along the anteroposterior body axis and migration of QL neuroblast descendants toward the posterior part. Maintains phosphatidylethanolamine (PE) asymmetry at the cell membrane and prevents the budding of ectosome vesicles that affect intercellular communication and morphogenesis.
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G5EBI4
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CEEH1_CAEEL
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Epoxide hydrolase 1 (EC 3.3.2.10) (CEEH1)
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MLFESIYIQCLNKFSKYKKFVCHTTCNCPNYKIIGYLLYFLCLCRPINCSLPLSRHDLAFGSFSYYLTMFLYRILVRLLQFYYFVKFSAILFLGFAVKGRSLFEKKQREKPNVLEGWDSRYIKLKKVRLHYVQTGSDDKPLMLFIHGYPEFWYSWRFQLKEFADKYRCVAIDQRGYNLSDKPKHVDNYSIDELTGDIRDVIEGLGYDKAIVVAHDWGGLVAWQFAEQYPEMVDKLICCNIPRPGSFRKRIYTSWSQFRKSWYMFFYQNEKIPEMLCSADDMKMLELCFRAKEIGIQNNKNFTDEDLEAWKYSFSMNGASFKYPINYYRNIFNAKKQQADLVLEMPTLIIWGTADGALDIEAAVDSLNTLKQGTMKKIEGASHWVQQDEPEMVNEHIKKFLNKYQ
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Catalyzes the hydrolysis of epoxide-containing fatty acids. Active against epoxyeicosatrienoic acids (EETs) including 8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate (8,9-EET), 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate (11,12-EET) and 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate (14,15-EET) and the linoleic acid metabolites 12,13-epoxy-(9Z)-octadecenoate (12,13-EpOME) and 9,10-epoxy-(12Z)-octadecenoate (9,10-EpOME). These epoxides function as lipid signaling molecules, the enzyme can deplete the supply of the epoxide signal by transforming them into diol species that are more readily eliminated through excretion.
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G5EBK1
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PBO4_CAEEL
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Na(+)/H(+) exchanger protein 7 (Na(+)/H(+) antiporter nhx-7) (PBoc defective protein pbo-4)
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MWIKLLFFFTTLLVSTSGLGDDGITALLDPNSTEFSTVLPSNNSEKFSYMLASVKNMNMTASEFEEFIKVLKHRQSKDHSGEHVGNEHDESHGISVVSWHWDYVKNELVLTLFFIVIGLFKLVYHHTFVTRKILPESCCLIFIGIAIGFFFVGDATHASIKFLEFKSKVFFFYLLPPIILESAYSLKDRAFIENIGTILLYAVVGTILNIVLLAAALLILIWVGIMGKYNLSVMDILTFASLVAAVDPVAVLAVFQEVGVNKMLYFMVFGESLFNDAVTIVCYNLAIEFQTLPDFTWYHGFLGLLSFLCVSIGGLIIGLICGAISSFVTKFTTDVRVVEPVVLFGMAYLAYLGSEMFHFSGIIALIACGLFQTHYACCNISYKSFTSVMYITKVCSTLCESLIFIILGVMLVNEREWFWTDWHPVFSAVSVVLCVVVRFGVTFFLTYFVNQFTGGVRHISFQEQFIMSYGGLRGAVSFSLVFMISANPDVKNTMLGATYAVILFTNIIQGSTIKLFVKWLNIRLAKKEDHFRLFIEFNNGMVQHLSQGIEDLCGDKSLSLINRMSELSKKYVRPLLEKNYTANKAKKEGKLVELNRAVAMREALNNSPSQSSFQRQHTIDEMAESGALPHDLLDEEHQGHHHHGQVHPDNEDADQRANELIKDVSSIRQLMHNPFEDCYLDRNLTHEEEKEQARLKMKKTRAFKFSSVRKTIGFFGKKKSVRRHATQQGILHSAIATIGVQSVDRPSTSTRVSVEDEEQGLTMKEMEEEHPLMTITESEETSF
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Na+/H+ exchanger which mediates the transient acidification of the coelomic space and plays a role in contraction of posterior body muscles during defecation. Probably by regulating the defecation motor program, required for fatty acid uptake by intestinal cells.
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G5EBL2
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MES1_CAEEL
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Protein mes-1 (Maternal-effect sterile protein 1)
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MKIHHFLTLLCTFLPLTTTALTNSTPLSLLGPCYKRCVTKFGETKEQLTNAETISLEYDVSNNTEFSLCKLGCNSHEYTDLNLAAFRYGQLAYQKILTTVEDVPTRGTVLNDVFIVCLDTSFMPSNNSAPSAKRLLSGTVLLVLDEDVAKADNVFLIEVLARNADKSAVQVISQQWCYSSNCNITFNAPTEVSSFDVRLRVSTFDSNGQVGGINFSKWHNINQILTKTFVDMSLKSVVWKAEKAAANFVFNLTASDHVPACSLQMIYRSSLSSELLHRNFYLDHTLEVFVNNLDFDKIYTMQLAPSGTHDRSTPSLASAVIEIPPCRHLVDDYSMCAPPPVSSLSYNWNLSPTSEYELLIKWKLLNYMDGLNVTEELSIPVAYFLLNAHPLITANNEQCEKYEKIRRVVSYGLRELVFHVPDTDCNYEVEMTAVDTNQRISEVKKIQVFRFNVPPYVSFLQASDIPTSVELMAVVLATSAIFALIALFLLYRKRKRDKKARFQMYKDAEAGVSYDYVATTESLGSVVQIRSTNFRFEPVENIDGNIEAALAQQQKFEGGTMNSMFRTYYNLDHPVKVPAHMAEASSDEDNGYENIRYSYFGSELSDDVFEEDIYMTHKSLSIYCQDSPLTTPMAPIAPYEHFDDIPSHQYRNFQVHNFNERIEKQAYWLMATVVDVVRRELYSLKVPKDYTPETISAMRKELEFLRTLAPHGNCRRFEGVVIGRWDDLPRQVIGILIENTRGGTLRNYIAAVGSVFRNCSLATDHDSFASQQDMNSTQHPFDKLSTEADENNSKKVKIQEITDSLSIRFCQFAEQVSSALEHLHSAGSVHTRVTTLNIYLLHNYSDPFDMLPDQVVKLGNFGFAVQNSEDVVLDDNLQPPEVIKGEKYEARGDIWQFGLCLAEMCSLGDLEQSEVGTLKSGHDTFKNLPSTQVLRDAAKRCLSARTRPSASDLCGVFKSVNVAATV
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During early embryogenesis, controls asymmetric cell division and the asymmetric localization of P granules of germline precursor P2 and its descendant P3. Probably upstream of tyrosine kinase src-1, plays a role in endoderm development by controlling spindle orientation during EMS blastomere cell division. Controls EMS spindle orientation probably by promoting lin-5 and gpr-1/2 enrichment at, and let-99 exclusion from the junction between P2 and EMS cells.
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G5EBL3
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SDC2_CAEEL
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Sex determination and dosage compensation protein sdc-2
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MSDESELGNQSEMESFNESDSPDEADPDVVIIHDIVHLRASTTGDYSQSEIGKLPEQNTFFLPGRVKRNISSNDSDVIIDEDEIPDGAIRITSDTHFIGSSRGTSELGDFEMDEQEFLNITIEENGNEQELEEHLRNAYRHEEEECFEEEDDIIELPPLPVKPAVKKPRRKLPKHLSIESGSTAKTSKLVAEVVHDHPRPVNYRMKPAVTDDGKVVEQKRTRVTRNIMSHTIPQYHLEGEETEFGRVKESTLSKTIEQYLQAGKLVSPKCDQFREQIVATAVEYDGSVKMLQFENALKKHSGKQKRLKYQTGWWKASKSHYERAVNGYVAMPKTPVLSISDDPVLYKHHSLFPKNQSSELEKINVQLRIRLNSKRQNNDVIPDSSYFVREFLMQKHSISLRMNRSSDLPELFVPPTLECGYFPQDAVTVQQQEHYLMMRFEEAQDEYHNITYRSIAPPVEFQVGTISAKELHKFHRIGRHIHGFFVVWENKFPEYDESGICCPRKRYLVDMFNLICFPLYTEYEQWESRLRVAFDKTIVYNLHLSEILRCNRPVFDFLSKNKSMLQPITLKEIVYLIEQSNMDAKSFAVKFGLRTFYDHGRATSNKDYLSAFLIITGGAKVVTEEIDSERLRVFNSDYMESGVLTSSGDVYTFEFDKIPNNYQISIGCNADGVAEMEQEDVRHELSECSSRITRIIGDSKKPEKIIARPLVKTNQNDGMKFFTRKDLLNYRIKLYDPSYVVPRAKKQIVNEPAKKKPGRKSKTRYDAAMQQNNFEIEGVPSDVDSEFEGYLSDSENVFQKPSKLMRSTSSDSVFIDYQYREKMFLDVSWFHQQKMIDRSLPPLKKRKRKMNRIYHKHSVRYTMLQANGCAFTEMYRCYDKILPCGTKEIARTKNAIRFPHRFRTYNIPQVYGPGDKQLITEVFGVVKDVITRATGFESASIRTANDIAQAVYDANIARRELLENLEPSDNGILPSPAYLAIEMLSHQKMSGRLCLESARKDVQNNVDKMYNDYMDLDPLDKELHFEISQSIRQSKLNESLEEYERNRERQLAKTLKTVPMDKRSQAALARREEKRRESRRKLADKYAEQRRMMASTRRLEKRTTQKQVDPETIQRLRREDEVRKRKRFEEEDRRGMIRRREERVALQEKVDRMLEEGLRLEKVREAERIRQQQEEERIEMETILISRRVREEEEEKMRLERLRKAEREREQERLKREEEEERKRLEQLREAEKLKAEIEKENERKLQEERTRKALELERKIEEIKRVSTLKDMFGPLPIAKENEQTEKDFQILLDDHELTLLTISRDPLNEKYQEARTEFERLDIKSMLLRKAEKLIDVLTIHYDVPIEQTCRYFTSSIESNENRMAVNEQLNKLFENMANCFTFNIQDGENGLQSKRKWDFQFKKCAVFDGVSQSTVNFIEEKMRENTKKKHLATPKTVISIDTSLLKQSLLRSHARFDPDISLYAQNHTANSIGDVTLKMSNYSLDFATQSIHDKELAEKATPKKGPTVRRHIKNLFGSEKVIVRRSLAAGKPASLNSEDSDSEDSREGSPVAEFLPTNPVCSFWKLVVKIENSTTDKEKTELCEDLDKLILRKDDLFSKSLKWMFPLLATFYVLLSNAVLNENEEIISDKNQTGVTKDEILKSTINDLMIIAAYFEEGSRERSNLRKMISMNGFSVVFNRVILFAKKTCTLAKELESNSRSLSGYVIEDLFESLLAEIERTMRQELGSSVRKTGKLERDFEEIVKLIQNEKKLALSHKSHKNDENRRFRLNTVVKWYDAIICHCKEELTQAIVDAFPLNAITKNKETSHVAMENGDDEAMLSDTSDNQMSTTDYQMPKNICRNSEIFPEDAFAKAYAVVRIPSKKERAQMLSVYRKKNAQSGCVENKGLSRMPKFEEPFVDSVWRTIEKRINNMTHSEEKQIKRFIPVSRSHKLNEKVKFYAMVMIQERDSRDTRLFNSKFQDDNLWHCYSKSSLNHEKMESRILQHIEHTVLSKSNFNQMKWSVQCVNGNKKDAIHYFTDLYKYRSESEFRSALSCGKLKFNFKVYTHLWFMGNLLPTSYNPDSHDDKLFVPCSGCTSGDVIIIHKCTCAYHNDTFSDKFIYANTSLPVGIDKVTRLVGRFVCEHGPSSFLILEHCSANVDANIPFESENVEFSAELRIVKRKTMHSQLVKTFAEEHTHLRDASRHRAISTVTLDSSGSGRSTRCEIFEDSPSEDENDENQLDTTRIGRKIDPIIVDSDKAYLIAEGERMALRIKRLLDPELQKFRSKNFVSRSKSVDAPKTSKQKTVIRRSQSVCDLNDVNEYAQKKVRNTKDSFATLFRDHEYSTRRTYEEQLNNELLDVVTTFGGASNVSADKKYNILASILAFEKEVQLVNDKNGELFKTVSNLVQRNSLQHVKGVILAEDNQTLRSTDNTSEVFPESKAVNEYLKFEIYKRKMMVNAKLMADTVKDLKLKHAEYRPFAKLIATYDSIFKFNVYLFEHFLNCISKHVFNPYAIYCEETRPTGTELSKFQLTLKLIETSMPTVLSMLFNTEPLRRQLSELSEIHKKVRSEDLACTIASLCRYAIERIRIPQTADKRLCDFSWLNSAEDHRETVSFIRLTLEHTLPDMKTENEQTRFVEFLKEAEGFHFSYKFVEAQCKTFVRNHGDSKQAFFTAFYNQNEAFYGSLQKFMSNGTIDPKMKLYYQHQAFLRLHNIVKKRSHIITSDDYHRSSDVCKAMLLSEIVSNPKIAQEAYISGSVLDRMYTSLCKIKAKMPLISPSYIGTSLTCFEDELLFSAVREAKVHTDTRVVFRSKSCMRPNEKAGDANFKTCKVTLLVNLETALLSMVFKSRDQSEIDKDDRLDIDILDEEVIKPIIDWNRIFETFIQPTYNTLFSRMEKRERVSILPENPLGRLENYAFTNPNQDKDCQAVLEYIDVASDTDAEESIEDPLDIVEMTLKRALPRSMSPSSKRRRMR
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Component of the SDC complex that functions in sex determination and in X chromosome dosage compensation specifically in hermaphrodite (XX) animals. Required for the recruitment of the condensin I-like dosage compensation complex to the male sex-determining autosomal gene her-1, thereby contributing to its repression and initiating hermaphrodite sexual development. Plays a central role in X-chromosome recognition and in the recruitment and assembly of the dosage compensation complex and the dosage compensation protein dpy-21 onto the X chromosomes in hermaphrodites, which leads to a reduction of X-linked gene transcription and an equalization of X-linked gene expression between the sexes. May confer protection against toxicity induced by heavy metals such as arsenite.
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G5EBM1
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CSP1_CAEEL
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Caspase A (EC 3.4.22.36) [Cleaved into: Caspase A subunit p16; Caspase A subunit p14]
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MVLKTIEDNCKSQFDDDLVEDFNNFQTTSSMSSSTTISTEDFNTIEIESTFEICRSGSYTEEPILGENDEFLIDFEMERFLKFLKDKTKQVEKRKEPFSQKEIYAVFQRRIKSELCIETVKKKFQPLLPNAIQTCEFDEETMIRMIYGAGIRIDSVDFWNRFTSKATISLDCYSRLISYSSDSLTLSGTHRSGFTYHWISTPPVTYHRTENKDPNIQEPSPVEFLDVQSSLGSSMKPPILDKPTKLDDPAETRHDCSYSLEEYDSQSRMPRTDAKKSNHKHKYCYEMNSNPRGTVLILSNENFKNMERRVGTKQDEVNLTKLFQKLQYTVICKRNLEAESMLEAIKEFAEMAHTDSIILFLLSHGDGAGSVFGIDDMPVNVMEVSTYLAYHQNLLLKPKWVAVSACRGGKLNMGVPVDGLPALEDKCAPISKFWNLMMSRIMPGTFTSLNADVIISFSTTDGFTSYRDEEAGTWYIKSMCKVFNKHSKTMHLLDILTETGRNVVTKYENVQGNVVLKQAPEILSRLTKQWHFSRSM
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Cysteine protease which, in vitro, cleaves itself and caspase ced-3 into their mature active forms. Also cleaves, in vitro, inactive caspase csp-2 isoform b. Required maternally to induce apoptosis in a subset of cells fated to die during embryogenesis, mostly independently of the ced-9, ced-4 and ced-3 canonical apoptosis pathway. Involved in the degeneration of dopaminergic CEP neurons in response to high Mn(2+) levels.
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G5EBN9
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SNF3_CAEEL
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Sodium- and chloride-dependent betaine transporter (Betaine transporter SNF-3) (Na(+)/Cl(-) betaine/GABA transporter) (Sodium:neurotransmitter symporter family protein 3)
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MGTSEHVPLPTDEAKAKELEQSQHSEEPDRGQWTGKFDFLMSMVAYAVGLGNVWRFPYLCYKNGGGSFLVVYMIFFCLAAVPIFLMEVTVGQYLQKGAMEMWLMCPLFRGVGIGNVVIAFMCIAYFCVIVAWAMFYMISSIAWVFPWETCNNYWNDATCVTGKENFTELARIKALVASAGGHTQTSVEQFWEKRVLHDTGDISEFGGIQWELFFIMAAAWLIVYFALWKGITQARKFVYFCALFPYVLIFILLIRGLTLEGAGTGIYFYLKPNATRLLDTAVWKDAGTQVFYSYGVGFGALIALGSHNKFNHNCFKDAITMCFINGCTSITAGFAVFSILGYMSHVAQKDISEIVKPGVGLAFLAYPEVASNLPMKQVFAVLFFLMITILGLDSQVCMMEGLFTALEDAFPILRKYKKQSLGIFCLFFFCIGIPMVTHSGSHWLTLFDAYGASGYALLFVVFFEVVGLAYGFGAHNIRKALHEMIGVTLPKGIEYVWKFCAPATSLVLFVFCVVYYHPVKYPDGKDFPFWANAFGWFLSSCSMVVIPGYAIYYLFFTNKHLTLKERVRKGLNLDGSFESPAKKNLVNNAEELKFIESSSQ
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Betaine transporter dependent on Na(+) and Cl(-) ions that functions primarily in the epidermis to clear betaine from the extracellular space. Elicits current in response to betaine but not in response to GABA, L-carnitine, sarcosine, glycine or dimethylglycine.
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G5EBQ8
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CHS2_CAEEL
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Chitin synthase chs-2 (EC 2.4.1.16) (Chitin-UDP acetyl-glucosaminyl transferase chs-2)
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MMNTLDHRPLGRMETMEGKPDEDEVPTSSNSDAKGKGYYYSSGTVPTDDSTLEEKCQQKTFDPSCPTPKTPVIVPNREFDPNFSTVTENKGWDIFRLLPPKPDRLGHGFWHDASLQVLKLATFLVLFLLTLGSAVVAKSTFILMTSAIGWGGQTITICNQVISEATQNTVKLKNAHVVKWVWATLLALSAPEALCFVRSMHRTMFRNVKRPTFIQFVFVLIIETFHSIGVGILVFRIFPDLDAVTAAQLTNAMCFVPAILSVISRKPNKSALLLVIIDFAAIAAQSSGFWALPMFLPNLQKHLVAIPVSLTLISLAWWQNFVHRDSVFPPVRTLAKFAQRLSERRSKTYAFVSLWKICIYVVCCFLFISSRMKIEDMLQKDPFGEKLLSVAGHDMNQTQIEKFQLRINQMIEQANREAGFYAAAEKKKQPPKKQPKADEAEQVDAGEYMMKRFKRFIGDAGENEEEEPEEEEFSSYNIYSNYVERNQLTMAYDALWLVIFQFGAVFVCYHSSKFACKVMMQRMGFALPMALSVPVTVLLLSTNCRMRQKDSCYGTNVLTVELFWQCNGASMSLADFILTPQTWIWLCWLASQFWITIHLWNPKHERLAKSEKLFILPYYIGAFVDQSLAFNRRRDDKAKIKAEDLEFDAEDSSLTYETIPGLQNKTPPSVCSASSSKLENGLIRDSASSADAITKIYACATMWHETGVEMTCMLKSLFRMDEDQCARRNAQKYLKVIDPDYYEFEAHIFFDDAYDVNEYGEPEINKFVKQIVNVIDQAASAVHQTQMRLKPPKKAKTPYGGKLTYIMPGKNKLFIHLKDNQKIRHRKRWSQVMYLYYLLGYRLMMKVDDPSRKEIISENTFILTLDGDVDFTPSSVYLLVDLMKKNRRLGAACGRIHPRGDGAMVWYQKFEYAIGHWLQKATEHMIGCVMCSPGCFSLFRAYALMDDNVARRYALKSEEPKHFIQYDQGEDRWLCTLLLQRGYRVEYCAASDAQTFAPEGFNEFFNQRRRWIPSTIFNIMDLLKDYRNVVRVNESISIWYIIYQLVMLISSILGPGTIFVMIIGAISISFSIDTLISLVIVSIPVVVFIVVCLTAKPEHQLICAQTIGAIFAMLMTAVVVGTSLQLQKDGLLSPHSMFTVAVATSFLTAAILHPLEFTCIIPGTIYFLAIPCMYMLLPIYSVCNMHTVSWGTREDPRPTEKNTLAKKTPGNLESGDGAGNSENWCTRFLCCGRGTVHPMTMVINEKLNEVIKKVDRLDRKHHPSLARRASILSSTGGTIQIDKCSEADEDEQAEIEDALEMSNQSHAAKKNQKWKQAQSEAWLADKALKRAEREYLEPEEESFWNDVIERYLSPLIMDGKDMDRLRAGLIAIRNSHTVYFLMINIVFIISVLVLQIHKDCLNIEWPLGPKFNHTVRPCYANHDDNQKEEVWVMTRLQLEPIGLVFLIFFVSILVIQFLAMLCHRFGTLAHIIASTELFCFRKTMDRLSEDELVAQNAVEIARELQAIRGIDENAHNIDNPTEDRGISRRRVVQNLESSRKSMMKRKTETLDAAFKKRFFALSSEQTPDPAGFSARDNSKRLTLRKGTIRALEHRRDSLFGTLDNRKDDEVDATSMRGPAQRRLERLFTAQQDQNSPTSDGNRRKSNSRPWDQPTSSATSSGDVELRRF
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May be involved in chitin synthesis in the pharynx during larval development.
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G5EBR3
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GLUCL_CAEEL
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Glutamate-gated chloride channel alpha (Avermectin-sensitive glutamate-gated chloride channel GluCl alpha) (GluCl alpha)
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MATWIVGKLIIASLILGIQAQQARTKSQDIFEDDNDNGTTTLESLARLTSPIHIPIEQPQTSDSKILAHLFTSGYDFRVRPPTDNGGPVVVSVNMLLRTISKIDVVNMEYSAQLTLRESWIDKRLSYGVKGDGQPDFVILTVGHQIWMPDTFFPNEKQAYKHTIDKPNVLIRIHNDGTVLYSVRISLVLSCPMYLQYYPMDVQQCSIDLASYAYTTKDIEYLWKEHSPLQLKVGLSSSLPSFQLTNTSTTYCTSVTNTGIYSCLRTTIQLKREFSFYLLQLYIPSCMLVIVSWVSFWFDRTAIPARVTLGVTTLLTMTAQSAGINSQLPPVSYIKAIDVWIGACMTFIFCALLEFALVNHIANKQGVERKARTEREKAEIPLLQNLHNDVPTKVFNQEEKVRTVPLNRRQMNSFLNLLETKTEWNDISKRVDLISRALFPVLFFVFNILYWSRFGQQNVLF
|
Glutamate-gated chloride channel subunit channel properties depend on the subunit composition. Glutamate binding triggers a rapidly reversible current in heteromeric channels formed by glc-1 and glc-2, while the anti-helmintic drug ivermectin and other avermectins trigger a permanently open channel configuration. Channels containing only glc-1 are activated by ivermectin, but not by glutamate alone (in vitro). The heteromeric channel formed by glc-1 and glc-2 is also activated by ibotenate, and it is blocked by picrotoxin and flufenamic acid. Plays a role in the regulation of locomotor behavior.
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G5EBT1
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SMA5_CAEEL
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Mitogen-activated protein kinase sma-5 (EC 2.7.11.24)
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MVFADFLEKIKSLFAKTKDPITSMSPPQENRSPKAEYLNNFFNTNPTNGKSRGSQEAPRKPLGQTNLNVQGSMPAKKEGFNRVLDGLKKRQLQHDFKLERAAETYEPTQNIGSGAFGIVCEAVETSSNQKVAIKKVAHASATPTLARRTLREIRVLRYINHPNIVPLRDIFRTKGPLGIDVFLVMDLMQNNLHHIIYGNEDPLEEHYINAFLGQLLRGLEYLHAACIAHRDLKPSNLLVNQDGTLRIADFGMAKCADNSSKKHDDEEHCYYMTQHVATLPYRAPELLFVLPEHSTAVDMWAVGCIFGEMVIRNEILPGRSVQGQIKMLLTMLGQPPQEVINEVRCDRTRKLIQDFGRKADAEWDDIMFCKARGDDQIVRGNCDTIDFVKQLFQYDAQKRINIQDALLHPYIQRVIPAEAPQKKCPFRVKKDMMQVEDLNHQELISMMKQDVRSAENPITYSELHSGDSTGSTSDMSTNTSGEYSPIAQHEQLLEDVATQISICEPTCDL
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Serine/threonine-protein kinase involved in the postembryonic regulation of body size, mainly through control of cell growth. In particular, controls the volume of intestine, muscles and hypodermis. In addition, regulates growth, intestinal granule distribution, lifespan and number of offspring.
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G5EBU3
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MMPC_CAEEL
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Matrix metalloproteinase-C (MMP-C) (MMP-C31) (EC 3.4.24.-) (Zinc metalloprotease 3)
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MRLIYVIAILLVSTCQAGFFSSLVSRFTGGGNSSPSSSSSSSSFSNSRKPSLSDEKARSYLQTFGYVPPSNSLQSRNGMAGDIQSAEQVFKSAIRKFQEFAGIAKTGFLDAATKAKMALSRCGVTDAPLALTSGSSQFKWSKTRLTYSIESWSSDLSKDDVRRAISEAYGLWSKVTPLEFSEVPAGSTSDIKIRFGVRNHNDPWPFDGEGGVLAHATMPESGMFHFDDDENWTYKDARKIHNNEATDLLAVAIHEGGHTLGLEHSRDENAIMAPFYQKTTDSSGNYVYPNLKSDDISAIQAIYGAGSGRSSSGSDFGGSSGGGSRTTARPTTTTRSWFGRFFGDDDDDVRSRTTTRRTTLWPTTQSPFSGDDWGSGSGSSGRGGSSSGSSGGGCPSHIDAYTPSSSFSYAFSGSQVYTISGTKVTKVQSIHDLFPSAPTPVNAALWNPISGSMLLFSSNRVYSYYFSNIRQIFQMDSGFPKTLPSDLGFSVSGALRWINGHQILMSSGDEFAVYDEFWNQVTLKNRISSYFPNLPRGVKGVESPAGSVITAFTSNQVFEYNSRTKSIGRQSGFSSYIAC
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Metalloproteinase.
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G5EBU4
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ZAG1_CAEEL
|
Zinc finger E-box-binding homeobox protein zag-1 (Zinc finger involved in axon guidance 1) (ZAG-1)
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MVDIAEAMPTTASSLPSDEALRKFKCPECTKAFKFKHHLKEHIRIHSGEKPFECQQCHKRFSHSGSYSSHMSSKKCVQQASPSMVTPFNPYQLMMYRNIMLQLQTPQVSFLPSTAANNMDYMSLLQANLFQSLENGTSPTPTQEPSAPASPEPKIEVVDEPEVSSEVKTEVKTEVKTEDSVPEESITPAVSMSLSPAPEQNGNESMNNGGSGSDGKSSPDWRPLRSRSFLNDSQVAVLQNHFKRNPFPSKYELSAVAEQIGVNKRVVQVWFQNTRAKERRSNRLPSMPRGSVASAAAAAATSPTVWQTPVQLMAAWASQFSNGNNSLTASQDERNNENTDEVMDHDGLKDGKETPLDLTLSTDDTEPEWSPEKLIGFLDQTGGVIQELLRQAGNGFVTNQEDEEEKPIKAEESPVSSGSSSIWPSFIGQYPSILDSASLSVLEKALDQQKSSEDDASSLCSNESKLLKFPTTPLKEEEGLFSCDQCDKVFGKQSSLARHKYEHSGQRPYKCDICEKAFKHKHHLTEHKRLHSGEKPFQCDKCLKRFSHSGSYSQHMNHRYSYCKPYREQPASPSDVLNGGSVTVSPSSSNTPPPST
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Transcription factor. Down-regulates expression of genes involved in either the synthesis or reuptake of serotonin, dopamine and GABA. Acts as a transcriptional repressor to regulate multiple, discrete, neuron-specific aspects of terminal differentiation, including cell migration, axonal development and gene expression. Promotes touch receptor neuron differentiation by repressing the expression of egl-44 and egl-46. As egl-44 and egl-46, probably acting as a heterodimer, repress expression of zag-1 in FLP neurons, together these proteins form a bistable, negative-feedback loop that regulates the choice between neuronal fates. Required for axon guidance. Involved in the proper development of the pharynx. Required for pharynx isthmus peristalsis, probably via a role in the differentiation of the M4 cholinergic motor neuron. Directly represses its own transcription by interacting with conserved E-box sequence motifs 5'-CACCTG-3' in its own promoter. May also act as a transcriptional activator of the homeodomain ceh-28.
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G5EBV0
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EGL9_CAEEL
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Hypoxia-inducible factor prolyl hydroxylase (HIF-PH) (EC 1.14.11.29) (Egg-laying defective protein 9) (Hypoxia-inducible factor-proline dioxygenase)
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MSSAPNDDCEIDKGTPSTASLFTTLMLSQPSSSTAVLQCTYCGSSCTSSQLQTCLFCGTVAYCSKEHQQLDWLTHKMICKSLQTSGMVPSNLMPQAAPAVMAPIPPTVSFDDPALTTSLLLSLQNNPILNQTISNFPPTFSITSKTEPEPSIPIQIPQRISSTSTVPFSSEGSAFKPYRNTHVFNSISSESMSSMCTSHEASLEHMSSASLAMFPTSSTAQSDISRLAQVLSLAGDSPASLALVTTSVPSTASTATIPPPATTTSSATSSGKSETITVGKEKIIQTDDPDIQIIETEGGSKPTVSRTRKRPTPSNSADPKINYKDHNKNVVYSTTLQEHQKHLQNRGLALSIHQAMVLRLRYIAEHVIRSLNEFGWAVVDNFLGSDHYKFTAKEIERLYERGLFSPGQLMEAKHKDEFHIKDIRSDHIYWYDGYDGRAKDAATVRLLISMIDSVIQHFKKRIDHDIGGRSRAMLAIYPGNGTRYVKHVDNPVKDGRCITTIYYCNENWDMATDGGTLRLYPETSMTPMDIDPRADRLVFFWSDRRNPHEVMPVFRHRFAITIWYMDKSERDKALAKGKESDAACASKKENDPTSSSLNSLIGSLLRPRKNPSTHDLSKLDLRLFPSTSSDPALVSAADEDRVDISADFQSTSSLAHPESTDSGVSLSTFNVAHNHMERTTSLQSISDHFRSERSHERRSSTSSDQDLDEGLPPPPSTNPEYYI
|
Cellular oxygen sensor which regulates the stability and the activity of hypoxia-inducible transcription factor, hif-1. In normoxic conditions, hydroxylates hif-1 targeting it for vhl-1-mediated proteasomal degradation. In addition, regulates hif-1 transcriptional activity in a vhl-1-independent manner and independently of its hydroxylase activity. By regulating hif-1 activity, controls several cellular responses. Mediates susceptibility to B.thuringiensis and V.cholerae pore-forming toxins and enteropathogenic E.coli. Mediates susceptibility to P.aeruginosa PAO1-mediated killing by regulating resistance to cyanide produced by P.aeruginosa. Mediates resistance to S.aureus-mediated killing. In addition, plays a role in heat acclimation, neuronal development, behavioral responses to reoxygenation and hydrogen sulfide, iron homeostasis and aging. In neurons, involved in mitochondrion fusion during reoxygenation. Involved in egg laying. [Isoform e]: Regulates the trafficking of the glutamate receptor glr-1, probably independently of hif-1, by regulating lin-10 subcellular localization in response to oxygen levels. May hydroxylate lin-10.
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G5EBV6
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PGL3_CAEEL
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Guanyl-specific ribonuclease pgl-3 (EC 4.6.1.24) (P granule abnormality protein 3)
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MEANKRQIVEVDGIKSYFFPHLAHYLASNDELLVNNIAQANKLAAFVLGATDKRPSNEEIAEMILPNDSSAYVLAAGMDVCLILGDDFRPKFDSGAEKLSQLGQAHDLAPIIDDEKKISMLARKTKLKKSNDAKILQVLLKVLGAEEAEEKFVELSELSSALDLDFDVYVLAKLLGFASEELQEEIEIIRDNVTDAFEACKPLLKKLMIEGPKIDSVDPFTQLLLTPQEESIEKAVSHIVARFEEASAVEDDESLVLKSQLGYQLIFLVVRSLADGKRDASRTIQSLMPSSVRAEVFPGLQRSVFKSAVFLASHIIQVFLGSMKSFEDWAFVGLAEDLESTWRRRAIAELLKKFRISVLEQCFSQPIPLLPQSELNNETVIENVNNALQFALWITEFYGSESEKKSLNQLQFLSPKSKNLLVDSFKKFAQGLDSKDHVNRIIESLEKSSSSEPSATAKQTTTSNGPTTVSTAAQVVTVEKMPFSRQTIPCEGTDLANVLNSAKIIGESVTVAAHDVIPEKLNAEKNDNTPSTASPVQFSSDGWDSPTKSVALPPKISTLEEEQEEDTTITKVSPQPQERTGTAWGSGDATPVPLATPVNEYKVSGFGAAPVASGFGQFASSNGTSGRGSYGGGRGGDRGGRGAYGGDRGRGGSGDGSRGYRGGDRGGRGSYGEGSRGYQGGRAGFFGGSRGGS
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Guanyl-specific endoribonuclease which cleaves the phosphodiester bond in single-stranded RNA between the 3'-guanylic residue and the 5'-OH residue of adjacent nucleotide, resulting in the formation of a corresponding 2',3'-cyclic phosphate intermediate. P-granule component involved in germline development. Together with the P-granule component pgl-1, is involved in the formation of P-granules. Together with pgl-1, probably recruits other granule components such as pos-1, mex-3 and glh-1, and RNA to P-granules. In vitro, binds mRNA this interaction is required for the formation of liquid-like droplets that resemble P-granules. Most likely recruits pgl-1 into P-granules during autophagy. Associates with adapters such as sepa-1 and is required for the accumulation and degradation of P-granules by autophagy in somatic cells. This ensures exclusive localization of the P-granules in germ cells. In addition, may act redundantly with pgl-1 to protect germ cells from excessive germline apoptosis during normal oogenesis and development of the two gonadal arms. This may in part be through regulating the localization of sir-2.1 which is involved in germ cell apoptosis. May protect somatic cells from excessive apoptosis during normal development.
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G5EBX9
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PPE_CAEEL
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Serine/threonine-protein phosphatase with EF-hands pef-1 (CePPEF) (EC 3.1.3.16) (Phosphatase with EF hands 1)
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MGCGPSSGRQNPSTELKKSTRATTTTTSSSQRNNYNDNNQNTSSSSGNKKESSSSSKQHSSKKSKKSNSKKNRSPSPQPQLTIKSAILIQKWYRRCEARLEARRRATWQIFTALEYAGEQDQLKLYDFFADVIRAMAEENGKGGVENGRNSPLMSALSHYAKPSLMDSEGETVKKMLEDTSPTNVDIDRNYKGPTLSLPLDKPQVAKMIEAFKVNKVLHPKYVLMILHEARKIFKAMPSVSRISTSISNQVTICGDLHGKFDDLCIILYKNGYPSVDNPYIFNGDFVDRGGQSIEVLCVLFALVIVDPMSIYLNRGNHEDHIMNLRYGFIKELSTKYKDLSTPITRLLEDVFSWLPIATIIDRDIFVVHGGISDQTEVSKLDKIPRHRFQSVLRPPVNKGMESEKENSAVNVDEWKQMLDIMWSDPKQNKGCWPNVFRGGGSYFGADITASFLEKHGFRLLVRSHECKFEGYEFSHNNTCLTVFSASNYYETGSNRGAYVKFIGKSKQPHFVQYMASKTHRKSTLRERLGVVEESAVKELKEKLSSFHTDLQKEFEIMDIEKSGKLPILKWSDCVERITGLNLPWIALAPKVATLSEDGKYVMYKEDRRIAQVGGTHAQEKDIVESLYRHKSTLETLFRFMDKDNSGQVSMKEFIDACEVLGKYTKRPLQTDYISQIAESIDFNKDGFIDLNELLEAFRLVDRPLLR
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Probably acts as a protein phosphatase.
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G5EBY8
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UN129_CAEEL
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BMP-like protein unc-129 (Uncoordinated protein 129)
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MRRLPIVLLLSVFSIANCAKVDVDLINETIRDLLHFKSSDPNVTSFHRSSHTLTEHMKNLYENFIDEDSNEDGNLVRAIEPAVGKFEGQEVLVFDVEGFDSHESIMRAELHFYLRRRDSFARRRSRQIRAKSVCVNEYCRQQTLKKIRVGGDENLEEYKVIWDATKSVFDSYHLDAKQAVFRITREHSKMRPYAEMIRKSTPFLVIYSKVNHTLDTVSVMKQTEQTKRKRRDLGNEELREYYNYNSIPLDNDDREPIKRKNGKKNSLSEEISSEDVWQGFGEETSREERERIANEELANDVRVVLLQNKNRCHKEGVLVSLKHFGWDRYVIEPKTIETSFCKGKCAKPMLTSGKASNHAMLQSLFAAEPVCCAPTNLKSLNFWYRDEKGRTVIRNYSKMLIGSCSCL
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Required for the migration of axonal growth-cones and distal tip cells (DTC) along the dorsal-ventral axis of the body wall. Acts cell nonautonomously and independently of the classical daf-4, sma-6 or daf-1 TGFbeta receptor signaling. During axon migration, facilitates long-range repulsive guidance of unc-6/netrin by enhancing unc-5-unc-40 signaling at the expense of unc-5 alone signaling, probably through direct interaction with receptor unc-5. Involved in cell-cell contact formation in sensory rays in the developing male tail, via a pathway involving plx-2 and mab-20/semaphorin-2A.
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G5EBZ4
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LE418_CAEEL
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Protein let-418 (Lethal protein 418)
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MSTEEDPSLVDAEESMEEGSVTQDATEETEEEEEQEQGDEAGPSERKRSSRKKGGKGGKKGSKKSAAAASKVEIPDPYNSTSEEVCAAIGLTDVEFDYDEEEFQGISNLKTFSSIIKPQILEANPGTNVSKMYPMFQVKYKEYQDHMAAQGKPVQKQARGSKTPAVSTPVIPPRSAPTKTRSARRKRRDSDAPDSDQEFEAFIKQQEQLEDDLVKDKEDARIKRAAEREEKKKGALEAARAAKKAKLEKGEEAENNDYCEECKQDGELLLCDTCPRAYHTVCIDENMEEPPEGDWSCAHCIEHGPEVVKEEPAKQNDEFCKICKETENLLLCDSCVCSFHAYCIDPPLTEVPKEETWSCPRCETVKPEHKIEKILCWRWKEIPYPEPLEAGKEASSDDAMLKPPRKMEPRREREFFVKWKYLSYWQCSWVSEMLLEVHFRMLILLYWRKNDSDAPPEFEESVTSRHHSDNDPYKLRERFYQYGIKPEWMQIHRIINHQSYAKSQQDYLVKWKELSYDQATWERDDSNIANYEEAIIKYWQHRESKLNEDIPKNVQKMIAKHREAKGLPPKEDEKKKKKREKIDIRKKYEVQPDYVTETGGKLHPYQLEGLNWLRHCWSNGTDAILADEMGLGKTVQSLTFLYSLMKEGHCKGPFLIAAPLSTIINWEREAEQWCPDFYVVTYVGLRDARVVLREHEFSFVEGAVRSGPKASKMKTTENMKFHVLLTSYETINMDKTILSSIEWGALVVDEAHRLKNNQSLFFKNLNEYTIHYRVLLTGTPLQNNLEELFHLLNFLSKERFNQLEAFTAEFNEISKEDQIEKLHNLLGPHMLRRLKADVLTGMPSKSELIVRVELSAMQKKWYKNILTRNFDALNVKNGGTQMSLMNVLMELKKCCNHPYLFVKAELEAPKEKNGMYEGTALIKNSGKFVLLQKMLRKLKDGGHRVLIFSQMTRMLDIMEDLCEYEGYRYERIDGSIMGQMRQDAIDRYNAPGAQQFIFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRLGQKHKVMIYRFVTKKSVEEKITSVAKKKMLLNHLVVRAGLGGKEGKTMSKTELDDVLRWGTEELFSEDLDAAEGEGSEKKGAAAQEIVWDDAAVDALLDRSNKEETPAGEDGEEKAEWQNEYLSSFKVASYQTKETEGQEEEEEEETEVIKEDEKEPDPDYWEKLLKHHYEQDREIELQKLGKGKRVRKQINYASENMGTDWSKQNQTQDDDDDNESYRGSDNGDGLNSDEDDYDEKKKRRRDEEKMPPLMAKVNGQVEILGFNPRQRKAFYGAVMRWGMPPQDSHQSQWLVRDLRNKSEKVFRAYASLFMRHLCEPGADGHDTFNDGVPREGLNRQHVLGRIGLLSLVRRKVQEFEQYNGQWSMPEIQDEVLAKAANGSAQGSSRSTPKPKEEPKEEPMEKEDATETVNGATSEPATDAESEQNAPVDEPMDTDEAKEPKEEPIETEKPRAARPSFKFNICDGGFTELHSLWANEEKVARNGKEYEIWYRRHDYWLLAGVVVHGYGRFQANFNDIINDPRFSVLNEPFKEVGAEATGSDIKAKFMQRRFKLIEQSLVIEEQLRRAAHANRHLQPDNVGPLAQRFADLENIAESQANIAKESSAGNRNANAVLHKTLVQLDEILSDMKADVSRLPSTFTQLATVTERLNMTERQILSRLTTKDEDAIANRSVLPPPGPFVTPILRQQMDGIQPKFAALYSKFMSENGERMEEDEPVEAEEEEGVKQEPDDETQDSAEAPPVLSAEVNSDDSNDVPSTSAAAAVSSETAADAEPASAEDQAPTDEPEPMET
|
Part of a NuRD (Nucleosome Remodeling and Deacetylase) complex which is implicated in the synMuv B pathway that negatively regulates specification of vulval cell fate. This negative regulation is thought to be mediated via interaction with the promoter of lin-39, a key regulator in vulva development, and is dependent on the presence lin-1. Contributes to negative regulation of lag-2 which is expressed in the gut during larval development. Has a broad role in development. In association with akir-1, plays a role in regulating the transcription of antimicrobial peptide genes in response to fungal infection.
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G5EBZ8
|
ARK1_CAEEL
|
Ack-related non-receptor tyrosine kinase (EC 2.7.10.2) (EC 2.7.11.1) (Ras-regulating kinase ark-1)
|
MREEPTAGTADATLNKLLQAADLSGYESDLRRKLKLRNAADLQYVEEVDLLSVGMSRPEQKRLRKEYTKMFPSGIFGKVKKAFKRAESLDRKTSNSVANQDDNDHHVIPIEKITLCKELGQGEFGSVWQAGWKNSAGSDVIQVAVKCVGSDKLLATSSSFLQEAAIMTRMRHEHVVRLYGVVLDTKKIMLVSELATCGSLLECLHKPALRDSFPVHVLCDYAEQIAMGMSYLELQRLIHRDLAARNVLVFSPKLVKISDFGLSRSLGIGEDYYRSEFTPNLKLPIAWCAPECINFLKFTSKSDVWAYGVTIWEMFSYGEMPWKGRSGAQILELVDRKKELLTRPKACPEDIYDMLKETWTHQVQDRPTFSDIVAKFPERRAQSVRAVVDCKDSAADHLHFKKDDLIVVISRSPAQYPDGYYWFGSLRNGKLGLFRPTDTVAHLGSEPPCSNGTIENGFSEKEKGGKKNKKAEKESERERKKLLISEPVGDVRHTCHVGIDGTAFGLLQLDKKAMCPTSSSPSTSRGSQASPAPSHTSSSTTSSVHLRETVARNGVPIKETMSLRDVGPLSRDALNLRDTVSPPVARAPSQPPSYSQPRPPPRSVSSVSSGNQHSVQVHDQFSSLDRSRGSLTPTAPPLTASAANSLKDPLTGISLSIPSNNLISYMDDQEDDHRWTRSPGAISQSTTLTALSSSRKDPIPAPRGPVAAVYARGKDIPTPASKSDIALCEKIEDLNRDLTNYSIGTICDYSEDRPLLDSMNRTISSSTTHQPPPQSSEARIRFMTEQEVRKINEKSAREHRKTEDLLREERQKEQKPGEIEEPQQPAESLYSTRTPQQEGWSSAAQEAYKLLVECGTNLKQASVSPPPMSPTSSRLSTLDRSSISPAPPRPVTPPLSVRNETISMRKSQQEEMEHVTVEENSPKRVHIIETKLIDGPARGMSPIQDRHIPAFTTPMSNGSFRKAPAPTPVSPAPAGSTDQKPPPCRPPKTRQFPLVIDERNLAYDNLNGFGAGARVAPPVPPKPKVRTIFSFADDQKKQKEVAN
|
Probable tyrosine protein kinase which plays a role in vulva development, probably by acting as a negative regulator of the let-23/EGFR and let-60/ras pathway. Involved in the negative regulation of germline development.
|
G5EC23
|
HCF1_CAEEL
|
Host cell factor homolog hcf-1 (HCF homolog)
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MDEDVGLEATNYSRGDESRSEEQEKNVVRWRIVQQSTGPNPKPRHGHRAVVLKELIVIFGGGNEGMIDELHAYNTQKREWTAPQCCGDVPTPAAAFGAISLGNKIYRFGGMTEYGKYTNDLYELQSTRWEWRRLNPRVHSNGHLPCPRIGHSFVVSQKSQKAYVFGGLSNDLNDPKRNVPHYLDDLYVINLSGPQHLIWEKLNATGPGPISRESHTAVIYEKDSISRMVVYGGMNGVRLGDLWYLNLNTLHWTEIKFDDPRTGIPPMPRSLHSSVLIGDKMFVYGGWVPLLEHASTEQQTEKEWKCTSSLGCWNITEDRWVPLHLYCSDEDTIPRGRAGHCAAAVGDRMYIWSGRDGYRKAWSNQVCCRDMWLLDTILPEQPGKVQLGRAGFNSLEISWPIVQGASGYFLQIGFGDAKEQSVSPIKRATTSPRKQPSIVPPSQKETEQSPKKPQGTAPSIISTQGTTYTAPADPKPATDEGGLPQDLFEDTEKNETASPKRSNDAQSADSSTCEQKKTDESGLEEDSEKDQKPSDAGETDEMKEENGDDDLPWFDVGIIDKATINVTHYFNDRQQSLEKQLNDLIDHNAFKCVNDSVFTTEDKIPLINGQSYRFRVSAINGLGKGAWSETASCKTCVPGYPSAPSSIRITKSHEGAQLTWEPPSNTNISGKIIEYSVYLAVKNQSANSADSQLAFMRVYCGPQADCQVLQSNLGTAFVDQTNKPAIIFRIAARNEKGYGPATQVRWLQDQQKIPVRTNYPNNSGFIYQQHGGQQKRARFDHQ
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Transcriptional coregulator. Involved in control of the cell cycle and in modulating mitotic histone phosphorylation. Plays a role in modulating lifespan by regulating the transcriptional activity of daf-16/Forkhead box protein O, in concert with protein deacetylase sir-2.1/SIRT1, and perhaps acting independently of the Insulin/IGF-1-like signaling (IIS) mediated pathway. Negatively modulates responses to environmental stresses, including oxidative stress, heat stress, and exposure to heavy metals acting via regulation of the transcription factors daf-16 and skn-1. May play a role in pharyngeal development via positive modulation of expression of sup-35.
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G5EC24
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PTP2_CAEEL
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Tyrosine-protein phosphatase non-receptor type ptp-2 (EC 3.1.3.48) (Protein-tyrosine phosphatase 2)
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MPRLALRQYNFYYRVNGEKAEELLKEYGEDGDFLLRYSESNPQNFSISVRVAEDKILHIKVTKYESDMLSIFEDERTTPNQFGSITELAEFYMEFPEKLREKNGLFLELKKPVYVPYHLEACAEEQRRTQLYRWWHGNLPASSANKLLQTEKNGTYLLRASQHIPGALVISAKTEGQVVHLTIYQDPSTGRFNIDGDRTKFQSAWLLIDSYSKNPIVEKGEASRVLYLEEPLFNTFIEADLFVDRFEIIRRPINPRESMEKTGISEEFDRLSQEALPAEQYLSKREGRRPVNAEKNRYKNIVPFDHTRVILTDRPNTPGSDYINASYVRFENSQRTKNVTFACEKSFIATQGCLETTISDFWSMVWQENSRVIVMPTMENERKEKCARYWPAEVNKPEVHGDISLTCTIERKVQRAVSDEVKAELEQEKTNRIAKGLVPEAELNGDGISYILRTLVMKKGKDTREIRQLQYLTWPDHGCPLHPYAVLNFLEDVDREYDYFNAQPIAASLPQGPIVVHCSAGIGRTGTVLVLDALLNQVKKVGLLCPMDVYKMVKYVRTYRSGLVQTEQQYQFLYKALAFYLKNNNPYPVKSFIDGDTDAFDFPRRLRPTPNASRPSSARQVTSSRPSSSASSRTSHSRPRTGPQAEPIFERSTSSTSSSSTLLKSTKK
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Involved in embryonic and larval development. Plays a role in oogenesis by regulating mpk-1 phosphorylation and oocyte maturation in response to major sperm protein (MSP). During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles probably downstream of receptor egl-15. Plays a role in fluid homeostasis probably downstream of receptor egl-15 and adapter soc-1. Promotes vulva induction and negatively regulates fertility probably downstream of receptor let-23. Negatively regulates daf-2-mediated repression of dauer formation.
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G5EC32
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SRBS1_CAEEL
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Sorbin and SH3 domain-containing protein 1 homolog
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MMHHPHPFGSNLANSSEPQQPSGQYLNPAADAYNFDTFEDSDKFSPKGNVAALRNVIHGQLDMKTPTGNSSRYQKPAPPPVDSTPSWAKNVKVYEPNGYVDPHLNKHNMGRVLDGPVNPNKYFQGVPPASYSQVKHNESKPPVPPSTKPPHSAAQALQAQVLQSSKAPSQPQQSQKTSYRIPYDVALDPRHHLGEFDIDDSASIISSCISTFGESSEIAGFSAAAEQRHLYEQYRKKLMEEKNELKEGSETPCVSLSEKVMTSSTENLKNGNNQQNQQPEPQPPSSSIFNSELTPFGHVAPVAKQFEPTNFPPFSPEKESEIKRSIDLESSQLLVKSKSPAPYSTSSTDHYGTIRRKHKPVAIDLSKSSPNLASQSPSNLFFGASFEEKQNRSPMTSTPSYKEQGFKNDSLNDSLNQAFEIASSIETTKNAYEAPPTPKSASHDRSISDTYPVSSSTTSTWPSHTTTPTTTTAAAPIAAVAPQTYTEQQPMSTSMSSSVMSTNMDEPIVVGSHQQIPQQSPDSSPERNEDMSQWYRKMFKQMHRKGEDGSNEGKEQHFINPSNVTDGIGRTTPTASNLGRSRENLSFNQHRPDHPSSYFDSLEHGPNDQYNNQERVKQSNEEELLRLKAEKLAEELRKEKERKHSFIPSSAPSLQNNMDRLNSLLYDFSSDIQEPAHRDYTPQPVMTATAVYKFEPRSARELPLNRGDIIRIIREVDGYWMEGERNGRSGIFPTSYVQINTGNQGDSQKMRAIYPFTARSDTELSLKRGEIITRRRQIDSNWLEGSNQIGIVGIFPASYVEPIEQVEQHIPTIVPNRPKTPKIEDQVYNQVYKPNETVIMQSNQGYYDKAAVVPNNKVRFDLPSGSDSNLQMSLNPHQNQFPPTHTQTSTQQPSNYGMKKIEYEREKVVEEVPPMHMDQYRKLNDEPKNPKKDTNILMNAASLIPKGSEMYRAVYPYQPQKEDELQLYTNDIIFVVEKCDDGWFIGTSLRTGDFGIFPGNYVKRH
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Required for organization of sarcomeres in body wall muscles and for maintaining normal mitochondrial position in myocytes.
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G5EC36
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LIM7_CAEEL
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LIM/homeobox protein lim-7
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MNICMRNGYEQFSLTSPGTSDLEIGGSFWKDEPDTKYLCLDSPVEQRQHQPPMAVCAGCRLEISDRYFLRVNPNLEFHAQCLKCVQCSRPLDENQTAFVKNGQTYCRDDYRRLFTTRCSRCHGDFDKTDLVMRAGPQNVFHLNCFACVACEKRLQTGEEFQIKNNSLYCRSDCRGLDNPDTSASVPDYSKLNNNNNNDNNNSSSNFDEDEWDEERSTLTSLDNNTSSPLGSPKSDGVRTPLFGHHNSGSGGSTSSCGKKKKDKQATRVRTVLNENQLKILRDCYSINSRPDATLKERLVEMTGLSARVIRVWFQNKRCKDKKRQIQITENRLNSEREEVLNRVRVNGIGPLMVQPATPHIDNTLGGPIDIQHFAQWNGTPPPPPPQYGNPMMFNSPSTFDVSVILAPVAPNVTSPSEALGPLGASVFPHFSPQHAPFTATSHDISSPAPCGE
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Probable DNA-binding transcriptional activator.
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G5EC37
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SEPA1_CAEEL
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Protein sepa-1 (Suppressor of ectopic P granules in autophagy)
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MTPLSALTSNPAPSPPPKFALGKCPATAIHVVSVLRPNRQRFCYEKTDAGDLIPHKCLICQPILTEKHISPYYAVYSDLLEDFVLFGYNTMTGKMEQFIYAFKTDCFVEVNRPEIKYNPAFLVKGNVVVALNGPEGELVVIERDCRGLLSKESTSYGQFRTLPTAALRTLTLQDLERDRWDRAANSDEVKISSGNESFDRLYAEYQKNLPRFQVRQCLHLNKEFLCVYSKTSGDYTRLEYIDETGDFQKISCTLCTCEVTESNLIPLYVERNASELVIHVHNTENNQIEQYIYDVRTFGFVQVKRNLVYDPKKITSGLNLFMAENIDNRKVYMIMRGRDGRLQKETSGSGGFEKMQPVAVKTFQVQWVEMKTEFEKKKASTERVEPQHPVQTEGEDIMETVLAMVESFNCDLRKELGLTQDQEIPRKAPRVESAETEENIVKNLEKLQIAKDPEEPTTAASEGGNTYGYQELDDTMSEGLLEKEAESKHQDANEPEPVKNVTYEPDVAAMDKKKKRRELKSRLNKINAQIDELEKRRMERAGKKQVVSSSVPSEEAAQVEAPASPALAENTNQISNEETPKIDIFEGYNGSFLFGTNTSKEWIVEDIRNHMVGKLLKAFWPRIQNVEEMNGELFKKLIANARKCETEILEASNDRDEYYRLMQLTVDQILKKTLKKDQRATEHNHQQPTQSSDELAKNHEKN
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Adapter protein that connects P-granules in somatic cells with the autophagic machinery. Association with other adapters such as epg-2 and P-granule components such as pgl-3 is required for the accumulation and degradation of P-granules by autophagy in somatic cells. This ensures exclusive localization of the P-granules in germ cells.
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G5EC44
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MRT2_CAEEL
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Cell cycle checkpoint protein RAD1 homolog mrt-2 (EC 3.1.11.2)
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MMELETGQCTIMELKKENVKELAQVFKTVAFKDTGTWHASEAGMKITVDDGSYQLASVFINPAFFSSFKVREEIVSMKISIKSISEFLSISENSSSSVKVSYPGMFQPVKMLVEDADGWVARGNFTTTLADQELDFEFDDAGVLATYLLKTQVLKEIIKDFDDTSRTVRIQFTKNSLCFTTFGDVGETTVSIPSRSLQMESVKCLEEVEFSYLLSLIQRMTTAFILATKLILRVDERGVLSCQFSIDHGEGNASYIEFLTVPADEEE
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May be a component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. Promotes DNA double strand break-induced cell cycle arrest and apoptosis, thereby playing a role in genome stability. Also required for telomere length maintenance and germline immortality. May possess 3'->5' double stranded DNA exonuclease activity (By similarity).
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G5EC86
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MOE1_CAEEL
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CCCH-type zinc finger protein oma-1 (Maturation oocyte expansion protein 1) (Oocyte maturation defective protein 1)
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MNVNGENNEKIDEHHLESSLAGVPTLPVSPLDHAKDLSQTNPNAQIGDLVTQTANLIAIKKQLLEDIAFNQHIQSMQVRAIQSFPQNNQVAPPFQQFDPRRRGLARMQKPESYKTVICQAWLESKTCSFADNCRFAHGEEELRPTFVEPLQNNKYKTKLCDKYTTTGLCPYGKRCLFIHPDHGPNAYIRADKLLEVSQRHALADIRDQMEQHIMTNGRIAAPPLSAIQHPLEMFARPSTPDEPAAKLPLGPTPVSTRGPRYELPTKELHDAEGAMTYPPSRWPLDPSMFALDAWNMAHRPASPLDSMVLGSAPNAGSFGMLGKQNTPGGVSGYSSAGSTPSQDLSSSSLNAASAAAAAAYFANSAVAQSLLMKSVATDPMMSCNGPFSPMPGFDQLAENMTKHLNLW
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Zinc-finger RNA-binding protein that binds to 5'-UA[AU]-3' motifs in the 3'-UTR of maternal mRNAs to suppress translation in oocytes and embryos. Acts as a ribonucleoprotein particle component that may exert part of its function within cytoplasmic foci of unfertilized oocytes. Acts redundantly with oma-2 to control the temporal expression and distribution of maternal proteins and thereby promote meiotic progression, oocyte maturation, fertilization and embryonic development. Recruits the translational repressor ifet-1 to the 3'-UTR of mei-1 and zif-1 to negatively regulate their translation. By suppressing the translation of the E3 ligase zif-1, may in turn play a role in the stabilization of zif-1 targets such as the maternal transcriptional repressor protein pie-1. Following fertilization, sequesters the transcription initiation factor, taf-4, in the cytoplasm, which prevents its nuclear localization and thus allows for transcriptional suppression in early embryos, but not in oocytes. Also, together with oma-2, is involved in P-granule distribution during embryonic development.
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G5EC89
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CEH17_CAEEL
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Homeobox protein ceh-17
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MMMEYGGYFSSSAVAQQSGDVPTTAPSAVTNSFFYTPQSHNIYHQYATPYLQSGRALTTAHNTSSSSAGNSTSSSSSSSNYRNTTHDSLQAFFNTGLQYQLYQKSQLIGSDTIQRTSSNVLNGLPRSSLVGALCSTGGAPLNPAERRKQRRIRTTFTSGQLKELERSFCETHYPDIYTREEIAMRIDLTEARVQVWFQNRRAKYRKQEKIRRVKDEEEDPLKKEPGQISLEEIIDQI
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Probable transcription factor involved in postembryonic differentiation of the ALA neuron, and regulation of genes that contribute to behavioral quiescence, a sleep-like behavior mediated by ALA. Regulates its own expression and also that of homeodomain ceh-14, together forming an autoregulatory loop in the ALA neuron. Involved in fasciculation-independent longitudinal axonal navigation in many neurons.
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G5ECB2
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GABR2_CAEEL
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Gamma-aminobutyric acid type B receptor subunit 2
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MSRWLSLLLFAVQAVGGYEAGEELSCKRRHGGIPLPLGVFTVQKEGFPDALPAIRTALSHVHSRSCILQGYRLEMIVKDTHCKTSQGMKALFDLIASRPRPVAILGGQCTEVNEPIAMALKYWQIVQLSYAETHAKFASSDSHELFTTFFRVVPGSRNTNMAKCKFVNHFGWKRVGTVKQNDQPRYALPHEALTTRLEHGFGVKIVHTAGVNWEQIETVGGELDELKERDVRIILVDVDEEMAATVLCAGYHRGMYGDNYVWILPGYHSDKWLNQTHDNCTVEEMREAAKNHFSVEFALTRRDVDTKIVGNTRAGDVWNEITQLDPNNTWRGYLYDGLWTLAIALSHSMGDNAEFSHHKMMEAIDNSSFQGLTGKVKFANNERLGLVDIKQWSDGQYVPFAVYDGADDEFKIIDSTTKGWSPPLDSTITERRREHISSILFLAMSLLALIGIFLALIFLLINFRYRNHRFIKMSSPNLNNIIIAGSICTFASVIMLGLDTRIVSPDVFVWLCYTKTWTLCIGFTLSFGAMFSKTWRVHSIFTNIRMDRKAIKDSKLFIILGILLFIDICVLVTWAFVSPFSYTVTELPHIPEDNIVIIPEVEKCNSSHSGVFQAVLYAVKGVLMILGCFLAWETRHVNVPALNDSKYIGTSVYCCVVMSVLGLSTSVILQERVNEMFSLASFFVIFSTTLTLCLVFVPKVIELARNPVGNEPRAYRRGLMKSVVAKTSQPMSPQPRSDSSGDLIGKAESENKLRRRYLHQKSTQLWDLVEKLRAQGDTRFLQQEWCLSSASPSSQERETSLLLRQPSSSNNREETSLTAAGPNGERSSDWPWVDPDEPSTKL
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Component of a heterodimeric G-protein coupled receptor for GABA, formed by gbb-1 and gbb-2 (By similarity). Within the heterodimeric GABA receptor, only gbb-1 seems to bind agonists, while gbb-2 mediates coupling to G proteins (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (By similarity). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (By similarity). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (By similarity). Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (By similarity). Along with gbb-1, may couple to the G(o)-alpha G-protein goa-1 to negatively regulate cholinergic receptor activity in the presence of high levels of acetylcholine in ventral cord motor neurons. As acetylcholine depolarizes body wall muscles, modulation of acetylcholine levels most likely results in the control of locomotory behavior. Regulates locomotory behavior in response to GABA release by GABAergic motor neurons.
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G5ECC7
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UBP48_CAEEL
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Ubiquitin carboxyl-terminal hydrolase usp-48 (EC 3.4.19.12) (Ubiquitin-specific protease 48)
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MTKETDKKPKERPNQRKVAFRNEAINALVNTDEDQVTFSKAMEVAKLDCQKCLLHDMHSSKSSNCRDNPFCIHRLGLEKFEKLITQEQETKEEAKKDQKRRDLNDQPAGLINGGNFCYVNSFLQVWFNVPEFRQLIYDFRPSENFVPPEAPRMNVQATMLALQDIFYTLQTTPFNETDKTSNLGKLLRLNSEQQDSQEFGLKFFNALERCLPDHPNGKETLKRLKDLFTGETCTRIVCKCGQRSEREETAISLTLNIEGYCTLLDALDAYFGEEHLDDFKCSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKYTSKGRQKLKTPMAYPREIPAKAFQRTNNSIPPPAEMYDLFAVTIHEGNNAECGHYYDLIKSPLNQKWYRYNDEAIEAIPKPPGTEKPTTAKTEKSRKKDKEKYPTDQKACYGLLYRRRDAFKPLPHPKLPPEELIIDSKTEIEELFEGLTKKKIEKSEKRLYDLERRINKVKISYGKLETHSDKYKEANEVVFLPTTLLQDVLAQEYEVAKGEKKKKKKEASENEEKKKNEEDEALSAAIAASEADQRDKASSEPSTSAAATEAGDDEELRAESETPNPENAESTQVAIMETDEIMDTTPTKDIDILAKAMEDNALPTVEVPQPELKKRTRQQNGEVKYVYSQRTPRKSHNGTNGTNSSPQKQPVSSRVAALLSSHEIPTCGHGKMSIDPILYGDVKAVSRAPAIALLREYDFRVKIVYDNGENVFPENEKERDVFIFTAEDICMECVREMREEGNFNNQLEDDEKLVRRILKEEKQRCSVKCPSERPDGYLYVAKFALSNFKKSAMSARENRLAQSHNKQGTLHFDSHPMFQQKSNSGYLTLSLKRTRGKPRKSLSEIPEKMQKLDEIGSKELPDEIIADEEEISENMGSDIPTKPVESINPDALVPFEKIEFNSELRCSHGGINFNQFRLSVSPEEWAHLKVYFDECYEVKCSDDVCDQCRQMEVDAQNGSENMRGLVREMRKRISDTLKTVESRAESKEDGADIKYGICSVFIDKLRKLTSRQSTSPPSICQECLLCPHQQPFKGFLNEDNHKDSHVVGLTEEEWNTFLTEIRKLEEAGDDQSIAVDPCPIPIENGQIVDMCEKCFEQHIKFTEEQKYMFENENIYVKLVNLNVEEDIAKANGKARRGRAKNLYAIKMSSTNKLMELKVQLYDKTHQLPNDQLLYRTAGGEQFDVSNNQKTLFDLRLSPNNNDNPLILIAQQFSPSASQADETGDRAPERGFVDTALAH
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Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin (By similarity). Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity). Required post-developmentally to restrict the plasticity of epidermal cells, probably by regulating gene expression.
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G5ECD6
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CHS1_CAEEL
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Chitin synthase chs-1 (EC 2.4.1.16) (Chitin-UDP acetyl-glucosaminyl transferase chs-1)
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MNDGENYWNAFRSHKRSATDGPTLSPWMVTVLQATKLLLFALCNIVLTLGSVFSKLIVLIMATNIVPRAHLIGKFARKCTKAAVRRTSTTTAGIYLSLLLIQCFPDTINLIRSGIDMWKGQCGQLVKSVVVLESLRAIGLAVLSFHVFPQLDLARCLVLSACFPLVAVLQRSLVAMVSAARTGRSFRNRLGRCFVAIPHVIMFLVLMSSCYVWALFDNKFTAIIALPIGVICTSAGFWESWIDTTHSGTSFDELYRLKYAVRKMNTTTKLIVSLMRIVCTVSVLVSAVYINDHKKLNSSHFVKAFFSFSTRQPHTRLLLLATGIIVLHFVMRGISRFLAALDLHPFSFVHPLSIAPLIAYGYVRYACQSPTCSIARRLARFGLHWVCDQWFQSARGIASPDFYICLIWLLVGCYRGWRLVRQRYFDTNEEIISSMPPVCNGLCIEQSLVVFQHSLNRQEKTMLTEEEDISDENDELRIRNDEVDRVSTVYGCATMWHETETEMRQVLRSILKLDVDHATRMNNKKANELRYRLEGHIFFDDAWEDVEEDGIEKRQPNEYFNMFFDLLNEMTGERLNEEGKMETRILVNTPYGGRLVVKLPSGTLLFVHLKDKKMIRHKKRWSQVMYMYYLLGHRIMDCPLSIEDRQQMADNTFILAIDGDSKFEPDALLRLLHLMNAKSDIGCACGRIHPIGNGIMVWYQKFEYAIAHWFQKAAEHVFGCVLCAPGCFSLFRASALMDDNIMHKYTKTASEPRHYVQYDQGEDRWLSTLLLKQGYRIEYAAASDAETYAPEGFEEFFNQRRRWTPSSIANTVDLLMDYKRASENNDAISYAYIAYQFLVIFFSMLGPAIIFTMLVFAQVAAFELRGSDVMLYNGIPIGFFIVLCFTTESNIQLIYAKYMSIAYAFVMLAVLVATSSQIVLETVLAPTSLFIVTMVGIFFFAACLHPKEFTNIIHGVVFFLMIPSTYVFLTLYSLINLNVITWGTREAVAKATGQKTKKAPMEQFIDRVIDIVKKGFRLISCREKKEHEERREKMEKKMQRMELALRSIESGADVKKILDATEEKEKREEETQTADFPIEENVEKTQKEIQKANRYVWMTSHSLKVCERGKLKSAEKVFWNELINAYLKPIKTTPAEMKAVAEGLASLRNQIAFTILLVNSLLALAIFLIQKHKNVLSIKFSPIKNFRWTKMNEMTGQYEETDEPLKIDPLGMGIVVFLLIILFVQTLGMLLHRLNTMIGAFQEVKNLYEYGVSPVINTKNDDERIMNNARLMINSLGVSTGHAADGYTRHRGEESDTGNVLYKLQKARLAKRMQRSALSTTE
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Essential for the embryonic synthesis of chitin, a component of the eggshell.
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G5ECD9
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AEX2_CAEEL
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G-protein coupled receptor aex-2 (Aboc, expulsion defective protein 2)
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MNSTDIIANVTKPFVENLTLGETAFYISCGIVGTVFNALVLWIALTYINTEDKPRQIIVINMTVADLLMCIVYMKTRPWLSHFNLWLCHPYYVIIWTCQMCSCLNLVWLNVDKLIYIQFPLHYYQIVNRKRLLWITAATWGGLYAMNIALVTFLKITRGSCLGVSLNPYVYLLSPIFYVVMILTSFSLSALIYCIAHNLTHMEERQRSKLFRRLFFLFSSTLWTFFTCLPYRLLYLFSIFCGETCQINNYYKTATNLFFRLLIVGIMINPVITIWTQRIYRLRLMRMFGRLRENSSTEVLMVSNRRASERPPEHTPLRCDM
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G-protein coupled receptor for the nlp-40 neuropeptide. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Plays a role in the defecation motor program, which is a coordinated series of three muscle contractions that occurs every 45 seconds. Specifically, acts in GABAergic neurons, such as AVL and DVB, to control the expulsion step of defecation. Required for fatty acid uptake and metabolism by intestinal cells and therefore regulates the levels of triglycerides in the intestine.
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G5ECE3
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LAM3_CAEEL
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Laminin subunit alpha lam-3 (Laminin alphaA)
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MRLWLGLLAVSNIALGGWNTSEDASIWENYVEDSNYHEFISSESERGLFPNIFNLATNSLITATDTCGQYTAEEYCKLVEHVLLRKTTNTQSPQCDICDANNVHKRHPIEYAIDGTRRWWQSPSLANGLRFEKVNITIDLRQEYQVAYIILKMGNSPRPGTWVLEKSLDGEYYEPWQYYAMQDAECMRQFGIPATTGVPRFQKEDEVHCTSEYSKITPLENGEIHTSLVNGRPGAENTSLELQKFTRARFVRLRLISPRTLNADLMIINKKSDSLDKSVTMRYFYSISDISIGGQCICYGHAESCPSDPVTGQFKCECRHNTCGESCNRCCPLFNQLPWKPGTNSHPNVCQQCQCFNHAHSCVYDDELDRNKWSITPEGVYEGGGRCLECAHNTEGFNCERCKDGYYRPSGLSHYREDACRTCECDPVGSVSDACVRDDQSAENGQKPGDCICKPGFGGRRCERCAPGYRNHPTCEPCPCNRAGSVNFDTCDGASCQCKANVEGIYCDRCKAGTIHLSASNPLGCQPCFCFGHSSTCTQGKWNKAQIINNIGWHLTDLTGGKDVKPEVENGEVLMFNANQNQDRSLYYWKAPDSFKGNMLNSYGGYLHYDVYYVPTEQGATVFVADVAIEGNGIKIEYHSRIEFLPREKMTVAIPMSELSGWYNAEARSPVDKADMMRALANVDRFTVRATYHQPQLQSSIFGLSLDTAVPAPDEIVEEDTSLKALAYHTQDTLMGGVEVCECPENFAGNSCESCVPGYRRVNNQLYGGRCEKCDCHGNSEECDPFTGECLNCRHNTTGSRCELCKPGHVGNPSRGGELGACEQCECPSLDLNPNPECISTELAVLGSVASNEDNYVCINCPLGYEGNKCEYCSDGFFEDPLTGKCIECTCNGNIDPMGIGNCDSETGKCLKCIGHTTGDSCESCKEHHWGNAQLHTCKPCGCHTQGAVNPQCSEENGECECKENYIGAQCDRCKENHGDVENGCPACDCNDTGSIGSDCDQVSGQCNCKQGVFGKQCDQCRPSYFNFTDAGCQFCHCNIYGSIEDGKCDQTTGKCECRENVEGTMCEKCADGYFNITSGDGCEDCGCDPTGSEDVSCNLVTGQCVCKPGVTGLKCDSCLPNFYGLTSEGCTECEPCPAPGQVCDPIDGSCVCPPNTVGEMCENCTTNAWDYHPLNGCKLCDCSDIGSDGGMCNTFTGQCKCKAAYVGLKCDLCTHGFFNFPTCEPCGCNAAGTDPLQCKDGQCLCNEIGECPCKKNVHGTKCDQCGEGTFSLDSSNLKGCTECFCFNRTSNCEQSDLVWQQMYAEDRRAVFQEPWEFYTKKHNINLLREKPSHFNSYPTDATPLYWPLPSTMLGDRTASYNGFLRFKIWNEDNRRGLHGIRPDQQYFRHFPQVIIFGNNRIELEHIPMEINDDGIYKIRLHESEWRVRHSPELTLTRKQMMVALQDTQGIYIRGTYTYPARGDAINIQEVSLDVAVPESKIVAGLSTTKAIGVEKCLGCPQGYTGLSCQNPEVGYYRKKHREYLNQADDIALIGWSEPCSCHGHSQTCNPDTSVCTDCEHNTFGDFCEHCLPGYIGDAREGGANACTKCACPLVENSFSDSCVAVDHGRGYVCNSCKPGYTGQYCETCVAGYYGDPQHIGGTCSPCDCHPDGSLHGACNPLSGQCECKPGVTGRTCSMCQERHAFINRVCTSCDQGCYLPLMETMDTMEEHLGRQNFSGLKPIPWKRVWRIGNESQDLSTFVGGIDKDGEIVKDSKWAKDAFALLDEVNFQMGRSNKSAVSIKQFTGIAEQLILDAQIHYANAFNTTNFLKMFAEHGATTVGGAALDGMLMEAEAHLNATVERGEYVEKRLNRAQQEHKKAEELLKMVTAQKLNETIFEDLKNRIDVLEQWMNDYRETIYDVSKKDTADAERMSLVVGKRINRYKEVSNEIEKLRVEAEDQIAYSRNSIEKARSEELMNMFEDKEKINMTLAELPDLVEQCQNITLLYSQLIDEYDEEYVQTAGRHAEKLEVQAQKIVDRFVDTRTETENPLKASHAYENIVEALKNATEAVDSAAEASEAVSKMLGSEGSESGDANEESLRSQLEKLKNESSLSNVDNSNAVKIVEELKKEKKDLTDRLGHLNELKTSIVKRLGVIKNEASSWDDKHDRMHSILKNGAKTAHERSANVKKESEGIKTEVSAIKAEVEKLMNSTSSGVQEDMEKIRASRTGMEYGAQKLTKVNKLSTANQGRTDKMARNIAILKAKIEQAREKAYQIRLSLNSGERGLCKRSYISPASPSPVNTFHVSYRPLQQVSDAVILVSKTKGRRTQPSEHLAVEIRDKRVVVHWDIGSGKKMITNSHPINYVPSNDRVTWYHIDVLRIGNAVNLTVALKESYDGGFKPRGAPVSVFVGNSKDDNSIFNTIPGETTIDVGTDETVASDIGLTTHKFSGIVGGLRIDEVPLPLWSFESTTGECEGATSPPKTSQRGHLFRDGFANVSMSVSERTMSAITVIFNAFSPNGLLYFRGSEASGDFVAIYLNDGKVMFKINLGGGSVAELTSQNVYNDGKEHTVKAIRTGSEMYLQVDSDADRFNTVITGENTALNIENENHYVAGVPMTLNKEVFGDINWNGFIGCILTVKPSQVGELDLDHPEHSQGKTDGCSQVSGVTDKIIGFPKPGYLITKGISIDNSSTFAFSFRTREENGTLVYQSSKLQKVSKRDSEDDGKGYIAFYLFRGYLVLHFGKDASSRKEVVTFRSSHPYNDGQVHAVFMERNGKIISVKVDDKEIGDSQSLSDETSVGTTSGRLILGGFSDDLKPPNNEIPITSFFIGCISDVFLNMKRVSLAPEKHNAQIGMCSMDDTQGLSPIDDPIDGNGHNGHRKSSKLSFEATNRNYYEVSTQSSHLVMNPNGEETVEKTCETSLGSLQGAVRYGLSKSSHSRINFEAPYPNITDFTVKLSLQTETSNGMIWAWANYKNYTRYIFLDIIDGFATLEVKGHKQPKILKHLGNRINDGQWHDITVEKKNRSLKLIIDSLGPVEMTDCPTPKVMKKRVYVGGVISRHRRQFGLTTPGLDGCIRDFEMNNRIFNNLDEPSTSKNVMPCAKACKLKRSSKRKRNSKN
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Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components (By similarity). Required to assemble a stable basement membrane and for organizing receptor complexes and cytoskeletal components to the proper cell surfaces. During embryogenesis, does not require the presence of collagen type IV in order to associate with cell surfaces, prior to assembly of the prototypical basement membrane. Plays an important role in muscle contraction of the body. Probably plays a distinct role from the related laminin subunit alpha epi-1.
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G5ECG0
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TACC1_CAEEL
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Transforming acid coiled-coil-containing protein 1
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MSLNTTFTKEDGTEVVIPFNGSQNGHPENEEPEVEEAAEPSSSVETLCGATRGDIIVMKHTTKALTELIERLLHSDEFEVRRCSNGQIISQGRCNGTTPGNGIGGGGASSEELEKALKDRDAARAEADKLHANYATLFASFNTVREAANDIRGEYEDARDKLKLAAAEVDEWQAKFLAVKDNANSELERASVEYDDLLRSHDENTKGLRLRVKRQEIELSSKNDEIKVLTNRVSELSQICDQLLNDVDVSDGMSVISTDA
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Involved in microtubule formation, polymerization and assembly, regulating microtubule nucleation and length. Plays a role in pronuclear migration and mitotic and meiotic spindle elongation during early embryogenesis. In complex with zyg-9, functions during the early stages of embryonic development to regulate microtubule assembly throughout the cell cycle. Specifically, the complex is required for the formation and growth of astral microtubules and spindle microtubules during mitotic spindle assembly. At anaphase, the complex is required for mitotic spindle positioning in one-cell stage embryos. The complex acts in a partially redundant manner with the tac-1/zyg-8 complex to regulate microtubule assembly and processes during interphase, mitosis and meiosis in embryos. Plays a role in injury-induced axonal regrowth, regeneration and microtubule stability in PLM neurons and this may be downstream of efa-6.
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G5ECG2
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FOS1_CAEEL
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Transcription factor fos-1
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MFEQPSSTTNTTTSSGSGSDSNHYFELGPRNPINQAHPTSVIVPPRQHHHQIHQQQTDNSPLTPCTPYYPSNAYGLPLFFGTDFLQFQPSDIPSPLTPNISSPLTPHPFGPIPAIPTNQIYNRTFTDFYSTAASSPMVQYSTVKKSSAGRKPKEEDNMEDDDDDKRLKRRQRNKEAAARCRQRRIDLMKELQDQVNDFKNSNDKKMAECNNIRNKLNSLKNYLETHDCKLSREERTHEINRLIIPPSTVPPSQPYLQHSLRVHPPRADSVPYSIRSGHSSSSSEQHSPVEDYKPSIDQLLLPPISCIQNIKDRNINSMPPPALPASTSAAGIHVITSIPVSHANSLHGRSENVFAEPERKIPKIELDQTLTSLTMPDDVERPSALPTLSRIVENQPITTPSRPFRLGGEYQNQTPQSTGNGLFGGPPGPFDLLSSNTGLTPSGQPTMNFVSTPTPIQPHPDADLRPL
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Developmentally regulated transcription factor which binds and recognizes the enhancer DNA sequence 5'-TGA[CG]TCA-3'. [Isoform a]: Plays a role the development of the reproductive system, controlling events including anchor cell (AC) fusion and invasion. Regulates downstream transcriptional targets, including zmp-1, cdh-3, him-4 and mig10b, to promote the removal of the gonadal basement membrane during AC invasion. Regulates aff-1 expression to promote AC fusion. With jun-1 regulates egl-1 and lin-12 expression to allow uterine cell specification and development. [Isoform b]: Required for ovulation. Controls plc-1 expression in the spermatheca to regulate spermathecal valve dilation. Acts with hda-1 as a downstream repressor of the kgb-1 mediated stress response pathway that transcriptionally represses genes involved in the response to heavy metals, such as kreg-1.
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G5ECG7
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MTP_CAEEL
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Microsomal triglyceride transfer protein homolog (Defecation suppressor of clk-1)
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MFSSRIWLLLAVTVGVCLAVPDLDEIKKNLRKHGPDYYKNQPKMNENTVRLLKVDYWFRTESMIYDDIDNKEKDPSTVIAGNFSFETLHHDVEGGMLGRFTLTQCNTDNCGNPSPIYIAFRQGGNNAEHILKASDESDATWNFLYAIVNTIYTPAEYGEGDEQTVDTIYGRCFVNFGRPEDKRFRRIIEKCDLGYGTNFTKFEGIESVQYDQDVWYTQNTKVDADIIMVDAIEMLAFKSPLHEKYGFTLESRTHVEITNRTRVFVTSYCNDTVPSAKCAEQAFGAVRVGGKLYEHVKIAQEQSNKLTKLIGTYRRHLQDMGDSHICEKHSLLYSQIAQEARLAKRQDWEAAIQYPENDHVLSLIASALGGVGTAESITTAREVLLTASPDYLDDLLFGISQSSSNNEKWHKQLMYWLGSLDKKSEEYWKVANTIATVLNKRCEASTSSLNSCNKGKETIVNKFITDLTAGGVEVRVLEVLENIPIFGSYTFAKKFICETESEDVQKAALNVILAASKNLYETQLTHKLIKLFRNTCSQETPTSHSQLAIDILLKCVPDHQNVATLILRTETLNPDDQEKWHYLYKAIEASGNKDELKAEFWSRMRKFKVFRPNFLHRALQADSHVHWQEIADASNFQLFSTANTEFLQKSFKRSIFELSMKKGRKEHNLFSLSIDTEHLEQFVTGSASSRSGAPQGSVRIGVAGHKLPTHHIFKGSTDLLSTVWEADGRTHKAFEGHVPVRDVRLSVPLLSGLTLDVDSVGAISMRVLASAEVSLWNQRSNAKAEAYTSGSLHLTASLYHHSEPVRHVESTISALSTFTTDTRAIFETLPYDFCLRTSNSNVDINQKTVVQDQIGKHKKKTLNRKRVHPGVTYRLDDSTIRQCNSYLEQFRL
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Catalyzes the transport of cholesteryl ester, and phospholipid between phospholipid surfaces (By similarity). Does not catalyze transport of triglycerides. Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B. Required for normal expression of klf-3.
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G5ECH5
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PP4R1_CAEEL
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Serine/threonine-protein phosphatase 4 regulatory subunit 1
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MIKSQFATLIRVLIDFQKFWVFLSIFCTFLVVFKFDNLMFQKVRRVFQQNRKNSESIQPKLSTVSGSNSGEGMDKRNTGFSNLQQLGGAIFIDDAEDEPPRVKSSEDSRPAPHWLDSPRDSTTLPDIIASTYSDFIDEAEYATKQMLAILETLNPIEEYIELFESSFKAIEVRLPFDVILNDEKKPDWDAIRRKLIMGSLTVNTTSEKPGITTNQMTAIFDAIPFLFDAVACNPELYEYQNTLSMIVMIAMTGNSMIRRQSINAVQALMERNMLDQDFMRDGVVPGLFNIYQSGVGAFQSNDLRMECVQALCQVISYDAIHDRRWLFDNFLPRFSQMLKDPTMHVRKSALHIFGNLGNMFGQKFTEVFLVPHLITLSCDMTWAVRKVACEIFVKVAECASNQVRIDILSPNFVRLLNDPNKWVSFIAYQQLGPFISLFANPDITGLELRNGQVVVRDPVVLEPSVTEQEDPSNSTFSEDTSDDFRTLPKDTWLPEVDFNDDFEYQLGSIDNTQNQKELTTVTTALVKTPKRGERVMDSVLSGINKMFGSLERSSPKSKEVEKIAATFSSPSKRSPLSLHSAVSLIDKFSKRSNPNNPQRFPVFDSANSDSTLSSNSSNNNSSEQQNSTGIAAKCSSTDDLTKLGLEDDDSPDAAEDSDDFTSETRTTSPRGRRIATNAWSKLDIRQKIFLRRLGALPPSFPKKKATHSSSSSPRKSPTRSPLLSSRKKGLLFDFAAPIEIKSSSSDHSETIPVRTANQQQEKADDDKLNTDERQQYMENSGPKFNTDEDSTNDSDSDDEDNDFEKSFVADEDDGEQDDSPLSIEIKSSSSSDFESVSAATPTSQEPVSNEFSLTYWSSNYAISSIEDELKPFGSSSSFTNSPTSNSYLESRFDVMKVNLSPRARSVSFGTNGSPISTSPRRKANSTSEPSPPNTGNLKSDDSIVMLNTEEKEKLGILDFDEMNMSISSNSSIHGEAAMTEDSDISLTSIEQAALQHVPVDLVESYMRVMGPIGGSGSGGGGNGSSTTIATGDPSLCAETYRHCAHNFPAVCYTLGRAAWPRLKLVFRKLAMDEQARVRQSISHSIHEIANMLGQEITDEDLLPVFYDLRNDQNPDVRNGILIHLYDFVKFLSPEKRDEMILSLPQFFPIGAQPGNQAQNGDWRSRFELISQLSKLCSLYSIQDVNFHMSGIALTLADDRVAEVRREAVMLVSTIVGALVTAEWDNIKGVRDIENGHVDVKKKSNKTDFLSEQFVDDIVSSFAKTQKWTRRQTFCFICAQILRDKQCDGIQFRYFFATPLQQLAQDKVPNVRLASCEALSVWRKTLIAARAQERRGQSPISSPASEPSAIRRDINLVSDMMVKLSNDSDIDAAFIAKKCQGLTDDHQPVDVASRTTRMREREEQFFGDIILSYSPGCNARVSGKEIKQLIRHDQGAVQKAAPLQSMEDFGDEILAHAADSVNIQTPPEVVATVQRVSITNEQFEDNTEAVDMEIEEDEDENSTEKKENTEKTAEEESENVKNTEDELDIPMDPAPTLPPPVTSKNQSSSPITASSSDNNETSA
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Probable regulatory subunit of serine/threonine-protein phosphatase PP4 which may play a role in meiosis and embryonic mitosis. Probably in association with catalytic subunit pph-4.1, regulates microtubule severing during oocyte meiosis II by dephosphorylating and likely activating mei-1, a component of the katanin microtubule severing complex.
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G5ECH7
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CDK5_CAEEL
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Cyclin-dependent-like kinase 5 (EC 2.7.11.1) (Cell division protein kinase 5)
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MLNYDKMEKIGEGTYGTVFKARNKNSGEIVALKRVRLDDDDEGVPSSALREICILRELKHRNVVRLYDVVHSENKLTLVFEYCDQDLKKFFDSLNGYMDAQTARSLMLQLLRGLSFCHAHHVLHRDLKPQNLLINTNGTLKLADFGLARAFGVPVRCFSAEVVTLWYRPPDVLFGAKLYNTSIDMWSAGCIFAEISNAGRPLFPGADVDDQLKRIFKQLGSPSEDNWPSITQLPDYKPYPIYHPTLTWSQIVPNLNSRGRDLLQKLLVCNPAGRIDADAALRHAYFADTSDV
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Proline-directed serine/threonine-protein kinase which, in several motor neurons, promotes the polarized trafficking of synaptic vesicles and dense-core vesicles (DCV). In the ventral nerve cord, phosphorylates lin-10 and thereby prevents lin-10-mediated anterograde trafficking of the glutamate receptor glr-1. Involved in the inhibition of glr-1 trafficking in hypoxic conditions. In DA motor neurons but not in DB motor neurons, regulates axonal transport of synaptic vesicle precursors by inhibiting dynein-mediated retrograde transport. Regulates the trafficking of dense-core vesicles in DA and DB motor neurons by promoting anterograde trafficking to the axon and preventing dynein-dependent trafficking to the dendrite. May regulate these processes in association with cdka-1/p35. Activity may be regulated by cyy-1. Involved in synapse formation during DD motor neuron remodeling by regulating transport of disassembled synaptic material to the new synaptic sites probably by activating the motor protein unc-104/kinesin-3. Regulates microtubule polarity in the dendrite of DB motor neurons. May also play a role in GABAergic synaptic vesicle localization in the ventral nerve cord.
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G5ECJ0
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GBR1_CAEEL
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Gamma-aminobutyric acid receptor exp-1 (Expulsion defective protein 3) (GABA(A) receptor)
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MSASILILATCHQVLADFNSYVVPQPHAQRDHRQDISQHYDYLMEENDEPLGRGAAPSKYRSSHGQAQHRPEMTESENFAQPNTESVFSSGGVDSYGETRDFLQFLRRIQYDHRQVPENEKGEATYVEVSVVVSNIRAVSEVTMDYALELFYRESWRDPRLQYDRKLFKNKTELALHESYTNFLWFPDTFVPNAIASKNPQRNSISHRSLLRLDETGKLLYSRRISLVCECTMDLTLFPFDKQLCKLGIESYGYTADHVVYKWSKGARTALELKKIRLPDFTIQEAYVTSQMESYATGNYSRLYVCFVFSRSSGFCFLQLIIPSTAVVITSWVSLWMETETEFQDMISIILAITFLIFSYNEMMPRVSYIKAMDIYLGVCFMIVFLSLIKLALVKYMRQKIMLTSDSGNSLREMSQMSTRQRLRARKTSNMNFRNNGGGSIPINEEHQQMLTVPNGEDKMANGDDKEANNNGKSHLSDMLEIRITQRTMHRFHWISQMLFFFGFVIFCLFYFLIYPNLHIVSVDPACDKNLAEWFADIY
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GABA receptor that functions as an excitatory cation channel. Permeable to monovalent cations such as Na(+) and K(+). Has negligible divalent cation permeability. Does not act as a chloride channel. Mediates enteric muscle contractions required for defecation. Probably by regulating the defecation motor program, required for fatty acid uptake by intestinal cells.
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G5ECJ6
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CSK1_CAEEL
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Tyrosine-protein kinase csk-1 (EC 2.7.10.2) (C-terminal src kinase)
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MSNGNSYNHHHQFPMSIPISCSSHSIQSQSRMNTLNANRDLLSPGNDVIVTRTVSPSFYSHGMPARDNVFRKDDHVRILGNTTDPAWYRARNANQEEGLVHADCVVRINGQAYDNGIVRMRASGCDVAPGAASTTSSTSSHHSTAANHQPWFHSMISRENTEKLLRGKPDGTFLVRESTNFPGDFTLCMSFHGKVEHYRIEQTSGGQLTCDKEEYFSNLTQLVSHYKRDADGLCHRLVTPIICETATFSSNGSSSFGSSSTVDLEDRTSVFRHAGLVISSNDIDVGDTIGHGEFGDVRLGTYKNRKVALKVSKRHGNGMLDSLLDEAKFMVGLSHPNLVTLVGVVLDDVNVYMITEYMANGNLIDLLRSRGRHALERRQLMMFAMDICQGMCYLESKQIVHRDLAARNVLLDDDLVAKVSDFGLAKKANSQSHDSASGKFPIKWTAPEALRHSQFTTKSDVWSFGILLWEIFSFGRVPYPRIPIQDVVRYIEKGYRMEAPEGCPPEIFKVMNETWALSAQDRPSFGQVLQRLTTIRNTV
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Non-receptor tyrosine-protein kinase which plays a role in pharynx function by regulating pumping and the orientation of pharyngeal muscle fibers, independently of src-1 and src-2. May phosphorylate and thereby negatively regulate src-1 and src-2 activities.
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G5ECK3
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MAB23_CAEEL
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DM domain-containing protein mab-23
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MPKEQYMCQLCANHGIFNQPKKGHKQKCPYRTCPCSLCALNTKRRALDQIERQLKHTNEPMTGQTATSMASPTPECPLSPTTPKMTPHTPTSGKDTFRNSISSSNMAFTVQLPATITKKELKLLRRDDTPLQNSLERPFPRSIDEAIETIKKEKMSSIFHSAEMLAVGESATSLI
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Probable transcription factor that plays a role in the development of the dopaminergic neurons of the male-specific genital sensilla (simple sense organs) known as rays, by negatively regulating the activity of the transcription factor ast-1. Involved in male mating behavior, probably as a result of a role in the differentiation of male-specific diagonal muscles. Required for development of the male proctodeum. May be dispensable in hermaphrodites.
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G5ECL2
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SYNJ_CAEEL
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Synaptojanin (EC 3.1.3.36) (Synaptic inositol 1,4,5-trisphosphate 5-phosphatase) (Uncoordinated protein 26)
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MSVRGIRIWRRNDARFQPSILVEKNGLDGSLLFQGGAIATLDSDSTDVERRSYQKIVDAYGILGVLAITKDEAVLVAVTGVLSVGQLYGADILKITNVEFISLRTFGSVENVDSRIIDLQRLLSSQMFYFSSLQSYDLTRSAQHRDSHDCSDARFFWNRSLHFSFQRYGIDTDNWLLKCMAGSVLVRVVYVGANTGRVALISRLSCERVGTRFNVRGANYLGNVANFVETEQLLLFDEKECSLLQIRGSIPLFWEQPGVNVGSHKVKLRAFETSLPAYHRHLSQLQHRYGEFAIVNLLGRKEGERVLGDAFKTQHKSSHFAPLVDFIDFDYHAQMKISKEAIVQLKKKMSPHMTKHGFFYSMGKEIVKRQTGVIRTNCLDCLDRTNAVQTAIGLQMSHDQVAFLNLNAGKVNVEQRVEEILRDLWQKNGDQCSTIYAGTGALDGKSKLKDASRSLARTIQNNLMDGAKQESFDLFLTGAAYDPRLFDRACNILPPSLIQESYYYHEYADAVSQLVERSPEIAEPQSIKIFVGTWNVNGGKNIHNVAFRNESSLSHWIFANSMTRLVSVEDEQLADIVAIGVEELVDLNASNMVKASTTNQRMWCESIRKTLSEKAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHFAAGQNEIRDRNEDFATTLKKIRFPLGREIDSHDVIFWLGDFNYRINLSGDEVKNAVRNGDYAKLVENDQLTQQKALGQTFVGFNEGQLTFAPTYKYDTFSDDYDTSEKCRAPAWTDRILWKDQRKKGKTQLLSYDRSELKTSDHRPVGAVFKVETFKVGGRKCVELIEDVVESMGPPDGTIIVSIAGKPRFPPQMFPPIHEKLKELGAQVQLSKFDDGDLWIVLNSGEMALAALSMDGLKIGGTDQINVKLKSPDWAYALKPHLSDFDLESFEVTAEEEALLGGTDGAVFEFADEDEDAISVSSLTLTGSAPDRPRPPSARSEAISVAKLEWPTEQPNVLSTSMPTRASSASLANSSWYEHVPPLAPPQSNNNKSPPQACLFNPFTQSAPSPAPPPSTIPLPPTRGASVGPGPPAVPVRKAPPPPPRPVIPPRPKNM
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Probable inositol 5-phosphatase which regulates synaptic vesicle recycling in neurons by regulating clathrin-mediated endocytosis.
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G5ECL4
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BRAM2_CAEEL
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Neurexin-related protein bam-2 (Branching abnormal protein 2)
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MSSERRKDNPLRFALILHLLAVLVQGDIQPRFSCYNHYLAGIRTSSVLPISGHSSAPSNVKCIFENDVAFTEIHSALENSYQVMGKKSVNFQVLDLFHLRELVRRSHCTQTLTVTWKNVPEAGKGGLKVVSLLNETTRIEYSGDERQDFLFDETFAGVRHLIPDEDDNESNPTVTTTRLLCKHIPQPECLVRGKFEVDLEANLEWSYAFSFKTDITNQTLFTLRCGDTTSEVRLENDFFIRADGNAPVAVTHLSDATWHTAIVKHNQPDSHFLKIDDFPEIELGKSISDDTDKTITLSISVNGNIQLIDPTDTNDDCMYSFDKPQKRLQETVSTRTMCVGCGCPKLSGTFDGLSKCDEEDENSYNLRRDVDRLSFIHIDNAFDIDSNGAAIPAISTSFKSDSDVGLIFFGYWQNFHGKGRLQVYYHYDTISAVFCKHTDDEECSSCSIRSSEGFGKDQWIQTILWGGGDEIHLAVDSSVCRLQQLSNISLAEVYAIPQISGGAGLFIGGTWHEKKRRGLYKADAEQKYFENTREKAPVLRGCIKDVFVRGSKTDVSEMFEVQKQAMLNEPDDSNAFAVRKYCQSCIPACSEGTRCRSRAPLQDSAMICDCADELQFNTSEGTCNRERDTPVALSTAFLSENQIVLDIQNTKAILSKVWLKFALPKQINQAQRIVEFNSHRETLFNINLETDGTVNVQLHGQDTASRQLNLLDDRVHLLQLQRRTPMGTRHSAKKYDLYIDGFHTVVSDIGKLVLNNVSVTAAETEDEWSSVIVHDLGLSYEYDEHFAISHPSNVIHQVDLHSQLLPYQIRAPDLSKTGILDDSLWEKPAYVTDSEAAPVLESSPHGEVVDFTADIIEPEQLLSGRWILYSLFLTILLCLFILMCIVCYWCVLRPRAMRRTDTGSQRTIIRDSPDYAPVKMRRDSIGGISIDDDGSIGTDDTDLQAYRDIPSHRVKIYRESMVSILVPSIDQPAEAAIVKRSHSTISDQTPSRPHDTSHAPLVAVNDD
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Maintains the normal guidance and termination of axonal branches of VC motorneurons. By associating with cell adhesion protein casy-1, mediates axonal interactions to establish synaptic connections between the male-specific sensory neuron HOA and the AVG interneuron. Plays a role in regulating male mating behavior.
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G5ECM9
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CPI2_CAEEL
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Cystatin cpi-2 (Ce-cpi-2a) (Cysele2)
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MKAILVFALIAISIISVNAGMMTGGSVEQDASQKEYSDKAWKAVKGINDQASNNGPYYYAPIKVTKASTQVVAGISTKLEVLVGESNCKKGELQAHEITSSNCQIKDGGSRALYQVTIWEKPWENFEQFTVEKIRDVTADEQF
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Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation.
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G5ECN5
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STRD1_CAEEL
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STE20-related kinase adapter protein strd-1 (STRAD STE20-related adapter homolog)
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MADTTILDTTCSSTLAANVEFSHATDSAIGISLKNATITEAEGVPNLKETGYDCVRYMGTCNGGQIYLGRERKKLKDYVAIKKFAIDDVDDYAAIAKESSNLRLMHHPNIIELCECFVYERSIYQITPAMNLGSLFDIVFEYMKWGINEKSAAAITRQLLDALSYLHQRRYIHRDLKPKHILIDSSGNVKLSGFRFMIELNHHLDCVFEFDAHLQNQLYYLAPEVLAQNIHGYTSKSDIYMLGISICEAINGVMPFGELEPLEMLHRKLNGQVPRPVDMISLKDDQKMGLDISHRPQEHLTRRFSKEMHEFIANCLDYDPQQRGSASDLKSSAWLGSKIHKNLGPVDVRQELNLDYAHFDLSLWEQEPLIPMEPDQKYEIVFDYSPIS
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Pseudokinase which may act as an adapter for kinases sad-1 and par-4 and thereby is involved in several developmental processes. Regulates cell-autonomously both neuronal polarity and synaptic organization when bound to sad-1. Required for sad-1 localization to synapses. Required to establish germline stem cell (GSC) quiescence during dauer development, to promote cell shedding during embryogenesis and to control asymmetric cell division of the Q.p neuroblast lineage, probably when bound to par-4. May be involved in maintaining the integrity of the early embryonic cortex when bound to par-4.
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G5ECN9
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NEC2_CAEEL
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Neuroendocrine convertase 2 (NEC 2) (EC 3.4.21.94) (Egg-laying defective protein 3) (Kex2-like prohormone convertase 2) (CELPC2) (Prohormone convertase 2) (PC2) (Proprotein convertase 2)
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MKNTHVDLICVFLSIFIGIGEAVDVYTNHFHVHLKEGGGLEDAHRIAKRHGFINRGQVAASDNEYHFVQPALVHARTRRSAGHHAKLHNDDEVLHVEQLKGYTRTKRGYRPLEQRLESQFDFSAVMSPSDPLYGYQWYLKNTGQAGGKARLDLNVERAWAMGFTGKNITTAIMDDGVDYMHPDIKNNFNAEASYDFSSNDPFPYPRYTDDWFNSHGTRCAGEIVAARDNGVCGVGVAYDGKVAGIRMLDQPYMTDLIEANSMGHEPSKIHIYSASWGPTDDGKTVDGPRNATMRAIVRGVNEGRNGLGSIFVWASGDGGEDDDCNCDGYAASMWTISINSAINNGENAHYDESCSSTLASTFSNGGRNPETGVATTDLYGRCTRSHSGTSAAAPEAAGVFALALEANPSLTWRDLQHLTVLTSSRNSLFDGRCRDFPSLGINDNHRDSHGNCSHFEWQMNGVGLEYNHLFGFGVLDAAEMVMLAMAWKTSPPRYHCTAGLIDTPHEIPADGNLILEINTDGCAGSQFEVRYLEHVQAVVSFNSTRRGDTTLYLISPMGTRTMILSRRPKDDDSKDGFTNWPFMTTHTWGENPTGKWRLVARFQGPGAHAGTLKKFELMLHGTREAPYNLIEPIVGQTNKKLDTVQKAHKRSH
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Serine endoprotease which cleaves preproteins at paired basic amino acids. Processes FMRFamide-like (flp) and neuropeptide-like protein (nlp) neuropeptides. Probably by processing flp-1 and flp-18, modulates the neuronal excitation-inhibition balance and thus the level of activity of the locomotor circuit. Regulates sensitivity to mechanosensory stimuli. By processing neuropeptides, modulates basal acetylcholine release at the ventral cord neuromuscular junctions. Probably by processing flp neuropeptides, regulates the turning step of male mating behavior. Cleaves pro-insulin-like proteins ins-3, ins-4 and ins-6 into their mature active forms. Together with convertase kpc-1, cleaves pro-insulin-like protein ins-18. By controlling ins-4 and ins-6 processing and thus the activation of the daf-2/InsR pathway, negatively modulates synapse development and synaptic transmission at neuromuscular junctions. Similarly, by controlling ins-4 and ins-6 processing, negatively regulates dauer formation under optimal environmental conditions. Under adverse environmental conditions, may promote dauer formation by processing ins-18, a daf-2/InsR antagonist. May cleave dense-core vesicle membrane protein ida-1. Involved in egg-laying, fat storage and locomotion.
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G5ECP4
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PIK1_CAEEL
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Pelle-like serine/threonine-protein kinase pik-1 (EC 2.7.11.1)
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MDDSLGVSEVVMIPFMKREVLQQICAILDTDNTWETIAPYMPGIELRDVEGCKRYSSYNQSPSELLLRIWSSKGYSTTHLYQLFAKTKLIRLMRMMRSQVHEKYHYLENKVTNSTSRVSKQMVQPPGSQSASRLKKTEIKESSPSPAAAAASQLSRSNTDDTLRVAIEGTLPVTYCELLEATNGFAVSNVIGKGGYGTVYKGELKGTGGIVAVKRLHSGNDTSQNGSRERLRQSLTELRTLARFRHDNILPIYAYSLEGSEPCLVYQFMSNGSLEDRLLCRKGSVPLTWIQRKEISIGAGRGLGFLHSFGKTPIIHGDIKTANILLDKHMEPKIGDFGLCRDGHVEAEAMEKHPLIASHIKGTLAYLAPEFITSKILTTKLDVYSFGIVLLEIASGQRAYSDSRETRGLVEYCQVNKELAAHRKIPVREIFIDRRAPPLVGDEEKSFLDALIEVGLAGANNDRKVRPTMSQIVEYLCKNSIPPVV
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Through association with the adapter actl-1, may act downstream of the receptor complex composed of ilcr-1 and ilcr-2, which is a signaling complex that modulates neuronal activity and animal behavior in response to sensory neuron input.
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G5ECQ2
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FRIZ2_CAEEL
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Frizzled-2
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MLLRISVLFLLLGSCGALFGKRQKCEQITIPLCKGIGYNMTSFPNSYGHEKQEEAGLEVHQFYPLVEVGCFQHLKFFLCTMYTPICQENYDKPILPCMELCVEARSKCSPIMAKYGFRWPETLSCEALPKMSDQMSTGNICAAPPDTPKKQHKGHHHKNQNQNQNQNHNYSPDGPEVGISKIDNEVIAGPSECQCTCNQPFQFVASEKSKVGNVTNCAYSCHSPALAESHSLVSNWMAFWSITCCVLASFTFLTFLIETDRFQYPERPIFMLAFCQLMVAVGFMIRYFVGHEEIACDSMRIKGADDNSGSLCFVVFLLTYFFGMAASVWWVILSLTWVLSAASKWSPEAISSFSFHFHVVGWCLPAIQTVLVIVFNAIDGDPITGICYVGNTDLQFQRIFVLFPLLVYFIVGVLFLVIGFCNLWSIRNEVQKQHPSLESAHKITQLMSKIGIFSLLYTIPSLLIICVLFYEQNHRSLWEQSQLCSCSPKQTIGDSSLIISLIKTCCMCILGWTSGFWVCSTKTLSSWKNAICCLGSSRSLPKYQPADILYAKSDMSSSQFYNTSLRHNHLYGGIPDKL
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Receptor for Wnt proteins. Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of gsk-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of gsk-3 kinase. Both pathways seem to involve interactions with G-proteins (Probable). Required for the migration and axon formation and guidance of different neuronal cell types including canal-associated neurons (CAN), hermaphrodite-specific neurons (HSN), anterior lateral microtubule neurons (ALM), and the right Q neuroblast (QR) and its descendants. Directs ALM migration through frizzled protein mom-5 and Wnt ligands cwn-1, cwn-2 and egl-20. May act redundantly with mom-5 to direct CAN migration. Plays a role in the organization of head ganglion cells. Probably by acting as a receptor for Wnt ligand cwn-2, plays a role in the positioning of the nerve ring and may in addition positively regulate the neurite outgrowth of RME GABAergic motor neurons along the anterior-posterior axis of the body.
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G5ECQ3
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SEL5_CAEEL
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Serine/threonine-protein kinase sel-5 (EC 2.7.11.1) (Suppressor/enhancer of lin-12 protein 5)
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MPLGLFSSGKAQVLCDEKIPGGKKKEPKQLSENKCKGVTLKLDHTRVTIEKQIAEGGFAIVYVASDRKNNKFALKRQFTKDNEKQLEACCREHSFLKQCIGHKNIVEFVDSYTNCLGNGIWECMLLTEYHQKNVLQLMNERISQNQYLTNDEILSIFTDLCEAVSFIHNRPQPIIHRDLKVENVLISSHKPPHYVLCDFGSATTQILSVEKYGVEYVKSEVERNTTMCYRSPEMIDFYSGLEIGLKSDIWALGVLLYRLCFFCVPFEESPLAIQSVNYQFPSVPNIPDEIKVLIYMLLDIDVNRRPSIYQTSVLAFEANHRKPLSEEIQNKKCTDAVPSLKSCIQLMRDGSNPRNKRDSSPRNPEAPPIQSSSKMASLSQQVPSISNISMPSGSGTVETSVAPRLRPKATTVVPNVPSISPVPPVGLPHLRLPSKGSTDETDGSQVRKVPIDFHHRQSFSGEEQLKPAAEADSAGPLSCPLIKPTDLGFTDLDKPALPRDRAQTDGKRRLPHESDIIFQQQHRRNVSDTSQISRSAFKPYSSQQTTSKTSSQVVRSVEDMSQRQNGGSGEWNPFLVAPFSNNSISRKDGQESAFMMDDSHFGMVFDEIRRKEIPAELDSETSSIDSRDPFGAAPFDQLTVSTSSSAQPVSLPPATDEDDERQLLSETDEEEKYEIDEKEEIQTKKDETINEEDSEIDEQRMNDRRRYSYENIDGVGDDASSDSRGKTDRDDSEEEEDDDSRRGGDTSHDEDSQNTVGSEDGEGGSRPLLEDDGLEDDDDHELISSFSSSSTNYPPLFIGTSTPHTQNPITNPFLRDELTPKMIITAPLPTAKNNLDDDWDLGDRWTDRRDTVFERPASEHQNVFAPATLPRQATPLVCRFKPDLPTAAPVSIIPSMSNTSFPEAVRDSDTVPCEPIIGTLISVGAPTDPPPPPLPKKPTEASPTQETTATIPVALGKKEKLLKKEKKKEKKDGKKDKLKLEEYREKGSSEPETDGSEAEIWTNDGATTFSNKKKKKSTFGLRSSHPSIVANDLQFSSPMPPVVKKSSKDKKSSLTGKNASFVNTSFQPEDHDDPTDL
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Serine/threonine-protein kinase which may play a role in lin-12-mediated cell-fate decisions.
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G5ECR9
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UNC55_CAEEL
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Nuclear hormone receptor unc-55 (Uncoordinated protein 55)
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MQDGSSGAASLGNSSPDATDCVVCGDKSSGKHYGQFSCEGCKSFFKRSIRRSLSYTCRATKNCAIDVQHRNQCQYCRLTKCIRMGMRKEGRRSNETQTAVSAVQRGRLPVTMPSLFPPNMFLRSPFPFMSVPFNPLMTAQFTKPSIKESIFEFAAQTIFATVNWARTSMSNLVKGDQLILLRHSWTPIFIFALAQSNFALNLSTHLTAVTATAASTENGSSSLGSKSEDEEKSEEKPERVFDEPQFQGFQAKIDKIRDFHLDVVESSSLRAVLLFSCDEEALEEKGKIEEIVEKLKSAVDEYCKMNKRSERYHQICECLQLLKSTRNLPISRLFFSRLLGTTPLETILSDLLITPPPPTLPFFPQLPSRN
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Transcription factor. Involved in motor neuron fate determination and maintenance, acting as a transcriptional repressor to counteract gene activation by transcription factors unc-3 or irx-1 in subsets of motor neurons. Probably acts by binding to specific promoter elements. Required for ventral D (VD) motor neurons to adopt their normal synaptic pattern. Suppresses expression of flp-13 in VD motor neurons to ensure formation of the correct synaptic pattern. Maintains low cAMP levels in VD motor neurons by enhancing expression of pde-4 which hydrolyzes cAMP and repressing expression of acy-1 which catalyzes cAMP formation. This prevents respecification of synapses by VD neurons. During copulation, required in males for correct movement of the spicules, a pair of prong-like structures which are inserted into the vulva of the hermaphrodite and anchor the male to the hermaphrodite. Required for spicule prodding which allows detection of the vulva location and for spicule insertion into the vulva.
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G5ECT0
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PBO5_CAEEL
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Proton-gated ion channel subunit pbo-5 (PBoc defective protein pbo-5)
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MTRLSILQHLLTFLILSKINATSTTESYFDSSEEAPNVLLNHLNNESEGEELTQINDTQPAFVPGSSKRLTEYLLSRHNLNAPPDGLLYVEYELELVHILGIDELKQTMTVLIYVDEHWVDPSLTWDPALFGGITKTWIPLDKIWVPDIIVFNMVKSNRLAHEDLLSAVRAPARIHYNGTIVASHPAVHTVSCEINIRHFPLDDQRCAIEIASWAYGQEKIRLHAHTDHSLEHYKRNEEWHLLNLNVSEEKYEHEGVEVSEVKFEISLKRRPLFYMVTLTFPSYIMCAISVVGLFARFSTTGEREERFTLGVTAILTMAVLSLVVSEKVPHSSTHVPLLVAYFLFNMVIVSIAAMTTGIVMKVHRLGRYGDEPSDFWMRCFLLKPVFRTSNRRKYRMNPEEPTQVILVSEAKNGEVLTKKSTELNGTVVKEIMLSSRLEALEEYIRKMVNRCETIKWELDEIDAAENIELVRRRSTNGYVRISERLDILFMFLFLSTVTIPVAVLFYLT
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Forms a proton-gated ion channel with pbo-6 that is activated by acidification of the posterior coelomic space, leading to posterior body wall muscle contraction (pBoc) during the defecation cycle. Probably by regulating the defecation motor program, required for fatty acid uptake by intestinal cells. Does not bind neurotransmitters such as acetylcholine, gamma-aminobutyric acid, glycine, serotonin, glutamate or choline.
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G5ECU1
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SKR1_CAEEL
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Skp1-related protein
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MADQKKVSEAAKEREIKISSSDNEIFLVPRNVIRLSNTINTLLMDLGLDDEEGTNAEPIPVQNVTASILKKVISWCNHHHSDPISTEDSDNREKRTDDIGSWDVEFLKVDQGTLFELILAANYLDIKGLLDVTCKTVANMIKGKSPEEIRRTFNIKNDFTPEEEEQIRKENAWCED
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Probable essential component of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Regulates cell proliferation during embryonic and larval development. Involved in synapse elimination in early synapse development. May negatively regulate the apoptotic activity of cep-1 in response to genotoxic stress. Plays a role in sex determination.
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G5ECU7
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JUN_CAEEL
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Transcription factor jun-1 (Transcription factor AP-1 subunit jun-1)
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MEEDQEEPPSSSTSSESPEVVLKAPKAPTRRRKNSKKDRRQDMEVDDGEKESTAQYCKGFYDALRVMQTTNKYEFTGGAVSSPVLPVLQTAAFSPITPASASDMHTIVMSLLGNTPITSGPSIAPLSSPTLLPLVTSGDLDDLSMKILASSAIPGPPIISSSNSPDSSTTAVTTSQITAFQPLLNNFVSSTTASTSRPDKLNLTPPQQSAEIYAFNGVNSDDSDGGLDSRSASRCGMALDDQEKKKLERKRARNRQAATKCRQKKMDRIKELEEQVLHEKHRGQRLDAELLELNRALEHFRRTVEHHSGNGCPNNSIRV
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Transcription factor that recognizes and binds to the AP-1 non-canonical enhancer heptamer motif 5'-TTAGTCA-3'. Required for ovulation. Controls plc-1 expression in the spermatheca to regulate spermathecal valve dilation.
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G5ECW5
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CSP3_CAEEL
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Non-catalytic caspase homolog csp-3
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MFFGKLGGFAFFLQRAVRCDGFIDNFFDRIPKFFQFMKSKFPSHQTSSSQADLLVSFSTSPGFLSFKDETKDTWYIQELYRVIIENAKDTHLADLLTETNRRVVEKYEADKVVFVCKQAPEFWSRFTKQLFFMSRNDVF
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Non-catalytic caspase homolog which does not contain the region necessary for caspase activity. Acts as an inhibitor of caspase ced-3 zymogen autoactivation and delays ced-4-induced ced-3 processing. Has no effect on active ced-3. Probably by preventing ced-3 activation, protects cells, whose fate is to live, from apoptosis during embryonic and larval development.
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G5ECY0
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DLG1_CAEEL
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Disks large homolog 1 (MAGUK protein DLG-1) (SAP97-like protein DLG-1)
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MSHESSEKAHKAIENVEDYCQTLTRHGNEELRTNLERVITTFKSNLMHSLLDIHDLYEQTLLSERKSDAEKNMEVRRVIERLEGGPHSYNSRPAATTSTSNYNLSSTTPLISDLRDRGGFSYLNGGGLGNGLGNGLGNGLLSSPYNSSSTHYLHERQRQTSHDGTWRETTTRTVDTPSGLERRVVEHTGVIDDHGRKWELENIVLEKGHTGLGFSITGGMDQPTEDGDTSIYVTNIIEGGAALADGRMRKNDIITAVNNTNCENVKHEVAVNALKSSGNVVSLSLKRRKDEAFLPIGGNFGGSTSYLRSGVTPSVSAGNLQHAIHSPSAPIHPPPPPPVHHGSLSQLSVGQYRSTRPNTSVIDLVKGARGLGFSIAGGQGNEHVKGDTDIYVTKIIEEGAAELDGRLRVGDKILEVDHHSLINTTHENAVNVLKNTGNRVRLLIQQGTGAIFNDSASQQFMPTTPILRPSSVQDYNRSQMGSQSHLSYGGPLNTSYSSQAPIAIPLEPRPVQLVKGQNGLGFNIVGGEDNEPIYISFVLPGGVADLSGNVKTGDVLLEVNGVVLRNATHKEAAEALRNAGNPVYLTLQYRPQEYQIFESKIEKLRNDVIAQSRMGTLSRKSEYVRALFDYDPSRENSVAPHRSMGFNYGDILHIINSSDDEWWTARKVHENGEETAEGVIPSKKRVEKRERLRRKQVNFNSGSQSLGRNSSTTGLENRRGSRSQLSFSRKFPFVKSTDRLNDLNEESSNVAEEPVWSYQAVEQQAINYVRPVIILGALKDRINDELVNRDPSKFSSCVPHTSRPPREGEVNGRDYYFVNKHNMEEDVKNNLFIEAGQFQNNLYGTSIQSVRDVANQGRHCILDVSGNAIRRLQSNANIQPISIFIKPSSAQQILELDSQLATNRQDDRAMSGEEAQAQYSRCHRIEQTFGDLFTQEISNVHSANDVLSKVYSIISRESQTPIWVPRH
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Essential multidomain scaffolding protein required for normal development (Probable). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells (By similarity). Required for proper embryonic elongation. Acts upstream of ajm-1 and becomes localized to apical junctions independently of ajm-1. With let-413, cooperatively regulates ajm-1 localization to apical junctions.
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G5ECZ4
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DYF2_CAEEL
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WD repeat-containing protein dyf-2 (Abnormal dye filling protein 2)
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MSLKVIPCTLTKNQEVFKCVSAQLQYRRGEEEHGSGPIIHRWRPNGHTVAVACANNTVIYYDKKGNVIDALNPTGKLIDIAWDKEGDVLAIAVANTGTIYLWDVNSRNTDTVESGATSSKELPTCLAWSPSTPTLVIGNNAGNIVVYNHRTSRRIAVMGKHQRSVTQITVTPEDYVISCSDDNTLSVTTLEGTTVSTTTTNGEPTNMDYGSVNGKGGSGVTMVSVVIGKKILMLAHYNALDEPVNLQFQEKYGNIHSYRWFNDGYILIGFDRGYIISISAHNNEIGSELVSFLEYRGYLASIAVSTSFNKLLTIGDNMVKVRDLDELTTVTMLTEIETEKNLSEIEVTEDGQLVAVSSQSGVLSIFVTKMPTLAASYNNSICYLTNLTQVTVVAEVEKKGSSTLELNIEPTVMGLGPLNLAVANNNTVFFYDYHTPAQMQAAQQLQSTQSAAEKPTIVAAEPINRVEYLSTVTNIQLNYMYAAVNFGSRLRLHRIRNSEDNVSIEFPEANRNATLYSYALTENFLIFTTSNNYIVYFSLSEWAIVSEYRHVVPVRSIFPHPTNVVCCCFDDRLEAMIYSAVDDEVFRLPSVGSSAHYKGAIWETFTIDKNTFAVFDSQNIYVFLLSKQHIQGESVIYVSATRLPHAYVPLSLNKGIVTCLMSNGKLSSVLLDSHKTESVISDKSETVIDDILTRSLLMHRWSTAWKICIHSNDGSHWNQFAMAALLDSDVGMAIKIFREIGDAAMVTALELIETIEEKNLLHAQIYTILSRYDDAEQLYLESSRPMEALNMRRDLLEWPKALVLAETMNPKEIPYLSKEYAQELELTGDHANSLANYEKGVMENPQNLPELQEHNEICQSGIARMAIKTGDLRRGVQLAKQLEGRVVKRDCAIILEQMKQYTEAAQLYEVGLFYDRAAAVCLKANAWAKVGELLDHVKSPKIHIQYGKIMEKEKKYKVAVKCYETGRDYDNQVRLLLDPLNDPDEAVRVVRESRSIEGAKLVAKFFVKLGDYNSAIQFLVMSQCVQEAFELAEKNNAVREYAKAIEQHGNISQALELAEYYNRVNDMFMAAKFYTQAGQYNNAINLLFKNGDDENCVALAVDCGIKSKDKTLNNKLVKFLLGEDGNVKDPAQLFRLYVGLGRTKDAAQTAVVVAQIHQAKGNYRIARDLLFQMHQQLREKMMRIPLDMNKSLMAIHSYIIVKALINRKETLLAARLLIRTCGEIQRFPTHVVPILTSSVVICTQANLKKSAHKFAAQLMTPEYRPKIHEKYKKKIEDIVRKGGNQKDLVEENTPCPICDDLMPAYAMSCDNCKSLVPYCILTGRHIVASDFSRCPHCEMPGFYSEFRKLSILNENCYMCGGDLKGAIPEDAKAYLEKMEQDYK
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Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport. Moves along the ciliary axoneme and is involved in the assembly, localization and the movement of other intraflagellar transport (IFT) proteins along the cilia axoneme. May also associate with the BBSome complex in order to mediate ciliary transport. Regulates cilia biogenesis, morphology and sensitivity to environmental cues.
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G5ED14
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PAX5H_CAEEL
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Paired box protein 5 homolog (Egg laying defective egl-38)
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MEPIWRNYPYPTYPGHHNFQFDPLLSDGSHTGVNQLGGVFVNGRPLADTVRAQIVEMSQHGTRPCDISRQLKVSHGCVSKILGRYYSTGSVRPGVIGGSKPKVATPRVVECIAGYKRANPTMFAWEIRQKLIEDQICGEENVPSVSSINRIVRNKSFMAQLAAPTSVTSSAARPSSATSHHQRSPPRGVQQHMQQSTSVQQLQQLQLTSAATVNSLMTPPAFAMPGTAYSINGLLGTLPQPSLLDDKFTNLSTQSADMSLVYSTGLVGEHDWTMRTPMVILPQNYCGQL
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Transcription factor. Binds to specific DNA sequence motifs in regulatory elements, for example in the genes encoding transcription factor lin-48, apoptosis regulator ced-9 and neuropeptide-like protein nlp-2. Specifies cell fate, playing an essential role in embryonic and larval development. Involved in morphogenesis of the vulva and uterus in hermaphrodites and of the rectal epithelium of the tail in males. Plays multiple roles in the development of the egg-laying system, acting in both lin-3/EGF-pathway-dependent and -independent processes. Positively regulates expression of neuropeptide-like proteins nlp-2 and nlp-7 in uvl cells in an EGF-pathway-dependent manner. Involved in negatively modulating apoptosis in germline and somatic cells, acting in partial redundancy with transcription factor pax-2, probably by directly regulating transcription of ced-9. Positively regulates transcription of lin-48 in hindgut cells and functions in the development of the hindgut.
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G5ED29
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ATX2_CAEEL
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Ataxin-2 homolog
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MSTPTGLPALNGDVLSAINDMIGRVIIINTTDKKRYSGVLGAVSQDFDFGMQCVVEITKENENNLLRTESECRDKMVFHYSDIVDFAYVTQEIKKQHAVSKFVTDRQYHGDTPIEGEELQEWNGGEEDGLGGSIEDDVVVAGGQTAARRSNNHNNGTGWSVNDMFAANEKMNVVSTFKEDLTQYTTVEVVGTDEDRARAERLAREIESNSSSKFMANLENDDDERDLDKITRQEDFENGNGRKRNNNSFNQQQQQRRNPNIAPNGQPVNRRAEGLRGDRRNSGSSSANNSRYGAPAAAQQNYSQNQQQQQGQKGYRRQNEENDWQMAKGKGQNQGHDHSFRQQQKQMLDPRPNNNVKPADDKAQSATTATAAAGGSRVTDLKNWGNEFSIATAPKDQAPAVPAGNSGSAWNRGPPSSLVAKGSSNESTPPPTTNGEEAETKKEEAPSTSVDVAAAPVQNVQNDAEKHQEDDNVSVTSENDSVITSKSSSFKFNINAPEFKPRVAPATPTATTPVQNEYHPQQQPHPAMMAPQQGPPAPGMGMVPPHMGGPQNQGQPPMMMWQQTGQQQQGGGGYPQNHQFPIQHVPMQGVPGQMYGPGAATPVTVAQQPNQQHQVPTSAAGGQNHQLRDGEYREKQPLYMPYGPPQMVPVTSQQFYHSQYQGQMQQAAPYQMKMMPQQAPQGAYQQRYQQPQVYMMPPQGQQQQPRYQGPPPPQQQQQQQPQQQQFSGEQSRPQSHPNSQPTTPGPRGELPKMSGAPQNGNMQAESSSNASHSGSTSSQSGQRSGSPPGAVPPPPPPQQQHQQQQHPPHHAPPHVGAPPPQMMQQQQQHIQQYMVMQGPHQMHPQIPNYYQQPQQVFYPMIMPQQMPMQQNQHPQQSLMGERSDQGFPTSGYFDYRTMPNYQQQQQQQQQQMHRQNSLPQQFQGNQGVNPSGQQSGPPPPPPPSQQGTPRDQQHSQSPP
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Probable RNA-binding protein that negatively regulates the translation of targets. Functions with RNA-binding protein szy-20 to ensure embryonic cell division, and to this end, plays a role in the regulation of centrosome assembly, position and size, and in astral microtubule outgrowth and nucleation. Required for gonad development, germ cell proliferation and for the production of oocytes. Regulates whole body growth and fat accumulation in response to food availability, and this may be through the mTOR pathway, upstream of daf-15 and rheb-1.
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G5ED35
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TTR52_CAEEL
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Transthyretin-like protein 52
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MSRFLIYFLPFFIYSGNVLSKTSCLMATGVLKCPTDPEAVKKVHIDLWDEDSLPLESDDLMGRTWSDRNGNFQVTGCASDFGPINTPDPYLYIQHNCPHRDSNATNPIQIDVIPLFLPSIVRLGNVYLDRYLEDY
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Plays a role as a bridging molecule that mediates recognition and engulfment of apoptotic cells by cross-linking the surface-exposed phosphatidylserine with the extracellular domain of the phagocyte receptor ced-1. Important for the generation of extracellular phosphatidylserine vesicles that promote loss of the exoplasmic leaflet from apoptotic cells in a time-dependent manner. Required for the exposure of exoplasmic leaflet on the phagocytic cells surrounding the apoptotic cells. Does not affect the phosphatidylserine externalization in living cells. May play a role in mediating transfer of phosphatidylserine from phosphatidylserine vesicles to ced-1 bearing phagocytes or alternatively result in the activation of a phosphatidylserine transporter in the phagocyte that promotes phosphatidylserine externalization.
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G5ED39
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SEP1_CAEEL
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Separin homolog sep-1 (EC 3.4.22.49) (Separase)
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MKITNKSVDKQHIEKLDELRKNVSCTVIGFAEQTAELQQEISELFIAEFGVNGPIDMNSLSKLARITSYYASSEYFQGLAKYQRTACKMFITWQTLRKEAMECRSKDREIFASIPAKLCFFYFYNGELCRAVVCLLDYIDLSDDTLAKEAALRWLMFLGETELIEKKLKTWKMDKSSKDMFSATEFAMNYLKKSEYRVEMLEKLMKLRDKVKSDPTRSFSRYELASYVSWLCSTLSNVPVGSALRECEFPDRVSHIQEAALKSDSLVRNRIPGLASSQFDNSVNASIWPFLDGHQEDSNYYVHIGSTIAWHFEMRRECALVNVTTAQTRDSMSAMILNLRVALKSASFFRVLQTTNTLAYYSSIIEEAGSEKNAKLMRVSCVNLLSSNPIIVRCSTPKETGATSRAHTPMAGSSVSEKQNTMRPDLADLLGDLELLDEQSFHPITRSCVCNVCTIYPLHSSFAAEYMMSYAIHSDFSQLSIKHFNDEFARIRERGMSSQVLMHRDSSVRPRPNIIQNEIFGMCVIRWLTKKLDSKESADEDTMEIFNNALKIVRYLQQRTTDMILAVTQLGRQLEFPMECNYSWMRPTIRKPRVKATIDCAVDILRAVSPFGRRPKVEKLEKNLQPFDKERFEKVRLAMRNEMNHYGHILYREWRCRLFAYVGRTSRDPWEAAYAWAESTQIGARNAVQSRLEKCKRGLVTMSGHDRFKTCVQSMPDEMTLVQIAMADDKTIYLVKLHADRDPIIMPLAHYSQAVELMDKFTFLLDEDEMIAKYPGDITPEEFWKRRKIVDGRMMTFVDEVQKHFLGVAASLLMPSGQLGPKAAELAIKIHKLSKGGLLLGEAKEMVYQSKLMDAKSWEALILRFCEMRTTDEKFKSFLPLMHRNSVEVMNQDDSIVTEKKYTYLVICPHLSQFCWERLPIFDEYPYVGRQVSIHSTFSQLEAMKSQEKQIPLQIDVQNAYYILDPDNNLGETQKRMVEYINKFNWEGTVGSAPKSNEISAALSQRDAFFFIGHGSGSSVMPRSVLKQSTCNAISLLMGCGSVRTIPQALGFDGKTAILDYAMAKCPLIVGCLWTVTDGEIDRFLIRMIDDCFEDSKSLTGIDKLRQLSEAMHEARSKARLKYLTGAAVVMYGLPVVAKQTTPFVEKDQRNLPQTPKTSARTSMRMETVPKTPKQEFVTSKSVPMTPIFSNNENKSPSRARMPSRVLKTPRQVKTFQEEDDEAPKRSTTRQLKPLVAPPIPATPTTRTTRSSARTPSRSRNL
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Cysteine protease, which plays a central role in homologous chromosome separation during meiosis I and in sister chromatid separation during embryonic mitosis. Promotes chromosome/sister chromatid segregation by cleaving the scc-1 (mitosis) and rec-8 (meiosis) subunits of the cohesin complex at the onset of anaphase (Probable). May cleave histone H3-like protein cpar-1 during meiosis I metaphase-anaphase transition. Promotes cortical granule exocytosis after oocyte fertilization during the first meiotic anaphase. Essential for embryonic cytokinesis by regulating rab-11-positive vesicle trafficking at the plasma membrane at the cleavage furrow and midbody. Regulates centriole segregation during spermatocyte meiosis. Required for embryonic anterior-posterior axis formation.
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G5ED46
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CASY1_CAEEL
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Calsyntenin-1 [Cleaved into: Secreted calsyntenin-1]
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MRTAYFIFVGALLGVSYAKHHHAARAPIINLQGAEELVAVVREDENIISTVPDFAILSETGPVCNYLLTSQNNEPVPFDIQVVDKYTGAAVLRVKDAATLDCKKPEYNLQVQAVKCDNDNVKSEGVSLKIRVKDTNNHAPEIENPWYTFHVEEGKVVEEVGVLKASDKDCGHPNGEICEYEITNGLKELPFAINNHGVLRTTQPLNFTQSKSYILTVVAIDCAMRKSKSSLVTVHVDEKCVQGITAMNERVNYAPGVGSKLLLPDVSLEFCEKETICEPKSVQSVIELRAGHVTQGCARDTVYDNQTIQSCGLSTATVKLLNEEALTSSAENQILADQGIEFDGARGVTVSDENHQGLIPDHFTLSFSMKHAAGTKDEQSNKQNILCESDDFNMNRHHFSVYIRHCKLEVVLRREAGATSDFRAAEWRWSMPEVCDNEWHSYSLLFNGIDDVNVIVDGKSFKADERNPEILDDWPLHKTKATKTKLVVGACWHGRQQKLAQFFRGQLSSLYLLSGAVESERAIKCAHTCPEQLQFTGVDELLESQSATFSPDQTSLTLKAETSKQIGQMLKRVAYVNTQEKPAPGHRVFLVETEVTCKQDDKKMKLPSSKGYVFVQQAAEPTLSISASSQLKSNQHMVKVGQAMVPDLTITISQNNADGELEDVTQSHKIDYCKMHLQPARDMDVEYFSSPASLIAALNIEFEHDKDGILLRGEESAQGYKEVLSKVHYFNTRPESYAKRVYTVQCAMLKGRVLSNQLFVTMTIDGVTTTTSTTTEAPAPAQPDPIQFNFNSGETALDSLELIERHFEPAFDQLGSSRLQNILEMDLPRPKALLSHHGYDVGQGAIAGGAVAVVVVVCVGFLLVLLVIGVLKMRDTPMPRRRRQKRQSDGGMHWDDSGMNITVNPLDDVEKNGGAIDEFSDEEEEEETDGESECSYRDEEDDVSEDEEDQTEVLPHLDANQRVVGGLEWDDEDAISTNARSYRV
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Cell adhesion molecule involved in associative learning and memory. Acts as a regulator of GABAergic synaptic transmission at neuromuscular junctions by regulating GABA synaptic vesicle precursor transport: possibly functions as a cargo adapter for unc-104-mediated transport of synaptic vesicle precursors. Promotes localization of isoform c of daf-2 (daf-2c) to synaptic regions by acting as a signaling adapter between klc-2 and daf-2c. [Isoform a]: Acts as aregulator of glutamate signaling in the sensory neurons by inhibiting the activity of command interneurons, thereby negatively regulating motor circuit activity and locomotion.
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G5ED47
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HIZR1_CAEEL
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High zinc activated nuclear receptor protein (Nuclear hormone receptor family member nhr-33)
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MQKVMNDPEDLGNCKICLQRADGIHFAVSSCRACAAFFRRTVILKLNYTCKEKGNCTVEKSLRNLCRSCRYTRCINEGMKIELVQLQRDSIGRKKSGASISIDPLFTPNVASSLSAIFKNEKEDVLSTSCTILSQMTSGYAMFLNIRRSTNTLVQSSVITPTFKMPKIELHASRFDSAKQVCKAEAHLVTDIVNSYFSPFNSLKFEDKVALFKNFFCYFSHTDRAYQSFKQFESDNLNDKILMPDGGFIKRTELGRFYENAEGVHTSAEDAAKIFQPALNYILDVIVDYMRRIHIIETEYLALLGFCLWDDAVPGLSKEAKSLAVQTQSKLLAELQNFYSSQNKDAVEITQRVGVLLLLVPKLTKCVIMLRENSVLAELFNYYEADVCCKNFKEDASVDLDCTSQCIVHTKND
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Nuclear receptor transcription factor that binds to DNA enhancer elements to promote the transcription of genes required to maintain micronutrient homeostasis. Direct binding to its ligand zinc allows for nuclear accumulation and activation, which thereby induces the transcription of genes required to promote the storage and detoxification of excess dietary zinc. This in turn, allows for internal zinc levels to be detected and regulated.
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G5ED66
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PAX3H_CAEEL
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Paired box protein 3 homolog
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MTTDSITFNHILGQGRVNQLGGVFINGRPLPIHVRHAIISMAKKGIKPCHISRQLKVSHGAVSKILNRYAETGSISPGQIGGSPRARLTVQAVEKEILIACDENPQMSAAELRDWLIHKDICTKGNAPTVPAIKRLIGNKGVGVPKKMERKRLSYSIDSILGISIDECSKSSSDDEEGSSPSNDASSRRNRTSFTAEQLDVLENAFRADTYPHANARESISKETGLSEEKIMTWFSNRRARCRKNMPMYQQYNVQGFGSSPPSYPTLLPSPMMFLPSYSTSPQLNPLFFQHILQSSPPSSQSSPPSSS
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Transcriptional activator (By similarity). Regulates the lateral/ventral epidermal cell fate decision.
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G5ED68
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MTMR6_CAEEL
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Myotubularin-related protein 6 (Phosphatidylinositol-3-phosphate phosphatase) (EC 3.1.3.64)
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MRFEDIGISKVDKVCLVDRLGCQENLVGTVHVTTTHIIFRAENGSKELWLATGLISSVEKGTLTAAGCMLVIRCKHFQVITLLISRDKSCQDLYETLQRAAKPVSVNVTELLAFENREPVEDVRGWRRLDWNSEMTRQGITKSQWTESNINEGYTICDTYPNKLWFPTAASTSVLLGSCKFRSRGRLPVLTYFHQQTEAALCRCAQPLTGFSARCVEDEKLMELVGKANTNSDNLFLVDTRPRVNAMVNKVQGKGFEDERNYSNMRFHFFDIENIHVMRASQARLLDAVTKCRDVTEYWKTLEASGWLKHVRSVVECSLFLAESISRGTSCVVHCSDGWDRTSQVVALCQLLLDPYYRTIHGFQVLIEKDWLGFGHKFDDRCGHVGALNDEAGKEVSPIFTQWLDCIWQIMQQKPRAFQFNERYLIEMHEHVYSCQFGTFIGNCDKDRRDLNLSKRTKSLWTWMDARHDDYMNPFYSPTAHVALLDLDTRAARFTVWTAMYNRFDNGLQPRERLEDLTMAAMEHVGVLESHVAQLRTRLAELKTQQNQQITSTNTPTNMVDSGMSSATDDLKNLSLSHPLDPLSSTLPILERATSQESGVMDSSLYYPDEALTKYSLKWQPLRGADRCSNPACRGEFSSTIERRIHCHLCGMIFCRRCLKVSADERERVCDKCKTD
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May dephosphorylate phosphatidylinositol-3-phosphate (PI3P). In association with mtm-9, plays a role in endosome trafficking probably by regulating phosphatidylinositol-3-phosphate levels. Regulates fluid phase endocytosis in coelomocytes. Controls the endosomal localization of sorting nexin snx-3 and the levels of sorting receptor mig-14. By regulating the retrograde transport of mig-14, may be involved in the secretion of Wnt ligands such as egl-20. Regulates posterior migration of QL neuroblast descendants and the anterior migration of QR neuroblast descendants and HSN neurons during larval development. Involved in the formation of correct synapse number in DA9 motor neurons probably in part by regulating the secretion of Wnt ligand egl-20.
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G5EDA5
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KSRB_CAEEL
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Kinase suppressor of Ras B
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MSDEKKKKRGFFRYSVLTTSSFSSWRRSSTSGSISQSSRTTSKTTTSSSVTSSNPINAPPPTATSSSSVLPSTSSEPPPPASAPPRISIYHKMVPSKSKFRQCDVCEHIFIFDFVRKQHLDDVYACNVCGIRVHKGCLDRVKNDCKITTQYMGGILENAVIQSNKKQWEKPTTASISKSLTTSPTCSTSTTMSPAGVEKNVHKTRKLISMTTSTLDDVTTFNSEINEEMDEETVLMTWEDVTIKLTDVDVMTKIGDGRFGSVYFGGYHGNAAVRFVNMNYLSQEDRRADVFATEIVSAYKNSRHDHIALFYGYVSDPVTNTYAIVTNFYQHNTLYHRIHEQLSEDFDQSWTFQISLQICQAMSYLHKKKILHRDLRTKNILLDNPNRVVVTDFALMKLERLENPRRNCTLLIPNHWIDYLSPEIAGNLMIDWRGDVLFQHELPFSQESDVYSFGTIFFELLLRRMPTGCDSWDQKLYAKMCGQKAALQRLDAQLQKIDGKLHELLLECWSSQPEKRPSFQQIVKRITVQMPRKESNKQKRRSTAHENPLF
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Probable inactive protein kinase which positively regulates Ras-mediated signaling probably acting at the level of let-60/ras or/and lin-45/raf. In the germline, regulates meiotic progression during oogenesis and mpk-1 (isoform b) phosphorylation. Plays a role in meiotic recombination events. Functions redundantly with ksr-1 in the Ras-mediated regulation of larval survival, the development of excretory canal, in determining vulval precursor cell fate during vulval induction and in mpk-1 phosphorylation in somatic cells.
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