entry
stringlengths 6
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stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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G5EFX6
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SLIT1_CAEEL
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Slit homolog 1 protein (Slt-1)
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MLICFIFILLIPESATCPAECVCVDRTVSCVGQQLTEVPQNIPNDTIRLDLQDNEITKIGPNDFSSLMNLKALQLMDNQIVTIHNQSFSSLVFLQKLRLSRNRIRHLPDNVFQNNLKLTHLDLSENDITVVSDAQLQGPEFLEVLNLDKNHIFCLENNVISSWVSLEVLTLNGNRLTTFEEPSNARFRQLDLFNNPWNCDCRLRWMRKWLEKAEGQNKTVCATPLNLQGSSIEILQDKFMTCSGNRKRRYKKTCETAEICPLPCTCTGTTVDCRDSGLTYVPTNLPPSTTEIRLEQNQISSIPSHSFKNLKNLTRLDLSKNIITEIQPKAFLGLHNLHTLVLYGNNITDLKSDTFEGLGSLQLLLLNANQLTCIRRGTFDHVPKLSMLSLYDNDIKSISEVTFQNLTSLSTLHLAKNPLICDCNLQWLAQINLQKNIETSGARCEQPKRLRKKKFATLPPNKFKCKGSESFVSMYADSCFIDSICPTQCDCYGTTVDCNKRGLNTIPTSIPRFATQLLLSGNNISTVDLNSNIHVLENLEVLDLSNNHITFINDKSFEKLSKLRELRLNDNKLHHFSSMVLDEQSNLEILDLSGNNIQCFSSIFFNKATRIREIKVIGNDLLCDCRILPLMSWLRSNSSHSIDIPPCQQFQYSDNESDKQRCAAFPEETCSDDSNLCPPKCSCLDRVVRCSNKNLTSFPSRIPFDTTELYLDANYINEIPAHDLNRLYSLTKLDLSHNRLISLENNTFSNLTRLSTLIISYNKLRCLQPLAFNGLNALRILSLHGNDISFLPQSAFSNLTSITHIAVGSNSLYCDCNMAWFSKWIKSKFIEAGIARCEYPNTVSNQLLLTAQPYQFTCDSKVPTKLATKCDLCLNSPCKNNAICETTSSRKYTCNCTPGFYGVHCENQIDACYGSPCLNNATCKVAQAGRFNCYCNKGFEGDYCEKNIDDCVNSKCENGGKCVDLINSYRCDCPMEYEGKHCEDKLEYCTKKLNPCENNGKCIPINGSYSCMCSPGFTGNNCETNIDDCKNVECQNGGSCVDGILSYDCLCRPGYAGQYCEIPPMMDMEYQKTDACQQSACGQGECVASQNSSDFTCKCHEGFSGPSCDRQMSVGFKNPGAYLALDPLASDGTITMTLRTTSKIGILLYYGDDHFVSAELYDGRVKLVYYIGNFPASHMYSSVKVNDGLPHRISIRTSERKCFLQIDKNPVQIVENSGKSDQLITKGKEMLYIGGLPIEKSQDAKRRFHVKNSESLKGCISSITINEVPINLQQALENVNTEQSCSATVNFCAGIDCGNGKCTNNALSPKGYMCQCDSHFSGEHCDEKRIKCDKQKFRRHHIENECRSVDRIKIAECNGYCGGEQNCCTAVKKKQRKVKMICKNGTTKISTVHIIRQCQCEPTKSVLSEK
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Functions as a ligand for sax-3 receptor during larval development. Acts via the sax-3/Robo receptor to direct ventral axon guidance and guidance at the midline during embryonic development.
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G5EFY4
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EGL46_CAEEL
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Transcription factor egl-46 (Egg-laying defective protein 46)
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MVPMNDFWVKAILSSTNPSPVPSTTSTVSNDENLDKTLDFDCSTQTVFPTLPMFWNPTLVQQMLALYQIQQQQIQFSAKLAPQPLFQEPTIQKEFLPFPHQSRKRPLPIDPKKTKLRKLNEDTVTSSPVSGMFIKEEADVKSVEELQKEADLLDETAAYVEVTEESRQKIDEIPNVIGDCICRLCKVKYEDVFKLAQHKCPRIAHEEYKCPDCDKVFSCPANLASHRRWHKPRNELGGSPPAQSSTIVSCSTCFNSFPTKKMLKLHSSTCQRSPLQDLLSRVIPTM
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Transcription factor. Represses expression of genes involved in differentiation of touch receptor neurons (TRN), probably acting as a heterodimer with egl-44, perhaps by occupying similar cis-regulatory elements as an unc-86/mec-3 heterodimer. Plays a role in cell fate specification of neurons, including the hook neuron HOB, the gas-sensing neuron BAG and touch receptor neurons. Plays a role in neuron differentiation by repressing the expression of zag-1 in FLP neurons, probably acting as a heterodimer with egl-44 because zag-1 represses expression of egl-46 and egl-44, together these proteins form a bistable, negative-feedback loop that regulates the choice between neuronal fates. Acts downstream of egl-44 to prevent touch cell differentiation in FLP neurons. Involved in male mating behavior, acting in concert with egl-44, via modulation of expression of polycystins lov-1 and pkd-2, homeodomain protein ceh-26, and neuropeptide-like protein nlp-8. Modulates the expression of a subset of terminal differentiation genes involved in O(2)- and CO(2)-sensing, acting in parallel to ets-5 and egl-13. May act upstream of RFX transcription factor daf-19 to regulate gene expression specifically in the HOB neuron. Plays a role in specifying commissural dendrites of the PVD nociceptive neurons, acting in concert with egl-44. In association with egl-44, regulates cell cycle exit in the neuronal Q cell lineage.
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G5EFY5
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NOB1_CAEEL
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Homeobox protein nob-1
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MISVMQQMINNDSPEDSKESITSVQQTPFFWPSAAAAIPSIQGESRSERESETGSSPQLAPSSTGMVMPGTAGMYGFGPSRMPTANEFGMMMNPVYTDFYQNPLASTGWYSYGQPYQFTANYSIPSLDGNLSDITIPTTAGSSAATTPNAAMHLPWAISHDGKKKRQPYKKDQISRLEYEYSVNQYLTNKRRSELSAQLMLDEKQVKVWFQNRRMKDKKLRQRHSGPFPHGAPVTPCIERLIN
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Transcription factor, involved in posterior embryonic patterning, morphogenetic movements of the posterior hypodermis, and cell fate specification. Binds to the 5'-TAGT-3' motif in regulatory elements of genes, including Meis protein psa-3 and microRNA mir-57. Involved in a negative regulatory loop with mir-57 to specify posterior cell identities. Required for asymmetric division of the T hypodermal cell, acting via the regulation of asymmetric expression of psa-3 in cooperation with ceh-20 and the Wnt-MAPK pathway. Involved in the regulation of the onset of non-apoptotic cell death in the linker cell, acting together with the Wnt signaling pathway. Involved in promoting embryogenesis, in concert with orphan nuclear receptor nhr-25. May regulate expression of transcription factor dmd-3.
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G5EFY7
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PQM1_CAEEL
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Zinc finger transcription factor pqm-1 (CePqM132) (Paraquat responsive protein)
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MSFLNNDFGSPPATSSPPTTMPKLPTIQDMLNNIGASTVNLMQPNPYLMQNQIPLPVPNLPLNPFLHLNPAISQEIIQQFIAMSFNTPNVLASIANMGDDEGPSCNPKMRRGDLLKSVSMDSTEDPPSITLDNNGDMIVPNNDKEGWCRNKKYIEQTENGYMCTVCRKVYGRYNSVSYHVTIYHRNPPIKCNVPNCQFTTREARYIHFHKNYRHGIPLPESIDQGSRKCPHCRHVSKSPAMLEKHIRRHQIKDGLSNINEAIRERTSTICDEAMEIEPAETEVDPIETKPRSCTL
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Zinc finger transcription factor which acts as both a transcriptional activator and repressor. Binds to the promoters of genes that contain the 5'-CTTATCA-3' DNA consensus sequence in their regulatory region. Functions downstream of the Insulin/IGF-1-like signaling (IIS) mediated pathway. Involved in normal development, lifespan, stress response, lipid metabolism, innate immunity and exit from the developmentally arrested larval state known as dauer. Required for stress-induced expression of hsp-90 and resistance to heat stress, perhaps as part of a systemic stress signaling pathway. Involved in maintenance of proteostasis. Under hypoxic stress increases lipid levels by positively regulating fatty acid synthesis via fat-7 expression. Associates with homeobox protein ceh-60 at the promoters of some stress-responsive genes to regulate expression may require phosphorylation for transcriptional repression activity. Acts downstream of nhr-14 to activate transcription of intestinal metal transporter smf-3, modulating innate immunity and iron uptake. May act downstream of the mTORC2 signaling mediated pathway. May act in a mutually exclusive manner with the FOXO transcription factor daf-16.
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G5EFZ1
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GPMI_CAEEL
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2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGM) (EC 5.4.2.12) (Cofactor-independent phosphoglycerate mutase homolog)
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MFVALGAQIYRQYFGRRGMAMANNSSVANKVCLIVIDGWGVSEDPYGNAILNAQTPVMDKLCSGNWAQIEAHGLHVGLPEGLMGNSEVGHLNIGAGRVIYQDIVRINLAVKNNKFVTNESLVDACDRAKNGNGRLHLAGLVSDGGVHSHIDHMFALVKAIKELGVPELYLHFYGDGRDTSPNSGVGFLEQTLEFLEKTTGYGKLATVVGRYYAMDRDNRWERINVAYEAMIGGVGETSDEAGVVEVVRKRYAADETDEFLKPIILQGEKGRVQNDDTIIFFDYRADRMREISAAMGMDRYKDCNSKLAHPSNLQVYGMTQYKAEFPFKSLFPPASNKNVLAEWLAEQKVSQFHCAETEKYAHVTFFFNGGLEKQFEGEERCLVPSPKVATYDLQPEMSAAGVADKMIEQLEAGTHPFIMCNFAPPDMVGHTGVYEAAVKACEATDIAIGRIYEATQKHGYSLMVTADHGNAEKMKAPDGGKHTAHTCYRVPLTLSHPGFKFVDPADRHPALCDVAPTVLAIMGLPQPAEMTGVSIVQKI
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
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G5EFZ3
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ASH2_CAEEL
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Set1/Ash2 histone methyltransferase complex subunit ash-2
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MRSSKGGRGRQAAPKTAPTTVCYCDGKRELGSVEVVCSTCLKWFHGRCLKEFHELNSNGVPFMICYTFTCKQCRPTAEDWKAKKADLVQMCVTVLATLSAERLKADGKLSAEHVPEDFTYLSLKDEIVPYMNENWYMLTAIKQKKEWHQNLAPTLLKEKNIFVQHNDDDDLFALAEKNLSLLGPLHEAVKLIGKRPIERENREPRHIELPPIEGPKTRGASKRRHAEAPVTGKKQKLAADYSSTAAPNGVQIDIPFSKDNYRYYLTEVDPNVPEDPAWNQNQSSAYVIPSFHYRELLNPTVNVSSNDRAFQLSINGNSITGFEGYSMARASHGVSKGTWYFEVNFDDQPDDSHIRIGWSQSYASLQACVGYNKFSYGWRSKHGTKFHEAKGKKYHFGGFKQGDVLGCLIHLPVDKKLQIPANLPSEKYLPVSHKGFNLISFKANYFFEVQEESADIAKTLVEMPGSYIEFFHNGKSCGKAYENIYAGAYYPSISIFKSATATMNLGPKFRNLPRGATGIHARADEQQHEQTLSDMLYLVSKEVNLDHPPRVKREDDDDVKDIKKEIKQEI
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Component of the set-2/ash-2 histone methyltransferase (HMT) complex (Probable). Required for the di- and trimethylation at 'Lys-4' of histone H3, a mark associated with epigenetic transcriptional activation. Implicated in the epigenetic inheritance of lifespan over several generations. Functions as transcriptional regulator. Acts in the germline to limit the longevity of the soma, probably by regulating a lipid metabolism pathway that signals from the germline to the intestine, thereby preventing accumulation of mono-unsaturated fatty acids.
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G5EG11
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FAT4_CAEEL
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Delta(5) fatty acid desaturase fat-4 (FAT-4) (EC 1.14.19.37) (EC 1.14.19.44) (FAT-4 Delta(5) desaturase) (Fatty acid desaturase 4)
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MVLREQEHEPFFIKIDGKWCQIDDAVLRSHPGGSAITTYKNMDATTVFHTFHTGSKEAYQWLTELKKECPTQEPEIPDIKDDPIKGIDDVNMGTFNISEKRSAQINKSFTDLRMRVRAEGLMDGSPLFYIRKILETIFTILFAFYLQYHTYYLPSAILMGVAWQQLGWLIHEFAHHQLFKNRYYNDLASYFVGNFLQGFSSGGWKEQHNVHHAATNVVGRDGDLDLVPFYATVAEHLNNYSQDSWVMTLFRWQHVHWTFMLPFLRLSWLLQSIIFVSQMPTHYYDYYRNTAIYEQVGLSLHWAWSLGQLYFLPDWSTRIMFFLVSHLVGGFLLSHVVTFNHYSVEKFALSSNIMSNYACLQIMTTRNMRPGRFIDWLWGGLNYQIEHHLFPTMPRHNLNTVMPLVKEFAAANGLPYMVDDYFTGFWLEIEQFRNIANVAAKLTKKIA
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Can function as a Delta(5) fatty acid desaturase and behaves as a (8-3) desaturase. Introduces a double bond in the fatty acid chain 5 carbons away from carboxy terminal to biosynthesize polyunsaturated fatty acids (PUFAs) endogenously (PUFAs are essential for membrane structure and many cellular and physiological processes). Acts on a variety of substrates such as dihomo-gamma-linoleoyl-CoA ((8Z,11Z,14Z)-eicosatrienoyl-CoA, 20:3n-6) to generate arachidonoyl-CoA ((5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA, 20:4n-6). Also acts on a number of other substrates, including fatty acids that do not contain a double bond at the 8 position like (11Z,14Z,17Z)-eicosatrienoyl-CoA (20:3n-3) to produce (5Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA (20:4n-3). Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (By similarity).
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G5EG14
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CATIN_CAEEL
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Splicing factor Cactin
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MGKDSKKHKKERRRERSPSTSDSDEERLQKRLAEQRSLKKDEKRRQKEEMKKNESAEEKRARRMEKKMRKDAKRKDADAEDTLIPPELNYTNLNNPFNDTKLTQTFVWGKKLEREGKSGLTQDEITKQTSQRIRKNLHEAAEFKRIRDSRAAAKEDMEMMKRDADLRAGQISDTKEREFQMDQIKERTRIRIDQGRAKAIDLLSRYARFADENPHTAKIPDFELENPMEYLKASCKSVDDYEDLIEDIKTYREVDGWAKNETWWMDVTRIAEDEIQKKAAQNRGDVHASVQTEVQNMFKNKSIDELLKLEDQMDAKIRGNSGNKGYWQDLDDQLKVFIARKRLREHHGRVLRLQLAIIKEEQKKEIQQQESEELLPVAEVPPQVKIQKEEEEEEEEDEDDEKISKKVRRKIDVQTLDDPELDEPERERKWRALTGDQLDDVTRELYRIGCYSPTYISADDTMPGIEILDEQADVDNLTERRNRNRGTLPSSSAASSGAPQGASSKMMAIAREGMEADESIFGAEEQLAAQRHLWSDKYRPRKPTYLNRVQTGFDWNKYNQTHYDQDNPPPKIVQGYKFNIFYPDLLDMTVAPRFGLTSCEDPDFAIIRFKAGPPYEDIAFKVVNREWETLHKNGYKCQFQNGVFQLWFMFKKYRYRR
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Plays a role in pre-mRNA splicing by facilitating excision of a subset of introns (By similarity). Plays a role during early embryonic development. Required for the distal tip cell migration at the end of larval development and for gonad morphogenesis.
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G5EG17
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SMC6_CAEEL
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Structural maintenance of chromosomes protein 6 homolog smc-6
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MGKRDIPSPNENIAPRTIGMRDVDLTAAPAKKAKLDTGERIAVSGRVASVKLTNFMCHANLQIDFKTAQNNCFYIGGPNGSGKSALFAAINLGLGGRGSDNDRGNTVKSYIKDGTTQSKITITLTNAGLNAHPDFDDLISIERTINQASSTYIMKSVKVTSSDNHVERIVSRKKADVDRIVSRFSIHLSNPAFWMSQDRSRSFLANFKPANVYKLYLESTNLENIRLSYIRFADALDECFALIQLKAGEILNEQKKLKRMQEQRDLQAKLDQDRALVASFCWKLLFCKVRDYNDQIELTLKKQEAQKTLQDETKKEYAKNRAARTEVEKKIQEFRDEVEVQDAEIAEAREDLDAKKRKVLEFEEKIRECEQSIRKKTSEKKYMERTIVNAKNEVRILLEKQGNQDLTKRLTKVENDYKDISQQRENMELGGESAKLREKLDTVITDYKRKEEEKYTIQRDINQLRRKIEQDMETMRRSRATKKDAINKFGSHMAEILMEINRSKSRFQTVPKGPLGKYITLIDPKWAFTVEECIGNLANNFLCSSHLDAEILRNIFQSLRIPAQDRPTIIVAKCNGRAYTNLHEPSSDFKSIYRVLKFSDPDVHNVIIDKSNCEQFILIEDKTEAMELMGSNYPPQNAVKAYTLDGSQAYANGPNSQYRFYSGRGGHARGTFGNDQGDVDEGALARLIEDTKSEAMRLETQDLRKQDHELKVIYNERDQTKAAIDEFDRKLSNLRSQELQKERQAKDLRAELAQTANEDQVENLNESIEEMQKKIPLIEDEVKDILKNVADITADMAPVIQERKEAEHTLAEIQKETRDFASKSQKLQNELSKYDDAGEILKIRLDKVKADEGVFFHTEAKLKSERDDAMEMVENDKKNHPMPPGETDPPDLSSFPSTTEAQRKIEEMQKAVDRATVGCDTTITLECVKDFKDKLKRLKYLCRMIEDVLIELKNLHAARVKAYPSLKKFTELKVCNKFQELLAVRGHFIGGLEFDHEKETLNVNVQSSKEKDAMAGRRPEVLEVEEVDEHSYDDDSDDSTGPRRKKSKKSGQKKKRVRDLKGLSGGERSFVTAALVMSLWEVMEQPFRMMDEFDVFMDMMNRKLVMDLLVELATKKFPHNQFIFFTPQGIKELNMVDGLQVFEMNRVRD
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Core component of the smc-5/smc-6 complex. Involved in DNA double-strand break repair by promoting sister-chromatid homologous recombination during meiosis. Also plays a role in the DNA damage repair of ultraviolet (UV) radiation-induced DNA lesions. Promotes efficient DNA replication.
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G5EG38
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CDC16_CAEEL
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Cell division cycle protein 16 homolog (Abnormal embryogenesis protein 27) (Anaphase-promoting complex subunit 6) (APC6)
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MSAISPDTKSFAIPTLADEGSSSKPASSLDLPKHESIRFKPIKTLASRIDGSEYYDEASMEKVMEMLEIGRTDEAVAYADTLYSNIIDDEQQDIVTIAEYVKILVVLRQWRRISHIIARGNYHQIHIVFAYYAATALFQRKLYEDVAELSVGHLLPSNGQIGPLPVRTLSQVTGRYVEEERMKYSFANMAELDNSSKKLRMVPALMITIAESFLKLMNRDAAMICINYALSLDNTTLHVERLMAKYNLVEPAMWEKYRKVRNEQLKLHEGNHDPRILMERAQRAYEMGRFRETKKITDELFDLFGPHPECIILRIHCLTMLKDSRSLLELGHQLVSDDPHIPLPWYCVAMYYYSIGANSRARNFISKCTMMDSTFAEGWVAFGHILHYEVEHEQSMSCYYRASKLVDKSSEPFLYTSLQYSTHSQKLSKKFMGEAVARAPNDPLIRHEEACVAYTAKSYAEADILFRTVLYMVTETDEIIPIEEVLKKKIDDFWHPMLNNIGHIARRQGRLNEAIMFYQKAIRMEPKFVDAIASTALCYAVLGNIDKATEFFNKALAIDPFNETIRQCLSKMIQASKESYSVDQQTLPPAYNSETYFGAQEILPYCAIRKPRNDGFVVPSIVSSSQPFMSMLRDRLRRQDQLYAQEPDNDAGNQV
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Probable component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (By similarity). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins (By similarity). Developmental role in early embryogenesis and the metaphase to anaphase transition in oocyte and spermatocyte meiosis and mitosis in germ cells. Required for embryonic anterior-posterior axis formation. Plays a role in regulating the abundance of glr-1 receptors in postmitotic neurons, which may in turn control animal locomotion. Involved in regulating GABA neurotransmitter release at neuromuscular junctions in GABA motor neurons.
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G5EG44
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MDL1_CAEEL
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Mad-like protein 1
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MEQQLNLGHLLTAARLLDIGALDISSLDLGALTSTSSSPGSSSPAMFDLSNESELRSLFCGKLKVDKKQSSCASNASTSSQPYCSSPPARKSSKHSRTAHNELEKTRRANLRGCLETLKMLVPCVSDATRNTTLALLTRARDHIIELQDSNAAQMKKLNDLRDEQDELVAELAQLQADEEVAQATSQACQTLSQSRPESRASSFTSTSSRDSPCYLEYSPSSKPMDSHKPTIIDLYAEGLIPRGPITFPRPLVYPHNVFDLMNLPPTPFDVSQFLPINLQV
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Transcriptional regulator which binds to the E box motif 5'-CACGTG-3', when in a heterodimeric complex with mxl-1. Involved in the control of lifespan in response to dietary restriction, the decline in protein homeostasis associated with normal aging, germline signaling and may overlap with the insulin-like signaling pathway. Plays a role in autophagy. Involved in promoting infection by the microsporidian pathogen N.parisii, possibly together with transcription factors pha-4 and zip-10.
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G5EG78
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PXDN2_CAEEL
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Peroxidasin homolog pxn-2 (EC 1.11.2.-)
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MLLEFLLLIGISLSTACPSECRCAGLDVHCEGKNLTAIPGHIPIATTNLYFSNNLLNSLSKSNFQALPNLQYLDLSNNSIRDIEETLLDSFPGLKYLDLSWNKIRYVPKLSTAPNALVSLNLVHNEISRLDNDLVSHSPYMQTFLIQRNRIQSLPHDFFNSRMVPTLKTVKMAGNPWSCDCRMVNVKQFADSLFAHSNQNIFIVGKCFFPKGLRNYVFRNLSIENLECEKPEYSKTDDGMFKMSCPNNEMEGYHYDSIFLENNKEARHTAHFARDKDGSLLSNGQFTRNYQCAFYRQKQSIHMQKKMQASSSTEPPITTTTMEPMTTSTMDSMDTTESVVTMTTMPEIDTKIVFEHKQLDTTSRDGETLELKCEASGEPTPTITWLFEKQKLTESRKHKLTKNGSVLKIFPFLNTDIGQYECVASNGEESKSHIFSVSLKESEQPVIIDAPMDTNATIGQQVTLRCNAKGFPVPDVVWLFEGIRIPRRNTRYTISDNNIELTIEKVTRHDSGVFTCQAVNSVGSAVATANLLVGAELTEKVDKLLDDSTIEKIAKEAKQKVEKALSSTKDQQRMDKIESPNDLSKLFKFAINLKKVDLGKAREIYEESIRLVQMHIDNGLAFESAMISPNVSYEAVLPVSYVQTLMEKSGCQTGQFAESCEDHCFFSKYRSYDGQCNNHEHPWWGVSEMAFMRLLPPRYENGFNTPVGWEKGKRYNGYEVPNARKVSRVLIGTDETTPHSHLSAMTMQWGQFIDHDLTLTAPALTRHSYKEGAFCNRTCENADPCFNIQLEADDPKLHTGLYQKHPCMEFERNGAACGSGETSPIFQRVTYRDQLNLLTSYLDASGIYGNSEEQALELRDLYSDHGLLRFDIVSGANKPYMPFEKDSDMDCRRNFSRENPIKCFLAGDVRANEQLGLMSMHTIFLREHNRIASRLLEVNENWDGETIFQETRKLIGAMLQHITYNAWLPKILGKATYNTIIGEYKGYNPDVNPTIANEFATAALRFAHTLINTHLFRFDKDFKETKQGHLPLHNAFFAPERLVSEGGVDPLLRGLFAAPIKMPRPDQVLNKELTEKLFNRFHEVALDLAALNIQRGRDHGLPSWTEYRKFCNLTVPKTWSDMKNIVQNDTVISKLQSLYGVTENIDLWVGGVTEKRTADALMGPTLACIIADQFKRLRDGDRFWYENEEMFSKAQLRQIKKVTLSKIICTNGDDIDRIQRDIFVYHGNSTQFYEPCESLPEINLNMWTTCCDAMCSSSSTLARNAIGGDEKAKRRKRRHHHSKKSCHDKGKRRKSGDRWNHSNDICVECMCHDGEVWCKTNNFCKSQV
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Catalyzes the two-electron oxidation of bromide by hydrogen peroxide and generates hypobromite as a reactive intermediate which mediates the formation of sulfilimine cross-links between methionine and hydroxylysine residues within an uncross-linked collagen IV/COL4A1 NC1 hexamer (By similarity). Required for embryonic morphogenesis playing a role in epidermal elongation at the twofold stage of embryonic development. Required post-embryonically for basement membrane integrity and muscle-epidermal attachments, and specifically in the function of basement membrane components such as the type IV collagens. May have a role in inhibiting axon regeneration. May functionally antagonize the peroxidasin pxn-1.
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G5EG86
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BRC2_CAEEL
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DNA repair protein brc-2
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MGDSSKKVKDSFDTISEPDSFDEPKGVPISMEPVFSTAAGIRIDVKQESIDKSKKMLNSDLKSKSSSKGGFSSPLVRKNNGSSAFVSPFRREGTSSTTTKRPASGGFEDFEAPPAKKSTSSSSKKSKKHSKKEKKKEFKEIHADVLRVSRIYEKDKFRIILQESSSTPLILATCSYNRGSDIKFGDRIHVDAEVCKKSSSGDVTEIYIDRVLKNKENGAKSGIRRHSIAKKPFCIKPRFIHELSDTKIKKTVVQVNLLDLNLDFYAGCSKCKHSLPEAANQCEFCKDSQGKSELSMYSRVRVMDFSGQMFINVTTKNMKKLLDLLGYEGFDNWFRFKDPQERQNYVFRPVMVEIEKSNDEWECTDVAEVDWKDFGSYLKHKEDKKKRRSKKKHP
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Required for the homologous recombination repair of DNA double strand breaks, thereby playing a role in chromosome integrity. Acts by targeting rad-51 to sites of DNA damage and stabilizing rad-51-DNA filaments by blocking ATP hydrolysis catalyzed by rad-51. Promotes rad-51 mediated displacement-loop (D-loop) formation during strand invasion between the invading single-stranded DNA (ssDNA) and the homologous duplex DNA. Also functions independently of rad-51 in DNA double-strand break (DSB) repair by promoting DNA single-strand annealing (SSA) when the homologous recombination (HR) and non-homologous end joining (NHEJ) pathways are compromised. Binds selectively to single-stranded (ssDNA) via its C-terminus. Involved in telomere maintenance and replicative senescence.
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G5EG88
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ACH23_CAEEL
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Betaine receptor acr-23 (Acetylcholine receptor subunit alpha-type acr-23)
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MHRIYTFLIFISQLALGLSNNPDIPIQYELANNIMENYQKGLIPKVRKGSPINVTLSLQLYQIIQVNEPQQYLLLNAWAVERWVDQMLGWDPSEFDNETEIMARHDDIWLPDTTLYNSLEMDDSASKKLTHVKLTTLGKNQGAMVELLYPTIYKISCLLNLKYFPFDTQTCRMTFGSWSFDNSLIDYFPRTFTNGPIGLANFLENDAWSVLGTKVNREEKKYTCCPVNYTLLHYDVVIQRKPLYYVLNLIAPTAVITFISIIGFFTSVNPFTNFCNVSSSVHDLRQEKITLGITTLLSMSIMIFMVSDKMPSTSTCVPLIALFYTLMITIISVGTLAASSVIFVQKLGSIGNPPASKTMKWTHRIAPFVLIQMPLVMKQAYAKRAKEEKHRKRMSRKNSMWTKVYHLARDHSKLMETVPDGAVKFNQISDFKNNDIGNMESPRMAESQTSETFAAPMDTSFTESLHIPELNRVASSNSIQSVLKPTEIQLTPYCTRNIVELEWDWVAAVLERVFLIFFTICFLFSAIGINLYGWYIWYTENHFLF
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Betaine receptor that functions as a ligand-gated non-selective monovalent cation channel in mechanosensory neurons to maintain basal levels of locomotion. The channel is permeable to Na(+) and K(+) but not to Ba(2+) or Ca(2+) ions. Elicits current in response to betaine, very weak current in response to choline, virtually no current in response to acetylcholine and nicotine, and no current in response to glycine and GABA.
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G5EGA3
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ANKL1_CAEEL
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Ankyrin repeat and LEM domain-containing protein 1 homolog (EC 3.1.-.-) (LEM-domain containing protein 3)
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MPPNGAITTTPRSRMPPTTPSSGKSRPKKETLHYLAASSSTTSVDAARTLLERGANVNAIDRDGATPLHYACTHDNVAMAQLLLTFGADPMSADKLGRTAYSIAKGNTLRFLRRYKKSSNRQRLGFFRRFFACHSRNETFFIVRNNQEVAPLRPTALAEAASISFNRGNVLTNSYRCAKKKIRATFHAIRRSRSNSTATLQDVVLTSEGIRTVTTPSRRAPKATVYAKRSMSVSDLLLIPDRRDIKNEDVKTRGSPVKKTRGTGRSRTPEAILNPRKQRTPVNHHKRSKSQETKLVAMPSPNSMAYYNTSRARNAGLRPAPSAPPLSPEPAIAAVKTPKTPTTPKTSKGRSKSPANTTAYFTADESLELLGNNMEKLNIESKSAKSSKLKTPSKPTTSSSTSFSSAEDDKEAEVSTPTTVDDGEIRKIRRLREGELKSELKKFGISPAGPLDARTRRLYEKKLLIERRKITNRGYSPDADVVSCRNSPQLELVLRNGFLPADFASRARKCDENVRSEFSGNGFGYNAFCYLIMDPRILGSNVENLTLETFVRSIFYVGKGSKNRPLAHFIDARNERRDKLDKLKTCEKLKTIDELWTLGFGIPRHEISHGVSDEEAFVREASIIEAVKLKNLRNKKAGEFHGTTKSWDNITKSEYGTFLLDRALSTLKLEGIRLITEDNLPDSLYPYVNNRRGAGGGRTPKTPK
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Endonuclease which, in association with baf-1, plays an essential role during embryogenesis in the DNA repair response following DNA damage probably by ensuring proper chromosome segregation. Also required during postembryonic cell divisions after DNA damage caused by ionizing radiation to ensure normal cell proliferation. Resolves chromatin bridges in late mitosis that result from incomplete DNA replication, defective chromosome condensation or unresolved recombination intermediates. Together with brc-1, contributes to genome integrity by resolving mitotic chromatin bridges that result from incomplete processing of DNA breaks. In parallel to the slx-1/mus-81 pathway, acts in processing early recombination intermediates in meiotic prophase I to prevent illegitimate recombination. Also involved in processing remaining, erroneous recombination intermediates that persist into the second meiotic division.
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G5EGA5
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FAT2_CAEEL
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Delta(12) fatty acid desaturase fat-2 (FAT-2) (EC 1.14.19.-) (EC 1.14.19.6) (Fatty acid desaturase 2)
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MTIATKVNTNKKDLDTIKVPELPSVAAVKAAIPEHCFVKDPLTSISYLIKDYVLLAGLYFAVPYIEHYLGWIGLLGWYWAMGIVGSALFCVGHDCGHGSFSDYEWLNDLCGHLAHAPILAPFWPWQKSHRQHHQYTSHVEKDKGHPWVTEEDYNNRTAIEKYFAVIPISGWLRWNPIYTIVGLPDGSHFWPWSRLFETTEDRVKCAVSGVACAICAYIAFVLCDYSVYTFVKYYYIPLLFQGLILVIITYLQHQNEDIEVYEADEWGFVRGQTQTIDRHWGFGLDNIMHNITNGHVAHHFFFTKIPHYHLLEATPAIKKALEPLKDTQYGYKREVNYNWFFKYLHYNVTLDYLTHKAKGVLQYRSGVEAAKAKKAQ
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Can function as a Delta(12)/Delta(15) bifunctional desaturase and behaves as a nu +3' desaturase. Introduces a double bond in the fatty acid chain three carbons away from an existing double bond to biosynthesize polyunsaturated fatty acids (PUFAs) endogenously (PUFAs are essential for membrane structure and many cellular and physiological processes). Acts on a number of substrates like oleoyl-CoA ((9Z)-octadecenoyl-CoA, 18:1n-9), palmitoleoyl-CoA ((9Z)-hexadecenoyl-CoA, 16:1n-7), and gamma-linolenoyl-CoA ((6Z,9Z,12Z)-octadecatrienoyl-CoA, 18:3n-6), to generate linoleoyl-CoA ((9Z,12Z)-octadecadienoyl-CoA, 18:2n-6), (9Z,12Z)-hexadecadienoyl-CoA (16:2n-4) and (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA (18:4n-3) respectively. Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (Probable).
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G5EGB2
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LIN29_CAEEL
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Zinc finger transcription factor lin-29 (abnormal cell lineage 29)
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MDQTVLDSAFNSPVDSGIAGTTTGSGSTTHFGVGTNFKVSVRSSSRSTDGTDSTDGANSDNVTGSTGSTPAHHSITNLNMALSQHSIDSATAASSTNPFPHFNQADLLNFHQNSLLPHHMFSQFGRYPQFEQKPDVGVLQQQMQMREAKPYKCTQCVKAFANSSYLSQHMRIHLGIKPFGPCNYCGKKFTQLSHLQQHIRTHTGEKPYKCKFTGCDKAFSQLSNLQSHSRCHQTDKPFKCNSCYKCFTDEQSLLDHIPKHKESKHLKIHICPFCGKSYTQQTYLQKHMTKHADRSKASNFGNDVVPADPFDPSLLSWNPMQGMGDNAHDSSSFNISSLTDQFAANTMIGSQSTNYNPAFQNSAFSQLFNIRNNRYLSEYPTSTKNGERAPGFNMITPLENIQRYNGSSSSATAVVTATGSAVVSSTPSSTSSSSAGSSSSQGGVFNPQSLINNMKNHSY
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Transcription factor which regulates the expression of various genes, including those involved in cuticle synthesis and maintenance, such as collagens, and in lipid metabolism. Binds to promoter regions of genes, at 5'-[(T/G)TTTTTT(A/T/C/G)]-3' consensus sequences. Heterochronic protein which controls the choice of stage specific cell fates, including at the juvenile to adult transition. Promotes differentiation, together with transcriptional cofactor mab-10, perhaps as part of a transcriptional complex. Required for vulval morphogenesis and egg laying perhaps by acting in a subset of the lateral seam cells. Involved in the exit of seam cells from the cell cycle. Required for specification of uterine pi-cell fate, acting upstream of lin-12 Notch signaling, perhaps via maintenance of lag-2 expression in the anchor cell (AC). Involved in morphogenesis of the specialized male tail used in mating. Acts cell non-autonomously from the hypodermis to regulate expression of genes in the intestine, including genes involved in lipid metabolism. May regulate vitellogenesis via the mTORC2 signaling mediated pathway, independently of daf-16. May promote nuclear accumulation of mab-10 in seam cells post-transcriptionally. Dispensable for seam cell fusion.
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G5EGC9
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PES1_CAEEL
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Forkhead box protein pes-1 (Pattern expression site 1)
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MTSSIKSDAPQFLLDLDNCSSLPPTPPKTASPGNSKMKGFNISDLCLDLDSSTSSSCSVSPASSFHTRSESVGQQQSGRNSPVSSSTESPTKRPKYSYNALIAMAIQSSPFKSLRVSEIYKYISSNFSYYKNQKPLQWQNSVRHNLSLHKEFRKVRTLDGKGSYWAMTADLGTDVYISNNCGKLRRQKSKVAKFPPMQQHFPIPQLPTQNIHQLCMQNPQILATLLQNMYLQNMQNLQNIPMVPGFPIIPVPINPTSFHFPKSS
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Transcription factor (By similarity). Plays a role in embryogenesis and later development, perhaps acting redundantly with forkhead protein fkh-2.
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G5EGD2
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HIF1_CAEEL
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Hypoxia-inducible factor 1 (Hypoxia-induced factor 1)
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MEDNRKRNMERRRETSRHAARDRRSKESDIFDDLKMCVPIVEEGTVTHLDRIALLRVAATICRLRKTAGNVLENNLDNEITNEVWTEDTIAECLDGFVMIVDSDSSILYVTESVAMYLGLTQTDLTGRALRDFLHPSDYDEFDKQSKMLHKPRGEDTDTTGINMVLRMKTVISPRGRCLNLKSALYKSVSFLVHSKVSTGGHVSFMQGITIPAGQGTTNANASAMTKYTESPMGAFTTRHTCDMRITFVSDKFNYILKSELKTLMGTSFYELVHPADMMIVSKSMKELFAKGHIRTPYYRLIAANDTLAWIQTEATTITHTTKGQKGQYVICVHYVLGIQGAEESLVVCTDSMPAGMQVDIKKEVDDTRDYIGRQPEIVECVDFTPLIEPEDPFDTVIEPVVGGEEPVKQADMGARKNSYDDVLQWLFRDQPSSPPPARYRSADRFRTTEPSNFGSALASPDFMDSSSRTSRPKTSYGRRAQSQGSRTTGSSSTSASATLPHSANYSPLAEGISQCGLNSPPSIKSGQVVYGDARSMGRSCDPSDSSRRFSALSPSDTLNVSSTRGINPVIGSNDVFSTMPFADSIAIAERIDSSPTLTSGEPILCDDLQWEEPDLSCLAPFVDTYDMMQMDEGLPPELQALYDLPDFTPAVPQAPAARPVHIDRSPPAKRMHQSGPSDLDFMYTQHYQPFQQDETYWQGQQQQNEQQPSSYSPFPMLS
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A transcription factor which is a key regulator in various cellular processes including environment stress resistance (oxygen levels, hydrogen sulfide and cyanide levels and heat), negative regulation of cell apoptosis in ASJ neurons by inhibition of cep-1 via transcriptional activation of tyr-2, resistance/susceptibility to pathogenic bacteria, lifespan and brood size. Involved in mediating susceptibility to enteropathogenic E.coli. Increased levels of hif-1 activity confer resistance to P.aeruginosa-mediated death but also confer susceptibility to S.aureus infection. Required for aha-1 nuclear localization. Following hypoxic stress, up-regulates serotonin levels through activation of tph-1 expression. Role in life span extension is dependent of temperature. Not required for survival in anoxic conditions. Involved in iron homeostasis by repressing transcription of ferritin ftn-1 and ftn-2, and divalent metal transporter smf-3. May be involved in manganese homeostasis by repressing divalent metal transporter smf-3.
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G5EGE9
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DPY26_CAEEL
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Condensin complex subunit dpy-26
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MDVPSSSNVTGRRKRQVLDDDEDDGFRSTPLRKVRGTKKIRPADVVPETIMTKIGAHIDDIVNKKKVGELNCFEYKSPLEIHTIEDMIKAKASIQEMAVVLEGAQCIIGYRVDRLHHDVRQIDSALSSGTVMRDSNGEEIHLTLESRKAKKKMAVVDGMNGMLDFLNNMDDALTTTELDADNDKNWKEDEENIAGEPRIDFKANSKDVDAFLQRDIFPEKLIYALSIKRATDLRADLLSDVSNYISADDTAHDLKDANIDWLRANPTFQKATKGSVCNSSNSFHSLNYYGIHSPDGRTLMLHNRIADKNADDRFFTSDVSVSLVKNTRALLTNSLDKKPRILDNYLMLEVKDRPVIGRYKIMSKDVKKSTLPLAESSREKDLANLTFAEMNHRPSNLDMTVAGASDMSMLPGNQGLPLAQGENDETIALDRLTPPLQSSVSQKASDEYVLPPLEANDLDEHLIGKLPIEPNEMDQTLANMFDKKLEVFNTSDTLESKVWKNGIRAEEWGEDDEAIMKNDTKHPRQAGIEGWIKATDAWTNYDVVKMNVNREARSQLDENAIDEQESYRNMVPEIGKNLFLVKSDDYMNNYPGDRPADFTVNDEVSDVMKMWSGEDSTAEDDVPLEQIQQEIREQVQQQDVDMEPIEEMDYDAGGAAFDVDFDDRLAAPVEVEEMEGDNNRNDGRVADILFNEQMDETEVEERNEQDVQRELEDIALAADEVAELMTSAPPPQLVGPSAEMREEIQNIGKNDNAHWVPPVVGDQERQAAVTAQRKRREKKAKSRKATVEDFVHYFRDIPDDEIEREITAAKCSKIADEKSTFLSEQQLYLPTLGIENKPHVAFEMGLLGNSGMFFKKSYGKIRLERVKNQKAEQDLFIDEARGNKDSDCLNWLLSFSGFRCMENPEPITGSDSDENLRTAVEQPFDDDFANDYYDEDRYDPNYEQQLAAAQMGPDMQRKLALTASHINQMFPNIHSKRYGGEYGDSDDEFDDSFDRQSIQAKNLDAAKHKKCLAEILKTDSLSMPSIQYVLEQLTSNQTLRMNNTTIRAADDRNETGRPATPTMEADKTLTSVFDYRSPNKSNHDVNETMKALTEMPDYQAADERPNNQPTTSTYGTANTENRKVHINGCHTLLSLALSMPSRMGETVRPSSIVSFLLHIANENNLQIVQDRSKRSWMSDFIVLNSSESLPRGLKMGRIEDQDEFWKRTQDPDAIEGTASDANNVFSNLMRRPKAVPVRKGRGAGGQPTTSDLGAIVEEEEMEE
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Required for both chromosome condensation and segregation and for X-chromosome dosage compensation depending on its binding partners. Member of the condensin I complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes and for proper chromosome segregation in mitosis and meiosis. As a member of the condensin I complex, further controls the crossover number and distribution in meiosis by restricting double strand break formation, probably by influencing higher-order chromosome structure. Plays a role in robust cytokinesis upon presence of chromatin obstructions. Also a member of the condensin I-like dosage compensation complex that associates specifically with hermaphrodite X chromosomes to reduce their gene transcription during interphase, possibly through chromatin reorganization. As a member of the dosage compensation complex, also binds to regulatory regions of the autosomal her-1 gene, required for male development, possibly contributing to its repression in hermaphrodites.
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G5EGF4
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EGL18_CAEEL
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Putative transcription factor egl-18 (Egg laying defective egl-18) (Erythroid-like transcription factor family egl-18)
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MSISIMTETRPESAEQQHHEVLQRPSDEPCSGCKQLQKDVAKTISMVMERMDKLQYRLDELLKENNELKSSSVSSGKASPSPAESRSSPKLVETVVAPVSGARKRKPKERSPPAAASPLPDFSNLMNGFMFDPLNMSNPNGMMQLLSMVQQQQQQQQHHQHIENQQSVSPPQSKSVKIEDPMDQDVKQEESERSDIPTATEAQNLLDALTAQFSSNGQATSTTSPPSSSSQVQAVIEAVATPSSQSQDSSMFEKTETSGDPNAARCSNCRTDKTTAWRRDAEGKLVCNPCGLYYRLHKVRRPIEMRKNHIQQRYRRKNKEKESSAATQIFNQLLTQMPTMATGGVSTDGAINTFNLLEQISQFTQAQELMNSSATF
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Probable transcription factor. Involved in embryonic development and in vulval development in larvae, acting redundantly, at least in part, with elt-6. Perhaps acting together with elt-6, may form a positive feedback loop to initiate and maintain lin-39 gene expression to ensure proper vulval precursor cell (VPC) fate specification. Together with elt-6, acts as a downstream target of the Wnt/beta-catenin asymmetry pathway, required to adopt or maintain the seam cell fate. Required in seam cells, acting redundantly with elt-6, to promote production of alae, expression of several seam-specific genes and maintenance of seam cells in an unfused state. Plays a role in longevity. May form a transcriptional circuit with GATA factors elt-3 and elt-6.
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G5EGH6
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FAT7_CAEEL
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Delta(9)-fatty-acid desaturase fat-7 (FAT-7) (EC 1.14.19.-) (EC 1.14.19.1) (Fatty-acid desaturase 7) (Stearoyl-CoA desaturase fat-7)
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MTVKTRASIAKKIEKDGLDSQYLFMDPNEVLQVQEESKKIPYKMEIVWRNVALFAALHVAAAIGLYELVFHAKWQTAVFSFALYVFSGFGITAGAHRLWSHKSYKATTPMRIFLMLLNNIALQNDIIEWARDHRCHHKWTDTDADPHNTTRGFFFTHMGWLLVRKHPQVKEHGGKLDLSDLFSDPVLVFQRKHYFPLVILFCFILPTIIPVYFWKETAFIAFYVAGTFRYCFTLHATWCINSAAHYFGWKPYDTSVSAVENVFTTVVAVGEGGHNFHHTFPQDYRASEYSLIYNWTRVLIDTAAVLGLVYDRKTIADEFISRQVANHGSEESRKKSIM
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Delta(9)-fatty acid desaturase that acts preferentially on stearoyl-CoA (octadecanoyl-CoA) producing the monounsaturated oleoyl-CoA ((9Z)-octadecenoyl-CoA), one of the most abundant monounsaturated fatty acid in Caenorhabditis elegans phospholipids and triacylglycerols. Also acts on palmitoyl-CoA (hexadecanoyl-CoA), heptadecanoyl-CoA and (11E)-octadecenoyl-CoA (trans-vaccenoyl-CoA), the monounsaturated fatty acids (MUFAs) produced are further used by several other desaturases and elongases as substrates to synthesize polyunsaturated fatty acids (PUFAs) endogenously (PUFAs are essential for membrane structure and many cellular and physiological processes). Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (By similarity). Partially inhibits expression of genes involved in beta-oxidation, such as ech-1 and acs-2, perhaps signaling via the actions of one of its fatty acid products. May form part of a negative feedback loop with the transcription factor nhr-49 to limit beta-oxidation, in which nhr-49 stimulates expression of fat-7 and acs-2, and in turn fat-7 indirectly inhibits acs-2 and other genes also involved in beta-oxidation.
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G5EGJ5
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IDA1_CAEEL
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Receptor-type tyrosine-protein phosphatase-like ida-1 (Dense-core vesicle membrane protein ida-1) (Related to islet cell diabetic autoantigen protein)
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MRFFHSIIVLLFSISTGSAFLLYGCNLSENLCDNDESCYPDGVFGQCYSSESGSPEPTVLDNLDDTQLELLKLELTRLAAKDKDWGDEETQCVLAYFKMSMFYQLQYDPDFCQVRKPANVWALIQLIDTGLTEDPTILDEDVNPENVTDEDMAQIIEQLKEPSLPTEEDIEEALNAQNEDVDDEILDQYVQAVVNNENPDFSELSDGQLNILIGRLVDLKKNVENEEAQLLTGDGEQEMAVPLDDLEERGEQAILKKDIEQVGEINQGLDNTEHKIVKGRKDQVVTRVDANRVYLKVHLKNEDQLMPLIEFLQNTIAIPNNLYFDDFQFENGQLSMRISRFEGAKPKADKRIDSVEGVASAVYKRRKDIARLSGADVRETGIGSGEDGSLPVESSERDWLLMPVLFVCAFTVTALGLVAAVQIARSRRHYKDNIQQIAEQLDGKNSFAYQDLCRQRADGGRASKSSSTSSWCEETAVPTIDISTGHVVLNFLQEYLSEPTKIEAQWNGIKDYRNEERTKTKAEKFASQNRTILPFDDNIVDIDGKTAENEDFYLNASFIYDDDPRQAVYIAAQTPASSQIAAFWQTIWQHGVCLVVNLSTPEECKQEKNYWPDTGSEVHGAFEIHLVSEHIWSDDYLVRSFYLKNLQNSQTRTITQFHYLSWQKESTPTSAKSILEFRRKVNKSYRGRSSAVLVHSWDGSGRTGVYCAVDVLCARLLRGIRQIDVVATVEHLRDQRDGMVATGDQFKLVYGCVAQEVNHLLKSIATK
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Regulates dense-core vesicle (DCV) trafficking and/or secretion. Probably by controlling DCV trafficking, plays a role in the AVG neuron-mediated formation of the right axon tract of the ventral nerve cord. Involved in locomotion by regulating acetylcholine release. Probably by controlling the secretion of FLP neuropeptides, regulates the turning step of male mating behavior. Plays a role in preventing dauer formation.
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G5EGJ9
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DEP1_CAEEL
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Receptor-type tyrosine-protein phosphatase dep-1 (EC 3.1.3.48) (Density-enhanced phosphatase homolog 1)
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MIRWKYELHSLIWLFLVLHLSKCQSDSLTTSAEQHELFAIKKDSLSPWSQILVSLPRRHPLYQSFAAKIQDVTENISDEVRDSNKTFVSSDDAPYSIRIHALRAGHRYSIAIHGQKDGSTSLIKEESVVMDPRAPDFRSMDSDIQVAEHNITMRTIKNDSYLQDSFSIEYRQINPDKKFPVLQILDIPEQKNLEFYLGNLNSGFDYSVRVIAHKDGMSSRPWISTLTTKPSPLKEVNINQNAGSCVEVSWQNDEFSGADFYTIQYSLQSTPNNSTNMTIPSTESSISICDSMLQGEAYQIIATVQKGGQVSEPLITKFQLRPLPPIDFRVRADLKRGKYKLLAELPTSSKIDKCQITVAGDEAERSVNYANIEQTKSGHKICWFNFALSPGERFDFSISSMANESASQKLQKSIVLTPAFDFNAFGLTLQESNGGIELIWPKSEVFMTRVKDIWNKVVGAESLLNMRITPIGNNDETDKTLKFETSPKNIDPVFAKNLVKGACYRVQLFTVTKTGIISETRHNETIRMSSPAVNVSLESVTRSSATLRIVFSTHHDSTSISNCQMHIVVRDMNGKSVFDKRMQLTATFAPLLNLDGLSPFHKYTVNTQIICGSGSSETPQCPAATRTMRQLSFSTRQDKPAAVQDLKVEPLNSYSVMLTWLPPALPNGILTHYAVNVTKIGSDETRTIDVGVSSNRSDHTVQVVIDELFGGHTYSFSVRAVTEAGFGENSPVVPTVSMPLMAPPVPTVAPMIMKESVGSHNMIVRFPTTMFDNRNGEIKQFAIIVSETTADESINRWIESDNGTYTWQQVQRFDVWPSYVAKLQDIQKVKQDVDVSIFEELGEDETCLEVRADRICNGPLRSASKYRVRIRLFTSPTLFTDSPPSQVMTTGSATPAIPLLTVVAVLIVIAFVGIVGTIFLFFWNRTKKARLAAAAFKNGPSKEKESQWEALKMMMAERAADCLAKLGLDATTPPPSSTTSSNSPTSTSTTMTDCGSNPHLGAPNAGGHRRTRSLRERTGVEHRLERLSSGPVHRTPLYTVVTGANTNKSRPVRIEDFADHVRLMSADSDFRFSEEYDMMRNVGVGQSVAASELPINRPKNRFTNIPSYDHSRVKLSNPNNIEGGDYINANYVPGFSSRREFIAAQGPLPTTRDHFWQMTWEQQCPAIIALTKCVEKGRDKCHQYWPDHENVPVLYGDIEVTIVAEKEFDEFVIRDIRLEKSGPDGRVTRFVRHWHYMAWPDFGAPSHPNGIIQFSRMFRHHLPHSPHNAPTIVHCSAGVGRSGTFISIDRLLQSSSFGDPIDVFGTVCEMRYERCQMVQNEQQYIFIHYCILQVLQGSSPSPTSTSTGAHHNAGFVQDGQMIVESGF
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Phosphatase which may dephosphorylate receptor let-23 and thereby regulate cell fate during the development of the vulva and the excretory system. By inhibiting let-23 signaling prevents the establishment of a primary cell fate in the descendants of vulva precursor cells P5.p and P7.p. Similarly, may prevent duct cell fate in ABpr precursor. Also dephosphorylates the beta-integrin subunit pat-3, probably within the alpha pat-2/beta pat-3 integrin receptor complex, which leads to down-stream effects including the negative regulation of let-23 signaling and vulval induction. In particular, by dephosphorylating pat-3, promotes the recruitment (by unphosphorylated pat-3) of the cytoplasmic adapter protein tln-1 to the plasma membrane of secondary vulval precursor cells. This promotes the linking of focal adhesion sites to the F-actin cytoskeleton, and also acts to restrict the mobility of the let-23 receptor on the plasma membrane of vulval cells thereby attenuating let-23 signaling.
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G5EGK5
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CAM1_CAEEL
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Tyrosine-protein kinase receptor cam-1 (EC 2.7.10.1)
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MSPRPEDDDLVIEPADDEGLHYGNASMEGTSTGQRPYIRLTSQLRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAASVNTTSVLRVNNVPDAVKLSQKKGSHHSTKHIAFDEYEDYEMMDRGRLPDEEDADLYRVPDSAAGSNYAPVAVSERWLDGIKYRVGDCVQYRGEACRQYLSNKFVMMTNESREEMYDIDRNLRAAMLFINGAPTISQKCRQLSQAVACHHMYKVCESDSNNQIVSICKHDCDVIQNDECPSELALAAQHELVGDTPKALFPLCSRLSSTSNCIPVMSTALQSSPVAEVNRGHLTHWCYVNSGTQYEGTVAQTSSGKQCAPWIDSTSRDFNVHRFPELMNSKNYCRNPGGKKSRPWCYSKPMGQEEYCDVPQCPSDMYPHLNDKKVEGSTKGGVSESVTALWDSLDPTMQVALVGGGVFFSLLLLLLFCCACCCRAKKKSQKTRHQNAHCSSAPSVINSAANSAYYRKLNGTSTPIMGRVPPHVEMTSLLPSAQHLGPPPYPMDQHLQQARRFPSQEPIDDNSYKVFEITPSQLSVREKIGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRVPPADHDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSWSLASPAHSILQQHNNRAGSHSGSSGAGRPPTHQRGYPSQKLHRRVEGASPLMKRHDANYAYSEDGDSD
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Tyrosine-protein kinase receptor for Wnt ligands egl-20, mom-2 and cwn-1. Involved in the final positioning of migrating ALM, CAN, BDU and HSN neurons during development. Involved in the anterior-posterior migration of QR neuroblast descendants, QR.p and QR.pa, by maintaining QR.p cell polarization, probably through mig-2. In addition, plays a role in ASI sensory neuron positioning and functions. Regulates asymmetric division of V cells (seam cells) and CA/CP neuroblast, and axon outgrowth. Probably by acting as a receptor for Wnt ligand cwn-2, plays a role in the positioning of the nerve ring by controlling axon guidance of SIA and SIB neurons. Involved in synapse plasticity by regulating delivery and/or stabilization of acetylcholine receptor acr-16 at post-synaptic membrane sites and the distribution of synaptic vesicles at pre-synaptic release sites. Probably by acting as a receptor for Wnt ligands cwn-1 and cwn-2, negatively regulates developmental neurite pruning of AIM neurons. Plays a role in ALM neuron polarity. By binding Wnt ligands mom-2, cwn-1 and egl-20 and thereby restricting their availability, negatively regulates Wnt signaling. This mechanism is involved in HSN neuron and QR neuronal descendent migration, and in vulva development. Involved in dauer formation, locomotion, tail morphology and egg-laying. May be involved in distal tip cell (DTC) migration during the development of the posterior gonad.
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G5EGK6
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DIN1_CAEEL
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Daf-12-interacting protein 1
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MVQVPSTNTVKESRHVAISGLPSTLPDDRLQLHFTKFGEIQRLVRQHGNPEIVLVSYMDARGALRARSTKPQFEDSIEYKISAYIPEPTQNSSMASMSSTPSSGQSSSPRNAELSPQRYGDTRGAEVKSPSFRNQMEARRGGPHLSVQSQQRHSREYWPIPEFPSESTACVVYEIQSGSTPERDLFELVKKHSKRSGVPIDIQLESTTEPGWKKARVHYYRLDTDGLKADKSLILGRPPKFRVYYPTSGEQKHPQCHPSTSYAIPKLKGDHLLKASCSVHVPHLDRHSPDHYRRRFESYGQVIDVDMVKSNDNKAFAVVQFTNIDDAQKALQDTNIPKPMSYQSRPSHRIIIFYLPIECTNEEIMLIIRSLSDRIVDICVDWWDRSAVITLDDMEPANLLLKRMKLVGRNNFGEHKVAVDFCSDRFNLYFINRKKENIEVAARSSSPTSKSENDQGSSSPSSSRDRQNLHDPLQTRSSVEHHTNQEDQENNASGSDSSSDSDSEEGSSSSNEDSDEQNDVDEEDDEDVVSEEKRHEPEEGKSSSPGNGHRDESNGDKDHEDSSERFSQPSTSSHHETSHSPEKDSEAYQSRSFSPLNYQSQSPGYEFLESKEIKQEFSPTTSSASSSDLELDMEMPDNPLTRMLERMHWRPFIDVSSFVNRIDEIVELNQKARASYEKFTGRPFPKCNNDEVLSIQKIVFHEPRDYYYYENPCSELEVRIRDWRKLSDTADLDDFRATDSKELGRDQPAGGRTSGRPSLDESRTNRLSFDSTHHPAELAQRSHSLCIGPMTPSTPFPTSQPLLVNTTHLPGTSQPSTSGGITTPRSSQPPPLMSPVSRHNSMSSTGRPASIQTLRHQSVMFPPDVSIPPPPIPPTHDEMMAPRGTPPSRRSSETMVPLRSPPFGTPIQNLLTMPIVPPPHLIAATSTGTHSVSSSAHSTPRHSISGTPVHCEPSNSKTSQPPTPKSRPEKVQIRHDTISKSGPSNAINALQARSQSMTSGDPKKSAPSTPVVRDAGSDLVAQIMSNQPNLGLRKLPRIEKKSSALQNIQNHQPPHSNANSTPSTPSTSTHQAMFKDKEKERKKKEKEKEEREREARREMKRKETKEERNKRKEMERAKRLEDERQERKREKKKERDERKKEKEKVRKKAEKEKLKKKKHRKGDSSDESDSDSNDELDLDVRKSTKEMTQEEKDHQLALLLSKGGIIENLKSRRRSDKRAHDSFEKMQQKSQQRRVLIESSDDEGGKDGDKGNSSNGEESDSEKADLPPPPAPPSLSESADQRLKVLKEREKGELTTSSDDEDHNDAGEIHQQRLTEDRENRKRQKSLTAYSSDEQGERKNVPKRMRRDDSEDAAAKHPGWSAKDDQKQRKRKLEHRRSSEDESKKNAKRDFRDIPHEDVSDEEETEDGSRSRRQSTSSTISNVTAKERKEKSGKTPLRIVPEPTGTPLLSPKILSPKHLSPKTSTSSTKRSSISDHENLISPRQRNRTTSSTSTATTSSKHEALSIPEKPLSPPVTAKSSVSSIDDPSIRDEFSMNSAADSPMSTTGRPMVLTKAAMKAFNSTPPKKKNSSSGQHDSSSGSSSDSSSSDGSTSSDDSSDDEVPKQTEPVTSIPVVASDNGSPENVVVETPSIVSQTPREPEPFTISEQSSESEPEAVPECPEASVEPQMETSQNVEPVSEEHEDSHEHGDSEVAVESQQQPLEHQEEKEELENKILDVAAEHHEEQVQGDEDSVESSIPAPSDEPDPVTQAQEKSAHTLISDQETDQAVQSIFDEEEADEFPQYPDFGISTNEKEVSGKDPHNIKPTEPLNNGHTDLLFSPSSSAHASEKQSTKSEDDMEEDSELVVMEKEVPMEQVIAQEVHVPSEPSPMEEEVKLETSPVPKEEPIKMEESPEQTPTPDLISNNESQDTPGAVNNHLHENHDAVQTPIQLQPASQHQVAQPSPRPAVAPDSQQNGPVLVSQQSQPSPMSSQQSDMAQNLILSSKDINDLAAKLHKNPEALAQATRGDCSGIFQHLLLHAQGNGQNMTPEMLQLKAAFFAQQQENEANQMMQAKMKQQTINKDRIKEQERVKRMYEENERKVEEDRREKQRKEEERQRLAAATAAATMATQKAAEALKQKQEVPRHGFQHVLSMMTPEARSLYEQFPGLSSYINRDSIGATNGVLHLPTQSIQRPSSTASTSSNPPKAPLQPSASVNQNTIDPAEIEEIRVQRWFYKHFPMVWTGRLALKSTEAMINLHLINGSETFLNDVLGRQVTEENPRRDSVKILQRLRLDNGQVEHIYRILTNPEYACCLALSSVNNIENLKENDTNLKSHFIDYLINKKIAGISSLGEVETKFKSARVHVFAPGEIVNRYLSELATSLHDYLQNTDTRYLLIVFTNDKADPNMTGPPSVASLAVPPVSST
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[Isoform d]: Probable transcriptional corepressor which modulates activity of the nuclear hormone receptor daf-12 to regulate the dauer diapause.
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G5EGK8
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PP2A_CAEEL
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Serine/threonine-protein phosphatase 2A catalytic subunit (PP2A) (EC 3.1.3.16)
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MAAAPPSADPLDKALIVDVDQWIEQLYECKPLSENQVKTLCEKAKEILEKEPNVQEVRCPVTVCGDVHGQFHDLMELFKMGGKSPDTNYLFMGDYVDRGYYSVETVSLLVCLKIRYKDRVTLLRGNHESRQITQVYGFYDECLRKYGNSNVWKYFTDLFDCFPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRIQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHSNGLTLISRAHQLVMEGYNWSHDRNVVTVFSAPNYCYRCGNQAAMVELDDDLKYSFLQFDPAPRRGEPHVTRRTPDYFL
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Protein phosphatase which plays an essential role in early embryonic cell division. Probably together with constant regulatory subunit paa-1 and regulatory subunit sur-6, positively regulates centriole duplication by preventing the degradation of sas-5 and kinase zyg-1. In addition, plays a role in the recruitment of sas-6 and maybe sas-5 to centrioles and may dephosphorylate sas-5 and zyg-1 negative regulator szy-20. During vulva development, may play a role with regulatory subunits paa-1 and sur-6 in the induction of vulva cell precursors by positively regulating let-60/Ras-MAP kinase signaling, probably by promoting lin-45 activation. In association with regulatory subunit rsa-1 and probably paa-1, regulates microtubule outgrowth from centrosomes and mitotic spindle assembly ensuring the stability of kinetochore microtubules. Plays a negative role in axon guidance probably by dephosphorylating unc-51, unc-14 and vab-8.
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G5EGL9
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AFF1_CAEEL
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Cell fusion protein aff-1 (Anchor cell fusion failure protein 1)
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MRLWQWSIAVAICLVMVTEARLRRHHRKRRFVSSNFDEFYCGESAHAQSQFEEERESNSSKVSSVHSTQFNWGLDNTICIKLQNVVHVLKYERLEQRYPIENSYTFSVPLIDTNCKCHCYGFGTNDVCNVEKYADDRNCTTSSEFPTCYTKYHPAVEPLDCPVTSIPAKACCDIKLKPRDGRMFRAVKLQQPINDMIISHSIFANNSGKMMKVLGPDEFRINLLKGKEQFELTEYHRISVQLVASSPQQQLREGMYYFPEENHNDLREGKINEITESDLDKLGWYRRVGNDWQVATSGLLLRNAHKVVIKNCKGQVHMDQFSGTKNFVLRGTQYNDTYNERRVSDNNFVRSVKVDESSREITIVHEHGTAAQVSLKTDTRPNLTKSQSLLANFTGSITLDHDGNRMLNVTFFGVKGTVHIKMYVNDRKLIATFACTAQFGTSLKDDGSRISLPSTINQAQWVCILPDEQPTKSEICKWIPYEEKAMRTPRQEQSWSKGHSPCSQAECNSLKSGVSDLFPWIMNFDYFMAHGGDFTEWLKIGIHIVIAVGLLLLLILLFTKCLVPLACCSLSIPFKNRNKKKKKKNSSDY
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Required for cell fusion events during development including the fusion of anchor cells (AC), vulval A and vulval D rings, and late epidermal seam cells. Required for amphid sheath cell fusion induced by entry into dauer stage.
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G5EGM1
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MMPA_CAEEL
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Matrix metalloproteinase-A (MMP-A) (MMP-Y19) (EC 3.4.24.-) (Zinc metalloprotease 1)
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MFTGLHDILIILFLLVTLKIAQNVDHTKFLQKYGYLTSGDNQLSSESLSDALKNMQRMAGLEETGELDERTIQMMERPRCGHPDVEDHQKSRGKRYAPPQFKWKEKIITYGCKAVGTSTRISLDDLRRTMHQAASQWSELADVEIVESSVKNPMMVISAGRENHYPCTVRFDTKTLAHAFFPTNGQIHINDRVQFAMTNYTERMGANSLYSVVAHEMGHALGFSHSPDIDSVMFAYDTPRKWKFTSMDKYNMRSYYGAKASKKENEEEERKTENEDKRRKTEKDRGRTREHESDDIRPNECRVENPIVVQYRGEYLIFKSQWVWRVSSDWKRLIIKAVPINQLFPGLPNPIDAAVTVGHNLWVFVGEMIYVIYGNHMVHAPLRLSDIGINEKYVDLAYEWHYFNPPAVYIWKGSRYWKLDEKMYHRRVDERYPKDTDLNWARVPKGVHSAFTYEKEIHLLRGNQVFRMNSSRSVFDIADGYPQPLQSFFGFCPRNEKLVLNSSSSHFSLIYATITILILIF
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Metalloprotease which, together with cadherin cdh-3 and hemicentin him-4, plays a role in anchor cell (AC) invasion during postembryonic vulval development probably by promoting the degradation of the basement membrane separating the gonad from the vulva epithelium.
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G5EGM3
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TAF1_CAEEL
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Transcription initiation factor TFIID subunit 1 (TBP-associated transcription factor 1)
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MNNTHHHTNGYRTEKPKNEEDLEDPYANLSDFYKNHPAARNEACSSASNGGSKSVKMEPKVEKNEEFEEYIGDPVRLEDMEPFARPSLRDDAPLSSILHPDLDGIDPRIFFKDFNPNKTLRFSRLFAQNIKHTSRAEIWWASRTFSKHQRKKEPEEPLADDVIVGAKKLKLNIIEKVPRVMLADDEEERMRRPILTDAEEMAKKNEEGTVVQPWRTGPAKIWYDMMNLPMTSQAVNYGFKLKKSPQKVSIRSGKPLNYRTPDDLPSTSSGPAPNSAPFLDKVEVIDKSCEASTSEDILLPYQVIEWENDVILDGEEVKDQLLEEFSNGRGCGWIPTQYTRTYEHFVYAANNNAFEQMFDGKSAPINLTGPDSAILPTPGHSIFPSAPCDLDILPWETNIIWDADAMPSTLEPIDFLVDFQDDPLIYGMPEDRRHDEGPDHHHHHHHHRKDGQYTKKSKMILGQVQQRQKQEEDEQMESTMAQFTDNDPFNLSNDDYYVPKATSKTLSNNSLLIQHSTPATNIATHFFPTHPSAFRLRYWHRTPFTRRIVRHWQPMRFQPIQTPVKHQQRVAAMREAMRQAQGGGEVFYMRDVQDLSGKDETLVMIEYSEEHPVILSQPGMASKMKNYFKRRQANDSEPTFTFGELAFSHQIPFLGQLQPGQSLQSIENMLYRAPIYLHKRQNTDFLLIRSMNQWYIRPLPSIFVAGQQCPLYEVPSPNSKRATVFVRDFLFAFIYRLFWASDSSPRRLKMDDVRNAFPHYAESNIRKRLKMCSTFVRQGSETYWSLKPDFRLPSKEEVLSMVTPEMCCAQYSMMAAEQRLKDAGYGEKYFFTPENDEGSEDEVTIEDEIKCAPWNTTRAFLASQREKCLLDQTGIADPTGCGQGFSYVRVSQKPHKDENATPVPKKLVTGTNADLRKLPLKEAKQICRGYGVKEEEISALTRWEIIDVIRTLSTQAAKATKDGEIIAVSGMARFARGNTRFSSADMQEKYRKHCQRIFDQQNQTLANTDPISTDDDSTDADSDNEELASRLESMLEANKGKKNISMSEKAKIDFETEEKEREDLKRMIHGTTNQVEKGEKKEEGEVTAEEKKSASQFGEDVAMSASKISGITANQQLKIYRTCKGPDGKDVTRIEIVTRPQLIEAYTRIRMTRDDTFIQVYAQMDEQYKEEKRKKKRRLQDQIRRMKKNEEKAAHKVQKMTEKKVKPIKPPNPNLQKMRCSACHAYGHMKTNRNCPLYGKDPLTPLKEEDEGSTIMTSVSSASLVAPDAVQVDGTKVKFNLNFAEIRKEQNREEKLKRKLAKMAEAAVRERQMAHLMEYGGGASSSGGAGGGGSGIGGSTGGGITDNDDDDRFSQISGTSSFLNGPPGAIRGGNRNSSVSGSKRRSSMMPEEDYLQGPLKVAHRARADPKVVMSSMLTDIVNELKMISGSDAFVTPVNSKKVVDYYNIIKNPISLQEIKKKISEQSYLLRKDFLDDIKLMFDNSRMYNGDNNILTLTAQQMLQLAGKRMIEREQKFIGLEKQINPLLDTNDLIGFSYLLGEIVQKMKNIPKSALFHTRVDPKKIPAYYLKISDPMDLSIMEQKSKSQEYKSIDEFLKDAEKIYTNSVVFNGAESVYSLKAKEMFEMAEMLVKDQMDTLGELERNINPSAINDAAAAQRGLAMDSDDHMDEMEDHPTEEEEEDDDDEIMDDDMDIDATGYSYDHDDNVAVGQIFNDLAMSDSDEDERAEDVKRPANGDDNLLDSF
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The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (By similarity). TFIID recognizes and binds promoters via its subunit tbp-1, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (By similarity). The TFIID complex consists of tbp-1 and TBP-associated factors (TAFs), including taf-1 (By similarity). May regulate RNA polymerase II activity and thereby may control transcription initiation by RNA polymerase II. Required for early embryonic development. Essential for embryonic transcription of several genes.
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G5EGN2
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FAT6_CAEEL
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Delta(9)-fatty-acid desaturase fat-6 (EC 1.14.19.-) (EC 1.14.19.1) (Fatty-acid desaturase 6) (FAT-6) (Stearoyl-CoA desaturase fat-6)
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MTVKTRSNIAKKIEKDGGPETQYLAVDPNEIIQLQEESKKIPYKMEIVWRNVALFAALHFAAAIGLYQLIFEAKWQTVIFTFLLYVFGGFGITAGAHRLWSHKSYKATTPMRIFLMILNNIALQNDVIEWARDHRCHHKWTDTDADPHNTTRGFFFAHMGWLLVRKHPQVKEQGAKLDMSDLLSDPVLVFQRKHYFPLVILCCFILPTIIPVYFWKETAFIAFYTAGTFRYCFTLHATWCINSAAHYFGWKPYDSSITPVENVFTTIAAVGEGGHNFHHTFPQDYRTSEYSLKYNWTRVLIDTAAALGLVYDRKTACDEIIGRQVSNHGCDIQRGKSIM
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Delta(9)-fatty acid desaturase that acts preferentially on stearoyl-CoA (octadecanoyl-CoA) producing the monounsaturated oleoyl-CoA ((9Z)-octadecenoyl-CoA), one of the most abundant monounsaturated fatty acid in Caenorhabditis elegans phospholipids and triacylglycerols. Also acts on palmitoyl-CoA (hexadecanoyl-CoA), heptadecanoyl-CoA and (11E)-octadecenoyl-CoA (trans-vaccenoyl-CoA), the monounsaturated fatty acids (MUFAs) produced are further used as substrates to synthesize polyunsaturated fatty acids (PUFAs) by several other desaturases and elongases. Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (By similarity).
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G5EGP4
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VPP3_CAEEL
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V-type proton ATPase 116 kDa subunit a 3 (V-ATPase 116 kDa isoform a 3)
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MGSIYRSEHMKLCQIFFQSESAYQCVAELGELGMAQFIDLNEEQNAYTRKFVNEVRRCDEMERKINFVEDEITKDLVPIPDYDEHIPAPQPKHMGEMEANLEKLEEELVQINKNCKVLKNNHVQLLEMKAVLEHVTSLLDPHSKREAAMSISEAARGEAGPISFGMKDEFDKPVKDEKELKFVTGVVKRSKAIAFERFLWRLSRAKVFAKFIQIQEQTELFSNEFEDKCVFILFFSGEQLRAKVKKICDGFQAKCYTVPENPAERTKLLLNIKVQTTDMKAVIEKTLDYRSKCIHAAATNLRKWGIMLLKLKSIFHTLNMFSVDVTQKCLIAECWVPEADIGQVKNSLHMGTIHSGSTVPAILNEMETDKYPPTYFKLNKFTQGFQNIVDAYGIANYREVNPAPWTIISFPFLFAVMFGDAGHGIIMLIAASAFVIFEKKLISMKIKDEIFNTFFGGRYVVLLMGMFAIYTGFIYNDFYSKSVNIFGSSWVNPYNQTLLANMDAQGADSNTDLSLTFPPEIAFNHDYGPYPFGVDPVWNLAINRLNFLNPMKMKTSILLGISQMAFGIMLSLMNHIGNRSVVDIVFVFIPQCLFLGCIFVYLCLQVLMKWIFFYVKPAYIFGRLYPGSNCAPSLLIGLINMFMVKSRDASFAHDVGTAAGKEWVIVNGQNVTYTINDQCYLQQWYPNQSLVELILLLIAVVSVPVMLLVKPFYIRWRHSRGLHIDLGHGPDEHGEFNFGDIMVHQAIHTIEFVLGCVSHTASYLRLWALSLAHAQLSDVLWTMVLRMSLTMGGWGGSAAITILFYFIFSILSVCILILMEGLSAFLHAIRLHWVEFQSKFYGGTGIQFEPFCFTKIIRVYEGLDQ
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Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. In the intestine, required for the rhythmic defecation behavior by promoting acidification in the gut lumen following defecation. Also, luminal acidification is required for nutrient uptake.
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G5EGP8
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CATZ1_CAEEL
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Cathepsin Z-1 (EC 3.4.18.1)
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MRTFVLLLALCAICILASSAYGKVRKYSNRNRYNLKGCYKQTGRVFEHKRYDRIYETEDFDSEDLPKTWDWRDANGINYASADRNQHIPQYCGSCWAFGATSALADRINIKRKNAWPQAYLSVQEVIDCSGAGTCVMGGEPGGVYKYAHEHGIPHETCNNYQARDGKCDPYNRCGSCWPGECFSIKNYTLYKVSEYGTVHGYEKMKAEIYHKGPIACGIAATKAFETYAGGIYKEVTDEDIDHIISVHGWGVDHESGVEYWIGRNSWGEPWGEHGWFKIVTSQYKNAGSKYNLKIEEDCVWADPIV
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Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (By similarity). Plays an essential role in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed. Probably, required for the degradation of the old cuticle.
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G5EGQ3
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MAX2_CAEEL
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Serine/threonine-protein kinase max-2 (EC 2.7.11.1) (Motor axon guidance protein 2) (p21-activated kinase)
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MSTSKSSKVRIRNFIGRIFSPSDKDKDRDDEMKPSSSAMDISQPYNTVHRVHVGYDGQKFSGLPQPWMDILLRDISLADQKKDPNAVVTALKFYAQSMKENEKTKFMTTNSVFTNSDDDDVDVQLTGQVTEHLRNLQCSNGSATSPSTSVSASSSSARPLTNGNNHLSTASSTDTSLSLSERNNVPSPAPVPYSESAPQLKTFTGETPKLHPRSPFPPQPPVLPQRSKTASAVATTTTNPTTSNGAPPPVPGSKGPPVPPKPSHLKIASSTVSSGCSSPQQYSSARSVGNSLSNGSVVSTTSSDGDVQLSNKENSNDKSVGDKNGNTTTNKTTVEPPPPEEPPVRVRASHREKLSDSEVLNQLREIVNPSNPLGKYEMKKQIGVGASGTVFVANVAGSTDVVAVKRMAFKTQPKKEMLLTEIKVMKQYRHPNLVNYIESYLVDADDLWVVMDYLEGGNLTDVVVKTELDEGQIAAVLQECLKALHFLHRHSIVHRDIKSDNVLLGMNGEVKLTDMGFCAQIQPGSKRDTVVGTPYWMSPEILNKKQYNYKVDIWSLGIMALEMIDGEPPYLRETPLKAIYLIAQNGKPEIKQRDRLSSEFNNFLDKCLVVDPDQRADTTELLAHPFLKKAKPLSSLIPYIRAVREK
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Serine/threonine-protein kinase, which phosphorylates mlk-1. Involved in the stress response to heavy metals by activating the mlk-1/mek-1/kgb-1 pathway. In ventral cord commissural motoneurons, required for dorsal axon guidance downstream of unc-6/netrin repulsion receptor unc-5 and probably of Rho GTPases ced-10 and mig-2. Plays a redundant role with mig-10 in orientating axonal growth of HSN neurons. Plays a redundant role with pak-1 in P neuroblast migration and in distal tip cell (DTC)-mediated guidance of gonad elongation probably downstream of Rho GTPases. In association with pak-2, plays a role in embryogenesis. In association with pak-1, may be involved in spermatogenesis.
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G5EGQ6
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TEN1_CAEEL
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Teneurin-1
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MFQHRTTNAQGPPPNRPMPRPPAGMPMMTSSHEHDYTNDYEDPEEMARSRGEGFSNHLLIKTTPPPQPHPNFNSYEMSMSQQRRSQQHQQPMAPPLSDCWGSGVHDSGVLHKNADGAYYIPSGSLRTTSSTLSPASGQRYLDQPHTSGGAPNPTYSDASTTLLKYPLAAGTNQNRRRQQVGTMNNGDPVAGGPMALSKKKKKFDDDSDTCSRWPSKWNILLAAALLVALFVICILLFRAPNYVYTQPAPSSDATSSAAAAASRYQDLGLRALPPAISLGERVDVEFFPKSMATTELTVTKPSRIRFNATVGSGAQLVLLMSAGVHPSLSLHDALFPIRADRIRDSKSPTHIVEEFGSRSRRSLGASSSRHRNIEILSPRSATFEQFVLEGRHYLTFINERSRVEPISFVAEELQRPTTPPKTSSSGTSGAKEHPLASVLVCESNCNQRGECVHGKCHCAPGFTGRTCDEAVCPVVCSGNGVFSGGICVCKSGFKGKECEMRHNWCEVADCNGRGRCDTDGRCRCNPGWTGEACELRACPHASCHDRGVCVNGTCYCMDGWRGNDCSVFADAIVHVPQAQSPPRRGQEPTESSKTRKAQVKPTPTSEKKKESRELQKPIIATVQVPTESSHPCSAHGQLIDDICQCESGWDSVDCSQQACQCVNGDCLDDGSCQCWKGWRGSNCTDKKCAIGCEDRGKCASDGSCKCSSGWNGENCAIDGCPNQCSGKGECGMDRRSSEWSCRCQAGSTGVDCSVSVEMHCDDGLDNDSDGLIDCDDPECCSSSSCSSESVCSTAASPIEVLMRMPPIFNANFAQRVGFLIMEKSVQSYTDSSQFNENLISVIRGRVMWGGSPTGSDDLSTYSNKSTVPLVGVRVSDAAHPLYGFTLTREDGYFDLTVNGARSVTLQFLRTQFQSVKKSVFVSPRQIIHIDDIVLYRQSGGSPPAISMAPARAKCSPTLRRIPDVVLISNWQYTSDGIETDETSDSSRIVVDSRSIFESLPIQGTDVRLVYDSARSPAAPSTMLIGLLYDRVDKELRKVHINIRIAGRRFDRVLAPRTNLTYVFAWDKMNAYRQSESGLVPVTVRVGYEYQGCDRTSERVWQTRRSQMMGATARKMIGTMWTLDIHHHLDIVNNVVEMGNGGYRLITESEPRVSTFAGLDGVKRDVECLKCEGKVDSISLFRPTTVVYAQDGSLIIGDHNMIRRVSQDGQVSTILTLGLADTSHSYYIAVSPVDGTIAISLPLHKQVWRISSLEPQDSRNNYDVLAGDGTVCASAVDSCGDGALAQNAQLIFPKGISFDKMGNLYLADSRRIRVIDTTGHIRSIGETTPDQHPIRTCAQITKLVDLQMEWPTSLTIDPITGSVLVLDTNVVYEIDVVHDVVTIALGSPTTCDLANATSSASAKSLDHRRHLIQNARDITVGTDGAIYVVESDGRRLNQVRKLSSDRSTFSILTGGKSPCSCDVAACGCDDAVSLRDVAASQAHLSSPYAVCVSPSGDVIIADSGNSKIKKVSARMAKYDGRSRTYEVTDAERQEKYTFNRHGQHSSTVSLITGRTFFNFSYQVDSPISMISEIRAASGVVLRVLKRNDSLFDLETTLGQRTTLTMSAYDGTLEQVSKRDSATSRDATKLFYKKGLLTSRIDVATAVGFEYDEYGRAIGLKRDREYWRLGEETISMGSVNTEVLLNGQRFQQVRLGEGNLAVHSTNGATTRLISLRNEGYSLASPLGTSTLYDKSSSIPDSNGEPLISRRRTKVPAIGNPQRRELTTRWDWRHVARRGDDSDGSLGRRKVAEINGVNMFSMEYDVKSNQDTLRLGSTTDDAQALLFIDYTSSGRIRRISAPEDSQMAEMNITWDGAGRKSEVTWGSWKIRLTYDNSNRLTEHAIDGARVPIKMSYAGASRRPNEIQHDGAKWNIQYDNYDRIKEVISKSQEATSFSSIALGGDEWVLKRRTSLNSKPSLVRLSREGKVLESTTPDENHYWLERKDPITGRTTEILNDEETTVVTCWSPEGAPMCSRSRNLQENTTMQGHLVARKSVTIMTPTSSEPSITSSFTYEYDDMLRVTTIQPVIEQSVLESIQLSYDERRGHVAAINGFKWARDASTSRCQGHGLMYETSKANDHRQVVERKLIFGDARASIKIIRDKAGRASESHLEISSSGTQRNQKITRTFDAAGRVASVEQNDQEPVRIIWNSDARVEKINDRVVEWNRGGALKTFQDISYQVDSIGWVVKRDNTTVFGYDGKGRLVSARSSQLRINIFYDREDRVVQIQNSKDFIHFYYGYIDTPKLVSHFSKNGKISTLFYDDDSVPFAMQSDDGTRYALLTDETSTIKAIIGDSNVLRIIDRSVFGALLPSSSSSHPFLPIGYLGGIEISEISVSILNNGRPLDLYSERYMSISPEAVVRLELNEKFSNSIDLMALEIDRQPFRVENVPEDFETWFSLAGLSPNLLPSAHLGLPASSAIVHRLLSSFPRKLRPLTHLTTVLPTRLASDISLTSPTSETSWSIDDVGFSNLLILNEDATTGEVMVEMLSDLKSEEREVISKLFDGVKSLDFATWGLVPTRHLWRAPNSKLELSSTSFSHFTMAVNKDSVELRNGKSKIVVHFSENKAEIVKKIVEELKTRENIAVWRAERKRAEAGEKTWRQWSDRETRELTSKGSVSGYDIEMKPAHQSGLLASVHSWKFRKSE
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Plays a role in the gonadal basement membrane maintenance and/or adhesion early in development. Contributes to the guidance of pharyngeal neurons.
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G5EGS3
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KLP12_CAEEL
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Kinesin-like protein klp-12 (EC 3.6.4.-)
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MADTCVQVALRIRPQGNREKLEGSRVCTSVLPNDPQVTIGGDRSFTYDHVFDMPTLQYVVYESCVEKLVDGLFDGYNATVLAYGQTGSGKTHTMGTAFDAAVTQKEEDLGVIPRAIQHTFRKIAECKAQAIEQGLLEPAFEVSVQFVELYNDDVLDLLSDDRSMSSSIRIHEDSRGEIVLHGVEQRSVFDMHGTMDILKNGALNRTVAATNMNEQSSRSHAIFTLHLKQQRVAANPLDESGEQKTGELEMEMLCAKFHFVDLAGSERMKRTGATGDRAKEGISINVGLLALGNVIAALGGANGKVSHVPYRDSKLTRLLQDSLGGNSRTLMIACCSPSDSDFVETLNTMKYANRAKEIKNKVVANQDKSSKMIGELRSRIAALEAELLEFKQGRRTVDVDGHEVVNDQYHENVYLTSEVNHLRFRVKALNETLDILRTENIDLKAKQEFNSIASLPTAGSGGAEGEVDAIQSTFRKYLEELERTKSLLYESQSTCDQLRKDNARWKALGASRGSGGGNAEFNSQKLIEMAKQEVEKQRKLMESVNIGGENVSSEYSSMAQDEDGTSNEAEELLDEEDLDEDEDETAEEKQEQEESEALQIDLSEVMIELDIKEKLIDQLERAERQNQQIRETYEKKLRELMERIKDTETERDRVLNEGGKRGGNNEQMKAIKQEYELKITDLRKELKKIEALDKEHLKVIAKSQRELQEKTRLKSEVVDLKKAKVELIKKMNEDKKKQKTQQLANARAFATKEKQTRLQANKIRTLEMKDKQREQFLKKTTQEVNALRKEKAVAAATARQANRGTPRGGAAVTNSPARRVRGVVGGVQAIKELAFSAKASKVKWDVIVRKIEESARRRQIVQKMEAELERYLNERHAVMVEIVENEKQFTQSQDVIYRDGLLEAIDSAKQKLQYVQDQITYQQKLICDVDEDITASNAENEPILDVGLKKQTIKQLFDGCDTLSEARYLLQHLFDLCIDKAALAAKVESEFKECAARIEQLEQQSSLKEQLLTSIIEDKNLVDEIEGFVPSDLRKSRTSSQSSLLRSGSPSVVEDAHTLQNYKVRRHTATQEELLFANSEENSMVSDANANPTVDVGADVGDSDERKEKKKRIAFVSTSPASTSFANSTSQSPSFSRNTRFRSTVGGVSNNNNIRKSVQPLINGKGVSSTARKGISRLPSVTEDPEIGIFAKSFPGRSRSNLMSSSSSTTTTTLSSSNLLNPRGTTSSSSSKSVFARISPSWLSDTCAELIMRNNNRKQSRIVPVKDGMRGNVITRTHTLEGHARGVLSVDVNEKLMVTGSKDRTAKLWDIEACREIRTLGIHPNNVHLVKFVPFSNYVFTFSMFEARAWDYRTPECICVKVLNSSGQVNEGDSIDVSQVMPRQNTIPFLETLITAADVDPTGQLLFTSFSAYVRVWNLREWKPLGRLNAASHSPKSEVSCLRTTMTPEGSILAYTGSRDHYVKEYEVGLGTGVIESKCEFTPPHYDNVTAVLPLNGHLYTASKDVNIMKFSLKDGKREHLELRAHQQYIQSLTGFGPKGKELLVSACKDGTIRFWDVGSSSRMKLVEEYSKAHQEGINDMCSTKSMLFTASGDSTVGFWKSNAV
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Microtubule-binding motor protein which has ATPase activity. In complex with alpha and beta tubulins, preferentially binds to the growing microtubule plus-end to stabilize it and detaches following ATP hydrolysis. Negatively regulates axonal length through inhibiting microtubule polymerization at its plus-end.
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G5EGS5
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GBF1_CAEEL
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Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 homolog (BFA-resistant GEF 1)
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MATNGVYIVMGEANCVVALLNKARRQYQLSQVPTLEDTDPLLRNFTDLKEVLNEVADLADMNPQTYLSPFLDVIKAQNTNGPITEAALAAVAKFLNYGLIDASSIKAANAVESIAYAVVHTKFIGGKSTGSDECVLFKILQVLRSLLLSPPGILLSNEAVCDMMQSCFRIVFEQNLSLLLRKAAESTLADMTQLIFTRLPTFVEDTRHPYIRQLVNPTEKRQKRKKKRQLSVHIETKAKEPENVPTEMTKLIGEAAETAETDGAANLGYDVVLTTDPPVDTVTHPDPPIEEIIKLAEPISAGDEADSESEGGGGEEHHERPPVRAHAGLQREIVSDEEEIDTEQTVGGEEKMPYGLPCCRELLRFLITMTNPVDRHNTESMVILGLNLLIVALEAIADFLPNYDILMPLIKNELCRNLLQLLDTNRLPVLAATNRCCFLLFESMRMHMKFQLESYLKKLQSIVLTEEKQHENGGGGTEQKEMALESLVQLWRIPGLVTEMYLNFDCDLYCGNIFEDLTKLLVENSFPTVGGHTASLLSLDALLVVIETIEQNCEDRENGRGEVAKEQEHKDLKKLGLPVLSGYDLAKKMAISTGGKASPMPVSSSIVLRSNRHAPSTELPSMSQIIEQKKRKRLIAEGTELFNQSPKKGIAFLREKGILGHDEQSLVQWLRTNPQLDKKAIADYICNRKHAEVLNAFVKSFPFENTRLDVALRMFLETFRLPGESAEIALVMQHFSEEWFRANNEPFFHVDAAFTLSYAIIMLNVDQHNPQAKRSQPPMTVDCFRRNLSGTNDSRDFDPEMLADMYQAIKTEEIVMPAEQKGTVKEDYMWKVLLRRGETAEGSFYHAPTGWNDHDLFAVCWGPAVAALSYVFDKSEHEQILQKALTGYRKCAKIAAYYGMKEVFDNLCIHLCKFTTLTSMRDGGAGGGADEDVDLSAAALLSHSSSPEAVALAFGENHKAQLATRTLFYLVHENGNILREGWRNLFEALLQLFRARLLPAELTEVEDYVDEKGWVNIQRVHQKELPHTRNDSGLLSWFGLGGGASEADRRKPTQEQLSSMKLASQVISECRPSQIVADSKYLTSTSLAELLSSIAANSAQIVEQAEPQQKTASLSGEDEDALVFYLELIVAITLENKDRLPLVWPHVRRHLEWLLSPRFGRCPVLVERAVVGLLRVANRNLFRDNTVSDDVLHSLSMLLRLSPKALFIFSRQIAFGLYELIRANAANVHKKEHWAVLFALLEAAGAAVLPDDYVMMTTTEKQQQSLRVGGDQQQQRMAYSDVEGASGRGGGAHEERAYTSEGEERRRGGYDSNSDLESRVDSAGSLLGAQKQPADWIHLDHKDAAKATEEALTALGANVVSSKKNFRQFGSLVLRNGLGRHEPAAFLKVCECLAFLLRDAVHVTPDNFESSLQCLRTMVEASLDGGVYAAGPLSGDAQNRLRSNVTDEKAVKKHHHHHHGHKKKELCTDVTEDADESRNEEQQLIGNYQQMSLHLLDLCSQLHSQTPAIFAKWAQGASPAASDLATVAFIWTDIWRPLLQAIGRLSCDCRRGVRAAALTHLQRAFLPANMATLGAAEWQSCFGEVLFPLLTKLLEPFSQMDPIGMEDTRVRTLQIVAKTLLNHLSALSALDSFPDLWMLLLDYMEQYLRVDSCGNLNEAVPESLKNMLLVMDSTGIFAATPRLYDVTVERLNKFMPELIKDTIPNPPRPGQQQSEASEPKKEHASGLEPPPPSSNSTAATSTSDPSIATAQSSISTASSVVGPLVTCPEDAGISAPIPIQHPLTEVIVHSGPTSPIGSPPQTEPPASSPPQHQHSEHQQYEQYRQQQAAAAQQYQQYNQNYPQQQQQQQQQYAYSPEHAAYYQQQYAHQQQQYAEHYANQYQHYQQQQQQQQQHPVNPTSPSVHGQYSVANPLPLPAHPAYHPIVAPSVNSAFTHVYTPPQNNAPALAPSAPTTTSADSPYFTPIPYNPSQQEKP
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Guanine-nucleotide exchange factor (GEF) for members of the Arf family of small GTPases involved in trafficking in the early secretory pathway its GEF activity initiates the coating of nascent vesicles via the localized generation of activated ARFs through replacement of GDP with GTP (By similarity). Also, plays a role in receptor-mediated endocytosis in oocytes and endosomal trafficking. Involved in vesicle retrograde transport from the ERGIC and cis-Golgi compartments to the endoplasmic reticulum (ER). Plays a role in maintaining mitochondrial morphology, network organization and function. May be required for the basolateral cell membrane localization of the serine threonine protein kinase sgk-1 in intestinal cells.
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G5EGS7
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SEL7_CAEEL
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Putative transcription factor sel-7 (Suppressor/enhancer of lin-12 protein 7)
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MAQPNQPTPQFQMAQIPLAAFFDNNESKTMLNSMNLRLNDMDLKLSLILELLATRLPDQRLPSIFTSPPQTVISEAPPQSFTPSATNSTSDKTSSSLKTELKTEDSDGDLDMEGEEDTEELFDNESQPSQRNQSPKETEVEDEKVLADGPFPEGAVKRAAEKAARSFQSTQPKVFAWQILRESVTDDELRNVQISLRTFHGETADHLLGRQLPKIRLVVEATMKYFKWDLLSTESQLSKAKLILSHLKNNAKVRNWTLREGRPNRVAPATPPVNVDLVWKRYLALLGPAGFTGILPNLPQNLCNGGTQSPSIPQIDPSLFKVDA
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Putative transcription factor. Positive regulator of the lin-12/Notch signaling pathway. Binds to specific DNA sequences in regulatory elements. Involved in cell fate decisions that require cell-cell interactions, such as the anchor cell (AC) / ventral uterine (VU) precursor cell fate decision. Heterochronic protein which controls the choice of stage specific cell fates, including the larval L3 stage-specific fate of seam cells. Involved in regulating the temporal expression pattern of hunchback-like protein hbl-1, thereby playing a role in the progression between larval stages L2 and L3.
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G5EGT9
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RYK_CAEEL
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Inactive tyrosine-protein kinase RYK (Abnormal cell lineage protein 18)
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MILRYLIFFAQLWALCLANVNMFISKEEMNRTFGVKAELNYIEMGNVSSYSTKFHYRVMANIDYLSFTWNAVGIVHYEVYVESDDSSVLPIVRIPLKGTVPESLQDFTVEYRCAGHRSGQFAVSLYFTFKYGNKEPLKVKLRQEKICASRDGRRGLNGGYEGHEVDDTDSIDKAFFVIICIAAAFLLIVAATLICYFKRSKKEDMIPTRLPTSFRNSLKSTKSAQPFLLSTPRDGPPTLSAISSAPCSSSSASGNSIIPSKPRNIDVRRALLQLYQDRDAFQSLPLDMEGTFGEVRYAIWRQVDDVLNGDVDDEEDTFCNQEAVYTKTLKNNASPIQLDRFLSDALLFYNITPHQNLSQVACVASFGRFDRPETVTDFPLVCYRHQGFGNLKKFLTICRHGDKTKGAQTLRTHQLVSLATQVSSAVAHIHKYRIVHNDIAARNCLIAEVNGRLQVQLCDSALSRDLFPADYHCLGDNENRPLKWMSPEAIANELYSSAADVWSLGVLLWELMSLGGSPHAEIDPEEVYTMILKGKRLQQPNNCPDQLYEVMLCCWRVLSEDRPSSEQVVHGLRDFNIQLSQYI
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Has no detectable kinase activity in vitro and is unlikely to function as a tyrosine kinase in vivo (By similarity). Receptor which may act as a receptor for Wnt ligand mom-2. Plays a role in controlling P7.p vulva precursor cell lineage orientation during vulva development. Regulates pop-1 asymmetric distribution in P7.p and its daughter cells. Plays a role in the migration of ALM neurons during embryogenesis.
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G5EGU9
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SZY20_CAEEL
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Suppressor of zyg-1 protein 20
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MSKENVVADSWDDADADPVKELMDKVEKVKLLQRKEEKKEAFFEKVKAEESSGVVSKLQTEEGLGPSAEEPKRVFLRRPKDGFAASENVIEASPPTSADTEEQPVTNVRSRSHHKLNQKEKQPAPTYEERQAAYQAARNRILGTEYKPDNQEIKEIKFIDRSKSPETLKMTQQNMVEHYGEELSRELMEQPAEIVPPERQYTPDFTQPPPSVSESGGVYNGPPGFQQKQPNFQPTLQQQSLHQQQYLDNQYMMQMNVQIPIQYHNQTQHQFVPHEASAISTTSQNSNGDGQNDQAIYYYQAPTQQPMNYIPYNLPNMAYPPPNFQPQGQLHHQMNAGQLHQIQQQQQQCQQIQHQPPQQHQQVINGQVMNQQNQRNQVNSYPQQNGAGRGQNRQPMMYQMPCNSGPTAKPPPLMNQMQNRCMTNNGQNYQNRNMQQQGQQRSYSSQPQNGQFYQNGNSNQNNPNNGRKQQHQPQQQQNKSGKFGQNRNDMQKNNYQPNLQQPPMSQNPIPFGCPPRNVNAIREQHANNGSPNTGAGILGPHPMMSASQWPALQQNRPQ
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RNA binding protein that is required for normal cell division and cytokinesis during embryonic development. Functions with RNA-binding protein atx-2 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. Furthermore, negatively regulates the levels of the protein kinase zyg-1 at the centrosome. Also involved in ensuring centrosome attachment to the nuclear envelope.
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G7CBF5
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IRTA_MYCT3
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Mycobactin import ATP-binding/permease protein IrtA (EC 7.2.2.-)
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MARGFQGVMLRGLGARDHQATVVDKEYIAPHFVRVRLVSPTLFDEVIVEPTSWLRFWFPDPDGSDTEFQRAYTITESDPETGRFAVDMVLHEPAGPASTWARTVEPGATIAVMSMGSRGFSVPEDPEDRPVGYLLIGDSASTPAINGIIEVVPHDIPIELYLEQHHDDDVLIPLAEHPRLRVHRVSRDDASSLAAALELRDWSNWYCWAGPEAGALKQVRTRLRDEFGFPKREVYAQAYWTEGRAMGSSRGETSTPAKPAAKTAPAKAAAKPAAASGAGTPEHAAAPAAATTGAPQAAPAPGAAQPRTPVRGRWRAEAGSRLLAPLKKPLIVSGVLQALITLIELAPFVLLVELARLLLGGAEAERLWTLGLTAVSLIGLGAVLAAAMTLWLHRVDARFAHELRGRLLTKLSRLPLGWFTRRGSASTKQLVQDDTLALHYLITHAIPDAVAAVVAPVAVLVYLFVADWRVALVLFIPVLVYLVLMSVMTIQSGSKIAQAPRWAERMGGEAGAFLEGQPVIRIFGGAAASRFRRRLDDYIDFLVSWQRPFVGKKTLMDLVTRPATFLWIILVAGVPLVVTGRMDPVNLLPFLLLGTTFGARLLGIGYGLSGIQTGMLAARRIQTVLDEPELVVRDRTGQAGTDHASGDQARPGTVELDRVSFEYRPGVPVIRDVTLTLRPGTVTALVGPSGSGKSTLAALVARFHDVTQGAIRVDGRDIRTLTADELYRRVGFVLQDAQLVHGSVAENIALAEPDAGLERIRTAARDAQIHDRITRMPDGYDSVLGAGSALSGGERQRVTIARAILADTPVLVLDEATAFADPESEYLVQQAINRLTRDRTVLVIAHRLHTITHADQIVVLDDGRIVEVGTHDELLAAGGRYRGLWDSGRYSSPDAGRPVSADAVEVGR
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Part of the ABC transporter complex IrtAB involved in the import of iron-bound mycobactin (Fe-MBT) and carboxymycobactin (Fe-cMBT). Has a preference for Fe-MBT over Fe-cMBT. Mycobactins are then reduced by the siderophore interaction domain to facilitate iron release in the bacterial cell. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation.
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G7CES0
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LPQY_MYCT3
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Trehalose-binding lipoprotein LpqY (Extracellular solute-binding protein) (SugABC transporter substrate-binding protein LpqY) (SugABC transporter SBP LpqY)
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MDGRQVVRARRWCATAAVALMTASTVAACGSDSGEIVISYYTPANEAATFTAVAQRCNAELGGRFRIEQRSLPREADAQRLQLARRLTGNDRSLDVMALDVVWTAEFAEAGWALPLSEDPAGLAEADATTNTLPGPLETAKWNGELYAAPITTNTQLLWYRADLMDEPPATWDEMLSEAARLHAQGGPSWIAVQGKQYEGLVVWFNTLLESAGGQVLSDDGQRVTLTDTPEHRAATVKALEIIKAVATAPGADPSITQTDENTARLALEQGRAALEVNWPYVLPSLLENAIKGGVGFLPLNENPALRGSINDVGTFAPTDEQFDLALNASKEVFGFARYPGVRPDEPARVTLGGLNLAVASTTRHKAEAFEAVRCLRNEENQRLTSIEGGLPAVRTSLYDDPQFQAKYPQYEIIRDQLINAAVRPATPVYQAMSTRMSATLAPISQIDPERTADELAEQVQQAIDGKGLIP
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Part of the ABC transporter complex LpqY-SugA-SugB-SugC, which is highly specific for uptake of trehalose. Involved in the recycling of extracellular trehalose released from trehalose-containing molecules synthesized by M.thermoresistibile. Trehalose uptake is essential for virulence (By similarity). Binds deuterated trehalose with similar high affinity to trehalose, trehalose analogs including galactotrehalose, 4-azido-4-deoxy-trehalose, 6-azido-6-deoxy-trehalose, 3-azido-3-deoxy-trehalose and mannotrehalose in the order of decreasing affinity, respectively, and 2-azido-2-deoxy-trehalose and kojibiose (alpha1,2-glycosidic bond) with very low affinity. Does not recognize single glucose, 6-amino-6-deoxy-trehalose, trehalose-6-phosphate, nigerose (alpha1,3-glycosidic bond), maltose (alpha1,4-glycosidic bond), isomaltose (alpha1,6-glycosidic bond) or glycerophosphocholine. Decreased recognition of alpha,beta-trehalose and almost no recognition of beta,beta-trehalose. Substrate specificity indicates a strict requirement for an alpha1,1-linked disaccharide.
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G7IYC1
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CAD2_MEDTR
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Cinnamoyl-CoA reductase CAD2 (EC 1.2.1.44) (Cinnamyl alcohol dehydrogenase 2) (Mt-CAD2) (Coumaroyl-CoA reductase) (Feruloyl-CoA reductase) (Sinapoyl-CoA reductase)
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MSSSNLGNVVCVTGASGYIASWLVRLLLHRGYTVKATVRDPNDPKKVDHLVKLDGAKERLQLFKANLLEEGAFDSVVQGCHGVFHTASPFYHDVKDPQAELIDPALKGTLNVLNSCAKSPSLKRVVLTSSIAAVAYNGKPRTPDVVVDETWFTDADFCAKSNLWYVVSKTLAEEAAWKFVKENNIDMVTINPAMVIGPLLQPVLNTSAAAILNLINGAQTFPNASFGWVNVKDVANAHILAYENASASGRHCLVERVAHYSEVVRILRELYPSLQLPEKCADDKPYVPIYQVSKEKAKSLGLEYTPLEVSIKETVESLKEKKFANL
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Involved in lignin biosynthesis (By similarity). Regulates the monolignol composition by catalyzing the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (By similarity). Can use coumaraldehyde and coniferaldehyde as substrates, but barely sinapaldehyde.
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G7JEE5
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CCR2_MEDTR
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Cinnamoyl-CoA reductase 2 (Mt-CCR2) (EC 1.2.1.44) (Caffeoyl-CoA reductase) (EC 1.2.1.-) (Coumaroyl-CoA reductase) (Feruloyl-CoA reductase) (Sinapoyl-CoA reductase)
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MPAYDNTSSVSGGDQTVCVTGAGGFIASWLVKLLLERGYTVRGTVRNPEDPKNGHLKELEGARERLTLHKVDLLDLQSIQSVVHGCHGVFHTASPVTDNPDEMLEPAVNGTKNVIIASAEAKVRRVVFTSSIGTVYMDPNTSRDVVVDESYWSDLEHCKNTKNWYCYGKTVAEQSAWDIAKENQVDLVVVNPVVVLGPLLQPTINASTIHILKYLNGAAKTYVNATQSYVHVKDVALAHLLVYETNSASGRYICCETALHRGEVVEILAKYFPEYPLPTKCSDEKNPRVKPYKFSNQKLKDLGLEFTPVKQCLYDTVRSLQEKGHLPIPPMQEDSA
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Involved in the latter stages of lignin biosynthesis. Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes. Mediates the conversion of caffeoyl-CoA and coumaroyl-CoA to caffaldehyde and coumaraldehyde, respectively. Also active, with a lower efficiency, toward feruloyl-CoA and sinapoyl-CoA. Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (By similarity).
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G7JFU5
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ARGI_MEDTR
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Arginase, mitochondrial (EC 3.5.3.1) (Agmatinase ARGAH) (EC 3.5.3.11) (Arginine amidohydrolase) (MtARGAH)
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MSTIARRGFHYMQRLNSANVSPALLEKAQNRVIDAALTFIRERAKFKGELMRSLGGVAATSSLLGVPLGHHSSFHEGSAFAPPRIREAIWCDSTNSTTEEGKNLRDPRVITNVGDVPIEEIRDCGVDDKRLANVISESVKLVMDEDPLRPLVLGGDHSISFPVVRAVSEKLGGAVDILHFDAHPDLYHDFEGNYYSHASPFARIMEGGYARRLVQVGIRSITNDVREQVKKYGVETHEMRTLSRDRPILENLKLGEGVKGVYVSIDVDSLDPSIAPGVSHHEPGGLLFRDILNILQNLQGDIVGGDVVEYNPQRDTYDGITALVAAKLVRELAAKMSK
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Catalyzes the hydrolysis of L-arginine to urea and L-ornithine (Probable). The latter can be utilized in the urea cycle or as a precursor for the synthesis of both polyamines and proline (Probable). Possesses agmatinase activity. Catalyzes the formation of putrescine from agmatine (By similarity).
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G7JIK2
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SUNN_MEDTR
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Leucine-rich repeat receptor-like kinase protein SUNN (EC 2.7.11.1) (Protein SUPER NUMERIC NODULES)
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MKNITCYLLLLCMLFTTCYSLNNDLDALLKLKKSMKGEKAKDDALKDWKFSTSASAHCSFSGVKCDEDQRVIALNVTQVPLFGHLSKEIGELNMLESLTITMDNLTGELPTELSKLTSLRILNISHNLFSGNFPGNITFGMKKLEALDAYDNNFEGPLPEEIVSLMKLKYLSFAGNFFSGTIPESYSEFQKLEILRLNYNSLTGKIPKSLSKLKMLKELQLGYENAYSGGIPPELGSIKSLRYLEISNANLTGEIPPSLGNLENLDSLFLQMNNLTGTIPPELSSMRSLMSLDLSINGLSGEIPETFSKLKNLTLINFFQNKLRGSIPAFIGDLPNLETLQVWENNFSFVLPQNLGSNGKFIYFDVTKNHLTGLIPPELCKSKKLKTFIVTDNFFRGPIPNGIGPCKSLEKIRVANNYLDGPVPPGIFQLPSVQIIELGNNRFNGQLPTEISGNSLGNLALSNNLFTGRIPASMKNLRSLQTLLLDANQFLGEIPAEVFALPVLTRINISGNNLTGGIPKTVTQCSSLTAVDFSRNMLTGEVPKGMKNLKVLSIFNVSHNSISGKIPDEIRFMTSLTTLDLSYNNFTGIVPTGGQFLVFNDRSFAGNPSLCFPHQTTCSSLLYRSRKSHAKEKAVVIAIVFATAVLMVIVTLHMMRKRKRHMAKAWKLTAFQKLEFRAEEVVECLKEENIIGKGGAGIVYRGSMANGTDVAIKRLVGQGSGRNDYGFKAEIETLGRIRHRNIMRLLGYVSNKDTNLLLYEYMPNGSLGEWLHGAKGCHLSWEMRYKIAVEAAKGLCYLHHDCSPLIIHRDVKSNNILLDADFEAHVADFGLAKFLYDPGASQSMSSIAGSYGYIAPEYAYTLKVDEKSDVYSFGVVLLELIIGRKPVGEFGDGVDIVGWINKTELELYQPSDKALVSAVVDPRLNGYPLTSVIYMFNIAMMCVKEMGPARPTMREVVHMLTNPPHSTSHNLINL
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LRR receptor kinase involved in the regulation of root growth and root nodule organogenesis. Involved in long distance nodulation signaling events (Probable). Involved in the autoregulation of nodulation (AON), a long distance systemic signaling from root to shoot and back again, which allows legumes to limit the number of root nodules formed based on available nitrogen and previous rhizobial colonization (Probable). Acts from shoot to root to control AON. Interacts with CLE12 and CLE13 signaling to control nodule numbers. Required for the modulation of shoot-to-root auxin transport in response to altered nitrogen tissue concentrations and in the absence of rhizobia. Shoot-to-root auxin transport influences lateral root density and length. Involved in the regulation of root colonization by arbuscular mycorrhizal (AM) fungi. Interacts with CLE33 and CL53 signaling to repress strigolactone biosynthetic genes and strigolactone content in the roots, and consequently reduces the promotion of further colonization by AM fungi.
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G7KDA1
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PHT18_MEDTR
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Low affinity inorganic phosphate transporter 8 (MtPT8) (MtPht1;8) (Arbuscular mycorrhiza-induced phosphate transporter PT8) (AM-induced phosphate transporter PT8) (H(+)/Pi cotransporter PT8)
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MATSHGVLRSLDNAKTQSYHYLAIVIAGMGFFTDAYDLFCITAVTKLIGRLYYSDPTNHSPGILPTNVNNAITGVALCGTLAGQLFFGWLGDKLGRKKVYGITLTTMVGFALLSGLSFGSTPKTVVTSLCFFRFWLGFGIGGDYPLSAVIMSEYANQKTRGSFIAAVFAMQGVGILVAGGVAMFVSKLFLLYFPAPDFETDAVLSTQPEGDFVWRIVLMFGAVPAALTYYWRMKMPETARYTALVEGDHKKAVEDMAKVLDRNILSEESNTRIAIRPLESHSYGLFSSEFLNRHGLHLLGTTSTWFLLDIAFYSLQLTQKDIYPTSGLVYKASKMNAIEEVFQLSRAMFAVALIATVPGYWCTVFLIEKIGRFRIQLIGFLVMSVCMWFLGHNYRSFRGEESACKNGSKYSFCNGNPVMFAILFGLTLFFANFGPNSTTFIVPAELFPARLRSTCHGISAAAGKSGAIVGAFGVQSYIGNSHDKSKGTKQAIMALAVVNLLGFFFTFLVPETQGRSLEEISGEEKDFQGNNADEEISGERNGTRNASVDKSPETSMV
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Low-affinity transporter for external inorganic phosphate (Pi) that may be involved in the acquisition of phosphate released by arbuscular mycorrhizal (AM) fungi (e.g. Glomus versiforme and G.intraradices) during AM symbiosis not required for mycorrhizal arbuscule development.
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G7L166
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RAM1_MEDTR
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GRAS family protein RAM1 (Protein REQUIRED FOR ARBUSCULAR MYCORRHIZATION 1) (MtRAM1)
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MINSLCGSSNSLKEKCLQPNSSNQTNTHSKKNATNSCGDLEQINVLTPQSLNLPSLKFDLDGDVEVQSPDSSMWEAFFNDHLDNDFMISSPIRNINPNSPQASTYNNCNYNYAQGMQIQSLSGCSPPRFASQIGSLNSNNQQKGKGLSPLHRVFNSPNNQYMQHVENLSLPAIEEFLEDFQGDVDHFSSTKVSSECFDMETPISTILDSLTMQNSSSYGASVNEESTLLHGGNSSSQISQESDIYHQMGSMASASLSQALQQERYQEKHQKMQAQQQSLTVPIQIGIEQEQDSGLQLVHLLLACAEAVAKGEYMLARRYLHQLNRVVTPLGDSMQRVASCFTESLSARLAATLTTKSSSTKKLAPSSLSSSSSSSCLSTFPSNPMEVLKIYQIVYQACPYIKFAHFTANQAIFEAFEAEERVHVIDLDILQGYQWPAFMQALAARPGGAPFLRITGVGPCIESVRETGRCLTELAHSLRIPFEFHPVGEQLEDLKPHMFNRRVGEALAVNTVNRLHRVPGNHLGNLLSMIRDQAPNIVTLVEQEASHNGPYFLGRFLEALHYYSAIFDSLDATFPVESAPRAKVEQYIFAPEIRNIVACEGEERIERHERLEKWRKIMEGKGFKGVPLSPNAVTQSRILLGLYSCDGYRLTEDKGCLLLGWQDRAIIAASAWRC
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Transcription factor acting as a central regulator of arbuscular mycorrhiza (AM)-related genes (e.g. AMT24, AMT25, EXO70I, STR, RAM2, LEC5, PT4, VPY, BCP1, SCP1 and RAD1) required for the morphogenesis of arbuscules upon symbiosis with AM fungi (e.g. Rhizophagus irregularis and Glomus versiforme). Promotes directly the expression of RAM2, EXO70I, STR and RAD1. Not necessary to enable hyphopodium formation or hyphal entry into the root but essential to support arbuscule branching. Involved in the phosphate-mediated suppression of AM fungi colonization in mycorrhiza. Also involved in restricting mycorrhizal colonization of the root meristem (By similarity). Required for Myc factor signaling from mycorrhizal fungi, but has no function in Nod factor signaling from rhizobial bacteria. Regulates the expression of RAM2, a glycerol-3-phosphate acyl transferase that promotes cutin biosynthesis to enhance mycorrhizal hyphopodia formation.
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G7LCV1
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KI106_MEDTR
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Kunitz type trypsin inhibitor 106
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MSMRLSIRTLIILAHVCLFITTTTIAQFVLDTVGEPVEGDEEYFIRPVITNKGGRSTMVSRNESCPLHVGLELTGLGRGLVVKFTPFAPHHDFDDVRVNRDLRITFQASSSCVQSTEWRLGEKDTKSGRRLIITGTDSATNGSYGNFFRIVETPLEGMYNIQWCPTEVCPSCKFECGTVDMLNENGKILLALDGGPLPLVFQKE
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Protease inhibitor that, together with SCP1, controls mycorrhiza establishment and arbuscule development during root colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis), probably by degrading SCP1 in the apoplast of the periarbuscular region.
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G8BAW7
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FAS2_CANPC
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Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: Acyl carrier; 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Beta-ketoacyl synthase)]
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MKPEIEQELSHTLLTELLAYQFASPVRWIETQDVFLKQHNTERVIEIGPSPTLAGMASRTIKAKYQSYDAALSLQRQVLCYSKDAKEIYYTPDPAEPPAAEEPKAETGKESAPAASAAAAAATQPAAAVAPPPQSAGPVESIPDEPVKASLLIHVLVAQKLKKPLDAVPMSKAIKDLVNGKSTVQNEILGDLGKEFGSTPEKPEETPLEELAEQFQDTFSGSLGKTSTSLIGRLMSSKMPGGFSITNARKYLESRFGLGPGRQDSVLLTALCNEPASRLGSEGDAKSFLDTMAQKYASHAGISLSSPSAGGASSGAGAAVVDSAALDALIAENKKLARQQLETLARYLQVDLTKGEKAFIKEKEATTVLQQELDLWEAEHGEFYAKGIKPVFSPLKSRTYDSYWNWARQDLLSMWFDILFGKLTSVDRETINQCIQIMNRANPTLIKFMQYHVELCPTYRGETYKLGKRLGEQLIENCKQILGQSPVYKDVSRITGPKTTVSAKGDIVYEEANKESVRKFEQYVFEMAQGGSMTKMKQSSIQEDLARVYKAISKQASRDSKLELQKVYDQLLKVVEGSTEIETEQTTQDALAIPTGSNTPTEEDELSTASDDDEIASLPDKTSIAQPVSSTIPNKTIPFLHIQSKSESGNWEYDRKLSSIYLDGLESAAINGLTFKDKYVLVTGAGAGSIGAEILQGLISGGAKVIVTTSRYSKKVTEYYQNMYARYGAAGSTLIVVPFNQGSKQDVDALVEYIYNDQKKGGLGWDLDVIIPFAAIPENGNGIDNIDSKSEFAHRIMLTNLLRLLGAVKARKTTDTRPAQCILPLSPNHGTFGFDGLYSESKISLETLFNRWYSEDWGTKLTICGAIIGWTRGTGLMSANNIIAEGIEKLGVRTFSQKEMAFNILGLLTPEIVNLCQEEPVMADLNGGLQFIDNLKEFTSKLRNDLTETADIRRAVSIESAIEQKVVNGDNVDSNYNKVTVRPRANMKFDFPTLKSYDEIKQIAPDLEGMLDLENVVVVTGFAEVGPWGNARTRWEMESKGEFSLEGAIEMAWIMGMIKYHNGNLKGKPYSGWIDAKTQTPVDDKDIKAKYEEEILEHSGIRLIEPELFNGYDPKKKQMIQEVVIQHDLEPFECSKETAEQYKHEHGDKCEISEIEESGEYSVRILKGATLFIPKALRFDRLVAGQIPTGWDARTYGIPEDTINQVDPITLYVLVATVEALLSAGITDPYEFYKYVHVSEVGNCSGSGMGGVSALRGMFKDRYADKPVQNDILQESFINTMSAWVNMLLLSASGPIKTPVGACATAVESVDIGIETILSGKAKVVMVGGYDDFQEEGSYEFANMNATSSAIDEFKHGRTPKEMSRPTTTTRNGFMEAQGSGIQVIMSADLALKMGVPIHAVLAMSATATDKIGRSVPAPGKGILTTAREHHGNLKYPSPLLNVKYRKRQLSKRLDQIKSWESSELNYLQEEAHLAKEEFGEEFSEAEFLRERTEEIYRESKRQVADAKKQWGNAFYKSDPRIAPLRGALATFNLTIDDIGVASFHGTSTVANDKNESATIDSMMKHLGRSEGNPVFGVFQKYLTGHPKGAAGAWMLNGAIQILESGIVPGNRNADNVDKVLEQYEYVLYPSRSIQTDGIKAVSVTSFGFGQKGAQAVVVHPDYLYAVLDRSTYEDYAKRVTARNKKTYRYMHNAITRNTMFVAKDKAPYSDELTMDVYLDPLARVSKTKNEFVFTKKSVQSDKSYVSNIANSTAKALSSLNKSSKGVGVDVELLSELNIDNETFLERNFTPEEIKYCQNSANPQASFTGTWSAKEATFKALGVSSQGGGASLKEIEIVRDGNGAPQVVLNDNAKAAAKAAGVKNVNVSISHDDFQATAVALSEF
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Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase.
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G8GER6
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PETH1_THEFU
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Cutinase cut1 (EC 3.1.1.74) (Poly(ethylene terephthalate) hydrolase) (PET hydrolase) (PETase) (EC 3.1.1.101)
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MPPHAARPGPAQNRRGRAMAVITPRRERSSLLSRALRFTAAAATALVTAVSLAAPAHAANPYERGPNPTDALLEARSGPFSVSEERASRFGADGFGGGTIYYPRENNTYGAVAISPGYTGTQASVAWLGERIASHGFVVITIDTNTTLDQPDSRARQLNAALDYMINDASSAVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVRVPTLIIGADLDTIAPVLTHARPFYNSLPTSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF
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Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Probable). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world.
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G8H5M7
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TPS9_SOLHA
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Terpene synthase 9 (ShTPS9) ((1E,4E)-germacrene B synthase TPS9) (EC 4.2.3.71) (Alpha-humulene synthase TPS9) (EC 4.2.3.-) (Beta-myrcene synthase TPS9) (EC 4.2.3.15) (Germacrene A synthase TPS9) (EC 4.2.3.-) (Limonene synthase TPS9) (EC 4.2.3.-) (Terpinolene synthase TPS9) (EC 4.2.3.113)
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MAASSANKSRPLANFHPTVWGYHFLSYTHEITNQEKVEVDEYKETIRKMLVEAPEGSEQKLVLIDAMQRLGVAYHFHNEIETSIQNIFDAPKQNNNLHIVSLHFRLVRQQGHYMSSDVFKQFTNQDGKFKERLTNDVQGLLSLYEASYLRVRDEEILEEALAFTTTHLKSIVSNMSNNNNSLKVEVSEALTQPIRMTLPRMEARRYISIYENNDAHNHLLLKFAKLDFNMLQKLHQRELSDLTRWWKDLDFANKYPYARDRLVECYFWILGVYFEPKYSRARKMMTKVLKMTSIIDDTFDAYATFDELEPFNDAIQRWDANAIDSIQPYMRPAYQAFLDIYSEMEQVLSKEGKLDRVYYAKNEMKKLVRAYFKETQWLNDCDHIPKYEEHMENSLVSGGYMMIPTTCLVGMEEFISIETFEWLMNDPLIVRASSLIARAMNDIVGHEVEQERGHVASLIECYMKDYGASKQEAYAKFKKDVTNAWKDINKEFFRPTEVPMFVLERVLNLTRAADTLYKEKDAYTNAKGKLKNMINSILIESVKI
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Sesquiterpene synthase involved in the biosynthesis of volatile compounds. Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (1E,4E)-germacrene B, but also smaller amounts of germacrene A and C, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into alpha-humulene, germacrene A and germacrene B. Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene, limonene and terpinolene.
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G8H5M8
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TPS12_SOLHA
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Sesquiterpene synthase 12 (ShTPS12) ((E)-beta-ocimene synthase TPS12) (EC 4.2.3.106) ((Z)-gamma-bisabolene synthase TPS12) (EC 4.2.3.-) (Alpha-humulene synthase TPS12) (EC 4.2.3.104) (Beta bisabolene synthase TPS12) (EC 4.2.3.-) (Beta caryophyllene synthase TPS12) (EC 4.2.3.57) (Beta-myrcene synthase TPS12) (EC 4.2.3.15) (Gamma-curcumene synthase TPS12) (EC 4.2.3.-) (Limonene synthase TPS12) (EC 4.2.3.-) (Terpinolene synthase TPS12) (EC 4.2.3.113)
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MAASSADKSRPLANFSPTVWGYHFLSYTPEISSQEKHEVDELKEIFRKMLVETCDNSTQKLVLIDTIQRLGVAYHFDNEIETSIQNIFDASKQNDNDDNLHIVSLRFRLVRQQGHYMSSDVFKQFTNQDGKFKETLTNDVQGLLSLYEASHLRVRDEEILEEALTFTTTHLESIVSNLSNNNKVEVSEALTQPIRMTLPRMGARKYISIYENNDAHNHLLLKFAKLDFNMLQKLHQRELSDLTRWWKDLDFANKYPYARDRLVECYFWILGVYFEPKYSRARKMMTKVIQMASFFDDTFDAYATFDELEPFNDAIQRWDINAIDSVPPYLRHAYQALLDIYSEMEQELAKEFKSDRVYYAKYEMKKLVRAYFKEAQWLNDDNHIPKYEEHMENAMVSAGYMMGATTCLVGVDEFISQETFEWIINEPLIVRASSLIARAMDDIAGHEVEQQREHGASLIECYMKDYGVSKQEAYVKFQKEVTNGWMDINKEFFCLDVQVPKFVLERVLNFTRVINTLYKEKDEYTNSKGKFKNMIITLLVESVEI
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Sesquiterpene synthase involved in the biosynthesis of volatile compounds. Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (1E,4E,8E)-alpha-humulene and (-)-(E)-beta-caryophyllene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into beta-bisabolene, gamma-curcumene and (Z)-gamma-bisabolene. Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene, (E)-beta-ocimene, limonene and terpinolene.
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G8H5M9
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TS14A_SOLHA
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Sesquiterpene synthase 14a (ShTPS14a) ((E)-beta-farnesene synthase TPS14a) (EC 4.2.3.47) ((E)-gamma-bisabolene synthase TPS14a) (EC 4.2.3.59) ((Z)-alpha-bisabolene synthase TPS14a) (EC 4.2.3.-) ((Z)-beta-farnesene synthase TPS14a) (EC 4.2.3.-) (Beta-acoradiene synthase TPS14a) (EC 4.2.3.-) (Beta-bisabolene synthase TPS14a) (EC 4.2.3.-) (Beta-myrcene synthase TPS14a) (EC 4.2.3.15) (Limonene synthase TPS14a) (EC 4.2.3.-)
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MNQLAMVNTTITRPLANYHSSVWGNYFLSYTPQLTETSSQEKRELEELKEKVRQMLVETPDNSTQKLVLIDTIQRLGVAYHFENHIKISIQNIFDEFEKNKNKDNDDDLCVVALRFRLVRGQRHYMSSDVFTRFTNDDGKFKETLTKDVSGLLNLYEATHLRVHGEEILEDALSFTVTHLKSMSPKLDNSLKAQVSEALFQPIHTNIPRVVARKYIRIYENIESHDDLLLKFAKLDFHILQKMHQRELSELTRWWKYLDYENKYPYARDKLVECYFWATGVYFGPQYKRARKTLTKLIVIITITDDLYDAYATYDELVPYTDAVERCEISAMHSISPYMRPLYQVFLDYFDEMEKELTKDGKAHYVYYAKIETNKWIKSYLKEAEWLKNDIIPKCEEYKRNATITVSSQMILITCLIVAGEFISKETFEWMINESLIAPASSLINRLKDDIIGHEHEQQREHGASFIECYVKEYRASKQEAYVEARRQIANAWKDINTDYLHATQVPTFVLEPALNLSRLVDILQEDDFTDSQNFLKDTITLLFVDSVNSTSCG
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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, beta-farnesene, (E)-gamma-bisabolene, beta-acoradiene, selinene and (Z)-alpha-bisabolene. Low or no activity with (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP). Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene and limonene.
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G8H5N0
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TPS17_SOLHA
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Terpene synthase 17 (ShTPS17) ((+)-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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MELCTQTVAADHEVIITRRSGSHHPTLWGDHFLAYADLRGANEGEEKQNEDLKEEVRKMLVMAPSNSLEKLELINTIQCLGLAYHFQSEIDESLSYMYTHYEEYSIGDLHAIALCFRLLRQQGYYVSCDAFKKFTNDQGNFKEELVKDVEGMLSLYEAAQFRVHGEQILDEALNFTITKLKQILPKLSNSQLAQQITNALKFPIKDGIVRVETRKYISFYQQNQNHNQVLLNFAKLDFNILQTLHKKELSDMTRWWKKMELVNTLPYARDRLVECYFWCLGTYFEPQYSVARKMLTKISFFISIIDDTYDIYGKLDELTLFTQAIERWNIDASEQLPLYMKIIYRDLLDVYDEIEKELANENKSFLVNYSINEMKKVVRGYFQEAKWYYGKKVPKMEQYMKNAISTSAYILLTTTSWLAMGNVATKDVFDWVATEPKLVVASCHIIRLLNDLVSHEEEQKRGNAASAVECYMNEYSVTQEEAHVKIRDIIENYWKDLNEEYFKVDMIIIPRVLLMCIINLTRVAEFIYKDEDAYTFSKNNLKDVISDILVDPII
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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.
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G8H5N1
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TS14B_SOLHA
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Sesquiterpene synthase 14b (ShTPS14b) ((+)-thujopsene synthase TPS14b) (EC 4.2.3.79) ((E)-alpha-bisabolene synthase TPS14b) (EC 4.2.3.-) ((E)-beta-farnesene synthase TPS14b) (EC 4.2.3.47) ((E)-gamma-bisabolene synthase TPS14b) (EC 4.2.3.59) ((Z)-beta-farnesene synthase TPS14b) (EC 4.2.3.-) (Alpha-acoradiene synthase TPS14b) (EC 4.2.3.-) (Alpha-cederene synthase TPS14b) (EC 4.2.3.-) (Beta-acoradiene synthase TPS14b) (EC 4.2.3.-) (Beta-bisabolene synthase TPS14b) (EC 4.2.3.-) (Beta-myrcene synthase TPS14b) (EC 4.2.3.15) (Limonene synthase TPS14b) (EC 4.2.3.-) (Terpinolene synthase TPS14b) (EC 4.2.3.113)
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MNQLAMVNTTITRPLANYHSSVWGNYFLSYTPQLTEISSQEKRELEELKEKVRQMLVETPDNSTQKLVLIDTIQRLGVAYHFENHIKISIQNIFDEFEKNKNKDNDDDLCVVALRFRLVRGQRHYMSSDVFTRFTNDDGKFKETLTKDVQGLLNLYEATHLRVHGEEILEEALSFTVTHLKSMSPKLDNSLKAQVSEALFQPIHTNIPRVVARKYIRIYENIESHDDLLLKFAKLDFHILQKMHQRELSELTRWWKDLDHSNKYPYARDKLVECYFWAIGVYFGPQYKRARRTLTKLIVIITITDDLYDAYATYDELVPYTNAVERCEISAMHSISPYMRPLYQVFLDYFDEMEEELTKDGKAHYVYYAKIETNKWIKSYLKEAEWLKNDIIPKCEEYKRNATITISNQMNLITCLIVAGEFISKETFEWMINESLIAPASSLINRLKDDIIGHEHEQQREHGASFIECYVKEYRASKQEAYVEARRQITNAWKDINTDYLHATQVPTFVLEPALNLSRLVDILQEDDFTDSQNFLKDTITLLFVDSVNSTSCG
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Sesquiterpene synthase involved in the biosynthesis of volatile compounds. Mediates the conversion of (2E,6E)-farnesyl diphosphate ((EE)-FPP) into (+)-thujopsene, beta-bisabolene, alpha-cederene, beta-acoradiene, (E)-gamma-bisabolene, (Z)-alpha-bisabolene, (Z)-beta-farnesene and (E)-beta-farnesene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into (E)-gamma-bisabolene, (E)-alpha-bisabolene, (E)-beta-farnesene, (Z)-beta-farnesene, beta-bisabolene, beta-acoradiene and alpha-acoradiene. Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene, limonene and terpinolene.
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G8JYC6
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PDF1_CAEEL
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Pigment dispersing factor homolog pdf-1
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MNRFIISMIALLAVFCAVSTASPLLYRAPQYQMYDDVQFVKRSNAELINGLIGMDLGKLSAVGKRSNAELINGLLSMNLNKLSGAGRR
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Probable ligand of isoforms a and b of the calcitonin receptor-like protein, pdfr-1, a G-protein coupled receptor. May not signal through isoform c of pdfr-1. Involved in locomotion more specifically mate searching behavior of males, independent of nutritional status. Involved in regulating the male-specific expression of TGFbeta-like daf-7 in the ASJ chemosensory neurons. Plays a role in circadian rhythms of locomotor activity. Involved in mediating arousal from the sleep-like state called lethargus, which occurs during molting between larval and adult stages, in part by regulating touch sensitivity, and working in concert with neuropeptide flp-2. In the presence of food, plays a role in initiating and extending exploratory roaming behavior, in opposition to 5-hydroxytryptamine (serotonin) signaling.
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G8JZS4
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SUSB_BACTN
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Glucan 1,4-alpha-glucosidase SusB (EC 3.2.1.3) (Alpha-glucosidase SusB) (Glucoamylase SusB) (Starch-utilization system protein B)
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MKKRKILSLIAFLCISFIANAQQKLTSPDNNLVMTFQVDSKGAPTYELTYKNKVVIKPSTLGLELKKEDNTRTDFDWVDRRDLTKLDSKTNLYDGFEVKDTQTATFDETWQPVWGEEKEIRNHYNELAVTLYQPMNDRSIVIRFRLFNDGLGFRYEFPQQKSLNYFVIKEEHSQFGMNGDHIAFWIPGDYDTQEYDYTISRLSEIRGLMKEAITPNSSQTPFSQTGVQTALMMKTDDGLYINLHEAALVDYSCMHLNLDDKNMVFESWLTPDAKGDKGYMQTPCNTPWRTIIVSDDARNILASRITLNLNEPCKIADAASWVKPVKYIGVWWDMITGKGSWAYTDELTSVKLGETDYSKTKPNGKHSANTANVKRYIDFAAAHGFDAVLVEGWNEGWEDWFGNSKDYVFDFVTPYPDFDVKEIHRYAARKGIKMMMHHETSASVRNYERHMDKAYQFMADNGYNSVKSGYVGNIIPRGEHHYGQWMNNHYLYAVKKAADYKIMVNAHEATRPTGICRTYPNLIGNESARGTEYESFGGNKVYHTTILPFTRLVGGPMDYTPGIFETHCNKMNPANNSQVRSTIARQLALYVTMYSPLQMAADIPENYERFMDAFQFIKDVALDWDETNYLEAEPGEYITIARKAKDTDDWYVGCTAGENGHTSKLVFDFLTPGKQYIATVYADAKDADWKENPQAYTIKKGILTNKSKLNLHAANGGGYAISIKEVKDKSEAKGLKRL
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Glucoamylase that hydrolyzes alpha-1,4-glucosidic linkages, alpha-1,6-, alpha-1,3- and alpha-1,2-glucosidic linkages during starch degradation.
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G8JZS6
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SUSF_BACTN
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Outer membrane protein SusF (Starch-utilization system protein F)
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MKKHLIYTGMFLAAIGFSACNEDFKDWADPQSNPQEESAGQLTATFTAGKDASIVMDAATADSVEIAKLSSTTAEEGSKIAVNSLTLNENHTIPFSMTEDHVFKVALAQLDSVTQEAYKSRASVVRELKISINASAVTPSGEGIQLVGNEVSITLQPATTPAVDPDGYYIVGDFTGWDGNSAQQMKKDALDENLYILEAEIESTSNFKIFPASAINGNDIDWTKALGSSVDGDDSGDNFVSWTNAGAINTALDGKIKISFDAFNYRFTVKDNSAPTELYMTGSAYNWGTPAGDPNAWKALVPVNGTKGTFWGIFYFAANDQVKFAPQANWGNDFGFVDAISQESKDLAGLSDEGGNLKVGIAGWYLVYVSVIGDDKVIEFEKPNVYLMGDTSYNGWDAQLVEQDLFTVPGTADGEFVSPAFLKDGAVRICVNPKAVSAGDWWKTEFIIFDGQIAYRGNGGDQAAVQGKTGQKVYLNFGNGTGRIE
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Starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation. SusE and SusF do not constitute the major starch-binding proteins in starch degradation pathway. Has lower affinity for starch compared to SusE.
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G8JZT0
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SUSE_BACTN
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Outer membrane protein SusE (Starch-utilization system protein E)
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MKKISNILLAVTFALPLFTACETDNDSNPILNEPDTFTLNTPAYAANNVYDLKNAQTVELTCSQPDYGFPAATTYTVQASFEQDFIEATDESKANYTVLESTSPTAKINVDASELNNALLDLWTAVNGEQAELPTEPVAVYIRLKANITSSGKGVCFSNVIELPNVLISKSTSSLTPPKTMFIVGSMLDTDWKVWKPMAGVYGMDGQFYSMIYFDANSEFKFGTKENEYIGINDNRVTVTDKAGAGVSGSDNFVVENAGWYLFYVKAAVKGDDYQFTITFYPAEVYLFGNTTGGSWAFNDEWKFTVPATKDGNFVSPAMTASGEVRMCFKTDLDWWRTEFTLHDGEIFYRDFNLIDSWTEKGDGYSIQGSAGNVIHLNFTAGTGEKK
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Starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation. SusE and SusF do not constitute the major starch-binding proteins in starch degradation pathway. Has higher affinity for starch compared to SusF.
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G8XQX1
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OXLA_DABRR
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L-amino-acid oxidase (DrLAO) (LAAO) (EC 1.4.3.2)
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MNVFFMFSLLFLATLGSCADDKNPLEECFREDDYEEFLEIAKNGLKKTSNPKHIVIVGAGMSGLSAAYVLAGAGHKVTVLEASERPGGRVRTHRNVKEGWYANLGPMRVPEKHRIIREYIRKFGLKLNEFVQETENGWYFIKNIRKRVGEVKKDPGLLKYPVKPSEAGKSAGQLYQESLGKAVEELKRTNCSYILNKYDTYSTKEYLIKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDQLPTSMYRAIEESVHFKARVIKIQQNAEKVTVTYQTTQKNLLLETADYVIVCTTSRAARRITFKPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIQGGKSTTDLPSRFIYYPNHNFTTGVGVIIAYGIGDDANFFQALNLNECADIVFNDLSSIHQLPKKDLQTFCYPSIIQKWSLDKYAMGAITTFTPYQFQHFSEALTAPVGRIFFAGEYTANAHGWIDSTIKSGLTAARDVNRASEL
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Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Is highly active on L-Tyr followed by L-Phe, L-Met, L-Leu, L-Trp, and weakly active on L-Ile, L-Arg, L-Val, L-Lys, and L-Ala. Inhibits ADP- and collagen-induced platelet aggregation. This inhibition is inhibited by catalase, indicating the importance of generated H(2)O(2) for the inhibitory effect. This effect on platelets among snake L-amino-acid oxidases is however controversial, since some of them induce aggregation, whereas the other inhibit agonist-induced aggregation (By similarity). In vivo, this enzyme induces a rapid, substantial and reversible increase in the paw volume of mice (edema). In addition, myofibrosis, and inflammatory cell infiltration on the paw tissue are also observed.
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G8XYX6
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MOT8_DANRE
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Monocarboxylate transporter 8 (MCT 8) (Solute carrier family 16 member 2)
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MHSESDDNTAGGTPGSEDPQAEESSSPAEEFEEQERKLAPEDSTVQLIHTGCTDKRPATPPGAHPGQGFVPPEGGFGWVVVFAATWCNGSIFGIQNSFGILHMMLVKHHEKQPDQASQFKVAWVGALAMGMIFFCSPVVSMFTDHFGCRKTAVCGAFVAFIGLLTSSFATTLGLWYFTYGILFGCGSSFAFQPSLVILGHYFRQRLGLANGVVTAGSSLFSMGLPVLLKKVVEPLGLPRTFQILSIFMLVQALLALAFKPLLPSGMCPMPGMALDGGPSTPESASRWQKGLAKIRRYFNVRVFSILTYRIWAFGVATAVLGYFVPYVHLLNFVKEQFGDTQREWLLLVCIGASSGVGRLLFGKIGDLIPGVKKIYMQVASFILLGVMSMMIPQCAVFEGLVVVFVLMGLCDGCFITIMAPIAFELVGPMQASQAIGYLLGLMAIPMTAGPPIAGLLHDHFGNYHVAFYLAGVPPIVGGIVMFFVPLVHQRMQKRRKETDDPSMDKMLKNCSNGDMLPGYTDMETHI
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Specific thyroid hormone transmembrane transporter, that mediates both uptake and efflux of thyroid hormones across the cell membrane independently of pH or a Na(+) gradient. The substrate preference is 3,3-diiodothyronine (3,3'-T2) and T3 and to a lesser extentd T4 and rT3. Acts as a crucial regulator during embryonic development.
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G9BY57
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PETH_UNKP
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Leaf-branch compost cutinase (LC-cutinase) (LCC) (EC 3.1.1.74) (PET-digesting enzyme) (Poly(ethylene terephthalate) hydrolase) (PET hydrolase) (PETase) (EC 3.1.1.101)
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MDGVLWRVRTAALMAALLALAAWALVWASPSVEAQSNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDYPDSRASQLSAALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELDNASHFAPNSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALSDFRTNNRHCQ
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Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters), with a preference for short-chain substrates (C4 substrate at most). Cannot hydrolyze olive oil. Is also able to degrade poly(ethylene terephthalate), the most abundant polyester plastic in the world. Can also depolymerize poly(epsilon-caprolactone) (PCL), a synthetic aliphatic biodegradable polyester.
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G9FRD6
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HSDHB_CLOSR
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7beta-hydroxysteroid dehydrogenase (7beta-HSDH) (EC 1.1.1.201) (NADP-dependent 7beta-hydroxysteroid dehydrogenase)
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MNFREKYGQWGIVLGATEGIGKASAFELAKRGMDVILVGRRKEALEELAKAIHEETGKEIRVLPQDLSEYDAAERLIEATKDLDMGVIEYVACLHAMGQYNKVDYAKYEQMYRVNIRTFSKLLHHYIGEFKERDRGAFITIGSLSGWTSLPFCAEYAAEKAYMMTVTEGVAYECANTNVDVMLLSAGSTITPTWLKNKPSDPKAVAAAMYPEDVIKDGFEQLGKKFTYLAGELNREKMKENNAMDRNDLIAKLGKMFDHMA
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7beta-hydroxysteroid dehydrogenase that catalyzes the reduction of the 7-oxo group of 7-oxosteroids, such as 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate, 7-oxolithocholate, 7,12-dioxo-lithocholate and dehydrocholate, to the corresponding 7beta-hydroxysteroids. Is also able to catalyze the reverse oxidation reactions. Together with 7alpha-HSDH encoded in the adjacent gene, is likely involved in the epimerization of the hydroxy group at C-7 of primary bile acids through 7-keto bile acid intermediates.
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G9FRD7
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HDHA_CLOSR
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7alpha-hydroxysteroid dehydrogenase (7alpha-HSDH) (EC 1.1.1.-) (NADP-dependent 7alpha-hydroxysteroid dehydrogenase)
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MKRLEGKVAIVTSSTRGIGRASAEALAKEGALVYLAARSEELANEVIADIKKQGGVAKFVYFNAREEETYTSMVEKVAEAEGRIDILVNNYGGTNVNLDKNLTAGDTDEFFRILKDNVQSVYLPAKAAIPHMEKVGGGSIVNISTIGSVVPDISRIAYCVSKSAINSLTQNIALQYARKNIRCNAVLPGLIGTRAALENMTDEFRDSFLGHVPLNRVGRPEDIANAVLYYASDDSGYVTGMIHEVAGGFALGTPQYSEYCPR
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7alpha-hydroxysteroid dehydrogenase that catalyzes the NADP(+)-dependent oxidation of the 7alpha-hydroxy group of 7alpha-hydroxysteroids, such as cholate, chenodeoxycholate, glycochenodeoxycholate and taurochenodeoxycholate, to the corresponding 7-oxosteroids. Is also able to catalyze the reverse reduction reactions. Together with 7beta-HSDH encoded in the adjacent gene, is likely involved in the epimerization of the hydroxy group at C-7 of primary bile acids through 7-keto bile acid intermediates.
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G9I929
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VKTA_MICTN
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Kunitz-type neurotoxin MitTx-alpha
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MSSGGLLLLLGLLTLCAELTPVSSQIRPAFCYEDPPFFQKCGAFVDSYYFNRSRITCVHFFYGQCDVNQNHFTTMSECNRVCHG
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MitTx, a heteromeric complex between Kunitz- and phospholipase-A2-like proteins, potently, persistently and selectively activates rat and chicken acid-sensing ion channel ASIC1. Both alternatively spliced rat isoforms ASIC1a and ASIC1b are activated, with a higher potency for ASIC1a (EC(50)=9.4 nM) vs ASIC1b (EC(50)=23 nM). The rat ASIC3 subtype is also sensitive to the heterodimer, but with a lower potency (EC(50)=830 nM). On rat ASIC2a, the toxin shows a very weak activation, but produces a remarkable potentiation (>100-fold) of protons when the extracellular pH drops below neutrality. Moderate and weak activations are also observed on the heterotrimers Asic1a-Asic2a and Asic1a-Asic3 (expressed in CHO cells), respectively. The binding sites of the beta subunit of MitTx and the spider psalmotoxin-1 overlap, explaining why these toxins are mutually exclusive. In vivo, the heterodimer elicits robust pain-related behavior in mice by activation of ASIC1 channels on capsaicin-sensitive nerve fibers.
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G9I930
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PA2HB_MICTN
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Basic phospholipase A2 homolog MitTx-beta (svPLA2 homolog)
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MDKMNPAHLLVLAAVCVSLLGASSIPPQALNLNQFRLMIKCTNDRVWADFVDYGCYCVARDSNTPVDDLDRCCQAQKQCYDEAVKVHGCKPLVMFYSFECRYLASDLDCSGNNTKCRNFVCNCDRTATLCILTATYNRNNHKIDPSRCQ
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Heterodimer: MitTx, a heteromeric complex between Kunitz- and phospholipase-A2-like proteins, potently, persistently and selectively activates rat and chicken acid-sensing ion channel ASIC1. Both alternatively spliced rat isoforms ASIC1a and ASIC1b are activated, with a higher potency for ASIC1a (EC(50)=9.4 nM) vs ASIC1b (EC(50)=23 nM). The rat ASIC3 subtype is also sensitive to the heterodimer, but with a lower potency (EC(50)=830 nM). On rat ASIC2a, the toxin shows a very weak activation, but produces a remarkable potentiation (>100-fold) of protons when the extracellular pH drops below neutrality. Moderate and weak activations are also observed on the heterotrimers Asic1a-Asic2a and Asic1a-Asic3 (expressed in CHO cells), respectively. The binding sites of the beta subunit of MitTx and the spider psalmotoxin-1 toxin overlap, explaining why these toxins are mutually exclusive. In vivo, the heterodimer elicits robust pain-related behavior in mice by activation of ASIC1 channels on capsaicin-sensitive nerve fibers. Monomer: does not have phospholipase A2 activity but may maintain some lipid-binding character from its PLA2 lineage, which could aid in effecting neuronal depolarization.
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G9M9M3
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F6H22_IPOBA
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Bi-functional coumaroyl CoA and feruloyl CoA ortho-hydroxylase F6H2-2-1 (IbF6H2-2-1) (EC 1.14.11.61) (EC 1.14.11.62) (2-oxoglutarate-dependent dioxygenase F6H2-2-1) (2OGD F6H2-2-1)
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MPSTTLSTVLSDINDFVVKQGHGVKGLSELGLQTLPNQYVHPPEERLSSMDVVSDDSIPVIDVSNWEDPKVAKLICDAAEKRGFFQIVNHGIPIEMLEKAKAATYRFFREPAEEKKKYSKENCPTSHVRYSTSFLPQIEKALEWKDHLSMFYVSDEEAAQYWPPSCRDDAVEYLKSCEMVSRKLLEALMQGLNVNQIDDSKESLLMGSRRININYYPKCPNPDLTVGVGRHSDISTLTLLLQDDIGGLYVRKLEHEAWSHVPPVKGALVINIGDALQIMSNGRYKSIEHRVMANESNDRISVPVFVNPRPNDIVGPLPEVLASGEKPVYKPVLYSDYAKHFYRKAHNGKDTIAFARIE
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2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis. Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA, but has no activity toward caffeoyl-CoA.
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G9M9M4
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F6H21_IPOBA
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Bi-functional coumaroyl CoA and feruloyl CoA ortho-hydroxylase F6H2-1-1 (IbF6H2-1-1) (EC 1.14.11.61) (EC 1.14.11.62) (2-oxoglutarate-dependent dioxygenase F6H2-1-1) (2OGD F6H2-1-1)
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MPSTTLSTVLSDINEFVVKQGHGVKGLSELGLQTLPNQYVHPPEERLSSMDVVSDDSIPVIDVSNWEDPKVAKLICDAAEKRGFFQIVNHGIPLEMLEKAKAATYRFFREPAEEKKKYSKENCPTSHVRYSTSFLPQIEKALEWKDHLSMFYVSDEEAAQYWPPSCRDDALEYLKSCEMVSRKLLEALMQGLNVNEIDDAKESLLMGSRRININYYPKCPNPDLTVGVGRHSDISTLTLLLQDDIGGLYVRKLEHEAWSHVPPVKGALVINIGDALQIMSNGRYKSIEHRVLANETNDRISVPVFVNPKPNDIVGPLPEVLASGEKPVYKPVLYSDYAKHFYRKAHNGKDTIAFARIE
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2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis. Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA, but has no activity with caffeoyl-CoA.
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G9M9M5
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F6H28_IPOBA
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Bi-functional coumaroyl CoA and feruloyl CoA ortho-hydroxylase F6H2-1-8 (IbF6H2-1-8) (EC 1.14.11.61) (EC 1.14.11.62) (2-oxoglutarate-dependent dioxygenase F6H2-1-8) (2OGD F6H2-1-8)
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MMPSTTLSTVLSDINEFVVKQGHGVKGLSELGLQTLPNQYVHPPEERLSSMDVVSDDSIPVIDVSNWEDPKVAKLICNAAEKRGFFQIVNHGIPLEMLEKAKAATYRFFREPAQEKKKYSKENCPTSHVRYSTSFLPQIEKALEWKDHLSMFYVSDQEAAQYWPPSCRDDALEYLKSCELVSRKLLEALMQGLNVNQIDDSKESLLMGSRRININYYPKCPNPDLTVGVGRHSDISTLTLLLQDDIGGLYVRKLEHEAWSHVPPVKGALVINIGDALQIMSNGRYKSIEHRVMANESNDRISVPVFVNPKPNDIVGPLPEVLASGEKPVYKPVLYSDYAKHFYRKAHNGKDTIAFARIE
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2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis. Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA, but has no activity with caffeoyl-CoA.
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G9MAN7
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TPS4_SELML
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Bifunctional diterpene synthase, chloroplastic (Copalyl diphosphate synthase) (EC 5.5.1.12) (Miltiradiene synthase) (SmMDS) (EC 4.2.3.131) (Terpene synthase 4) (SmTPS4)
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MAKVLFSSFQQTGISGSLKSGQLSGVFINGTNLKSNAHAKRFRKNSTSSITIRCCASNSPTLENTKLAGAPEKRQKKKQLPYQGILHVPGDRVEELDTRETSLLVAEVKGWLMKLASGKGEISPSAYDTAWVARIASESDSSLPEFPEALEWIINSQLPDGSWGDDRHLQLYDRVLSTLSCLVTLKTWDIGHNSIAQGTKFLRENMIKLKQDDGDLLSGFEVTFPMMLHEAKQLGLDIPYETEFTRLLEISTKKKLAKIPLDKLHSAPTTLLYSLEGLQDLEIDWQKILKLQSKDGSFLSSPSSTACVYLKTKDRKSLQYLQNAMEDQNYAVPCHYPIDLFESLWVVDTIERLGIDVFFRDEIKAVLDYVYSFWTNEGIGWGSTCLVNDIDDTAMAFRILRMHGYNVSPDAFNQFWLPGDKFCCFVGELSHGVSEMLNLHRASQVDFPNEAILTKTFKYSHDYLLNVDSAHMDKWATKKNLMGEVAFELANPFHDCLPRIYNNAYIKHYGMDDLWIAKTIYRLPLVNNKVFLELANRYAQQCQLYQPAELTKLVNWWHSSRFEDIPSTRLTANIDMLPYIYYVICATFHEQEFAQLRVFFSKACCLNTLFDDLMDCATSIEELDRLQNVIERWDISLSHELPLEYRIPFQEFYNTVLVMTEAASKIHKNLSPEFICKYLSGIYTKLIKSEIADARWKIEGYIPSFEEYMENAEVSISTWVHVLMSILFCGEPLTEEILNTIYDSRPLKLDRIICRLCNDIQTYKIEMKLGQPTQGVSCYMKEHPGATEEDALVYLQSLLEKTKRELNESYFITHENDLPKNIKRFNFEMVRMMLITYNETRQVDLFRNPDNELKDMIKFCLETYRTL
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Bifunctional diterpene cyclase that catalyzes the successive two-step type-B (protonation-initiated cyclization) and type-A (ionization-initiated cyclization) reactions of geranylgeranyl diphosphate (GGDP) producing successively (+)-copalyl diphosphate and miltiradiene.
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H0VCJ6
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NAAA_CAVPO
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N-acylethanolamine-hydrolyzing acid amidase (EC 3.5.1.60) (Acylsphingosine deacylase NAAA) (EC 3.5.1.23) [Cleaved into: N-acylethanolamine-hydrolyzing acid amidase subunit alpha; N-acylethanolamine-hydrolyzing acid amidase subunit beta]
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MRSPGIVLLLLLLLLLPPGAAPCPADLCPAPPRVNVSLDAAPAARWLPVLRLFDPGLLRAAVARIVGDRVPKWRDVIGKLVAEMESFLPQPYTKEIRGISDFLNLSLADGFIVNLAYEASAFCTSVVAQDSRGHIYHGRNLDYPFGDLLRKMTVDVQFLKNGQIAFTGTTFIGYVGLWTGQSPYKFTVSGDERDKGWWWENMIAALFQGHSPVSWLIRTTLSESEDFEASVYKLAKTPLIADVYYIVGGTAPGEGVVVTRNRGGPADIWPLDPLNGAWFRVETNYDHWKPVPKSDDRRTPAIKALNATGQANLSLEALFQVLSVVPVCNKITVYTTVMSAATPDKYMTRIRNLS
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Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N-myristoylethanolamine > N-stearoylethanolamine > N-oleoylethanolamine > N-linoleoylethanolamine > N-arachidonoylethanolamine.
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H0VVW3
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APOA1_CAVPO
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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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MKAVLLVVAALFLAGSQARHFWQQDDPKTSWDVVKEFANKYVDAVKESGKGYVEQLDASSLGQQLNLRLSDNWDTLSTILTKLQADFGLATQEFWDTLEKETEWLKQIVSEDLQDVKHKVQPYLENFQKKVQEEVEHYREKVRPLGIELRDGARQKLQELQEKLTPLGEDLRDRTREHVDVLRTQLAPFSEEMRQRLAKRLEELKDSATLADYHAKASEHLKMLGEKAKPALEDLRQGLLPVLENLKASILSSIDQASKQLAAQ
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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.
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H0WFA5
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BUCKY_DANRE
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Bucky ball (buc) (Prion-like protein Bucky ball)
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MEGINNNSQPMGVGQPHHPVNHTRPFFYVQPPSQPYFMYQWPMNPYGHYGFPGPALHFGRPYMAPYQFMQYPGYVIPHAPMQPIDYRRINPHYPSVASYDLRVRHHFQNAGMHRETACSEVQTDPSDSVNKLIDKIESLKACELGSDKGPNNVVSSTPDVVQGEKLTRLNEDSNLEVATKECKEDPVTRPTTYSDSAYDAESSQGRLDECVFSDVLPLDSSSVHEEEEEEEKDVNEEDEPQTVADEICSQNEMSASTTSNVFCSGVQSIADPTECHDLEKLGDEQKQDIPSADAAAVIEPLISLSEDFDLPYQILRLPCNKTTTGLSLEREIDPLVYFDSPSTLLPPQNYLSSIGSAYSYSYYPQVTQERQSVLSPSIDELSSRDEMFSTDVEDLEVVPGHVYVGGGRLAEASDMPVRSRKELPSVDKTCSVCQKTCACCGSTLQDEVGMCKMAEHSHPERDEMSDQDCDYDLEAEVRSNCESPRVSKRKCCSRHALPSCGHHCAKHRHRKLLCEGQESCDLREQARVHPKGECCEEYGALAKADKRIQKGALCRPCIEQQWREGVVSDQENWASCGAKPRSWRQVTGPQDQGRTPLRRSTCKSIHQQRPRSEYNDYDETEFTYCQRGRGSMKKRGSRY
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Prion-like protein required for the formation of Balbiani body (electron-dense aggregates in the oocyte) and germ plasm assembly, and for the establishment of oocyte polarity during early oogenesis. Mobility and aggregation properties are improved by tudor domain-containing protein tdrd6 through interaction with dimethylated arginines Tri-RG domains. Establishes oocyte polarity through interactions with RNA-binding proteins rbpms2 and dazl, initiating a positive feedback loop amplification mechanism in the Balbiani body. Interaction of BUC protein and mRNA with rbpms2 and dazl is required to mediate Balbiani body formation. Involved in recruitment of germ plasm to embryonic cleavage furrows and dorsoventral patterning through interaction with Kinesin-1/KIF5BA.
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H0YL14
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TM250_HUMAN
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Transmembrane protein 250 (Herpes virus UL25-binding protein)
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MPVMPIPRRVRSFHGPHTTCLHAACGPVRASHLARTKYNNFDVYIKTRWLYGFIRFLLYFSCSLFTAALWGALAALFCLQYLGVRVLLRFQRKLSVLLLLLGRRRVDFRLVNELLVYGIHVTMLLVGGLGWCFMVFVDM
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May play a role in cell proliferation by promoting progression into S phase.
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H0ZAB5
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GALT3_TAEGU
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Polypeptide N-acetylgalactosaminyltransferase 3 (EC 2.4.1.41)
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MALKKAPKLFKTFFHWKLWKFSIIVFVFLVFLFLLQREVGVQDFKDEAGIEPVVGKKSHVLGLVLNAMNNIKGAKPKMQIKAPIRQTKVPGERHCLPGHYTPVELKPFLDRPLQDPNAPGASGKAFKTINLNSEEQKEKQAGEEKHCFNAFASDRISLHRDLGPDTRPPECIEQKFKRCPPLPTTSIIIVFHNEAWSTLLRTVHSVMYTSPAILLKEIILVDDASVDEYLHDKLDEYVKQFQIVKVVRQKERKGLITARLLGASVATGETLTFLDAHCECFYGWLEPLLARIAENPVAVVSPDIASIDLNTFEFSKPSPYGHSHNRGNFDWSLSFGWESLPKHENKRRKDETYPIRTPTFAGGLFSISKDYFEYIGSYDEEMEIWGGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSKSPHTFPKGTQVITRNQVRLAEVWMDEYKEIFYRRNTEAAKIVKQKTFGDISKRIDLRQRLQCKNFTWYLSNVYPEAYVPDLNPLFSGYLKNIGNRMCLDVGENNHGGKPLIMYSCHGLGGNQKELCLHASKGPVQLRECTYKGQKTFAVGEEQWLHQKDQTLYNEALHMCLTGNGEHPSLASCNPSDPFQKWIFGQND
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Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Glycosylates FGF23.
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H1UBK1
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MAP2_CAEEL
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Methionine aminopeptidase 2 (MAP 2) (MetAP 2) (EC 3.4.11.18) (Peptidase M)
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MPPANGKKGKKGGAAKAVRRIQYRPKSFKHSRFVKHAHFWSAAPEEDFDAILAEMQLADAKTAAKEATKKDAKGGKGKANGSAAATAAPEEAKQAWQAEIAAMKPIDEQFPDGKFPHGIDESPYYLKGKDGRVATDRESNEEKKALDISYEEVWQDYRRSAEAHRQVRKYVKSWIKPGMTMIEICERLETTSRRLIKEQGLEAGLAFPTGCSLNHCAAHYTPNAGDTTVLQYGDVCKIDYGIHVRGRLIDSAFTVHFDPKFDPLVEAVREATNAGIKESGIDVRLCDVGEIVEEVMTSHEVELDGKSYVVKPIRNLNGHSIAQYRIHAGKTVPIVKGGEQTKMEENEIYAIETFGSTGKGYVHDDMETSHYMKNFELADEKIPLRLQKSKGLLNLIDKNFATLAFCRRWIDRLGETKYLMALKDLCDKGIVDPYPPLCDVKGCYTAQWEHTILMRPTVKEVVSRGDDY
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Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for germ cell proliferation and/or differentiation.
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H1ZV38
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GEOA_CASDE
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Geraniol dehydrogenase (GeDH) (EC 1.1.1.347) (Geraniol oxidation pathway protein A) (Perillyl-alcohol dehydrogenase) (EC 1.1.1.144)
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MNDTQDFISAQAAVLRQVGGPLAVEPVRISMPKGDEVLIRIAGVGVCHTDLVCRDGFPVPLPIVLGHEGSGTVEAVGEQVRTLKPGDRVVLSFNSCGHCGNCHDGHPSNCLQMLPLNFGGAQRVDGGQVLDGAGHPVQSMFFGQSSFGTHAVAREINAVKVGDDLPLELLGPLGCGIQTGAGAAINSLGIGPGQSLAIFGGGGVGLSALLGARAVGADRVVVIEPNAARRALALELGASHALDPHAEGDLVAAIKAATGGGATHSLDTTGLPPVIGSAIACTLPGGTVGMVGLPAPDAPVPATLLDLLSKSVTLRPITEGDADPQRFIPRMLDFHRAGKFPFDRLITRYRFDQINEALHATEKGEAIKPVLVF
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Catalyzes the NAD(+)-dependent oxidation of geraniol to geranial. Is involved in the anaerobic degradation of the monoterpene beta-myrcene. Can also catalyze the oxidation of (S)-perillyl alcohol to perillyl aldehyde, and to a lesser extent, the oxidation of nerol, citronellol, cumic alcohol, and benzyl alcohol. Cannot use NADP(+) instead of NAD(+) as cosubstrate.
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H2AM12
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GP_SBVBH
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Envelopment polyprotein (M polyprotein) [Cleaved into: Glycoprotein N (Gn) (Glycoprotein G2); Non-structural protein M (NSm); Glycoprotein C (Gc) (Glycoprotein G1)]
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MLLNIVLISNLACLAFALPLKEGTRGSRCFLNGELVKTVNTSKVVSECCVKDDISIIKSNAEHYKSGDRLAAVIKYYRLYQVKDWHSCNPIYDDHGSFMILDIDNTGTLIPKMHTCRVECEIALNKDTGEVILNSYRINHYRISGTMHVSGWFKNKIEIPLENTCESIEVTCGLKTLNFHACFHTHKSCTRYFKGSILPELMIESFCTNLELILLVTFILVGSVMMMILTKTYIVYVFIPIFYPFVKLYAYMYNKYFKLCKNCLLAVHPFTNCPSTCICGMIYTTTESLKLHRMCNNCSGYKALPKTRKLCKSKISNIVLCVITSLIFFSFITPISSQCIDIEKLPDEYITCKRELANIKSLTIDDTYSFIYSCTCIIVLILLKKAAKYILYCNCSFCGMVHERRGLKIMDNFTNKCLSCVCAENKGLTIHRASEKCLFKFESSYNRTGLIIFMLLLVPTIVMTQETSINCKNIQSTQLTIEHLSKCMAFYQNKTSSPVVINEIISDASVDEQELIKSLNLNCNVIDRFISESSVIETQVYYEYIKSQLCPLQVHDIFTINSASNIQWKALARSFTLGVCNTNPHKHICRCLESMQMCTSTKTDHAREMSIYYDGHPDRFEHDMKIILNIMRYIVPGLGRVLLDQIKQTKDYQALRHIQGKLSPKSQSNLQLKGFLEFVDFILGANVTIEKTPQTLTTLSLIKGAHRNLDQKDPGPTPILVCKSPQKVVCYSPRGVTHPGDYISCKSKMYKWPSLGVYKHNRDQQQACSSDTHCLEMFEPAERTITTKICKVSDMTYSESPYSTGIPSCNVKRFGSCNVRGHQWQIAECSNGLFYYVSAKAHSKTNDITLYCLSANCLDLRYAFRSSSCSDIVWDTSYRNKLTPKSINHPDIENYIAALQSDIANDLTMHYFKPLKNLPAIIPQYKTMTLNGDKVSNGIRNSYIESHIPAINGLSAGINIAMPNGESLFSIIIYVRRVINKASYRFLYETGPTIGINAKHEEVCTGKCPSPIPHQDGWVTFSKERSSNWGCEEWGCLAINDGCLYGSCQDIIRPEYKIYKKSSIEQKDVEVCITMAHESFCSTVDVLQPLISDRIQLDIQTIQMDSMPNIIAVKNGKVYVGDINDLGSTAKKCGSVQLYSEGIIGSGTPKFDYVCHAFNRKDVILRRCFDNSYQSCLLLEQDNTLTIASTSHMEVHKKVSSVGTINYKIMLGDFDYNAYSTQATVTIDEIRCGGCYGCPEGMACALKLSTNTIGSCSIKSNCDTYIKIIAVDPMQSEYSIKLNCPLATETVSVSVCSASAYTKPSISKNQPKIVLNSLDETSYIEQHDKKCSTWLCRVYKEGISVIFQPLFGNLSFYWRLTIYIIISLIMLILFLYILIPLCKRLKGLLEYNERIYQMENKFK
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[Glycoprotein N]: Glycoprotein C and glycoprotein N interact with each other and are present at the surface of the virion (By similarity). Glycoprotein N probably locks the Gn-Gc complex in a prefusion state (By similarity). Glycoprotein N and glycoprotein C are able to attach the virion to host cell receptors (By similarity). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity).
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H2DF87
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RHVI1_ROSHC
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Acid beta-fructofuranosidase 1, vacuolar (EC 3.2.1.26) (Vacuolar invertase 1) (RvVI1)
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MDTSTSAYAPLPGEDPLFSGHPPASLRRSWKGFAVIFASVLFLLSLVGLIIHQGPQQPPDVMPDKQDEHHHPQSTTPASETTASWEPRGKALGVSAKSNPPVSDELSYNWTNAMFSWQRTAFHFQPERNWMNDPNGPLFYKGWYHLFYQYNPDSAIWGNITWGHAVSTDLIHWLYLPIAMVADQWYDANGVWSGSATLLPDGQIVMLYTGDTVDAVQVVCLAHPANLSDPLLLDWVKYSGNPVLTPPPGILTTDFRDPTTAWTGPDGKWRITIGSKVNTTGISFVYHTEDFKTYNMSKGVLHAVPGTGMWECIDFYPVAINGSKGVETSVNNPSVKHVLKASLDNTKVDHYALGTYFEENETWVPDNPGLDVGIGLRYDYGRYYASKTFYDQNKERRILRGWINETDTESDDLAKGWASVQTIPRTVLFDNKTGTNLIQWPVEEIEELRLNNTDFSDVLVEAGTVVELDIGTATQLDILVEFELEPLESSETVNSSVGCGGGAVDRGTFGPFGILVIADETLTELTPIYFNLANSTEGDVITYFCADERRSSKAPDVFKQVYGSEVPVLDGEKHFARVLRALRKEVGR
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Acidic vacuolar invertase involved in light-induced bud burst.
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H2E7Q8
|
POPB_GALM3
|
Dual function macrocyclase-peptidase POPB (EC 3.4.21.26) (Prolyl oligopeptidase B) (POP B) (Toxin-processing prolyl oligopeptidase)
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MSSVTWAPGNYPSTRRSDHVDTYQSASKGEVPVPDPYQWLEESTDEVDKWTTAQADLAQSYLDQNADIQKLAEKFRASRNYAKFSAPTLLDDGHWYWFYNRGLQSQSVLYRSKEPALPDFSKGDDNVGDVFFDPNVLAADGSAGMVLCKFSPDGKFFAYAVSHLGGDYSTIYVRSTSSPLSQASVAQGVDGRLSDEVKWFKFSTIIWTKDSKGFLYQRYPARERHEGTRSDRNAMMCYHKVGTTQEEDIIVYQDNEHPEWIYGADTSEDGKYLYLYQFKDTSKKNLLWVAELDEDGVKSGIHWRKVVNEYAADYNIITNHGSLVYIKTNLNAPQYKVITIDLSKDEPEIRDFIPEEKDAKLAQVNCANEEYFVAIYKRNVKDEIYLYSKAGVQLTRLAPDFVGAASIANRQKQTHFFLTLSGFNTPGTIARYDFTAPETQRFSILRTTKVNELDPDDFESTQVWYESKDGTKIPMFIVRHKSTKFDGTAAAIQYGYGGFATSADPFFSPIILTFLQTYGAIFAVPSIRGGGEFGEEWHKGGRRETKVNTFDDFIAAAQFLVKNKYAAPGKVAINGASNGGLLVMGSIVRAPEGTFGAAVPEGGVADLLKFHKFTGGQAWISEYGNPSIPEEFDYIYPLSPVHNVRTDKVMPATLITVNIGDGRVVPMHSFKFIATLQHNVPQNPHPLLIKIDKSWLGHGMGKPTDKNVKDAADKWGFIARALGLELKTVE
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Dual function macrocyclase-peptidase involved in the biosynthesis of the highly toxic amanitin toxin family of macrocycles. Cleaves peptide bonds on the C-terminal side of prolyl residues. The enzyme first removes 10 residues from the N-terminus of a 35-residue substrate. Conformational trapping of the 25 amino-acid peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization. The enzyme rebinds the 25 amino-acid peptide in a different conformation and catalyzes macrocyclization of the N-terminal eight residues.
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H2ELN1
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TER_NICLA
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Terpineol synthase, chloroplastic (EC 4.2.3.111) (1,8-cineol synthase, chloroplastic) (EC 4.2.3.108) (Alpha-pinene synthase) (EC 4.2.3.-) (Beta-myrcene synthase) (EC 4.2.3.15) (Limonene synthase) (EC 4.2.3.-) (Sabinene synthase) (EC 4.2.3.-)
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RRSGNYQPTMWDFEYIQSIHNDYAGDKYMKRFNELKEEMKKMIMAEGSQELEKLELIDNLQRLGVSYHFKHEIMQILSSIKQHSTPADSLYATALKFRLLREHGFHISQEIFDGLSETHTKDTKGMLYLYEASFLATEGESELEQAWTEKHLREYLKNKNIDQNVAKLVHRALELPLHWRMLRLEARWFISFYKKRQDMIPLLLELAILDFNIVQAAHIQDLKYVARWWKETGLAENLPFARDRLVENFFWTIGVNFLPQYGYSRRIETKVNALVTAIDDVYDVFGTLDELQCFTDAIQRWNTDELDNLPDNMKMCYFALDDFINEVACDALIVPYLRNAWTDLCKSYLIEAKWYFSKYIPTMEEYMDNAWISISAPVILVHAYFLIANPVNKEALHYLRNYHDIIRWSALILRLANDLGTSSDELKRGDVPKSIQCYMNEKKVSEEEARQHIRLLISETWKKLNEAHNVAAHPFPKMFVKSAMNLARMAQCMYQHGDGHGGQNSETQNRIMALLFESIPPA
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Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products of the 'cineole cassette', volatile compounds present in floral scent. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into alpha-terpineol and, as minor products, sabinene, beta-myrcene, limonene, alpha-pinene and 1,8-cineole.
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H2EQR6
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DSG21_DANRE
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Desmoglein-2.1
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MARRISPVVAFLLCFGLSHFFEAEARLQHSVALHRQKREWIVPPQILEENVDYTKKDFIAKIRSDKEVAHMKYLRYSLRGVGADQEPFNLFVVNPETGYVRITGILDRESISQYNLSGIALFTDGSIAENDIGLRIKVKDQNDNAPVFGVMNPGAVDELSAVGTEVMRLNCFDADEPGNPNSQIKYEIVDQQPAGQSMFTVENNRRVVVANPNLDRETVDQYVLLVKASDLNGAPGGNAATGTVTIKINDVNDNVPTLGGPYEASIEENTEKVEVMRLKVSDLHLKGTDNWEGDCYIASGNEAGYFSIHMDPKTNEAVLMLDKAVDYEDVKDLNLGIGVANKAPFHPSVSGGSQGATISFGGSGGGAGSGAAGGAGAMGGASGSGGGTGASSWSSSGVPLYNVNIKVKNQPEGPKFFPGTKAIPISEGKAFDSTEIIARYPAIDTDTGKEATNVKYIKSSDPDNWLTIDEKTGAIRMNKAPDRESKYLVNGTYYAKVLSITQDLPSKTATGTIAIQVEDFNDHCPTLISNVQTLCTDKDAVLVTAKDEDAPPNGAPFDFNIVSEGTAGKWTVEYMNDTTAIFRTHEKLWPGPHELMVEVTDQQGLKCPEPQKLQVDVCTCKNQGGCDRTATGDAKKGSRLGPAGIGLLLLALLALLLIPLLLLLCTCGMTGAFTDMPFETKVHLISSNTEGQGEDRDVPLMCPPSNVDGMGFMTKDYMAVGAMHSAGLGLGVGAGVGAAGFLESTSTMGGRGYNEMELDYMNSIGRNNAYSSRDMAGDFDGMALSDGYLCEYYSQKSRVVDGFGKDDPMVYDYEGKGSPVGSVGCCSLLEDQNDLEFLNDLGPKFTTLADICGGKKTEIPAPAPAPLPPPPKPVVDRSEVVSSTTNILNTGNIATNRVNTVNVASNMATASSTRVENVLVTDNRPTMITSVHPAPTLLVQPQPMYYMVEQQPSTVLVAERPAMTQGMYVLNSGPVAEGMVVQGGNIAANTLTRGERMVLVFRGGPAQALNNGMLHTSNLSGSQLLLVDGGATSGQVLQGTIQRGVAGSQGLMFVDGQGGQVIQGSINNGISTHGGSQNVFYVENKGGSSVVQGGLQMGKASTAGSLIGDVGIGGSSVKITQNPSSHKVVVQERKVVTTQSVK
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Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion (By similarity). Required for embryogenesis, specifically for progression of epiboly and normal convergence-extension movements during gastrulation.
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H2FH31
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LEC_CREGR
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Galactose-binding lectin (CGL) (GalNAc/Gal-specific lectin)
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MTTFLIKHKASGKFLHPYGGSSNPANNTKLVLHSDIHERMYFQFDVVDERWGYIKHVASGKIVHPYGGQANPPNETNMVLHQDRHDRALFAMDFFNDNIMHKGGKYIHPKGGSPNPPNNTETVIHGDKHAAMEFIFVSPKNKDKRVLVYA
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Galactose-binding lectin. Binds both alpha and beta anomer of galactose (Gal), but has a stronger interaction with the glycans having alpha Gal at the non-reducing end and binds beta Gal weakly only in highly branched glycans. Has high affinity to Galalpha1-4Galbeta1-4GlcNAc. Binds N-acetyl-2-deoxy-2-amino-galactose (2-deoxy-GalNAc). Binds N-acetylgalactosamine (GalNAc). Binds porcine stomach mucin (PSM) with high affinity. Binds galactosamine. Binds laminin, bovine submaxillary mucin (BSM), fibronectin, type I collagen and gelatin with a decreasing affinity, respectively (Ref.3). Has hemagglutinating activity towards human type A erythrocytes (PubMed:9568372, PubMed:26439416, Ref.3). Hemagglutinates also human type 0, B and AB erythrocytes as well as rabbit and mouse erythrocytes. Agglutinates both Gram-positive and Gram-negative bacteria including B.subtilis ATCC 6633, S.aureus ATCC 21027 and E.coli 3254, respectively. No agglutination activity towards Gram-positive S.amurskyense CMM 3673. Has bacteriostatic activity on S.amurskyense CMM 3673, B.subtilis ATCC 6633, S.aureus ATCC 21027 and E.coli 3254. However, has no agglutination nor bacteriostatic activity on Gram-negative C.scophthalmum CIP 104199 or A.troitsensis KMM 3674. Inhibits growth of fungi from the genera Aspergillus, Penicillium, Trichoderma and st. Mycelia. Inhibits germination of spores and hyphal growth of them. Has dose-dependent cytotoxic effect on the human globotriaosylceramide (Gb3)-expressing Burkitt's lymphoma (Raji) cell line. Binds to Gb3 in these cells leading to activation of caspase-9/3 and PARP. Has dose-dependent cytotoxic effect on the Gb3-expressing human MCF-7 breast cancer cell line. No cytotoxic effect on myelogenous leukemia K562 cell line, which does not express Gb3. Activates immune responses in mice and increases cytokine production of TNF-alpha, IL-6 and MCP-1 in the serum and the peritoneal lavage of mice. Induces TNF-alpha and IL-6 secretion in mouse RAW264.7 macrophages, mouse bone marrow-derived macrophages, human THP-1 macrophages, human peripheral blood mononuclear cells (PBMCs) and human blood monocyte-derived macrophages. TNF-alpha production in macrophages could not be inhibited by GalNAc, GalN or Gal, indicating that induced cytokine production is separate from its sugar binding activity. Increases intracellular reactive oxygen species levels, expression and phosphorylation of protein kinases PKC alpha/delta, expression of COX-2 and NF-kappaB, and activates the MAPK pathway by increasing the phosphorylation of ERK1/2, JNK1/2 and p38 in mouse RAW264.7 macrophages. Induces endotoxin tolerance in lipopolysaccharide(LPS)-activated macrophages by down-regulating IRAK2 expression, reducing JNK1/2 phosphorylation and NF-kappaB activation. Can slightly increase the bactericidal activity of RAW264.7 macrophages. Has DNA-binding activity. Recognizes pathogen-associated molecular patterns (PAMPs) and binds to LPS from E.coli, but has only little binding to beta-1,3-glucan from E.gracilis and peptidoglycan from S.aureus. Activates secretion of TNF-alpha and IFN-gamma by the human peripheral blood cells (HPBCs). May be involved in innate immunity acting as an antibacterial and antifungal agent involved in the recognition and clearance of pathogens.
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H2KY84
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CMTA1_CAEEL
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Calmodulin-binding transcription activator homolog 1
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MNNSVTRLLFKRLLTLQLCHHFDIIPHRDQSFDCVQMQQPQNETANNFIPSIQLLWSTDPPQIRPDGTYPQAVELFPCFKDKWNTKEEILNIILAANADPKSNCVTVQSSPRPCSSSQFIYPRLDNAWYKNDGYIWKKRTNGKQNREDHLNLKISGHPHISAKYIHSAIVPTFHRRSYSVPDSDCHVLVHYLNVKTNNKIDDQAEEIARSMIENKVFISLSQLHDQLSPIFLQTLNVNQLVAEINEHLKKKGVNLPTSPLPQEPSSSTSRELERRNSCSSAFRKGLSSVALRRQPSANSEIDANHIGTMLKRFGCNGSSSDRISIIQPTMQNFQSIRSHQNHVAMESRSPSGDGDSRPITFEEDASYQQLSIKSSTNVSTPASAFAEKMKIRSGSQESPMGPPSSSSVTSTSLIPIIEMTPSSSSLKGGQKMLVVGGYYRKGHEYKISFGRGRMMPAVLIHAGVLSCVIPPSAKPEVVQIRVFCNGQAISTASEFTYEPQSAHLIKENDDTLVQIFEKIRIMACAFNAYSSIENIQSSSCMESLLANIVQQIDNEVSSQNLNYKTELLNGSAHFPSKTVLHLVASLDYDRLFEALIDLSRKVPACREFDIFARDNDGSTPLHTACKNSASRIARLIISIDSSAIDVVDDRGRTPVEVAPEHSIDMLSDKNNEEERVNATELWVMTNGKAFTTDKILDGKISRAPIAEKPDDLLREATSSYSIMSEMYEGPMLQAGTSRECDEDCESCCDPDSTQQLHVEIAMDTDVHVPDSPKMARLFHAVTSPGIVVPPNARARMADLARQIIEALPDRIKRNSEVSMCPDEEDPGQNHHGGVEPMFYQQASCSMSTDSPNMMDDYFDMMATETRNDIFTEPRSTETTETSASKSAQLFATHCNFFDDRSFASSSTRANTFESDTLDFDKDLGEFFTIHVDRFVDPIQQRLANLKYNDDEQRDVYEAAMVIQRAYRVYRARSTTRRQEDIERRAALKIQGCYRRYKQFCYFKKLHNAAIVVQKHFRMRKRDDKEEGAVEAVIASVPEHPTLDGQSICIQVPKTNSTMLRERAATTIQVAYRYRHRKRQAAARKIQNFMRQNRNNVNIDDGHTQHLIAENACAKRRRYVACPQTSGDQRNKRDSDGERKRDAHHDAPEFIPIGATPSSTTIPHRPTQRHHPWDQLKPPYGCGTLA
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Transcription factor. Positively modulates neuronal levels of the ubiquitous Ca2+ sensor calmodulin/cmd-1, probably by direct binding to the cmd-1 promoter, thereby regulating Ca2+ signaling, physiology, and behavior.
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H2KY86
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HELQ_CAEEL
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Helicase POLQ-like (EC 3.6.4.12)
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MNRTPIRRCKSAEIEEDPFSPIPKFSRLRTPRTSREYVCPLKSTSPQSPSSSTENEPPPVSVTSPPARKRALEESTVTPIQQKIGPPVLKRSSLSKLADGFRTAAYLNNESENDDDPFGLSFRNEQVLMSKCAPAPEKRPETLTLDPSKCLPERDMEMYRKIKKLDKFYDWQQECLSDKRLLDGENCILSLPTGAGKTLIAEVLMLREAIVRKRNAILVLPYVAIVQEKISALAPFEDAFGINIEEYASNKGRFPPIKRRKRVSVYVATIEKANMLINSLITQGQLDRVGMVVVDELHMIGDGGRGAILEQLLAKFLYKGTGQIVGMSATLPNIDDLKFALRAFVYSTNFRPVELTEFVKIGQTMHQVSENGDLNPAGDLPTNNLKSTDPDGICQLLAKLIPKNSAVIFCPNKKNCENVAVLIAKTLPAHIRQAKRAESDAFLQSYLSDNDDERMDAVLKQCILSGVAYHHSGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLPVRRVIIKAPMVGRERLGKAQYLQMAGRAGRAGFDTKGDCITIIKAGEEERWFREMLKSDIPRCMSSLSSEESMGSFILDCVVLKLAENIEEIMTAVRYSLFYAQESPENIRKLVESSVKRLEEHYFITIEPLEQDVASEPSAQASSIPRVPGKISPSDLGNAVFNAGFDPDEATRLHADLVSSLNQGVIFASHFHLLFIITPYEQVCNINWDLFLLMYNALPSSERKLLAECGLEEKFILEAIITRVDLTAGTPRMRLYIALMLQKIWNHEPMYTVAERFGVEKGWLQATLQSSISQAASIAKFSEKITTMWPLRKLLPELVQRLSEAAQPELLPLMTVDGIKKARAAILFKAGYKTVGMIARANPLKLVQELGTIRMAQANSIIASARMVLRDQVDEKMEELDVWGVATDSFNYF
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Single-stranded 3'-5' DNA helicase that plays a key role in homology-driven double-strand break (DSB) repair. Involved in different DSB repair mechanisms that are guided by annealing of extensive stretches of complementary bases at break ends, such as microhomology-mediated end-joining (MMEJ), single-strand annealing (SSA) or synthesis-dependent strand annealing (SDSA).
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H2KYH3
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RING2_CAEEL
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E3 ubiquitin-protein ligase RING2 homolog spat-3 (RING domain-containing protein spat-3) (EC 2.3.2.27)
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MDDSPGPSTSKSARDKAENAEENTSDSSSDSEVSSASEKSEESRPSSEKKKVITRVIPVRPPTRDKGHRVNLLESGNESETKSLYQRAKEGIPSYKGKPEIKLPTTSEQYYDLEEVLMNPARMEGRELTLNAYDAVRNKYNVLPGKSVCEADLQKVIGSFSCDVCQELIQGSIMTKKCGHRFCDQCILVAFMRSGNTCPTCRQNLGSKRELQQDPRFDQLIYQVVESRSIVGRMMAENREHEKDVYFGRKGYIEGGSDWNKRYGIDPNSKLKAPRPLKSAGRKKIRWFHESDEDGSVRKVMESKKGAPKEDDTNYLENDKEGTSVAAEKEVLEEGEMDFPIEIKSSDEEQTDLDDEEESMLDSDFEISDNEDVSKPSCSTSKKTTNRSRDSSESDNDSRDNELQKKKRKMKRKNVPKTDGSDVSNESFDEDASGEVVATKLIKESKKKPCGRPKKKFAPELIEGDIPTPSEDSLTSSDEERDDNAADPYAFVFQKEFNRDPRRDGHPEKDKLYNFDFMIDMNHQVDRKFEKDGEIHVISDDSNSEHESDEAEDRESSIDSEHEKEISKFLSHRQPLPNPTSVDDDCQVITVVKKDVKQSAITSKPGETSPDSSSKIEEKPDKVSEEVSDDEMTPEHITADKGTDTFLNNIMEHDDEMYGGYLFRPGDTGISRPKVQRAPGTNRLSMNVCPEAVYVVYPQPVLKEGKKKLVIPPEDYEISSDETVTLSDSEETSPSAEMEQSETSEAGPSTIIKTSGTERETQGSSSPSEPSTSRDRKMHKRKLDTRRRKLADDSDLSDFDVFSIDGNELVATGKPIIKHKVFYDSANRMPSKSNLDFTGRRNAREIPMEEISRLAEEQVAHEEYKIHRRRQVVLEAVEAASKKLNVYVDTTEEEEIEEEETPEEEVVKVASPTAPIATENPTTSTAPFEEGVAMKETPIEEIFFDPDEPCSSAQAAQRELIIERVGKEQQIIEDSLEQNRKPSSKTVKESESREAQEPRIEKDEMESEQQKKDADNPTVEVDKESEASSSESDKSDFEDETLDAQSKTVKISLKHEKTVSDEEIEDFDTKFGEFVATADAKMIKRTIGEYVSTEFLKLVAQQPAVTDEVLALGFCVRNTDQEFSTIKETGKRTNKNPDDVRLESMVKNFRESFAAKHRPVPRKLPTNIERMYIERAHMVKYKHVVDMEPLHMKILIALQKQQIAATCANLSQPVTVTPEEHAEQVQLLHNLQNPSILRPLLNNPQFALTLHKAQQQAIQQQRAQQKAQTQKELAARQAEQARVEELARKRIAQEDAEKALRQKGEQMSNVSGIPVSSDQNAQSSNAQQTGLIENQTTTTNSDSLTRPNTLADNSHLGESQQIPVIESIQSSTSEALKESENYKDMPILTPASTVSSKSSAPATRRPSRPCSSYDRPSSPSVVIRERLGSDGALINRPPNRCNIDKSRSRSPISRAPVETVRINDHGQNETILAGNITHTVETTILEEGTSIGQDSTIRYDGECSTTQYIDKTIDLDNSKNGTNVDEEQSNVLKLRENDLNREMLRYANRYHPSTMLAMGNLSINERHNKVQQVLASQELQDLIARHTSGAVSQTQVEVVGGEGVCAGTSDAIGETDEDDDVEEEPEFTVDQLELAKKILKQRQGLESSEDSDSDEDMVYDNVDGSVIRRAPHKKRETRKKKNIFVPNIPPKIRRKYVDKKIEMERAKYRARIKSQKMASIRIAVPQKPTQQFATPQQPVRGPGKHSAAAAARATPKPKKAKMSNVQMSIVQPPLPLHQLQGHMSAPTKITAVPNVAAGFHQNQQQLYSDMAQAPQSTPIRTTPQPGTGSAPQAQTPQSHLAQLGQFVNGANQQQAPQQQGMYTAAQLQAMQAAVAQTAQAAQAAYAAEAAYQAQVAQQARAAPPQQLVQRQVPVGHPGQVNVPMPAQMLNQGNPQMAVNPAQAQMMDERRKMEEVNAVYHLMQSRGQFPPTNQELFQVQFAQAQADLRSAAAQAAQAAQAQAQMTNMRAQAEAVARQQAMMKQEQARAQAAAKEAARLKAETEAAKAKVQAEAEARRKAEQEMRVRQAQAAQTQAAQAQAQSQAHAQNQAQTQAIVEIQRMIQSGQPLSMQQMQQLQQMSQVQMQHAQQVQQMQQMQMQQLQMQQFAARMQQGTPKPAVSQQAVQQGMPAGIQGMPTGMGMQQLQGLGMPGMQLPQQAGQSQQTSQAQQQQLFMQLQLQQQQLMQHQLQQQLQMQQHQQHQQQQQQIQMQQQQQLAQQGLVPNVSSAWLQQQAQLAQQQQQVVQQNLLMRVPSAQTPVAPRAPTVAPQSVVQQAPAPATPIAISVATTQVTRPETVEPFRSISSGTGTGTERINNNVELELWPTNGYSEKKRKEGSQASPIFGASAGDSTFYHVACLIRSRSACNADDVGSLWVLRLEDQTLLQFQLQQTLAEAQRFVGKQHLVIFYDDVMSGEVQQSKEYVINREFKPSNRQIPN
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E3 ubiquitin-protein ligase playing a central role in histone code and gene regulation (By similarity). Involved in ubiquitination of histone H2A. Plays a role in the formation of the male-specific genital sensilla (simple sense organs) known as rays. Required for normal migration of the hermaphrodite specific neurons (HSN) and for extension of some neuronal processes. Represses vulval fates in hypodermal cells that do not normally contribute to vulval development.
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H2KYH4
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HAM2_CAEEL
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Zinc finger protein ham-2 (HSN abnormal migration protein 2)
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MPYRAELKRPDLKGSFPCSICQKVFCHSSSLSRHRMQAHFKSYTCTTCNNEIPSNDTLRSHMYRVHNITRMFMCRCCNWAFPDKTSLHIHMQSMLKNGTPGEAAVLAKSSDVVDSTSESGSPRQSPPFSPDLLMQKRMLQVAANNNNIGSIFPTLLKSPDSKSMFPLDLSNMGPSQFLSAWLANNPINTAALNLAAQQTPSKDSIQSSNISDYDDLEVQTTEEDIKFEVESSDVSPRSVIVKTEPTFKRELEHDADIDVEGDDGEPPLKMTIDDKNIHISHDQPSPTVSDSHISGGSSSHSGESLKCFDCQVARGKLVAVEDKCRAYEKTIRELQVQVDFLRKIQPNPMPPVMLPPPMMPMPSPGPNNLFQNPAMRMLLNNLIHMNRPSVVP
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Probable transcription factor that acts downstream of egl-15, to promote migration of the HSN motor neurons from the tail to the gonad primordium during HSN cell differentiation.
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H2KYJ8
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NHR66_CAEEL
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Nuclear hormone receptor family member nhr-66
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MPPINEPTATTTSASSVWQGMTQLKSQVDLINIARGILSTPATTSTSCLDIQNSTPIIGSLASGKSQTPILTATMTPQIGLTGLGSLTSLPPELLLQFARLDGFNLLPAVGSPAIPSSSSCSEPSTSQASTVVSAPTLPPPSPLTSLPQKPAPLMPSGHVTTVDQQNRQQHQQQQRQQQQAQQQNSMARKYSMDTIQHHTMQHPHQLQYIPNHFMTASTDVFAAMDMSQKQSSPPGIFKIVAAKNEPSSSSNSQPGTPAMGDRRAVPACAICGTDSTGIHFGVDACAACSAFFRRTVVLNKDYSCNKGGKCTVVKDGSAGQKCRACRFRKCISSGMDKNSVQHRRDAIGKYSAGVKRELSPDAEFEPSAKVSTVSEPSTSSGPSGGFNQNVSSPAGIPRVPSTLRTTQASTCMNSACGQKSVLHELICRQNFLTEQRQLFYAGCLGDWFRKPSSIENQTLSELTDFSSCMFHLWKIEPRLAADFMNRNRYLDPLPIVEKLKIYRNFVIMRQSVEEPYLTWRHGGLEKRWFVMPNNTYIDFNNIAKYFENGALKDLKLDYETTTNLFLPSFTHAMDTIGEKMKKNNITETELTILLGLVLLDPGIYGIHESTRKFLKRIRDQLIHDVYMYYEDEMSHLYDPEIRMADIFMLVAAIKIHSIKTSENMHMLRVFDLIPADACFNQMLDVESVNVSPDGQKDSEAEQGPSPVSVPEAARGSYQDDDMPPVLEKNCDL
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Transcription factor. Binds to regulatory elements and regulates transcription of target genes, including the potassium channel accessory subunit mps-2. Negatively regulates transcription of mps-2, thereby modulating age-dependent memory decline. In concert with nuclear hormone receptor nhr-49, involved in regulating target genes with roles in sphingolipid breakdown and lipid remodeling. Plays a role in modulating mitochondrial morphology and function.
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H2KYQ5
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GYG1_CAEEL
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Glycogenin-1 (GN) (EC 2.4.1.186)
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MSEAWITLATNDNYAQGALVLVHSLRTAGTTRKIHCLISNEVSAPVRKQLEEHFDDVSIVDVFNSNDSDNLRLIERPDLGVTFTKLHCWRLTQYTKCVFLDADTLVLRNADELFTRPDFSAASDIGWPDSFNSGVFVYVPNNETYRQLVDFAVTHGSYDGGDQGLLNDFFSNWRDLPSEHRLPFIYNMTAGAFYTYAAAYKRYGANTKIVHFIGSVKPWHGSAAVHTGEHFQQWQKIYHAHVNHTSRTNEHAAVFPSHHHTPEHRSHSADHPKIERKDSIVREIGNFVMHVVQSVNILPSYDTDANTSDSHRNNEPHKHDQQREEHHELPHNKFQTPHEESQDIVGSTDCFGSQMPKYNADSETDREVEQITNNTPCPAFVPFERREEYQAASPSTEERRAAWEAGQPDYLGRDAFVHIQEALNRALNE
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Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for gsy-1.
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H2KYS3
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DAF9_CAEEL
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3-ketosteroid oxygenase (EC 1.14.14.-) (Cytochrome P450 daf-9) (DAF-9)
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MHLENRVLSSVLDYASKFYKRMSSLVFFSANSIQVQMNISQSSWIKCRDWMAFALSHHIIMGIYLLILRNFLPQVVPDFEWQHYFMRVFIVHIIYIIISYFIRITRYPPGPPPMAVFGNSPFVNILTPEQTFLEYREIYGPIFTLHLSQPTIILAEYKTIQEALVKNGQQTSGRSSAESFVLFTGDRLNGDGVILAMRQKWKDMRHEISRFMNKWYGAPMDELVLHHTRCLEQELAKIAETKSLIDLRDPLAGAIANVIQQITIGRNYMYQDQEFQTQLRDINAVVKEIMTAEVFFVNCYPWLRYLPEGILRKWTNYKRSGFRLQQWFRTILEEHHVNRHQGDFMSHMIDLQESKQEQFRDLSIILTCGDMWTGGMETTVTTLRWGIIYLLNNPEVQAKCQMEILDVFGNDIPDMGKMNQTPYVRATLSEIQRLANVLPWAIPHKTIEECNIGGYDIPVNTEIIPALGAVLFDPNVFESPKQFKPERFLDEEGKYRVMEEFRPFGLGPRVCLGERIARTELYLIFASLLQNFRFYLNRGDPIPVAERVIGGITAPPKPYATRVEYLGNRLIN
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Converts the 3-keto steroids 4-cholesten-3-one and lathosterone into the carboxylic metabolites 3-keto-4-cholestenate (Delta(4)-dafachronic acid, Delta(4)-DA) and 3-keto-7,(5a)-cholestenate (Delta(7)-dafachronic acid, Delta(7)-DA) respectively, by catalyzing successive oxidations at C-26. Dafachronic acids bind directly to the nuclear hormone receptor (NHR) DAF-12, suppressing dauer formation and inducing reproductive growth. In a non-cell autonomous manner, negatively regulates body wall muscle arm extensions to motor neurons probably by preventing daf-12 isoform b activation. May be involved in thermotolerance.
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H2KYS8
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CPNA1_CAEEL
|
Copine family protein 1 (Atypical copine family protein 1)
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MVFDARLGYDPDEWEECPEPEHFLVFSGFTRYMLTFAAIAFVYYFFKLLDDKNKKESGEKEEPQTSVESVLAKAGDKLHDVKEQVQQHIPESAEELMREADQYLKEQAHSVQNNVHQFAEQAANKFPSLEVDLNLGHPIDATREKFDTVLSSVNNHLHETKNMDLSPTSRDSTQFEQIPSIAPEESAFGHDFEHVPPHLKTAAEQYYAQQHQPPPVPQHKIVQPVPISPTDQQLLHEFDIYDAPAHQRMNQISEQLGQLGQKTPAQLQQLQHAQLAHQQLQQQGVFQPIQQPSPLQIQTHPQQPYFDFSQLSPASQARYNQQQFVDISQLSPGAGALIAEQQASGAFQPVTKKLGREKRLSEQDERALQDWEKEKALLEADRLKKLLDHEVGGDSTDLDSSQKAYDHFAPASHISYESHSGAAQIQPMTPTAPKRADVPAPQVTSITNVRDSQLTDYDISDFHAHDEPHYHTVLTPQQLQQNQQQHQQPSAIDRRRTTADSDDYVKVSEPIYDYPPKGHEAPVAEPKRISPTEAAQLQELYQEYDLGLDLPGVAPIQGVAKPPVQQRTPLQIQQQVVQNVQNQPNMMARQNSVPESPRTVINVPISRKTDVPIQVQQQQNQFSYNVPIQVKDDPRNLATADLFVQDAQEYVAHQQNQQDKGSFVMEEEMLSLHEPETGSNKKKLTPKNPSFEATSRQVRTNDVFERIEHDEHDDMTYAPEIQSVEIPPDQMSETSENMIDYFDKVAAESEQQIQHLQEQQNTLKKQQIETSIPDSSLLKPVGRAPQILPAFGNRISSNSSLGSAGRSGSGVSSSDVYPYRHLRKQSSLLSVLGVTSMQEMLLAITSLDSLSEAMRKAGLETTNLIFGIDYTASNKYQGEESFGGRSLHTIHPHVTNPYQQVISILGRTLAPFAGQGRLGVYGFGDAKTGDWSVFNLKGEGGDCRSLDEVLNVYNTVTPTVALSGPTNFAPLIYQAMEICQKSRDYHILVIIADGQVTNERATRRAIVQACQHPLSIIVVGVGDGPWDMMRIFDESLPKRPWDNFHFVEFHEIVKKSTNMEDGDVKLAVQSLLEIPDQYRCICELGLLDRSIPPRGSEIRREMMHNPL
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Involved in the assembly of dense bodies and M lines during body wall muscle development. Acts by recruiting downstream of integrin-associated protein pat-6/actopaxin several dense bodies and M line components including unc-89, lim-9, scpl-1 and unc-96 to integrin-mediated attachment sites.
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H2KYU6
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NPL41_CAEEL
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Nuclear protein localization protein 4 homolog 1
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MVLEVPQTERVNDVDVFLSTQDGQIQRPKGPNCRHPVRQKCTNCLPVDPFDEEYLKEKDIKHMSFHAHVRKLLGSQGKGTTLKKPLENFRCSLKPNCDAHKPFPKGICTKCKPQVVTLNRQKFRHVDNIQIENQELVNQFLDYWRLSGHQRVGFLIGQYQPHLEVPLGIKATVAAIYEPPQHCREDGIEFLEDKNQKTIDNLLEMLGLQRVGWIFTDCWTANSAEGTVHYTRHKDSFFLSAEECITAAMLQNQHPNITEYSMDRHYGSKFVTVVASGDESMHVNFHGYQVSNQCAAMVEADILCPTLYTPELAYVRETPLSEEHYITDVQFSMKNEYGAEVMKNGRPLPVEYLLVDVPAGMPKEPHYTFHVGTSNKSKSAKFNVENRQAIGQLQGGANLIQYSSEFSKNQFLEQATNFHFLLYLVTNDQVQISDEWMKRLCDAVKAQDRGTAMEWAQECEDWHQLMALAHANGGSGNDVSDIPVIPNGDPFSGSSSGGSGGAVWNCGHCTFQNEAARQDCSMCGLPAAD
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In association with ufd-1 and ATPase cdc-48.1 and/or cdc-48.2, involved in the cytoplasmic elimination of misfolded proteins exported from the ER. This pathway, known as ERAD, prevents the activation of the unfolded protein response (UPR) caused by the accumulation of misfolded proteins in the ER. During S phase and in association with ufd-1, cdc-48.1 and/or cdc-48.2 and ubxn-3, ensures the degradation of DNA licensing factor cdt-1 after the initiation of DNA replication and thus the disassembly of the DNA replication CGM helicase complex by promoting the dissociation from chromatin of several of its components including cdc-45 and sld-5. Regulates ubxn-3 nuclear localization during S phase.
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H2KZ60
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RIG6_CAEEL
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Contactin rig-6
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MMMLIRCISIFLLFGFVNALIDEASCPIGWQIASDQCVRIVIAPANLKHSKKYCHHEGGELMDTSVTLLLEDVMDLLKNLHENGLSEPTFHVGGMGQALNRTEDGNYKIITINPSSHFPFICSLNKMARRSLLFQQKLLPVGAPQISLTGQSEIYFHPRHDADYIALPCTVQGNPKPTVAWYKNDVEVLSPSMSNVSYLLSGGNLLVPASSTLAYSSFHCTARNSLGEVRSPPILLKPSFIDPFRPHRLDVYSLATGGAKLDCDAPAHQPKSLTYSWLYGSSTDRILSQNERKFISLDGTLFFSYVTAEDEDSYACSLSVYSTQSGHYGPFFRLISSTPKLVNSTFPPKLDSTQPQIFPEDPKVGDSIYLECFAYASPLPQYKWSRVDGKPIPARSHISNYGRVLKIEKVNYGDAGKYKCVAMNAFGSAAGEVHVKLRAPPSILQGLHDRLVPTESNVSFECLLSNADSYSSVEWFKDAKPIVPLLLPAEKRKRLKIDHNVLHLKFADETDSGVYQCVASNDVGSSSSSALLTVKDSAPVFPPNAMSRKVFAAFGSTVSIPCIFEASPRFHGKWADAGGSKLPQKGRIRDEEGVISIEKVLHEDAGLFFCTAHNKLGKAHAQVQLIVVNKPSIKTNFLDEETVNMSCEVELTCENSAECPEALFEWKINDRPAKEYPSLKSKVHEKKSGHKGRHLKQKVDLEVPKSLAGSRQIGRFACSSLYGGSSEFVTKPQLPSPIALTVEQMDEDGKKKKMFRLRWRLPPQHRDTRDHSPKVEGYLVELRTRKNRKWRAAERQLVGNMEKDSITVENLLPNTEYQFRVRSVESAAIGEPSIPSDWVKTAPGAPSETIDNLKWRSLDSQTLLVEWQPIEIGQESSGDNLRYRVSWSEATVGKNATDDMKLSNQDDDFENHLDSDQPQAILKLNTTEGCRMVVLAVRPVNDQGNGSVGTDTIAFLNSHGELKKVSLHNVKPINASHVNISWTWDNTSDCDTKHAVQITCINLSGSEISATVASDRIFWMLGGLEAETAYDCDLKAIDNHGSFGPASKKFRIHTKQHPPSETPLIGKLMMKQMKDTYTTILEWSSIELQKPNRTENGCGYKIFIYISETATEAIELDMPLQRLSDRRNPSARLDGLKLMYMYTIKVAGYNPGGIGPISEPRSIRLGSPGTMDYTTGSSDVPIPSLLLLLLLLLWRL
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Probable cell adhesion protein involved in patterning of the nervous system, playing a role in ALM and PLM touch receptor axon growth and VNC axon navigation. By associating with the transmembrane protein sax-7, mediates axonal interactions to establish synaptic connections between the AVG interneuron and the two PHC sensory neurons. Also required for non-neuronal cell migration in the excretory canal, regulating excretory canal elongation and excretory cell morphogenesis. Plays a role in regulating male mating behavior.
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H2KZB2
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ANKL2_CAEEL
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Ankyrin repeat and LEM domain-containing protein 2 homolog (LEM domain-containing protein 4-like)
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MGRKSAILAVILAIIYFRSNFSKMSNTPVQETEGPVYVAYSMEDMLKSPRDLYKSVKEVAKFVNSAEGKSMSARFKKFGTPREAMDFLAYGDAPTTPKTVPPVAPTEPNSPFSGVNRIQMNEFKKYVEKGDMENFLRLVDSNPRFLVNTGGDVASIVMEGFRYNALHIAAKAGQTEIIAKILELIQNIDFLIRLYGTGADDVTLRKINILDSYLNTPDKGNSDTPLHFASKFGKIGVVRVLTENSATDRTLLNKSGKSALDCAGERYTGEDKDMVQRDIHLAIEGFYVFLHRNPTTGSTQLTVSQKPPATYSTSPTTATVTVSAQAGPFFTEREARDFAKSWQTAGKELKRTDFDKGWERVGRVLAEQSEAMWRETWHFLGSMELLDLGSEQGLGVLEAFLREKRRGNLRNSEISEISTKKSIFRRGIHARKLDFGILDGEKSAEISENLTPDGSDSADDEDDDDIFYDTFSEIPAAAEKSINDPDDTLGSLTDRFAAISIFSPLPPPPPPQWSNSPNFDYSEGEDSFATPPTTPPPTFVADDEPCKIDNDLFEVLAQISSELISKFPLTQDYVQKLGKLTAHDRSTWRPIDSPARCDSRRKI
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Involved in mitotic nuclear envelope reassembly by promoting dephosphorylation of baf-1 during mitotic exit. Coordinates the control of baf-1 dephosphorylation by inhibiting VRK1 kinase and promoting dephosphorylation of baf-1 by protein phosphatase 2A (PP2A), thereby facilitating nuclear envelope assembly. It is unclear whether it acts as a real PP2A regulatory subunit or whether it is involved in recruitment of the PP2A complex.
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H2KZH5
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TOE2_CAEEL
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Target of ERK kinase mpk-1
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MSSSRHFSIPYDEDVVHSVILENTPSPPPKPPRGILRKEAPMKPQRSALKIEPARDDDKENNSQPQARSQFKAKDTMEQMQSYFKRSISVLRKSEEHFTGAEAADILTAYIETHRNEFPRDNIGRSNAVKLLEIWLESNTIQSVESHQKKFVDSERTFYRLGGDSESLYIVNTPIASRNHDDSASVSRSESSRRSNSIKRLFSPFVRRNRSNSRGRDKDKDNLKDGSSTNLKSTWSLFSSSSEKNEKKLKKAEQQLIKEEEAEVYELSLFHLLSLIDVEFLEDVALPVQDSKNNASFLSSILGKVGLGASEERLDPHQEDHMDLLIETHPLIRDASQWFQMARCCAPLLYFEAKPVASNHKTSHNEQLYLWCRAALDAVKNRLEKMTQNGSSPLFPSEFAPLLTKIAQQLINDMDSGEKLSTAVMYIFLMVPHPIRKTIDQLVQWLQLTMRTDAVEDLRSPYYLGKKDPRRYKENVNVIIGELSSFIFPRGCMTNVQQDIFIETLVELRQKGKLGQRPAQLESSLRAKSVNGQIKWQRKERKHNSLEGDLTPVRYTVRRESIRSKTSKSKDGLNETDSALVTMINSVIDNKELSLTEKKKQLMNFKKFYPKLYNDFFPGMI
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Involved in promoting a consistent pattern of asymmetric cell division and fate assignment, perhaps by regulating apoptosis of specific cells, including in the Q neuroblast lineage. Downstream target of MAP kinase mpk-1.
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H2KZM6
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PTPR_CAEEL
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Receptor-type tyrosine-protein phosphatase (EC 3.1.3.48)
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MRINRWIWWATVILLYLRTGLAADFFRSSEENDRKSSDDLDNFNSTKIEPDKPKTAKELGVKSCESNQDCVHDGVCHRGNDGHGICMCPRSCPAITPKQCGYNYRTPSTCLLMDADYRSKYDVKEPTCYSRKCVCPPQFDDVHVTANQKPLRLNSTLLPTKCDKRDLAVVARAHPSTSVSKGIDVTLFCCINVDPEGFIDVASVFFIQNGTIMREATSHPFAPRNGLARRVHEKYSCWELEIKNAQTSDSGSYMCRVTASASDLDVTDTMQFEVKAPRQIKNLTVNPSERDAIVTWESEGGEDMAIDLRLVRRTDTRGQVVFSKDNLTSPVSIKDLRAATPYTLFVSGNNGQVPFEFTEHFTTKQKRPFPPKEEDVRVLNSGSALSCEVEWKSPAEPNGRITKYFVSVRGAMRKSDGSLTPDDLPAAVEVDKRCANWDGDENTSKHNGINPIDFANEFYSCKFGPLKPNRNYTVTVWAENSAGRSLPAVFHKNCVTNYAQPDMVETPQPLLSNNHSTFSLTFPQPPDDINGPISCYYIAIVPLPANVSLDILPKSEEIVMHSFSKVFTNNLLPSSAEEKRFFAYIAESYVQLPEETTIGDGVRVSDLKACNVQYLSRYSSEDLALRRGLKYTGFLIVRVDKEEELNRKDVRNGADPNIFRNLIDKSVSPTSRTRTASPMSRHLRQLHLSGPAYGYSAYFKPILLDTESSSSGFGIFMKIILPFLLFLAFATGVTMFFVNRKGHMLSTWCPLFTKMTSKDVVERTLLKQTFGAIPVDDLPTEYVVRHRDTDFLFAQEYESLPHFQLDTVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGECGPDVIPNGNGVEYANVPIVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEWHMYGDTDEDVRDFEDHYQRLCASNRDRAVSFNQQSSTNGSISPRVAIVSSRESMTTSNGETGLEEEFKKLERNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFDYIAAQDPVSEGTAFDFWRMIADQNVTTVVMLSDETDWSDVEKYWPIDGSGTECHFGSERNSVNVTCVSEEHHQDFIIRNLSYSMKDNESMPANQEVVQYSYTGWPSDSIVPKSANSLMNLIEMVLQRQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYISKTYR
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Possesses an intrinsic protein tyrosine phosphatase (PTPase) activity. Regulates egl-15 activity which is required for hypodermis-mediated fluid homeostasis and protein degradation in muscle. During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles. Plays a role in nicotinic acetylcholine receptor (nAChR)-mediated sensitivity to nicotine. Regulates synaptic levels of nAchR subunit lev-1 in the nerve cord. Promotes the outgrowth of the quaternary dendritic branches of the PVD sensory neurons. In parallel to the sax-7/mnr-1 pathway, also controls the extension of the PVD primary branches. Acts in the netrin/DCC pathway to mediate the formation of synapses between the AVA interneurons and the PHB sensory neurons. Also required for the formation of synapses between the AVA interneurons and the VA10 motor neurons.
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H2KZM9
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TTL11_CAEEL
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Tubulin polyglutamylase ttll-11 (EC 6.-.-.-) (Tubulin--tyrosine ligase-like protein 11)
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MGCKISTEFCSDNPVGSISTSKVHPTDLSTPSYAIKPVEFYEEPLKDDQLFYKVALAKKEYREKEKDKKEQLSSNRRVSLQVEPNKLPIPLTRSSSLSSIMENRPPSGISNSSFIRSRNTASRRFTIDTSRAKSNQYVVSLCSKKIGIIEYPDGRSDKQPCDVYWHNVVLSDMNKIVTSPQSRVNKFPGMTELAKKISLTHSISSMQKLFPDEYAFYPNSWFLPAHLADFHAFYRKAQALGKTEMWFIVKPDEGAQGTGIYLINSPNQIRNVDQRQLVQEYVADPLLMNDKLKFDFRVYGVIKSINPLSIYVAREGMARFCTEKYEKPDSSNFKNLYAHLTNYSLNKANEAYVHSNTLQDQTRGSKRLLSTVFHQLESRGVKTKRLWHDIKLILVKTTLAMLPEIMLHYEHHFYDSTGPQCFQIMGFDVMIREDGTPILLEVNAAPSLTADHIVPHPGRTLLEGGQRVRSIVDEVIKIPLVRDTLLLVLGLMEEEYQNNSLKGETKSLDDMQTIKQRRKPHLSEIFPTRYGAHSGHLLFLDKAMYIYMQFVQLRSNVNITNAGLKQFVRKCNLIDIIPVVHVDAKVSEINYYFTGEKRTNGNGLPFHAFLMFLFFIAEKKFVLENDLLSKVQRLLSFCDMSLRRYGVRSARLRRAEVDSTIGNVEIYMLPSRMARNRSGTNGRKQNFTDDNNNPNSFAHLPKINERL
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Polyglutamylase which preferentially modifies tubulin. Involved in the side-chain initiation step of the polyglutamylation reaction. By controlling tubulin glutamylation, regulates ciliary specialization and motor-based transport. Promotes the formation of A and B tubule singlets by splaying microtubule doublets in cilia. Together with ttll-4 and 5, required for male mating. [Isoform a]: Specifically promotes tubulin glutamylation in a subset of ciliated neurons including amphid, phasmid, CEP and RnA neurons. [Isoform b]: Specifically promotes tubulin glutamylation in male ciliated CEM, HOB and RnB neurons that release bioactive extracellular vesicles. Regulates the localization of TRP channel pdk-2 in male CEM, HOB and RnB neurons. Regulates the environmental release of bioactive extracellular vesicles in cilia.
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H2KZU7
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SVH2_CAEEL
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Tyrosine-protein kinase receptor svh-2 (EC 2.7.10.1) (Met/Ron-like receptor tyrosine kinase svh-2) (Suppressor of vhp-1 deletion lethality protein svh-2)
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MVLGSSQSSAKELTTQSSIFRFLVLLLCFTSATGGQINGKLLNGNGVFVSRDELQNKNVLGVITGFDLLVVATHSRFQVFENNEERRTVGHVSLDMHPRTKFLELKLFSKSEIFYCDESSCGLCTYSGVTSSCSTFMLNGDEPKIQEILSSSAVKIENLGQIMLAISFKNEEDPDNPRTMILRYNAQDTGTVIPTAYHADSSFIHNNHALTGFEREGFVYFVMTASQIFEPEVFLHDQSNNKVTVTKVIRFCATDQTADLASKISILVGCDQEFRNISSRGETAVYDHANDLINIVMFNHTSMNHLMCRFKMANIEKRFKTIWSTCQETSFSGSTAKTTRCKYPQIFDQMKVKKGCLTYSRLDDESSPTLCVRYGRGDALDNCQLHTAKSNSYRYGWLEDYNVLQGELMMRIPYPFFGIAESLITDGKSYFAAVSGEFDMSDVLRFSASESADIRPHWRTNISVVGKFSITKTKENQLLYTTVEGLQSLDISCKGLYPNCQTLRQGGWEDPLECSWCADDNAQRTITSSEVSSCKNNLKHECPPSMRWIHKYNNNSGFTAVVDGFRALKNPKLNACGTNCVVTVVDSSSIQCDTNPDEVIGDSCKQVFLSGMIGDKNYSFPFDYQQADRGTQTDVKNSQVDDKKGSSPGWKIAIAIISVMTIILIVAIIVYYMRNRFPRIKTHVRPPIGQRIENEYDMGHMAGRQAQLAINGDNYVKVFRSMRPDLKVDFKNLRVDKLDPIGQGHYGVVYKAMYSPSKSLEEKVVCKYLKEGKISEFYEEARTMSEFDHPNILKLIGVALDDSSHLPIIITEYMAKGDLKSFIENVENTIKMRDLFEFAFDIAKGMNYMHSKKFIHRDLACRNCLLDEHLRVKIADFGLCRKVDIETELYVQMHERDLPVRWFPPEISEQGFGITSDIWSFGVVIWELFTRGSTPYSNMASWILILPWLKESETNRLRKPPYCPEKLYTDVMLACWKANPAERPQFSDLVTIIPNVVKYMEGYDRSQLQAGYERVSSRFLSLSRHDPAFPIYQNEMPNTPLLANCQNDTNDSKTLAELPSDSPSTSTAIPQSTPYQLLSECSETSV
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Receptor tyrosine kinase which may phosphorylate mlk-1, a component of the mlk-1, mek-1 and kgb-1 pathway. Involved in axon regeneration after injury by promoting the generation of productive and stable growth cones.
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H2KZW3
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M3K20_CAEEL
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Mitogen-activated protein kinase kinase kinase zak-1 (Mitogen-activated protein kinase kinase kinase 20 homolog) (EC 2.7.11.25)
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MSTPTSNESTSSSSNNSDQRVLFPDIQRDDIQVGDHIGVGTFGAVFSGNWTLPDGSQRTIALKKVFVLEKEAEILSKIRHKNIIQFYGICKATGNDFFIVTEYAEKGSLYDFIHSEESQSFASSSGGNSFDVVVKWASQIASGIQYLHYDAVDTIIHRDLKSKNVVLDKNLVCKICDFGTSKDLTHSCTAPSWGGTAAWMSPEMILQSEGLTTATDVWSYGVVLWEILSKEVPYKDYSEFRIFTMITQSGITLAIPPSCPAPLKQLMSNCWKMTPKDRANMRQIQGELNRLAGNQKVMDECEKFMGLEDWKTEIEKQEKNVEKMRKDLEKRREQLEIREKALKQRMKVEQAVLDSARHPPEDVHQWSEHHTSHWVETVLGRVANDKKFLDRVNAAVFRNRITGARLLGMTQNDLEHLGVHKVGSRIELMKMIRKLADTQKALHNFPTLEQAKRIEMTLKTEKEAAGQLANDVDIVIIVGMYVRKMNATRRKFKFYADSDWIDDTDIPAKSKSKHASSLIKTVCFSVLDENTKKPINEPACSISSGMTTNPDWITVDTEDDVKIRVIVSVYYADIVTQPRNTEVIKVVTSLEESKILEERHVHLRLRRSSSSASISTPSPVIAPVYHPFGHLNNGFHHTTSSPQLRGFWHRKQTGMNRHGLTETELSSLQEQLRTPSPDKKVVDENVIIHVPKLTRRRRTTTTNSEDTEKSDTNNKTPESQARRVHVHGGKDKWNWKKGKSRPKFT
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Stress-activated component of a protein kinase signal transduction cascade that promotes programmed cell death in response to ribotoxic stress. Acts as the proximal sensor of ribotoxic stress: directly binds to the ribosome, thereby acting as a sentinel for colliding ribosomes (By similarity). Upon ribosome collisions, activates the stress-activated protein kinase signal transduction cascade, leading to programmed cell death (By similarity). Acts by catalyzing phosphorylation of MAP kinase kinases, leading to activation of the JNK and MAP kinase p38 pathways.
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