LinkDB: D3YT91_CAEEL D3YT92_CAEEL O45611_CAEEL
Original site: D3YT91_CAEEL D3YT92_CAEEL O45611_CAEEL
ID D3YT91_CAEEL Unreviewed; 533 AA. AC D3YT91; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 24-JAN-2024, entry version 91. DE SubName: Full=Rho-GAP domain-containing protein {ECO:0000313|EMBL:CBK19454.1}; GN Name=rga-5 {ECO:0000313|EMBL:CBK19454.1, GN ECO:0000313|WormBase:H08M01.2c}; GN ORFNames=CELE_H08M01.2 {ECO:0000313|EMBL:CBK19454.1}, H08M01.2 GN {ECO:0000313|WormBase:H08M01.2c}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CBK19454.1, ECO:0000313|Proteomes:UP000001940}; RN [1] {ECO:0000313|EMBL:CBK19454.1, ECO:0000313|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CBK19454.1, RC ECO:0000313|Proteomes:UP000001940}; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RA Sulson J.E., Waterston R.; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX284604; CBK19454.1; -; Genomic_DNA. DR RefSeq; NP_001255759.1; NM_001268830.1. DR AlphaFoldDB; D3YT91; -. DR SMR; D3YT91; -. DR EnsemblMetazoa; H08M01.2c.1; H08M01.2c.1; WBGene00010374. DR GeneID; 178348; -. DR AGR; WB:WBGene00010374; -. DR WormBase; H08M01.2c; CE44621; WBGene00010374; rga-5. DR HOGENOM; CLU_004268_0_0_1; -. DR OrthoDB; 2879256at2759; -. DR Proteomes; UP000001940; Chromosome IV. DR Bgee; WBGene00010374; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues. DR ExpressionAtlas; D3YT91; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central. DR GO; GO:0050770; P:regulation of axonogenesis; IBA:GO_Central. DR GO; GO:0008361; P:regulation of cell size; IBA:GO_Central. DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central. DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP_dom. DR PANTHER; PTHR46005; RHO GTPASE-ACTIVATING PROTEIN 190; 1. DR PANTHER; PTHR46005:SF4; RHO GTPASE-ACTIVATING PROTEIN 190; 1. DR Pfam; PF00620; RhoGAP; 1. DR SMART; SM00324; RhoGAP; 1. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1. DR PROSITE; PS50238; RHOGAP; 1. PE 4: Predicted; KW Reference proteome {ECO:0000313|Proteomes:UP000001940}. FT DOMAIN 340..529 FT /note="Rho-GAP" FT /evidence="ECO:0000259|PROSITE:PS50238" FT REGION 42..65 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 116..171 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 236..258 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 236..251 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 533 AA; 59191 MW; 40AB90838742AA26 CRC64; MMEFLHDICD GQVQPITSNA NSEIDSIEND RPSILSSSGI QLLAKPDSSN RSRRPKPVVN SNLRNRVTRT DPLIMSHFYS QPIEIQPAPL ATPEAVDFSP AYSLVNDAVH TVIQVNGSTP LKSPPTFHSY ESSTPDSRST TSTVSGSSPA PRAVSADVTR RSRTSNVSLS TDSINRLHRT SNLFQLRPEA ALTAEQKRKS LSIESLTKVP EKEKGNRFVR KVATSFRLRK SLLDTTCDGE SDKKENKKKT STTTSPEQIS SFLEKMATRS LPQSPRTDRK AKLYSSLNST TEKVSNVLSW LPSKTSKKLM KNKSATHDLS TSLINYPAST STQGVIAANE TLETLCSKSP SQIPIYLEKC IQFIEQNGGF EQEGLYRVPG NQTHLAEVEK RFLKYGEFDV SSFDTPVHVA ATALKSFFSC LPESLIPTAY HLRWKQIMMV SDDIKKIDGI RDALAILPVS NQKVLQYLVT HLTKVSCSPK TVMNSNNLSK VWTPTLFRPV FASYEELSSG IIAFQLALEM LIFNSHSLFN QSF //
ID D3YT92_CAEEL Unreviewed; 224 AA. AC D3YT92; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 24-JAN-2024, entry version 87. DE SubName: Full=Rho-GAP domain-containing protein {ECO:0000313|EMBL:CBK19455.1}; GN Name=rga-5 {ECO:0000313|EMBL:CBK19455.1, GN ECO:0000313|WormBase:H08M01.2d}; GN ORFNames=CELE_H08M01.2 {ECO:0000313|EMBL:CBK19455.1}, H08M01.2 GN {ECO:0000313|WormBase:H08M01.2d}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CBK19455.1, ECO:0000313|Proteomes:UP000001940}; RN [1] {ECO:0000313|EMBL:CBK19455.1, ECO:0000313|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CBK19455.1, RC ECO:0000313|Proteomes:UP000001940}; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RA Sulson J.E., Waterston R.; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX284604; CBK19455.1; -; Genomic_DNA. DR RefSeq; NP_001255760.1; NM_001268831.1. DR AlphaFoldDB; D3YT92; -. DR SMR; D3YT92; -. DR EnsemblMetazoa; H08M01.2d.1; H08M01.2d.1; WBGene00010374. DR GeneID; 178348; -. DR AGR; WB:WBGene00010374; -. DR WormBase; H08M01.2d; CE44576; WBGene00010374; rga-5. DR HOGENOM; CLU_004268_0_0_1; -. DR OrthoDB; 2879256at2759; -. DR Proteomes; UP000001940; Chromosome IV. DR Bgee; WBGene00010374; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues. DR ExpressionAtlas; D3YT92; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central. DR GO; GO:0050770; P:regulation of axonogenesis; IBA:GO_Central. DR GO; GO:0008361; P:regulation of cell size; IBA:GO_Central. DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central. DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP_dom. DR PANTHER; PTHR46005; RHO GTPASE-ACTIVATING PROTEIN 190; 1. DR PANTHER; PTHR46005:SF4; RHO GTPASE-ACTIVATING PROTEIN 190; 1. DR Pfam; PF00620; RhoGAP; 1. DR SMART; SM00324; RhoGAP; 1. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1. DR PROSITE; PS50238; RHOGAP; 1. PE 4: Predicted; KW Reference proteome {ECO:0000313|Proteomes:UP000001940}. FT DOMAIN 31..220 FT /note="Rho-GAP" FT /evidence="ECO:0000259|PROSITE:PS50238" SQ SEQUENCE 224 AA; 25076 MW; E23A216A999A46F4 CRC64; MKNKSATHDL STSLINYPAS TSTQGVIAAN ETLETLCSKS PSQIPIYLEK CIQFIEQNGG FEQEGLYRVP GNQTHLAEVE KRFLKYGEFD VSSFDTPVHV AATALKSFFS CLPESLIPTA YHLRWKQIMM VSDDIKKIDG IRDALAILPV SNQKVLQYLV THLTKVSCSP KTVMNSNNLS KVWTPTLFRP VFASYEELSS GIIAFQLALE MLIFNSHSLF NQSF //
ID O45611_CAEEL Unreviewed; 1341 AA. AC O45611; DT 01-JUN-1998, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 3. DT 27-MAR-2024, entry version 161. DE SubName: Full=Rho-GAP domain-containing protein {ECO:0000313|EMBL:CAB07634.3}; GN Name=rga-5 {ECO:0000313|EMBL:CAB07634.3, GN ECO:0000313|WormBase:H08M01.2b}; GN ORFNames=CELE_H08M01.2 {ECO:0000313|EMBL:CAB07634.3}, H08M01.2 GN {ECO:0000313|WormBase:H08M01.2b}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAB07634.3, ECO:0000313|Proteomes:UP000001940}; RN [1] {ECO:0000313|EMBL:CAB07634.3, ECO:0000313|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB07634.3, RC ECO:0000313|Proteomes:UP000001940}; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RA Sulson J.E., Waterston R.; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX284604; CAB07634.3; -; Genomic_DNA. DR PIR; T23061; T23061. DR RefSeq; NP_001023257.1; NM_001028086.3. DR AlphaFoldDB; O45611; -. DR SMR; O45611; -. DR STRING; 6239.H08M01.2b.1; -. DR EPD; O45611; -. DR PaxDb; 6239-H08M01-2b; -. DR PeptideAtlas; O45611; -. DR EnsemblMetazoa; H08M01.2b.1; H08M01.2b.1; WBGene00010374. DR GeneID; 178348; -. DR KEGG; cel:CELE_H08M01.2; -. DR UCSC; H08M01.2a; c. elegans. DR AGR; WB:WBGene00010374; -. DR WormBase; H08M01.2b; CE36176; WBGene00010374; rga-5. DR eggNOG; KOG4271; Eukaryota. DR GeneTree; ENSGT00940000154610; -. DR HOGENOM; CLU_004268_0_0_1; -. DR InParanoid; O45611; -. DR OMA; GFSECFE; -. DR OrthoDB; 2879256at2759; -. DR PhylomeDB; O45611; -. DR Reactome; R-CEL-416550; Sema4D mediated inhibition of cell attachment and migration. DR Reactome; R-CEL-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases. DR Reactome; R-CEL-8980692; RHOA GTPase cycle. DR Reactome; R-CEL-9013148; CDC42 GTPase cycle. DR Reactome; R-CEL-9013149; RAC1 GTPase cycle. DR Reactome; R-CEL-9013405; RHOD GTPase cycle. DR Reactome; R-CEL-9013406; RHOQ GTPase cycle. DR Reactome; R-CEL-9013409; RHOJ GTPase cycle. DR Reactome; R-CEL-9013423; RAC3 GTPase cycle. DR Reactome; R-CEL-9035034; RHOF GTPase cycle. DR Proteomes; UP000001940; Chromosome IV. DR Bgee; WBGene00010374; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues. DR ExpressionAtlas; O45611; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central. DR GO; GO:0050770; P:regulation of axonogenesis; IBA:GO_Central. DR GO; GO:0008361; P:regulation of cell size; IBA:GO_Central. DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central. DR CDD; cd00882; Ras_like_GTPase; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP_dom. DR InterPro; IPR045786; RhoGAP_pG1_pG2. DR InterPro; IPR039006; RhoGAP_pG2. DR PANTHER; PTHR46005; RHO GTPASE-ACTIVATING PROTEIN 190; 1. DR PANTHER; PTHR46005:SF4; RHO GTPASE-ACTIVATING PROTEIN 190; 1. DR Pfam; PF00620; RhoGAP; 1. DR Pfam; PF19518; RhoGAP_pG1_pG2; 1. DR SMART; SM00324; RhoGAP; 1. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51853; PG2; 1. DR PROSITE; PS50238; RHOGAP; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|PeptideAtlas:O45611}; KW Reference proteome {ECO:0000313|Proteomes:UP000001940}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}. FT DOMAIN 640..822 FT /note="PG2 pseudoGTPase" FT /evidence="ECO:0000259|PROSITE:PS51853" FT DOMAIN 1148..1337 FT /note="Rho-GAP" FT /evidence="ECO:0000259|PROSITE:PS50238" FT REGION 850..873 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 924..980 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1044..1066 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1044..1059 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1341 AA; 151064 MW; 0978DDB7A84A9FB3 CRC64; MSSTSQTYSN STKIKEINVI VVGVSGSEAV KGPSGVGKSL LCNRFVRPAA DEFHREHSSV LSQIDFCGSP VINKDHWLYW GSRVLSNPES SASNILIRVA EQTEFLDDET FETIAGCSKS ENYCQRCCQT SLQSRDKLMY IQKEQLGLES EFPQQLLPNG KFNVDGFILA CDISKPTSAH LHSSHVLNIA KAISKTKKPV IIAFTKCDEA SEECKKNYLN LFYSTKELKH IMSHVPPVET SSVKNVNVEY LFGTLANLCL KSQKIVKKPL AYHEASLFVE QRNLHVKCCF STLLSQAVPL CTYPKKCLSW NQVLADIDRH PDLMNFVTVF GSRVAFEMYE RYVSEAKELW AINRLRTLVP RLFEIFQVFL DVVDLAEMEW SQARDFMRCH PLFHVLFESN EYNLEMWSPP SSFNKDEKSR LPSEILLLPE AAKVFEQFRL STLNLRLKHQ LGQEFEYLLN EIPQILPGCS METAFPLFQN FNVIKKLTPD IVTTVYDRFQ KKLMENARKQ LEECILEVSP GIQLQNLKIK SWKTPGLSHF DMSMDFNQKL ETVKNFLEVD DRYEWMRIMA GERDQIIVNH LPFIFDVSPV NCPSTDMCID LVGTSILNDF SEQNSTFCGS SGFSECFEAT RKNSGKNMPR IQISAMCGDQ LSIDSLAGAL FHNTLIRPSN YNFSNDGATF IEVLDENTQI WNNIEINMCS YHSWFHKNDS NPSESIDLND GYLFVYNSQR ASSFNYARCA IEKLAETNSV NFDCILLLAV VKGGGSDSMK LNLENLTEGA ELCKSIGARF SAIDFRKRKT KSNGINHQMM EFLHDICDGQ VQPITSNANS EIDSIENDRP SILSSSGIQL LAKPDSSNRS RRPKPVVNSN LRNRVTRTDP LIMSHFYSQP IEIQPAPLAT PEAVDFSPAY SLVNDAVHTV IQVNGSTPLK SPPTFHSYES STPDSRSTTS TVSGSSPAPR AVSADVTRRS RTSNVSLSTD SINRLHRTSN LFQLRPEAAL TAEQKRKSLS IESLTKVPEK EKGNRFVRKV ATSFRLRKSL LDTTCDGESD KKENKKKTST TTSPEQISSF LEKMATRSLP QSPRTDRKAK LYSSLNSTTE KVSNVLSWLP SKTSKKLMKN KSATHDLSTS LINYPASTST QGVIAANETL ETLCSKSPSQ IPIYLEKCIQ FIEQNGGFEQ EGLYRVPGNQ THLAEVEKRF LKYGEFDVSS FDTPVHVAAT ALKSFFSCLP ESLIPTAYHL RWKQIMMVSD DIKKIDGIRD ALAILPVSNQ KVLQYLVTHL TKVSCSPKTV MNSNNLSKVW TPTLFRPVFA SYEELSSGII AFQLALEMLI FNSHSLFNQS F //