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RPGF1_CAEEL
ID   RPGF1_CAEEL             Reviewed;        1038 AA.
AC   P34578;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Rap guanine nucleotide exchange factor 1;
DE   AltName: Full=Exchange protein activated by cyclic AMP 1;
GN   Name=epac-1; ORFNames=T20G5.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, INTERACTION WITH DRN-1, AND TISSUE SPECIFICITY.
RX   PubMed=22897658; DOI=10.1111/j.1365-2443.2012.01627.x;
RA   Tada M., Gengyo-Ando K., Kobayashi T., Fukuyama M., Mitani S., Kontani K.,
RA   Katada T.;
RT   "Neuronally expressed Ras-family GTPase Di-Ras modulates synaptic activity
RT   in Caenorhabditis elegans.";
RL   Genes Cells 17:778-789(2012).
CC   -!- FUNCTION: Guanine nucleotide-releasing protein (By similarity).
CC       Together with GTPase drn-1, may regulate acetylcholine release at the
CC       neuromuscular junctions probably downstream of G-protein gsa-1 and
CC       adenylate cyclase acy-1 (PubMed:22897658).
CC       {ECO:0000250|UniProtKB:Q13905, ECO:0000269|PubMed:22897658}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with drn-1.
CC       {ECO:0000269|PubMed:22897658}.
CC   -!- TISSUE SPECIFICITY: Expressed specifically in neurons including the
CC       nerve ring, ventral and dorsal nerve cord motor neurons and tail
CC       ganglia. {ECO:0000269|PubMed:22897658}.
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DR   EMBL; Z30423; CAA83013.3; -; Genomic_DNA.
DR   PIR; S42368; S42368.
DR   RefSeq; NP_499256.2; NM_066855.3.
DR   AlphaFoldDB; P34578; -.
DR   SMR; P34578; -.
DR   BioGRID; 41626; 1.
DR   STRING; 6239.T20G5.5; -.
DR   PaxDb; P34578; -.
DR   EnsemblMetazoa; T20G5.5.1; T20G5.5.1; WBGene00004255.
DR   GeneID; 176432; -.
DR   KEGG; cel:CELE_T20G5.5; -.
DR   CTD; 176432; -.
DR   WormBase; T20G5.5; CE43630; WBGene00004255; epac-1.
DR   eggNOG; KOG2378; Eukaryota.
DR   GeneTree; ENSGT00940000172554; -.
DR   HOGENOM; CLU_006829_1_0_1; -.
DR   InParanoid; P34578; -.
DR   OMA; CMHEHEL; -.
DR   OrthoDB; 143470at2759; -.
DR   PhylomeDB; P34578; -.
DR   Reactome; R-CEL-354192; Integrin signaling.
DR   Reactome; R-CEL-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR   Reactome; R-CEL-392517; Rap1 signalling.
DR   PRO; PR:P34578; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00004255; Expressed in pharyngeal muscle cell (C elegans) and 2 other tissues.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd06224; REM; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.840.10; -; 1.
DR   Gene3D; 2.60.120.10; -; 2.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR008937; Ras-like_GEF.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR   InterPro; IPR023578; Ras_GEF_dom_sf.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   InterPro; IPR036964; RASGEF_cat_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR23113; PTHR23113; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF48366; SSF48366; 1.
DR   SUPFAM; SSF51206; SSF51206; 2.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS00720; RASGEF; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   1: Evidence at protein level;
KW   Guanine-nucleotide releasing factor; Reference proteome; Repeat.
FT   CHAIN           1..1038
FT                   /note="Rap guanine nucleotide exchange factor 1"
FT                   /id="PRO_0000068900"
FT   DOMAIN          234..316
FT                   /note="DEP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT   DOMAIN          516..654
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT   DOMAIN          795..1028
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT   BINDING         10..140
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         375..492
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1038 AA;  118871 MW;  E8356D9D44E05819 CRC64;
     MERIVSRVRR LSPLHTFSDA LLISLLSESD FQPDSIQQGV VLFEKDEPTE YWYLLLSGEV
     QLYSKTYTGD FNHLKTLRCG ALFGDLSTLT HSCSCLVTRP AQLIRIAQNH FLSVYNKHGD
     HLQPFIIIMH DILTDETPSD PIHPHSSGLF NGQRSMDLIS TEINPSEIVS VSTNGMLSKM
     ILPSIPNQRE KPMNRVVVNQ QKNEERNFIE FHNPTGIEKQ IRDSGGILHR KMLTDNHQVI
     RDITTEHTRV QNCMIGAEMI DWLLTLFVST STTCSSLSRI QMSAIWQVLL NNGLISHIDG
     EHQFLDKTNS YYRWVQQFRS RNKVAPSIEE VSKSITLLSS VAPETLFLMI VSKPGFERSP
     EELEVVYEEL TFIKALSHLS TMVKRQLSNF VKVEQYVHAG SVVFRQGEIG VYWYIVLKGA
     VEVNVNGKIV CLLREGDDFG KLALVNDLPR AATIVTYEDD SMFLVVDKHH FNQILHQVEA
     NTVRLKDYGE DVLVLEKVDI PRGAALENSN SCNFNCGYSV MAGKAEKILE YVLETRIDAL
     GDDISELDVF VEDFILTHDA FMPDNTVCNF LKSYYFRTPY RATRDSITDS CTEEVRCKRR
     VVQFVYVWCS LLRVNFFLNP VTNSFVEELF CHVIDDRKRL GGMEDILTRI GSIRSTRENM
     QLVLARHPAI VLDCGVLSAH TPCPVLPSDV CNQIIYLADT TCFVLPIRVD KTAEEICELS
     RRRMSFSAEP LNLVEVKSNG EKLIFSPNDR AIPTVLSLNS KLYVVNREEI PLLVPMEDQN
     GPTPSSHSSI LHLIDSQELA HQLFLFHLQL LRSTDSNELL YQVIGRESFP LSMPFNLDLL
     VRRFNEVQHW STTEILLATE ENRMEILKKF ISIATIAREY RDLLTVFAIT LGLSHTSISR
     LTLTWSKLPP ASLKTFSELE NLLDPTRNHR MYRLLVSKMS SPYIPFVPLI LKDLMFIHQG
     NKSFYNGLVN FEKMHMFAKI FRSFRQCKSQ MDNGAEHEFI EPQSLIRNLR VIDNQKKLMQ
     LSYEIEPKSA PKRNVIFH
 
 
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