RPGF_CAEEL
ID RPGF_CAEEL Reviewed; 1470 AA.
AC G5EDB9; G5EBY1; G5EEX2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Rap guanine nucleotide exchange factor;
DE Short=RA-GEF;
DE AltName: Full=PDZ-domain-containing exchange factor;
GN Name=pxf-1; Synonyms=ra-gef; ORFNames=T14G10.2;
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 [MRNA] (ISOFORM A), AND POSSIBLE FUNCTION.
RC STRAIN=Bristol N2;
RX PubMed=10608844; DOI=10.1074/jbc.274.53.37815;
RA Liao Y., Kariya K., Hu C.-D., Shibatohge M., Goshima M., Okada T.,
RA Watari Y., Gao X., Jin T.-G., Yamawaki-Kataoka Y., Kataoka T.;
RT "RA-GEF, a novel Rap1A guanine nucleotide exchange factor containing a
RT Ras/Rap1A-associating domain, is conserved between nematode and humans.";
RL J. Biol. Chem. 274:37815-37820(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND D), FUNCTION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15525675; DOI=10.1091/mbc.e04-06-0492;
RA Berkel W.P., Verheijen M.H., Cuppen E., Asahina M., de Rooij J., Jansen G.,
RA Plasterk R.H., Bos J.L., Zwartkruis F.J.;
RT "Requirement of the Caenorhabditis elegans RapGEF pxf-1 and rap-1 for
RT epithelial integrity.";
RL Mol. Biol. Cell 16:106-116(2005).
RN [3]
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).
CC -!- FUNCTION: Acts as a guanine nucleotide exchange factor for small G
CC protein GTPases like rap-1 and rap-2. Required in the hypodermis,
CC especially in the seam cells, for proper formation of the cuticle.
CC {ECO:0000269|PubMed:15525675}.
CC -!- INTERACTION:
CC G5EDB9; Q6BEV5: R06F6.12; NbExp=2; IntAct=EBI-2918010, EBI-2002318;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a; Synonyms=PXF-1-A;
CC IsoId=G5EDB9-1; Sequence=Displayed;
CC Name=b; Synonyms=PXF-1-B;
CC IsoId=G5EDB9-2; Sequence=VSP_053269, VSP_053270;
CC Name=d; Synonyms=PXF-1-C;
CC IsoId=G5EDB9-3; Sequence=VSP_053271;
CC -!- TISSUE SPECIFICITY: Expressed in hermaphrodite-specific neurons (HSNs),
CC oviduct sheath cells and lateral seam cells.
CC {ECO:0000269|PubMed:15525675}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the comma stage in endodermal
CC precursor and hypodermal cells of the embryo. Expressed in the
CC hypodermis and gut during elongation and larval stages. Expressed in
CC neuronal precursor cells at the comma stage. Expressed in neuronal
CC cells in the head and tail, in cells of the ventral nerve cord and of
CC the pharynx at the L1 hatched larvae stage.
CC {ECO:0000269|PubMed:15525675}.
CC -!- DISRUPTION PHENOTYPE: Beginning in the L2 stage, onward, animals
CC display striking and progressive defects in morphology of the
CC epidermis. Worms show molting defect and exhibit a trail of old cuticle
CC that remains attached to the posterior part of the body. Longitudinal
CC ridges termed alae, which are cuticular structures secreted by lateral
CC hypodermal seam cells, are poorly distinct or interrupted. Sensory rays
CC in males are malformed. Developed a fairly normal gonad but have a
CC strongly reduced fertility. Show uncoordinated movement and an enlarged
CC gut lumen. Died as a 'bag of worms', or alternatively, as a result of a
CC burst vulva. {ECO:0000269|PubMed:15525675}.
CC -!- SIMILARITY: Belongs to the RAPGEF2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL09435.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF170796; AAF22963.1; -; mRNA.
DR EMBL; AF308447; AAL09433.1; -; mRNA.
DR EMBL; AF308448; AAL09434.1; -; mRNA.
DR EMBL; AF308449; AAL09435.1; ALT_INIT; mRNA.
DR EMBL; Z68880; CAA93100.2; -; Genomic_DNA.
DR EMBL; Z69664; CAA93100.2; JOINED; Genomic_DNA.
DR EMBL; Z68880; CAC42342.1; -; Genomic_DNA.
DR EMBL; Z68880; CCD31121.1; -; Genomic_DNA.
DR PIR; T23314; T23314.
DR RefSeq; NP_001023389.1; NM_001028218.4. [G5EDB9-1]
DR RefSeq; NP_001023390.1; NM_001028219.2. [G5EDB9-2]
DR RefSeq; NP_001255465.1; NM_001268536.1. [G5EDB9-3]
DR AlphaFoldDB; G5EDB9; -.
DR BioGRID; 42996; 2.
DR IntAct; G5EDB9; 5.
DR STRING; 6239.T14G10.2a.1; -.
DR EPD; G5EDB9; -.
DR PaxDb; G5EDB9; -.
DR PeptideAtlas; G5EDB9; -.
DR PRIDE; G5EDB9; -.
DR EnsemblMetazoa; T14G10.2a.1; T14G10.2a.1; WBGene00004254. [G5EDB9-1]
DR EnsemblMetazoa; T14G10.2b.1; T14G10.2b.1; WBGene00004254. [G5EDB9-2]
DR EnsemblMetazoa; T14G10.2b.2; T14G10.2b.2; WBGene00004254. [G5EDB9-2]
DR EnsemblMetazoa; T14G10.2b.3; T14G10.2b.3; WBGene00004254. [G5EDB9-2]
DR EnsemblMetazoa; T14G10.2b.4; T14G10.2b.4; WBGene00004254. [G5EDB9-2]
DR EnsemblMetazoa; T14G10.2b.5; T14G10.2b.5; WBGene00004254. [G5EDB9-2]
DR EnsemblMetazoa; T14G10.2d.1; T14G10.2d.1; WBGene00004254. [G5EDB9-3]
DR GeneID; 177894; -.
DR KEGG; cel:CELE_T14G10.2; -.
DR CTD; 177894; -.
DR WormBase; T14G10.2a; CE28080; WBGene00004254; pxf-1. [G5EDB9-1]
DR WormBase; T14G10.2b; CE28081; WBGene00004254; pxf-1. [G5EDB9-2]
DR WormBase; T14G10.2d; CE46125; WBGene00004254; pxf-1. [G5EDB9-3]
DR eggNOG; KOG3542; Eukaryota.
DR InParanoid; G5EDB9; -.
DR OMA; FMQHMSA; -.
DR OrthoDB; 31139at2759; -.
DR PhylomeDB; G5EDB9; -.
DR Reactome; R-CEL-5673001; RAF/MAP kinase cascade.
DR SignaLink; G5EDB9; -.
DR PRO; PR:G5EDB9; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004254; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; G5EDB9; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0060102; C:collagen and cuticulin-based cuticle extracellular matrix; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:WormBase.
DR GO; GO:0040002; P:collagen and cuticulin-based cuticle development; IMP:WormBase.
DR GO; GO:0008544; P:epidermis development; IMP:WormBase.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IMP:WormBase.
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; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000159; RA_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 PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50200; RA; 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 Alternative splicing; GTPase activation;
KW Guanine-nucleotide releasing factor; Reference proteome.
FT CHAIN 1..1470
FT /note="Rap guanine nucleotide exchange factor"
FT /id="PRO_0000423876"
FT DOMAIN 478..592
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 597..679
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 782..869
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 894..1124
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT REGION 130..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1422..1455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..204
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 347..463
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT VAR_SEQ 1..123
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000303|PubMed:15525675"
FT /id="VSP_053271"
FT VAR_SEQ 1309..1311
FT /note="NGR -> VLI (in isoform b)"
FT /evidence="ECO:0000303|PubMed:15525675"
FT /id="VSP_053269"
FT VAR_SEQ 1312..1470
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:15525675"
FT /id="VSP_053270"
SQ SEQUENCE 1470 AA; 163808 MW; 59404704C1346BC8 CRC64;
MDPRKPRQDP VNDARFYESL IKPPHLRTPD DIRNVYEQLR QLDTFSNLFI GPLKALCKTA
RYERHPAQYI LFRDGDVARS WYILLSGSVF IENQIYMPYG CFGKRTGQNH RRTHNCLLLQ
ESEMIVIDYP TEPQSNGMSP RTPPRGIHHS GEPVHQKTPR KSAPNMSVDS IAMPPPPVPP
RPLRLPQTAA KGPAPLPPRG LPRTYPLDFP VDIPTTSSSS SNTSYNDQHR SQVYLNGLSA
DEDTLVRVKH RREKSNSVGG QAQNGISTAR RLRGRSTASS TTTEGETASN EGADSDEDEG
SMPSQESSSG GFMDLRDSVR ECLEKEPSER NSEDLAVLLD FMQHMSAFAA LPMSIKRQLC
LKMVFAVVND AGTVVLAHNE KLDSWSVIVN GCVEVVKPSG ERVEYKLGDS FGAEPTPATQ
IHIGEMRTMV DDCEFVLVEH RDFCSIMSTI GDHIEKDRDG LTGEVVSEVE RRTVGTHCGQ
VLIKGKPDKL IHHLVDERDH NVDPHYVDDF LLTYRVFIRD PTTIFEKLML WFADSIYRDK
VARLVLLWVN NHFNDFETND EMWNLLERFE GALERDGMHS QLSLLNIACS VKAKPRQVIL
TRRKDDKMMM RLVGGQESGN SVYVAEVFPD TSAAREGVKR ADEMLEVNQQ SAKYLSAKKA
EDLLTGSLSL TLMLKNNVLG YKETIGKIEH NKPKNGTSRS GAGIPMVIPV HKTSITGKKS
STTSSKSGMM EKLMTILKSS KEDSMDFTDE AKISSADLRP SRSNPDITSI SQYYGPVRSE
CPEHVLKIYR NDQTFKYLPV YKETSAQNVV QLALQEFNMT AEGSPEWSLC ECTVTIDGVI
KQRRLPPQME NLAERIALNS RYYLKNNSRS EPLVPDELAP ELLKEAQTQL LSLNAQVVAA
QLTLQDFSVF SAIEPTEFLD NLFKLDSKYG SPKLEEFEQL FNREMWWVAT EICTERHVQK
RAKLIKKFIK VARYCRDLRN FNSMFAIMSG LDKPAVRRLH SSWERVSSKY IRMLDEIHQL
VDPSRNMSKY RQHLAEVAQE PPVVPIYPVI KKDLTFAHDG NATYSEKLIN FEKLRLIAKS
IRGVMKLSSA PYEIASMAER SGGVVMDALL HMNSFENSNV ATMRKGMSGK QNQPRKKVYE
QALMVRKVKS YLEGLHVVDN EMELDSMSYD IEPQVQTAHR GANSSSTANI RRVPSPTPSS
LSSQSAGSAD QSSRHRLLFN GTGSISSAGG GSKFGVESPQ AVQKMLSLVQ NSKVKGAPPQ
ITSPSTSARS SLQRNMPRVT GRQATSSAQG PVQLNEETST VTTYYQSDNG RRQRSGSEGR
FDNIPPSTFY LTSDGLTVSP RQSLSVVIPT HPHGHSPTSP RCRSRSPASS GCSSFSTIAS
IAATSMAAAP SAFVSNPYQH HQTVRGHVIG HRPMPIVTSG SATLPNHVSP RGLPPKSRPT
ILPGSHTNSS SRMGTIKEAT FLTSEQVSRV
