RPGF5_MOUSE
ID RPGF5_MOUSE Reviewed; 814 AA.
AC Q8C0Q9; Q8BJJ9; Q8C0R5;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Rap guanine nucleotide exchange factor 5;
DE AltName: Full=Guanine nucleotide exchange factor for Rap1;
DE AltName: Full=M-Ras-regulated Rap GEF;
DE Short=MR-GEF;
GN Name=Rapgef5; Synonyms=Gfr, Kiaa0277, Mrgef;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for RAP1A, RAP2A and
CC MRAS/M-Ras-GTP. Its association with MRAS inhibits Rap1 activation (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8C0Q9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C0Q9-2; Sequence=VSP_007617, VSP_007618;
CC Name=3;
CC IsoId=Q8C0Q9-3; Sequence=VSP_007619, VSP_007620;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65516.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK030016; BAC26736.1; -; mRNA.
DR EMBL; AK029995; BAC26723.1; -; mRNA.
DR EMBL; AK083591; BAC38963.1; -; mRNA.
DR EMBL; AK122234; BAC65516.1; ALT_INIT; mRNA.
DR EMBL; BC046627; AAH46627.1; -; mRNA.
DR CCDS; CCDS36577.1; -. [Q8C0Q9-1]
DR RefSeq; NP_787126.3; NM_175930.5. [Q8C0Q9-1]
DR AlphaFoldDB; Q8C0Q9; -.
DR SMR; Q8C0Q9; -.
DR BioGRID; 229981; 22.
DR STRING; 10090.ENSMUSP00000105313; -.
DR iPTMnet; Q8C0Q9; -.
DR PhosphoSitePlus; Q8C0Q9; -.
DR EPD; Q8C0Q9; -.
DR MaxQB; Q8C0Q9; -.
DR PaxDb; Q8C0Q9; -.
DR PeptideAtlas; Q8C0Q9; -.
DR PRIDE; Q8C0Q9; -.
DR ProteomicsDB; 300478; -. [Q8C0Q9-1]
DR ProteomicsDB; 300479; -. [Q8C0Q9-2]
DR ProteomicsDB; 300480; -. [Q8C0Q9-3]
DR Antibodypedia; 25491; 245 antibodies from 29 providers.
DR DNASU; 217944; -.
DR Ensembl; ENSMUST00000109691; ENSMUSP00000105313; ENSMUSG00000041992. [Q8C0Q9-1]
DR Ensembl; ENSMUST00000222105; ENSMUSP00000152875; ENSMUSG00000041992. [Q8C0Q9-2]
DR Ensembl; ENSMUST00000222185; ENSMUSP00000152339; ENSMUSG00000041992. [Q8C0Q9-3]
DR GeneID; 217944; -.
DR KEGG; mmu:217944; -.
DR UCSC; uc007pib.2; mouse. [Q8C0Q9-1]
DR CTD; 9771; -.
DR MGI; MGI:2444365; Rapgef5.
DR VEuPathDB; HostDB:ENSMUSG00000041992; -.
DR eggNOG; KOG2378; Eukaryota.
DR GeneTree; ENSGT00940000155137; -.
DR HOGENOM; CLU_006829_1_0_1; -.
DR InParanoid; Q8C0Q9; -.
DR OMA; YQLHRRH; -.
DR OrthoDB; 143470at2759; -.
DR PhylomeDB; Q8C0Q9; -.
DR TreeFam; TF313184; -.
DR BioGRID-ORCS; 217944; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Rapgef5; mouse.
DR PRO; PR:Q8C0Q9; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8C0Q9; protein.
DR Bgee; ENSMUSG00000041992; Expressed in superior cervical ganglion and 283 other tissues.
DR ExpressionAtlas; Q8C0Q9; baseline and differential.
DR Genevisible; Q8C0Q9; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
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; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.840.10; -; 1.
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; 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; PF00610; DEP; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
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; SSF54236; SSF54236; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Guanine-nucleotide releasing factor; Nucleus;
KW Reference proteome.
FT CHAIN 1..814
FT /note="Rap guanine nucleotide exchange factor 5"
FT /id="PRO_0000068874"
FT DOMAIN 43..118
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 301..434
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 578..813
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT VAR_SEQ 1..234
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007619"
FT VAR_SEQ 1..202
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_007617"
FT VAR_SEQ 203..220
FT /note="NADKHVTVTEANNGPDPQ -> MSWDCGFKYLFAFSPTLK (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_007618"
FT VAR_SEQ 235..301
FT /note="RIELVHKLARENCQFLQTEKKESEKLEQQDDEVTMVQVKEQGQSVLVLKKVA
FT SCGPAPTSGSAENDA -> MGSSRLRVFDPPLERKDSAALSERQLPLPTFDVPYFKYID
FT EEDEDDEWSSRSQSSTEDDSVDSLLSD (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007620"
FT CONFLICT 410
FT /note="R -> W (in Ref. 1; BAC26736)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="E -> K (in Ref. 2; AAH46627)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="R -> L (in Ref. 1; BAC26723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 814 AA; 93725 MW; 2E30E9956D25F0E2 CRC64;
MTTGDCQTLS RRISNPYLEH SPSQIYGENS SCAGRALRNI IILQAADLVK DRVNLKGFYR
RSCVGSELVD WLLEHCPFVQ CRSMAIGVWQ LLLDMGIMSS VDQHLYFQDN YVFYQFSSDE
CSYLYCEFER EEEWQKGVKL LLELVHLIPA RAGICDLSHQ KTEDSEESSD EILARLTSAV
QRELAAVIAL KARKSAIEQD DENADKHVTV TEANNGPDPQ AGVMCKLQER DDIGRIELVH
KLARENCQFL QTEKKESEKL EQQDDEVTMV QVKEQGQSVL VLKKVASCGP APTSGSAEND
ARYVVVSGTP EKILEHLLND LHLAEVQHKE TETLLDDFLL TYTVFMTTDD LCQALLRHYS
AKKYQGEEEN SDVPCRKRKV LHLVSQWISL YKDWLHEDEH SKMFLKTIYR NVLDDVYEYP
ILEKELKEFQ KILGVYRRHT VDEYSPQKKN KALFHQFSLK ENWLQHRGTV AETEEIFCHV
YITEHSYISV KAKVSSTAQE ILKVVAEKLQ RAEEDLALVA ITFSGEKHEF QPNDLAISKS
LEASGRIYVY RKDLADTLNP LAENEESQQR SMRILGMNTW DLALELMSFD WSLFNSIHEQ
ELIYFTFSRQ GNGENTVNLS LLLQRCNEVQ LWVATEILLC SQLGKRVQLV KKFIKIAAHC
KAQQNLNSFF AIVMGLNTAS VSRLSQTWEK IPGKFKKLFS ELESLTDPSL NHKAYRDAFK
KMKPPKIPFM PLLLKDVTFI HEGNKTFLDN LVNFEKLHMI ADTVRTLRHC RTNQFGSDVS
PKEQQELKSY VNHLYVIDSQ QALFELSHRL EPRA
