RGF1B_PONAB
ID RGF1B_PONAB Reviewed; 472 AA.
AC Q5RC04; Q5NVD6;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Ras-GEF domain-containing family member 1B;
GN Name=RASGEF1B;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) with specificity for
CC RAP2A, it doesn't seems to activate other Ras family proteins (in
CC vitro). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CCDC124 during cytokinesis. Interacts with Ras
CC family proteins (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250}. Late endosome
CC {ECO:0000250}. Midbody {ECO:0000250}. Note=Localizes to midbody at
CC telophase (By similarity). Localizes to midbody at telophase (By
CC similarity). May shuttle between early and late endosomes. Does not
CC colocalize with lysosomal markers (By similarity). {ECO:0000250}.
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DR EMBL; CR858478; CAH90706.1; -; mRNA.
DR EMBL; CR926101; CAI29727.1; -; mRNA.
DR RefSeq; NP_001127119.1; NM_001133647.1.
DR RefSeq; XP_009238410.1; XM_009240135.1.
DR AlphaFoldDB; Q5RC04; -.
DR SMR; Q5RC04; -.
DR STRING; 9601.ENSPPYP00000016618; -.
DR GeneID; 100174165; -.
DR KEGG; pon:100174165; -.
DR CTD; 153020; -.
DR eggNOG; KOG3417; Eukaryota.
DR eggNOG; KOG3541; Eukaryota.
DR HOGENOM; CLU_022907_3_0_1; -.
DR InParanoid; Q5RC04; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
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 PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF48366; SSF48366; 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 Endosome; Guanine-nucleotide releasing factor; Reference proteome.
FT CHAIN 1..472
FT /note="Ras-GEF domain-containing family member 1B"
FT /id="PRO_0000297640"
FT DOMAIN 34..164
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 204..452
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT CONFLICT 347
FT /note="Y -> C (in Ref. 1; CAI29727)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="S -> P (in Ref. 1; CAH90706)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="G -> S (in Ref. 1; CAH90706)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 55217 MW; EFF6AFF61E8CAEC7 CRC64;
MPQTPPFSAM FDSSGYNRNL YQSAEDSCGG LYYHDNNLLS GSLEALIQHL VPNVDYYPDR
TYIFTFLLSS RLFMHPYELM AKVCHLCVEH QRLSDPDSDK NQMRKIAPKV LQLLTEWTET
FPYDFRDERM MRNLKDLAHR IASGEETYRK NVQQMMQCLI RKLAALSQYE EVLAKISSTS
TDRLTVLKTK PQSIQRDIIT VCNDPYTLAQ QLTHIELERL NYIGPEEFVQ AFVQKDPLDN
DKSCYSERKK TRNLEAYVEW FNRLSYLVAT EICMPVKKKH RARMIEYFID VARECFNIGN
FNSLMAIISG MNMSPVSRLK KTWAKVKTAK FDILEHQMDP SSNFYNYRTA LRGAAQRSLT
AHSSREKIVI PFFSLLIKDI YFLNEGCANR LPNGHVNFEK FWELAKQVSE FMTWKQVECP
FERDRKILQY LLTVPVFSED ALYLASYESE GPENHIEKDR WKSLRSSLLG RV