RAB25_CANLF
ID RAB25_CANLF Reviewed; 213 AA.
AC E2RQ15;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Ras-related protein Rab-25;
DE Flags: Precursor;
GN Name=RAB25;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP FUNCTION.
RX PubMed=19451275; DOI=10.1083/jcb.200809122;
RA Tzaban S., Massol R.H., Yen E., Hamman W., Frank S.R., Lapierre L.A.,
RA Hansen S.H., Goldenring J.R., Blumberg R.S., Lencer W.I.;
RT "The recycling and transcytotic pathways for IgG transport by FcRn are
RT distinct and display an inherent polarity.";
RL J. Cell Biol. 185:673-684(2009).
CC -!- FUNCTION: Involved in the regulation of cell survival. Promotes
CC invasive migration of cells in which it functions to localize and
CC maintain integrin alpha-V/beta-1 at the tips of extending pseudopodia.
CC Involved in the regulation of epithelial morphogenesis through the
CC control of CLDN4 expression and localization at tight junctions (By
CC similarity). May selectively regulate the apical recycling pathway.
CC Together with MYO5B regulates transcytosis (By similarity).
CC {ECO:0000250|UniProtKB:P46629, ECO:0000250|UniProtKB:P57735,
CC ECO:0000250|UniProtKB:Q9WTL2, ECO:0000269|PubMed:19451275}.
CC -!- SUBUNIT: Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4.
CC Interacts (via the hypervariable C-terminal region) with ITGB1 (via the
CC cytoplasmic region); the interaction is GTP-dependent. Interacts with
CC ITGAV. Associates with the integrin alpha-V/beta-1 heterodimer.
CC {ECO:0000250|UniProtKB:P57735}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection,
CC pseudopodium membrane {ECO:0000250|UniProtKB:P57735}. Cytoplasmic
CC vesicle {ECO:0000250|UniProtKB:P57735}. Note=Colocalizes with integrin
CC alpha-V/beta-1 in vesicles at the pseudopodial tips.
CC {ECO:0000250|UniProtKB:P57735}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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 RefSeq; NP_001300794.1; NM_001313865.1.
DR AlphaFoldDB; E2RQ15; -.
DR SMR; E2RQ15; -.
DR STRING; 9615.ENSCAFP00000024805; -.
DR PaxDb; E2RQ15; -.
DR PRIDE; E2RQ15; -.
DR Ensembl; ENSCAFT00030000715; ENSCAFP00030000619; ENSCAFG00030000419.
DR Ensembl; ENSCAFT00040039278; ENSCAFP00040034265; ENSCAFG00040021172.
DR GeneID; 490418; -.
DR KEGG; cfa:490418; -.
DR CTD; 57111; -.
DR eggNOG; KOG0087; Eukaryota.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; E2RQ15; -.
DR OMA; KRACCIN; -.
DR OrthoDB; 1133775at2759; -.
DR TreeFam; TF300099; -.
DR Reactome; R-CFA-8873719; RAB geranylgeranylation.
DR Proteomes; UP000002254; Unplaced.
DR Bgee; ENSCAFG00000016866; Expressed in nose and 37 other tissues.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0031260; C:pseudopodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0031489; F:myosin V binding; IEA:Ensembl.
DR GO; GO:0003382; P:epithelial cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0031268; P:pseudopodium organization; IEA:Ensembl.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell projection; Cytoplasmic vesicle; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..210
FT /note="Ras-related protein Rab-25"
FT /id="PRO_0000409023"
FT PROPEP 211..213
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409024"
FT MOTIF 41..49
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 19..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 155..157
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 210
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 209
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 210
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 213 AA; 23620 MW; 28ECF25D1407EDAC CRC64;
MGNRTEEDYN FVFKVVLIGE SGVGKTNLLS RFTRNEFSHD SRTTIGVEFS TRTVMLGTAA
IKAQIWDTAG LERYRAITSA YYRGAVGALL VFDLTKHQTY AVVERWLKEL YDHAEATIVV
MLVGNKSDLH QAREVPTEEA RMFAENNGLL FLETSALDST NVELAFETVL KEIFTKVSKQ
RQNSTRTNAI ALGSAQAGQE PGAGQKRACC ISL
