RAB25_RABIT
ID RAB25_RABIT Reviewed; 213 AA.
AC P46629;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Ras-related protein Rab-25;
DE Flags: Precursor;
GN Name=RAB25;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Gastric fundic mucosa;
RX PubMed=8360141; DOI=10.1016/s0021-9258(17)46639-7;
RA Goldenring J.R., Shen R.K., Vaughan H.D., Modlin I.M.;
RT "Identification of a small GTP-binding protein, Rab25, expressed in the
RT gastrointestinal mucosa, kidney, and lung.";
RL J. Biol. Chem. 268:18419-18422(1993).
RN [2]
RP FUNCTION.
RX PubMed=9880326; DOI=10.1091/mbc.10.1.47;
RA Casanova J.E., Wang X., Kumar R., Bhartur S.G., Navarre J., Woodrum J.E.,
RA Altschuler Y., Ray G.S., Goldenring J.R.;
RT "Association of Rab25 and Rab11a with the apical recycling system of
RT polarized Madin-Darby canine kidney cells.";
RL Mol. Biol. Cell 10:47-61(1999).
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 (PubMed:9880326). Together with MYO5B regulates transcytosis (By
CC similarity). {ECO:0000250|UniProtKB:E2RQ15,
CC ECO:0000250|UniProtKB:P57735, ECO:0000250|UniProtKB:Q9WTL2,
CC ECO:0000269|PubMed:9880326}.
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 -!- TISSUE SPECIFICITY: Expressed in the gastrointestinal mucosa, (highest
CC expression seen in the ileum and colon), kidney, and lung. A very minor
CC and variable level of expression is seen in the splenic tissue.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; L03303; AAA31261.1; -; mRNA.
DR PIR; A48500; A48500.
DR AlphaFoldDB; P46629; -.
DR SMR; P46629; -.
DR STRING; 9986.ENSOCUP00000004890; -.
DR eggNOG; KOG0087; Eukaryota.
DR InParanoid; P46629; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0031143; C:pseudopodium; ISS:UniProtKB.
DR GO; GO:0031260; C:pseudopodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003382; P:epithelial cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0031268; P:pseudopodium organization; ISS:UniProtKB.
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 2: Evidence at transcript level;
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_0000121217"
FT PROPEP 211..213
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370823"
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; 23428 MW; B7BEC400AB32ECC2 CRC64;
MGNGKEEDYN FVFKVVLIGE SGVGKTNLLS RFTRNEFSHD SRTTIGVEFS TRTVLLGTAA
VKAQIWDTAG LERYRAITSA YYRGAVGALL VFDLTKHQTY AVVERWLKEL YDHAEATIVV
MLVGNKSDLS QAREVPTEEA RMFAENNGLL FLETSALDST NVELAFETVL KEIFAKVSKQ
IQNSPRSNAI ALGSAQAGQE PGPGQKRACC INL
