RAB25_MOUSE
ID RAB25_MOUSE Reviewed; 213 AA.
AC Q9WTL2; Q9D1P3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Ras-related protein Rab-25;
DE Flags: Precursor;
GN Name=Rab25 {ECO:0000312|MGI:MGI:1858203};
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 [GENOMIC DNA / MRNA].
RX PubMed=10708602; DOI=10.1006/bbrc.2000.2334;
RA Bhartur S.G., Calhoun B.C., Woodrum J., Kurkjian J., Iyer S., Lai F.,
RA Goldenring J.R.;
RT "Genomic structure of murine rab11 family members.";
RL Biochem. Biophys. Res. Commun. 269:611-617(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [4]
RP PROTEIN SEQUENCE OF 15-25 AND 76-83, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION.
RX PubMed=22696678; DOI=10.1091/mbc.e12-02-0097;
RA Senga K., Mostov K.E., Mitaka T., Miyajima A., Tanimizu N.;
RT "Grainyhead-like 2 regulates epithelial morphogenesis by establishing
RT functional tight junctions through the organization of a molecular network
RT among claudin3, claudin4, and Rab25.";
RL Mol. Biol. Cell 23:2845-2855(2012).
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
CC (PubMed:22696678). May selectively regulate the apical recycling
CC pathway. Together with MYO5B regulates transcytosis (By similarity).
CC {ECO:0000250|UniProtKB:E2RQ15, ECO:0000250|UniProtKB:P46629,
CC ECO:0000250|UniProtKB:P57735, ECO:0000269|PubMed:22696678}.
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}.
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DR EMBL; AF119675; AAD39911.1; -; mRNA.
DR EMBL; AF119676; AAD39912.1; -; Genomic_DNA.
DR EMBL; AK003260; BAB22676.1; -; mRNA.
DR EMBL; BC006624; AAH06624.1; -; mRNA.
DR CCDS; CCDS17477.1; -.
DR RefSeq; NP_058595.2; NM_016899.4.
DR AlphaFoldDB; Q9WTL2; -.
DR SMR; Q9WTL2; -.
DR IntAct; Q9WTL2; 3.
DR MINT; Q9WTL2; -.
DR STRING; 10090.ENSMUSP00000008745; -.
DR iPTMnet; Q9WTL2; -.
DR PhosphoSitePlus; Q9WTL2; -.
DR jPOST; Q9WTL2; -.
DR MaxQB; Q9WTL2; -.
DR PaxDb; Q9WTL2; -.
DR PRIDE; Q9WTL2; -.
DR ProteomicsDB; 300222; -.
DR Antibodypedia; 1660; 306 antibodies from 29 providers.
DR DNASU; 53868; -.
DR Ensembl; ENSMUST00000008745; ENSMUSP00000008745; ENSMUSG00000008601.
DR GeneID; 53868; -.
DR KEGG; mmu:53868; -.
DR UCSC; uc008pvn.1; mouse.
DR CTD; 57111; -.
DR MGI; MGI:1858203; Rab25.
DR VEuPathDB; HostDB:ENSMUSG00000008601; -.
DR eggNOG; KOG0087; Eukaryota.
DR GeneTree; ENSGT00940000158230; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; Q9WTL2; -.
DR OMA; KRACCIN; -.
DR OrthoDB; 1133775at2759; -.
DR PhylomeDB; Q9WTL2; -.
DR TreeFam; TF300099; -.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 53868; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Lamtor2; mouse.
DR PRO; PR:Q9WTL2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9WTL2; protein.
DR Bgee; ENSMUSG00000008601; Expressed in urinary bladder urothelium and 138 other tissues.
DR ExpressionAtlas; Q9WTL2; baseline and differential.
DR Genevisible; Q9WTL2; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0031143; C:pseudopodium; ISS:UniProtKB.
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; ISO:MGI.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0031268; P:pseudopodium organization; ISS:UniProtKB.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; ISO:MGI.
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 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Direct protein sequencing; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..210
FT /note="Ras-related protein Rab-25"
FT /id="PRO_0000121216"
FT PROPEP 211..213
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370822"
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"
FT CONFLICT 203
FT /note="P -> L (in Ref. 1; AAD39911/AAD39912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 213 AA; 23473 MW; 1359F7B4EA88D070 CRC64;
MGNRTDEDYN FVFKVVLIGE SGVGKTNLLS RFTRNEFSHD SRTTIGVEFS TRTVMLGTAA
VKAQIWDTAG LERYRAITSA YYRGAVGALL VFDLTKHQTY AVVERWLKEL YDHAEATIVV
MLVGNKSDLS QAREVPTEEA CMFAENNGLL FLETSALDST NVELAFQTVL KEIFAKVSKQ
KQNSTRTSAI TLGNAQAGQD PGPGEKRACC ISL
