RAB25_HUMAN
ID RAB25_HUMAN Reviewed; 213 AA.
AC P57735; Q5VYA2; Q8NG24; Q96GB1; Q9BT12;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Ras-related protein Rab-25;
DE AltName: Full=CATX-8;
DE Flags: Precursor;
GN Name=RAB25 {ECO:0000312|HGNC:HGNC:18238}; Synonyms=CATX8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon;
RA Wang L., Kairo A., Gao Z.Q., Gao Z.P., Boman B.M.;
RT "Isolation of novel genes from human colonic epithelial cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yu L.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, Pancreas, and Skin;
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 [6]
RP INTERACTION WITH RAB11FIP1; RAB11FIP2; RAB11FIP3 AND RAB11FIP4.
RX PubMed=11495908; DOI=10.1074/jbc.m104831200;
RA Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D., Kumar R.,
RA Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R.;
RT "Identification and characterization of a family of Rab11-interacting
RT proteins.";
RL J. Biol. Chem. 276:39067-39075(2001).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15502842; DOI=10.1038/nm1125;
RA Cheng K.W., Lahad J.P., Kuo W.L., Lapuk A., Yamada K., Auersperg N.,
RA Liu J., Smith-McCune K., Lu K.H., Fishman D., Gray J.W., Mills G.B.;
RT "The RAB25 small GTPase determines aggressiveness of ovarian and breast
RT cancers.";
RL Nat. Med. 10:1251-1256(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH ITGAV AND ITGB1.
RX PubMed=17925226; DOI=10.1016/j.devcel.2007.08.012;
RA Caswell P.T., Spence H.J., Parsons M., White D.P., Clark K., Cheng K.W.,
RA Mills G.B., Humphries M.J., Messent A.J., Anderson K.I., McCaffrey M.W.,
RA Ozanne B.W., Norman J.C.;
RT "Rab25 associates with alpha5beta1 integrin to promote invasive migration
RT in 3D microenvironments.";
RL Dev. Cell 13:496-510(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 7-180 IN COMPLEX WITH GDP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human RAB25 in complex with GDP.";
RL Submitted (FEB-2009) to the PDB data bank.
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 (PubMed:17925226). Involved in the regulation of epithelial
CC morphogenesis through the control of CLDN4 expression and localization
CC at tight junctions (By similarity). May selectively regulate the apical
CC recycling pathway. Together with MYO5B regulates transcytosis (By
CC similarity). {ECO:0000250|UniProtKB:E2RQ15,
CC ECO:0000250|UniProtKB:P46629, ECO:0000250|UniProtKB:Q9WTL2,
CC ECO:0000269|PubMed:17925226}.
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:0000269|PubMed:11495908, ECO:0000269|PubMed:17925226,
CC ECO:0000269|Ref.10}.
CC -!- INTERACTION:
CC P57735; Q9ULV0-2: MYO5B; NbExp=3; IntAct=EBI-1050500, EBI-14093244;
CC P57735; Q7L804: RAB11FIP2; NbExp=5; IntAct=EBI-1050500, EBI-1049676;
CC P57735; Q7L8J4: SH3BP5L; NbExp=3; IntAct=EBI-1050500, EBI-747389;
CC P57735; PRO_0000041303 [P08563]; Xeno; NbExp=2; IntAct=EBI-1050500, EBI-11477912;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection,
CC pseudopodium membrane {ECO:0000269|PubMed:17925226}. Cytoplasmic
CC vesicle {ECO:0000269|PubMed:17925226}. Note=Colocalizes with integrin
CC alpha-V/beta-1 in vesicles at the pseudopodial tips.
CC {ECO:0000269|PubMed:17925226}.
CC -!- TISSUE SPECIFICITY: Expressed in ovarian epithelium (NOE) and breast
CC tissue. Expressed in ovarian cancer; expression is increased relative
CC to NOE cells. Expression in ovarian cancer is stage dependent, with
CC stage III and stage IV showing higher levels than early stage cancers.
CC Expressed in breast cancer; expression is increased relative to normal
CC breast tissue. {ECO:0000269|PubMed:15502842}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF98238.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM69362.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF083124; AAF98238.1; ALT_FRAME; mRNA.
DR EMBL; AF274025; AAM69362.1; ALT_INIT; mRNA.
DR EMBL; AL355388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53003.1; -; Genomic_DNA.
DR EMBL; BC004416; AAH04416.1; -; mRNA.
DR EMBL; BC009831; AAH09831.1; -; mRNA.
DR EMBL; BC033322; AAH33322.1; -; mRNA.
DR CCDS; CCDS41413.1; -.
DR RefSeq; NP_065120.2; NM_020387.3.
DR PDB; 2OIL; X-ray; 2.30 A; A=7-180.
DR PDB; 3TSO; X-ray; 1.80 A; A/B=7-180.
DR PDBsum; 2OIL; -.
DR PDBsum; 3TSO; -.
DR AlphaFoldDB; P57735; -.
DR SMR; P57735; -.
DR BioGRID; 121377; 69.
DR IntAct; P57735; 9.
DR MINT; P57735; -.
DR STRING; 9606.ENSP00000354376; -.
DR iPTMnet; P57735; -.
DR PhosphoSitePlus; P57735; -.
DR SwissPalm; P57735; -.
DR BioMuta; RAB25; -.
DR DMDM; 46577696; -.
DR EPD; P57735; -.
DR jPOST; P57735; -.
DR MassIVE; P57735; -.
DR MaxQB; P57735; -.
DR PaxDb; P57735; -.
DR PeptideAtlas; P57735; -.
DR PRIDE; P57735; -.
DR ProteomicsDB; 57023; -.
DR Antibodypedia; 1660; 306 antibodies from 29 providers.
DR DNASU; 57111; -.
DR Ensembl; ENST00000361084.10; ENSP00000354376.5; ENSG00000132698.15.
DR GeneID; 57111; -.
DR KEGG; hsa:57111; -.
DR MANE-Select; ENST00000361084.10; ENSP00000354376.5; NM_020387.4; NP_065120.2.
DR UCSC; uc001fnc.4; human.
DR CTD; 57111; -.
DR DisGeNET; 57111; -.
DR GeneCards; RAB25; -.
DR HGNC; HGNC:18238; RAB25.
DR HPA; ENSG00000132698; Tissue enhanced (esophagus, skin).
DR MIM; 612942; gene.
DR neXtProt; NX_P57735; -.
DR OpenTargets; ENSG00000132698; -.
DR PharmGKB; PA34115; -.
DR VEuPathDB; HostDB:ENSG00000132698; -.
DR eggNOG; KOG0087; Eukaryota.
DR GeneTree; ENSGT00940000158230; -.
DR HOGENOM; CLU_041217_23_0_1; -.
DR InParanoid; P57735; -.
DR OMA; KRACCIN; -.
DR OrthoDB; 1133775at2759; -.
DR PhylomeDB; P57735; -.
DR TreeFam; TF300099; -.
DR PathwayCommons; P57735; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; P57735; -.
DR BioGRID-ORCS; 57111; 22 hits in 1066 CRISPR screens.
DR ChiTaRS; RAB25; human.
DR EvolutionaryTrace; P57735; -.
DR GeneWiki; RAB25; -.
DR GenomeRNAi; 57111; -.
DR Pharos; P57735; Tbio.
DR PRO; PR:P57735; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P57735; protein.
DR Bgee; ENSG00000132698; Expressed in lower esophagus mucosa and 138 other tissues.
DR Genevisible; P57735; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0031143; C:pseudopodium; IDA: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; IPI:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0031268; P:pseudopodium organization; IDA:UniProtKB.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IMP:UniProtKB.
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 3D-structure; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..210
FT /note="Ras-related protein Rab-25"
FT /id="PRO_0000121215"
FT PROPEP 211..213
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370821"
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 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 BINDING 155..157
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
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; AAF98238)"
FT /evidence="ECO:0000305"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:3TSO"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:3TSO"
FT STRAND 46..56
FT /evidence="ECO:0007829|PDB:3TSO"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:3TSO"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:3TSO"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:3TSO"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:3TSO"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:3TSO"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3TSO"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:3TSO"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:3TSO"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:3TSO"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:3TSO"
FT HELIX 162..177
FT /evidence="ECO:0007829|PDB:3TSO"
SQ SEQUENCE 213 AA; 23496 MW; 119523C3036C370E CRC64;
MGNGTEEDYN FVFKVVLIGE SGVGKTNLLS RFTRNEFSHD SRTTIGVEFS TRTVMLGTAA
VKAQIWDTAG LERYRAITSA YYRGAVGALL VFDLTKHQTY AVVERWLKEL YDHAEATIVV
MLVGNKSDLS QAREVPTEEA RMFAENNGLL FLETSALDST NVELAFETVL KEIFAKVSKQ
RQNSIRTNAI TLGSAQAGQE PGPGEKRACC ISL
