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   27-MAR-2024, entry version 201.
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   INTERACTION WITH VPS33B.
RX   PubMed=28017832; DOI=10.1016/j.jid.2016.12.010;
RA   Gruber R., Rogerson C., Windpassinger C., Banushi B.,
RA   Straatman-Iwanowska A., Hanley J., Forneris F., Strohal R., Ulz P.,
RA   Crumrine D., Menon G.K., Blunder S., Schmuth M., Mueller T., Smith H.,
RA   Mills K., Kroisel P., Janecke A.R., Gissen P.;
RT   "Autosomal Recessive Keratoderma-Ichthyosis-Deafness (ARKID) Syndrome Is
RT   Caused by VPS33B Mutations Affecting Rab Protein Interaction and Collagen
RT   Modification.";
RL   J. Invest. Dermatol. 137:845-854(2017).
RN   [11]
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       Interacts with VPS33B (PubMed:28017832). {ECO:0000269|PubMed:11495908,
CC       ECO:0000269|PubMed:17925226, ECO:0000269|PubMed:28017832,
CC       ECO:0000269|Ref.11}.
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; 293.
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; 9606-ENSP00000354376; -.
DR   PeptideAtlas; P57735; -.
DR   ProteomicsDB; 57023; -.
DR   Pumba; P57735; -.
DR   Antibodypedia; 1660; 336 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   AGR; HGNC:18238; -.
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; 3487147at2759; -.
DR   PhylomeDB; P57735; -.
DR   TreeFam; TF300099; -.
DR   PathwayCommons; P57735; -.
DR   Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR   SignaLink; P57735; -.
DR   BioGRID-ORCS; 57111; 23 hits in 1144 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 140 other cell types or tissues.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
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   CDD; cd01868; Rab11_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47979; DRAB11-RELATED; 1.
DR   PANTHER; PTHR47979:SF8; RAS-RELATED PROTEIN RAB-25; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   Genevisible; P57735; HS.
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
//