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RAB25_BOVIN
ID   RAB25_BOVIN             Reviewed;         213 AA.
AC   Q58DW6; Q0VCM9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Ras-related protein Rab-25;
DE   Flags: Precursor;
GN   Name=RAB25;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal lung;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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:E2RQ15, ECO:0000250|UniProtKB:P46629,
CC       ECO:0000250|UniProtKB:P57735, ECO:0000250|UniProtKB:Q9WTL2}.
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; BT021481; AAX46328.1; -; mRNA.
DR   EMBL; BC120091; AAI20092.1; -; mRNA.
DR   RefSeq; NP_001017936.1; NM_001017936.1.
DR   AlphaFoldDB; Q58DW6; -.
DR   SMR; Q58DW6; -.
DR   STRING; 9913.ENSBTAP00000025170; -.
DR   PaxDb; Q58DW6; -.
DR   PRIDE; Q58DW6; -.
DR   Ensembl; ENSBTAT00000025170; ENSBTAP00000025170; ENSBTAG00000018914.
DR   GeneID; 506482; -.
DR   KEGG; bta:506482; -.
DR   CTD; 57111; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018914; -.
DR   VGNC; VGNC:33632; RAB25.
DR   eggNOG; KOG0087; Eukaryota.
DR   GeneTree; ENSGT00940000158230; -.
DR   HOGENOM; CLU_041217_23_0_1; -.
DR   InParanoid; Q58DW6; -.
DR   OMA; KRACCIN; -.
DR   OrthoDB; 1133775at2759; -.
DR   TreeFam; TF300099; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000018914; Expressed in surface of tongue and 78 other tissues.
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; 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; ISS:UniProtKB.
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; ISS:UniProtKB.
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   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_0000244429"
FT   PROPEP          211..213
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000370773"
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        191
FT                   /note="T -> I (in Ref. 2; AAI20092)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   213 AA;  23537 MW;  29ECDCE77E266B9B CRC64;
     MGNRAEEDYN FVFKVVLIGE SGVGKTNLLS RFTRNEFSHD SRTTIGVEFS TRTVMLGTAA
     IKAQIWDTAG LERYRAITSA YYRGAVGALL VFDLTKHQTY AVVERWLKEL YDHAEATIVV
     MLVGNKSDLS QSREVPTEEA RMFAENNGLL FLETSALDST NVELAFETVL KEIFAKVSKQ
     RQNNARTNAV TLGSGPAGQE LGPGEKRACC ISL
 
 
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