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Database: UniProt
Entry: H0V568_CAVPO
LinkDB: H0V568_CAVPO
Original site: H0V568_CAVPO 
ID   H0V568_CAVPO            Unreviewed;       214 AA.
AC   H0V568;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=small monomeric GTPase {ECO:0000256|ARBA:ARBA00011984};
DE            EC=3.6.5.2 {ECO:0000256|ARBA:ARBA00011984};
GN   Name=RAB5A {ECO:0000313|Ensembl:ENSCPOP00000004786.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000004786.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000004786.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000004786.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000249};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000256|ARBA:ARBA00000249};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342};
CC       Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004342}. Early endosome membrane
CC       {ECO:0000256|ARBA:ARBA00043949}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00043949}. Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004455}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004455}. Melanosome
CC       {ECO:0000256|ARBA:ARBA00004223}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004635}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000256|ARBA:ARBA00006270}.
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DR   EMBL; AAKN02001804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02001805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H0V568; -.
DR   STRING; 10141.ENSCPOP00000004786; -.
DR   Ensembl; ENSCPOT00000005379.3; ENSCPOP00000004786.3; ENSCPOG00000005322.4.
DR   VEuPathDB; HostDB:ENSCPOG00000005322; -.
DR   eggNOG; KOG0092; Eukaryota.
DR   GeneTree; ENSGT00940000154337; -.
DR   HOGENOM; CLU_041217_10_2_1; -.
DR   InParanoid; H0V568; -.
DR   OMA; RSYADDN; -.
DR   TreeFam; TF300199; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000005322; Expressed in cerebellum and 12 other cell types or tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0098559; C:cytoplasmic side of early endosome membrane; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0032009; C:early phagosome; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR   GO; GO:0036477; C:somatodendritic compartment; IEA:Ensembl.
DR   GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
DR   GO; GO:0019003; F:GDP binding; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:Ensembl.
DR   GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR   GO; GO:0150093; P:amyloid-beta clearance by transcytosis; IEA:Ensembl.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0045022; P:early endosome to late endosome transport; IEA:Ensembl.
DR   GO; GO:0044788; P:modulation by host of viral process; IEA:Ensembl.
DR   GO; GO:0045921; P:positive regulation of exocytosis; IEA:Ensembl.
DR   GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
DR   GO; GO:0051036; P:regulation of endosome size; IEA:Ensembl.
DR   GO; GO:0051489; P:regulation of filopodium assembly; IEA:Ensembl.
DR   GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR   GO; GO:0036465; P:synaptic vesicle recycling; IEA:Ensembl.
DR   CDD; cd01860; Rab5_related; 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; PTHR47978; -; 1.
DR   PANTHER; PTHR47978:SF65; RAB43, MEMBER RAS ONCOGENE FAMILY; 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   PROSITE; PS51421; RAS; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT   REGION          180..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   214 AA;  23572 MW;  058CF598BA20C72A CRC64;
     MANRGATRPN GPNTGNKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEFQE STIGAAFLQT
     VCLDDTTVKF EIWDTAGQER YHSLAPMYYR GAQAAIVVYD ITNEESFARA KNWVKELQRQ
     ASPNIVIALS GNKADLANKR AVDFQEAQSY AEDNSLLFME TSAKTSMNVN EIFMAIAKKL
     PKNEPQNPGA NSARGRGVDL TEPTQPTRSQ CCSN
//
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