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RAB5A_CANLF
ID   RAB5A_CANLF             Reviewed;         215 AA.
AC   P18066;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 188.
DE   RecName: Full=Ras-related protein Rab-5A;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P20339};
GN   Name=RAB5A;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX   PubMed=2115402; DOI=10.1016/0092-8674(90)90369-p;
RA   Chavrier P., Parton R.G., Hauri H.P., Simons K., Zerial M.;
RT   "Localization of low molecular weight GTP binding proteins to exocytic and
RT   endocytic compartments.";
RL   Cell 62:317-329(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Cocker spaniel; TISSUE=Kidney;
RX   PubMed=2123294; DOI=10.1128/mcb.10.12.6578-6585.1990;
RA   Chavrier P., Vingron M., Sander C., Simons K., Zerial M.;
RT   "Molecular cloning of YPT1/SEC4-related cDNAs from an epithelial cell
RT   line.";
RL   Mol. Cell. Biol. 10:6578-6585(1990).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH RABEP1.
RX   PubMed=8521472; DOI=10.1016/0092-8674(95)90120-5;
RA   Stenmark H., Vitale G., Ulrich O., Zerial M.;
RT   "Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic
RT   membrane fusion.";
RL   Cell 83:423-432(1995).
RN   [4]
RP   LACK OF INTERACTION WITH THE BLOC-3 COMPLEX.
RX   PubMed=20048159; DOI=10.1074/jbc.m109.069088;
RA   Kloer D.P., Rojas R., Ivan V., Moriyama K., van Vlijmen T., Murthy N.,
RA   Ghirlando R., van der Sluijs P., Hurley J.H., Bonifacino J.S.;
RT   "Assembly of the biogenesis of lysosome-related organelles complex-3 (BLOC-
RT   3) and its interaction with Rab9.";
RL   J. Biol. Chem. 285:7794-7804(2010).
RN   [5]
RP   INTERACTION WITH RINL, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX   PubMed=21419809; DOI=10.1016/j.bbamcr.2011.03.005;
RA   Woller B., Luiskandl S., Popovic M., Prieler B.E., Ikonge G., Mutzl M.,
RA   Rehmann H., Herbst R.;
RT   "Rin-like, a novel regulator of endocytosis, acts as guanine nucleotide
RT   exchange factor for Rab5a and Rab22.";
RL   Biochim. Biophys. Acta 1813:1198-1210(2011).
CC   -!- FUNCTION: Small GTPase which cycles between active GTP-bound and
CC       inactive GDP-bound states. In its active state, binds to a variety of
CC       effector proteins to regulate cellular responses such as of
CC       intracellular membrane trafficking, from the formation of transport
CC       vesicles to their fusion with membranes. Active GTP-bound form is able
CC       to recruit to membranes different sets of downstream effectors directly
CC       responsible for vesicle formation, movement, tethering and fusion
CC       (PubMed:8521472). RAB5A is required for the fusion of plasma membranes
CC       and early endosomes. Contributes to the regulation of filopodia
CC       extension. Required for the exosomal release of SDCBP, CD63, PDCD6IP
CC       and syndecan. Regulates maturation of apoptotic cell-containing
CC       phagosomes, probably downstream of DYN2 and PIK3C3 (By similarity).
CC       {ECO:0000250|UniProtKB:P20339, ECO:0000250|UniProtKB:Q9CQD1,
CC       ECO:0000269|PubMed:8521472}.
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:0000250|UniProtKB:P20339};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P20339};
CC   -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC       (GEFs) which promote the exchange of bound GDP for free GTP.
CC       {ECO:0000269|PubMed:21419809}.
CC   -!- SUBUNIT: Interacts with GDI1; this promotes dissociation from
CC       membranes; phosphorylation at Ser-84 disrupts this interaction (By
CC       similarity). Interacts with GDI2; phosphorylation at Ser-84 disrupts
CC       the interaction (By similarity). Binds EEA1. Interacts with ALS2CL,
CC       SUN2, ZFYVE20 and RUFY1. Interacts with RIN1 and GAPVD1, which regulate
CC       its pathway, probably by acting as a GEF. Interacts with SGSM1 and
CC       SGSM3. Interacts with PIK3CB (By similarity). Interacts with RABEP1 and
CC       RINL (PubMed:8521472, PubMed:21419809). Interacts with OCRL and INPP5F.
CC       May be a component of a complex composed of RAB5A, DYN2 and PIK3C3 (By
CC       similarity). Does not interact with the BLOC-3 complex (heterodimer of
CC       HPS1 and HPS4) (PubMed:20048159). Interacts with CLN5 (By similarity).
CC       Interacts with APPL2 (By similarity). Interacts with F8A1/F8A2/F8A3 (By
CC       similarity). Found in a complex with F8A1/F8A2/F8A3, HTT and RAB5A;
CC       mediates the recruitment of HTT by RAB5A onto early endosomes (By
CC       similarity). {ECO:0000250|UniProtKB:P20339,
CC       ECO:0000250|UniProtKB:Q0IIG7, ECO:0000250|UniProtKB:Q9CQD1,
CC       ECO:0000269|PubMed:20048159, ECO:0000269|PubMed:21419809,
CC       ECO:0000269|PubMed:8521472}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2115402};
CC       Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC       {ECO:0000269|PubMed:2115402}. Early endosome membrane
CC       {ECO:0000269|PubMed:2115402}; Lipid-anchor {ECO:0000305}. Melanosome
CC       {ECO:0000250|UniProtKB:P20339}. Cytoplasmic vesicle
CC       {ECO:0000269|PubMed:2115402}. Cell projection, ruffle
CC       {ECO:0000269|PubMed:21419809}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P20339}. Membrane {ECO:0000269|PubMed:2115402}.
CC       Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9CQD1}.
CC       Endosome membrane {ECO:0000250|UniProtKB:P20339}. Note=Alternates
CC       between membrane-bound and cytosolic forms.
CC       {ECO:0000250|UniProtKB:P20339}.
CC   -!- PTM: Phosphorylation of Ser-84 in the switch II region by LRRK2
CC       prevents the association of RAB regulatory proteins, including RAB GDP
CC       dissociation inhibitors GDI1 and GDI2. {ECO:0000250|UniProtKB:P20339}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; M35520; AAA30889.1; -; mRNA.
DR   PIR; A30413; A30413.
DR   RefSeq; NP_001003317.1; NM_001003317.2.
DR   AlphaFoldDB; P18066; -.
DR   SMR; P18066; -.
DR   IntAct; P18066; 1.
DR   STRING; 9615.ENSCAFP00000008690; -.
DR   PaxDb; P18066; -.
DR   PRIDE; P18066; -.
DR   Ensembl; ENSCAFT00030043680; ENSCAFP00030038124; ENSCAFG00030023727.
DR   Ensembl; ENSCAFT00040042303; ENSCAFP00040036899; ENSCAFG00040022761.
DR   Ensembl; ENSCAFT00845037438; ENSCAFP00845029329; ENSCAFG00845021204.
DR   GeneID; 404008; -.
DR   KEGG; cfa:404008; -.
DR   CTD; 5868; -.
DR   VEuPathDB; HostDB:ENSCAFG00845021204; -.
DR   eggNOG; KOG0092; Eukaryota.
DR   GeneTree; ENSGT00940000154337; -.
DR   HOGENOM; CLU_041217_10_2_1; -.
DR   InParanoid; P18066; -.
DR   OMA; DGIDCAE; -.
DR   OrthoDB; 1340129at2759; -.
DR   TreeFam; TF300199; -.
DR   Reactome; R-CFA-1660499; Synthesis of PIPs at the plasma membrane.
DR   Reactome; R-CFA-8854214; TBC/RABGAPs.
DR   Reactome; R-CFA-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-CFA-8873719; RAB geranylgeranylation.
DR   Reactome; R-CFA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   Reactome; R-CFA-983231; Factors involved in megakaryocyte development and platelet production.
DR   Proteomes; UP000002254; Chromosome 23.
DR   Bgee; ENSCAFG00000005814; Expressed in occipital cortex and 46 other tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IBA:GO_Central.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0098559; C:cytoplasmic side of early endosome membrane; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
DR   GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
DR   GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098842; C:postsynaptic early endosome; IBA:GO_Central.
DR   GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR   GO; GO:0097443; C:sorting endosome; IDA:CAFA.
DR   GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0150093; P:amyloid-beta clearance by transcytosis; IEA:Ensembl.
DR   GO; GO:0045022; P:early endosome to late endosome transport; IEA:Ensembl.
DR   GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0044788; P:modulation by host of viral process; IEA:Ensembl.
DR   GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0045921; P:positive regulation of exocytosis; IEA:Ensembl.
DR   GO; GO:2000286; P:receptor internalization involved in canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR   GO; GO:0051036; P:regulation of endosome size; IEA:Ensembl.
DR   GO; GO:0051489; P:regulation of filopodium assembly; IBA:GO_Central.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IBA:GO_Central.
DR   GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR   GO; GO:0036465; P:synaptic vesicle recycling; IEA:Ensembl.
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; Cytoplasm; Cytoplasmic vesicle;
KW   Endocytosis; Endosome; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW   Nucleotide-binding; Phagocytosis; Phosphoprotein; Prenylation;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..215
FT                   /note="Ras-related protein Rab-5A"
FT                   /id="PRO_0000121103"
FT   REGION          181..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           49..57
FT                   /note="Effector region"
FT                   /evidence="ECO:0000255"
FT   BINDING         27..35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         46..52
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         75..79
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         133..136
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         163..165
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   LIPID           212
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   LIPID           213
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
SQ   SEQUENCE   215 AA;  23659 MW;  DDDE3FD8B37C2606 CRC64;
     MANRGATRPN GPNTGNKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEFQE STIGAAFLTQ
     TVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNEESFAR AKNWVKELQR
     QASPNIVIAL SGNKADLANK RAVDFQEAQS YADDNSLLFM ETSAKTSMNV NEIFMAIAKK
     LPKNEPQNPG ANSARGRGVD LTEPTQPTRS QCCSN
 
 
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