Database: UniProt
Entry: P18067
LinkDB: P18067
Original site: P18067 
ID   RAB7A_CANFA             Reviewed;         207 AA.
AC   P18067;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   16-SEP-2015, entry version 132.
DE   RecName: Full=Ras-related protein Rab-7a;
GN   Name=RAB7A; Synonyms=RAB7;
OS   Canis familiaris (Dog) (Canis lupus familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
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
RT   and endocytic compartments.";
RL   Cell 62:317-329(1990).
RN   [2]
RC   STRAIN=Cocker spaniel; TISSUE=Kidney;
RX   PubMed=2123294;
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]
RX   PubMed=8522602; DOI=10.1083/jcb.131.6.1435;
RA   Feng Y., Press B., Wandinger-Ness A.;
RT   "Rab 7: an important regulator of late endocytic membrane traffic.";
RL   J. Cell Biol. 131:1435-1452(1995).
RN   [4]
RX   PubMed=9490721; DOI=10.1083/jcb.140.5.1075;
RA   Press B., Feng Y., Hoflack B., Wandinger-Ness A.;
RT   "Mutant Rab7 causes the accumulation of cathepsin D and cation-
RT   independent mannose 6-phosphate receptor in an early endocytic
RT   compartment.";
RL   J. Cell Biol. 140:1075-1089(1998).
RN   [5]
RX   PubMed=16282324; DOI=10.1074/jbc.M504175200;
RA   Ceresa B.P., Bahr S.J.;
RT   "rab7 activity affects epidermal growth factor:epidermal growth factor
RT   receptor degradation by regulating endocytic trafficking from the late
RT   endosome.";
RL   J. Biol. Chem. 281:1099-1106(2006).
CC   -!- FUNCTION: Key regulator in endo-lysosomal trafficking. Governs
CC       early-to-late endosomal maturation, microtubule minus-end as well
CC       as plus-end directed endosomal migration and positioning, and
CC       endosome-lysosome transport through different protein-protein
CC       interaction cascades (By similarity). Plays a central role, not
CC       only in endosomal traffic, but also in many other cellular and
CC       physiological events, such as growth-factor-mediated cell
CC       signaling, nutrient-transportor mediated nutrient uptake,
CC       neurotrophin transport in the axons of neurons and lipid
CC       metabolism (By similarity). Also involved in regulation of some
CC       specialized endosomal membrane trafficking, such as maturation of
CC       melanosomes, pathogen-induced phagosomes (or vacuoles) and
CC       autophagosomes (By similarity). Plays a role in the maturation and
CC       acidification of phagosomes that engulf pathogens, such as
CC       S.aureus and Mycobacteria (By similarity). Plays a role in the
CC       fusion of phagosomes with lysosomes (By similarity). Plays
CC       important roles in microbial pathogen infection and survival, as
CC       well as in participating in the life cycle of viruses (By
CC       similarity). Microbial pathogens possess survival strategies
CC       governed by RAB7A, sometimes by employing RAB7A function (e.g.
CC       Salmonella) and sometimes by excluding RAB7A function (e.g.
CC       Mycobacterium) (By similarity). In concert with RAC1, plays a role
CC       in regulating the formation of RBs (ruffled borders) in
CC       osteoclasts (By similarity). Controls the endosomal trafficking
CC       and neurite outgrowth signaling of NTRK1/TRKA (By similarity).
CC       Regulates the endocytic trafficking of the EGF-EGFR complex by
CC       regulating its lysosomal degradation (By similarity). Involved in
CC       the ADRB2-stimulated lipolysis through lipophagy, a cytosolic
CC       lipase-independent autophagic pathway (By similarity).
CC       {ECO:0000250|UniProtKB:P51149, ECO:0000250|UniProtKB:P51150}.
CC   -!- SUBUNIT: Interacts with NTRK1/TRKA (By similarity). Interacts with
CC       RILP (By similarity). Interacts with PSMA7 (By similarity).
CC       Interacts with RNF115 (By similarity). Interacts with FYCO1 (By
CC       similarity). Interacts with the PIK3C3/VPS34-PIK3R4 complex (By
CC       similarity). The GTP-bound form interacts with OSBPL1A (By
CC       similarity). The GTP-bound form interacts with RAC1 (By
CC       similarity). Interacts with CLN3 (By similarity). Interacts with
CC       CHM, the substrate-binding subunit of the Rab
CC       geranylgeranyltransferase complex (By similarity). Interacts with
CC       C9orf72 (By similarity). {ECO:0000250|UniProtKB:P09527,
CC       ECO:0000250|UniProtKB:P51149, ECO:0000250|UniProtKB:P51150}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane
CC       {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome
CC       membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane
CC       protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome
CC       membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane
CC       protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome
CC       membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane
CC       protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic
CC       vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P51149};
CC       Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC       {ECO:0000305}. Lipid droplet {ECO:0000250|UniProtKB:P51150}.
CC       Note=Colocalizes with OSBPL1A at the late endosome (By
CC       similarity). Found in the ruffled border (a late endosomal-like
CC       compartment in the plasma membrane) of bone-resorbing osteoclasts
CC       (By similarity). Recruited to phagosomes containing S.aureus or
CC       Mycobacterium (By similarity). Lipid droplet localization is
CC       increased upon ADRB2 stimulation (By similarity).
CC       {ECO:0000250|UniProtKB:P51149, ECO:0000250|UniProtKB:P51150}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
DR   EMBL; M35522; AAA30890.1; -; mRNA.
DR   PIR; B30413; B30413.
DR   RefSeq; NP_001003316.1; NM_001003316.1.
DR   RefSeq; XP_005632072.1; XM_005632015.1.
DR   UniGene; Cfa.29293; -.
DR   ProteinModelPortal; P18067; -.
DR   IntAct; P18067; 2.
DR   MINT; MINT-8387239; -.
DR   STRING; 9615.ENSCAFP00000034211; -.
DR   BindingDB; P18067; -.
DR   PaxDb; P18067; -.
DR   PRIDE; P18067; -.
DR   Ensembl; ENSCAFT00000038482; ENSCAFP00000034211; ENSCAFG00000004157.
DR   GeneID; 404007; -.
DR   KEGG; cfa:404007; -.
DR   CTD; 7879; -.
DR   eggNOG; COG1100; -.
DR   GeneTree; ENSGT00760000119125; -.
DR   HOGENOM; HOG000233968; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P18067; -.
DR   KO; K07897; -.
DR   OrthoDB; EOG7G4QG8; -.
DR   TreeFam; TF105605; -.
DR   Reactome; R-CFA-2132295; MHC class II antigen presentation.
DR   NextBio; 20817494; -.
DR   PRO; PR:P18067; -.
DR   Proteomes; UP000002254; Chromosome 20.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034045; C:pre-autophagosomal structure membrane; IEA:Ensembl.
DR   GO; GO:0030904; C:retromer complex; IEA:Ensembl.
DR   GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR   GO; GO:0019003; F:GDP binding; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0045022; P:early endosome to late endosome transport; IMP:UniProtKB.
DR   GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR   GO; GO:0007174; P:epidermal growth factor catabolic process; IMP:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0090383; P:phagosome acidification; ISS:UniProtKB.
DR   GO; GO:0090385; P:phagosome-lysosome fusion; ISS:UniProtKB.
DR   GO; GO:1903543; P:positive regulation of exosomal secretion; IEA:Ensembl.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0048524; P:positive regulation of viral process; IEA:Ensembl.
DR   GO; GO:0006622; P:protein targeting to lysosome; IEA:Ensembl.
DR   GO; GO:0022615; P:protein to membrane docking; IEA:Ensembl.
DR   GO; GO:0032482; P:Rab protein signal transduction; IBA:GO_Central.
DR   GO; GO:2000785; P:regulation of autophagosome assembly; IEA:Ensembl.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:Ensembl.
DR   GO; GO:0019076; P:viral release from host cell; IEA:Ensembl.
DR   Gene3D;; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR003579; Small_GTPase_Rab_type.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00175; RAB; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Complete proteome; Cytoplasmic vesicle; Endosome;
KW   GTP-binding; Lipid degradation; Lipid droplet; Lipid metabolism;
KW   Lipoprotein; Lysosome; Membrane; Methylation; Nucleotide-binding;
KW   Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN         1    207       Ras-related protein Rab-7a.
FT                                /FTId=PRO_0000121120.
FT   NP_BIND      15     22       GTP. {ECO:0000250}.
FT   NP_BIND      34     40       GTP. {ECO:0000250}.
FT   NP_BIND      63     67       GTP. {ECO:0000250}.
FT   NP_BIND     125    128       GTP. {ECO:0000250}.
FT   NP_BIND     156    157       GTP. {ECO:0000250}.
FT   MOTIF        37     45       Effector region. {ECO:0000250}.
FT   MOD_RES      72     72       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51149}.
FT   MOD_RES     207    207       Cysteine methyl ester. {ECO:0000250}.
FT   LIPID       205    205       S-geranylgeranyl cysteine. {ECO:0000250}.
FT   LIPID       207    207       S-geranylgeranyl cysteine. {ECO:0000250}.
SQ   SEQUENCE   207 AA;  23520 MW;  E3AF33B16A67296D CRC64;
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