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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   29-OCT-2014, entry version 124.
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]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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]
RP   FUNCTION.
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]
RP   FUNCTION.
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]
RP   FUNCTION.
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. Plays a central role, not only in endosomal
CC       traffic, but also in many other cellular and physiological events,
CC       such as growth-factor-mediated cell signaling, nutrient-
CC       transportor mediated nutrient uptake, neurotrophin transport in
CC       the axons of neurons and lipid metabolism. Also involved in
CC       regulation of some specialized endosomal membrane trafficking,
CC       such as maturation of melanosomes, pathogen-induced phagosomes (or
CC       vacuoles) and autophagosomes. Plays a role in the maturation and
CC       acidification of phagosomes that engulf pathogens, such as
CC       S.aureus and Mycobacteria. Plays a role in the fusion of
CC       phagosomes with lysosomes (By similarity). Plays important roles
CC       in microbial pathogen infection and survival, as well as in
CC       participating in the life cycle of viruses. Microbial pathogens
CC       possess survival strategies governed by RAB7A, sometimes by
CC       employing RAB7A function (e.g. Salmonella) and sometimes by
CC       excluding RAB7A function (e.g. Mycobacterium). In concert with
CC       RAC1, plays a role in regulating the formation of RBs (ruffled
CC       borders) in osteoclasts. Controls the endosomal trafficking and
CC       neurite outgrowth signaling of NTRK1/TRKA. Regulates the endocytic
CC       trafficking of the EGF-EGFR complex by regulating its lysosomal
CC       degradation. {ECO:0000250, ECO:0000269|PubMed:16282324,
CC       ECO:0000269|PubMed:8522602, ECO:0000269|PubMed:9490721}.
CC   -!- SUBUNIT: Interacts with NTRK1/TRKA, RILP, PSMA7, RNF115 and FYCO1.
CC       Interacts with the PIK3C3/VPS34-PIK3R4 complex. The GTP-bound form
CC       interacts with OSBPL1A and RAC1 (By similarity). Interacts with
CC       CLN3. Interacts with CHM, the substrate-binding subunit of the Rab
CC       geranylgeranyltransferase complex (By similarity). Interacts with
CC       C9orf72 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Late endosome. Lysosome {ECO:0000250}.
CC       Cytoplasmic vesicle, phagosome {ECO:0000250}. Cytoplasmic vesicle,
CC       phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Melanosome {ECO:0000250}.
CC       Note=Colocalizes with OSBPL1A at the late endosome. Found in the
CC       ruffled border (a late endosomal-like compartment in the plasma
CC       membrane) of bone-resorbing osteoclasts. Recruited to phagosomes
CC       containing S.aureus or Mycobacterium (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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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   SMR; P18067; 7-190.
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   OMA; DYPDPIK; -.
DR   OrthoDB; EOG7G4QG8; -.
DR   TreeFam; TF105605; -.
DR   Reactome; REACT_221251; MHC class II antigen presentation.
DR   NextBio; 20817494; -.
DR   GO; GO:0070062; C:extracellular vesicular 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; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR   GO; GO:0045022; P:early endosome to late endosome transport; IMP:UniProtKB.
DR   GO; GO:0008333; P:endosome to lysosome transport; IEA:Ensembl.
DR   GO; GO:0007174; P:epidermal growth factor catabolic process; IMP:UniProtKB.
DR   GO; GO:0090383; P:phagosome acidification; ISS:UniProtKB.
DR   GO; GO:0090385; P:phagosome-lysosome fusion; ISS:UniProtKB.
DR   GO; GO:0006622; P:protein targeting to lysosome; IEA:Ensembl.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
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   InterPro; IPR003579; Small_GTPase_Rab_type.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
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   Complete proteome; Cytoplasmic vesicle; Endosome; GTP-binding;
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. {ECO:0000250}.
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;
     MTSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV MVDDRLVTMQ
     IWDTAGQERF QSLGVAFYRG ADCCVLVFDV TAPNTFKTLD SWRDEFLIQA SPRDPENFPF
     VVLGNKIDLE NRQVATKRAQ AWCYSKNNIP YFETSAKEAI NVEQAFQTIA RNALKQETEV
     ELYNEFPEPI KLDKNDRAKT SAESCSC
//
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