RAB7A_CANLF
ID RAB7A_CANLF Reviewed; 207 AA.
AC P18067;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Ras-related protein Rab-7a;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P51149};
GN Name=RAB7A; Synonyms=RAB7;
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].
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.
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-independent
RT mannose 6-phosphate receptor in an early endocytic 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: 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 playing a key role in the regulation of endo-
CC lysosomal trafficking. Governs early-to-late endosomal maturation,
CC microtubule minus-end as well as plus-end directed endosomal migration
CC and positioning, and endosome-lysosome transport through different
CC protein-protein interaction cascades (By similarity). Plays a central
CC role, not only in endosomal traffic, but also in many other cellular
CC and physiological events, such as growth-factor-mediated cell
CC signaling, nutrient-transporter-mediated nutrient uptake, neurotrophin
CC transport in the axons of neurons and lipid metabolism (By similarity).
CC Also involved in regulation of some specialized endosomal membrane
CC trafficking, such as maturation of melanosomes, pathogen-induced
CC phagosomes (or vacuoles) and autophagosomes (By similarity). Plays a
CC role in the maturation and acidification of phagosomes that engulf
CC pathogens, such as S.aureus and Mycobacteria (By similarity). Plays a
CC role in the fusion of phagosomes with lysosomes (By similarity). Plays
CC important roles in microbial pathogen infection and survival, as well
CC as in participating in the life cycle of viruses (By similarity).
CC Microbial pathogens possess survival strategies governed by RAB7A,
CC sometimes by employing RAB7A function (e.g. Salmonella) and sometimes
CC by excluding RAB7A function (e.g. Mycobacterium) (By similarity). In
CC concert with RAC1, plays a role in regulating the formation of RBs
CC (ruffled borders) in osteoclasts (By similarity). Controls the
CC endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA (By
CC similarity). Regulates the endocytic trafficking of the EGF-EGFR
CC complex by regulating its lysosomal degradation (By similarity).
CC Involved in the ADRB2-stimulated lipolysis through lipophagy, a
CC cytosolic lipase-independent autophagic pathway. Required for the
CC exosomal release of SDCBP, CD63 and syndecan (By similarity). Required
CC for vesicular trafficking and cell surface expression of ACE2 (By
CC similarity). May play a role in PRPH neuronal intermediate filament
CC assembly (By similarity). {ECO:0000250|UniProtKB:P51149,
CC ECO:0000250|UniProtKB:P51150, ECO:0000269|PubMed:16282324,
CC ECO:0000269|PubMed:8522602, ECO:0000269|PubMed:9490721}.
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:P51149};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P51149};
CC -!- SUBUNIT: Interacts with NTRK1/TRKA (By similarity). Interacts with RILP
CC (By similarity). Interacts with PSMA7 (By similarity). Interacts with
CC RNF115 (By similarity). Interacts with FYCO1 (By similarity). Interacts
CC with the PIK3C3/VPS34-PIK3R4 complex (By similarity). The GTP-bound
CC form interacts with OSBPL1A (By similarity). The GTP-bound form
CC interacts with RAC1 (By similarity). Interacts with CLN3 (By
CC similarity). Interacts with CHM, the substrate-binding subunit of the
CC Rab geranylgeranyltransferase complex (By similarity). Interacts with
CC C9orf72. Does not interact with HPS4 and the BLOC-3 complex
CC (heterodimer of HPS1 and HPS4). Interacts with CLN5 (By similarity).
CC Interacts with PLEKHM1 (via N- and C-terminus) (By similarity).
CC Interacts with RUFY4 (By similarity). Interacts with PRPH; the
CC interaction is direct (By similarity). Interacts with VPS13A (By
CC similarity). The GDP-bound form interacts with RIMOC1 (By similarity).
CC Interacts with the MON1A-CCZ1B complex and this interaction is enhanced
CC in the presence of RIMOC1 (By similarity).
CC {ECO:0000250|UniProtKB:P09527, ECO:0000250|UniProtKB:P51149,
CC ECO:0000250|UniProtKB:P51150}.
CC -!- INTERACTION:
CC P18067; Q5T4F4-1: ZFYVE27; Xeno; NbExp=2; IntAct=EBI-7991906, EBI-16152863;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome membrane
CC {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane
CC {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome membrane
CC {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle,
CC autophagosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lipid
CC droplet {ECO:0000250|UniProtKB:P51150}. Endosome membrane
CC {ECO:0000250|UniProtKB:P51149}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:P51150}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein
CC {ECO:0000305}. Note=Colocalizes with OSBPL1A at the late endosome.
CC Found in the ruffled border (a late endosomal-like compartment in the
CC plasma membrane) of bone-resorbing osteoclasts. Recruited to phagosomes
CC containing S.aureus or Mycobacterium. Lipid droplet localization is
CC increased upon ADRB2 stimulation. Recruited to damaged mitochondria
CC during mitophagy in a RIMOC1-dependent manner.
CC {ECO:0000250|UniProtKB:P51149, ECO:0000250|UniProtKB:P51150}.
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 AlphaFoldDB; P18067; -.
DR SMR; P18067; -.
DR DIP; DIP-61531N; -.
DR IntAct; P18067; 3.
DR MINT; P18067; -.
DR STRING; 9615.ENSCAFP00000043782; -.
DR BindingDB; P18067; -.
DR PaxDb; P18067; -.
DR PRIDE; P18067; -.
DR Ensembl; ENSCAFT00000060815; ENSCAFP00000043782; ENSCAFG00000004157.
DR Ensembl; ENSCAFT00030025595; ENSCAFP00030022348; ENSCAFG00030013725.
DR Ensembl; ENSCAFT00040048535; ENSCAFP00040042399; ENSCAFG00040025936.
DR Ensembl; ENSCAFT00845034249; ENSCAFP00845026809; ENSCAFG00845019242.
DR GeneID; 404007; -.
DR KEGG; cfa:404007; -.
DR CTD; 7879; -.
DR VEuPathDB; HostDB:ENSCAFG00845019242; -.
DR VGNC; VGNC:45293; RAB7A.
DR eggNOG; KOG0394; Eukaryota.
DR GeneTree; ENSGT00940000155864; -.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; P18067; -.
DR OMA; KAMQHET; -.
DR OrthoDB; 1172019at2759; -.
DR TreeFam; TF105605; -.
DR Reactome; R-CFA-2132295; MHC class II antigen presentation.
DR Reactome; R-CFA-6798695; Neutrophil degranulation.
DR Reactome; R-CFA-8854214; TBC/RABGAPs.
DR Reactome; R-CFA-8873719; RAB geranylgeranylation.
DR Reactome; R-CFA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-CFA-9013148; CDC42 GTPase cycle.
DR Reactome; R-CFA-9013149; RAC1 GTPase cycle.
DR Reactome; R-CFA-9013404; RAC2 GTPase cycle.
DR Reactome; R-CFA-9013405; RHOD GTPase cycle.
DR Reactome; R-CFA-9013407; RHOH GTPase cycle.
DR Reactome; R-CFA-9013408; RHOG GTPase cycle.
DR Reactome; R-CFA-9013409; RHOJ GTPase cycle.
DR Reactome; R-CFA-9035034; RHOF GTPase cycle.
DR PRO; PR:P18067; -.
DR Proteomes; UP000002254; Chromosome 20.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IDA:SynGO-UCL.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
DR GO; GO:0032419; C:extrinsic component of lysosome membrane; ISS:GO_Central.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; ISS:GO_Central.
DR GO; GO:0005811; C:lipid droplet; ISS:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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:0099638; P:endosome to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0007174; P:epidermal growth factor catabolic process; IMP:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0061724; P:lipophagy; ISS:GO_Central.
DR GO; GO:0090383; P:phagosome acidification; ISS:UniProtKB.
DR GO; GO:0090385; P:phagosome-lysosome fusion; ISS:UniProtKB.
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 Acetylation; Autophagy; Cytoplasmic vesicle; Endosome; GTP-binding;
KW Hydrolase; Lipid degradation; Lipid droplet; Lipid metabolism; Lipoprotein;
KW Lysosome; Membrane; Methylation; Mitochondrion; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P51149"
FT CHAIN 2..207
FT /note="Ras-related protein Rab-7a"
FT /id="PRO_0000121120"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 34..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 63..67
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 156..157
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P51149"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51149"
FT MOD_RES 207
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 205
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 207
FT /note="S-geranylgeranyl cysteine"
FT /evidence="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
