RAB7A_MOUSE
ID RAB7A_MOUSE Reviewed; 207 AA.
AC P51150;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Ras-related protein Rab-7a;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P51149};
GN Name=Rab7a; Synonyms=Rab7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8547311; DOI=10.1016/0167-4781(95)00188-3;
RA Vitelli R., Chiariello M., Bruni C.B., Bucci C.;
RT "Cloning and expression analysis of the murine Rab7 cDNA.";
RL Biochim. Biophys. Acta 1264:268-270(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 11-31; 70-79; 114-126 AND 147-157, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=12545426; DOI=10.1086/367847;
RA Verhoeven K., De Jonghe P., Coen K., Verpoorten N., Auer-Grumbach M.,
RA Kwon J.M., FitzPatrick D., Schmedding E., De Vriendt E., Jacobs A.,
RA Van Gerwen V., Wagner K., Hartung H.-P., Timmerman V.;
RT "Mutations in the small GTP-ase late endosomal protein RAB7 cause Charcot-
RT Marie-Tooth type 2B neuropathy.";
RL Am. J. Hum. Genet. 72:722-727(2003).
RN [6]
RP INTERACTION WITH RNF115.
RX PubMed=12972561; DOI=10.1091/mbc.e02-08-0495;
RA Mizuno K., Kitamura A., Sasaki T.;
RT "Rabring7, a novel Rab7 target protein with a RING finger motif.";
RL Mol. Biol. Cell 14:3741-3752(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP LACK OF INTERACTION WITH HPS4 AND 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 [10]
RP FUNCTION, INTERACTION WITH PRPH, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=23179371; DOI=10.1007/s00401-012-1063-8;
RA Cogli L., Progida C., Thomas C.L., Spencer-Dene B., Donno C., Schiavo G.,
RA Bucci C.;
RT "Charcot-Marie-Tooth type 2B disease-causing RAB7A mutant proteins show
RT altered interaction with the neuronal intermediate filament peripherin.";
RL Acta Neuropathol. 125:257-272(2013).
RN [11]
RP INTERACTION WITH C9ORF72.
RX PubMed=24549040; DOI=10.1093/hmg/ddu068;
RA Farg M.A., Sundaramoorthy V., Sultana J.M., Yang S., Atkinson R.A.,
RA Levina V., Halloran M.A., Gleeson P.A., Blair I.P., Soo K.Y., King A.E.,
RA Atkin J.D.;
RT "C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal
RT dementia, regulates endosomal trafficking.";
RL Hum. Mol. Genet. 23:3579-3595(2014).
RN [12]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=23708524; DOI=10.4161/auto.24893;
RA Lizaso A., Tan K.T., Lee Y.H.;
RT "beta-adrenergic receptor-stimulated lipolysis requires the RAB7-mediated
RT autolysosomal lipid degradation.";
RL Autophagy 9:1228-1243(2013).
RN [13]
RP INTERACTION WITH PLEKHM1.
RX PubMed=27777970; DOI=10.1172/jci.insight.86330;
RA Fujiwara T., Ye S., Castro-Gomes T., Winchell C.G., Andrews N.W.,
RA Voth D.E., Varughese K.I., Mackintosh S.G., Feng Y., Pavlos N.,
RA Nakamura T., Manolagas S.C., Zhao H.;
RT "PLEKHM1/DEF8/RAB7 complex regulates lysosome positioning and bone
RT homeostasis.";
RL JCI Insight 1:E86330-E86330(2016).
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. Plays a central role, not only in
CC endosomal traffic, but also in many other cellular and physiological
CC events, such as growth-factor-mediated cell signaling, nutrient-
CC transporter-mediated nutrient uptake, neurotrophin transport in the
CC axons of neurons and lipid metabolism. Also involved in regulation of
CC some specialized endosomal membrane trafficking, such as maturation of
CC melanosomes, pathogen-induced phagosomes (or vacuoles) and
CC autophagosomes. Plays a role in the maturation and acidification of
CC phagosomes that engulf pathogens, such as S.aureus and Mycobacteria.
CC Plays a role in the fusion of phagosomes with lysosomes. Plays
CC important roles in microbial pathogen infection and survival, as well
CC as in participating in the life cycle of viruses. Microbial pathogens
CC possess survival strategies governed by RAB7A, sometimes by employing
CC RAB7A function (e.g. Salmonella) and sometimes by excluding RAB7A
CC function (e.g. Mycobacterium). In concert with RAC1, plays a role in
CC regulating the formation of RBs (ruffled borders) in osteoclasts.
CC Controls the endosomal trafficking and neurite outgrowth signaling of
CC NTRK1/TRKA. Regulates the endocytic trafficking of the EGF-EGFR complex
CC by regulating its lysosomal degradation (By similarity). Involved in
CC the ADRB2-stimulated lipolysis through lipophagy, a cytosolic lipase-
CC independent autophagic pathway (PubMed:23708524). 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 (PubMed:23179371). {ECO:0000250|UniProtKB:P51149,
CC ECO:0000269|PubMed:23179371, ECO:0000269|PubMed:23708524}.
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), RILP (By
CC similarity), PSMA7 (By similarity), RNF115 (PubMed:12972561) and FYCO1
CC (By similarity). Interacts with the PIK3C3/VPS34-PIK3R4 complex (By
CC similarity). The GTP-bound form interacts with OSBPL1A and RAC1 (By
CC similarity). Interacts with CLN3 (By similarity). Interacts with CHM,
CC the substrate-binding subunit of the Rab geranylgeranyltransferase
CC complex (By similarity). Interacts with C9orf72 (PubMed:24549040). Does
CC not interact with HPS4 and the BLOC-3 complex (heterodimer of HPS1 and
CC HPS4) (PubMed:20048159). Interacts with CLN5 (By similarity). Interacts
CC with PLEKHM1 (via N- and C-terminus) (PubMed:27777970). Interacts with
CC RUFY4 (By similarity). Interacts with PRPH; the interaction is direct
CC (PubMed:23179371). Interacts with VPS13A (By similarity). The GDP-bound
CC form interacts with RIMOC1 (By similarity). Interacts with the MON1A-
CC CCZ1B complex and this interaction is enhanced in the presence of
CC RIMOC1 (By similarity). {ECO:0000250|UniProtKB:P09527,
CC ECO:0000250|UniProtKB:P51149, ECO:0000269|PubMed:12972561,
CC ECO:0000269|PubMed:20048159, ECO:0000269|PubMed:23179371,
CC ECO:0000269|PubMed:24549040, ECO:0000269|PubMed:27777970}.
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:0000269|PubMed:23708524}. Endosome membrane
CC {ECO:0000250|UniProtKB:P51149}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:23179371}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein
CC {ECO:0000305}. 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 (By
CC similarity). Recruited to phagosomes containing S.aureus or
CC Mycobacterium (By similarity). Lipid droplet localization is increased
CC upon ADRB2 stimulation (PubMed:23708524). Recruited to damaged
CC mitochondria during mitophagy in a RIMOC1-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:P51149,
CC ECO:0000269|PubMed:23708524}.
CC -!- TISSUE SPECIFICITY: Widely expressed. High expression in liver, heart
CC and kidney. Found in sensory and motor neurons.
CC {ECO:0000269|PubMed:12545426}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the dorsal root ganglia and the
CC sciatic nerve at 13.5 dpc (at protein level).
CC {ECO:0000269|PubMed:23179371}.
CC -!- DISRUPTION PHENOTYPE: Reduces both the basal and, to a greater degree,
CC agonist-stimulated glycerol releases. the ADRB2-stimulated liposlysis.
CC {ECO:0000269|PubMed:23708524}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X89650; CAA61797.1; -; mRNA.
DR EMBL; AK005004; BAB23738.1; -; mRNA.
DR EMBL; BC004597; AAH04597.1; -; mRNA.
DR EMBL; BC086793; AAH86793.1; -; mRNA.
DR CCDS; CCDS39552.1; -.
DR PIR; S62733; S62733.
DR RefSeq; NP_001280581.1; NM_001293652.1.
DR RefSeq; NP_001280582.1; NM_001293653.1.
DR RefSeq; NP_001280583.1; NM_001293654.1.
DR RefSeq; NP_001280584.1; NM_001293655.1.
DR RefSeq; NP_033031.2; NM_009005.3.
DR PDB; 5Z2M; X-ray; 2.14 A; A/C=1-176.
DR PDBsum; 5Z2M; -.
DR AlphaFoldDB; P51150; -.
DR SMR; P51150; -.
DR BioGRID; 202553; 46.
DR DIP; DIP-60513N; -.
DR IntAct; P51150; 14.
DR MINT; P51150; -.
DR STRING; 10090.ENSMUSP00000109230; -.
DR iPTMnet; P51150; -.
DR PhosphoSitePlus; P51150; -.
DR SwissPalm; P51150; -.
DR EPD; P51150; -.
DR jPOST; P51150; -.
DR PaxDb; P51150; -.
DR PeptideAtlas; P51150; -.
DR PRIDE; P51150; -.
DR ProteomicsDB; 255068; -.
DR ABCD; P51150; 21 sequenced antibodies.
DR Antibodypedia; 1885; 366 antibodies from 40 providers.
DR DNASU; 19349; -.
DR Ensembl; ENSMUST00000095048; ENSMUSP00000092658; ENSMUSG00000079477.
DR Ensembl; ENSMUST00000113596; ENSMUSP00000109226; ENSMUSG00000079477.
DR Ensembl; ENSMUST00000113597; ENSMUSP00000109227; ENSMUSG00000079477.
DR Ensembl; ENSMUST00000113598; ENSMUSP00000109228; ENSMUSG00000079477.
DR Ensembl; ENSMUST00000113600; ENSMUSP00000109230; ENSMUSG00000079477.
DR GeneID; 19349; -.
DR KEGG; mmu:19349; -.
DR UCSC; uc009cuv.2; mouse.
DR CTD; 19349; -.
DR MGI; MGI:105068; Rab7.
DR VEuPathDB; HostDB:ENSMUSG00000079477; -.
DR eggNOG; KOG0394; Eukaryota.
DR GeneTree; ENSGT00940000155864; -.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; P51150; -.
DR OMA; KAMQHET; -.
DR OrthoDB; 1172019at2759; -.
DR PhylomeDB; P51150; -.
DR TreeFam; TF105605; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 19349; 34 hits in 74 CRISPR screens.
DR ChiTaRS; Rab7; mouse.
DR PRO; PR:P51150; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P51150; protein.
DR Bgee; ENSMUSG00000079477; Expressed in secondary oocyte and 62 other tissues.
DR ExpressionAtlas; P51150; baseline and differential.
DR Genevisible; P51150; MM.
DR GO; GO:0097208; C:alveolar lamellar body; ISO:MGI.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0032419; C:extrinsic component of lysosome membrane; IDA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0031902; C:late endosome membrane; IDA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; IDA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
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:0034045; C:phagophore assembly site membrane; IDA:UniProtKB.
DR GO; GO:0030904; C:retromer complex; ISO:MGI.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:1905394; F:retromer complex binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0000045; P:autophagosome assembly; ISO:MGI.
DR GO; GO:0045453; P:bone resorption; ISO:MGI.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; ISO:MGI.
DR GO; GO:0099638; P:endosome to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0007174; P:epidermal growth factor catabolic process; ISO:MGI.
DR GO; GO:0051650; P:establishment of vesicle localization; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR GO; GO:0046907; P:intracellular transport; ISO:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0061724; P:lipophagy; IMP:GO_Central.
DR GO; GO:1903542; P:negative regulation of exosomal secretion; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0048524; P:positive regulation of viral process; ISO:MGI.
DR GO; GO:0006622; P:protein targeting to lysosome; ISO:MGI.
DR GO; GO:0022615; P:protein to membrane docking; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; ISO:MGI.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR GO; GO:0019076; P:viral release from host cell; ISO:MGI.
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 3D-structure; Acetylation; Autophagy; Cytoplasmic vesicle;
KW Direct protein sequencing; Endosome; GTP-binding; Hydrolase;
KW Lipid degradation; Lipid droplet; Lipid metabolism; Lipoprotein; Lysosome;
KW Membrane; Methylation; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Prenylation; Protein transport; Reference proteome; 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_0000121122"
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:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
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"
FT CONFLICT 145
FT /note="S -> R (in Ref. 1; CAA61797)"
FT /evidence="ECO:0000305"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:5Z2M"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:5Z2M"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:5Z2M"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:5Z2M"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:5Z2M"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:5Z2M"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:5Z2M"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:5Z2M"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:5Z2M"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:5Z2M"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:5Z2M"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:5Z2M"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:5Z2M"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:5Z2M"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5Z2M"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:5Z2M"
FT HELIX 162..174
FT /evidence="ECO:0007829|PDB:5Z2M"
SQ SEQUENCE 207 AA; 23490 MW; A2AF33B16A672971 CRC64;
MTSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV MVDDRLVTMQ
IWDTAGQERF QSLGVAFYRG ADCCVLVFDV TAPNTFKTLD SWRDEFLIQA SPRDPENFPF
VVLGNKIDLE NRQVATKRAQ AWCYSKNNIP YFETSAKEAI NVEQAFQTIA RNALKQETEV
ELYNEFPEPI KLDKNDRAKA SAESCSC
