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RAB20_MOUSE
ID   RAB20_MOUSE             Reviewed;         233 AA.
AC   P35295;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=Ras-related protein Rab-20;
GN   Name=Rab20;
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], AND SUBCELLULAR LOCATION.
RC   TISSUE=Kidney;
RX   PubMed=7706395; DOI=10.1242/jcs.107.12.3437;
RA   Luetcke A., Parton R.G., Murphy C., Olkkonen V.M., Dupree P., Valencia A.,
RA   Simons K., Zerial M.;
RT   "Cloning and subcellular localization of novel rab proteins reveals
RT   polarized and cell type-specific expression.";
RL   J. Cell Sci. 107:3437-3448(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.
RC   TISSUE=Kidney;
RX   PubMed=1555775; DOI=10.1016/0378-1119(92)90387-5;
RA   Chavrier P., Simons K., Zerial M.;
RT   "The complexity of the Rab and Rho GTP-binding protein subfamilies revealed
RT   by a PCR cloning approach.";
RL   Gene 112:261-264(1992).
CC   -!- FUNCTION: Plays a role in apical endocytosis/recycling. Plays a role in
CC       the maturation and acidification of phagosomes that engulf pathogens,
CC       such as S.aureus and Mycobacterium. Plays a role in the fusion of
CC       phagosomes with lysosomes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome
CC       {ECO:0000250|UniProtKB:Q9NX57}. Cytoplasmic vesicle, phagosome membrane
CC       {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC       {ECO:0000305}. Golgi apparatus {ECO:0000250|UniProtKB:Q9NX57}.
CC       Note=Recruited to phagosomes containing S.aureus or Mycobacterium (By
CC       similarity). Highly enriched on apical endocytic structures in
CC       polarized epithelial cells of kidney proximal tubules (PubMed:7706395).
CC       {ECO:0000250|UniProtKB:Q9NX57, ECO:0000269|PubMed:7706395}.
CC   -!- TISSUE SPECIFICITY: Present in a variety of tissues, but not in brain.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; X80332; CAA56582.1; -; mRNA.
DR   EMBL; M79310; AAK14834.1; -; mRNA.
DR   CCDS; CCDS22095.1; -.
DR   PIR; I48728; S46950.
DR   RefSeq; NP_035357.1; NM_011227.1.
DR   AlphaFoldDB; P35295; -.
DR   SMR; P35295; -.
DR   STRING; 10090.ENSMUSP00000033900; -.
DR   iPTMnet; P35295; -.
DR   PhosphoSitePlus; P35295; -.
DR   PaxDb; P35295; -.
DR   PRIDE; P35295; -.
DR   ProteomicsDB; 255064; -.
DR   Antibodypedia; 25565; 293 antibodies from 28 providers.
DR   DNASU; 19332; -.
DR   Ensembl; ENSMUST00000033900; ENSMUSP00000033900; ENSMUSG00000031504.
DR   GeneID; 19332; -.
DR   KEGG; mmu:19332; -.
DR   UCSC; uc009kvd.1; mouse.
DR   CTD; 55647; -.
DR   MGI; MGI:102789; Rab20.
DR   VEuPathDB; HostDB:ENSMUSG00000031504; -.
DR   eggNOG; KOG0092; Eukaryota.
DR   GeneTree; ENSGT00940000161024; -.
DR   HOGENOM; CLU_041217_12_0_1; -.
DR   InParanoid; P35295; -.
DR   OMA; HDCIYAL; -.
DR   OrthoDB; 1340129at2759; -.
DR   PhylomeDB; P35295; -.
DR   TreeFam; TF331574; -.
DR   Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR   BioGRID-ORCS; 19332; 3 hits in 72 CRISPR screens.
DR   ChiTaRS; Rab20; mouse.
DR   PRO; PR:P35295; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; P35295; protein.
DR   Bgee; ENSMUSG00000031504; Expressed in cleaving embryo and 137 other tissues.
DR   ExpressionAtlas; P35295; baseline and differential.
DR   Genevisible; P35295; MM.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
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   CDD; cd04126; Rab20; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041836; Rab20.
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   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW   Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..233
FT                   /note="Ras-related protein Rab-20"
FT                   /id="PRO_0000121203"
FT   REGION          119..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           33..41
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         55..59
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         113..116
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           231
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           232
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   233 AA;  25989 MW;  3A2E70A18D5280A9 CRC64;
     MRKPDGKIVL LGDMNVGKTS LLQRYMERRF PDTVSTVGGA FYLKQWRSFN ISIWDTAGRE
     QFHGLGSLYC RGAAAIILTY DVNHPQSLFE LEDRFLGLTE TANNDCLFAI VGNKVDLTSE
     RDTEGGEKEG PASGKVGSCV STKVPKQVQP EDAVALYKKI LKYKMLDERE MPAAEQMCFE
     TSAKTGYNVD LLFETLFDLV VPMIMRQRAE ESDQTVDIAS CKTPKQTRSG CCA
 
 
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