RAB32_HUMAN
ID RAB32_HUMAN Reviewed; 225 AA.
AC Q13637;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Ras-related protein Rab-32;
GN Name=RAB32;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Burke S., Seabra M.C.;
RT "Cloning of novel Rab proteins with the yeast two-hybrid system.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP PROTEIN SEQUENCE OF 2-22; 28-38; 66-72; 77-87; 111-119; 128-144; 164-186
RP AND 211-217, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-225, TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF GLN-85.
RC TISSUE=Platelet;
RX PubMed=11784320; DOI=10.1046/j.0014-2956.2001.02645.x;
RA Bao X., Faris A.E., Jang E.K., Haslam R.J.;
RT "Molecular cloning, bacterial expression and properties of Rab31 and
RT Rab32.";
RL Eur. J. Biochem. 269:259-271(2002).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP THR-39; ALA-185 AND LEU-188.
RX PubMed=12186851; DOI=10.1083/jcb.200204081;
RA Alto N.M., Soderling J., Scott J.D.;
RT "Rab32 is an A-kinase anchoring protein and participates in mitochondrial
RT dynamics.";
RL J. Cell Biol. 158:659-668(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP INTERACTION WITH ANKRD27, AND ACTIVITY REGULATION.
RX PubMed=21808068; DOI=10.1074/jbc.m111.261115;
RA Nottingham R.M., Ganley I.G., Barr F.A., Lambright D.G., Pfeffer S.R.;
RT "RUTBC1 protein, a Rab9A effector that activates GTP hydrolysis by Rab32
RT and Rab33B proteins.";
RL J. Biol. Chem. 286:33213-33222(2011).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x;
RA Seto S., Tsujimura K., Koide Y.;
RT "Rab GTPases regulating phagosome maturation are differentially recruited
RT to mycobacterial phagosomes.";
RL Traffic 12:407-420(2011).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23084991; DOI=10.1016/j.cub.2012.09.020;
RA Gerondopoulos A., Langemeyer L., Liang J.R., Linford A., Barr F.A.;
RT "BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine
RT nucleotide exchange factor.";
RL Curr. Biol. 22:2135-2139(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-225 IN COMPLEX WITH ANKRD27, AND
RP MUTAGENESIS OF GLY-89; ASN-90; MET-91; ARG-93 AND VAL-94.
RX PubMed=24856514; DOI=10.1016/j.devcel.2014.04.010;
RA Hesketh G.G., Perez-Dorado I., Jackson L.P., Wartosch L., Schafer I.B.,
RA Gray S.R., McCoy A.J., Zeldin O.B., Garman E.F., Harbour M.E., Evans P.R.,
RA Seaman M.N., Luzio J.P., Owen D.J.;
RT "VARP is recruited on to endosomes by direct interaction with retromer,
RT where together they function in export to the cell surface.";
RL Dev. Cell 29:591-606(2014).
CC -!- FUNCTION: Acts as an A-kinase anchoring protein by binding to the type
CC II regulatory subunit of protein kinase A and anchoring it to the
CC mitochondrion. Also involved in synchronization of mitochondrial
CC fission (PubMed:12186851). Plays a role in the maturation of phagosomes
CC that engulf pathogens, such as S.aureus and M.tuberculosis
CC (PubMed:21255211). Plays an important role in the control of melanin
CC production and melanosome biogenesis (PubMed:23084991). In concert with
CC RAB38, regulates the proper trafficking of melanogenic enzymes TYR,
CC TYRP1 and DCT/TYRP2 to melanosomes in melanocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q9CZE3, ECO:0000269|PubMed:12186851,
CC ECO:0000269|PubMed:21255211, ECO:0000269|PubMed:23084991}.
CC -!- ACTIVITY REGULATION: Regulated by a guanine nucleotide-exchange factor
CC (GEF) and a GTPase-activating protein (GAP) and alternates between an
CC inactive GDP-bound and an active GTP-bound form. The BLOC-3 complex
CC composed of HPS1 and HPS4 acts as its GEF, promotes the exchange of GDP
CC to GTP, converting it from an inactive GDP-bound form into an active
CC GTP-bound form (By similarity). SGSM2 acts as its GAP and inactivates
CC it by stimulating its GTPase activity (PubMed:21269460).
CC {ECO:0000250|UniProtKB:Q9CZE3}.
CC -!- SUBUNIT: Interacts with ANKRD27 (PubMed:24856514, PubMed:21269460). A
CC decreased interaction with ANKRD27 seen in the presence of SGSM2
CC (PubMed:21269460). {ECO:0000269|PubMed:24856514}.
CC -!- INTERACTION:
CC Q13637; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-9837586, EBI-742054;
CC Q13637; A0A087WWI0: LRMDA; NbExp=3; IntAct=EBI-9837586, EBI-18393842;
CC Q13637; Q5S007: LRRK2; NbExp=12; IntAct=EBI-9837586, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12186851}.
CC Mitochondrion outer membrane {ECO:0000269|PubMed:23084991,
CC ECO:0000305|PubMed:12186851}; Lipid-anchor
CC {ECO:0000305|PubMed:12186851}. Cytoplasmic vesicle, phagosome
CC {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Melanosome {ECO:0000250|UniProtKB:Q9CZE3}. Melanosome
CC membrane {ECO:0000269|PubMed:23084991}. Note=Recruited to phagosomes
CC containing S.aureus or M.tuberculosis (PubMed:21255211). The BLOC-3
CC complex, a heterodimer of HPS1 and HPS4 promotes its membrane
CC localization (PubMed:23084991). {ECO:0000269|PubMed:21255211,
CC ECO:0000269|PubMed:23084991}.
CC -!- TISSUE SPECIFICITY: Widely expressed with high levels in heart, liver,
CC kidney, bone marrow, testis, colon and fetal lung.
CC {ECO:0000269|PubMed:11784320, ECO:0000269|PubMed:12186851}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; U71127; AAB09599.1; -; mRNA.
DR EMBL; AF498958; AAM21106.1; -; mRNA.
DR EMBL; BT020016; AAV38819.1; -; mRNA.
DR EMBL; AL133539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015061; AAH15061.1; -; mRNA.
DR EMBL; U59878; AAB02833.1; -; mRNA.
DR CCDS; CCDS5210.1; -.
DR RefSeq; NP_006825.1; NM_006834.4.
DR PDB; 4CYM; X-ray; 2.80 A; A/B/C=1-225.
DR PDB; 4CZ2; X-ray; 2.97 A; A/B/C=1-225.
DR PDB; 5OEC; X-ray; 2.30 A; B=20-201.
DR PDB; 5OED; X-ray; 2.90 A; B=20-201.
DR PDB; 6FF8; X-ray; 2.13 A; A/B=20-198.
DR PDBsum; 4CYM; -.
DR PDBsum; 4CZ2; -.
DR PDBsum; 5OEC; -.
DR PDBsum; 5OED; -.
DR PDBsum; 6FF8; -.
DR AlphaFoldDB; Q13637; -.
DR SMR; Q13637; -.
DR BioGRID; 116177; 69.
DR DIP; DIP-61889N; -.
DR IntAct; Q13637; 41.
DR MINT; Q13637; -.
DR STRING; 9606.ENSP00000356465; -.
DR GlyGen; Q13637; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13637; -.
DR PhosphoSitePlus; Q13637; -.
DR BioMuta; RAB32; -.
DR DMDM; 2833245; -.
DR EPD; Q13637; -.
DR jPOST; Q13637; -.
DR MassIVE; Q13637; -.
DR MaxQB; Q13637; -.
DR PaxDb; Q13637; -.
DR PeptideAtlas; Q13637; -.
DR PRIDE; Q13637; -.
DR ProteomicsDB; 59632; -.
DR Antibodypedia; 19849; 184 antibodies from 29 providers.
DR DNASU; 10981; -.
DR Ensembl; ENST00000367495.4; ENSP00000356465.3; ENSG00000118508.5.
DR GeneID; 10981; -.
DR KEGG; hsa:10981; -.
DR MANE-Select; ENST00000367495.4; ENSP00000356465.3; NM_006834.5; NP_006825.1.
DR UCSC; uc003qln.2; human.
DR CTD; 10981; -.
DR DisGeNET; 10981; -.
DR GeneCards; RAB32; -.
DR HGNC; HGNC:9772; RAB32.
DR HPA; ENSG00000118508; Tissue enhanced (bone).
DR MIM; 612906; gene.
DR neXtProt; NX_Q13637; -.
DR OpenTargets; ENSG00000118508; -.
DR PharmGKB; PA34123; -.
DR VEuPathDB; HostDB:ENSG00000118508; -.
DR eggNOG; KOG4423; Eukaryota.
DR GeneTree; ENSGT00940000162477; -.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; Q13637; -.
DR OMA; HQSFPSE; -.
DR OrthoDB; 1240760at2759; -.
DR PhylomeDB; Q13637; -.
DR TreeFam; TF324491; -.
DR PathwayCommons; Q13637; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q13637; -.
DR SIGNOR; Q13637; -.
DR BioGRID-ORCS; 10981; 9 hits in 1081 CRISPR screens.
DR GenomeRNAi; 10981; -.
DR Pharos; Q13637; Tbio.
DR PRO; PR:Q13637; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q13637; protein.
DR Bgee; ENSG00000118508; Expressed in monocyte and 157 other tissues.
DR Genevisible; Q13637; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042470; C:melanosome; IDA:ParkinsonsUK-UCL.
DR GO; GO:0033162; C:melanosome membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0035650; F:AP-1 adaptor complex binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0035651; F:AP-3 adaptor complex binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0036461; F:BLOC-2 complex binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0005525; F:GTP binding; NAS:ParkinsonsUK-UCL.
DR GO; GO:0030742; F:GTP-dependent protein binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0019882; P:antigen processing and presentation; IMP:UniProtKB.
DR GO; GO:0035646; P:endosome to melanosome transport; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:1903232; P:melanosome assembly; IDA:UniProtKB.
DR GO; GO:0032438; P:melanosome organization; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0090382; P:phagosome maturation; IMP:UniProtKB.
DR GO; GO:0072657; P:protein localization to membrane; IMP:ParkinsonsUK-UCL.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd04107; Rab32_Rab38; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR030697; Rab29/Rab38/Rab32.
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; Cytoplasmic vesicle; Direct protein sequencing;
KW GTP-binding; Lipoprotein; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Phosphoprotein;
KW Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25489052, ECO:0000269|Ref.6,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..225
FT /note="Ras-related protein Rab-32"
FT /id="PRO_0000121235"
FT REGION 178..197
FT /note="PKA-RII subunit binding domain"
FT MOTIF 54..62
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 32..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 143..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:25489052, ECO:0000269|Ref.6,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT LIPID 224
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 225
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 39
FT /note="T->N: Decreased GTP-binding activity."
FT /evidence="ECO:0000269|PubMed:12186851"
FT MUTAGEN 85
FT /note="Q->L: No change in GTPase activity."
FT /evidence="ECO:0000269|PubMed:11784320"
FT MUTAGEN 89
FT /note="G->T: Impairs interaction with ANKRD27; when
FT associated with S-90 and L-94."
FT /evidence="ECO:0000269|PubMed:24856514"
FT MUTAGEN 90
FT /note="N->S: Impairs interaction with ANKRD27; when
FT associated with T-89 and L-94."
FT /evidence="ECO:0000269|PubMed:24856514"
FT MUTAGEN 91
FT /note="M->S: Impairs interaction with ANKRD27; when
FT associated with S-93."
FT /evidence="ECO:0000269|PubMed:24856514"
FT MUTAGEN 93
FT /note="R->S: Impairs interaction with ANKRD27; when
FT associated with M-91."
FT /evidence="ECO:0000269|PubMed:24856514"
FT MUTAGEN 94
FT /note="V->L: Impairs interaction with ANKRD27; when
FT associated with T-89 and S-90."
FT /evidence="ECO:0000269|PubMed:24856514"
FT MUTAGEN 185
FT /note="A->F: Abolishes binding to protein kinase A type II
FT regulatory subunit."
FT /evidence="ECO:0000269|PubMed:12186851"
FT MUTAGEN 188
FT /note="L->P: Abolishes binding to protein kinase A type II
FT regulatory subunit."
FT /evidence="ECO:0000269|PubMed:12186851"
FT STRAND 22..33
FT /evidence="ECO:0007829|PDB:6FF8"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:6FF8"
FT STRAND 59..70
FT /evidence="ECO:0007829|PDB:6FF8"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:6FF8"
FT HELIX 84..88
FT /evidence="ECO:0007829|PDB:6FF8"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:6FF8"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:6FF8"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:6FF8"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6FF8"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:6FF8"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:6FF8"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:6FF8"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:6FF8"
FT HELIX 181..197
FT /evidence="ECO:0007829|PDB:6FF8"
SQ SEQUENCE 225 AA; 24997 MW; 91D41BAC1E3434CA CRC64;
MAGGGAGDPG LGAAAAPAPE TREHLFKVLV IGELGVGKTS IIKRYVHQLF SQHYRATIGV
DFALKVLNWD SRTLVRLQLW DIAGQERFGN MTRVYYKEAV GAFVVFDISR SSTFEAVLKW
KSDLDSKVHL PNGSPIPAVL LANKCDQNKD SSQSPSQVDQ FCKEHGFAGW FETSAKDNIN
IEEAARFLVE KILVNHQSFP NEENDVDKIK LDQETLRAEN KSQCC
