RAB32_PIG
ID RAB32_PIG Reviewed; 226 AA.
AC Q06AU5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Ras-related protein Rab-32;
GN Name=RAB32;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Liu G.Y.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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. Plays a role in the maturation of phagosomes that engulf
CC pathogens, such as S.aureus and Mycobacterium. Plays an important role
CC in the control of melanin production and melanosome biogenesis. In
CC concert with RAB38, regulates the proper trafficking of melanogenic
CC enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes.
CC {ECO:0000250|UniProtKB:Q13637, ECO:0000250|UniProtKB:Q9CZE3}.
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. SGSM2 acts as its GAP and inactivates it by stimulating
CC its GTPase activity. {ECO:0000250|UniProtKB:Q9CZE3}.
CC -!- SUBUNIT: Interacts with ANKRD27. A decreased interaction with ANKRD27
CC seen in the presence of SGSM2 (By similarity).
CC {ECO:0000250|UniProtKB:Q13637, ECO:0000250|UniProtKB:Q9CZE3}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q13637}.
CC Mitochondrion outer membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q13637}.
CC Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome
CC {ECO:0000250|UniProtKB:Q9CZE3}. Melanosome membrane
CC {ECO:0000250|UniProtKB:Q13637}. Note=Recruited to phagosomes containing
CC S.aureus or M.tuberculosis. The BLOC-3 complex, a heterodimer of HPS1
CC and HPS4 promotes its membrane localization.
CC {ECO:0000250|UniProtKB:Q13637}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; DQ917630; ABI97175.1; -; mRNA.
DR RefSeq; NP_001116648.1; NM_001123176.1.
DR AlphaFoldDB; Q06AU5; -.
DR SMR; Q06AU5; -.
DR STRING; 9823.ENSSSCP00000004449; -.
DR PaxDb; Q06AU5; -.
DR PeptideAtlas; Q06AU5; -.
DR GeneID; 100144496; -.
DR KEGG; ssc:100144496; -.
DR CTD; 10981; -.
DR eggNOG; KOG4423; Eukaryota.
DR InParanoid; Q06AU5; -.
DR OrthoDB; 1240760at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0042470; C:melanosome; ISS:UniProtKB.
DR GO; GO:0033162; C:melanosome membrane; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; ISS: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:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:1903232; P:melanosome assembly; ISS:UniProtKB.
DR GO; GO:0032438; P:melanosome organization; IBA:GO_Central.
DR GO; GO:0090382; P:phagosome maturation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasmic vesicle; GTP-binding; Lipoprotein; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13637"
FT CHAIN 2..226
FT /note="Ras-related protein Rab-32"
FT /id="PRO_0000288610"
FT REGION 180..199
FT /note="PKA-RII subunit binding domain"
FT /evidence="ECO:0000250"
FT REGION 202..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 56..64
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT COMPBIAS 204..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34..41
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 83..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 145..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q13637"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13637"
FT LIPID 225
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 226
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 226 AA; 25005 MW; D13ED58E8B6FC084 CRC64;
MAGGGAGDPG QGAAAAAAAA PETREHLFKV LVIGELGVGK TSIIKRYVHQ LFSQHYRATI
GVDFALKVLN WDSRTLVRLQ LWDIAGQERF GNMTRVYYKE AVGALVVFDI SRGSPFEAVL
KWKNDLDSKV HLPNGSPIPA VLLANKCDQK KDSGQNPSQM DQFCKEHGFT GWFETSAKDN
INIDEAARFL VENILANHQS FPSEENDGRI KLDEETMKKE NKSHCC
