Detail Information for IndEnz0016000037
IED ID IndEnz0016000037
Enzyme Type ID tyrosinase000037
Protein Name Ras-related protein Rab-32
Gene Name Rab32
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MAGEGLGQQGASATAAPETREHLFKVLVIGELGVGKTSIIKRYVHQLFSQHYRATIGVDFALKVLNWDSRTLVRLQLWDIAGQERFGNMTRVYYKEALGAFVVFDISRSSTFDAVLKWKNDLDSKVHLPNGSPIPAVLLANKCDQKKDNSQSPSQMDQFCKDHGFTGWFETSAKDNINIDEATRFLVENMLANQQSFPSEEIDLDRIKLVEEPPTTKPRSQCC
Enzyme Length 223
Uniprot Accession Number Q9CZE3
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Regulated by a guanine nucleotide-exchange factor (GEF) and a GTPase-activating protein (GAP) and alternates between an inactive GDP-bound and an active GTP-bound form. The BLOC-3 complex composed of HPS1 and HPS4 acts as its GEF, promotes the exchange of GDP to GTP, converting it from an inactive GDP-bound form into an active GTP-bound form. SGSM2 acts as its GAP and inactivates it by stimulating its GTPase activity (PubMed:26620560). {ECO:0000269|PubMed:26620560}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Acts as an A-kinase anchoring protein by binding to the type II regulatory subunit of protein kinase A and anchoring it to the mitochondrion. Also involved in synchronization of mitochondrial fission. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and Mycobacterium (By similarity). Plays an important role in the control of melanin production and melanosome biogenesis (By similarity). In concert with RAB38, regulates the proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes (PubMed:26620560). {ECO:0000250|UniProtKB:Q13637, ECO:0000269|PubMed:26620560}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 30..37; /note=GTP; /evidence=ECO:0000250; NP_BIND 79..83; /note=GTP; /evidence=ECO:0000250; NP_BIND 141..144; /note=GTP; /evidence=ECO:0000250
Features Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (2); Motif (1); Mutagenesis (2); Nucleotide binding (3); Region (1); Sequence conflict (3)
Keywords Acetylation;Cytoplasmic vesicle;GTP-binding;Lipoprotein;Membrane;Mitochondrion;Mitochondrion outer membrane;Nucleotide-binding;Phosphoprotein;Prenylation;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q13637}. Mitochondrion outer membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q13637}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome {ECO:0000269|PubMed:26620560}. Melanosome membrane {ECO:0000250|UniProtKB:Q13637}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis. The BLOC-3 complex, a heterodimer of HPS1 and HPS4 promotes its membrane localization. {ECO:0000250|UniProtKB:Q13637}.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:Q13637; MOD_RES 69; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q13637
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10725249; 11217851; 12466851; 18614015; 21267068; 21677750; 24194600; 26275310; 26885862; 27626380; 30333037; 30338217; 31399401; 32703879;
Motif MOTIF 52..60; /note=Effector region; /evidence=ECO:0000250
Gene Encoded By
Mass 25,068
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda