| 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 |
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| 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 |
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| PH Dependency |
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| 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 |
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| Signal Peptide |
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| Structure 3D |
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| 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 |
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| Mass |
25,068 |
| Kinetics |
|
| Metal Binding |
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| Rhea ID |
|
| Cross Reference Brenda |
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