| IED ID |
IndEnz0016000038 |
| Enzyme Type ID |
tyrosinase000038 |
| Protein Name |
Ras-related protein Rab-38
|
| Gene Name |
Rab38 |
| 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 |
MQTPHKEHLYKLLVIGDLGVGKTSIIKRYVHQNFSSHYRATIGVDFALKVLHWDPETVVRLQLWDIAGQERFGNMTRVYYREAMGAFIVFDVTRPATFEAVAKWKNDLDSKLTLPNGKPVSVVLLANKCDQGKDVLMNNGLKMDQFCKEHGFVGWFETSAKENINIDEASRCLVKHILANECDLLESIEPDIVKPHLTSPKVVSCSGCAKS |
| Enzyme Length |
211 |
| Uniprot Accession Number |
Q8QZZ8 |
| 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: Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and Mycobacterium (By similarity). May be involved in melanosomal transport and docking. Involved in the proper sorting of TYRP1. Involved in peripheral melanosomal distribution of TYRP1 in melanocytes; the function, which probably is implicating vesicle-trafficking, includes cooperation with ANKRD27 and VAMP7 (PubMed:21187289). Plays an important role in the control of melanin production and melanosome biogenesis (By similarity). In concert with RAB32, regulates the proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes (PubMed:26620560). {ECO:0000250|UniProtKB:P57729, ECO:0000269|PubMed:21187289, ECO:0000269|PubMed:26620560}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
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| nucleotide Binding |
NP_BIND 16..23; /note=GTP; /evidence=ECO:0000250; NP_BIND 65..69; /note=GTP; /evidence=ECO:0000250; NP_BIND 127..130; /note=GTP; /evidence=ECO:0000250 |
| Features |
Chain (1); Lipidation (2); Motif (1); Mutagenesis (2); Natural variant (1); Nucleotide binding (3); Sequence conflict (3) |
| Keywords |
Albinism;Cell membrane;Cytoplasmic vesicle;Disease variant;GTP-binding;Lipoprotein;Membrane;Nucleotide-binding;Palmitate;Prenylation;Protein transport;Reference proteome;Transport |
| Interact With |
Q3UMR0 |
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P57729}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome {ECO:0000269|PubMed:26620560}. Melanosome membrane {ECO:0000250|UniProtKB:P57729}. 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:P57729}. |
| Modified Residue |
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| 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;
17043139;
17671165;
17724166;
1835927;
18477474;
18715234;
18832574;
19403694;
19493314;
21267068;
22660928;
22985540;
23426636;
24127780;
25360523;
25685662;
26876013;
28438206;
31399401;
8422502;
9585243;
|
| Motif |
MOTIF 38..46; /note=Effector region; /evidence=ECO:0000250 |
| Gene Encoded By |
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| Mass |
23,776 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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