| IED ID | IndEnz0009000182 |
| Enzyme Type ID | chitinase000182 |
| Protein Name |
Melanocyte protein PMEL Melanocyte protein Pmel 17 Premelanosome protein Silver locus protein Cleaved into: M-alpha; M-beta |
| Gene Name | Pmel D10H12S53E Pmel17 Si Silv |
| 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 | MVGVQRRSFLPVLVLSALLAVGALEGSRNQDWLGVPRQLVTKTWNRQLYPEWTEVQGSNCWRGGQVSLRVINDGPTLVGANASFSIALHFPGSQKVLPDGQVIWANNTIINGSQVWGGQPVYPQEPDDACVFPDGGPCPSGPKPPKRSFVYVWKTWGKYWQVLGGPVSRSSIATRHAKLGTHTMEVTVYHRRGSQSYVPLAHASSTFTITDQVPFSVSVSQLQALDGETKHFLRNHPLIFALQLHDPSGYLAEADLSYTWDFGDGTGTLISRALDVTHTYLESGSVTAQVVLQAAIPLVSCGSSPVPGTTDGYMPTAEAPGTTSRQGTTTKVVGTTPGQMPTTQPSGTTVVQMPTTEVTATTSEQMLTSAVIDTTLAEVSTTEGTGTTPTRPSGTTVAQATTTEGPDASPLLPTQSSTGSISPLLDDTDTIMLVKRQVPLDCVLYRYGSFSLALDIVQGIESAEILQAVPFSEGDAFELTVSCQGGLPKEACMDISSPGCQPPAQRLCQSVPPSPDCQLVLHQVLKGGSGTYCLNVSLADANSLAVASTQLVVPGQDGGLGQAPLLVGILLVLVAVVLASLILGIDLRSRAQFPKCHMVALTAAPASGLRARGLGENSPLLSGQQV |
| Enzyme Length | 626 |
| Uniprot Accession Number | Q60696 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Plays a central role in the biogenesis of melanosomes. Involved in the maturation of melanosomes from stage I to II. The transition from stage I melanosomes to stage II melanosomes involves an elongation of the vesicle, and the appearance within of distinct fibrillar structures (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (3); Domain (1); Glycosylation (4); Natural variant (5); Region (3); Repeat (7); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Cleavage on pair of basic residues;Disease variant;Disulfide bond;Endoplasmic reticulum;Endosome;Glycoprotein;Golgi apparatus;Melanin biosynthesis;Membrane;Reference proteome;Repeat;Secreted;Sialic acid;Signal;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus {ECO:0000250}. Melanosome {ECO:0000250}. Endosome, multivesicular body {ECO:0000250}. Note=Localizes predominantly to intralumenal vesicles (ILVs) within multivesicular bodies. Associates with ILVs found within the lumen of premelanosomes and melanosomes and particularly in compartments that serve as precursors to the striated stage II premelanosomes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [M-alpha]: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: A small amount of P1/P100 (major form) undergoes glycosylation to yield P2/P120 (minor form). P2 is cleaved by a furin-like proprotein convertase (PC) in a pH-dependent manner in a post-Golgi, prelysosomal compartment into two disulfide-linked subunits: a large lumenal subunit, M-alpha/ME20-S, and an integral membrane subunit, M-beta. Despite cleavage, only a small fraction of M-alpha is secreted, whereas most M-alpha and M-beta remain associated with each other intracellularly. M-alpha is further processed to M-alpha N and M-alpha C. M-alpha C further undergoes processing to yield M-alpha C1 and M-alpha C3 (M-alpha C2 in the case of PMEL17-is or PMEL17-ls). Formation of intralumenal fibrils in the melanosomes requires the formation of M-alpha that becomes incorporated into the fibrils. Stage II melanosomes harbor only Golgi-modified Pmel17 fragments that are derived from M-alpha and that bear sialylated O-linked oligosaccharides (By similarity). {ECO:0000250}.; PTM: N-glycosylated. O-glycosylated; contains sialic acid (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10594241; 11092553; 11217851; 11266470; 11277491; 12466851; 14610273; 14643677; 14681479; 16141072; 16185282; 16332269; 16412618; 16760433; 18397875; 18454205; 18715234; 18799693; 1912584; 1924386; 19493314; 19576202; 19659570; 19679373; 21610032; 21677750; 21949658; 22706087; 23203930; 23333945; 23382688; 23754390; 24218449; 24650003; 24769727; 24875170; 25633711; 25792196; 26732977; 26876013; 28249010; 28334846; 28746871; 30635393; 7479744; 7558008; 7665913; 7738386; 7761347; 7961886; 8041749; 8288218; 8432998; 8570653; 8592076; 8617263; 8617992; 8739560; 9101410; |
| Motif | |
| Gene Encoded By | |
| Mass | 65,980 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |