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Melanocyte protein PMEL (Melanocyte protein Pmel 17) (Premelanosome protein) (Silver locus protein) [Cleaved into: M-alpha; M-beta]

 PMEL_MOUSE              Reviewed;         626 AA.
Q60696;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-FEB-2018, entry version 112.
RecName: Full=Melanocyte protein PMEL;
AltName: Full=Melanocyte protein Pmel 17;
AltName: Full=Premelanosome protein;
AltName: Full=Silver locus protein;
Contains:
RecName: Full=M-alpha;
Contains:
RecName: Full=M-beta;
Flags: Precursor;
Name=Pmel; Synonyms=D10H12S53E, Pmel17, Si, Silv;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SILVER.
STRAIN=C57BL/6J; TISSUE=Skin;
PubMed=7870580; DOI=10.1093/nar/23.1.154;
Kwon B.S., Halaban R., Ponnazhagan S., Kim K., Chintamaneni C.,
Bennett D., Pickard R.T.;
"Mouse silver mutation is caused by a single base insertion in the
putative cytoplasmic domain of Pmel 17.";
Nucleic Acids Res. 23:154-158(1995).
[2]
PROTEOLYTIC PROCESSING.
PubMed=11694580; DOI=10.1091/mbc.12.11.3451;
Berson J.F., Harper D.C., Tenza D., Raposo G., Marks M.S.;
"Pmel17 initiates premelanosome morphogenesis within multivesicular
bodies.";
Mol. Biol. Cell 12:3451-3464(2001).
-!- 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}.
-!- SUBUNIT: Heterooligomer; disulfide-linked heterooligomers of M-
alpha and M-beta. Interacts with MLANA. Interacts (via luminal
domain) with CD63; this is important for normal sorting of the
luminal domain after proteolytic processing (By similarity).
{ECO:0000250}.
-!- 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}.
-!- TISSUE SPECIFICITY: Preferentially expressed in melanocytes.
-!- DOMAIN: The RPT domain is essential for the generation of the
fibrillar matrix of melanosomes. {ECO:0000250}.
-!- DOMAIN: The lumenal domain is necessary for correct processing and
trafficking to melanosomes. {ECO:0000250}.
-!- 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}.
-!- DISEASE: Note=Defects in Silv are the cause of the silver coat
color which seems to be due to premature death of pigment cells
during the hair cycle.
-!- SIMILARITY: Belongs to the PMEL/NMB family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U14133; AAA69538.1; -; mRNA.
PIR; S53871; S53871.
UniGene; Mm.16756; -.
UniGene; Mm.444804; -.
ProteinModelPortal; Q60696; -.
SMR; Q60696; -.
STRING; 10090.ENSMUSP00000051869; -.
iPTMnet; Q60696; -.
PhosphoSitePlus; Q60696; -.
PaxDb; Q60696; -.
PRIDE; Q60696; -.
MGI; MGI:98301; Pmel.
eggNOG; ENOG410IHN4; Eukaryota.
eggNOG; ENOG410Z44K; LUCA.
HOVERGEN; HBG099694; -.
InParanoid; Q60696; -.
PhylomeDB; Q60696; -.
ChiTaRS; Pmel; mouse.
PRO; PR:Q60696; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_SI; -.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0042470; C:melanosome; IDA:MGI.
GO; GO:0032585; C:multivesicular body membrane; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0048066; P:developmental pigmentation; IBA:GO_Central.
GO; GO:0042438; P:melanin biosynthetic process; IMP:MGI.
GO; GO:0032438; P:melanosome organization; ISO:MGI.
GO; GO:0048023; P:positive regulation of melanin biosynthetic process; IMP:CACAO.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR022409; PKD/Chitinase_dom.
InterPro; IPR000601; PKD_dom.
InterPro; IPR035986; PKD_dom_sf.
Pfam; PF00801; PKD; 1.
SMART; SM00089; PKD; 1.
SUPFAM; SSF49299; SSF49299; 1.
PROSITE; PS50093; PKD; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Complete proteome;
Disease mutation; Disulfide bond; Endoplasmic reticulum; Endosome;
Glycoprotein; Golgi apparatus; Melanin biosynthesis; Membrane;
Reference proteome; Repeat; Secreted; Sialic acid; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 626 Melanocyte protein PMEL.
/FTId=PRO_0000024713.
CHAIN 25 434 M-alpha. {ECO:0000250}.
/FTId=PRO_0000386649.
CHAIN 437 626 M-beta. {ECO:0000250}.
/FTId=PRO_0000386650.
TOPO_DOM 437 562 Lumenal. {ECO:0000255}.
TRANSMEM 563 583 Helical. {ECO:0000255}.
TOPO_DOM 584 626 Cytoplasmic. {ECO:0000255}.
DOMAIN 255 292 PKD. {ECO:0000255|PROSITE-
ProRule:PRU00151}.
REPEAT 315 327 1.
REPEAT 328 340 2.
REPEAT 341 353 3.
REPEAT 354 366 4.
REPEAT 367 379 5.
REPEAT 380 392 6.
REPEAT 393 411 7.
REGION 315 411 7 X 13 AA approximate tandem repeats, RPT
domain.
CARBOHYD 81 81 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 535 535 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 170 170 S -> L (in silver).
VARIANT 175 175 R -> G (in silver).
VARIANT 373 373 D -> N (in silver).
VARIANT 471 471 F -> S (in silver).
VARIANT 603 626 AAPASGLRARGLGENSPLLSGQQV -> SSASLRSSRPRPW
RKQPAPQWTAGLIILKAPWISWG (in silver).
SEQUENCE 626 AA; 65980 MW; 7AB941D2E3FB1044 CRC64;
MVGVQRRSFL PVLVLSALLA VGALEGSRNQ DWLGVPRQLV TKTWNRQLYP EWTEVQGSNC
WRGGQVSLRV INDGPTLVGA NASFSIALHF PGSQKVLPDG QVIWANNTII NGSQVWGGQP
VYPQEPDDAC VFPDGGPCPS GPKPPKRSFV YVWKTWGKYW QVLGGPVSRS SIATRHAKLG
THTMEVTVYH RRGSQSYVPL AHASSTFTIT DQVPFSVSVS QLQALDGETK HFLRNHPLIF
ALQLHDPSGY LAEADLSYTW DFGDGTGTLI SRALDVTHTY LESGSVTAQV VLQAAIPLVS
CGSSPVPGTT DGYMPTAEAP GTTSRQGTTT KVVGTTPGQM PTTQPSGTTV VQMPTTEVTA
TTSEQMLTSA VIDTTLAEVS TTEGTGTTPT RPSGTTVAQA TTTEGPDASP LLPTQSSTGS
ISPLLDDTDT IMLVKRQVPL DCVLYRYGSF SLALDIVQGI ESAEILQAVP FSEGDAFELT
VSCQGGLPKE ACMDISSPGC QPPAQRLCQS VPPSPDCQLV LHQVLKGGSG TYCLNVSLAD
ANSLAVASTQ LVVPGQDGGL GQAPLLVGIL LVLVAVVLAS LILGIDLRSR AQFPKCHMVA
LTAAPASGLR ARGLGENSPL LSGQQV


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