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Protein

Melanocyte protein PMEL

Gene

Pmel

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Biological processi

  • developmental pigmentation Source: GO_Central
  • melanin biosynthetic process Source: MGI
  • melanosome organization Source: MGI
  • positive regulation of melanin biosynthetic process Source: CACAO
Complete GO annotation...

Keywords - Biological processi

Melanin biosynthesis

Keywords - Ligandi

Sialic acid

Names & Taxonomyi

Protein namesi
Recommended name:
Melanocyte protein PMEL
Alternative name(s):
Melanocyte protein Pmel 17
Premelanosome protein
Silver locus protein
Cleaved into the following 2 chains:
Gene namesi
Name:Pmel
Synonyms:D10H12S53E, Pmel17, Si, Silv
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:98301. Pmel.

Subcellular locationi

M-alpha :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini437 – 562126LumenalSequence analysisAdd
BLAST
Transmembranei563 – 58321HelicalSequence analysisAdd
BLAST
Topological domaini584 – 62643CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

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.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 626602Melanocyte protein PMELPRO_0000024713Add
BLAST
Chaini25 – 434410M-alphaBy similarityPRO_0000386649Add
BLAST
Chaini437 – 626190M-betaBy similarityPRO_0000386650Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence analysis
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence analysis
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence analysis
Glycosylationi535 – 5351N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

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).By similarity
N-glycosylated. O-glycosylated; contains sialic acid (By similarity).By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ60696.
PRIDEiQ60696.

PTM databases

iPTMnetiQ60696.
PhosphoSiteiQ60696.

Expressioni

Tissue specificityi

Preferentially expressed in melanocytes.

Gene expression databases

CleanExiMM_SI.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000051869.

Structurei

3D structure databases

ProteinModelPortaliQ60696.
SMRiQ60696. Positions 229-300.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini255 – 29238PKDPROSITE-ProRule annotationAdd
BLAST
Repeati315 – 327131Add
BLAST
Repeati328 – 340132Add
BLAST
Repeati341 – 353133Add
BLAST
Repeati354 – 366134Add
BLAST
Repeati367 – 379135Add
BLAST
Repeati380 – 392136Add
BLAST
Repeati393 – 411197Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni315 – 411977 X 13 AA approximate tandem repeats, RPT domainAdd
BLAST

Domaini

The RPT domain is essential for the generation of the fibrillar matrix of melanosomes.By similarity
The lumenal domain is necessary for correct processing and trafficking to melanosomes.By similarity

Sequence similaritiesi

Belongs to the PMEL/NMB family.Curated
Contains 1 PKD domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IHN4. Eukaryota.
ENOG410Z44K. LUCA.
HOVERGENiHBG099694.
InParanoidiQ60696.
PhylomeDBiQ60696.

Family and domain databases

Gene3Di2.60.40.670. 1 hit.
InterProiIPR022409. PKD/Chitinase_dom.
IPR000601. PKD_dom.
[Graphical view]
PfamiPF00801. PKD. 1 hit.
[Graphical view]
SMARTiSM00089. PKD. 1 hit.
[Graphical view]
SUPFAMiSSF49299. SSF49299. 1 hit.
PROSITEiPS50093. PKD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q60696-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVGVQRRSFL PVLVLSALLA VGALEGSRNQ DWLGVPRQLV TKTWNRQLYP
60 70 80 90 100
EWTEVQGSNC WRGGQVSLRV INDGPTLVGA NASFSIALHF PGSQKVLPDG
110 120 130 140 150
QVIWANNTII NGSQVWGGQP VYPQEPDDAC VFPDGGPCPS GPKPPKRSFV
160 170 180 190 200
YVWKTWGKYW QVLGGPVSRS SIATRHAKLG THTMEVTVYH RRGSQSYVPL
210 220 230 240 250
AHASSTFTIT DQVPFSVSVS QLQALDGETK HFLRNHPLIF ALQLHDPSGY
260 270 280 290 300
LAEADLSYTW DFGDGTGTLI SRALDVTHTY LESGSVTAQV VLQAAIPLVS
310 320 330 340 350
CGSSPVPGTT DGYMPTAEAP GTTSRQGTTT KVVGTTPGQM PTTQPSGTTV
360 370 380 390 400
VQMPTTEVTA TTSEQMLTSA VIDTTLAEVS TTEGTGTTPT RPSGTTVAQA
410 420 430 440 450
TTTEGPDASP LLPTQSSTGS ISPLLDDTDT IMLVKRQVPL DCVLYRYGSF
460 470 480 490 500
SLALDIVQGI ESAEILQAVP FSEGDAFELT VSCQGGLPKE ACMDISSPGC
510 520 530 540 550
QPPAQRLCQS VPPSPDCQLV LHQVLKGGSG TYCLNVSLAD ANSLAVASTQ
560 570 580 590 600
LVVPGQDGGL GQAPLLVGIL LVLVAVVLAS LILGIDLRSR AQFPKCHMVA
610 620
LTAAPASGLR ARGLGENSPL LSGQQV
Length:626
Mass (Da):65,980
Last modified:November 1, 1996 - v1
Checksum:i7AB941D2E3FB1044
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti170 – 1701S → L in silver.
Natural varianti175 – 1751R → G in silver.
Natural varianti373 – 3731D → N in silver.
Natural varianti471 – 4711F → S in silver.
Natural varianti603 – 62624AAPAS…SGQQV → SSASLRSSRPRPWRKQPAPQ WTAGLIILKAPWISWG in silver.
Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14133 mRNA. Translation: AAA69538.1.
PIRiS53871.
UniGeneiMm.16756.
Mm.444804.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14133 mRNA. Translation: AAA69538.1.
PIRiS53871.
UniGeneiMm.16756.
Mm.444804.

3D structure databases

ProteinModelPortaliQ60696.
SMRiQ60696. Positions 229-300.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000051869.

PTM databases

iPTMnetiQ60696.
PhosphoSiteiQ60696.

Proteomic databases

PaxDbiQ60696.
PRIDEiQ60696.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:98301. Pmel.

Phylogenomic databases

eggNOGiENOG410IHN4. Eukaryota.
ENOG410Z44K. LUCA.
HOVERGENiHBG099694.
InParanoidiQ60696.
PhylomeDBiQ60696.

Miscellaneous databases

ChiTaRSiPmel. mouse.
PROiQ60696.
SOURCEiSearch...

Gene expression databases

CleanExiMM_SI.

Family and domain databases

Gene3Di2.60.40.670. 1 hit.
InterProiIPR022409. PKD/Chitinase_dom.
IPR000601. PKD_dom.
[Graphical view]
PfamiPF00801. PKD. 1 hit.
[Graphical view]
SMARTiSM00089. PKD. 1 hit.
[Graphical view]
SUPFAMiSSF49299. SSF49299. 1 hit.
PROSITEiPS50093. PKD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Mouse silver mutation is caused by a single base insertion in the putative cytoplasmic domain of Pmel 17."
    Kwon B.S., Halaban R., Ponnazhagan S., Kim K., Chintamaneni C., Bennett D., Pickard R.T.
    Nucleic Acids Res. 23:154-158(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SILVER.
    Strain: C57BL/6J.
    Tissue: Skin.
  2. "Pmel17 initiates premelanosome morphogenesis within multivesicular bodies."
    Berson J.F., Harper D.C., Tenza D., Raposo G., Marks M.S.
    Mol. Biol. Cell 12:3451-3464(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.

Entry informationi

Entry nameiPMEL_MOUSE
AccessioniPrimary (citable) accession number: Q60696
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.