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P40967

- PMEL_HUMAN

UniProt

P40967 - PMEL_HUMAN

Protein

Melanocyte protein PMEL

Gene

PMEL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    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. Release of the soluble form, ME20-S, could protect tumor cells from antibody mediated immunity.2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. melanin biosynthetic process Source: UniProtKB-KW
    2. melanosome organization Source: UniProtKB

    Keywords - Biological processi

    Melanin biosynthesis

    Keywords - Ligandi

    Sialic acid

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Melanocyte protein PMEL
    Alternative name(s):
    ME20-M
    Short name:
    ME20M
    Melanocyte protein Pmel 17
    Melanocytes lineage-specific antigen GP100
    Melanoma-associated ME20 antigen
    P1
    P100
    Premelanosome protein
    Silver locus protein homolog
    Cleaved into the following 2 chains:
    Alternative name(s):
    95 kDa melanocyte-specific secreted glycoprotein
    P26
    Secreted melanoma-associated ME20 antigen
    Short name:
    ME20-S
    Short name:
    ME20S
    Gene namesi
    Name:PMEL
    Synonyms:D12S53E, PMEL17, SILV
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:10880. PMEL.

    Subcellular locationi

    Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus. Melanosome. Endosomemultivesicular body
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. 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.

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB
    2. extracellular region Source: UniProtKB-SubCell
    3. Golgi apparatus Source: UniProtKB
    4. integral component of membrane Source: UniProtKB-KW
    5. melanosome Source: UniProtKB
    6. multivesicular body membrane Source: UniProtKB
    7. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi468 – 4692KR → QQ: Loss of proteolytic cleavage. 1 Publication

    Organism-specific databases

    PharmGKBiPA35781.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 661637Melanocyte protein PMELPRO_0000024712Add
    BLAST
    Chaini25 – 467443M-alphaPRO_0000292263Add
    BLAST
    Chaini470 – 661192M-betaPRO_0000386648Add
    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
    Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi568 – 5681N-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.5 Publications
    N-glycosylated. O-glycosylated; contains sialic acid.

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP40967.
    PRIDEiP40967.

    PTM databases

    PhosphoSiteiP40967.

    Expressioni

    Tissue specificityi

    Preferentially expressed in melanomas. Some expression was found in dysplastic nevi. Not found in normal tissues nor in carcinomas. Normally expressed at low levels in quiescent adult melanocytes but overexpressed by proliferating neonatal melanocytes and during tumor growth.

    Gene expression databases

    ArrayExpressiP40967.
    BgeeiP40967.
    CleanExiHS_SILV.
    GenevestigatoriP40967.

    Organism-specific databases

    HPAiHPA001337.

    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.3 Publications

    Protein-protein interaction databases

    DIPiDIP-48937N.
    MINTiMINT-4723252.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TVBX-ray1.80C/F209-217[»]
    1TVHX-ray1.80C/F209-217[»]
    3CC5X-ray1.91C/F25-33[»]
    4IS6X-ray2.50C44-59[»]
    ProteinModelPortaliP40967.
    SMRiP40967. Positions 232-296.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP40967.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini470 – 595126LumenalSequence AnalysisAdd
    BLAST
    Topological domaini617 – 66145CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei596 – 61621HelicalSequence AnalysisAdd
    BLAST

    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 – 405137Add
    BLAST
    Repeati406 – 418138Add
    BLAST
    Repeati419 – 431139Add
    BLAST
    Repeati432 – 4441310Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni315 – 44413010 X 13 AA approximate tandem repeats, RPT domainAdd
    BLAST

    Domaini

    The RPT domain is essential for the generation of the fibrillar matrix of melanosomes.1 Publication
    The lumenal domain is necessary for correct processing and trafficking to melanosomes.1 Publication

    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

    eggNOGiNOG39434.
    HOVERGENiHBG099694.
    InParanoidiP40967.
    KOiK17304.
    OMAiIYRRRLM.
    OrthoDBiEOG7DFXBP.
    PhylomeDBiP40967.
    TreeFamiTF334865.

    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]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P40967-1) [UniParc]FASTAAdd to Basket

    Also known as: Intermediate form, Pmel17-i

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDLVLKRCLL HLAVIGALLA VGATKVPRNQ DWLGVSRQLR TKAWNRQLYP    50
    EWTEAQRLDC WRGGQVSLKV SNDGPTLIGA NASFSIALNF PGSQKVLPDG 100
    QVIWVNNTII NGSQVWGGQP VYPQETDDAC IFPDGGPCPS GSWSQKRSFV 150
    YVWKTWGQYW QVLGGPVSGL SIGTGRAMLG THTMEVTVYH RRGSRSYVPL 200
    AHSSSAFTIT DQVPFSVSVS QLRALDGGNK HFLRNQPLTF ALQLHDPSGY 250
    LAEADLSYTW DFGDSSGTLI SRALVVTHTY LEPGPVTAQV VLQAAIPLTS 300
    CGSSPVPGTT DGHRPTAEAP NTTAGQVPTT EVVGTTPGQA PTAEPSGTTS 350
    VQVPTTEVIS TAPVQMPTAE STGMTPEKVP VSEVMGTTLA EMSTPEATGM 400
    TPAEVSIVVL SGTTAAQVTT TEWVETTARE LPIPEPEGPD ASSIMSTESI 450
    TGSLGPLLDG TATLRLVKRQ VPLDCVLYRY GSFSVTLDIV QGIESAEILQ 500
    AVPSGEGDAF ELTVSCQGGL PKEACMEISS PGCQPPAQRL CQPVLPSPAC 550
    QLVLHQILKG GSGTYCLNVS LADTNSLAVV STQLIMPGQE AGLGQVPLIV 600
    GILLVLMAVV LASLIYRRRL MKQDFSVPQL PHSSSHWLRL PRIFCSCPIG 650
    ENSPLLSGQQ V 661
    Length:661
    Mass (Da):70,255
    Last modified:November 1, 1997 - v2
    Checksum:i8A904FAB16715653
    GO
    Isoform 2 (identifier: P40967-2) [UniParc]FASTAAdd to Basket

    Also known as: Long form, Pmel17-l

    The sequence of this isoform differs from the canonical sequence as follows:
         587-587: P → PVPGILLT

    Show »
    Length:668
    Mass (Da):70,949
    Checksum:iCF204FFB7E026791
    GO
    Isoform 3 (identifier: P40967-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         26-111: Missing.

    Show »
    Length:575
    Mass (Da):60,581
    Checksum:i2D84400CD1A8FE4E
    GO
    Isoform 4 (identifier: P40967-4) [UniParc]FASTAAdd to Basket

    Also known as: Short form, Pmel17-ls

    The sequence of this isoform differs from the canonical sequence as follows:
         373-414: Missing.

    Show »
    Length:619
    Mass (Da):66,035
    Checksum:iCAE0E8B0EF10550B
    GO
    Isoform 5 (identifier: P40967-5) [UniParc]FASTAAdd to Basket

    Also known as: Short form, Pmel17-is

    The sequence of this isoform differs from the canonical sequence as follows:
         373-414: Missing.
         587-587: P → PVPGILLT

    Show »
    Length:626
    Mass (Da):66,729
    Checksum:i8ECA4B3E15B0CD51
    GO

    Sequence cautioni

    The sequence AAA35930.1 differs from that shown. Reason: Frameshift at position 642.
    The sequence AAA35930.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1621V → F no nucleotide entry (PubMed:8022805)Curated
    Sequence conflicti274 – 2741L → P in AAA60121. (PubMed:1924386)Curated
    Sequence conflicti274 – 2741L → P in AAB19181. (PubMed:8739560)Curated
    Sequence conflicti373 – 3731G → S in BAH13223. (PubMed:14702039)Curated
    Sequence conflicti592 – 5921G → GG AA sequence (PubMed:8179825)Curated
    Sequence conflicti597 – 5971P → R in AAA60121. (PubMed:1924386)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti320 – 3201P → H.
    Corresponds to variant rs2071024 [ dbSNP | Ensembl ].
    VAR_050606
    Natural varianti370 – 3701E → D.
    Corresponds to variant rs17118154 [ dbSNP | Ensembl ].
    VAR_050607

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei26 – 11186Missing in isoform 3. 1 PublicationVSP_038266Add
    BLAST
    Alternative sequencei373 – 41442Missing in isoform 4 and isoform 5. CuratedVSP_038267Add
    BLAST
    Alternative sequencei587 – 5871P → PVPGILLT in isoform 2 and isoform 5. 1 PublicationVSP_038268

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77348 mRNA. Translation: AAA60121.1.
    U01874 mRNA. Translation: AAA18479.1.
    S73003 mRNA. Translation: AAC60634.1.
    U31799
    , U31808, U31807, U31797, U31798 Genomic DNA. Translation: AAB00386.1.
    U20093, U19491 Genomic DNA. Translation: AAB19181.1.
    M32295 mRNA. Translation: AAA35930.1. Sequence problems.
    BT007202 mRNA. Translation: AAP35866.1.
    AK092881 mRNA. Translation: BAG52619.1.
    AK300150 mRNA. Translation: BAH13223.1.
    AC025162 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96853.1.
    BC001414 mRNA. Translation: AAH01414.1.
    CCDSiCCDS55833.1. [P40967-3]
    CCDS55834.1. [P40967-2]
    CCDS8897.1. [P40967-1]
    PIRiA41234.
    I38400.
    RefSeqiNP_001186982.1. NM_001200053.1. [P40967-3]
    NP_001186983.1. NM_001200054.1. [P40967-2]
    NP_008859.1. NM_006928.4. [P40967-1]
    XP_006719632.1. XM_006719569.1. [P40967-1]
    UniGeneiHs.95972.

    Genome annotation databases

    EnsembliENST00000449260; ENSP00000402758; ENSG00000185664. [P40967-2]
    ENST00000548493; ENSP00000447374; ENSG00000185664. [P40967-1]
    ENST00000548747; ENSP00000448828; ENSG00000185664. [P40967-1]
    ENST00000550464; ENSP00000450036; ENSG00000185664. [P40967-3]
    ENST00000552882; ENSP00000449690; ENSG00000185664. [P40967-1]
    GeneIDi6490.
    KEGGihsa:6490.
    UCSCiuc001sip.3. human. [P40967-1]
    uc001siq.3. human. [P40967-2]
    uc010spx.2. human. [P40967-3]

    Polymorphism databases

    DMDMi2507099.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77348 mRNA. Translation: AAA60121.1 .
    U01874 mRNA. Translation: AAA18479.1 .
    S73003 mRNA. Translation: AAC60634.1 .
    U31799
    , U31808 , U31807 , U31797 , U31798 Genomic DNA. Translation: AAB00386.1 .
    U20093 , U19491 Genomic DNA. Translation: AAB19181.1 .
    M32295 mRNA. Translation: AAA35930.1 . Sequence problems.
    BT007202 mRNA. Translation: AAP35866.1 .
    AK092881 mRNA. Translation: BAG52619.1 .
    AK300150 mRNA. Translation: BAH13223.1 .
    AC025162 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96853.1 .
    BC001414 mRNA. Translation: AAH01414.1 .
    CCDSi CCDS55833.1. [P40967-3 ]
    CCDS55834.1. [P40967-2 ]
    CCDS8897.1. [P40967-1 ]
    PIRi A41234.
    I38400.
    RefSeqi NP_001186982.1. NM_001200053.1. [P40967-3 ]
    NP_001186983.1. NM_001200054.1. [P40967-2 ]
    NP_008859.1. NM_006928.4. [P40967-1 ]
    XP_006719632.1. XM_006719569.1. [P40967-1 ]
    UniGenei Hs.95972.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TVB X-ray 1.80 C/F 209-217 [» ]
    1TVH X-ray 1.80 C/F 209-217 [» ]
    3CC5 X-ray 1.91 C/F 25-33 [» ]
    4IS6 X-ray 2.50 C 44-59 [» ]
    ProteinModelPortali P40967.
    SMRi P40967. Positions 232-296.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48937N.
    MINTi MINT-4723252.

    PTM databases

    PhosphoSitei P40967.

    Polymorphism databases

    DMDMi 2507099.

    Proteomic databases

    PaxDbi P40967.
    PRIDEi P40967.

    Protocols and materials databases

    DNASUi 6490.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000449260 ; ENSP00000402758 ; ENSG00000185664 . [P40967-2 ]
    ENST00000548493 ; ENSP00000447374 ; ENSG00000185664 . [P40967-1 ]
    ENST00000548747 ; ENSP00000448828 ; ENSG00000185664 . [P40967-1 ]
    ENST00000550464 ; ENSP00000450036 ; ENSG00000185664 . [P40967-3 ]
    ENST00000552882 ; ENSP00000449690 ; ENSG00000185664 . [P40967-1 ]
    GeneIDi 6490.
    KEGGi hsa:6490.
    UCSCi uc001sip.3. human. [P40967-1 ]
    uc001siq.3. human. [P40967-2 ]
    uc010spx.2. human. [P40967-3 ]

    Organism-specific databases

    CTDi 6490.
    GeneCardsi GC12M056350.
    HGNCi HGNC:10880. PMEL.
    HPAi HPA001337.
    MIMi 155550. gene.
    neXtProti NX_P40967.
    PharmGKBi PA35781.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39434.
    HOVERGENi HBG099694.
    InParanoidi P40967.
    KOi K17304.
    OMAi IYRRRLM.
    OrthoDBi EOG7DFXBP.
    PhylomeDBi P40967.
    TreeFami TF334865.

    Miscellaneous databases

    ChiTaRSi PMEL. human.
    EvolutionaryTracei P40967.
    GeneWikii PMEL_(gene).
    GenomeRNAii 6490.
    NextBioi 25221.
    PROi P40967.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P40967.
    Bgeei P40967.
    CleanExi HS_SILV.
    Genevestigatori P40967.

    Family and domain databases

    Gene3Di 2.60.40.670. 1 hit.
    InterProi IPR022409. PKD/Chitinase_dom.
    IPR000601. PKD_dom.
    [Graphical view ]
    Pfami PF00801. PKD. 1 hit.
    [Graphical view ]
    SMARTi SM00089. PKD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49299. SSF49299. 1 hit.
    PROSITEi PS50093. PKD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A melanocyte-specific gene, Pmel 17, maps near the silver coat color locus on mouse chromosome 10 and is in a syntenic region on human chromosome 12."
      Kwon B.S., Chintamaneni C., Kozak C.A., Copeland N.G., Gilbert D.J., Jenkins N.A., Barton D., Francke U., Kobayashi Y., Kim K.-K.
      Proc. Natl. Acad. Sci. U.S.A. 88:9228-9232(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Cloning and expression of the gene for the melanoma-associated ME20 antigen."
      Maresh G.A., Marken J.S., Neubauer M., Aruffo A., Hellstroem I., Hellstroem K.E., Marquardt H.
      DNA Cell Biol. 13:87-95(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 25-53.
    3. "Molecular characterization of the melanocyte lineage-specific antigen gp100."
      Adema G.J., de Boer A.J., Vogel A.M., Loenen W.A., Figdor C.G.
      J. Biol. Chem. 269:20126-20133(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Identification of a human melanoma antigen recognized by tumor-infiltrating lymphocytes associated with in vivo tumor rejection."
      Kawakami Y., Eliyahu S., Delgado C.H., Robbins P.F., Sakaguchi K., Appella E., Yannelli J.R., Adema G.J., Miki T., Rosenberg S.A.
      Proc. Natl. Acad. Sci. U.S.A. 91:6458-6462(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "Genomic organization and sequence of D12S53E (Pmel 17), the human homologue of the mouse silver (si) locus."
      Bailin T., Lee S.-T., Spritz R.A.
      J. Invest. Dermatol. 106:24-27(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
    6. "Genomic organization and FISH mapping of human Pmel 17, the putative silver locus."
      Kim K.K., Youn B.S., Heng H.H.Q., Shi X.-M., Tsui L.-C., Lee Z.H., Pickard R.T., Kwon B.S.
      Pigment Cell Res. 9:42-48(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
    7. "Sequence of a melanocyte specific secreted glycoprotein."
      Vogel A.
      Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Placenta and Spleen.
    10. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Placenta.
    13. "A novel splice variant of Pmel17 expressed by human melanocytes and melanoma cells lacking some of the internal repeats."
      Nichols S.E., Harper D.C., Berson J.F., Marks M.S.
      J. Invest. Dermatol. 121:821-830(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 4 AND 5).
    14. "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: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, SUBUNIT, FUNCTION, GLYCOSYLATION.
    15. "Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis."
      Berson J.F., Theos A.C., Harper D.C., Tenza D., Raposo G., Marks M.S.
      J. Cell Biol. 161:521-533(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, MUTAGENESIS OF 468-LYS--ARG-469.
    16. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    17. "Epitope mapping of the melanosomal matrix protein gp100 (PMEL17): rapid processing in the endoplasmic reticulum and glycosylation in the early Golgi compartment."
      Yasumoto K.-I., Watabe H., Valencia J.C., Kushimoto T., Kobayashi T., Appella E., Hearing V.J.
      J. Biol. Chem. 279:28330-28338(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, GLYCOSYLATION.
    18. "MART-1 is required for the function of the melanosomal matrix protein PMEL17/GP100 and the maturation of melanosomes."
      Hoashi T., Watabe H., Muller J., Yamaguchi Y., Vieira W.D., Hearing V.J.
      J. Biol. Chem. 280:14006-14016(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, INTERACTION WITH MLANA.
    19. "The repeat domain of the melanosomal matrix protein PMEL17/GP100 is required for the formation of organellar fibers."
      Hoashi T., Muller J., Vieira W.D., Rouzaud F., Kikuchi K., Tamaki K., Hearing V.J.
      J. Biol. Chem. 281:21198-21208(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN RPT, DOMAIN LUMENAL.
    20. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    21. "Premelanosome amyloid-like fibrils are composed of only Golgi-processed forms of Pmel17 that have been proteolytically processed in endosomes."
      Harper D.C., Theos A.C., Herman K.E., Tenza D., Raposo G., Marks M.S.
      J. Biol. Chem. 283:2307-2322(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, GLYCOSYLATION.
    22. "The tetraspanin CD63 regulates ESCRT-independent and -dependent endosomal sorting during melanogenesis."
      van Niel G., Charrin S., Simoes S., Romao M., Rochin L., Saftig P., Marks M.S., Rubinstein E., Raposo G.
      Dev. Cell 21:708-721(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CD63.

    Entry informationi

    Entry nameiPMEL_HUMAN
    AccessioniPrimary (citable) accession number: P40967
    Secondary accession number(s): B3KS57
    , B7Z6D7, Q12763, Q14448, Q14817, Q16565
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3