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P40967 (PMEL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. M-alpha
    Alternative name(s):
    95 kDa melanocyte-specific secreted glycoprotein
    P26
    Secreted melanoma-associated ME20 antigen
    Short name=ME20-S
    Short name=ME20S
  2. M-beta
Gene names
Name:PMEL
Synonyms:D12S53E, PMEL17, SILV
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length661 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Release of the soluble form, ME20-S, could protect tumor cells from antibody mediated immunity. Ref.14 Ref.22

Subunit structure

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. Ref.14 Ref.18 Ref.22

Subcellular location

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. Ref.14 Ref.16 Ref.18 Ref.20 Ref.22

M-alpha: Secreted Ref.14 Ref.16 Ref.18 Ref.20 Ref.22.

Tissue specificity

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.

Domain

The RPT domain is essential for the generation of the fibrillar matrix of melanosomes. Ref.19

The lumenal domain is necessary for correct processing and trafficking to melanosomes. Ref.19

Post-translational modification

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. Ref.14 Ref.15 Ref.17 Ref.18 Ref.21

N-glycosylated. O-glycosylated; contains sialic acid. Ref.14 Ref.17 Ref.21

Sequence similarities

Belongs to the PMEL/NMB family.

Contains 1 PKD domain.

Sequence caution

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

The sequence AAA35930.1 differs from that shown. Reason: Frameshift at position 642.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P40967-1)

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.
Isoform 2 (identifier: P40967-2)

Also known as: Long form; Pmel17-l;

The sequence of this isoform differs from the canonical sequence as follows:
     587-587: P → PVPGILLT
Isoform 3 (identifier: P40967-3)

The sequence of this isoform differs from the canonical sequence as follows:
     26-111: Missing.
Isoform 4 (identifier: P40967-4)

Also known as: Short form; Pmel17-ls;

The sequence of this isoform differs from the canonical sequence as follows:
     373-414: Missing.
Isoform 5 (identifier: P40967-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.2
Chain25 – 661637Melanocyte protein PMEL
PRO_0000024712
Chain25 – 467443M-alpha
PRO_0000292263
Chain470 – 661192M-beta
PRO_0000386648

Regions

Topological domain470 – 595126Lumenal Potential
Transmembrane596 – 61621Helical; Potential
Topological domain617 – 66145Cytoplasmic Potential
Domain255 – 29238PKD
Repeat315 – 327131
Repeat328 – 340132
Repeat341 – 353133
Repeat354 – 366134
Repeat367 – 379135
Repeat380 – 392136
Repeat393 – 405137
Repeat406 – 418138
Repeat419 – 431139
Repeat432 – 4441310
Region315 – 44413010 X 13 AA approximate tandem repeats, RPT domain

Amino acid modifications

Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation1061N-linked (GlcNAc...) Potential
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation3211N-linked (GlcNAc...) Potential
Glycosylation5681N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence26 – 11186Missing in isoform 3.
VSP_038266
Alternative sequence373 – 41442Missing in isoform 4 and isoform 5.
VSP_038267
Alternative sequence5871P → PVPGILLT in isoform 2 and isoform 5.
VSP_038268
Natural variant3201P → H.
Corresponds to variant rs2071024 [ dbSNP | Ensembl ].
VAR_050606
Natural variant3701E → D.
Corresponds to variant rs17118154 [ dbSNP | Ensembl ].
VAR_050607

Experimental info

Mutagenesis468 – 4692KR → QQ: Loss of proteolytic cleavage. Ref.15
Sequence conflict1621V → F no nucleotide entry Ref.4
Sequence conflict2741L → P in AAA60121. Ref.1
Sequence conflict2741L → P in AAB19181. Ref.6
Sequence conflict3731G → S in BAH13223. Ref.9
Sequence conflict5921G → GG AA sequence Ref.2
Sequence conflict5971P → R in AAA60121. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Intermediate form) (Pmel17-i) [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 8A904FAB16715653

FASTA66170,255
        10         20         30         40         50         60 
MDLVLKRCLL HLAVIGALLA VGATKVPRNQ DWLGVSRQLR TKAWNRQLYP EWTEAQRLDC 

        70         80         90        100        110        120 
WRGGQVSLKV SNDGPTLIGA NASFSIALNF PGSQKVLPDG QVIWVNNTII NGSQVWGGQP 

       130        140        150        160        170        180 
VYPQETDDAC IFPDGGPCPS GSWSQKRSFV YVWKTWGQYW QVLGGPVSGL SIGTGRAMLG 

       190        200        210        220        230        240 
THTMEVTVYH RRGSRSYVPL AHSSSAFTIT DQVPFSVSVS QLRALDGGNK HFLRNQPLTF 

       250        260        270        280        290        300 
ALQLHDPSGY LAEADLSYTW DFGDSSGTLI SRALVVTHTY LEPGPVTAQV VLQAAIPLTS 

       310        320        330        340        350        360 
CGSSPVPGTT DGHRPTAEAP NTTAGQVPTT EVVGTTPGQA PTAEPSGTTS VQVPTTEVIS 

       370        380        390        400        410        420 
TAPVQMPTAE STGMTPEKVP VSEVMGTTLA EMSTPEATGM TPAEVSIVVL SGTTAAQVTT 

       430        440        450        460        470        480 
TEWVETTARE LPIPEPEGPD ASSIMSTESI TGSLGPLLDG TATLRLVKRQ VPLDCVLYRY 

       490        500        510        520        530        540 
GSFSVTLDIV QGIESAEILQ AVPSGEGDAF ELTVSCQGGL PKEACMEISS PGCQPPAQRL 

       550        560        570        580        590        600 
CQPVLPSPAC QLVLHQILKG GSGTYCLNVS LADTNSLAVV STQLIMPGQE AGLGQVPLIV 

       610        620        630        640        650        660 
GILLVLMAVV LASLIYRRRL MKQDFSVPQL PHSSSHWLRL PRIFCSCPIG ENSPLLSGQQ 


V 

« Hide

Isoform 2 (Long form) (Pmel17-l) [UniParc].

Checksum: CF204FFB7E026791
Show »

FASTA66870,949
Isoform 3 [UniParc].

Checksum: 2D84400CD1A8FE4E
Show »

FASTA57560,581
Isoform 4 (Short form) (Pmel17-ls) [UniParc].

Checksum: CAE0E8B0EF10550B
Show »

FASTA61966,035
Isoform 5 (Short form) (Pmel17-is) [UniParc].

Checksum: 8ECA4B3E15B0CD51
Show »

FASTA62666,729

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.
J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract]
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]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M77348 mRNA. Translation: AAA60121.1.
U01874 mRNA. Translation: AAA18479.1.
S73003 mRNA. Translation: AAC60634.1.
U31799 expand/collapse EMBL AC list , 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.
CCDSCCDS55833.1. [P40967-3]
CCDS55834.1. [P40967-2]
CCDS8897.1. [P40967-1]
PIRA41234.
I38400.
RefSeqNP_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]
UniGeneHs.95972.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TVBX-ray1.80C/F209-217[»]
1TVHX-ray1.80C/F209-217[»]
3CC5X-ray1.91C/F25-33[»]
4IS6X-ray2.50C44-59[»]
ProteinModelPortalP40967.
SMRP40967. Positions 232-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48937N.
MINTMINT-4723252.

PTM databases

PhosphoSiteP40967.

Polymorphism databases

DMDM2507099.

Proteomic databases

PaxDbP40967.
PRIDEP40967.

Protocols and materials databases

DNASU6490.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000449260; ENSP00000402758; ENSG00000185664. [P40967-2]
ENST00000539511; ENSP00000445005; ENSG00000185664. [P40967-3]
ENST00000548493; ENSP00000447374; ENSG00000185664. [P40967-1]
ENST00000548747; ENSP00000448828; ENSG00000185664. [P40967-1]
ENST00000550464; ENSP00000450036; ENSG00000185664. [P40967-3]
ENST00000552882; ENSP00000449690; ENSG00000185664. [P40967-1]
GeneID6490.
KEGGhsa:6490.
UCSCuc001sip.3. human. [P40967-1]
uc001siq.3. human. [P40967-2]
uc010spx.2. human. [P40967-3]

Organism-specific databases

CTD6490.
GeneCardsGC12M056350.
HGNCHGNC:10880. PMEL.
HPAHPA001337.
MIM155550. gene.
neXtProtNX_P40967.
PharmGKBPA35781.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39434.
HOVERGENHBG099694.
InParanoidP40967.
KOK17304.
OMAIYRRRLM.
OrthoDBEOG7DFXBP.
PhylomeDBP40967.
TreeFamTF334865.

Gene expression databases

ArrayExpressP40967.
BgeeP40967.
CleanExHS_SILV.
GenevestigatorP40967.

Family and domain databases

Gene3D2.60.40.670. 1 hit.
InterProIPR022409. PKD/Chitinase_dom.
IPR000601. PKD_dom.
[Graphical view]
PfamPF00801. PKD. 1 hit.
[Graphical view]
SMARTSM00089. PKD. 1 hit.
[Graphical view]
SUPFAMSSF49299. SSF49299. 1 hit.
PROSITEPS50093. PKD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPMEL. human.
EvolutionaryTraceP40967.
GeneWikiPMEL_(gene).
GenomeRNAi6490.
NextBio25221.
PROP40967.
SOURCESearch...

Entry information

Entry namePMEL_HUMAN
AccessionPrimary (citable) accession number: P40967
Secondary accession number(s): B3KS57 expand/collapse secondary AC list , B7Z6D7, Q12763, Q14448, Q14817, Q16565
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM