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Melanocyte protein PMEL (ME20-M) (ME20M) (Melanocyte protein Pmel 17) (Melanocytes lineage-specific antigen GP100) (Melanoma-associated ME20 antigen) (P1) (P100) (Premelanosome protein) (Silver locus protein homolog) [Cleaved into: M-alpha (95 kDa melanocyte-specific secreted glycoprotein) (P26) (Secreted melanoma-associated ME20 antigen) (ME20-S) (ME20S); M-beta]

 PMEL_HUMAN              Reviewed;         661 AA.
P40967; B3KS57; B7Z6D7; Q12763; Q14448; Q14817; Q16565;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
05-DEC-2018, entry version 166.
RecName: Full=Melanocyte protein PMEL;
AltName: Full=ME20-M;
Short=ME20M;
AltName: Full=Melanocyte protein Pmel 17;
AltName: Full=Melanocytes lineage-specific antigen GP100;
AltName: Full=Melanoma-associated ME20 antigen;
AltName: Full=P1;
AltName: Full=P100;
AltName: Full=Premelanosome protein;
AltName: Full=Silver locus protein homolog;
Contains:
RecName: Full=M-alpha;
AltName: Full=95 kDa melanocyte-specific secreted glycoprotein;
AltName: Full=P26;
AltName: Full=Secreted melanoma-associated ME20 antigen;
Short=ME20-S;
Short=ME20S;
Contains:
RecName: Full=M-beta;
Flags: Precursor;
Name=PMEL; Synonyms=D12S53E, PMEL17, SILV;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=1924386; DOI=10.1073/pnas.88.20.9228;
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.;
"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.";
Proc. Natl. Acad. Sci. U.S.A. 88:9228-9232(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 25-53.
PubMed=8179825; DOI=10.1089/dna.1994.13.87;
Maresh G.A., Marken J.S., Neubauer M., Aruffo A., Hellstroem I.,
Hellstroem K.E., Marquardt H.;
"Cloning and expression of the gene for the melanoma-associated ME20
antigen.";
DNA Cell Biol. 13:87-95(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7519602;
Adema G.J., de Boer A.J., Vogel A.M., Loenen W.A., Figdor C.G.;
"Molecular characterization of the melanocyte lineage-specific antigen
gp100.";
J. Biol. Chem. 269:20126-20133(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8022805; DOI=10.1073/pnas.91.14.6458;
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.;
"Identification of a human melanoma antigen recognized by tumor-
infiltrating lymphocytes associated with in vivo tumor rejection.";
Proc. Natl. Acad. Sci. U.S.A. 91:6458-6462(1994).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
1).
PubMed=8592076; DOI=10.1111/1523-1747.ep12326976;
Bailin T., Lee S.-T., Spritz R.A.;
"Genomic organization and sequence of D12S53E (Pmel 17), the human
homologue of the mouse silver (si) locus.";
J. Invest. Dermatol. 106:24-27(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
1).
PubMed=8739560; DOI=10.1111/j.1600-0749.1996.tb00085.x;
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.;
"Genomic organization and FISH mapping of human Pmel 17, the putative
silver locus.";
Pigment Cell Res. 9:42-48(1996).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Vogel A.;
"Sequence of a melanocyte specific secreted glycoprotein.";
Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Placenta, and Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
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.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
ALTERNATIVE SPLICING (ISOFORMS 4 AND 5).
PubMed=14632201; DOI=10.1046/j.1523-1747.2003.12474.x;
Nichols S.E., Harper D.C., Berson J.F., Marks M.S.;
"A novel splice variant of Pmel17 expressed by human melanocytes and
melanoma cells lacking some of the internal repeats.";
J. Invest. Dermatol. 121:821-830(2003).
[14]
SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, SUBUNIT, FUNCTION, AND
GLYCOSYLATION.
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).
[15]
PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF 468-LYS--ARG-469.
PubMed=12732614; DOI=10.1083/jcb.200302072;
Berson J.F., Theos A.C., Harper D.C., Tenza D., Raposo G., Marks M.S.;
"Proprotein convertase cleavage liberates a fibrillogenic fragment of
a resident glycoprotein to initiate melanosome biogenesis.";
J. Cell Biol. 161:521-533(2003).
[16]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=12643545; DOI=10.1021/pr025562r;
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.;
"Proteomic analysis of early melanosomes: identification of novel
melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
[17]
PROTEOLYTIC PROCESSING, AND GLYCOSYLATION.
PubMed=15096515; DOI=10.1074/jbc.M401269200;
Yasumoto K.-I., Watabe H., Valencia J.C., Kushimoto T., Kobayashi T.,
Appella E., Hearing V.J.;
"Epitope mapping of the melanosomal matrix protein gp100 (PMEL17):
rapid processing in the endoplasmic reticulum and glycosylation in the
early Golgi compartment.";
J. Biol. Chem. 279:28330-28338(2004).
[18]
PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, AND INTERACTION WITH
MLANA.
PubMed=15695812; DOI=10.1074/jbc.M413692200;
Hoashi T., Watabe H., Muller J., Yamaguchi Y., Vieira W.D.,
Hearing V.J.;
"MART-1 is required for the function of the melanosomal matrix protein
PMEL17/GP100 and the maturation of melanosomes.";
J. Biol. Chem. 280:14006-14016(2005).
[19]
DOMAIN RPT, AND DOMAIN LUMENAL.
PubMed=16682408; DOI=10.1074/jbc.M601643200;
Hoashi T., Muller J., Vieira W.D., Rouzaud F., Kikuchi K., Tamaki K.,
Hearing V.J.;
"The repeat domain of the melanosomal matrix protein PMEL17/GP100 is
required for the formation of organellar fibers.";
J. Biol. Chem. 281:21198-21208(2006).
[20]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
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.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[21]
PROTEOLYTIC PROCESSING, AND GLYCOSYLATION.
PubMed=17991747; DOI=10.1074/jbc.M708007200;
Harper D.C., Theos A.C., Herman K.E., Tenza D., Raposo G., Marks M.S.;
"Premelanosome amyloid-like fibrils are composed of only Golgi-
processed forms of Pmel17 that have been proteolytically processed in
endosomes.";
J. Biol. Chem. 283:2307-2322(2008).
[22]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CD63.
PubMed=21962903; DOI=10.1016/j.devcel.2011.08.019;
van Niel G., Charrin S., Simoes S., Romao M., Rochin L., Saftig P.,
Marks M.S., Rubinstein E., Raposo G.;
"The tetraspanin CD63 regulates ESCRT-independent and -dependent
endosomal sorting during melanogenesis.";
Dev. Cell 21:708-721(2011).
-!- 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.
{ECO:0000269|PubMed:11694580, ECO:0000269|PubMed:21962903}.
-!- 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.
{ECO:0000269|PubMed:11694580, ECO:0000269|PubMed:15695812,
ECO:0000269|PubMed:21962903}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-14022409, EBI-14022409;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
type I membrane protein. Golgi apparatus. Melanosome. Endosome,
multivesicular 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.
-!- SUBCELLULAR LOCATION: M-alpha: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=Intermediate form, Pmel17-i;
IsoId=P40967-1; Sequence=Displayed;
Name=2; Synonyms=Long form, Pmel17-l;
IsoId=P40967-2; Sequence=VSP_038268;
Name=3;
IsoId=P40967-3; Sequence=VSP_038266;
Name=4; Synonyms=Short form, Pmel17-ls;
IsoId=P40967-4; Sequence=VSP_038267;
Name=5; Synonyms=Short form, Pmel17-is;
IsoId=P40967-5; Sequence=VSP_038267, VSP_038268;
-!- 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. {ECO:0000269|PubMed:16682408}.
-!- DOMAIN: The lumenal domain is necessary for correct processing and
trafficking to melanosomes. {ECO:0000269|PubMed:16682408}.
-!- 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.
{ECO:0000269|PubMed:11694580, ECO:0000269|PubMed:12732614,
ECO:0000269|PubMed:15096515, ECO:0000269|PubMed:15695812,
ECO:0000269|PubMed:17991747}.
-!- PTM: N-glycosylated. O-glycosylated; contains sialic acid.
-!- SIMILARITY: Belongs to the PMEL/NMB family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA35930.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAA35930.1; Type=Frameshift; Positions=642; Evidence={ECO:0000305};
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EMBL; M77348; AAA60121.1; -; mRNA.
EMBL; U01874; AAA18479.1; -; mRNA.
EMBL; S73003; AAC60634.1; -; mRNA.
EMBL; U31799; AAB00386.1; -; Genomic_DNA.
EMBL; U31808; AAB00386.1; JOINED; Genomic_DNA.
EMBL; U31807; AAB00386.1; JOINED; Genomic_DNA.
EMBL; U31797; AAB00386.1; JOINED; Genomic_DNA.
EMBL; U31798; AAB00386.1; JOINED; Genomic_DNA.
EMBL; U20093; AAB19181.1; -; Genomic_DNA.
EMBL; U19491; AAB19181.1; JOINED; Genomic_DNA.
EMBL; M32295; AAA35930.1; ALT_SEQ; mRNA.
EMBL; BT007202; AAP35866.1; -; mRNA.
EMBL; AK092881; BAG52619.1; -; mRNA.
EMBL; AK300150; BAH13223.1; -; mRNA.
EMBL; AC025162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW96853.1; -; Genomic_DNA.
EMBL; BC001414; AAH01414.1; -; mRNA.
CCDS; CCDS55833.1; -. [P40967-3]
CCDS; CCDS55834.1; -. [P40967-2]
CCDS; CCDS8897.1; -. [P40967-1]
PIR; A41234; A41234.
PIR; I38400; I38400.
RefSeq; NP_001186982.1; NM_001200053.1. [P40967-3]
RefSeq; NP_001186983.1; NM_001200054.1. [P40967-2]
RefSeq; NP_001307050.1; NM_001320121.1. [P40967-5]
RefSeq; NP_001307051.1; NM_001320122.1. [P40967-4]
RefSeq; NP_008859.1; NM_006928.4. [P40967-1]
RefSeq; XP_006719632.1; XM_006719569.1.
RefSeq; XP_011536987.1; XM_011538685.1.
UniGene; Hs.95972; -.
PDB; 1TVB; X-ray; 1.80 A; C/F=209-217.
PDB; 1TVH; X-ray; 1.80 A; C/F=209-217.
PDB; 3CC5; X-ray; 1.91 A; C/F=25-33.
PDB; 4IS6; X-ray; 2.50 A; C=44-59.
PDB; 5EU3; X-ray; 1.97 A; C=280-288.
PDB; 5EU4; X-ray; 2.12 A; C/F=280-288.
PDB; 5EU5; X-ray; 1.54 A; C=280-288.
PDB; 5EU6; X-ray; 2.02 A; C=280-287.
PDBsum; 1TVB; -.
PDBsum; 1TVH; -.
PDBsum; 3CC5; -.
PDBsum; 4IS6; -.
PDBsum; 5EU3; -.
PDBsum; 5EU4; -.
PDBsum; 5EU5; -.
PDBsum; 5EU6; -.
ProteinModelPortal; P40967; -.
SMR; P40967; -.
BioGrid; 112381; 59.
DIP; DIP-48937N; -.
IntAct; P40967; 1.
STRING; 9606.ENSP00000402758; -.
ChEMBL; CHEMBL3712988; -.
iPTMnet; P40967; -.
PhosphoSitePlus; P40967; -.
BioMuta; PMEL; -.
DMDM; 2507099; -.
EPD; P40967; -.
PaxDb; P40967; -.
PeptideAtlas; P40967; -.
PRIDE; P40967; -.
ProteomicsDB; 55393; -.
ProteomicsDB; 55394; -. [P40967-2]
ProteomicsDB; 55395; -. [P40967-3]
ProteomicsDB; 55396; -. [P40967-4]
ProteomicsDB; 55397; -. [P40967-5]
DNASU; 6490; -.
Ensembl; ENST00000449260; ENSP00000402758; ENSG00000185664. [P40967-2]
Ensembl; ENST00000548493; ENSP00000447374; ENSG00000185664. [P40967-1]
Ensembl; ENST00000548747; ENSP00000448828; ENSG00000185664. [P40967-1]
Ensembl; ENST00000550464; ENSP00000450036; ENSG00000185664. [P40967-3]
Ensembl; ENST00000552882; ENSP00000449690; ENSG00000185664. [P40967-1]
GeneID; 6490; -.
KEGG; hsa:6490; -.
UCSC; uc001sip.4; human. [P40967-1]
CTD; 6490; -.
DisGeNET; 6490; -.
EuPathDB; HostDB:ENSG00000185664.14; -.
GeneCards; PMEL; -.
HGNC; HGNC:10880; PMEL.
HPA; HPA031649; -.
MIM; 155550; gene.
neXtProt; NX_P40967; -.
OpenTargets; ENSG00000185664; -.
PharmGKB; PA35781; -.
eggNOG; ENOG410IHN4; Eukaryota.
eggNOG; ENOG410Z44K; LUCA.
GeneTree; ENSGT00940000153985; -.
HOVERGEN; HBG099694; -.
InParanoid; P40967; -.
KO; K17304; -.
OMA; LRQFFND; -.
OrthoDB; EOG091G05UD; -.
PhylomeDB; P40967; -.
TreeFam; TF334865; -.
SIGNOR; P40967; -.
ChiTaRS; PMEL; human.
EvolutionaryTrace; P40967; -.
GeneWiki; PMEL_(gene); -.
GenomeRNAi; 6490; -.
PRO; PR:P40967; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000185664; Expressed in 112 organ(s), highest expression level in pigmented layer of retina.
CleanEx; HS_SILV; -.
ExpressionAtlas; P40967; baseline and differential.
Genevisible; P40967; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0042470; C:melanosome; IDA:UniProtKB.
GO; GO:0032585; C:multivesicular body membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0032438; P:melanosome organization; IDA:UniProtKB.
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;
3D-structure; Alternative splicing;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Endosome; Glycoprotein; Golgi apparatus; Melanin biosynthesis;
Membrane; Polymorphism; Reference proteome; Repeat; Secreted;
Sialic acid; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 24 {ECO:0000269|PubMed:8179825}.
CHAIN 25 661 Melanocyte protein PMEL.
/FTId=PRO_0000024712.
CHAIN 25 467 M-alpha.
/FTId=PRO_0000292263.
CHAIN 470 661 M-beta.
/FTId=PRO_0000386648.
TOPO_DOM 470 595 Lumenal. {ECO:0000255}.
TRANSMEM 596 616 Helical. {ECO:0000255}.
TOPO_DOM 617 661 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 393 405 7.
REPEAT 406 418 8.
REPEAT 419 431 9.
REPEAT 432 444 10.
REGION 315 444 10 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 321 321 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 568 568 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 26 111 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038266.
VAR_SEQ 373 414 Missing (in isoform 4 and isoform 5).
{ECO:0000305}.
/FTId=VSP_038267.
VAR_SEQ 587 587 P -> PVPGILLT (in isoform 2 and isoform
5). {ECO:0000303|PubMed:1924386}.
/FTId=VSP_038268.
VARIANT 320 320 P -> H (in dbSNP:rs2071024).
/FTId=VAR_050606.
VARIANT 370 370 E -> D (in dbSNP:rs17118154).
/FTId=VAR_050607.
MUTAGEN 468 469 KR->QQ: Loss of proteolytic cleavage.
{ECO:0000269|PubMed:12732614}.
CONFLICT 162 162 V -> F (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 274 274 L -> P (in Ref. 1; AAA60121 and 6;
AAB19181). {ECO:0000305}.
CONFLICT 373 373 G -> S (in Ref. 9; BAH13223).
{ECO:0000305}.
CONFLICT 592 592 G -> GG (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 597 597 P -> R (in Ref. 1; AAA60121).
{ECO:0000305}.
SEQUENCE 661 AA; 70255 MW; 8A904FAB16715653 CRC64;
MDLVLKRCLL HLAVIGALLA VGATKVPRNQ DWLGVSRQLR TKAWNRQLYP EWTEAQRLDC
WRGGQVSLKV SNDGPTLIGA NASFSIALNF PGSQKVLPDG QVIWVNNTII NGSQVWGGQP
VYPQETDDAC IFPDGGPCPS GSWSQKRSFV YVWKTWGQYW QVLGGPVSGL SIGTGRAMLG
THTMEVTVYH RRGSRSYVPL AHSSSAFTIT DQVPFSVSVS QLRALDGGNK HFLRNQPLTF
ALQLHDPSGY LAEADLSYTW DFGDSSGTLI SRALVVTHTY LEPGPVTAQV VLQAAIPLTS
CGSSPVPGTT DGHRPTAEAP NTTAGQVPTT EVVGTTPGQA PTAEPSGTTS VQVPTTEVIS
TAPVQMPTAE STGMTPEKVP VSEVMGTTLA EMSTPEATGM TPAEVSIVVL SGTTAAQVTT
TEWVETTARE LPIPEPEGPD ASSIMSTESI TGSLGPLLDG TATLRLVKRQ VPLDCVLYRY
GSFSVTLDIV QGIESAEILQ AVPSGEGDAF ELTVSCQGGL PKEACMEISS PGCQPPAQRL
CQPVLPSPAC QLVLHQILKG GSGTYCLNVS LADTNSLAVV STQLIMPGQE AGLGQVPLIV
GILLVLMAVV LASLIYRRRL MKQDFSVPQL PHSSSHWLRL PRIFCSCPIG ENSPLLSGQQ
V


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