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Q16655 (MAR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Melanoma antigen recognized by T-cells 1

Short name=MART-1
Alternative name(s):
Antigen LB39-AA
Antigen SK29-AA
Protein Melan-A
Gene names
Name:MLANA
Synonyms:MART1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length118 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in melanosome biogenesis by ensuring the stability of GPR143. Plays a vital role in the expression, stability, trafficking, and processing of melanocyte protein PMEL, which is critical to the formation of stage II melanosomes. Ref.10 Ref.11

Subunit structure

Interacts with PMEL. Interacts with GPR143. Ref.10 Ref.11

Subcellular location

Endoplasmic reticulum membrane; Single-pass type III membrane protein. Golgi apparatus. Golgi apparatustrans-Golgi network membrane. Melanosome. Note: Also found in small vesicles and tubules dispersed over the entire cytoplasm. A small fraction of the protein is inserted into the membrane in an inverted orientation. Inversion of membrane topology results in the relocalization of the protein from a predominant Golgi/post-Golgi area to the endoplasmic reticulum. Melanoma cells expressing the protein with an inverted membrane topology are more effectively recognized by specific cytolytic T-lymphocytes than those expressing the protein in its native membrane orientation. Ref.8 Ref.9 Ref.10

Tissue specificity

Expression is restricted to melanoma and melanocyte cell lines and retina.

Post-translational modification

Acylated (Ref.9).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 118118Melanoma antigen recognized by T-cells 1
PRO_0000096238

Regions

Transmembrane27 – 4721Helical; Potential
Topological domain48 – 11871Cytoplasmic Potential

Amino acid modifications

Modified residue1081Phosphoserine Ref.12

Secondary structure

... 118
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16655 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B755BFF39CFCB16E

FASTA11813,157
        10         20         30         40         50         60 
MPREDAHFIY GYPKKGHGHS YTTAEEAAGI GILTVILGVL LLIGCWYCRR RNGYRALMDK 

        70         80         90        100        110 
SLHVGTQCAL TRRCPQEGFD HRDSKVSLQE KNCEPVVPNA PPAYEKLSAE QSPPPYSP 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the gene coding for a shared human melanoma antigen recognized by autologous T cells infiltrating into tumor."
Kawakami Y., Eliyahu S., Delgado C.H., Robbins P.F., Rivoltini L., Topalian S.L., Miki T., Rosenberg S.A.
Proc. Natl. Acad. Sci. U.S.A. 91:3515-3519(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Melanoma.
[2]"A new gene coding for a differentiation antigen recognized by autologous cytolytic T lymphocytes on HLA-A2 melanomas."
Coulie P.G., Brichard V., van Pel A., Woelfel T., Schneider J., Traversari C., Mattei S., de Plaen E., Lurquin C., Szikora J.-P., Renauld J.-C., Boon T.
J. Exp. Med. 180:35-42(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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].
Tissue: Amygdala.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
Tissue: Skin.
[8]"Subcellular localization of the melanoma-associated protein Melan-AMART-1 influences the processing of its HLA-A2-restricted epitope."
Rimoldi D., Muehlethaler K., Salvi S., Valmori D., Romero P., Cerottini J.C., Levy F.
J. Biol. Chem. 276:43189-43196(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"The melanocytic protein Melan-A/MART-1 has a subcellular localization distinct from typical melanosomal proteins."
De Maziere A.M., Muehlethaler K., van Donselaar E., Salvi S., Davoust J., Cerottini J.-C., Levy F., Slot J.W., Rimoldi D.
Traffic 3:678-693(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"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: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SILV.
[11]"The ocular albinism type 1 (OA1) G-protein-coupled receptor functions with MART-1 at early stages of melanogenesis to control melanosome identity and composition."
Giordano F., Bonetti C., Surace E.M., Marigo V., Raposo G.
Hum. Mol. Genet. 18:4530-4545(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GPR143.
[12]"Structural basis for the presentation of tumor-associated MHC class II-restricted phosphopeptides to CD4+ T cells."
Li Y., Depontieu F.R., Sidney J., Salay T.M., Engelhard V.H., Hunt D.F., Sette A., Topalian S.L., Mariuzza R.A.
J. Mol. Biol. 399:596-603(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 100-114 IN COMPLEX WITH HLA-DR1, PHOSPHORYLATION AT SER-108.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U06452 mRNA. Translation: AAA19238.1.
U06654 mRNA. Translation: AAA20389.1.
CR450299 mRNA. Translation: CAG29295.1.
AK312149 mRNA. Translation: BAG35083.1.
AL365360 Genomic DNA. Translation: CAI95312.1.
CH471071 Genomic DNA. Translation: EAW58755.1.
CH471071 Genomic DNA. Translation: EAW58756.1.
BC014423 mRNA. Translation: AAH14423.1.
CCDSCCDS6466.1.
PIRA55253.
RefSeqNP_005502.1. NM_005511.1.
XP_006716805.1. XM_006716742.1.
UniGeneHs.154069.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GT9X-ray1.75C/F26-35[»]
2GTWX-ray1.55C/F27-35[»]
2GTZX-ray1.70C/F27-35[»]
2GUOX-ray1.90C/F27-35[»]
3HG1X-ray3.00C26-35[»]
3L6FX-ray2.10C100-114[»]
3MROX-ray2.35P26-35[»]
3MRPX-ray2.10P26-35[»]
3MRQX-ray2.20P26-35[»]
3QDMX-ray2.80C26-35[»]
3QEQX-ray2.59C27-35[»]
3QFDX-ray1.68C/F27-35[»]
4EUPX-ray2.88C/F27-35[»]
4EUQX-ray2.69C/F26-35[»]
4JFFX-ray2.43C26-35[»]
ProteinModelPortalQ16655.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108604. 3 interactions.
IntActQ16655. 3 interactions.
MINTMINT-7889633.
STRING9606.ENSP00000370880.

PTM databases

PhosphoSiteQ16655.

Polymorphism databases

DMDM2833278.

Proteomic databases

PaxDbQ16655.
PRIDEQ16655.

Protocols and materials databases

DNASU2315.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381471; ENSP00000370880; ENSG00000120215.
ENST00000381476; ENSP00000370885; ENSG00000120215.
ENST00000381477; ENSP00000370886; ENSG00000120215.
GeneID2315.
KEGGhsa:2315.
UCSCuc003zjo.1. human.

Organism-specific databases

CTD2315.
GeneCardsGC09P005846.
HGNCHGNC:7124. MLANA.
HPACAB000057.
HPA048662.
MIM605513. gene.
neXtProtNX_Q16655.
PharmGKBPA30842.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39695.
HOGENOMHOG000113481.
HOVERGENHBG006327.
InParanoidQ16655.
KOK17303.
OMAATRAHNE.
OrthoDBEOG708W29.
PhylomeDBQ16655.
TreeFamTF338577.

Gene expression databases

BgeeQ16655.
CleanExHS_MLANA.
GenevestigatorQ16655.

Family and domain databases

InterProIPR029242. MLANA.
[Graphical view]
PfamPF14991. MLANA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ16655.
GeneWikiMLANA.
GenomeRNAi2315.
NextBio9401.
PROQ16655.
SOURCESearch...

Entry information

Entry nameMAR1_HUMAN
AccessionPrimary (citable) accession number: Q16655
Secondary accession number(s): Q6ICU4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 104 of the entry and version 1 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

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 chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM