MAGA3_HUMAN
ID MAGA3_HUMAN Reviewed; 314 AA.
AC P43357; Q6FHI6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Melanoma-associated antigen 3 {ECO:0000305};
DE AltName: Full=Antigen MZ2-D;
DE AltName: Full=Cancer/testis antigen 1.3;
DE Short=CT1.3;
DE AltName: Full=MAGE-3 antigen {ECO:0000303|PubMed:8113684};
GN Name=MAGEA3 {ECO:0000303|PubMed:29779948, ECO:0000312|HGNC:HGNC:6801};
GN Synonyms=MAGE3 {ECO:0000303|PubMed:8113684};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF ASP-170 AND TYR-176.
RC TISSUE=Blood;
RX PubMed=8113684; DOI=10.1084/jem.179.3.921;
RA Gaugler B., van den Eynde B., van der Bruggen P., Romero P., Gaforio J.J.,
RA De Plaen E., Lethe B.G., Brasseur F., Boon T.;
RT "Human gene MAGE-3 codes for an antigen recognized on a melanoma by
RT autologous cytolytic T lymphocytes.";
RL J. Exp. Med. 179:921-930(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RX PubMed=8037761; DOI=10.1006/bbrc.1994.1963;
RA Ding M., Beck R.J., Keller C.J., Fenton R.G.;
RT "Cloning and analysis of MAGE-1-related genes.";
RL Biochem. Biophys. Res. Commun. 202:549-555(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10854409; DOI=10.1101/gr.10.6.758;
RA Mallon A.-M., Platzer M., Bate R., Gloeckner G., Botcherby M.R.M.,
RA Nordsiek G., Strivens M.A., Kioschis P., Dangel A., Cunningham D.,
RA Straw R.N.A., Weston P., Gilbert M., Fernando S., Goodall K., Hunter G.,
RA Greystrong J.S., Clarke D., Kimberley C., Goerdes M., Blechschmidt K.,
RA Rump A., Hinzmann B., Mundy C.R., Miller W., Poustka A., Herman G.E.,
RA Rhodes M., Denny P., Rosenthal A., Brown S.D.M.;
RT "Comparative genome sequence analysis of the Bpa/Str region in mouse and
RT man.";
RL Genome Res. 10:758-775(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Lung, Prostate, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH TRIM28.
RX PubMed=17942928; DOI=10.1158/0008-5472.can-07-1478;
RA Yang B., O'Herrin S.M., Wu J., Reagan-Shaw S., Ma Y., Bhat K.M.,
RA Gravekamp C., Setaluri V., Peters N., Hoffmann F.M., Peng H., Ivanov A.V.,
RA Simpson A.J., Longley B.J.;
RT "MAGE-A, mMage-b, and MAGE-C proteins form complexes with KAP1 and suppress
RT p53-dependent apoptosis in MAGE-positive cell lines.";
RL Cancer Res. 67:9954-9962(2007).
RN [9]
RP FUNCTION, AND INTERACTION WITH TRIM28.
RX PubMed=20864041; DOI=10.1016/j.molcel.2010.08.029;
RA Doyle J.M., Gao J., Wang J., Yang M., Potts P.R.;
RT "MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases.";
RL Mol. Cell 39:963-974(2010).
RN [10]
RP UBIQUITINATION.
RX PubMed=29779948; DOI=10.1016/j.cell.2018.04.028;
RA Koren I., Timms R.T., Kula T., Xu Q., Li M.Z., Elledge S.J.;
RT "The eukaryotic proteome is shaped by E3 ubiquitin ligases targeting C-
RT terminal degrons.";
RL Cell 173:1622-1635(2018).
RN [11]
RP FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF GLU-314.
RX PubMed=31267705; DOI=10.15252/embr.201847352;
RA Ravichandran R., Kodali K., Peng J., Potts P.R.;
RT "Regulation of MAGE-A3/6 by the CRL4-DCAF12 ubiquitin ligase and nutrient
RT availability.";
RL EMBO Rep. 20:e47352-e47352(2019).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 271-279 IN COMPLEX WITH HLA CLASS
RP I HISTOCOMPATIBILITY COMPLEX.
RA Orth P., Alings C., Saenger W., Ziegler A.;
RT "Human class I histocompatibility antigen (HLA-A complex with a nonameric
RT peptide from melanoma-associated antigen 3 (residues 271-279).";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Activator of ubiquitin ligase activity of RING-type zinc
CC finger-containing E3 ubiquitin-protein ligases that acts as a as
CC repressor of autophagy (PubMed:20864041, PubMed:31267705). May enhance
CC ubiquitin ligase activity of TRIM28 and stimulate p53/TP53
CC ubiquitination by TRIM28. Proposed to act through recruitment and/or
CC stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate
CC complex (PubMed:17942928, PubMed:20864041). May play a role in
CC embryonal development and tumor transformation or aspects of tumor
CC progression (PubMed:17942928, PubMed:20864041). In vitro promotes cell
CC viability in melanoma cell lines (PubMed:17942928). Antigen recognized
CC on a melanoma by autologous cytolytic T-lymphocytes (PubMed:8113684).
CC {ECO:0000269|PubMed:17942928, ECO:0000269|PubMed:20864041,
CC ECO:0000269|PubMed:31267705, ECO:0000269|PubMed:8113684}.
CC -!- SUBUNIT: Interacts with TRIM28. {ECO:0000269|PubMed:17942928,
CC ECO:0000269|PubMed:20864041, ECO:0000269|Ref.12}.
CC -!- INTERACTION:
CC P43357; O00154-4: ACOT7; NbExp=3; IntAct=EBI-5651459, EBI-12007918;
CC P43357; Q8IXM2: BAP18; NbExp=3; IntAct=EBI-5651459, EBI-4280811;
CC P43357; Q9BQE9: BCL7B; NbExp=3; IntAct=EBI-5651459, EBI-2560588;
CC P43357; Q9BW66: CINP; NbExp=3; IntAct=EBI-5651459, EBI-739784;
CC P43357; O00471: EXOC5; NbExp=3; IntAct=EBI-5651459, EBI-949824;
CC P43357; P42858: HTT; NbExp=6; IntAct=EBI-5651459, EBI-466029;
CC P43357; A0A0C4DGT3: IQSEC1; NbExp=3; IntAct=EBI-5651459, EBI-12064916;
CC P43357; Q86VH2: KIF27; NbExp=3; IntAct=EBI-5651459, EBI-7950718;
CC P43357; Q9Y333: LSM2; NbExp=3; IntAct=EBI-5651459, EBI-347416;
CC P43357; P49585: PCYT1A; NbExp=3; IntAct=EBI-5651459, EBI-2563309;
CC P43357; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-5651459, EBI-6257312;
CC P43357; P06702: S100A9; NbExp=3; IntAct=EBI-5651459, EBI-1055001;
CC P43357; Q96FJ0: STAMBPL1; NbExp=4; IntAct=EBI-5651459, EBI-745021;
CC P43357; Q13263: TRIM28; NbExp=3; IntAct=EBI-5651459, EBI-78139;
CC -!- TISSUE SPECIFICITY: Expressed in many tumors of several types, such as
CC melanoma, head and neck squamous cell carcinoma, lung carcinoma and
CC breast carcinoma, but not in normal tissues except for testes and
CC placenta. Never expressed in kidney tumors, Leukemias and lymphomas.
CC {ECO:0000269|PubMed:8113684}.
CC -!- PTM: Ubiquitinated by the DCX(DCAF12) complex specifically recognizes
CC the diglutamate (Glu-Glu) at the C-terminus, leading to its
CC degradation. {ECO:0000269|PubMed:29779948,
CC ECO:0000269|PubMed:31267705}.
CC -!- CAUTION: In vitro experiments measuring cell viability in melanoma cell
CC lines used siRNA specific for MAGEA3 and MAGEA6.
CC {ECO:0000269|PubMed:17942928}.
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DR EMBL; U03735; AAA17446.1; -; Genomic_DNA.
DR EMBL; U82671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR541767; CAG46566.1; -; mRNA.
DR EMBL; CR541774; CAG46573.1; -; mRNA.
DR EMBL; AK292384; BAF85073.1; -; mRNA.
DR EMBL; BC000340; AAH00340.1; -; mRNA.
DR EMBL; BC005963; AAH05963.1; -; mRNA.
DR EMBL; BC011744; AAH11744.1; -; mRNA.
DR EMBL; BC016803; AAH16803.1; -; mRNA.
DR EMBL; BC017389; AAH17389.1; -; mRNA.
DR CCDS; CCDS76045.1; -.
DR PIR; JC2361; JC2361.
DR RefSeq; NP_005353.1; NM_005362.3.
DR RefSeq; XP_005274733.1; XM_005274676.3.
DR RefSeq; XP_006724881.1; XM_006724818.2.
DR RefSeq; XP_011529462.1; XM_011531160.2.
DR RefSeq; XP_011529463.1; XM_011531161.2.
DR PDB; 1QEW; X-ray; 2.20 A; C=271-279.
DR PDB; 4V0P; X-ray; 2.07 A; A=104-314.
DR PDB; 5BRZ; X-ray; 2.62 A; C=168-176.
DR PDBsum; 1QEW; -.
DR PDBsum; 4V0P; -.
DR PDBsum; 5BRZ; -.
DR AlphaFoldDB; P43357; -.
DR SMR; P43357; -.
DR BioGRID; 110276; 137.
DR DIP; DIP-44886N; -.
DR IntAct; P43357; 15.
DR STRING; 9606.ENSP00000473093; -.
DR ChEMBL; CHEMBL4662941; -.
DR iPTMnet; P43357; -.
DR PhosphoSitePlus; P43357; -.
DR BioMuta; MAGEA3; -.
DR DMDM; 1170857; -.
DR jPOST; P43357; -.
DR MassIVE; P43357; -.
DR MaxQB; P43357; -.
DR PaxDb; P43357; -.
DR PeptideAtlas; P43357; -.
DR PRIDE; P43357; -.
DR ProteomicsDB; 55619; -.
DR Antibodypedia; 30766; 459 antibodies from 30 providers.
DR DNASU; 4102; -.
DR Ensembl; ENST00000370278.4; ENSP00000359301.3; ENSG00000221867.9.
DR Ensembl; ENST00000598245.2; ENSP00000473093.1; ENSG00000221867.9.
DR GeneID; 4102; -.
DR KEGG; hsa:4102; -.
DR MANE-Select; ENST00000370278.4; ENSP00000359301.3; NM_005362.4; NP_005353.1.
DR UCSC; uc033faf.1; human.
DR CTD; 4102; -.
DR DisGeNET; 4102; -.
DR GeneCards; MAGEA3; -.
DR HGNC; HGNC:6801; MAGEA3.
DR HPA; ENSG00000221867; Tissue enriched (testis).
DR MIM; 300174; gene.
DR neXtProt; NX_P43357; -.
DR OpenTargets; ENSG00000221867; -.
DR PharmGKB; PA30547; -.
DR VEuPathDB; HostDB:ENSG00000221867; -.
DR eggNOG; KOG4562; Eukaryota.
DR GeneTree; ENSGT00940000164672; -.
DR HOGENOM; CLU_039582_1_2_1; -.
DR InParanoid; P43357; -.
DR OMA; HEWALRD; -.
DR OrthoDB; 1195799at2759; -.
DR PhylomeDB; P43357; -.
DR TreeFam; TF328505; -.
DR PathwayCommons; P43357; -.
DR SignaLink; P43357; -.
DR SIGNOR; P43357; -.
DR BioGRID-ORCS; 4102; 6 hits in 625 CRISPR screens.
DR ChiTaRS; MAGEA3; human.
DR EvolutionaryTrace; P43357; -.
DR GeneWiki; MAGEA3; -.
DR GenomeRNAi; 4102; -.
DR Pharos; P43357; Tbio.
DR PRO; PR:P43357; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P43357; protein.
DR Bgee; ENSG00000221867; Expressed in right testis and 31 other tissues.
DR ExpressionAtlas; P43357; baseline and differential.
DR Genevisible; P43357; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0089720; F:caspase binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR GO; GO:0010507; P:negative regulation of autophagy; IDA:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010955; P:negative regulation of protein processing; IDA:ParkinsonsUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.1200; -; 1.
DR Gene3D; 1.10.10.1210; -; 1.
DR InterPro; IPR037445; MAGE.
DR InterPro; IPR021072; MAGE_N.
DR InterPro; IPR041898; MAGE_WH1.
DR InterPro; IPR041899; MAGE_WH2.
DR InterPro; IPR030097; MAGEA3/MAGEA6.
DR InterPro; IPR002190; MHD_dom.
DR PANTHER; PTHR11736; PTHR11736; 1.
DR PANTHER; PTHR11736:SF60; PTHR11736:SF60; 1.
DR Pfam; PF01454; MAGE; 1.
DR Pfam; PF12440; MAGE_N; 1.
DR SMART; SM01373; MAGE; 1.
DR SMART; SM01392; MAGE_N; 1.
DR PROSITE; PS50838; MAGE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Tumor antigen; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..314
FT /note="Melanoma-associated antigen 3"
FT /id="PRO_0000156703"
FT DOMAIN 109..308
FT /note="MAGE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00127"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 170
FT /note="D->A: Abolishes HLA-A1 binding."
FT /evidence="ECO:0000269|PubMed:8113684"
FT MUTAGEN 176
FT /note="Y->A: Abolishes HLA-A1 binding."
FT /evidence="ECO:0000269|PubMed:8113684"
FT MUTAGEN 314
FT /note="E->EDNYNEPKANQ: Abolished recognition by the
FT DCX(DCAF12) complex and ubiquitination."
FT /evidence="ECO:0000269|PubMed:31267705"
FT HELIX 104..126
FT /evidence="ECO:0007829|PDB:4V0P"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:4V0P"
FT HELIX 141..146
FT /evidence="ECO:0007829|PDB:4V0P"
FT HELIX 147..162
FT /evidence="ECO:0007829|PDB:4V0P"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:4V0P"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:4V0P"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:4V0P"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:4V0P"
FT HELIX 199..212
FT /evidence="ECO:0007829|PDB:4V0P"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:4V0P"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:4V0P"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:4V0P"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:4V0P"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:4V0P"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:4V0P"
FT HELIX 283..292
FT /evidence="ECO:0007829|PDB:4V0P"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:4V0P"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:4V0P"
SQ SEQUENCE 314 AA; 34747 MW; 3F5EB13D1C9946A1 CRC64;
MPLEQRSQHC KPEEGLEARG EALGLVGAQA PATEEQEAAS SSSTLVEVTL GEVPAAESPD
PPQSPQGASS LPTTMNYPLW SQSYEDSSNQ EEEGPSTFPD LESEFQAALS RKVAELVHFL
LLKYRAREPV TKAEMLGSVV GNWQYFFPVI FSKASSSLQL VFGIELMEVD PIGHLYIFAT
CLGLSYDGLL GDNQIMPKAG LLIIVLAIIA REGDCAPEEK IWEELSVLEV FEGREDSILG
DPKKLLTQHF VQENYLEYRQ VPGSDPACYE FLWGPRALVE TSYVKVLHHM VKISGGPHIS
YPPLHEWVLR EGEE
