MAGD1_PIG
ID MAGD1_PIG Reviewed; 784 AA.
AC Q6ITT4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Melanoma-associated antigen D1;
DE AltName: Full=MAGE-D1 antigen;
GN Name=MAGED1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim J.G., Vallet J.L., Nonneman D., Christenson R.K.;
RT "Characterization of porcine melanoma antigen, family D, 1 (MAGED1).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the apoptotic response after nerve growth factor
CC (NGF) binding in neuronal cells. Inhibits cell cycle progression, and
CC facilitates NGFR-mediated apoptosis. May act as a regulator of the
CC function of DLX family members. May enhance ubiquitin ligase activity
CC of RING-type zinc finger-containing E3 ubiquitin-protein ligases.
CC Proposed to act through recruitment and/or stabilization of the Ubl-
CC conjugating enzyme (E2) at the E3:substrate complex. Plays a role in
CC the circadian rhythm regulation. May act as RORA co-regulator,
CC modulating the expression of core clock genes such as ARNTL/BMAL1 and
CC NFIL3, induced, or NR1D1, repressed (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DLX5, DLX7 and MSX2 and forms homomultimers.
CC Interacts with UNC5A. Interacts with TRIM28 and PJA1. Interacts with
CC NGFR/p75NTR and RORA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus
CC {ECO:0000250}. Note=Expression shifts from the cytoplasm to the plasma
CC membrane upon stimulation with NGF. {ECO:0000250}.
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DR EMBL; AY626238; AAT45729.1; -; mRNA.
DR RefSeq; NP_001001860.1; NM_001001860.1.
DR RefSeq; XP_005673678.1; XM_005673621.2.
DR RefSeq; XP_013841594.1; XM_013986140.1.
DR RefSeq; XP_013841595.1; XM_013986141.1.
DR AlphaFoldDB; Q6ITT4; -.
DR SMR; Q6ITT4; -.
DR STRING; 9823.ENSSSCP00000013109; -.
DR PaxDb; Q6ITT4; -.
DR PRIDE; Q6ITT4; -.
DR Ensembl; ENSSSCT00005025585; ENSSSCP00005015493; ENSSSCG00005016162.
DR Ensembl; ENSSSCT00005025628; ENSSSCP00005015526; ENSSSCG00005016162.
DR Ensembl; ENSSSCT00015068560; ENSSSCP00015027455; ENSSSCG00015051346.
DR Ensembl; ENSSSCT00025055330; ENSSSCP00025023502; ENSSSCG00025040739.
DR Ensembl; ENSSSCT00030070815; ENSSSCP00030032316; ENSSSCG00030050793.
DR Ensembl; ENSSSCT00035020340; ENSSSCP00035007294; ENSSSCG00035015939.
DR Ensembl; ENSSSCT00040033687; ENSSSCP00040013876; ENSSSCG00040025138.
DR Ensembl; ENSSSCT00045051304; ENSSSCP00045035669; ENSSSCG00045030089.
DR Ensembl; ENSSSCT00050068239; ENSSSCP00050029270; ENSSSCG00050050152.
DR Ensembl; ENSSSCT00055059196; ENSSSCP00055047411; ENSSSCG00055029732.
DR Ensembl; ENSSSCT00055059233; ENSSSCP00055047437; ENSSSCG00055029732.
DR Ensembl; ENSSSCT00055059274; ENSSSCP00055047468; ENSSSCG00055029732.
DR Ensembl; ENSSSCT00060108766; ENSSSCP00060048546; ENSSSCG00060078654.
DR Ensembl; ENSSSCT00065010782; ENSSSCP00065004483; ENSSSCG00065008022.
DR Ensembl; ENSSSCT00070009498; ENSSSCP00070007790; ENSSSCG00070005001.
DR Ensembl; ENSSSCT00070010044; ENSSSCP00070008247; ENSSSCG00070005001.
DR GeneID; 414852; -.
DR KEGG; ssc:414852; -.
DR CTD; 9500; -.
DR eggNOG; KOG4562; Eukaryota.
DR HOGENOM; CLU_394113_0_0_1; -.
DR InParanoid; Q6ITT4; -.
DR OrthoDB; 1195799at2759; -.
DR TreeFam; TF352132; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unassembled WGS sequence.
DR Genevisible; Q6ITT4; SS.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR Gene3D; 1.10.10.1200; -; 1.
DR Gene3D; 1.10.10.1210; -; 1.
DR InterPro; IPR037445; MAGE.
DR InterPro; IPR041898; MAGE_WH1.
DR InterPro; IPR041899; MAGE_WH2.
DR InterPro; IPR030083; MAGED1.
DR InterPro; IPR002190; MHD_dom.
DR PANTHER; PTHR11736; PTHR11736; 1.
DR PANTHER; PTHR11736:SF28; PTHR11736:SF28; 1.
DR Pfam; PF01454; MAGE; 1.
DR SMART; SM01373; MAGE; 1.
DR PROSITE; PS50838; MAGE; 1.
PE 2: Evidence at transcript level;
KW Biological rhythms; Cell membrane; Cytoplasm; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Tumor antigen;
KW Ubl conjugation pathway.
FT CHAIN 1..784
FT /note="Melanoma-associated antigen D1"
FT /id="PRO_0000156725"
FT REPEAT 302..307
FT /note="1"
FT REPEAT 308..313
FT /note="2"
FT REPEAT 314..319
FT /note="3"
FT REPEAT 338..343
FT /note="4"
FT REPEAT 344..349
FT /note="5"
FT REPEAT 350..355
FT /note="6"
FT REPEAT 356..361
FT /note="7"
FT REPEAT 362..367
FT /note="8"
FT REPEAT 368..373
FT /note="9"
FT REPEAT 374..379
FT /note="10"
FT REPEAT 380..385
FT /note="11"
FT REPEAT 386..391
FT /note="12"
FT REPEAT 392..397
FT /note="13"
FT REPEAT 398..403
FT /note="14"
FT REPEAT 404..409
FT /note="15"
FT REPEAT 410..415
FT /note="16"
FT REPEAT 416..421
FT /note="17"
FT REPEAT 422..427
FT /note="18"
FT REPEAT 428..433
FT /note="19"
FT REPEAT 434..438
FT /note="20; approximate"
FT REPEAT 439..444
FT /note="21"
FT REPEAT 445..450
FT /note="22"
FT DOMAIN 477..675
FT /note="MAGE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00127"
FT REGION 41..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..450
FT /note="22 X 6 AA tandem repeats of W-[PQ]-X-P-X-X"
FT REGION 379..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5V3"
SQ SEQUENCE 784 AA; 86533 MW; 5F71BCC7C1E2C0FA CRC64;
MAQKMDCGAG LLGFQAEASV EDSTLLMQTL MEAIQISEAP PTNQATAAAS GPNASPQSSQ
PPSANEVADI QALAAATKPK TAFKAQNATT KGPNAAYDFS QALNAKEIPS TPPTVAFKAP
NAPSKGPNAA YDFSQAATTS ELTAKPEMAF KAQNATTKVG PNATYNFSPS LNANEMVNTQ
PKTAFKAWND TTKAPTAETQ TQNINQAKMA TSQADIEADP GPGICESDGA AAQTSADGSQ
AQNLESRTII RGKRTRKINN LNVEESSSGD QRRAPLAPGT WRSAPVPITT QSPPGAPPNV
LWQTPLAWQN PSGWQNQPAR QTPPARQSPP ARQTPPAWQN PVAWQNPVIW PNPVIWQNPV
IWPNPIVWPG PVVWPNPLAW QNPPGWQTPP GWQTPPGWQG PPDWQGPPDW PLPPDWPLPP
DWPLPTDWPL PPDWIPTDWP VPPDWQNLRP SPNLRPSPNS RASQNLGASQ PRDVALLQER
ANKLVKYLML KDYTKVPIKR SEMLRDIIRE YTDVYPEIIE RACFVLEKKF GIQLKEIDKE
EHLYILISTP ESLAGILGTT KDTPKLGLLL VILGVIFMNG NRASEAVLWE ALRKMGLRPG
VRHPLLGDLR KLLTYEFVKQ KYLDYRRVPN SNPPEYEFLW GLRSYHETSK MKVLRFIAEV
QKRDPRDWTA QFMEAADEAL DALDAAAAEA EARAEARTRM GIGDEAVSGP WSWDDIEFEL
LTWDEEGDFG DPWSRIPFTF WARYHQNARS RFPQTFAGPI IGPGGTASAN FAANFGAIGF
FWVE
