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MAGD1_RAT
ID   MAGD1_RAT               Reviewed;         775 AA.
AC   Q9ES73; Q66HP3; Q9JHZ6; Q9QX92;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 3.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Melanoma-associated antigen D1;
DE   AltName: Full=MAGE-D1 antigen;
DE   AltName: Full=Neurotrophin receptor-interacting MAGE homolog;
DE   AltName: Full=Sertoli cell necdin-related gene protein 1;
DE            Short=SNERG-1;
GN   Name=Maged1; Synonyms=Nrage;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN APOPTOSIS, AND INTERACTION WITH
RP   NGFR.
RC   STRAIN=Sprague-Dawley; TISSUE=Neural crest;
RX   PubMed=10985348; DOI=10.1016/s0896-6273(00)00036-2;
RA   Salehi A.H., Roux P.P., Kubu C.J., Zeindler C., Bhakar A., Tannis L.-L.,
RA   Verdi J.M., Barker P.A.;
RT   "NRAGE, a novel MAGE protein, interacts with the p75 neurotrophin receptor
RT   and facilitates nerve growth factor dependent apoptosis.";
RL   Neuron 27:279-288(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 206-775.
RC   TISSUE=Testis;
RX   PubMed=11014239; DOI=10.1210/endo.141.10.7705;
RA   Hennuy B., Reiter E., Cornet A., Bruyninx M., Daukandt M., Houssa P.,
RA   N'Guyen V.-H., Closset J., Hennen G.;
RT   "A novel messenger ribonucleic acid homologous to human MAGE-D is strongly
RT   expressed in rat Sertoli cells and weakly in Leydig cells and is regulated
RT   by follitropin, lutropin, and prolactin.";
RL   Endocrinology 141:3821-3831(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 178-775.
RA   Zhang C., He F.;
RT   "Rattus norvegicus mRNA for SNERG-1 protein, partial CDS.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH UNC5A.
RX   PubMed=12598531; DOI=10.1074/jbc.m300415200;
RA   Williams M.E., Strickland P., Watanabe K., Hinck L.;
RT   "UNC5H1 induces apoptosis via its juxtamembrane region through an
RT   interaction with NRAGE.";
RL   J. Biol. Chem. 278:17483-17490(2003).
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. {ECO:0000269|PubMed:10985348}.
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. {ECO:0000269|PubMed:10985348,
CC       ECO:0000269|PubMed:12598531}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC       protein. Nucleus {ECO:0000250}. Note=Expression shifts from the
CC       cytoplasm to the plasma membrane upon stimulation with NGF.
CC   -!- TISSUE SPECIFICITY: Ubiquitous and in the seminiferous tubules
CC       expressed in Sertoli cells but not in germ cells. Expression decreases
CC       in all tissues with increased age and is detectable only in brain
CC       cortex and lung.
CC   -!- DEVELOPMENTAL STAGE: Expressed at low levels throughout the embryo and
CC       is enriched in the developing brain and spinal cord.
CC   -!- INDUCTION: Follitropin decreased expression while lutropin and
CC       prolactin stimulated expression.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB65381.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF217964; AAG09705.1; -; mRNA.
DR   EMBL; BC081756; AAH81756.1; -; mRNA.
DR   EMBL; AJ133038; CAB65381.1; ALT_FRAME; mRNA.
DR   EMBL; AF274043; AAF75283.1; -; mRNA.
DR   RefSeq; NP_445861.1; NM_053409.2.
DR   AlphaFoldDB; Q9ES73; -.
DR   SMR; Q9ES73; -.
DR   BioGRID; 249969; 2.
DR   STRING; 10116.ENSRNOP00000009870; -.
DR   iPTMnet; Q9ES73; -.
DR   PhosphoSitePlus; Q9ES73; -.
DR   jPOST; Q9ES73; -.
DR   PaxDb; Q9ES73; -.
DR   PRIDE; Q9ES73; -.
DR   Ensembl; ENSRNOT00000009870; ENSRNOP00000009870; ENSRNOG00000006756.
DR   GeneID; 84469; -.
DR   KEGG; rno:84469; -.
DR   CTD; 9500; -.
DR   RGD; 70898; Maged1.
DR   eggNOG; KOG4562; Eukaryota.
DR   GeneTree; ENSGT00940000162070; -.
DR   HOGENOM; CLU_394113_0_0_1; -.
DR   InParanoid; Q9ES73; -.
DR   OMA; AVCHPLP; -.
DR   OrthoDB; 1195799at2759; -.
DR   PhylomeDB; Q9ES73; -.
DR   PRO; PR:Q9ES73; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000006756; Expressed in ovary and 20 other tissues.
DR   ExpressionAtlas; Q9ES73; baseline and differential.
DR   Genevisible; Q9ES73; RN.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
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; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0004705; F:JUN kinase activity; TAS:Reactome.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR   GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:RGD.
DR   GO; GO:1900181; P:negative regulation of protein localization to nucleus; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR   GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR   GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISO:RGD.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR   GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR   GO; GO:0042752; P:regulation of circadian rhythm; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
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   1: Evidence at protein level;
KW   Biological rhythms; Cell membrane; Cytoplasm; Membrane; Nucleus;
KW   Reference proteome; Repeat; Tumor antigen; Ubl conjugation pathway.
FT   CHAIN           1..775
FT                   /note="Melanoma-associated antigen D1"
FT                   /id="PRO_0000156726"
FT   REPEAT          293..298
FT                   /note="1"
FT   REPEAT          299..304
FT                   /note="2"
FT   REPEAT          305..310
FT                   /note="3"
FT   REPEAT          329..334
FT                   /note="4"
FT   REPEAT          335..340
FT                   /note="5"
FT   REPEAT          341..346
FT                   /note="6"
FT   REPEAT          347..352
FT                   /note="7"
FT   REPEAT          353..358
FT                   /note="8"
FT   REPEAT          359..364
FT                   /note="9"
FT   REPEAT          365..370
FT                   /note="10"
FT   REPEAT          371..376
FT                   /note="11"
FT   REPEAT          377..382
FT                   /note="12"
FT   REPEAT          383..388
FT                   /note="13"
FT   REPEAT          389..394
FT                   /note="14"
FT   REPEAT          395..400
FT                   /note="15"
FT   REPEAT          401..406
FT                   /note="16"
FT   REPEAT          407..412
FT                   /note="17"
FT   REPEAT          413..418
FT                   /note="18"
FT   REPEAT          419..424
FT                   /note="19"
FT   REPEAT          425..429
FT                   /note="20; approximate"
FT   REPEAT          430..435
FT                   /note="21"
FT   REPEAT          436..441
FT                   /note="22"
FT   DOMAIN          468..666
FT                   /note="MAGE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00127"
FT   REGION          37..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..441
FT                   /note="22 X 6 AA tandem repeats of W-[PQ]-X-P-X-X"
FT   REGION          374..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        178
FT                   /note="Q -> R (in Ref. 4; AAF75283)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        425..427
FT                   /note="WIP -> CIL (in Ref. 3; CAB65381 and 4; AAF75283)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        693..699
FT                   /note="IGDEAVS -> LETELCL (in Ref. 3; CAB65381 and 4;
FT                   AAF75283)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        724..725
FT                   /note="WS -> GP (in Ref. 4; AAF75283)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   775 AA;  85798 MW;  F8BF3B170B8A3742 CRC64;
     MAQKPDGGAG LRGFQAEASV EDSALLVQTL MEAIQISEAP PTSQATAAAS GPNASPQSSQ
     PPTANEKADT EVSAAAARPK TGFKAQNTTT KGPNDYSQAR NAKEMPKNQP KVAFKSQNAT
     SKGPHAASDF SHAASTGKSA AKKSEMAFKG QNTTTKAGPS ATYNFTQSPS ANEMTNNQPK
     TAKAWNDTTK IPGADAQTQN VNQAKMADVG TSAGISETDG AAAQTSADGS QAQNVESRTI
     IRGKRTRKIN NLNVEENSNG DQRRASLASG NWRSAPVPVT TQNPPGAPPN VLWQTPLAWQ
     NPSGWQNQTA RQTPPARQSP PARQTPSAWQ NPVAWQNPVI WPNPVIWQNP VIWPNPIVWP
     GPIVWPNPMA WQSTPGWQSP PSWQAPPSWQ SPQDWQGPPD WQLPPDWSMP PDWSFPSDWP
     FPPDWIPADW PIPPDWQNLR PSPNLRSSPN SRASQNQGPP QPRDVALLQE RANKLVKYLM
     LKDYTKVPIK RSEMLRDIIR EYTDVYPEII ERACFVLEKK FGIQLKEIDK EEHLYILIST
     PESLAGILGT TKDTPKLGLL LVILGIIFMN GNRATEAVLW EALRKMGLRP GVRHPLLGDL
     RKLLTYEFVK QKYLDYRRVP NSNPPEYEFL WGLRSYHETS KMKVLRFIAE VQKRDPRDWT
     AQFMEAADEA LDALDAAAAE AEARAEARNR MGIGDEAVSG PWSWDDIEFE LLTWDEEGDF
     GDPWSRIPFT FWARYHQNAR SRFPQAFTGP IIGPSGTATA NFAANFGAIG FFWVE
 
 
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