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CD83_MOUSE
ID   CD83_MOUSE              Reviewed;         196 AA.
AC   O88324;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=CD83 antigen;
DE            Short=mCD83;
DE   AltName: CD_antigen=CD83;
DE   Flags: Precursor;
GN   Name=Cd83;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129;
RX   PubMed=9799334; DOI=10.1007/s002510050449;
RA   Twist C.J., Beier D.R., Disteche C.M., Edelhoff S., Tedder T.F.;
RT   "The mouse Cd83 gene: structure, domain organization, and chromosome
RT   localization.";
RL   Immunogenetics 48:383-393(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Berchtold S., Muehl-Zuerbes P., Heufler C., Winklehner P., Schuler G.,
RA   Steinkasserer A.;
RT   "Cloning, recombinant expression and biochemical characterization of the
RT   murine CD83 molecule, which is specifically up-regulated during dendritic
RT   cell maturation.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Brain cortex, Spleen, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC   -!- FUNCTION: May play a significant role in antigen presentation or the
CC       cellular interactions that follow lymphocyte activation. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in spleen and brain, but is
CC       also detected in most tissues analyzed. {ECO:0000269|PubMed:9799334}.
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DR   EMBL; AF001036; AAC83185.1; -; mRNA.
DR   EMBL; AF001041; AAC83186.1; -; Genomic_DNA.
DR   EMBL; AF001037; AAC83186.1; JOINED; Genomic_DNA.
DR   EMBL; AF001038; AAC83186.1; JOINED; Genomic_DNA.
DR   EMBL; AF001039; AAC83186.1; JOINED; Genomic_DNA.
DR   EMBL; AF001040; AAC83186.1; JOINED; Genomic_DNA.
DR   EMBL; AJ245551; CAB63843.1; -; mRNA.
DR   EMBL; AK075888; BAC36032.1; -; mRNA.
DR   EMBL; AK139410; BAE23999.1; -; mRNA.
DR   EMBL; AK154862; BAE32886.1; -; mRNA.
DR   EMBL; AK156386; BAE33694.1; -; mRNA.
DR   EMBL; AK171716; BAE42629.1; -; mRNA.
DR   EMBL; AK172396; BAE42984.1; -; mRNA.
DR   EMBL; AK172449; BAE43011.1; -; mRNA.
DR   EMBL; AK172466; BAE43020.1; -; mRNA.
DR   EMBL; CH466546; EDL41001.1; -; Genomic_DNA.
DR   EMBL; BC107344; AAI07345.1; -; mRNA.
DR   EMBL; BC107345; AAI07346.1; -; mRNA.
DR   CCDS; CCDS26481.1; -.
DR   RefSeq; NP_033986.1; NM_009856.3.
DR   AlphaFoldDB; O88324; -.
DR   SMR; O88324; -.
DR   STRING; 10090.ENSMUSP00000015540; -.
DR   GlyGen; O88324; 3 sites.
DR   iPTMnet; O88324; -.
DR   PhosphoSitePlus; O88324; -.
DR   SwissPalm; O88324; -.
DR   PaxDb; O88324; -.
DR   PRIDE; O88324; -.
DR   ProteomicsDB; 280029; -.
DR   Antibodypedia; 3744; 973 antibodies from 41 providers.
DR   DNASU; 12522; -.
DR   Ensembl; ENSMUST00000015540; ENSMUSP00000015540; ENSMUSG00000015396.
DR   GeneID; 12522; -.
DR   KEGG; mmu:12522; -.
DR   UCSC; uc007qgj.2; mouse.
DR   CTD; 9308; -.
DR   MGI; MGI:1328316; Cd83.
DR   VEuPathDB; HostDB:ENSMUSG00000015396; -.
DR   eggNOG; ENOG502S7FP; Eukaryota.
DR   GeneTree; ENSGT00390000007302; -.
DR   HOGENOM; CLU_099481_0_0_1; -.
DR   InParanoid; O88324; -.
DR   OMA; SKPGMER; -.
DR   OrthoDB; 1491669at2759; -.
DR   PhylomeDB; O88324; -.
DR   TreeFam; TF337861; -.
DR   BioGRID-ORCS; 12522; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Cd83; mouse.
DR   PRO; PR:O88324; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; O88324; protein.
DR   Bgee; ENSMUSG00000015396; Expressed in peripheral lymph node and 198 other tissues.
DR   Genevisible; O88324; MM.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043367; P:CD4-positive, alpha-beta T cell differentiation; IMP:MGI.
DR   GO; GO:0032713; P:negative regulation of interleukin-4 production; IMP:MGI.
DR   GO; GO:0043372; P:positive regulation of CD4-positive, alpha-beta T cell differentiation; IMP:MGI.
DR   GO; GO:0032733; P:positive regulation of interleukin-10 production; IMP:MGI.
DR   GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:MGI.
DR   GO; GO:0014070; P:response to organic cyclic compound; IMP:MGI.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..196
FT                   /note="CD83 antigen"
FT                   /id="PRO_0000378451"
FT   TOPO_DOM        22..133
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        155..196
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          22..110
FT                   /note="Ig-like V-type"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        37..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   196 AA;  21313 MW;  026C1007BD7ABD1E CRC64;
     MSQGLQLLFL GCACSLAPAM AMREVTVACS ETADLPCTAP WDPQLSYAVS WAKVSESGTE
     SVELPESKQN SSFEAPRRRA YSLTIQNTTI CSSGTYRCAL QELGGQRNLS GTVVLKVTGC
     PKEATESTFR KYRAEAVLLF SLVVFYLTLI IFTCKFARLQ SIFPDISKPG TEQAFLPVTS
     PSKHLGPVTL PKTETV
 
 
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