CD20_MOUSE
ID CD20_MOUSE Reviewed; 291 AA.
AC P19437;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=B-lymphocyte antigen CD20;
DE AltName: Full=B-cell differentiation antigen Ly-44;
DE AltName: Full=Lymphocyte antigen 44;
DE AltName: Full=Membrane-spanning 4-domains subfamily A member 1;
DE AltName: CD_antigen=CD20;
GN Name=Ms4a1; Synonyms=Cd20, Ly-44, Ms4a2;
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 [MRNA].
RX PubMed=2461992;
RA Tedder T.F., Klejman G., Disteche C.M., Adler D.A., Schlossman S.F.,
RA Saito H.;
RT "Cloning of a complementary DNA encoding a new mouse B lymphocyte
RT differentiation antigen, homologous to the human B1 (CD20) antigen, and
RT localization of the gene to chromosome 19.";
RL J. Immunol. 141:4388-4394(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
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 [4]
RP SUBUNIT.
RX PubMed=8450218;
RA Dierks S.E., Bartlett W.C., Edmeades R.L., Gould H.J., Rao M., Conrad D.H.;
RT "The oligomeric nature of the murine Fc epsilon RII/CD23. Implications for
RT function.";
RL J. Immunol. 150:2372-2382(1993).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=14688067; DOI=10.1093/intimm/dxh009;
RA Uchida J., Lee Y., Hasegawa M., Liang Y., Bradney A., Oliver J.A.,
RA Bowen K., Steeber D.A., Haas K.M., Poe J.C., Tedder T.F.;
RT "Mouse CD20 expression and function.";
RL Int. Immunol. 16:119-129(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-219 AND THR-233, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=20038800; DOI=10.1172/jci40231;
RA Kuijpers T.W., Bende R.J., Baars P.A., Grummels A., Derks I.A.M.,
RA Dolman K.M., Beaumont T., Tedder T.F., van Noesel C.J.M., Eldering E.,
RA van Lier R.A.W.;
RT "CD20 deficiency in humans results in impaired T cell-independent antibody
RT responses.";
RL J. Clin. Invest. 120:214-222(2010).
CC -!- FUNCTION: B-lymphocyte-specific membrane protein that plays a role in
CC the regulation of cellular calcium influx necessary for the
CC development, differentiation, and activation of B-lymphocytes.
CC Functions as a store-operated calcium (SOC) channel component promoting
CC calcium influx after activation by the B-cell receptor/BCR.
CC {ECO:0000250|UniProtKB:P11836}.
CC -!- SUBUNIT: Forms homotetramers. Interacts with the heavy and light chains
CC of cell surface IgM, the antigen-binding components of the BCR.
CC {ECO:0000250|UniProtKB:P11836, ECO:0000269|PubMed:8450218}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11836};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P11836}. Cell
CC membrane {ECO:0000250|UniProtKB:P11836}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P11836}. Note=Constitutively associated with
CC membrane rafts. {ECO:0000250|UniProtKB:P11836}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice have severely impaired T-cell independent
CC antipolysaccharide antibody responses (PubMed:20038800). B-cell
CC development is predominantly normal in CD20-deficient mice but calcium
CC influx following CD19 or IgM ligation is reduced (PubMed:8450218).
CC {ECO:0000269|PubMed:20038800, ECO:0000269|PubMed:8450218}.
CC -!- SIMILARITY: Belongs to the MS4A family. {ECO:0000305}.
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DR EMBL; M62541; AAA37394.1; -; mRNA.
DR EMBL; AK017903; BAB30996.1; -; mRNA.
DR EMBL; BC028322; AAH28322.1; -; mRNA.
DR CCDS; CCDS37923.1; -.
DR PIR; A30558; A30558.
DR RefSeq; NP_031667.1; NM_007641.5.
DR AlphaFoldDB; P19437; -.
DR SMR; P19437; -.
DR BioGRID; 198580; 2.
DR IntAct; P19437; 2.
DR STRING; 10090.ENSMUSP00000126422; -.
DR iPTMnet; P19437; -.
DR PhosphoSitePlus; P19437; -.
DR jPOST; P19437; -.
DR PaxDb; P19437; -.
DR PRIDE; P19437; -.
DR ProteomicsDB; 281263; -.
DR Antibodypedia; 3497; 4004 antibodies from 61 providers.
DR DNASU; 12482; -.
DR Ensembl; ENSMUST00000169159; ENSMUSP00000126422; ENSMUSG00000024673.
DR GeneID; 12482; -.
DR KEGG; mmu:12482; -.
DR UCSC; uc008grw.1; mouse.
DR CTD; 931; -.
DR MGI; MGI:88321; Ms4a1.
DR VEuPathDB; HostDB:ENSMUSG00000024673; -.
DR eggNOG; ENOG502S6Z3; Eukaryota.
DR GeneTree; ENSGT00510000048781; -.
DR HOGENOM; CLU_082137_0_0_1; -.
DR InParanoid; P19437; -.
DR OMA; HFLKMER; -.
DR OrthoDB; 1251311at2759; -.
DR PhylomeDB; P19437; -.
DR TreeFam; TF335157; -.
DR BioGRID-ORCS; 12482; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ms4a1; mouse.
DR PRO; PR:P19437; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P19437; protein.
DR Bgee; ENSMUSG00000024673; Expressed in peripheral lymph node and 99 other tissues.
DR ExpressionAtlas; P19437; baseline and differential.
DR Genevisible; P19437; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019865; F:immunoglobulin binding; ISO:MGI.
DR GO; GO:0042113; P:B cell activation; ISO:MGI.
DR GO; GO:0030183; P:B cell differentiation; ISO:MGI.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISO:MGI.
DR GO; GO:1902656; P:calcium ion import into cytosol; ISO:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IDA:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0002115; P:store-operated calcium entry; ISO:MGI.
DR InterPro; IPR007237; CD20-like.
DR InterPro; IPR030417; MS4A.
DR InterPro; IPR030418; MS4A1.
DR PANTHER; PTHR23320; PTHR23320; 1.
DR PANTHER; PTHR23320:SF79; PTHR23320:SF79; 1.
DR Pfam; PF04103; CD20; 1.
PE 1: Evidence at protein level;
KW B-cell activation; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..291
FT /note="B-lymphocyte antigen CD20"
FT /id="PRO_0000158628"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..68
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..182
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 261..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 214
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 291 AA; 31958 MW; DF478ECD2C5C16FC CRC64;
MSGPFPAEPT KGPLAMQPAP KVNLKRTSSL VGPTQSFFMR ESKALGAVQI MNGLFHITLG
GLLMIPTGVF APICLSVWYP LWGGIMYIIS GSLLAAAAEK TSRKSLVKAK VIMSSLSLFA
AISGIILSIM DILNMTLSHF LKMRRLELIQ TSKPYVDIYD CEPSNSSEKN SPSTQYCNSI
QSVFLGILSA MLISAFFQKL VTAGIVENEW KRMCTRSKSN VVLLSAGEKN EQTIKMKEEI
IELSGVSSQP KNEEEIEIIP VQEEEEEEAE INFPAPPQEQ ESLPVENEIA P
