CD79B_MOUSE
ID CD79B_MOUSE Reviewed; 228 AA.
AC P15530; Q4FJP4;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=B-cell antigen receptor complex-associated protein beta chain;
DE AltName: Full=B-cell-specific glycoprotein B29;
DE AltName: Full=Ig-beta;
DE AltName: Full=Immunoglobulin-associated B29 protein;
DE AltName: CD_antigen=CD79b;
DE Flags: Precursor;
GN Name=Cd79b; Synonyms=Igb;
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].
RC TISSUE=B-cell;
RX PubMed=3137575; DOI=10.1073/pnas.85.18.6890;
RA Hermanson G.G., Eisenberg D., Kincade P.W., Wall R.;
RT "B29: a member of the immunoglobulin gene superfamily exclusively expressed
RT on beta-lineage cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6890-6894(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
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].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RX PubMed=2508087; DOI=10.1073/pnas.86.19.7341;
RA Hermanson G.G., Briskin M., Sigman D., Wall R.;
RT "Immunoglobulin enhancer and promoter motifs 5' of the B29 B-cell-specific
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7341-7345(1989).
RN [6]
RP INTERACTION WITH BLK.
RX PubMed=1506682;
RA Lin J., Justement L.B.;
RT "The MB-1/B29 heterodimer couples the B cell antigen receptor to multiple
RT src family protein tyrosine kinases.";
RL J. Immunol. 149:1548-1555(1992).
RN [7]
RP INTERACTION WITH LYN, AND PHOSPHORYLATION.
RX PubMed=15335855; DOI=10.1016/0960-9822(93)90062-s;
RA Law D.A., Chan V.W., Datta S.K., DeFranco A.L.;
RT "B-cell antigen receptor motifs have redundant signalling capabilities and
RT bind the tyrosine kinases PTK72, Lyn and Fyn.";
RL Curr. Biol. 3:645-657(1993).
RN [8]
RP FUNCTION.
RX PubMed=8175787; DOI=10.1016/s0021-9258(17)36863-1;
RA Taddie J.A., Hurley T.R., Hardwick B.S., Sefton B.M.;
RT "Activation of B- and T-cells by the cytoplasmic domains of the B-cell
RT antigen receptor proteins Ig-alpha and Ig-beta.";
RL J. Biol. Chem. 269:13529-13535(1994).
RN [9]
RP INTERACTION WITH BLK, AND PHOSPHORYLATION AT TYR-195 AND TYR-206.
RX PubMed=7592958; DOI=10.1074/jbc.270.45.27072;
RA Saouaf S.J., Kut S.A., Fargnoli J., Rowley R.B., Bolen J.B., Mahajan S.;
RT "Reconstitution of the B cell antigen receptor signaling components in COS
RT cells.";
RL J. Biol. Chem. 270:27072-27078(1995).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=10587346; DOI=10.1084/jem.190.11.1549;
RA Cheng P.C., Dykstra M.L., Mitchell R.N., Pierce S.K.;
RT "A role for lipid rafts in B cell antigen receptor signaling and antigen
RT targeting.";
RL J. Exp. Med. 190:1549-1560(1999).
RN [11]
RP FUNCTION.
RX PubMed=10352267;
RA Siemasko K., Eisfelder B.J., Stebbins C., Kabak S., Sant A.J., Song W.,
RA Clark M.R.;
RT "Ig alpha and Ig beta are required for efficient trafficking to late
RT endosomes and to enhance antigen presentation.";
RL J. Immunol. 162:6518-6525(1999).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=11238609; DOI=10.4049/jimmunol.166.6.3693;
RA Cheng P.C., Brown B.K., Song W., Pierce S.K.;
RT "Translocation of the B cell antigen receptor into lipid rafts reveals a
RT novel step in signaling.";
RL J. Immunol. 166:3693-3701(2001).
RN [13]
RP FUNCTION.
RX PubMed=12356683; DOI=10.1093/intimm/14.10.1179;
RA Li C., Siemasko K., Clark M.R., Song W.;
RT "Cooperative interaction of Ig(alpha) and Ig(beta) of the BCR regulates the
RT kinetics and specificity of antigen targeting.";
RL Int. Immunol. 14:1179-1191(2002).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15661879; DOI=10.4049/jimmunol.174.3.1245;
RA Fuentes-Panana E.M., Bannish G., van der Voort D., King L.B., Monroe J.G.;
RT "Ig alpha/Ig beta complexes generate signals for B cell development
RT independent of selective plasma membrane compartmentalization.";
RL J. Immunol. 174:1245-1252(2005).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, 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 [16]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 27-159, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=20696394; DOI=10.1016/j.str.2010.04.019;
RA Radaev S., Zou Z., Tolar P., Nguyen K., Nguyen A., Krueger P.D.,
RA Stutzman N., Pierce S., Sun P.D.;
RT "Structural and functional studies of Igalphabeta and its assembly with the
RT B cell antigen receptor.";
RL Structure 18:934-943(2010).
CC -!- FUNCTION: Required in cooperation with CD79A for initiation of the
CC signal transduction cascade activated by the B-cell antigen receptor
CC complex (BCR) which leads to internalization of the complex,
CC trafficking to late endosomes and antigen presentation. Enhances
CC phosphorylation of CD79A, possibly by recruiting kinases which
CC phosphorylate CD79A or by recruiting proteins which bind to CD79A and
CC protect it from dephosphorylation. {ECO:0000269|PubMed:10352267,
CC ECO:0000269|PubMed:12356683, ECO:0000269|PubMed:15661879,
CC ECO:0000269|PubMed:8175787}.
CC -!- SUBUNIT: Heterodimer of alpha and beta chains; disulfide-linked. Part
CC of the B-cell antigen receptor complex where the alpha/beta chain
CC heterodimer is non-covalently associated with an antigen-specific
CC membrane-bound surface immunoglobulin of two heavy chains and two light
CC chains. Interacts with LYN. {ECO:0000269|PubMed:1506682,
CC ECO:0000269|PubMed:15335855, ECO:0000269|PubMed:20696394,
CC ECO:0000269|PubMed:7592958}.
CC -!- INTERACTION:
CC P15530; P15530: Cd79b; NbExp=3; IntAct=EBI-15869050, EBI-15869050;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10587346,
CC ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:10587346,
CC ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}.
CC Note=Following antigen binding, the BCR has been shown to translocate
CC from detergent-soluble regions of the cell membrane to lipid rafts
CC although signal transduction through the complex can also occur outside
CC lipid rafts.
CC -!- TISSUE SPECIFICITY: B-cells.
CC -!- PTM: Phosphorylated on tyrosine upon B-cell activation by SRC-type Tyr-
CC kinases such as BLK, LYN and SYK. {ECO:0000269|PubMed:15335855,
CC ECO:0000269|PubMed:7592958}.
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DR EMBL; J03857; AAA37274.1; -; mRNA.
DR EMBL; AK143573; BAE25444.1; -; mRNA.
DR EMBL; CT010358; CAJ18566.1; -; mRNA.
DR EMBL; BC012226; AAH12226.1; -; mRNA.
DR EMBL; AF002279; AAB93965.1; -; Genomic_DNA.
DR CCDS; CCDS48960.1; -.
DR PIR; B60228; B60228.
DR RefSeq; NP_001300868.1; NM_001313939.1.
DR RefSeq; NP_032365.1; NM_008339.3.
DR PDB; 3KHO; X-ray; 3.11 A; A/B=27-159.
DR PDB; 3KHQ; X-ray; 1.70 A; A=27-159.
DR PDBsum; 3KHO; -.
DR PDBsum; 3KHQ; -.
DR AlphaFoldDB; P15530; -.
DR SMR; P15530; -.
DR BioGRID; 200546; 3.
DR DIP; DIP-59498N; -.
DR ELM; P15530; -.
DR STRING; 10090.ENSMUSP00000048239; -.
DR GlyGen; P15530; 3 sites.
DR iPTMnet; P15530; -.
DR PhosphoSitePlus; P15530; -.
DR PaxDb; P15530; -.
DR PRIDE; P15530; -.
DR ProteomicsDB; 280028; -.
DR ABCD; P15530; 2 sequenced antibodies.
DR Antibodypedia; 2218; 1044 antibodies from 42 providers.
DR DNASU; 15985; -.
DR Ensembl; ENSMUST00000167143; ENSMUSP00000129029; ENSMUSG00000040592.
DR GeneID; 15985; -.
DR KEGG; mmu:15985; -.
DR UCSC; uc007lyt.2; mouse.
DR CTD; 974; -.
DR MGI; MGI:96431; Cd79b.
DR VEuPathDB; HostDB:ENSMUSG00000040592; -.
DR eggNOG; ENOG502S7X8; Eukaryota.
DR GeneTree; ENSGT00940000154363; -.
DR InParanoid; P15530; -.
DR OMA; YRGCGTE; -.
DR OrthoDB; 1234092at2759; -.
DR Reactome; R-MMU-5690714; CD22 mediated BCR regulation.
DR Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR BioGRID-ORCS; 15985; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Cd79b; mouse.
DR EvolutionaryTrace; P15530; -.
DR PRO; PR:P15530; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P15530; protein.
DR Bgee; ENSMUSG00000040592; Expressed in peripheral lymph node and 90 other tissues.
DR ExpressionAtlas; P15530; baseline and differential.
DR Genevisible; P15530; MM.
DR GO; GO:0019815; C:B cell receptor complex; IDA:MGI.
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:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0030183; P:B cell differentiation; IBA:GO_Central.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IDA:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR039695; CD79a/CD79b.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
DR PANTHER; PTHR14334; PTHR14334; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF02189; ITAM; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00077; ITAM; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51055; ITAM_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT CHAIN 26..228
FT /note="B-cell antigen receptor complex-associated protein
FT beta chain"
FT /id="PRO_0000014561"
FT TOPO_DOM 26..158
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..132
FT /note="Ig-like V-type"
FT DOMAIN 184..212
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 195
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379,
FT ECO:0000269|PubMed:7592958"
FT MOD_RES 206
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379,
FT ECO:0000269|PubMed:7592958"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20696394"
FT DISULFID 65..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20696394"
FT DISULFID 135
FT /note="Interchain (with C-113 in alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20696394"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:3KHQ"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:3KHQ"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:3KHQ"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3KHQ"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3KHO"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:3KHQ"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:3KHQ"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:3KHQ"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3KHQ"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:3KHQ"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:3KHO"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:3KHQ"
SQ SEQUENCE 228 AA; 25726 MW; 9A3A2008648E8307 CRC64;
MATLVLSSMP CHWLLFLLLL FSGEPVPAMT SSDLPLNFQG SPCSQIWQHP RFAAKKRSSM
VKFHCYTNHS GALTWFRKRG SQQPQELVSE EGRIVQTQNG SVYTLTIQNI QYEDNGIYFC
KQKCDSANHN VTDSCGTELL VLGFSTLDQL KRRNTLKDGI ILIQTLLIIL FIIVPIFLLL
DKDDGKAGME EDHTYEGLNI DQTATYEDIV TLRTGEVKWS VGEHPGQE
