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B-cell antigen receptor complex-associated protein beta chain (B-cell-specific glycoprotein B29) (Ig-beta) (Immunoglobulin-associated B29 protein) (CD antigen CD79b)

 CD79B_MOUSE             Reviewed;         228 AA.
P15530; Q4FJP4;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
28-FEB-2018, entry version 163.
RecName: Full=B-cell antigen receptor complex-associated protein beta chain;
AltName: Full=B-cell-specific glycoprotein B29;
AltName: Full=Ig-beta;
AltName: Full=Immunoglobulin-associated B29 protein;
AltName: CD_antigen=CD79b;
Flags: Precursor;
Name=Cd79b; Synonyms=Igb;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=B-cell;
PubMed=3137575; DOI=10.1073/pnas.85.18.6890;
Hermanson G.G., Eisenberg D., Kincade P.W., Wall R.;
"B29: a member of the immunoglobulin gene superfamily exclusively
expressed on beta-lineage cells.";
Proc. Natl. Acad. Sci. U.S.A. 85:6890-6894(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
Mollenhauer J., Wiemann S., Schick M., Korn B.;
"Cloning of mouse full open reading frames in Gateway(R) system entry
vector (pDONR201).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
PubMed=2508087; DOI=10.1073/pnas.86.19.7341;
Hermanson G.G., Briskin M., Sigman D., Wall R.;
"Immunoglobulin enhancer and promoter motifs 5' of the B29 B-cell-
specific gene.";
Proc. Natl. Acad. Sci. U.S.A. 86:7341-7345(1989).
[6]
INTERACTION WITH BLK.
PubMed=1506682;
Lin J., Justement L.B.;
"The MB-1/B29 heterodimer couples the B cell antigen receptor to
multiple src family protein tyrosine kinases.";
J. Immunol. 149:1548-1555(1992).
[7]
INTERACTION WITH LYN, AND PHOSPHORYLATION.
PubMed=15335855; DOI=10.1016/0960-9822(93)90062-S;
Law D.A., Chan V.W., Datta S.K., DeFranco A.L.;
"B-cell antigen receptor motifs have redundant signalling capabilities
and bind the tyrosine kinases PTK72, Lyn and Fyn.";
Curr. Biol. 3:645-657(1993).
[8]
FUNCTION.
PubMed=8175787;
Taddie J.A., Hurley T.R., Hardwick B.S., Sefton B.M.;
"Activation of B- and T-cells by the cytoplasmic domains of the B-cell
antigen receptor proteins Ig-alpha and Ig-beta.";
J. Biol. Chem. 269:13529-13535(1994).
[9]
INTERACTION WITH BLK, AND PHOSPHORYLATION AT TYR-195 AND TYR-206.
PubMed=7592958; DOI=10.1074/jbc.270.45.27072;
Saouaf S.J., Kut S.A., Fargnoli J., Rowley R.B., Bolen J.B.,
Mahajan S.;
"Reconstitution of the B cell antigen receptor signaling components in
COS cells.";
J. Biol. Chem. 270:27072-27078(1995).
[10]
SUBCELLULAR LOCATION.
PubMed=10587346; DOI=10.1084/jem.190.11.1549;
Cheng P.C., Dykstra M.L., Mitchell R.N., Pierce S.K.;
"A role for lipid rafts in B cell antigen receptor signaling and
antigen targeting.";
J. Exp. Med. 190:1549-1560(1999).
[11]
FUNCTION.
PubMed=10352267;
Siemasko K., Eisfelder B.J., Stebbins C., Kabak S., Sant A.J.,
Song W., Clark M.R.;
"Ig alpha and Ig beta are required for efficient trafficking to late
endosomes and to enhance antigen presentation.";
J. Immunol. 162:6518-6525(1999).
[12]
SUBCELLULAR LOCATION.
PubMed=11238609; DOI=10.4049/jimmunol.166.6.3693;
Cheng P.C., Brown B.K., Song W., Pierce S.K.;
"Translocation of the B cell antigen receptor into lipid rafts reveals
a novel step in signaling.";
J. Immunol. 166:3693-3701(2001).
[13]
FUNCTION.
PubMed=12356683; DOI=10.1093/intimm/14.10.1179;
Li C., Siemasko K., Clark M.R., Song W.;
"Cooperative interaction of Ig(alpha) and Ig(beta) of the BCR
regulates the kinetics and specificity of antigen targeting.";
Int. Immunol. 14:1179-1191(2002).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15661879; DOI=10.4049/jimmunol.174.3.1245;
Fuentes-Panana E.M., Bannish G., van der Voort D., King L.B.,
Monroe J.G.;
"Ig alpha/Ig beta complexes generate signals for B cell development
independent of selective plasma membrane compartmentalization.";
J. Immunol. 174:1245-1252(2005).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 27-159, SUBUNIT, AND
DISULFIDE BONDS.
PubMed=20696394; DOI=10.1016/j.str.2010.04.019;
Radaev S., Zou Z., Tolar P., Nguyen K., Nguyen A., Krueger P.D.,
Stutzman N., Pierce S., Sun P.D.;
"Structural and functional studies of Igalphabeta and its assembly
with the B cell antigen receptor.";
Structure 18:934-943(2010).
-!- FUNCTION: Required in cooperation with CD79A for initiation of the
signal transduction cascade activated by the B-cell antigen
receptor complex (BCR) which leads to internalization of the
complex, trafficking to late endosomes and antigen presentation.
Enhances phosphorylation of CD79A, possibly by recruiting kinases
which phosphorylate CD79A or by recruiting proteins which bind to
CD79A and protect it from dephosphorylation.
{ECO:0000269|PubMed:10352267, ECO:0000269|PubMed:12356683,
ECO:0000269|PubMed:15661879, ECO:0000269|PubMed:8175787}.
-!- SUBUNIT: Heterodimer of alpha and beta chains; disulfide-linked.
Part of the B-cell antigen receptor complex where the alpha/beta
chain heterodimer is non-covalently associated with an antigen-
specific membrane-bound surface immunoglobulin of two heavy chains
and two light chains. Interacts with LYN.
{ECO:0000269|PubMed:1506682, ECO:0000269|PubMed:15335855,
ECO:0000269|PubMed:20696394, ECO:0000269|PubMed:7592958}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-15869050, EBI-15869050;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10587346,
ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}; Single-
pass type I membrane protein {ECO:0000269|PubMed:10587346,
ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}.
Note=Following antigen binding, the BCR has been shown to
translocate from detergent-soluble regions of the cell membrane to
lipid rafts although signal transduction through the complex can
also occur outside lipid rafts.
-!- TISSUE SPECIFICITY: B-cells.
-!- PTM: Phosphorylated on tyrosine upon B-cell activation by SRC-type
Tyr-kinases such as BLK, LYN and SYK.
{ECO:0000269|PubMed:15335855, ECO:0000269|PubMed:7592958}.
-----------------------------------------------------------------------
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EMBL; J03857; AAA37274.1; -; mRNA.
EMBL; AK143573; BAE25444.1; -; mRNA.
EMBL; CT010358; CAJ18566.1; -; mRNA.
EMBL; BC012226; AAH12226.1; -; mRNA.
EMBL; AF002279; AAB93965.1; -; Genomic_DNA.
CCDS; CCDS48960.1; -.
PIR; B60228; B60228.
RefSeq; NP_001300868.1; NM_001313939.1.
RefSeq; NP_032365.1; NM_008339.3.
UniGene; Mm.2987; -.
PDB; 3KHO; X-ray; 3.11 A; A/B=27-159.
PDB; 3KHQ; X-ray; 1.70 A; A=27-159.
PDBsum; 3KHO; -.
PDBsum; 3KHQ; -.
ProteinModelPortal; P15530; -.
SMR; P15530; -.
BioGrid; 200546; 2.
DIP; DIP-59498N; -.
ELM; P15530; -.
STRING; 10090.ENSMUSP00000129029; -.
iPTMnet; P15530; -.
PhosphoSitePlus; P15530; -.
PaxDb; P15530; -.
PRIDE; P15530; -.
Ensembl; ENSMUST00000167143; ENSMUSP00000129029; ENSMUSG00000040592.
GeneID; 15985; -.
KEGG; mmu:15985; -.
UCSC; uc007lyt.2; mouse.
CTD; 974; -.
MGI; MGI:96431; Cd79b.
eggNOG; ENOG410J02H; Eukaryota.
eggNOG; ENOG410Z4S5; LUCA.
GeneTree; ENSGT00510000048811; -.
HOVERGEN; HBG050855; -.
InParanoid; P15530; -.
KO; K06507; -.
Reactome; R-MMU-5690714; CD22 mediated BCR regulation.
Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
EvolutionaryTrace; P15530; -.
PRO; PR:P15530; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000040592; -.
CleanEx; MM_CD79B; -.
ExpressionAtlas; P15530; baseline and differential.
Genevisible; P15530; MM.
GO; GO:0019815; C:B cell receptor complex; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0030183; P:B cell differentiation; IBA:GO_Central.
GO; GO:0050853; P:B cell receptor signaling pathway; IDA:MGI.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
Pfam; PF07679; I-set; 1.
Pfam; PF02189; ITAM; 1.
SMART; SM00409; IG; 1.
SMART; SM00077; ITAM; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS51055; ITAM_1; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain;
Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 25
CHAIN 26 228 B-cell antigen receptor complex-
associated protein beta chain.
/FTId=PRO_0000014561.
TOPO_DOM 26 158 Extracellular. {ECO:0000255}.
TRANSMEM 159 180 Helical. {ECO:0000255}.
TOPO_DOM 181 228 Cytoplasmic. {ECO:0000255}.
DOMAIN 41 132 Ig-like V-type.
DOMAIN 184 212 ITAM. {ECO:0000255|PROSITE-
ProRule:PRU00379}.
MOD_RES 195 195 Phosphotyrosine; by SRC-type Tyr-kinases.
{ECO:0000255|PROSITE-ProRule:PRU00379,
ECO:0000269|PubMed:7592958}.
MOD_RES 206 206 Phosphotyrosine; by SRC-type Tyr-kinases.
{ECO:0000255|PROSITE-ProRule:PRU00379,
ECO:0000269|PubMed:7592958}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 43 124 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20696394}.
DISULFID 65 120 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20696394}.
DISULFID 135 135 Interchain (with C-113 in alpha chain).
{ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20696394}.
STRAND 45 49 {ECO:0000244|PDB:3KHQ}.
STRAND 51 56 {ECO:0000244|PDB:3KHQ}.
STRAND 61 71 {ECO:0000244|PDB:3KHQ}.
STRAND 73 78 {ECO:0000244|PDB:3KHQ}.
STRAND 84 86 {ECO:0000244|PDB:3KHO}.
TURN 90 93 {ECO:0000244|PDB:3KHQ}.
STRAND 94 99 {ECO:0000244|PDB:3KHQ}.
STRAND 102 107 {ECO:0000244|PDB:3KHQ}.
HELIX 112 114 {ECO:0000244|PDB:3KHQ}.
STRAND 116 124 {ECO:0000244|PDB:3KHQ}.
STRAND 131 134 {ECO:0000244|PDB:3KHO}.
STRAND 137 142 {ECO:0000244|PDB:3KHQ}.
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


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