P15530 (CD79B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
B-cell antigen receptor complex-associated protein beta chain

Alternative name(s):
B-cell-specific glycoprotein B29
Ig-beta
Immunoglobulin-associated B29 protein
CD_antigen=CD79b

Gene names

Name:	Cd79b
Synonyms:	Igb

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	228 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.8 Ref.11 Ref.13 Ref.14
Subunit structure	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. Ref.6 Ref.7 Ref.9 Ref.15
Subcellular location	Cell membrane; Single-pass type I membrane protein. 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. Ref.10 Ref.12 Ref.14
Tissue specificity	B-cells.
Post-translational modification	Phosphorylated on tyrosine upon B-cell activation by SRC-type Tyr-kinases such as BLK, LYN and SYK. Ref.7 Ref.9
Sequence similarities	Contains 1 Ig-like V-type (immunoglobulin-like) domain. Contains 1 ITAM domain.

Ontologies

Keywords
Biological process	Adaptive immunity Immunity
Cellular component	Cell membrane Membrane
Domain	Immunoglobulin domain Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell receptor signaling pathway Inferred from direct assay PubMed 1373499PubMed 8626447. Source: MGI
Cellular_component	B cell receptor complex Inferred from direct assay PubMed 1373499PubMed 8626447. Source: MGI Golgi apparatus Inferred from electronic annotation. Source: Compara external side of plasma membrane Inferred from direct assay PubMed 1373499. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	transmembrane signaling receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Chain

26 – 228

203

B-cell antigen receptor complex-associated protein beta chain

PRO_0000014561

Regions

Topological domain

26 – 158

133

Extracellular Potential

Transmembrane

159 – 180

22

Helical; Potential

Topological domain

181 – 228

48

Cytoplasmic Potential

Domain

41 – 132

92

Ig-like V-type

Domain

184 – 212

29

ITAM

Amino acid modifications

Modified residue

195

1

Phosphotyrosine; by SRC-type Tyr-kinases Ref.9

Modified residue

206

1

Phosphotyrosine; by SRC-type Tyr-kinases Ref.9

Glycosylation

68

1

N-linked (GlcNAc...) Potential

Glycosylation

99

1

N-linked (GlcNAc...) Potential

Glycosylation

130

1

N-linked (GlcNAc...) Potential

Disulfide bond

43 ↔ 135

Ref.15

Disulfide bond

65 ↔ 120

Ref.15

Disulfide bond

135

Interchain (with C-113 in alpha chain) Ref.15

Secondary structure

1

.

.

.

.

.

.

.

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.

.

.

.

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228

Helix Strand Turn

Details...

Beta strand

45 – 49

5

Beta strand

51 – 56

6

Beta strand

61 – 71

11

Beta strand

73 – 78

6

Beta strand

84 – 86

3

Turn

90 – 93

4

Beta strand

94 – 99

6

Beta strand

102 – 107

6

Helix

112 – 114

3

Beta strand

116 – 124

9

Beta strand

131 – 134

4

Beta strand

137 – 142

6

Sequences

	Sequence		Length	Mass (Da)
	P15530 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 9A3A2008648E8307	FASTA	228	25,726
	10 20 30 40 50 60 MATLVLSSMP CHWLLFLLLL FSGEPVPAMT SSDLPLNFQG SPCSQIWQHP RFAAKKRSSM 70 80 90 100 110 120 VKFHCYTNHS GALTWFRKRG SQQPQELVSE EGRIVQTQNG SVYTLTIQNI QYEDNGIYFC 130 140 150 160 170 180 KQKCDSANHN VTDSCGTELL VLGFSTLDQL KRRNTLKDGI ILIQTLLIIL FIIVPIFLLL 190 200 210 220 DKDDGKAGME EDHTYEGLNI DQTATYEDIV TLRTGEVKWS VGEHPGQE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"B29: a member of the immunoglobulin gene superfamily exclusively expressed on beta-lineage cells." Hermanson G.G., Eisenberg D., Kincade P.W., Wall R. Proc. Natl. Acad. Sci. U.S.A. 85:6890-6894(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: B-cell.
[2]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Spleen.
[3]	"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)." Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Salivary gland.
[5]	"Immunoglobulin enhancer and promoter motifs 5' of the B29 B-cell-specific gene." Hermanson G.G., Briskin M., Sigman D., Wall R. Proc. Natl. Acad. Sci. U.S.A. 86:7341-7345(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
[6]	"The MB-1/B29 heterodimer couples the B cell antigen receptor to multiple src family protein tyrosine kinases." Lin J., Justement L.B. J. Immunol. 149:1548-1555(1992) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BLK.
[7]	"B-cell antigen receptor motifs have redundant signalling capabilities and bind the tyrosine kinases PTK72, Lyn and Fyn." Law D.A., Chan V.W., Datta S.K., DeFranco A.L. Curr. Biol. 3:645-657(1993) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LYN, PHOSPHORYLATION.
[8]	"Activation of B- and T-cells by the cytoplasmic domains of the B-cell antigen receptor proteins Ig-alpha and Ig-beta." Taddie J.A., Hurley T.R., Hardwick B.S., Sefton B.M. J. Biol. Chem. 269:13529-13535(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Reconstitution of the B cell antigen receptor signaling components in COS cells." Saouaf S.J., Kut S.A., Fargnoli J., Rowley R.B., Bolen J.B., Mahajan S. J. Biol. Chem. 270:27072-27078(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BLK, PHOSPHORYLATION AT TYR-195 AND TYR-206.
[10]	"A role for lipid rafts in B cell antigen receptor signaling and antigen targeting." Cheng P.C., Dykstra M.L., Mitchell R.N., Pierce S.K. J. Exp. Med. 190:1549-1560(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[11]	"Ig alpha and Ig beta are required for efficient trafficking to late endosomes and to enhance antigen presentation." Siemasko K., Eisfelder B.J., Stebbins C., Kabak S., Sant A.J., Song W., Clark M.R. J. Immunol. 162:6518-6525(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Translocation of the B cell antigen receptor into lipid rafts reveals a novel step in signaling." Cheng P.C., Brown B.K., Song W., Pierce S.K. J. Immunol. 166:3693-3701(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[13]	"Cooperative interaction of Ig(alpha) and Ig(beta) of the BCR regulates the kinetics and specificity of antigen targeting." Li C., Siemasko K., Clark M.R., Song W. Int. Immunol. 14:1179-1191(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Ig alpha/Ig beta complexes generate signals for B cell development independent of selective plasma membrane compartmentalization." Fuentes-Panana E.M., Bannish G., van der Voort D., King L.B., Monroe J.G. J. Immunol. 174:1245-1252(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]	"Structural and functional studies of Igalphabeta and its assembly with the B cell antigen receptor." Radaev S., Zou Z., Tolar P., Nguyen K., Nguyen A., Krueger P.D., Stutzman N., Pierce S., Sun P.D. Structure 18:934-943(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 27-159, SUBUNIT, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03857 mRNA. Translation: AAA37274.1.
AK143573 mRNA. Translation: BAE25444.1.
CT010358 mRNA. Translation: CAJ18566.1.
BC012226 mRNA. Translation: AAH12226.1.
AF002279 Genomic DNA. Translation: AAB93965.1.

IPI

IPI00131458.

PIR

B60228.

RefSeq

NP_032365.1. NM_008339.2.

UniGene

Mm.2987.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3KHO	X-ray	3.11	A/B	27-159	[»]
3KHQ	X-ray	1.70	A	27-159	[»]

ProteinModelPortal

P15530.

SMR

P15530. Positions 43-142.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59498N.

STRING

10090.ENSMUSP00000048239.

PTM databases

PhosphoSite

P15530.

Proteomic databases

PaxDb

P15530.

PRIDE

P15530.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000167143; ENSMUSP00000129029; ENSMUSG00000040592.

GeneID

15985.

KEGG

mmu:15985.

Organism-specific databases

CTD

974.

MGI

MGI:96431. Cd79b.

Phylogenomic databases

eggNOG

NOG46934.

GeneTree

ENSGT00510000048811.

HOVERGEN

HBG050855.

InParanoid

P15530.

KO

K06507.

OrthoDB

EOG48D0X0.

Enzyme and pathway databases

Reactome

REACT_107772. Immune System.

Gene expression databases

ArrayExpress

P15530.

Bgee

P15530.

CleanEx

MM_CD79B.

Genevestigator

P15530.

GermOnline

ENSMUSG00000040592. Mus musculus.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR003110. Phos_immunorcpt_sig_ITAM.
[Graphical view]

Pfam

PF02189. ITAM. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]

SMART

SM00409. IG. 1 hit.
SM00077. ITAM. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 1 hit.
PS51055. ITAM_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P15530.

NextBio

288780.

SOURCE

Search...

Entry information

Entry name

CD79B_MOUSE

Accession

Primary (citable) accession number: P15530
Secondary accession number(s): Q4FJP4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	May 1, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program