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P35329 (CD22_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
B-cell receptor CD22
Alternative name(s):
B-lymphocyte cell adhesion molecule
Short name=BL-CAM
Sialic acid-binding Ig-like lectin 2
Short name=Siglec-2
T-cell surface antigen Leu-14
CD_antigen=CD22
Gene names
Name:Cd22
Synonyms:Lyb-8, Siglec2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length862 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules.

Subunit structure

Interacts with LYN, SYK, PIK3R1/PIK3R2, PLCG1, SHC1, INPP5D and GRB2 upon phosphorylation. May form a complex with INPP5D/SHIP, GRB2 and SHC1. Interacts with PTPN6/SHP-1 upon phosphorylation By similarity. Ref.6 Ref.7

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Tissue specificity

B-lymphocytes.

Domain

Contains 3 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.

Post-translational modification

Phosphorylated on tyrosine residues by LYN Probable. Ref.5 Ref.6 Ref.7

Phosphorylation of Tyr-777 and Tyr-837 are involved in binding to SYK. Phosphorylation of Tyr-822 is involved in binding to GRB2. Phosphorylation of Tyr-857 is involved in binding to SYK, PLCG2 and PIK3R1/PIK3R2.

Sequence similarities

Belongs to the immunoglobulin superfamily. SIGLEC (sialic acid binding Ig-like lectin) family.

Contains 6 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Grb2Q606314EBI-300059,EBI-1688
Ptpn6P293515EBI-300059,EBI-2620699

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35329-1)

Also known as: CD22-beta;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P35329-2)

The sequence of this isoform differs from the canonical sequence as follows:
     54-115: Missing.
Isoform 3 (identifier: P35329-3)

The sequence of this isoform differs from the canonical sequence as follows:
     100-133: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 862841B-cell receptor CD22
PRO_0000014874

Regions

Topological domain22 – 702681Extracellular Potential
Transmembrane703 – 72119Helical; Potential
Topological domain722 – 862141Cytoplasmic Potential
Domain22 – 142121Ig-like V-type
Domain147 – 24498Ig-like C2-type 1
Domain251 – 34191Ig-like C2-type 2
Domain346 – 42984Ig-like C2-type 3
Domain434 – 51582Ig-like C2-type 4
Domain520 – 59778Ig-like C2-type 5
Domain608 – 69184Ig-like C2-type 6
Motif775 – 7806ITIM motif 1
Motif835 – 8406ITIM motif 2
Motif855 – 8606ITIM motif 3

Sites

Binding site1241Sialic acid By similarity

Amino acid modifications

Modified residue7771Phosphotyrosine Probable
Modified residue8221Phosphotyrosine Probable
Modified residue8371Phosphotyrosine Probable
Modified residue8571Phosphotyrosine Probable
Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1391N-linked (GlcNAc...) Potential
Glycosylation1681N-linked (GlcNAc...) Potential
Glycosylation2651N-linked (GlcNAc...) Potential
Glycosylation2751N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential
Glycosylation4081N-linked (GlcNAc...) Potential
Glycosylation4601N-linked (GlcNAc...) Potential
Glycosylation5611N-linked (GlcNAc...) Potential
Glycosylation5891N-linked (GlcNAc...) Potential
Disulfide bond41 ↔ 171 By similarity
Disulfide bond46 ↔ 106 By similarity
Disulfide bond165 ↔ 229 By similarity
Disulfide bond272 ↔ 324 By similarity
Disulfide bond368 ↔ 411 By similarity
Disulfide bond457 ↔ 499 By similarity
Disulfide bond544 ↔ 586 By similarity
Disulfide bond631 ↔ 674 By similarity

Natural variations

Alternative sequence54 – 11562Missing in isoform 2.
VSP_002532
Alternative sequence100 – 13334Missing in isoform 3.
VSP_002533
Natural variant151A → V in strain: BALB/c, C57BL/6, BXSB and MRL.
Natural variant191Q → R in strain: BALB/c, C57BL/6, BXSB and MRL.
Natural variant761K → T in strain: BALB/c, C57BL/6 and MRL.
Natural variant83 – 864KAEP → ATKTEKDPES in strain: BALB/c, C57BL/6, BXSB and MRL.
Natural variant90 – 912PP → LS in strain: BALB/c.
Natural variant941R → G in strain: BALB/c.
Natural variant1021S → R in strain: BALB/c, C57BL/6, BXSB and MRL.
Natural variant112 – 1143PIR → LIH in strain: BXSB.
Natural variant1731E → G in strain: BALB/c, C57BL/6 and MRL.
Natural variant1791Q → K in strain: BALB/c, C57BL/6 and MRL.
Natural variant1861K → E in strain: BALB/c, C57BL/6 and MRL.
Natural variant1901V → I in strain: BALB/c, C57BL/6 and MRL.
Natural variant1921P → S in strain: BALB/c, C57BL/6 and MRL.
Natural variant2361E → K in strain: BALB/c, C57BL/6 and MRL.
Natural variant2411R → C in strain: BALB/c.
Natural variant2441R → H in strain: BALB/c and MRL.
Natural variant2731R → Q in strain: BXSB.
Natural variant3801T → I in strain: BXSB.
Natural variant3871P → H in strain: BXSB.
Natural variant4031P → L in strain: BXSB.
Natural variant4191H → R in strain: BXSB.
Natural variant4231D → G in strain: BXSB.
Natural variant4821P → S in strain: BXSB.
Natural variant5481E → K in strain: BXSB.
Natural variant6161S → I in strain: BALB/c.
Natural variant6201H → R in strain: BXSB.
Natural variant7141C → F in strain: BALB/c.
Natural variant7871M → T in strain: BALB/c, C57BL/6, BXSB and MRL.
Natural variant7901A → T in strain: C57BL/6.
Natural variant8081S → T in strain: BALB/c, BXSB and MRL.

Experimental info

Mutagenesis8221Y → F: Abolishes binding to GRB2. Ref.6
Sequence conflict871E → G in CAB85611. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CD22-beta) [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: A7662D6E87038E83

FASTA86296,582
        10         20         30         40         50         60 
MRVHYLWLLL ILGHAASAQY SSANDWTVDH PQTLFAWEGA CIRIPCKYKT PLPKARLDNI 

        70         80         90        100        110        120 
LLFQNYEFDK ATKKFKGTVL YNKAEPELYP PKQRRVTFLG NSIDNCTLKI HPIRANDSGN 

       130        140        150        160        170        180 
LGLRMTAGTE RWMEPIHLNV SEKPFQPYIQ MPSEIRESQS VTLTCGLNFS CFEYDILLQW 

       190        200        210        220        230        240 
FLEDSKITSV TPSVTSITSS VTSSIKNVYT ESKLTFQPKW TDHGKSVKCQ VQHSSEVLSE 

       250        260        270        280        290        300 
RTVRLDVKYT PKLEIKVNPT EVEKNNSVTM TCRVNSSNPK LRTVAVSWFK DGRPLEDQEL 

       310        320        330        340        350        360 
EQEQQMSKLI LHSVTKDMRG KYRCQASNDI GPGESEEVEL TVHYAPEPSR VHIYPSPAEE 

       370        380        390        400        410        420 
GQSVELICES LASPSATNYT WYHNRKPIPG DTQEKLRIPK VSPWHAGNYS CLAENRLGHG 

       430        440        450        460        470        480 
KIDQEAKLDV HYAPKAVTTV IQSFTPILEG DSVTLVCRYN SSNPDVTSYR WNPQGSGSVL 

       490        500        510        520        530        540 
KPGVLRIQKV TWDSMPVSCA ACNHKCSWAL PVILNVHYAP RDVKVLKVSP ASEIRAGQRV 

       550        560        570        580        590        600 
LLQCDFAESN PAEVRFFWKK NGSLVQEGRY LSFGSVSPED SGNYNCMVNN SIGETLSQAW 

       610        620        630        640        650        660 
NLQVLYAPRR LRVSISPGDH VMEGKKATLS CESDANPPIS QYTWFDSSGQ DLHSSGQKLR 

       670        680        690        700        710        720 
LEPLEVQHTG SYRCKGTNGI GTGESPPSTL TVYYSPETIG KRVALGLGFC LTICILAIWG 

       730        740        750        760        770        780 
MKIQKKWKQN RSQQGLQENS SGQSFFVRNK KARRTPLSEG PQSQGCYNPA MDDTVSYAIL 

       790        800        810        820        830        840 
RFPESDMHNA GDAGTPATQA PPPNNSDSVT YSVIQKRPMG DYENVNPSCP EDESIHYSEL 

       850        860 
VQFGAGKRPQ AKEDVDYVTL KH 

« Hide

Isoform 2 [UniParc].

Checksum: 394094553D0F14E6
Show »

FASTA80089,333
Isoform 3 [UniParc].

Checksum: 6C84F4BE3F0B6045
Show »

FASTA82892,857

References

[1]"Organization of the murine Cd22 locus. Mapping to chromosome 7 and characterization of two alleles."
Law C.-L., Torres R.M., Sundberg H.A., Parkhouse R.M., Brannan C.I., Copeland N.G., Jenkins N.A., Clark E.A.
J. Immunol. 151:175-187(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c and DBA/2J.
Tissue: Liver.
[2]"Polymorphisms in the Cd22 gene of inbred mouse strains."
Lajaunias F., Ibnou-Zekri N., Fossati Jimack L., Chicheportiche Y., Parkhouse R.M., Mary C., Reininger L., Brighouse G., Izui S.
Immunogenetics 49:991-995(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BXSB, C57BL/6 and MRL.
[3]"Dysregulated expression of the Cd22 gene as a result of a short interspersed nucleotide element insertion in Cd22alpha lupus-prone mice."
Mary C., Laporte C., Parzy D., Santiago M.L., Stefani F., Lajaunias F., Parkhouse M.E., O'Keefe T.L., Neuberger M.S., Izui S., Reininger L.
J. Immunol. 165:2987-2996(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-178 (ISOFORMS 1; 2 AND 3).
Strain: NZW.
Tissue: Spleen.
[4]"Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily."
Kelm S., Pelz A., Schauer R., Filbin M.T., Tang S., de Bellard M.E., Schnaar R.L., Mahoney J.A., Hartnell A., Bradfield P., Crocker P.R.
Curr. Biol. 4:965-972(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SIALIC ACID-BINDING.
[5]"Defective negative regulation of antigen receptor signaling in Lyn-deficient B lymphocytes."
Chan V.W., Lowell C.A., DeFranco A.L.
Curr. Biol. 8:545-553(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY LYN.
[6]"Analysis of tyrosine phosphorylation-dependent interactions between stimulatory effector proteins and the B cell co-receptor CD22."
Yohannan J., Wienands J., Coggeshall K.M., Justement L.B.
J. Biol. Chem. 274:18769-18776(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRB2; SYK; PIK3R1/PIK3R2 AND PLCG1, PHOSPHORYLATION AT TYR-777; TYR-822; TYR-837 AND TYR-857, MUTAGENESIS OF TYR-822.
[7]"CD22 forms a quaternary complex with SHIP, Grb2, and Shc. A pathway for regulation of B lymphocyte antigen receptor-induced calcium flux."
Poe J.C., Fujimoto M., Jansen P.J., Miller A.S., Tedder T.F.
J. Biol. Chem. 275:17420-17427(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRB2; SHC1 AND INPP5D, PHOSPHORYLATION BY LYN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L16928 mRNA. Translation: AAA02562.1.
AF115401 mRNA. Translation: AAD30392.1.
AF115400 mRNA. Translation: AAD30391.1.
AF102134 mRNA. Translation: AAF02417.1.
AJ250676 mRNA. Translation: CAB85609.1.
AJ250677 mRNA. Translation: CAB85610.1.
AJ250678 mRNA. Translation: CAB85611.1.
AJ250679 mRNA. Translation: CAB85612.1.
AJ250680 mRNA. Translation: CAB85613.1.
AJ250682 mRNA. Translation: CAB85615.1.
AJ250683 mRNA. Translation: CAB85616.1.
PIRA46512.
I49583.
RefSeqNP_001036782.1. NM_001043317.2.
NP_033975.3. NM_009845.3.
XP_006539556.1. XM_006539493.1.
XP_006539557.1. XM_006539494.1.
UniGeneMm.260994.

3D structure databases

ProteinModelPortalP35329.
SMRP35329. Positions 38-692.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP35329. 8 interactions.
MINTMINT-1659949.

Chemistry

BindingDBP35329.
ChEMBLCHEMBL1075279.

PTM databases

PhosphoSiteP35329.

Proteomic databases

MaxQBP35329.
PaxDbP35329.
PRIDEP35329.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID12483.
KEGGmmu:12483.

Organism-specific databases

CTD933.
MGIMGI:88322. Cd22.

Phylogenomic databases

eggNOGNOG287433.
HOVERGENHBG005272.
InParanoidP35329.
KOK06467.
PhylomeDBP35329.

Gene expression databases

CleanExMM_CD22.
GenevestigatorP35329.

Family and domain databases

Gene3D2.60.40.10. 6 hits.
InterProIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamPF08205. C2-set_2. 1 hit.
[Graphical view]
SMARTSM00409. IG. 2 hits.
SM00408. IGc2. 4 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio281386.
PROP35329.
SOURCESearch...

Entry information

Entry nameCD22_MOUSE
AccessionPrimary (citable) accession number: P35329
Secondary accession number(s): Q9JHL2 expand/collapse secondary AC list , Q9JJX9, Q9JJY0, Q9JJY1, Q9R056, Q9R094, Q9WU51
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 9, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot