CD22_HUMAN
ID CD22_HUMAN Reviewed; 847 AA.
AC P20273; F5GYU4; F5H7U3; O95699; O95701; O95702; O95703; Q01665; Q32M46;
AC Q92872; Q92873; Q9UQA6; Q9UQA7; Q9UQA8; Q9UQA9; Q9UQB0; Q9Y2A6;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=B-cell receptor CD22 {ECO:0000305};
DE AltName: Full=B-lymphocyte cell adhesion molecule;
DE Short=BL-CAM;
DE AltName: Full=Sialic acid-binding Ig-like lectin 2;
DE Short=Siglec-2;
DE AltName: Full=T-cell surface antigen Leu-14;
DE AltName: CD_antigen=CD22;
DE Flags: Precursor;
GN Name=CD22 {ECO:0000303|PubMed:1691828, ECO:0000312|HGNC:HGNC:1643};
GN Synonyms=SIGLEC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CD22-BETA).
RX PubMed=1691828; DOI=10.1038/345074a0;
RA Stamenkovic I., Seed B.;
RT "The B-cell antigen CD22 mediates monocyte and erythrocyte adhesion.";
RL Nature 345:74-77(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CD22-BETA), AND VARIANT HIS-639.
RC TISSUE=Tonsil;
RX PubMed=1985119; DOI=10.1084/jem.173.1.137;
RA Wilson G.L., Fox C.H., Fauci A.S., Kehrl J.H.;
RT "cDNA cloning of the B cell membrane protein CD22: a mediator of B-B cell
RT interactions.";
RL J. Exp. Med. 173:137-146(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS CD22-ALPHA AND CD22-BETA).
RX PubMed=8496602;
RA Wilson G.L., Najfeld V., Kozlow E., Menniger J., Ward D., Kehrl J.H.;
RT "Genomic structure and chromosomal mapping of the human CD22 gene.";
RL J. Immunol. 150:5013-5024(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Spleen;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-137; 139-239; 241-328 AND 418-502,
RP AND VARIANTS THR-34; GLU-152; LYS-203; GLY-664; CYS-669 AND ASP-745.
RX PubMed=10079291; DOI=10.1007/s002510050494;
RA Hatta Y., Tsuchiya N., Matsushita M., Shiota M., Hagiwara K., Tokunaga K.;
RT "Identification of the gene variations in human CD22.";
RL Immunogenetics 49:280-286(1999).
RN [8]
RP SIALIC ACID-BINDING.
RX PubMed=8463235; DOI=10.1016/s0021-9258(18)53140-9;
RA Powell L.D., Sgroi D., Sjoberg E.R., Stamenkovic I., Varki A.;
RT "Natural ligands of the B cell adhesion molecule CD22 beta carry N-linked
RT oligosaccharides with alpha-2,6-linked sialic acids that are required for
RT recognition.";
RL J. Biol. Chem. 268:7019-7027(1993).
RN [9]
RP INTERACTION WITH PTPN6.
RX PubMed=7618087; DOI=10.1126/science.7618087;
RA Doody G.M., Justement L.B., Delibrias C.C., Matthews R.J., Lin J.,
RA Thomas M.L., Fearon D.T.;
RT "A role in B cell activation for CD22 and the protein tyrosine phosphatase
RT SHP.";
RL Science 269:242-244(1995).
RN [10]
RP INTERACTION WITH LYN; SYK AND PIK3R1/PIK3R2.
RX PubMed=8647200; DOI=10.1002/eji.1830260610;
RA Tuscano J.M., Engel P., Tedder T.F., Agarwal A., Kehrl J.H.;
RT "Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl inositol-3
RT kinase in signal transduction via the human B lymphocyte antigen CD22.";
RL Eur. J. Immunol. 26:1246-1252(1996).
RN [11]
RP INTERACTION WITH PTPN6; SYK AND PLCG1.
RX PubMed=8627166; DOI=10.1084/jem.183.2.547;
RA Law C.L., Sidorenko S.P., Chandran K.A., Zhao Z., Shen S.H., Fischer E.H.,
RA Clark E.A.;
RT "CD22 associates with protein tyrosine phosphatase 1C, Syk, and
RT phospholipase C-gamma(1) upon B cell activation.";
RL J. Exp. Med. 183:547-560(1996).
RN [12]
RP REVIEW.
RX PubMed=9143697; DOI=10.1146/annurev.immunol.15.1.481;
RA Tedder T.F., Tuscano J., Sato S., Kehrl J.H.;
RT "CD22, a B lymphocyte-specific adhesion molecule that regulates antigen
RT receptor signaling.";
RL Annu. Rev. Immunol. 15:481-504(1997).
CC -!- FUNCTION: Mediates B-cell B-cell interactions. May be involved in the
CC localization of B-cells in lymphoid tissues. Binds sialylated
CC glycoproteins; one of which is CD45. Preferentially binds to alpha-2,6-
CC linked sialic acid. The sialic acid recognition site can be masked by
CC cis interactions with sialic acids on the same cell surface. Upon
CC ligand induced tyrosine phosphorylation in the immune response seems to
CC be involved in regulation of B-cell antigen receptor signaling. Plays a
CC role in positive regulation through interaction with Src family
CC tyrosine kinases and may also act as an inhibitory receptor by
CC recruiting cytoplasmic phosphatases via their SH2 domains that block
CC signal transduction through dephosphorylation of signaling molecules.
CC -!- SUBUNIT: Predominantly monomer of isoform CD22-beta. Also found as
CC heterodimer of isoform CD22-beta and a shorter isoform. Interacts with
CC PTPN6/SHP-1, LYN, SYK, PIK3R1/PIK3R2 and PLCG1 upon phosphorylation.
CC Interacts with GRB2, INPP5D and SHC1 upon phosphorylation (By
CC similarity). May form a complex with INPP5D/SHIP, GRB2 and SHC1.
CC {ECO:0000250, ECO:0000269|PubMed:7618087, ECO:0000269|PubMed:8627166,
CC ECO:0000269|PubMed:8647200}.
CC -!- INTERACTION:
CC P20273; P07948: LYN; NbExp=2; IntAct=EBI-78277, EBI-79452;
CC P20273; P19174: PLCG1; NbExp=2; IntAct=EBI-78277, EBI-79387;
CC P20273; P29350: PTPN6; NbExp=4; IntAct=EBI-78277, EBI-78260;
CC P20273; P43405: SYK; NbExp=4; IntAct=EBI-78277, EBI-78302;
CC P20273-5; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-13320645, EBI-12109402;
CC P20273-5; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-13320645, EBI-741158;
CC P20273-5; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-13320645, EBI-2844246;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=CD22-beta;
CC IsoId=P20273-1; Sequence=Displayed;
CC Name=CD22-alpha;
CC IsoId=P20273-2; Sequence=VSP_002531;
CC Name=3;
CC IsoId=P20273-3; Sequence=VSP_045363;
CC Name=4;
CC IsoId=P20273-4; Sequence=VSP_047223, VSP_047224;
CC Name=5;
CC IsoId=P20273-5; Sequence=VSP_054619, VSP_054620;
CC -!- TISSUE SPECIFICITY: B-lymphocytes.
CC -!- DOMAIN: Contains 4 copies of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC -!- PTM: Phosphorylation of Tyr-762, Tyr-807 and Tyr-822 are involved in
CC binding to SYK, GRB2 and SYK, respectively. Phosphorylation of Tyr-842
CC is involved in binding to SYK, PLCG2 and PIK3R1/PIK3R2.
CC -!- PTM: Phosphorylated on tyrosine residues by LYN. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC acid binding Ig-like lectin) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA36988.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Siglec-2 [3 Fc Domains];
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_00001";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Siglec-2;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_269";
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DR EMBL; U62631; AAB06448.1; -; Genomic_DNA.
DR EMBL; U62631; AAB06449.1; -; Genomic_DNA.
DR EMBL; X59350; CAA42006.1; -; mRNA.
DR EMBL; X52785; CAA36988.1; ALT_FRAME; mRNA.
DR EMBL; AK225625; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC002132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC109306; AAI09307.1; -; mRNA.
DR EMBL; AB012995; BAA36564.1; -; Genomic_DNA.
DR EMBL; AB012996; BAA36565.1; -; Genomic_DNA.
DR EMBL; AB012997; BAA36566.1; -; Genomic_DNA.
DR EMBL; AB012998; BAA36567.1; -; Genomic_DNA.
DR EMBL; AB012999; BAA36568.1; -; Genomic_DNA.
DR EMBL; AB013000; BAA36569.1; -; Genomic_DNA.
DR EMBL; AB013002; BAA36571.1; -; Genomic_DNA.
DR EMBL; AB013003; BAA36572.1; -; Genomic_DNA.
DR EMBL; AB013004; BAA36573.1; -; Genomic_DNA.
DR EMBL; AB013006; BAA36575.1; -; Genomic_DNA.
DR CCDS; CCDS12457.1; -. [P20273-1]
DR CCDS; CCDS54247.1; -. [P20273-4]
DR CCDS; CCDS54248.1; -. [P20273-3]
DR CCDS; CCDS54249.1; -. [P20273-2]
DR CCDS; CCDS62634.1; -. [P20273-5]
DR PIR; A35648; A35648.
DR RefSeq; NP_001172028.1; NM_001185099.1. [P20273-3]
DR RefSeq; NP_001172029.1; NM_001185100.1. [P20273-4]
DR RefSeq; NP_001172030.1; NM_001185101.1. [P20273-2]
DR RefSeq; NP_001265346.1; NM_001278417.1. [P20273-5]
DR RefSeq; NP_001762.2; NM_001771.3. [P20273-1]
DR PDB; 5VKJ; X-ray; 2.12 A; A=20-330.
DR PDB; 5VKM; X-ray; 2.20 A; A=20-330.
DR PDB; 5VL3; X-ray; 3.10 A; Q/R/S/T=22-330.
DR PDB; 7O52; X-ray; 2.41 A; U=504-687.
DR PDBsum; 5VKJ; -.
DR PDBsum; 5VKM; -.
DR PDBsum; 5VL3; -.
DR PDBsum; 7O52; -.
DR AlphaFoldDB; P20273; -.
DR SASBDB; P20273; -.
DR SMR; P20273; -.
DR BioGRID; 107371; 37.
DR ELM; P20273; -.
DR IntAct; P20273; 14.
DR MINT; P20273; -.
DR STRING; 9606.ENSP00000085219; -.
DR BindingDB; P20273; -.
DR ChEMBL; CHEMBL3218; -.
DR DrugBank; DB04958; Epratuzumab.
DR DrugBank; DB05889; Inotuzumab ozogamicin.
DR DrugBank; DB12688; Moxetumomab pasudotox.
DR DrugCentral; P20273; -.
DR GuidetoPHARMACOLOGY; 2786; -.
DR UniLectin; P20273; -.
DR GlyGen; P20273; 18 sites.
DR iPTMnet; P20273; -.
DR PhosphoSitePlus; P20273; -.
DR BioMuta; CD22; -.
DR DMDM; 6166019; -.
DR jPOST; P20273; -.
DR MassIVE; P20273; -.
DR MaxQB; P20273; -.
DR PaxDb; P20273; -.
DR PeptideAtlas; P20273; -.
DR PRIDE; P20273; -.
DR ProteomicsDB; 24846; -.
DR ProteomicsDB; 27594; -.
DR ProteomicsDB; 53740; -. [P20273-1]
DR ProteomicsDB; 53741; -. [P20273-2]
DR ABCD; P20273; 34 sequenced antibodies.
DR Antibodypedia; 3714; 2402 antibodies from 56 providers.
DR DNASU; 933; -.
DR Ensembl; ENST00000085219.10; ENSP00000085219.4; ENSG00000012124.17. [P20273-1]
DR Ensembl; ENST00000341773.10; ENSP00000339349.6; ENSG00000012124.17. [P20273-2]
DR Ensembl; ENST00000419549.6; ENSP00000403822.2; ENSG00000012124.17. [P20273-5]
DR Ensembl; ENST00000536635.6; ENSP00000442279.1; ENSG00000012124.17. [P20273-3]
DR Ensembl; ENST00000544992.6; ENSP00000441237.1; ENSG00000012124.17. [P20273-4]
DR Ensembl; ENST00000594250.5; ENSP00000469984.1; ENSG00000012124.17. [P20273-2]
DR GeneID; 933; -.
DR KEGG; hsa:933; -.
DR MANE-Select; ENST00000085219.10; ENSP00000085219.4; NM_001771.4; NP_001762.2.
DR UCSC; uc002nzb.6; human. [P20273-1]
DR CTD; 933; -.
DR DisGeNET; 933; -.
DR GeneCards; CD22; -.
DR HGNC; HGNC:1643; CD22.
DR HPA; ENSG00000012124; Tissue enhanced (brain, lymphoid tissue, ovary).
DR MIM; 107266; gene.
DR neXtProt; NX_P20273; -.
DR OpenTargets; ENSG00000012124; -.
DR PharmGKB; PA26201; -.
DR VEuPathDB; HostDB:ENSG00000012124; -.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT01050000244990; -.
DR HOGENOM; CLU_017949_0_0_1; -.
DR InParanoid; P20273; -.
DR OMA; GCYICNA; -.
DR PhylomeDB; P20273; -.
DR TreeFam; TF334827; -.
DR PathwayCommons; P20273; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; P20273; -.
DR BioGRID-ORCS; 933; 18 hits in 1080 CRISPR screens.
DR ChiTaRS; CD22; human.
DR GeneWiki; CD22; -.
DR GenomeRNAi; 933; -.
DR Pharos; P20273; Tclin.
DR PRO; PR:P20273; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P20273; protein.
DR Bgee; ENSG00000012124; Expressed in spleen and 160 other tissues.
DR ExpressionAtlas; P20273; baseline and differential.
DR Genevisible; P20273; HS.
DR GO; GO:0009986; C:cell surface; ISS:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; TAS:ARUK-UCL.
DR GO; GO:0005769; C:early endosome; IDA:ARUK-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0032809; C:neuronal cell body membrane; ISS:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:ARUK-UCL.
DR GO; GO:0055037; C:recycling endosome; IDA:ARUK-UCL.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0042609; F:CD4 receptor binding; ISS:ARUK-UCL.
DR GO; GO:0001791; F:IgM binding; TAS:ARUK-UCL.
DR GO; GO:0019903; F:protein phosphatase binding; ISS:ARUK-UCL.
DR GO; GO:0033691; F:sialic acid binding; ISS:ARUK-UCL.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ARUK-UCL.
DR GO; GO:0042113; P:B cell activation; IDA:ARUK-UCL.
DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; IDA:ARUK-UCL.
DR GO; GO:0050849; P:negative regulation of calcium-mediated signaling; ISS:ARUK-UCL.
DR GO; GO:0002638; P:negative regulation of immunoglobulin production; ISS:ARUK-UCL.
DR GO; GO:0030888; P:regulation of B cell proliferation; ISS:ARUK-UCL.
DR GO; GO:0030100; P:regulation of endocytosis; IDA:ARUK-UCL.
DR GO; GO:0050776; P:regulation of immune response; ISS:ARUK-UCL.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 7.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Isopeptide bond;
KW Lectin; Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..847
FT /note="B-cell receptor CD22"
FT /id="PRO_0000014873"
FT TOPO_DOM 20..687
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..706
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 707..847
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..138
FT /note="Ig-like V-type"
FT DOMAIN 143..235
FT /note="Ig-like C2-type 1"
FT DOMAIN 242..326
FT /note="Ig-like C2-type 2"
FT DOMAIN 331..416
FT /note="Ig-like C2-type 3"
FT DOMAIN 419..500
FT /note="Ig-like C2-type 4"
FT DOMAIN 505..582
FT /note="Ig-like C2-type 5"
FT DOMAIN 593..676
FT /note="Ig-like C2-type 6"
FT MOTIF 760..765
FT /note="ITIM motif 1"
FT MOTIF 794..799
FT /note="ITIM motif 2"
FT MOTIF 820..825
FT /note="ITIM motif 3"
FT MOTIF 840..845
FT /note="ITIM motif 4"
FT BINDING 120
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35329"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35329"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35329"
FT MOD_RES 762
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35329"
FT MOD_RES 807
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35329"
FT MOD_RES 822
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35329"
FT MOD_RES 842
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35329"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 634
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 44..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 161..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 265..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 353..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 442..484
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 529..571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 616..659
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..3
FT /note="MHL -> MSL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054619"
FT VAR_SEQ 4..175
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054620"
FT VAR_SEQ 241..417
FT /note="Missing (in isoform CD22-alpha)"
FT /evidence="ECO:0000305"
FT /id="VSP_002531"
FT VAR_SEQ 330..417
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045363"
FT VAR_SEQ 737..751
FT /note="VRRAPLSEGPHSLGC -> RCRVLRDAETSPGLR (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047223"
FT VAR_SEQ 752..847
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047224"
FT VARIANT 34
FT /note="A -> T (in dbSNP:rs201453271)"
FT /evidence="ECO:0000269|PubMed:10079291"
FT /id="VAR_014133"
FT VARIANT 152
FT /note="Q -> E (observed with a marginally higher frequency
FT in patients with systemic lupus erythematosus;
FT dbSNP:rs554866571)"
FT /evidence="ECO:0000269|PubMed:10079291"
FT /id="VAR_003913"
FT VARIANT 203
FT /note="E -> K (in dbSNP:rs752024645)"
FT /evidence="ECO:0000269|PubMed:10079291"
FT /id="VAR_014134"
FT VARIANT 551
FT /note="G -> R (in dbSNP:rs35715143)"
FT /id="VAR_049903"
FT VARIANT 639
FT /note="Y -> H (in dbSNP:rs1058407)"
FT /evidence="ECO:0000269|PubMed:1985119"
FT /id="VAR_014135"
FT VARIANT 664
FT /note="S -> G (in dbSNP:rs17719289)"
FT /evidence="ECO:0000269|PubMed:10079291"
FT /id="VAR_003914"
FT VARIANT 669
FT /note="R -> C (in dbSNP:rs749980313)"
FT /evidence="ECO:0000269|PubMed:10079291"
FT /id="VAR_003915"
FT VARIANT 745
FT /note="G -> D (in dbSNP:rs10406069)"
FT /evidence="ECO:0000269|PubMed:10079291"
FT /id="VAR_003916"
FT CONFLICT 486
FT /note="A -> R (in Ref. 1; CAA42006)"
FT /evidence="ECO:0000305"
FT CONFLICT 788..789
FT /note="PD -> RT (in Ref. 1; CAA42006)"
FT /evidence="ECO:0000305"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 54..65
FT /evidence="ECO:0007829|PDB:5VKJ"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:5VKJ"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:5VKJ"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:5VKJ"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:5VL3"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:5VKJ"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 127..139
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 187..196
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:5VKJ"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 216..225
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 239..250
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:5VL3"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:5VKM"
FT STRAND 261..272
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:5VKJ"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:5VKJ"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:5VKJ"
SQ SEQUENCE 847 AA; 95348 MW; 38EB0BE4220ACA2D CRC64;
MHLLGPWLLL LVLEYLAFSD SSKWVFEHPE TLYAWEGACV WIPCTYRALD GDLESFILFH
NPEYNKNTSK FDGTRLYEST KDGKVPSEQK RVQFLGDKNK NCTLSIHPVH LNDSGQLGLR
MESKTEKWME RIHLNVSERP FPPHIQLPPE IQESQEVTLT CLLNFSCYGY PIQLQWLLEG
VPMRQAAVTS TSLTIKSVFT RSELKFSPQW SHHGKIVTCQ LQDADGKFLS NDTVQLNVKH
TPKLEIKVTP SDAIVREGDS VTMTCEVSSS NPEYTTVSWL KDGTSLKKQN TFTLNLREVT
KDQSGKYCCQ VSNDVGPGRS EEVFLQVQYA PEPSTVQILH SPAVEGSQVE FLCMSLANPL
PTNYTWYHNG KEMQGRTEEK VHIPKILPWH AGTYSCVAEN ILGTGQRGPG AELDVQYPPK
KVTTVIQNPM PIREGDTVTL SCNYNSSNPS VTRYEWKPHG AWEEPSLGVL KIQNVGWDNT
TIACAACNSW CSWASPVALN VQYAPRDVRV RKIKPLSEIH SGNSVSLQCD FSSSHPKEVQ
FFWEKNGRLL GKESQLNFDS ISPEDAGSYS CWVNNSIGQT ASKAWTLEVL YAPRRLRVSM
SPGDQVMEGK SATLTCESDA NPPVSHYTWF DWNNQSLPYH SQKLRLEPVK VQHSGAYWCQ
GTNSVGKGRS PLSTLTVYYS PETIGRRVAV GLGSCLAILI LAICGLKLQR RWKRTQSQQG
LQENSSGQSF FVRNKKVRRA PLSEGPHSLG CYNPMMEDGI SYTTLRFPEM NIPRTGDAES
SEMQRPPPDC DDTVTYSALH KRQVGDYENV IPDFPEDEGI HYSELIQFGV GERPQAQENV
DYVILKH
