CD22_PANTR
ID CD22_PANTR Reviewed; 847 AA.
AC Q9N1E6; A0A6D2WBT6;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=B-cell receptor CD22 {ECO:0000250|UniProtKB:P20273};
DE AltName: Full=Sialic acid-binding Ig-like lectin 2;
DE Short=Siglec-2;
DE AltName: CD_antigen=CD22;
DE Flags: Precursor;
GN Name=CD22 {ECO:0000250|UniProtKB:P20273}; Synonyms=SIGLEC2;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-332.
RX PubMed=10722703; DOI=10.1074/jbc.275.12.8633;
RA Brinkman-Van der Linden E.C.M., Sjoberg E.R., Juneja L.R., Crocker P.R.,
RA Varki N., Varki A.;
RT "Loss of N-glycolylneuraminic acid in human evolution: implications for
RT sialic acid recognition by siglecs.";
RL J. Biol. Chem. 275:8633-8640(2000).
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 (By similarity). Upon ligand-induced tyrosine
CC phosphorylation in the immune response seems to be involved in
CC regulation of B-cell antigen receptor signaling. Plays a role in
CC positive regulation through interaction with Src family tyrosine
CC kinases and may also act as an inhibitory receptor by recruiting
CC cytoplasmic phosphatases via their SH2 domains that block signal
CC transduction through dephosphorylation of signaling cascade key
CC molecules. {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P20273}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
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 {ECO:0000250|UniProtKB:P20273}.
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 {ECO:0000250|UniProtKB:P20273}.
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}.
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DR EMBL; NBAG03000037; PNI95673.1; -; Genomic_DNA.
DR EMBL; AF199415; AAF44614.1; -; mRNA.
DR RefSeq; XP_009433588.1; XM_009435313.2.
DR RefSeq; XP_009433590.1; XM_009435315.2.
DR AlphaFoldDB; Q9N1E6; -.
DR STRING; 9598.ENSPTRP00000018557; -.
DR PaxDb; Q9N1E6; -.
DR Ensembl; ENSPTRT00000020070; ENSPTRP00000018557; ENSPTRG00000010840.
DR GeneID; 450167; -.
DR CTD; 933; -.
DR VGNC; VGNC:2369; CD22.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT01050000244990; -.
DR InParanoid; Q9N1E6; -.
DR Proteomes; UP000002277; Unplaced.
DR Proteomes; UP000236370; Unassembled WGS sequence.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0042609; F:CD4 receptor binding; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
DR GO; GO:0033691; F:sialic acid binding; IBA:GO_Central.
DR GO; GO:0042113; P:B cell activation; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0030888; P:regulation of B cell proliferation; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Isopeptide bond; Lectin; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..847
FT /note="B-cell receptor CD22"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014876"
FT TOPO_DOM 20..687
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..847
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 20..138
FT /note="Ig-like V-type"
FT /evidence="ECO:0000250|UniProtKB:P20273"
FT DOMAIN 143..235
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 242..326
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 331..416
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 419..500
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 505..582
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 593..676
FT /note="Ig-like C2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MOTIF 760..765
FT /note="ITIM motif 1"
FT /evidence="ECO:0000250|UniProtKB:P20273"
FT MOTIF 794..799
FT /note="ITIM motif 2"
FT /evidence="ECO:0000250|UniProtKB:P20273"
FT MOTIF 820..825
FT /note="ITIM motif 3"
FT /evidence="ECO:0000250|UniProtKB:P20273"
FT MOTIF 840..845
FT /note="ITIM motif 4"
FT /evidence="ECO:0000250|UniProtKB:P20273"
FT BINDING 120
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250|UniProtKB:P20273"
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 428
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 448
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 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 CONFLICT 65
FT /note="N -> S (in Ref. 2; AAF44614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 847 AA; 95274 MW; 8010FA3368F4EFE3 CRC64;
MHLLGPWLLL LVLEYLAFSD SSKWAFEHPE TLYAWEGACV WIPCTYRALD RDLESFILFH
NPEYNKNTSK FDGTRLYEST KDGKVPSEQK RVQFLGDKNK NCTLSIHPVH VNDSGQLGLR
MESKTAKWME RIHLNVSERP FPPHIQLPPE IQESQEVTLT CLLNFSCYGY PIQLQWLLEG
VPMRQAAVTS TSLTIKSVFT RSELKFSPQW SHHGKIVTCQ LQDADGKFLS NDTVQLNVKH
TPKLEIKVTP SDAIVREGES VTMTCEVSSS NPEYTTISWL KDGTSLKKQN TLMLNLHEVT
KDQSGKYCCQ VSNDVGPGRS AEVFLQVQYA PEPSTVQILH SPAVEGSQVE FLCMSLANPL
PTNYTWYHNG KEMQGRTEEK VHIPKILPWH AGTYSCVAEN ILGTGQRGPG AELDVQYPPK
KVTTVIQNPT PIREGDTVTL SCNYNSSNPS VTRYEWKPHG AWEEPSLGVL KIQNVGWGNT
TIACAACNSW CSWASPVALN VQYAPRDVRV RKIKPLSEIH SGNSVSLQCD FSSSHPKEVQ
FFWEKNGRLL GKESRLNFDS ISPEDAGSYS CWVNNSIGQT ASKAWTLEVL YAPRRLRVSM
SPGDQVMEGK SATLTCESDA NPPVSHYTWF DWNNQSLPYH SQKLRLEPVK VQHSGAYWCQ
GTNSVGKGHS PLSTLTVYYS PETIGRRVAV GFGSCLAILI LAICGLKLQR RWKRTQSQQG
LQENSSGQSF FVRNKKVRRA PLSEGPHSLG YYNPMMEDGI SYTTLRFPET NIPRTGDAET
SEMQSPPPDC DDTVTYSVLH KRQMGDYENV IPDFSEDEGI HYSELIQFGV GERPQAQENV
DYVILKH
