CD72_MOUSE
ID CD72_MOUSE Reviewed; 354 AA.
AC P21855; A2AIN6; Q64225;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=B-cell differentiation antigen CD72;
DE AltName: Full=Lyb-2;
DE AltName: Full=Lymphocyte antigen 32;
DE Short=Ly-32;
DE AltName: CD_antigen=CD72;
GN Name=Cd72; Synonyms=Ly-32, Ly32, Lyb-2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2645579; DOI=10.1073/pnas.86.4.1352;
RA Nakayama E., von Hoegen I., Parnes J.R.;
RT "Sequence of the Lyb-2 B-cell differentiation antigen defines a gene
RT superfamily of receptors with inverted membrane orientation.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1352-1356(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1634777;
RA Robinson W.H., Ying H., Miceli M.C., Parnes J.R.;
RT "Extensive polymorphism in the extracellular domain of the mouse B cell
RT differentiation antigen Lyb-2/CD72.";
RL J. Immunol. 149:880-886(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP PHOSPHORYLATION AT TYR-7 AND TYR-39, AND INTERACTION WITH PTPN6/SHP-1.
RX PubMed=9590210;
RA Adachi T., Flaswinkel H., Yakura H., Reth M., Tsubata T.;
RT "The B cell surface protein CD72 recruits the tyrosine phosphatase SHP-1
RT upon tyrosine phosphorylation.";
RL J. Immunol. 160:4662-4665(1998).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in B-cell proliferation and differentiation.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Associates with CD5. Interacts
CC (tyrosine phosphorylated) with PTPN6/SHP-1.
CC {ECO:0000269|PubMed:9590210}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Pre-B-cells and B-cells but not terminally
CC differentiated plasma cells.
CC -!- PTM: Phosphorylated upon engagement of the B-cell receptor, probably by
CC LYN or SYK. Phosphorylation at Tyr-7 is important for interaction with
CC PTPN6/SHP-1. {ECO:0000269|PubMed:9590210}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=CD72;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_174";
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DR EMBL; J04170; AAA37237.1; -; mRNA.
DR EMBL; S40777; AAB22615.1; -; mRNA.
DR EMBL; AL732506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38740.1; -.
DR PIR; A32331; A32331.
DR PIR; A46509; A46509.
DR RefSeq; NP_031680.2; NM_007654.2.
DR PDB; 5B1R; X-ray; 1.20 A; A=232-354.
DR PDBsum; 5B1R; -.
DR AlphaFoldDB; P21855; -.
DR SMR; P21855; -.
DR BioGRID; 198610; 4.
DR STRING; 10090.ENSMUSP00000030179; -.
DR GlyGen; P21855; 1 site.
DR iPTMnet; P21855; -.
DR PhosphoSitePlus; P21855; -.
DR SwissPalm; P21855; -.
DR jPOST; P21855; -.
DR MaxQB; P21855; -.
DR PaxDb; P21855; -.
DR PRIDE; P21855; -.
DR ProteomicsDB; 281270; -.
DR Antibodypedia; 3742; 594 antibodies from 39 providers.
DR DNASU; 12517; -.
DR Ensembl; ENSMUST00000107926; ENSMUSP00000103559; ENSMUSG00000028459.
DR GeneID; 12517; -.
DR KEGG; mmu:12517; -.
DR UCSC; uc008spr.2; mouse.
DR CTD; 971; -.
DR MGI; MGI:88345; Cd72.
DR VEuPathDB; HostDB:ENSMUSG00000028459; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00390000003668; -.
DR InParanoid; P21855; -.
DR OMA; TCRLEWN; -.
DR OrthoDB; 987250at2759; -.
DR Reactome; R-MMU-416700; Other semaphorin interactions.
DR BioGRID-ORCS; 12517; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Cd72; mouse.
DR PRO; PR:P21855; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P21855; protein.
DR Bgee; ENSMUSG00000028459; Expressed in peripheral lymph node and 123 other tissues.
DR ExpressionAtlas; P21855; baseline and differential.
DR Genevisible; P21855; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR039689; CD72-like.
DR InterPro; IPR016187; CTDL_fold.
DR PANTHER; PTHR15028; PTHR15028; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Lectin; Membrane;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..354
FT /note="B-cell differentiation antigen CD72"
FT /id="PRO_0000046586"
FT TOPO_DOM 1..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..354
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 231..342
FT /note="C-type lectin"
FT MOD_RES 7
FT /note="Phosphotyrosine; by LYN"
FT /evidence="ECO:0000269|PubMed:9590210"
FT MOD_RES 39
FT /note="Phosphotyrosine; by LYN"
FT /evidence="ECO:0000269|PubMed:9590210"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 232..243
FT /evidence="ECO:0000250"
FT DISULFID 260..340
FT /evidence="ECO:0000250"
FT DISULFID 315..332
FT /evidence="ECO:0000250"
FT VARIANT 279
FT /note="E -> EYLSDAPQ (in allele LYB-2A.2)"
FT CONFLICT 51
FT /note="Missing (in Ref. 2; AAB22615)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="N -> K (in Ref. 1; AAA37237 and 2; AAB22615)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="Y -> N (in Ref. 1; AAA37237 and 2; AAB22615)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="V -> L (in Ref. 1; AAA37237 and 2; AAB22615)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="R -> Q (in Ref. 1; AAA37237 and 2; AAB22615)"
FT /evidence="ECO:0000305"
FT CONFLICT 157..161
FT /note="LQKAR -> QESQ (in Ref. 2; AAB22615)"
FT /evidence="ECO:0000305"
FT CONFLICT 159..161
FT /note="KAR -> ESQ (in Ref. 1; AAA37237)"
FT /evidence="ECO:0000305"
FT CONFLICT 179..181
FT /note="EDA -> KDT (in Ref. 1; AAA37237 and 2; AAB22615)"
FT /evidence="ECO:0000305"
FT CONFLICT 223..226
FT /note="FFSD -> LSSC (in Ref. 1; AAA37237 and 2; AAB22615)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="G -> R (in Ref. 1; AAA37237 and 2; AAB22615)"
FT /evidence="ECO:0000305"
FT CONFLICT 306..308
FT /note="QDS -> HDY (in Ref. 1; AAA37237 and 2; AAB22615)"
FT /evidence="ECO:0000305"
FT CONFLICT 314..320
FT /note="HCVRIKT -> YCDKIKK (in Ref. 1; AAA37237 and 2;
FT AAB22615)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="E -> K (in Ref. 1; AAA37237 and 2; AAB22615)"
FT /evidence="ECO:0000305"
FT CONFLICT 329..331
FT /note="ISK -> FSE (in Ref. 1; AAA37237 and 2; AAB22615)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="N -> H (in Ref. 1; AAA37237 and 2; AAB22615)"
FT /evidence="ECO:0000305"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:5B1R"
FT STRAND 242..251
FT /evidence="ECO:0007829|PDB:5B1R"
FT HELIX 253..262
FT /evidence="ECO:0007829|PDB:5B1R"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:5B1R"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:5B1R"
FT STRAND 313..321
FT /evidence="ECO:0007829|PDB:5B1R"
FT STRAND 324..331
FT /evidence="ECO:0007829|PDB:5B1R"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:5B1R"
SQ SEQUENCE 354 AA; 40347 MW; A1E3325C6CF0F143 CRC64;
MADAITYADL RFVKVPLKNS ASNHLGQDCE AYEDGELTYE NVQVSPVPGG PPGLASPALA
DKAGVGSEQP TATWSSVNSS ALRQIPRCPT VCLQYFLLGL LVSCLMLGVA VICLGVRYLQ
VSRQFQEGTR IWEATNSSLQ QQLREKISQL GQKEVELQKA RKELISSQDT LQEKQRTHED
AEQQLQACQA ERAKTKENLK TEEERRRDLD QRLTSTRETL RRFFSDSSDT CCPCGWIPYQ
ERCFYISHTL GSLEESQKYC TSLSSKLAAF DEPSKYYYEV SLPSGLEELL DRSKSYWIQM
SKKWRQDSDS QSRHCVRIKT YYQKWERTIS KCAELHPCIC ESEAFRFPDG INLN
