CD33_MOUSE
ID CD33_MOUSE Reviewed; 403 AA.
AC Q63994; A2RT59; Q63997;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Myeloid cell surface antigen CD33;
DE AltName: Full=Sialic acid-binding Ig-like lectin 3;
DE Short=Siglec-3;
DE AltName: CD_antigen=CD33;
DE Flags: Precursor;
GN Name=Cd33; Synonyms=Siglec3;
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] (ISOFORMS 33-A AND 33-B).
RC STRAIN=BALB/cJ; TISSUE=Bone marrow;
RX PubMed=8193354;
RA Tchilian E.Z., Beverley P.C., Young B.D., Watt S.M.;
RT "Molecular cloning of two isoforms of the murine homolog of the myeloid
RT CD33 antigen.";
RL Blood 83:3188-3198(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 33-A).
RC TISSUE=Brain;
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 [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=12773563; DOI=10.1128/mcb.23.12.4199-4206.2003;
RA Brinkman-Van der Linden E.C., Angata T., Reynolds S.A., Powell L.D.,
RA Hedrick S.M., Varki A.;
RT "CD33/Siglec-3 binding specificity, expression pattern, and consequences of
RT gene deletion in mice.";
RL Mol. Cell. Biol. 23:4199-4206(2003).
CC -!- FUNCTION: Sialic-acid-binding immunoglobulin-like lectin (Siglec) that
CC plays a role in mediating cell-cell interactions and in maintaining
CC immune cells in a resting state (By similarity). Preferentially binds
CC sialic acid to the short O-linked glycans of certain mucins
CC (PubMed:12773563). {ECO:0000250|UniProtKB:P20138,
CC ECO:0000269|PubMed:12773563}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PTPN6/SHP-1 and
CC PTPN11/SHP-2 upon phosphorylation. Interacts with C1QA (via C-
CC terminus); this interaction activates CD33 inhibitory motifs.
CC {ECO:0000250|UniProtKB:P20138}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20138};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P20138}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=33-B;
CC IsoId=Q63994-1; Sequence=Displayed;
CC Name=33-A;
CC IsoId=Q63994-2; Sequence=VSP_002534;
CC -!- TISSUE SPECIFICITY: Expressed on myeloid precursors in the bone marrow.
CC In the peripheral blood, mostly expressed on granulocytes.
CC {ECO:0000269|PubMed:12773563}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P20138}.
CC -!- PTM: Phosphorylation is involved in binding to PTPN6 and PTPN11.
CC {ECO:0000250|UniProtKB:P20138}.
CC -!- DISRUPTION PHENOTYPE: CD33-deficient mice are viable and fertile in a
CC pathogen-free environment without any obvious deficiency in overall
CC organ development and growth. {ECO:0000269|PubMed:12773563}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC acid binding Ig-like lectin) family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Siglec-3;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_195";
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DR EMBL; S71345; AAB30842.1; -; mRNA.
DR EMBL; S71403; AAB30843.2; -; mRNA.
DR EMBL; BC132379; AAI32380.1; -; mRNA.
DR CCDS; CCDS21173.1; -. [Q63994-2]
DR CCDS; CCDS52224.1; -. [Q63994-1]
DR RefSeq; NP_001104528.1; NM_001111058.1. [Q63994-1]
DR RefSeq; NP_067268.1; NM_021293.3. [Q63994-2]
DR AlphaFoldDB; Q63994; -.
DR SMR; Q63994; -.
DR IntAct; Q63994; 5.
DR STRING; 10090.ENSMUSP00000004728; -.
DR GlyGen; Q63994; 3 sites.
DR iPTMnet; Q63994; -.
DR PhosphoSitePlus; Q63994; -.
DR MaxQB; Q63994; -.
DR PaxDb; Q63994; -.
DR PeptideAtlas; Q63994; -.
DR PRIDE; Q63994; -.
DR ProteomicsDB; 265623; -. [Q63994-1]
DR ProteomicsDB; 265624; -. [Q63994-2]
DR DNASU; 12489; -.
DR Ensembl; ENSMUST00000004728; ENSMUSP00000004728; ENSMUSG00000004609. [Q63994-1]
DR Ensembl; ENSMUST00000039861; ENSMUSP00000045458; ENSMUSG00000004609. [Q63994-2]
DR Ensembl; ENSMUST00000205503; ENSMUSP00000146225; ENSMUSG00000004609. [Q63994-2]
DR GeneID; 12489; -.
DR KEGG; mmu:12489; -.
DR UCSC; uc009gmz.2; mouse. [Q63994-2]
DR UCSC; uc009gna.1; mouse. [Q63994-1]
DR CTD; 945; -.
DR MGI; MGI:99440; Cd33.
DR VEuPathDB; HostDB:ENSMUSG00000004609; -.
DR eggNOG; ENOG502S41V; Eukaryota.
DR GeneTree; ENSGT01040000240469; -.
DR HOGENOM; CLU_024444_0_1_1; -.
DR InParanoid; Q63994; -.
DR OMA; CHAHILA; -.
DR OrthoDB; 850159at2759; -.
DR PhylomeDB; Q63994; -.
DR TreeFam; TF332441; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 12489; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Cd33; mouse.
DR PRO; PR:Q63994; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q63994; protein.
DR Bgee; ENSMUSG00000004609; Expressed in granulocyte and 82 other tissues.
DR ExpressionAtlas; Q63994; baseline and differential.
DR Genevisible; Q63994; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0033691; F:sialic acid binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
DR GO; GO:0002765; P:immune response-inhibiting signal transduction; ISO:MGI.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISO:MGI.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0150102; P:negative regulation of monocyte activation; ISO:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:1903615; P:positive regulation of protein tyrosine phosphatase activity; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 2.
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; IPR013106; Ig_V-set.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Lectin; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..403
FT /note="Myeloid cell surface antigen CD33"
FT /id="PRO_0000014879"
FT TOPO_DOM 18..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 17..120
FT /note="Ig-like V-type"
FT DOMAIN 145..228
FT /note="Ig-like C2-type"
FT BINDING 118
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 41..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 163..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 287..403
FT /note="RQEAITSYNHCLSPTASDAVTPGCSIHRLISRTPRCTAILRIQDPYRRTHLR
FT NRAVSTLRFPWISWEGSLRSTQRSKCTKLCSPVKNLCPLWLPVDNSCIPLIPEWVMLLC
FT VSLTLS -> AHQQDSKVHSNPENPRPLQKDSPQEQSSVHTKISLDFMGGKPQEYSEI
FT (in isoform 33-A)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8193354"
FT /id="VSP_002534"
SQ SEQUENCE 403 AA; 44824 MW; F1FE6D5C393F0FF1 CRC64;
MLWPLPLFLL CAGSLAQDLE FQLVAPESVT VEEGLCVHVP CSVFYPSIKL TLGPVTGSWL
RKGVSLHEDS PVATSDPRQL VQKATQGRFQ LLGDPQKHDC SLFIRDAQKN DTGMYFFRVV
REPFVRYSYK KSQLSLHVTS LSRTPDIIIP GTLEAGYPSN LTCSVPWACE QGTPPTFSWM
STALTSLSSR TTDSSVLTFT PQPQDHGTKL TCLVTFSGAG VTVERTIQLN VTRKSGQMRE
LVLVAVGEAT VKLLILGLCL VFLIVMFCRR KTTKLSVHMG CENPIKRQEA ITSYNHCLSP
TASDAVTPGC SIHRLISRTP RCTAILRIQD PYRRTHLRNR AVSTLRFPWI SWEGSLRSTQ
RSKCTKLCSP VKNLCPLWLP VDNSCIPLIP EWVMLLCVSL TLS
