SIGL5_MOUSE
ID SIGL5_MOUSE Reviewed; 569 AA.
AC Q920G3;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Sialic acid-binding Ig-like lectin 5;
DE Short=Siglec-5;
DE AltName: Full=Sialic acid-binding Ig-like lectin F;
DE Short=Siglec-F;
DE Short=mSiglec-F;
DE AltName: CD_antigen=CD170;
DE Flags: Precursor;
GN Name=Siglec5; Synonyms=Siglecf;
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].
RC STRAIN=C57BL/6J;
RX PubMed=11579105; DOI=10.1074/jbc.m108573200;
RA Angata T., Hingorani R., Varki N.M., Varki A.;
RT "Cloning and characterization of a novel mouse Siglec, mSiglec-F:
RT differential evolution of the mouse and human (CD33) Siglec-3-related gene
RT clusters.";
RL J. Biol. Chem. 276:45128-45136(2001).
CC -!- FUNCTION: Putative adhesion molecule that mediates sialic-acid
CC dependent binding to cells. Preferentially binds to alpha-2,3-linked
CC sialic acid. The sialic acid recognition site may be masked by cis
CC interactions with sialic acids on the same cell surface.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Predominantly expressed by immature
CC monocytic/myeloid lineage cells in bone marrow. Also found at lower
CC levels in mature neutrophils and monocytes.
CC -!- DOMAIN: Contains 1 copy 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 -!- 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-F;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_198";
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DR EMBL; AF293371; AAL11043.1; -; mRNA.
DR CCDS; CCDS21167.1; -.
DR RefSeq; NP_001257948.1; NM_001271019.1.
DR RefSeq; NP_663556.1; NM_145581.2.
DR AlphaFoldDB; Q920G3; -.
DR SMR; Q920G3; -.
DR IntAct; Q920G3; 4.
DR STRING; 10090.ENSMUSP00000113245; -.
DR GlyGen; Q920G3; 7 sites.
DR iPTMnet; Q920G3; -.
DR PhosphoSitePlus; Q920G3; -.
DR MaxQB; Q920G3; -.
DR PaxDb; Q920G3; -.
DR PRIDE; Q920G3; -.
DR DNASU; 233186; -.
DR Ensembl; ENSMUST00000012798; ENSMUSP00000012798; ENSMUSG00000039013.
DR Ensembl; ENSMUST00000122423; ENSMUSP00000113245; ENSMUSG00000039013.
DR GeneID; 233186; -.
DR KEGG; mmu:233186; -.
DR UCSC; uc009gml.2; mouse.
DR CTD; 233186; -.
DR MGI; MGI:2681107; Siglec5.
DR VEuPathDB; HostDB:ENSMUSG00000039013; -.
DR eggNOG; ENOG502S41V; Eukaryota.
DR GeneTree; ENSGT01040000240469; -.
DR InParanoid; Q920G3; -.
DR OMA; GSITCEM; -.
DR OrthoDB; 416689at2759; -.
DR PhylomeDB; Q920G3; -.
DR TreeFam; TF332441; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 233186; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Siglecf; mouse.
DR PRO; PR:Q920G3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q920G3; protein.
DR Bgee; ENSMUSG00000039013; Expressed in granulocyte and 49 other tissues.
DR ExpressionAtlas; Q920G3; baseline and differential.
DR Genevisible; Q920G3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0048029; F:monosaccharide binding; IDA:MGI.
DR GO; GO:0033691; F:sialic acid binding; IDA:ARUK-UCL.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; IDA:ARUK-UCL.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain; Lectin;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..569
FT /note="Sialic acid-binding Ig-like lectin 5"
FT /id="PRO_0000014945"
FT TOPO_DOM 17..439
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..569
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..116
FT /note="Ig-like V-type"
FT DOMAIN 139..224
FT /note="Ig-like C2-type 1"
FT DOMAIN 229..324
FT /note="Ig-like C2-type 2"
FT REGION 508..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 536..541
FT /note="ITIM motif"
FT MOTIF 559..564
FT /note="SLAM-like motif"
FT COMPBIAS 508..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 114
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250|UniProtKB:O15389"
FT BINDING 120
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250|UniProtKB:O15389"
FT BINDING 122
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250|UniProtKB:O15389"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 40..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 157..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 265..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 569 AA; 61476 MW; 8093838090484FC1 CRC64;
MRWAWLLPLL WAGCLATDGY SLSVTGSVTV QEGLCVFVAC QVQYPNSKGP VFGYWFREGA
NIFSGSPVAT NDPQRSVLKE AQGRFYLMGK ENSHNCSLDI RDAQKIDTGT YFFRLDGSVK
YSFQKSMLSV LVIALTEVPN IQVTSTLVSG NSTKLLCSVP WACEQGTPPI FSWMSSALTS
LGHRTTLSSE LNLTPRPQDN GTNLTCQVNL PGTGVTVERT QQLSVIYAPQ KMTIRVSWGD
DTGTKVLQSG ASLQIQEGES LSLVCMADSN PPAVLSWERP TQKPFQLSTP AELQLPRAEL
EDQGKYICQA QNSQGAQTAS VSLSIRSLLQ LLGPSCSFEG QGLHCSCSSR AWPAPSLRWR
LGEGVLEGNS SNGSFTVKSS SAGQWANSSL ILSMEFSSNH RLSCEAWSDN RVQRATILLV
SGPKVSQAGK SETSRGTVLG AIWGAGLMAL LAVCLCLIFF TVKVLRKKSA LKVAATKGNH
LAKNPASTIN SASITSSNIA LGYPIQGHLN EPGSQTQKEQ PPLATVPDTQ KDEPELHYAS
LSFQGPMPPK PQNTEAMKSV YTEIKIHKC
