SIG10_HUMAN
ID SIG10_HUMAN Reviewed; 697 AA.
AC Q96LC7; A8K1I5; A8K3C7; C9JJ33; C9JM10; F8W917; Q3MIR5; Q6UXI8; Q96G54;
AC Q96LC8;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Sialic acid-binding Ig-like lectin 10;
DE Short=Siglec-10;
DE AltName: Full=Siglec-like protein 2;
DE Flags: Precursor;
GN Name=SIGLEC10; Synonyms=SLG2; ORFNames=UNQ477/PRO940;
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 [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=11409878; DOI=10.1006/bbrc.2001.5053;
RA Yousef G.M., Ordon M.H., Foussias G., Diamandis E.P.;
RT "Molecular characterization, tissue expression, and mapping of a novel
RT Siglec-like gene (SLG2) with three splice variants.";
RL Biochem. Biophys. Res. Commun. 284:900-910(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP VARIANT VAL-226.
RC TISSUE=Spleen;
RX PubMed=11284738; DOI=10.1042/0264-6021:3550489;
RA Munday J., Kerr S., Ni J., Cornish A.L., Zhang J.Q., Nicoll G., Floyd H.,
RA Mattei M.-G., Moore P., Liu D., Crocker P.R.;
RT "Identification, characterization and leucocyte expression of Siglec-10, a
RT novel human sialic acid-binding receptor.";
RL Biochem. J. 355:489-497(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND VARIANT
RP VAL-226.
RC TISSUE=Dendritic cell;
RX PubMed=11358961; DOI=10.1074/jbc.m100467200;
RA Li N., Zhang W., Wan T., Zhang J., Chen T., Yu Y., Wang J., Cao X.;
RT "Cloning and characterization of Siglec-10, a novel sialic acid binding
RT member of the Ig superfamily, from human dendritic cells.";
RL J. Biol. Chem. 276:28106-28112(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING (ISOFORMS 4
RP AND 5), TISSUE SPECIFICITY, VARIANT VAL-226, PHOSPHORYLATION AT TYR-667,
RP MUTAGENESIS OF TYR-667, INTERACTION WITH PTPN6, AND FUNCTION.
RX PubMed=12163025; DOI=10.1016/s0006-291x(02)00885-9;
RA Kitzig F., Martinez-Barriocanal A., Lopez-Botet M., Sayos J.;
RT "Cloning of two new splice variants of Siglec-10 and mapping of the
RT interaction between Siglec-10 and SHP-1.";
RL Biochem. Biophys. Res. Commun. 296:355-362(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7), AND VARIANT
RP VAL-226.
RC TISSUE=Brain, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-226.
RC TISSUE=B-cell, and Liver;
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 [9]
RP INTERACTION WITH CD24 AND HMGB1, AND MUTAGENESIS OF ARG-119.
RX PubMed=19264983; DOI=10.1126/science.1168988;
RA Chen G.Y., Tang J., Zheng P., Liu Y.;
RT "CD24 and Siglec-10 selectively repress tissue damage-induced immune
RT responses.";
RL Science 323:1722-1725(2009).
RN [10]
RP FUNCTION.
RX PubMed=25450598; DOI=10.1016/j.jss.2014.09.035;
RA Zhang P., Lu X., Tao K., Shi L., Li W., Wang G., Wu K.;
RT "Siglec-10 is associated with survival and natural killer cell dysfunction
RT in hepatocellular carcinoma.";
RL J. Surg. Res. 194:107-113(2015).
CC -!- FUNCTION: Putative adhesion molecule that mediates sialic-acid
CC dependent binding to cells. Preferentially binds to alpha-2,3- or
CC alpha-2,6-linked sialic acid (By similarity). The sialic acid
CC recognition site may be masked by cis interactions with sialic acids on
CC the same cell surface. In the immune response, seems to act as an
CC inhibitory receptor upon ligand induced tyrosine phosphorylation by
CC recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that
CC block signal transduction through dephosphorylation of signaling
CC molecules (PubMed:11284738, PubMed:12163025). Involved in negative
CC regulation of B-cell antigen receptor signaling. The inhibition of B
CC cell activation is dependent on PTPN6/SHP-1 (By similarity). In
CC association with CD24 may be involved in the selective suppression of
CC the immune response to danger-associated molecular patterns (DAMPs)
CC such as HMGB1, HSP70 and HSP90 (By similarity). In association with
CC CD24 may regulate the immune repsonse of natural killer (NK) cells
CC (PubMed:25450598). Plays a role in the control of autoimmunity (By
CC similarity). During initiation of adaptive immune responses by CD8-
CC alpha(+) dendritic cells inhibits cross-presentation by impairing the
CC formation of MHC class I-peptide complexes. The function seems to
CC implicate recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of
CC the NADPH oxidase complex consequently promoting phagosomal
CC acidification (By similarity). {ECO:0000250|UniProtKB:Q80ZE3,
CC ECO:0000269|PubMed:11284738, ECO:0000269|PubMed:25450598,
CC ECO:0000305|PubMed:12163025}.
CC -!- SUBUNIT: Interacts with PTPN6/SHP-1 upon phosphorylation
CC (PubMed:12163025). Interacts with NCF1 (By similarity). Interacts with
CC CD24; the probable CD24:SIGLEC10 complex is proposed to inhibit HGMB1-
CC mediated tissue damage immune response. Interacts with HMGB1; the
CC interaction is dependent on CD24 (PubMed:19264983). Interacts with
CC DDX58, CBL and PTPN11 (By similarity). {ECO:0000250|UniProtKB:Q80ZE3,
CC ECO:0000269|PubMed:12163025, ECO:0000269|PubMed:19264983}.
CC -!- INTERACTION:
CC Q96LC7; P0DTC2: S; Xeno; NbExp=2; IntAct=EBI-8502656, EBI-25474821;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1; Synonyms=Long;
CC IsoId=Q96LC7-1; Sequence=Displayed;
CC Name=2; Synonyms=Short, Sv1;
CC IsoId=Q96LC7-2; Sequence=VSP_002565;
CC Name=3; Synonyms=Sv3;
CC IsoId=Q96LC7-3; Sequence=VSP_002564;
CC Name=4; Synonyms=Sv4;
CC IsoId=Q96LC7-4; Sequence=VSP_002561;
CC Name=5; Synonyms=Sv2;
CC IsoId=Q96LC7-5; Sequence=VSP_002562, VSP_002563;
CC Name=6;
CC IsoId=Q96LC7-6; Sequence=VSP_002564, VSP_002565;
CC Name=7;
CC IsoId=Q96LC7-7; Sequence=VSP_045365, VSP_002565;
CC Name=8;
CC IsoId=Q96LC7-8; Sequence=VSP_002564, VSP_045853, VSP_045854,
CC VSP_002565;
CC Name=9;
CC IsoId=Q96LC7-9; Sequence=VSP_045888, VSP_002565;
CC -!- TISSUE SPECIFICITY: Expressed by peripheral blood leukocytes
CC (eosinophils, monocytes and a natural killer cell subpopulation).
CC Isoform 5 is found to be the most abundant isoform. Found in lymph
CC node, lung, ovary and appendix. Isoform 1 is found at high levels and
CC isoform 2 at lower levels in bone marrow, spleen and spinal chord.
CC Isoform 2 is also found in brain. Isoform 4 is specifically found in
CC natural killer cells. {ECO:0000269|PubMed:11284738,
CC ECO:0000269|PubMed:11358961, ECO:0000269|PubMed:12163025}.
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 -!- PTM: Phosphorylation of Tyr-667 is involved in binding to PTPN6.
CC {ECO:0000269|PubMed:12163025}.
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-10 [5 Fc Domains];
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_00002";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Siglec-10 long;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_268";
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DR EMBL; AY029277; AAK40255.1; -; Genomic_DNA.
DR EMBL; AY029277; AAK40256.1; -; Genomic_DNA.
DR EMBL; AF310233; AAK55139.1; -; mRNA.
DR EMBL; AF311905; AAK92542.1; -; mRNA.
DR EMBL; AY032685; AAK51124.1; -; mRNA.
DR EMBL; AY358337; AAQ88703.1; -; mRNA.
DR EMBL; AK289900; BAF82589.1; -; mRNA.
DR EMBL; AK290542; BAF83231.1; -; mRNA.
DR EMBL; AK303514; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC008750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009955; AAH09955.2; -; mRNA.
DR EMBL; BC101725; AAI01726.1; -; mRNA.
DR CCDS; CCDS12832.1; -. [Q96LC7-1]
DR CCDS; CCDS54301.1; -. [Q96LC7-8]
DR CCDS; CCDS54302.1; -. [Q96LC7-6]
DR CCDS; CCDS54303.1; -. [Q96LC7-3]
DR CCDS; CCDS54304.1; -. [Q96LC7-7]
DR CCDS; CCDS54305.1; -. [Q96LC7-2]
DR RefSeq; NP_001164627.1; NM_001171156.1. [Q96LC7-3]
DR RefSeq; NP_001164628.1; NM_001171157.1. [Q96LC7-2]
DR RefSeq; NP_001164629.1; NM_001171158.1. [Q96LC7-7]
DR RefSeq; NP_001164630.1; NM_001171159.1. [Q96LC7-6]
DR RefSeq; NP_001164632.1; NM_001171161.1. [Q96LC7-8]
DR RefSeq; NP_001309034.1; NM_001322105.1.
DR RefSeq; NP_149121.2; NM_033130.4. [Q96LC7-1]
DR AlphaFoldDB; Q96LC7; -.
DR SMR; Q96LC7; -.
DR BioGRID; 124602; 22.
DR IntAct; Q96LC7; 11.
DR MINT; Q96LC7; -.
DR STRING; 9606.ENSP00000345243; -.
DR ChEMBL; CHEMBL4303061; -.
DR GlyGen; Q96LC7; 6 sites.
DR iPTMnet; Q96LC7; -.
DR PhosphoSitePlus; Q96LC7; -.
DR BioMuta; SIGLEC10; -.
DR DMDM; 118572721; -.
DR EPD; Q96LC7; -.
DR jPOST; Q96LC7; -.
DR MassIVE; Q96LC7; -.
DR MaxQB; Q96LC7; -.
DR PaxDb; Q96LC7; -.
DR PeptideAtlas; Q96LC7; -.
DR PRIDE; Q96LC7; -.
DR ProteomicsDB; 10427; -.
DR ProteomicsDB; 10785; -.
DR ProteomicsDB; 30242; -.
DR ProteomicsDB; 77195; -. [Q96LC7-1]
DR ProteomicsDB; 77196; -. [Q96LC7-2]
DR ProteomicsDB; 77197; -. [Q96LC7-3]
DR ProteomicsDB; 77198; -. [Q96LC7-4]
DR ProteomicsDB; 77199; -. [Q96LC7-5]
DR ProteomicsDB; 77200; -. [Q96LC7-6]
DR Antibodypedia; 19024; 312 antibodies from 27 providers.
DR DNASU; 89790; -.
DR Ensembl; ENST00000339313.10; ENSP00000345243.4; ENSG00000142512.15. [Q96LC7-1]
DR Ensembl; ENST00000353836.9; ENSP00000342389.5; ENSG00000142512.15. [Q96LC7-2]
DR Ensembl; ENST00000436984.6; ENSP00000414324.2; ENSG00000142512.15. [Q96LC7-7]
DR Ensembl; ENST00000439889.6; ENSP00000389132.2; ENSG00000142512.15. [Q96LC7-3]
DR Ensembl; ENST00000441969.7; ENSP00000408387.2; ENSG00000142512.15. [Q96LC7-6]
DR Ensembl; ENST00000442846.7; ENSP00000395475.2; ENSG00000142512.15. [Q96LC7-8]
DR GeneID; 89790; -.
DR KEGG; hsa:89790; -.
DR MANE-Select; ENST00000339313.10; ENSP00000345243.4; NM_033130.5; NP_149121.2.
DR UCSC; uc002pwo.4; human. [Q96LC7-1]
DR CTD; 89790; -.
DR DisGeNET; 89790; -.
DR GeneCards; SIGLEC10; -.
DR HGNC; HGNC:15620; SIGLEC10.
DR HPA; ENSG00000142512; Tissue enhanced (lymphoid).
DR MIM; 606091; gene.
DR neXtProt; NX_Q96LC7; -.
DR OpenTargets; ENSG00000142512; -.
DR PharmGKB; PA38004; -.
DR VEuPathDB; HostDB:ENSG00000142512; -.
DR eggNOG; ENOG502S41V; Eukaryota.
DR GeneTree; ENSGT01040000240469; -.
DR HOGENOM; CLU_024444_5_1_1; -.
DR InParanoid; Q96LC7; -.
DR OMA; CEAWNTH; -.
DR OrthoDB; 1124645at2759; -.
DR PhylomeDB; Q96LC7; -.
DR TreeFam; TF332441; -.
DR PathwayCommons; Q96LC7; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; Q96LC7; -.
DR SIGNOR; Q96LC7; -.
DR BioGRID-ORCS; 89790; 11 hits in 1065 CRISPR screens.
DR ChiTaRS; SIGLEC10; human.
DR GeneWiki; SIGLEC10; -.
DR GenomeRNAi; 89790; -.
DR Pharos; Q96LC7; Tbio.
DR PRO; PR:Q96LC7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96LC7; protein.
DR Bgee; ENSG00000142512; Expressed in granulocyte and 136 other tissues.
DR ExpressionAtlas; Q96LC7; baseline and differential.
DR Genevisible; Q96LC7; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; IMP:UniProtKB.
DR GO; GO:0033691; F:sialic acid binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0106015; P:negative regulation of inflammatory response to wounding; IPI:UniProtKB.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain;
KW Innate immunity; Lectin; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..697
FT /note="Sialic acid-binding Ig-like lectin 10"
FT /id="PRO_0000014950"
FT TOPO_DOM 17..550
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..697
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..121
FT /note="Ig-like V-type"
FT DOMAIN 146..231
FT /note="Ig-like C2-type 1"
FT DOMAIN 251..339
FT /note="Ig-like C2-type 2"
FT DOMAIN 344..441
FT /note="Ig-like C2-type 3"
FT REGION 606..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 595..600
FT /note="ITIM motif 1"
FT MOTIF 665..670
FT /note="ITIM motif 2"
FT COMPBIAS 633..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 119
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250"
FT MOD_RES 667
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:12163025"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 41..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 164..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 276..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 380..425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 125..214
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_002561"
FT VAR_SEQ 140..185
FT /note="TALTQKPDVYIPETLEPGQPVTVICVFNWAFEECPPPSFSWTGAAL -> TG
FT MRWGGNPCLSHWGGTLGTAYGLSREGSQGPLQHKNLPPRSLSQP (in isoform
FT 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_002562"
FT VAR_SEQ 141..198
FT /note="Missing (in isoform 3, isoform 6 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:12163025,
FT ECO:0000303|PubMed:12975309, ECO:0000303|PubMed:14702039"
FT /id="VSP_002564"
FT VAR_SEQ 141..188
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045365"
FT VAR_SEQ 146..228
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000305"
FT /id="VSP_045888"
FT VAR_SEQ 186..697
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_002563"
FT VAR_SEQ 252
FT /note="A -> D (in isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_045853"
FT VAR_SEQ 253..342
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_045854"
FT VAR_SEQ 445..539
FT /note="Missing (in isoform 2, isoform 6, isoform 7, isoform
FT 8 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:11358961,
FT ECO:0000303|PubMed:12975309, ECO:0000303|PubMed:14702039"
FT /id="VSP_002565"
FT VARIANT 226
FT /note="A -> V (in dbSNP:rs9304711)"
FT /evidence="ECO:0000269|PubMed:11284738,
FT ECO:0000269|PubMed:11358961, ECO:0000269|PubMed:12163025,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_019955"
FT VARIANT 520
FT /note="R -> S (in dbSNP:rs1833785)"
FT /id="VAR_019956"
FT MUTAGEN 119
FT /note="R->A: Disrupts interaction with CD24."
FT /evidence="ECO:0000269|PubMed:19264983"
FT MUTAGEN 667
FT /note="Y->F: Abolishes binding to PTPN6."
FT /evidence="ECO:0000269|PubMed:12163025"
FT CONFLICT 28
FT /note="S -> P (in Ref. 4; AAK51124)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="R -> T (in Ref. 5; AAQ88703)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="G -> R (in Ref. 4; AAK51124)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="K -> R (in Ref. 6; AK303514)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="P -> S (in Ref. 3; AAK92542)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="L -> P (in Ref. 4; AAK51124)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="L -> P (in Ref. 6; AK303514)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="R -> K (in Ref. 3; AAK92542)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="L -> P (in Ref. 5; AAQ88703)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="P -> S (in Ref. 3; AAK92542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 697 AA; 76592 MW; E1B787F34CF7201A CRC64;
MLLPLLLSSL LGGSQAMDGR FWIRVQESVM VPEGLCISVP CSFSYPRQDW TGSTPAYGYW
FKAVTETTKG APVATNHQSR EVEMSTRGRF QLTGDPAKGN CSLVIRDAQM QDESQYFFRV
ERGSYVRYNF MNDGFFLKVT ALTQKPDVYI PETLEPGQPV TVICVFNWAF EECPPPSFSW
TGAALSSQGT KPTTSHFSVL SFTPRPQDHN TDLTCHVDFS RKGVSAQRTV RLRVAYAPRD
LVISISRDNT PALEPQPQGN VPYLEAQKGQ FLRLLCAADS QPPATLSWVL QNRVLSSSHP
WGPRPLGLEL PGVKAGDSGR YTCRAENRLG SQQRALDLSV QYPPENLRVM VSQANRTVLE
NLGNGTSLPV LEGQSLCLVC VTHSSPPARL SWTQRGQVLS PSQPSDPGVL ELPRVQVEHE
GEFTCHARHP LGSQHVSLSL SVHYSPKLLG PSCSWEAEGL HCSCSSQASP APSLRWWLGE
ELLEGNSSQD SFEVTPSSAG PWANSSLSLH GGLSSGLRLR CEAWNVHGAQ SGSILQLPDK
KGLISTAFSN GAFLGIGITA LLFLCLALII MKILPKRRTQ TETPRPRFSR HSTILDYINV
VPTAGPLAQK RNQKATPNSP RTPLPPGAPS PESKKNQKKQ YQLPSFPEPK SSTQAPESQE
SQEELHYATL NFPGVRPRPE ARMPKGTQAD YAEVKFQ
