ID   SIG11_HUMAN             Reviewed;         698 AA.
AC   Q96RL6;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Sialic acid-binding Ig-like lectin 11;
DE            Short=Sialic acid-binding lectin 11;
DE            Short=Siglec-11;
DE   Flags: Precursor;
GN   Name=SIGLEC11; ORFNames=UNQ9222/PRO28718;
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 [MRNA] (ISOFORM 1), AND INTERACTION WITH PTPN6 AND
RP   PTPN11.
RX   PubMed=11986327; DOI=10.1074/jbc.m202833200;
RA   Angata T., Kerr S.C., Greaves D.R., Varki N.M., Crocker P.R., Varki A.;
RT   "Cloning and characterization of human Siglec-11. A recently evolved
RT   signaling molecule that can interact with SHP-1 and SHP-2 and is expressed
RT   by tissue macrophages, including brain microglia.";
RL   J. Biol. Chem. 277:24466-24474(2002).
RN   [2]
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   [3]
RP   PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
CC   -!- FUNCTION: Putative adhesion molecule that mediates sialic-acid
CC       dependent binding to cells. Preferentially binds to alpha-2,8-linked
CC       sialic acid. The sialic acid recognition site may be masked by cis
CC       interactions with sialic acids on the same cell surface. In the immune
CC       response, may act as an inhibitory receptor upon ligand induced
CC       tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via
CC       their SH2 domain(s) that block signal transduction through
CC       dephosphorylation of signaling molecules.
CC   -!- SUBUNIT: Interacts with PTPN6/SHP-1 and PTPN11/SHP-2 upon
CC       phosphorylation. {ECO:0000269|PubMed:11986327}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96RL6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96RL6-2; Sequence=VSP_008764;
CC   -!- TISSUE SPECIFICITY: Expressed by macrophages in various tissues
CC       including Kupffer cells. Also found in brain microglia.
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: Phosphorylated on tyrosine residues.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC       acid binding Ig-like lectin) family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-13 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK72907.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAQ88502.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF337818; AAK72907.1; ALT_INIT; mRNA.
DR   EMBL; AC011452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY358135; AAQ88502.1; ALT_INIT; mRNA.
DR   CCDS; CCDS12790.2; -. [Q96RL6-1]
DR   CCDS; CCDS46150.1; -. [Q96RL6-2]
DR   RefSeq; NP_001128635.1; NM_001135163.1. [Q96RL6-2]
DR   RefSeq; NP_443116.2; NM_052884.2. [Q96RL6-1]
DR   AlphaFoldDB; Q96RL6; -.
DR   SMR; Q96RL6; -.
DR   BioGRID; 125285; 5.
DR   IntAct; Q96RL6; 8.
DR   STRING; 9606.ENSP00000412361; -.
DR   GlyCosmos; Q96RL6; 7 sites, No reported glycans.
DR   GlyGen; Q96RL6; 8 sites.
DR   iPTMnet; Q96RL6; -.
DR   PhosphoSitePlus; Q96RL6; -.
DR   SwissPalm; Q96RL6; -.
DR   BioMuta; SIGLEC11; -.
DR   DMDM; 294862467; -.
DR   MassIVE; Q96RL6; -.
DR   PaxDb; 9606-ENSP00000412361; -.
DR   PeptideAtlas; Q96RL6; -.
DR   ProteomicsDB; 77982; -. [Q96RL6-1]
DR   ProteomicsDB; 77983; -. [Q96RL6-2]
DR   Antibodypedia; 32226; 237 antibodies from 30 providers.
DR   DNASU; 114132; -.
DR   Ensembl; ENST00000426971.2; ENSP00000398891.2; ENSG00000161640.15. [Q96RL6-2]
DR   Ensembl; ENST00000447370.6; ENSP00000412361.2; ENSG00000161640.15. [Q96RL6-1]
DR   GeneID; 114132; -.
DR   KEGG; hsa:114132; -.
DR   MANE-Select; ENST00000447370.6; ENSP00000412361.2; NM_052884.3; NP_443116.2.
DR   UCSC; uc010ybh.3; human. [Q96RL6-1]
DR   AGR; HGNC:15622; -.
DR   CTD; 114132; -.
DR   GeneCards; SIGLEC11; -.
DR   HGNC; HGNC:15622; SIGLEC11.
DR   HPA; ENSG00000161640; Group enriched (lymphoid tissue, ovary).
DR   MIM; 607157; gene.
DR   neXtProt; NX_Q96RL6; -.
DR   OpenTargets; ENSG00000161640; -.
DR   PharmGKB; PA38005; -.
DR   VEuPathDB; HostDB:ENSG00000161640; -.
DR   eggNOG; ENOG502S41V; Eukaryota.
DR   GeneTree; ENSGT01080000257333; -.
DR   HOGENOM; CLU_024444_5_1_1; -.
DR   InParanoid; Q96RL6; -.
DR   OMA; DCSLMIR; -.
DR   OrthoDB; 2963061at2759; -.
DR   PhylomeDB; Q96RL6; -.
DR   TreeFam; TF332441; -.
DR   PathwayCommons; Q96RL6; -.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   SignaLink; Q96RL6; -.
DR   BioGRID-ORCS; 114132; 68 hits in 1142 CRISPR screens.
DR   GenomeRNAi; 114132; -.
DR   Pharos; Q96RL6; Tbio.
DR   PRO; PR:Q96RL6; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q96RL6; Protein.
DR   Bgee; ENSG00000161640; Expressed in adrenal tissue and 107 other cell types or tissues.
DR   ExpressionAtlas; Q96RL6; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
DR   GO; GO:0033691; F:sialic acid binding; IDA:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   CDD; cd20987; IgC2_CD33_d2_like; 1.
DR   CDD; cd05712; IgV_CD33; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   PANTHER; PTHR12035; SIALIC ACID BINDING IMMUNOGLOBULIN-LIKE LECTIN; 1.
DR   PANTHER; PTHR12035:SF96; SIALIC ACID-BINDING IG-LIKE LECTIN 16; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 5.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00290; IG_MHC; 1.
DR   Genevisible; Q96RL6; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Lectin; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..698
FT                   /note="Sialic acid-binding Ig-like lectin 11"
FT                   /id="PRO_0000014951"
FT   TOPO_DOM        28..561
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        562..584
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        585..698
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          31..134
FT                   /note="Ig-like V-type"
FT   DOMAIN          159..244
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          251..350
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          355..452
FT                   /note="Ig-like C2-type 3"
FT   REGION          596..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          675..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           642..647
FT                   /note="ITIM motif"
FT   COMPBIAS        603..627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         132
FT                   /ligand="N-acetylneuraminate"
FT                   /ligand_id="ChEBI:CHEBI:35418"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         668
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96LC7"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        497
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        515
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        49..186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        54..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        177..228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        287..334
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        391..436
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         455..551
FT                   /note="YPPQLLGPSCSWEAEGLHCSCSSQASPAPSLRWWLGEELLEGNSSQGSFEVT
FT                   PSSAGPWANSSLSLHGGLSSGLRLRCKAWNVHGAQSGSVFQLLPG -> W (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_008764"
FT   CONFLICT        96
FT                   /note="E -> A (in Ref. 3; AAQ88502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        365
FT                   /note="A -> G (in Ref. 3; AAQ88502)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   698 AA;  75795 MW;  61CF0F530DCDD62F CRC64;
     MVPGQAQPQS PEMLLLPLLL PVLGAGSLNK DPSYSLQVQR QVPVPEGLCV IVSCNLSYPR
     DGWDESTAAY GYWFKGRTSP KTGAPVATNN QSREVEMSTR DRFQLTGDPG KGSCSLVIRD
     AQREDEAWYF FRVERGSRVR HSFLSNAFFL KVTALTKKPD VYIPETLEPG QPVTVICVFN
     WAFKKCPAPS FSWTGAALSP RRTRPSTSHF SVLSFTPSPQ DHDTDLTCHV DFSRKGVSAQ
     RTVRLRVAYA PKDLIISISH DNTSALELQG NVIYLEVQKG QFLRLLCAAD SQPPATLSWV
     LQDRVLSSSH PWGPRTLGLE LRGVRAGDSG RYTCRAENRL GSQQQALDLS VQYPPENLRV
     MVSQANRTVL ENLGNGTSLP VLEGQSLRLV CVTHSSPPAR LSWTRWGQTV GPSQPSDPGV
     LELPPIQMEH EGEFTCHAQH PLGSQHVSLS LSVHYPPQLL GPSCSWEAEG LHCSCSSQAS
     PAPSLRWWLG EELLEGNSSQ GSFEVTPSSA GPWANSSLSL HGGLSSGLRL RCKAWNVHGA
     QSGSVFQLLP GKLEHGGGLG LGAALGAGVA ALLAFCSCLV VFRVKICRKE ARKRAAAEQD
     VPSTLGPISQ GHQHECSAGS SQDHPPPGAA TYTPGKGEEQ ELHYASLSFQ GLRLWEPADQ
     EAPSTTEYSE IKIHTGQPLR GPGFGLQLER EMSGMVPK
//