SIG11_HUMAN
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 03-AUG-2022, entry version 175.
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 GlyGen; Q96RL6; 8 sites.
DR iPTMnet; Q96RL6; -.
DR PhosphoSitePlus; Q96RL6; -.
DR SwissPalm; Q96RL6; -.
DR BioMuta; SIGLEC11; -.
DR DMDM; 294862467; -.
DR MassIVE; Q96RL6; -.
DR PaxDb; Q96RL6; -.
DR PeptideAtlas; Q96RL6; -.
DR PRIDE; Q96RL6; -.
DR ProteomicsDB; 77982; -. [Q96RL6-1]
DR ProteomicsDB; 77983; -. [Q96RL6-2]
DR Antibodypedia; 32226; 218 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 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; ENSGT01040000240469; -.
DR HOGENOM; CLU_024444_5_1_1; -.
DR InParanoid; Q96RL6; -.
DR OMA; RNAHGEQ; -.
DR OrthoDB; 1124645at2759; -.
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 1065 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 tissues.
DR ExpressionAtlas; Q96RL6; baseline and differential.
DR Genevisible; Q96RL6; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; 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; 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 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
