ID SN_HUMAN Reviewed; 1709 AA.
AC Q9BZZ2; Q96DL4; Q9GZS5; Q9H1H6; Q9H1H7; Q9H7L7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 27-MAR-2024, entry version 194.
DE RecName: Full=Sialoadhesin;
DE AltName: Full=Sialic acid-binding Ig-like lectin 1;
DE Short=Siglec-1;
DE AltName: CD_antigen=CD169;
DE Flags: Precursor;
GN Name=SIGLEC1; Synonyms=SN;
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 CHARACTERIZATION.
RC TISSUE=Monocyte;
RX PubMed=11133773; DOI=10.1182/blood.v97.1.288;
RA Hartnell A., Steel J., Turley H., Jones M., Jackson D.G., Crocker P.R.;
RT "Characterization of human sialoadhesin, a sialic acid binding receptor
RT expressed by resident and inflammatory macrophage populations.";
RL Blood 97:288-296(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 733-1709 (ISOFORMS 1 AND 2).
RC TISSUE=Spleen;
RX PubMed=11214971; DOI=10.1093/dnares/7.6.357;
RA Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen.";
RL DNA Res. 7:357-366(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1539-1709 (ISOFORM 3).
RC TISSUE=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 [5]
RP FUNCTION.
RX PubMed=12940982; DOI=10.1046/j.1365-2958.2003.03634.x;
RA Jones C., Virji M., Crocker P.R.;
RT "Recognition of sialylated meningococcal lipopolysaccharide by siglecs
RT expressed on myeloid cells leads to enhanced bacterial uptake.";
RL Mol. Microbiol. 49:1213-1225(2003).
RN [6]
RP FUNCTION, INTERACTION WITH TYROBP, AND INDUCTION BY VIRAL INFECTION.
RX PubMed=26358190; DOI=10.1038/cr.2015.108;
RA Zheng Q., Hou J., Zhou Y., Yang Y., Xie B., Cao X.;
RT "Siglec1 suppresses antiviral innate immune response by inducing TBK1
RT degradation via the ubiquitin ligase TRIM27.";
RL Cell Res. 25:1121-1136(2015).
RN [7]
RP FUNCTION, INDUCTION BY INTERFERON-ALPHA, AND SUBCELLULAR LOCATION.
RX PubMed=28129379; DOI=10.1371/journal.ppat.1006181;
RA Hammonds J.E., Beeman N., Ding L., Takushi S., Francis A.C., Wang J.J.,
RA Melikyan G.B., Spearman P.;
RT "Siglec-1 initiates formation of the virus-containing compartment and
RT enhances macrophage-to-T cell transmission of HIV-1.";
RL PLoS Pathog. 13:e1006181-e1006181(2017).
RN [8]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=31160823; DOI=10.1038/s41564-019-0453-2;
RA Perez-Zsolt D., Erkizia I., Pino M., Garcia-Gallo M., Martin M.T.,
RA Benet S., Chojnacki J., Fernandez-Figueras M.T., Guerrero D., Urrea V.,
RA Muniz-Trabudua X., Kremer L., Martinez-Picado J., Izquierdo-Useros N.;
RT "Anti-Siglec-1 antibodies block Ebola viral uptake and decrease cytoplasmic
RT viral entry.";
RL Nat. Microbiol. 4:1558-1570(2019).
RN [9]
RP FUNCTION.
RX PubMed=33489013; DOI=10.1002/jev2.12046;
RA Benet S., Galvez C., Drobniewski F., Kontsevaya I., Arias L.,
RA Monguio-Tortajada M., Erkizia I., Urrea V., Ong R.Y., Luquin M., Dupont M.,
RA Chojnacki J., Dalmau J., Cardona P., Neyrolles O., Lugo-Villarino G.,
RA Verollet C., Julian E., Furrer H., Guenthard H.F., Crocker P.R., Tapia G.,
RA Borras F.E., Fellay J., McLaren P.J., Telenti A., Cardona P.J., Clotet B.,
RA Vilaplana C., Martinez-Picado J., Izquierdo-Useros N.;
RT "Dissemination of Mycobacterium tuberculosis is associated to a SIGLEC1
RT null variant that limits antigen exchange via trafficking extracellular
RT vesicles.";
RL J. Extracell. Vesicles 10:e12046-e12046(2021).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-116.
RX PubMed=34782760; DOI=10.1038/s41423-021-00794-6;
RA Perez-Zsolt D., Munoz-Basagoiti J., Rodon J., Elosua-Bayes M.,
RA Raich-Regue D., Risco C., Sachse M., Pino M., Gumber S., Paiardini M.,
RA Chojnacki J., Erkizia I., Muniz-Trabudua X., Ballana E., Riveira-Munoz E.,
RA Noguera-Julian M., Paredes R., Trinite B., Tarres-Freixas F., Blanco I.,
RA Guallar V., Carrillo J., Blanco J., Telenti A., Heyn H., Segales J.,
RA Clotet B., Martinez-Picado J., Vergara-Alert J., Izquierdo-Useros N.;
RT "SARS-CoV-2 interaction with Siglec-1 mediates trans-infection by dendritic
RT cells.";
RL Cell. Mol. Immunol. 18:2676-2678(2021).
CC -!- FUNCTION: Macrophage-restricted adhesion molecule that mediates sialic-
CC acid dependent binding to lymphocytes, including granulocytes,
CC monocytes, natural killer cells, B-cells and CD8 T-cells. Plays a
CC crucial role in limiting bacterial dissemination by engaging sialylated
CC bacteria to promote effective phagocytosis and antigen presentation for
CC the adaptive immune response (PubMed:12940982, PubMed:33489013).
CC Mediates the uptake of various enveloped viruses via sialic acid
CC recognition and subsequently induces the formation of intracellular
CC compartments filled with virions (VCCs)(PubMed:28129379). In turn,
CC enhances macrophage-to-T-cell transmission of several viruses including
CC HIV-1 or SARS-CoV-2 (PubMed:28129379, PubMed:34782760). Acts as an
CC endocytic receptor mediating clathrin dependent endocytosis.
CC Preferentially binds to alpha-2,3-linked sialic acid (PubMed:12940982).
CC Binds to SPN/CD43 on T-cells (By similarity). May play a role in
CC hemopoiesis. Plays a role in the inhibition of antiviral innate immune
CC by promoting TBK1 degradation via TYROBP and TRIM27-mediated
CC ubiquitination (PubMed:26358190). {ECO:0000250|UniProtKB:Q62230,
CC ECO:0000269|PubMed:12940982, ECO:0000269|PubMed:26358190,
CC ECO:0000269|PubMed:28129379, ECO:0000269|PubMed:33489013,
CC ECO:0000269|PubMed:34782760}.
CC -!- FUNCTION: (Microbial infection) Facilitates viral cytoplasmic entry
CC into activated dendritic cells via recognition of sialylated
CC gangliosides pesent on viral membrane. {ECO:0000269|PubMed:31160823}.
CC -!- SUBUNIT: Interacts with TYROBP. Interacts with CLEC10A (By similarity).
CC {ECO:0000250|UniProtKB:Q62230, ECO:0000269|PubMed:26358190}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:28129379}; Single-pass type I membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9BZZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZZ2-2; Sequence=VSP_002571;
CC Name=3;
CC IsoId=Q9BZZ2-3; Sequence=VSP_002572;
CC -!- TISSUE SPECIFICITY: Expressed by macrophages in various tissues. High
CC levels are found in spleen, lymph node, perivascular macrophages in
CC brain and lower levels in bone marrow, liver Kupffer cells and lamina
CC propria of colon and lung. Also expressed by inflammatory macrophages
CC in rheumatoid arthritis.
CC -!- INDUCTION: By interferon-alpha (PubMed:28129379). By viral infection
CC (PubMed:26358190). {ECO:0000269|PubMed:26358190,
CC ECO:0000269|PubMed:28129379}.
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-1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_267";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF230073; AAK00757.1; -; mRNA.
DR EMBL; AL109804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK024459; BAB15749.1; -; mRNA.
DR EMBL; AK024462; BAB15752.1; -; mRNA.
DR EMBL; AK024479; BAB15769.1; -; mRNA.
DR EMBL; AK057560; BAB71527.1; -; mRNA.
DR CCDS; CCDS13060.1; -. [Q9BZZ2-1]
DR RefSeq; NP_075556.1; NM_023068.3. [Q9BZZ2-1]
DR RefSeq; XP_006723673.1; XM_006723610.3.
DR RefSeq; XP_011527626.1; XM_011529324.2.
DR RefSeq; XP_011527627.1; XM_011529325.2.
DR RefSeq; XP_011527628.1; XM_011529326.2.
DR RefSeq; XP_011527629.1; XM_011529327.2.
DR RefSeq; XP_011527630.1; XM_011529328.2.
DR RefSeq; XP_011527631.1; XM_011529329.1.
DR AlphaFoldDB; Q9BZZ2; -.
DR SMR; Q9BZZ2; -.
DR BioGRID; 112498; 2.
DR STRING; 9606.ENSP00000341141; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DR GlyCosmos; Q9BZZ2; 14 sites, No reported glycans.
DR GlyGen; Q9BZZ2; 14 sites.
DR iPTMnet; Q9BZZ2; -.
DR PhosphoSitePlus; Q9BZZ2; -.
DR SwissPalm; Q9BZZ2; -.
DR BioMuta; SIGLEC1; -.
DR DMDM; 18202745; -.
DR jPOST; Q9BZZ2; -.
DR MassIVE; Q9BZZ2; -.
DR PaxDb; 9606-ENSP00000341141; -.
DR PeptideAtlas; Q9BZZ2; -.
DR ProteomicsDB; 79923; -. [Q9BZZ2-1]
DR ProteomicsDB; 79924; -. [Q9BZZ2-2]
DR ProteomicsDB; 79925; -. [Q9BZZ2-3]
DR Antibodypedia; 7559; 777 antibodies from 34 providers.
DR CPTC; Q9BZZ2; 1 antibody.
DR DNASU; 6614; -.
DR Ensembl; ENST00000344754.6; ENSP00000341141.4; ENSG00000088827.14. [Q9BZZ2-1]
DR Ensembl; ENST00000707083.1; ENSP00000516734.1; ENSG00000088827.14. [Q9BZZ2-3]
DR GeneID; 6614; -.
DR KEGG; hsa:6614; -.
DR MANE-Select; ENST00000344754.6; ENSP00000341141.4; NM_023068.4; NP_075556.1.
DR UCSC; uc002wja.3; human. [Q9BZZ2-1]
DR AGR; HGNC:11127; -.
DR CTD; 6614; -.
DR DisGeNET; 6614; -.
DR GeneCards; SIGLEC1; -.
DR HGNC; HGNC:11127; SIGLEC1.
DR HPA; ENSG00000088827; Low tissue specificity.
DR MIM; 600751; gene.
DR neXtProt; NX_Q9BZZ2; -.
DR OpenTargets; ENSG00000088827; -.
DR PharmGKB; PA35976; -.
DR VEuPathDB; HostDB:ENSG00000088827; -.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT01100000263535; -.
DR HOGENOM; CLU_243945_0_0_1; -.
DR InParanoid; Q9BZZ2; -.
DR OMA; VTFNSQK; -.
DR OrthoDB; 5360480at2759; -.
DR PhylomeDB; Q9BZZ2; -.
DR TreeFam; TF334827; -.
DR PathwayCommons; Q9BZZ2; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; Q9BZZ2; -.
DR BioGRID-ORCS; 6614; 18 hits in 1149 CRISPR screens.
DR ChiTaRS; SIGLEC1; human.
DR GenomeRNAi; 6614; -.
DR Pharos; Q9BZZ2; Tbio.
DR PRO; PR:Q9BZZ2; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9BZZ2; Protein.
DR Bgee; ENSG00000088827; Expressed in right adrenal gland cortex and 141 other cell types or tissues.
DR ExpressionAtlas; Q9BZZ2; baseline and differential.
DR Genevisible; Q9BZZ2; HS.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProt.
DR GO; GO:0030246; F:carbohydrate binding; NAS:UniProtKB.
DR GO; GO:0046790; F:virion binding; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; NAS:UniProtKB.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
DR GO; GO:0032480; P:negative regulation of type I interferon production; IDA:UniProt.
DR CDD; cd00096; Ig; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 17.
DR InterPro; IPR013162; CD80_C2-set.
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 InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR47243; SIALOADHESIN; 1.
DR PANTHER; PTHR47243:SF1; SIALOADHESIN; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13895; Ig_2; 6.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 17.
DR SMART; SM00408; IGc2; 14.
DR SUPFAM; SSF48726; Immunoglobulin; 11.
DR PROSITE; PS50835; IG_LIKE; 14.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Endocytosis; Glycoprotein; Immunoglobulin domain; Lectin; Membrane;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..1709
FT /note="Sialoadhesin"
FT /id="PRO_0000014968"
FT TOPO_DOM 20..1641
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1642..1662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1663..1709
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..136
FT /note="Ig-like V-type"
FT DOMAIN 139..233
FT /note="Ig-like C2-type 1"
FT DOMAIN 238..320
FT /note="Ig-like C2-type 2"
FT DOMAIN 326..405
FT /note="Ig-like C2-type 3"
FT DOMAIN 411..507
FT /note="Ig-like C2-type 4"
FT DOMAIN 511..593
FT /note="Ig-like C2-type 5"
FT DOMAIN 601..705
FT /note="Ig-like C2-type 6"
FT DOMAIN 708..785
FT /note="Ig-like C2-type 7"
FT DOMAIN 799..894
FT /note="Ig-like C2-type 8"
FT DOMAIN 898..977
FT /note="Ig-like C2-type 9"
FT DOMAIN 984..1083
FT /note="Ig-like C2-type 10"
FT DOMAIN 1085..1165
FT /note="Ig-like C2-type 11"
FT DOMAIN 1176..1248
FT /note="Ig-like C2-type 12"
FT DOMAIN 1259..1341
FT /note="Ig-like C2-type 13"
FT DOMAIN 1350..1442
FT /note="Ig-like C2-type 14"
FT DOMAIN 1445..1528
FT /note="Ig-like C2-type 15"
FT DOMAIN 1536..1631
FT /note="Ig-like C2-type 16"
FT BINDING 63
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250|UniProtKB:Q62230"
FT BINDING 116
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250|UniProtKB:Q62230"
FT BINDING 122..126
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 41..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 160..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 262..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 346..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 433..491
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 531..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 624..689
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 729..774
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 817..876
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 916..960
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1005..1067
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1107..1149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1193..1241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1281..1324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1367..1425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1465..1511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1554..1613
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1632..1709
FT /note="ALHRLHQFQQLLWVLGLLVGLLLLLLGLGACYTWRRRRVCKQSMGENSVEMA
FT FQKETTQLIDPDAATCETSTCAPPLG -> GEGRGLHLPGHSAQKPSS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11214971"
FT /id="VSP_002571"
FT VAR_SEQ 1666..1709
FT /note="RRRRVCKQSMGENSVEMAFQKETTQLIDPDAATCETSTCAPPLG -> SSLI
FT LMQPHVRPQPVPHPWADQWCCLPSGGESGQNL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_002572"
FT VARIANT 141
FT /note="V -> L (in dbSNP:rs35953127)"
FT /id="VAR_049943"
FT VARIANT 221
FT /note="V -> M (in dbSNP:rs6037651)"
FT /id="VAR_024502"
FT VARIANT 239
FT /note="K -> R (in dbSNP:rs625372)"
FT /id="VAR_014136"
FT VARIANT 464
FT /note="R -> H (in dbSNP:rs34924243)"
FT /id="VAR_049944"
FT VARIANT 919
FT /note="H -> P (in dbSNP:rs709012)"
FT /id="VAR_014137"
FT VARIANT 974
FT /note="A -> V (in dbSNP:rs3746638)"
FT /id="VAR_021926"
FT VARIANT 1335
FT /note="S -> Y (in dbSNP:rs3746636)"
FT /id="VAR_021927"
FT VARIANT 1487
FT /note="R -> W (in dbSNP:rs16988873)"
FT /id="VAR_049945"
FT VARIANT 1519
FT /note="A -> P (in dbSNP:rs2853217)"
FT /id="VAR_014138"
FT MUTAGEN 116
FT /note="R->A: Complete loss of sialic acid recognition
FT capacity."
FT /evidence="ECO:0000269|PubMed:34782760"
FT CONFLICT 1349
FT /note="A -> T (in Ref. 1; AAK00757)"
FT /evidence="ECO:0000305"
FT CONFLICT 1519
FT /note="A -> V (in Ref. 3; BAB15749/BAB15769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1709 AA; 182624 MW; 587C7CCA0B789A6D CRC64;
MGFLPKLLLL ASFFPAGQAS WGVSSPQDVQ GVKGSCLLIP CIFSFPADVE VPDGITAIWY
YDYSGQRQVV SHSADPKLVE ARFRGRTEFM GNPEHRVCNL LLKDLQPEDS GSYNFRFEIS
EVNRWSDVKG TLVTVTEEPR VPTIASPVEL LEGTEVDFNC STPYVCLQEQ VRLQWQGQDP
ARSVTFNSQK FEPTGVGHLE TLHMAMSWQD HGRILRCQLS VANHRAQSEI HLQVKYAPKG
VKILLSPSGR NILPGELVTL TCQVNSSYPA VSSIKWLKDG VRLQTKTGVL HLPQAAWSDA
GVYTCQAENG VGSLVSPPIS LHIFMAEVQV SPAGPILENQ TVTLVCNTPN EAPSDLRYSW
YKNHVLLEDA HSHTLRLHLA TRADTGFYFC EVQNVHGSER SGPVSVVVNH PPLTPVLTAF
LETQAGLVGI LHCSVVSEPL ATLVLSHGGH ILASTSGDSD HSPRFSGTSG PNSLRLEIRD
LEETDSGEYK CSATNSLGNA TSTLDFHANA ARLLISPAAE VVEGQAVTLS CRSGLSPTPD
ARFSWYLNGA LLHEGPGSSL LLPAASSTDA GSYHCRARDG HSASGPSSPA VLTVLYPPRQ
PTFTTRLDLD AAGAGAGRRG LLLCRVDSDP PARLQLLHKD RVVATSLPSG GGCSTCGGCS
PRMKVTKAPN LLRVEIHNPL LEEEGLYLCE ASNALGNAST SATFNGQATV LAIAPSHTLQ
EGTEANLTCN VSREAAGSPA NFSWFRNGVL WAQGPLETVT LLPVARTDAA LYACRILTEA
GAQLSTPVLL SVLYPPDRPK LSALLDMGQG HMALFICTVD SRPLALLALF HGEHLLATSL
GPQVPSHGRF QAKAEANSLK LEVRELGLGD SGSYRCEATN VLGSSNTSLF FQVRGAWVQV
SPSPELQEGQ AVVLSCQVHT GVPEGTSYRW YRDGQPLQES TSATLRFAAI TLTQAGAYHC
QAQAPGSATT SLAAPISLHV SYAPRHVTLT TLMDTGPGRL GLLLCRVDSD PPAQLRLLHG
DRLVASTLQG VGGPEGSSPR LHVAVAPNTL RLEIHGAMLE DEGVYICEAS NTLGQASASA
DFDAQAVNVQ VWPGATVREG QLVNLTCLVW TTHPAQLTYT WYQDGQQRLD AHSIPLPNVT
VRDATSYRCG VGPPGRAPRL SRPITLDVLY APRNLRLTYL LESHGGQLAL VLCTVDSRPP
AQLALSHAGR LLASSTAASV PNTLRLELRG PQPRDEGFYS CSARSPLGQA NTSLELRLEG
VRVILAPEAA VPEGAPITVT CADPAAHAPT LYTWYHNGRW LQEGPAASLS FLVATRAHAG
AYSCQAQDAQ GTRSSRPAAL QVLYAPQDAV LSSFRDSRAR SMAVIQCTVD SEPPAELALS
HDGKVLATSS GVHSLASGTG HVQVARNALR LQVQDVPAGD DTYVCTAQNL LGSISTIGRL
QVEGARVVAE PGLDVPEGAA LNLSCRLLGG PGPVGNSTFA WFWNDRRLHA EPVPTLAFTH
VARAQAGMYH CLAELPTGAA ASAPVMLRVL YPPKTPTMMV FVEPEGGLRG ILDCRVDSEP
LASLTLHLGS RLVASSQPQG APAEPHIHVL ASPNALRVDI EALRPSDQGE YICSASNVLG
SASTSTYFGV RALHRLHQFQ QLLWVLGLLV GLLLLLLGLG ACYTWRRRRV CKQSMGENSV
EMAFQKETTQ LIDPDAATCE TSTCAPPLG
//
