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Sialic acid-binding Ig-like lectin 7 (Siglec-7) (Adhesion inhibitory receptor molecule 1) (AIRM-1) (CDw328) (D-siglec) (QA79 membrane protein) (p75) (CD antigen CD328)

 SIGL7_HUMAN             Reviewed;         467 AA.
Q9Y286; Q9NZQ1; Q9UJ86; Q9UJ87; Q9Y502;
08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
25-OCT-2017, entry version 162.
RecName: Full=Sialic acid-binding Ig-like lectin 7;
Short=Siglec-7;
AltName: Full=Adhesion inhibitory receptor molecule 1;
Short=AIRM-1;
AltName: Full=CDw328;
AltName: Full=D-siglec;
AltName: Full=QA79 membrane protein;
AltName: Full=p75;
AltName: CD_antigen=CD328;
Flags: Precursor;
Name=SIGLEC7; Synonyms=AIRM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Dendritic cell;
PubMed=10567377; DOI=10.1074/jbc.274.48.34089;
Nicoll G., Ni J., Liu D., Klenerman P., Munday J., Dubock S.,
Mattei M.-G., Crocker P.R.;
"Identification and characterization of a novel siglec, siglec-7,
expressed by human natural killer cells and monocytes.";
J. Biol. Chem. 274:34089-34095(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), PHOSPHORYLATION,
AND INTERACTION WITH PTPN6.
TISSUE=Lymphoid tissue;
PubMed=10499918; DOI=10.1084/jem.190.6.793;
Falco M., Biassoni R., Bottino C., Vitale M., Sivori S.,
Augugliaro R., Moretta L., Moretta A.;
"Identification and molecular cloning of p75/AIRM1, a novel member of
the sialoadhesin family that functions as an inhibitory receptor in
human natural killer cells.";
J. Exp. Med. 190:793-802(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Dendritic cell;
Zhang W., Wan T., Cao X.;
"Characterization of a novel siglec from dendritic cells.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10764831; DOI=10.1093/glycob/10.4.431;
Angata T., Varki A.;
"Siglec-7: a sialic acid-binding lectin of the immunoglobulin
superfamily.";
Glycobiology 10:431-438(2000).
[5]
FUNCTION.
PubMed=10611343; DOI=10.1073/pnas.96.26.15091;
Vitale C., Romagnani C., Falco M., Ponte M., Vitale M., Moretta A.,
Bacigalupo A., Moretta L., Mingari M.C.;
"Engagement of p75/AIRM1 or CD33 inhibits the proliferation of normal
or leukemic myeloid cells.";
Proc. Natl. Acad. Sci. U.S.A. 96:15091-15096(1999).
[6]
DISIALOGANGLIOSIDE-BINDING.
PubMed=11389909; DOI=10.1016/S0014-5793(01)02476-0;
Ito A., Handa K., Withers D.A., Satoh M., Hakomori S.;
"Binding specificity of siglec7 to disialogangliosides of renal cell
carcinoma: possible role of disialogangliosides in tumor
progression.";
FEBS Lett. 498:116-120(2001).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[8]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 18-144, DISULFIDE BOND, AND
GLYCOSYLATION AT ASN-105.
PubMed=12438315; DOI=10.1074/jbc.M210602200;
Alphey M.S., Attrill H., Crocker P.R., van Aalten D.M.;
"High resolution crystal structures of Siglec-7. Insights into ligand
specificity in the Siglec family.";
J. Biol. Chem. 278:3372-3377(2003).
[9]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 19-150, AND DISULFIDE BOND.
PubMed=14747738; DOI=10.1107/S0907444903028439;
Dimasi N., Moretta A., Moretta L., Biassoni R., Mariuzza R.A.;
"Structure of the saccharide-binding domain of the human natural
killer cell inhibitory receptor p75/AIRM1.";
Acta Crystallogr. D 60:401-403(2004).
[10]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 18-144 IN COMPLEX WITH
SIALYLATED LIGAND, GLYCOSYLATION AT ASN-105, AND DISULFIDE BOND.
PubMed=16623661; DOI=10.1042/BJ20060103;
Attrill H., Takazawa H., Witt S., Kelm S., Isecke R., Brossmer R.,
Ando T., Ishida H., Kiso M., Crocker P.R., van Aalten D.M.;
"The structure of siglec-7 in complex with sialosides: leads for
rational structure-based inhibitor design.";
Biochem. J. 397:271-278(2006).
[11]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 18-144 IN COMPLEX WITH
ALPHA(2,8)-DISIALYLATED LIGAND GT1B, GLYCOSYLATION AT ASN-105, AND
DISULFIDE BOND.
PubMed=16895906; DOI=10.1074/jbc.M601714200;
Attrill H., Imamura A., Sharma R.S., Kiso M., Crocker P.R.,
van Aalten D.M.;
"Siglec-7 undergoes a major conformational change when complexed with
the alpha(2,8)-disialylganglioside GT1b.";
J. Biol. Chem. 281:32774-32783(2006).
[12]
VARIANT [LARGE SCALE ANALYSIS] PRO-215.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Putative adhesion molecule that mediates sialic-acid
dependent binding to cells. Preferentially binds to alpha-2,3- and
alpha-2,6-linked sialic acid. Also binds disialogangliosides
(disialogalactosyl globoside, disialyl lactotetraosylceramide and
disialyl GalNAc lactotetraoslylceramide). The sialic acid
recognition site may be masked by cis interactions with sialic
acids on the same cell surface. In the immune response, may act as
an inhibitory receptor upon ligand induced tyrosine
phosphorylation by recruiting cytoplasmic phosphatase(s) via their
SH2 domain(s) that block signal transduction through
dephosphorylation of signaling molecules. Mediates inhibition of
natural killer cells cytotoxicity. May play a role in hemopoiesis.
Inhibits differentiation of CD34+ cell precursors towards
myelomonocytic cell lineage and proliferation of leukemic myeloid
cells (in vitro). {ECO:0000269|PubMed:10611343}.
-!- SUBUNIT: Interacts with PTPN6/SHP-1 upon phosphorylation.
{ECO:0000269|PubMed:10499918, ECO:0000269|PubMed:16623661,
ECO:0000269|PubMed:16895906}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=AIRM-1b;
IsoId=Q9Y286-1; Sequence=Displayed;
Name=2; Synonyms=AIRM-2;
IsoId=Q9Y286-2; Sequence=VSP_002555;
Name=3; Synonyms=AIRM-3;
IsoId=Q9Y286-3; Sequence=VSP_002556, VSP_002558;
Note=No experimental confirmation available. May be produced at
very low levels due to a premature stop codon in the mRNA,
leading to nonsense-mediated mRNA decay.;
Name=4;
IsoId=Q9Y286-4; Sequence=VSP_002557, VSP_002558;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Predominantly expressed by resting and
activated natural killer cells and at lower levels by granulocytes
and monocytes. High expression found in placenta, liver, lung,
spleen, and peripheral blood leukocytes.
-!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to
as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This
motif is involved in modulation of cellular responses. The
phosphorylated ITIM motif can bind the SH2 domain of several SH2-
containing phosphatases.
-!- PTM: Tyrosine phosphorylated. {ECO:0000269|PubMed:10499918}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC
(sialic acid binding Ig-like lectin) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF44346.1; Type=Frameshift; Positions=406; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Siglec-7;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_274";
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EMBL; AF170485; AAF12759.1; -; mRNA.
EMBL; AJ007395; CAB46011.1; -; mRNA.
EMBL; AJ130710; CAB51126.1; -; mRNA.
EMBL; AJ130711; CAB51127.1; -; mRNA.
EMBL; AJ130712; CAB51128.1; -; mRNA.
EMBL; AJ130713; CAB51129.1; -; mRNA.
EMBL; AF178981; AAF44346.1; ALT_FRAME; mRNA.
EMBL; AF193441; AAF06790.1; -; mRNA.
CCDS; CCDS12826.1; -. [Q9Y286-1]
CCDS; CCDS42601.1; -. [Q9Y286-2]
CCDS; CCDS62771.1; -. [Q9Y286-4]
RefSeq; NP_001264130.1; NM_001277201.1. [Q9Y286-4]
RefSeq; NP_055200.1; NM_014385.3. [Q9Y286-1]
RefSeq; NP_057627.2; NM_016543.3. [Q9Y286-2]
UniGene; Hs.655393; -.
PDB; 1NKO; X-ray; 1.45 A; A=19-150.
PDB; 1O7S; X-ray; 1.75 A; A=18-144.
PDB; 1O7V; X-ray; 1.90 A; A=18-144.
PDB; 2DF3; X-ray; 1.90 A; A=18-144.
PDB; 2G5R; X-ray; 1.60 A; A=18-144.
PDB; 2HRL; X-ray; 1.85 A; A=18-144.
PDBsum; 1NKO; -.
PDBsum; 1O7S; -.
PDBsum; 1O7V; -.
PDBsum; 2DF3; -.
PDBsum; 2G5R; -.
PDBsum; 2HRL; -.
ProteinModelPortal; Q9Y286; -.
SMR; Q9Y286; -.
BioGrid; 117967; 5.
IntAct; Q9Y286; 1.
STRING; 9606.ENSP00000323328; -.
BindingDB; Q9Y286; -.
ChEMBL; CHEMBL3603730; -.
DrugBank; DB03740; N-acetyl-alpha-D-glucosamine.
iPTMnet; Q9Y286; -.
PhosphoSitePlus; Q9Y286; -.
DMDM; 25009269; -.
PaxDb; Q9Y286; -.
PeptideAtlas; Q9Y286; -.
PRIDE; Q9Y286; -.
Ensembl; ENST00000305628; ENSP00000306757; ENSG00000168995. [Q9Y286-2]
Ensembl; ENST00000317643; ENSP00000323328; ENSG00000168995. [Q9Y286-1]
Ensembl; ENST00000536156; ENSP00000437609; ENSG00000168995. [Q9Y286-3]
Ensembl; ENST00000600577; ENSP00000472529; ENSG00000168995. [Q9Y286-4]
GeneID; 27036; -.
KEGG; hsa:27036; -.
UCSC; uc002pvv.1; human. [Q9Y286-1]
CTD; 27036; -.
DisGeNET; 27036; -.
EuPathDB; HostDB:ENSG00000168995.13; -.
GeneCards; SIGLEC7; -.
H-InvDB; HIX0040323; -.
HGNC; HGNC:10876; SIGLEC7.
MIM; 604410; gene.
neXtProt; NX_Q9Y286; -.
OpenTargets; ENSG00000168995; -.
PharmGKB; PA35777; -.
eggNOG; ENOG410IJT6; Eukaryota.
eggNOG; ENOG410YKZU; LUCA.
GeneTree; ENSGT00760000119139; -.
HOGENOM; HOG000236324; -.
HOVERGEN; HBG036161; -.
InParanoid; Q9Y286; -.
KO; K06739; -.
OMA; FQGEGTA; -.
OrthoDB; EOG091G0445; -.
PhylomeDB; Q9Y286; -.
TreeFam; TF332441; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
EvolutionaryTrace; Q9Y286; -.
GeneWiki; SIGLEC7; -.
GenomeRNAi; 27036; -.
PRO; PR:Q9Y286; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000168995; -.
CleanEx; HS_SIGLEC7; -.
ExpressionAtlas; Q9Y286; baseline and differential.
Genevisible; Q9Y286; HS.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
GO; GO:0004872; F:receptor activity; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
Pfam; PF13895; Ig_2; 1.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 1.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Lectin; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 467 Sialic acid-binding Ig-like lectin 7.
/FTId=PRO_0000014947.
TOPO_DOM 19 353 Extracellular. {ECO:0000255}.
TRANSMEM 354 376 Helical. {ECO:0000255}.
TOPO_DOM 377 467 Cytoplasmic. {ECO:0000255}.
DOMAIN 39 122 Ig-like V-type.
DOMAIN 150 233 Ig-like C2-type 1.
DOMAIN 240 336 Ig-like C2-type 2.
REGION 131 135 Sialic acid binding.
{ECO:0000269|PubMed:12438315,
ECO:0000269|PubMed:16623661,
ECO:0000269|PubMed:16895906}.
MOTIF 435 440 ITIM motif.
BINDING 124 124 Sialic acid.
{ECO:0000269|PubMed:16623661,
ECO:0000269|PubMed:16895906}.
MOD_RES 429 429 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 105 105 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16623661,
ECO:0000269|PubMed:16895906}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 334 334 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 46 106 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:12438315,
ECO:0000269|PubMed:14747738,
ECO:0000269|PubMed:16623661,
ECO:0000269|PubMed:16895906}.
DISULFID 168 217 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 276 320 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 145 238 ALTHRPNILIPGTLESGCFQNLTCSVPWACEQGTPPMISWM
GTSVSPLHPSTTRSSVLTLIPQPQHHGTSLTCQVTLPGAGV
TTNRTIQLNVSY -> D (in isoform 2).
{ECO:0000303|PubMed:10499918,
ECO:0000303|PubMed:10764831,
ECO:0000303|Ref.3}.
/FTId=VSP_002555.
VAR_SEQ 145 145 A -> E (in isoform 3).
{ECO:0000303|PubMed:10499918}.
/FTId=VSP_002556.
VAR_SEQ 145 145 A -> G (in isoform 4).
{ECO:0000303|PubMed:10499918}.
/FTId=VSP_002557.
VAR_SEQ 146 467 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:10499918}.
/FTId=VSP_002558.
VARIANT 215 215 L -> P (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035523.
CONFLICT 42 42 V -> A (in Ref. 4; AAF44346).
{ECO:0000305}.
HELIX 23 25 {ECO:0000244|PDB:1NKO}.
STRAND 27 30 {ECO:0000244|PDB:1NKO}.
STRAND 32 37 {ECO:0000244|PDB:1NKO}.
STRAND 42 44 {ECO:0000244|PDB:1NKO}.
STRAND 46 49 {ECO:0000244|PDB:1NKO}.
TURN 54 58 {ECO:0000244|PDB:1NKO}.
STRAND 62 67 {ECO:0000244|PDB:1NKO}.
STRAND 69 71 {ECO:0000244|PDB:2HRL}.
HELIX 72 74 {ECO:0000244|PDB:1O7V}.
STRAND 78 81 {ECO:0000244|PDB:1NKO}.
HELIX 85 88 {ECO:0000244|PDB:2HRL}.
HELIX 89 91 {ECO:0000244|PDB:1NKO}.
TURN 92 94 {ECO:0000244|PDB:1NKO}.
STRAND 95 97 {ECO:0000244|PDB:1NKO}.
HELIX 101 103 {ECO:0000244|PDB:1NKO}.
STRAND 108 110 {ECO:0000244|PDB:1NKO}.
HELIX 115 117 {ECO:0000244|PDB:1NKO}.
STRAND 119 127 {ECO:0000244|PDB:1NKO}.
STRAND 130 133 {ECO:0000244|PDB:1NKO}.
STRAND 139 144 {ECO:0000244|PDB:1NKO}.
SEQUENCE 467 AA; 51143 MW; 8AFE44462B001F52 CRC64;
MLLLLLLPLL WGRERVEGQK SNRKDYSLTM QSSVTVQEGM CVHVRCSFSY PVDSQTDSDP
VHGYWFRAGN DISWKAPVAT NNPAWAVQEE TRDRFHLLGD PQTKNCTLSI RDARMSDAGR
YFFRMEKGNI KWNYKYDQLS VNVTALTHRP NILIPGTLES GCFQNLTCSV PWACEQGTPP
MISWMGTSVS PLHPSTTRSS VLTLIPQPQH HGTSLTCQVT LPGAGVTTNR TIQLNVSYPP
QNLTVTVFQG EGTASTALGN SSSLSVLEGQ SLRLVCAVDS NPPARLSWTW RSLTLYPSQP
SNPLVLELQV HLGDEGEFTC RAQNSLGSQH VSLNLSLQQE YTGKMRPVSG VLLGAVGGAG
ATALVFLSFC VIFIVVRSCR KKSARPAADV GDIGMKDANT IRGSASQGNL TESWADDNPR
HHGLAAHSSG EEREIQYAPL SFHKGEPQDL SGQEATNNEY SEIKIPK


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bs-0794P Peptides: CD169_sialoadhesin(Sn)(Sialic acid-binding Ig-like lectin 1;Siglec-1) Protein Length:12-25 amino acids. 200ug lyophilized
EIAAB38464 Homo sapiens,Human,Protein FOAP-9,Sialic acid-binding Ig-like lectin 9,SIGLEC9,Siglec-9,UNQ668_PRO1302
C788 Recombinant Human Sialic Acid-Binding Ig-Like Lectin 9 per Siglec 9 per CD329 (C-Fc) 10ug
E0422r ELISA Brain neuron cytoplasmic protein 3,Mag,Myelin-associated glycoprotein,Rat,Rattus norvegicus,Sialic acid-binding Ig-like lectin 4a,Siglec-4a 96T


 

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