SIGLEC7

SIGLEC7

Available structures

Human UniProt search: PDBe RCSB

List of PDB id codes
1NKO, 1O7S, 1O7V, 2DF3, 2G5R, 2HRL

Identifiers

Aliases

SIGLEC7, AIRM1, CD328, CDw328, D-siglec, QA79, SIGLEC-7, SIGLEC19P, SIGLECP2, p75, p75/AIRM1, sialic acid binding Ig like lectin 7, AIRM-1

External IDs

OMIM: 604410 HomoloGene: 130668 GeneCards: SIGLEC7

Gene location (Human)

Chr.	Chromosome 19 (human)^[1]

Band	19q13.41	Start	51,142,299 bp^[1]
Band	19q13.41	End	51,153,526 bp^[1]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

monocyte

blood

spleen

appendix

amniotic fluid

lymph node

cancellous bone

right lobe of liver

upper lobe of left lung

bone marrow

n/a

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	carbohydrate binding signaling receptor activity
Cellular component	integral component of membrane plasma membrane integral component of plasma membrane membrane
Biological process	cell adhesion regulation of immune response signal transduction
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


27036


n/a

Ensembl


ENSG00000168995


n/a

UniProt


Q9Y286


n/a

RefSeq (mRNA)


NM_001277201 NM_014385 NM_016543


n/a

RefSeq (protein)


NP_001264130 NP_055200 NP_057627


n/a

Location (UCSC)

Chr 19: 51.14 – 51.15 Mb

n/a

PubMed search

^[2]

n/a

Wikidata

View/Edit Human

Sialic acid-binding Ig-like lectin 7 is a protein that in humans is encoded by the SIGLEC7 gene.^[3]^[4] SIGLEC7 has also been designated as CD328 (cluster of differentiation 328).

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000168995 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Nicoll G, Ni J, Liu D, Klenerman P, Munday J, Dubock S, Mattei MG, Crocker PR (Dec 1999). "Identification and characterization of a novel siglec, siglec-7, expressed by human natural killer cells and monocytes". J Biol Chem. 274 (48): 34089–95. doi:10.1074/jbc.274.48.34089. PMID 10567377.
^ "Entrez Gene: SIGLEC7 sialic acid binding Ig-like lectin 7".

Reif K, Buday L, Downward J, Cantrell DA (1994). "SH3 domains of the adapter molecule Grb2 complex with two proteins in T cells: the guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases". J. Biol. Chem. 269 (19): 14081–7. doi:10.1016/S0021-9258(17)36757-1. PMID 8188688.
Falco M, Biassoni R, Bottino C, et al. (1999). "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 (6): 793–802. doi:10.1084/jem.190.6.793. PMC 2195632. PMID 10499918.
Ye X, Mehlen P, Rabizadeh S, et al. (1999). "TRAF family proteins interact with the common neurotrophin receptor and modulate apoptosis induction". J. Biol. Chem. 274 (42): 30202–8. doi:10.1074/jbc.274.42.30202. PMID 10514511.
Vitale C, Romagnani C, Falco M, et al. (2000). "Engagement of p75/AIRM1 or CD33 inhibits the proliferation of normal or leukemic myeloid cells". Proc. Natl. Acad. Sci. U.S.A. 96 (26): 15091–6. doi:10.1073/pnas.96.26.15091. PMC 24778. PMID 10611343.
Angata T, Varki A (2000). "Siglec-7: a sialic acid-binding lectin of the immunoglobulin superfamily". Glycobiology. 10 (4): 431–8. doi:10.1093/glycob/10.4.431. PMID 10764831.
Ito A, Handa K, Withers DA, et al. (2001). "Binding specificity of siglec7 to disialogangliosides of renal cell carcinoma: possible role of disialogangliosides in tumor progression". FEBS Lett. 498 (1): 116–20. doi:10.1016/S0014-5793(01)02476-0. PMID 11389909. S2CID 6755832.
Mingari MC, Vitale C, Romagnani C, et al. (2001). "Regulation of myeloid cell proliferation and survival by p75/AIRM1 and CD33 surface receptors". Progress in Basic and Clinical Immunology. Advances in Experimental Medicine and Biology. Vol. 495. pp. 55–61. doi:10.1007/978-1-4615-0685-0_8. ISBN 978-1-4613-5194-8. PMID 11774609.
Yousef GM, Ordon MH, Foussias G, Diamandis EP (2002). "Genomic organization of the siglec gene locus on chromosome 19q13.4 and cloning of two new siglec pseudogenes". Gene. 286 (2): 259–70. doi:10.1016/S0378-1119(02)00432-8. PMID 11943481.
Alphey MS, Attrill H, Crocker PR, van Aalten DM (2003). "High resolution crystal structures of Siglec-7. Insights into ligand specificity in the Siglec family". J. Biol. Chem. 278 (5): 3372–7. doi:10.1074/jbc.M210602200. PMID 12438315.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Nicoll G, Avril T, Lock K, et al. (2003). "Ganglioside GD3 expression on target cells can modulate NK cell cytotoxicity via siglec-7-dependent and -independent mechanisms". Eur. J. Immunol. 33 (6): 1642–8. doi:10.1002/eji.200323693. PMID 12778482. S2CID 7541832.
Dimasi N, Moretta A, Moretta L, et al. (2004). "Structure of the saccharide-binding domain of the human natural killer cell inhibitory receptor p75/AIRM1". Acta Crystallogr. D. 60 (Pt 2): 401–3. doi:10.1107/S0907444903028439. PMID 14747738.
Ikehara Y, Ikehara SK, Paulson JC (2004). "Negative regulation of T cell receptor signaling by Siglec-7 (p70/AIRM) and Siglec-9". J. Biol. Chem. 279 (41): 43117–25. doi:10.1074/jbc.M403538200. PMID 15292262.
Avril T, Floyd H, Lopez F, et al. (2005). "The membrane-proximal immunoreceptor tyrosine-based inhibitory motif is critical for the inhibitory signaling mediated by Siglecs-7 and -9, CD33-related Siglecs expressed on human monocytes and NK cells". J. Immunol. 173 (11): 6841–9. doi:10.4049/jimmunol.173.11.6841. PMID 15557178.
Yamaji T, Mitsuki M, Teranishi T, Hashimoto Y (2005). "Characterization of inhibitory signaling motifs of the natural killer cell receptor Siglec-7: attenuated recruitment of phosphatases by the receptor is attributed to two amino acids in the motifs". Glycobiology. 15 (7): 667–76. doi:10.1093/glycob/cwi048. PMID 15703304.
Attrill H, Takazawa H, Witt S, et al. (2006). "The structure of siglec-7 in complex with sialosides: leads for rational structure-based inhibitor design". Biochem. J. 397 (2): 271–8. doi:10.1042/BJ20060103. PMC 1513286. PMID 16623661.
Rapoport EM, Pazynina GV, Sablina MA, et al. (2006). "Probing sialic acid binding Ig-like lectins (siglecs) with sulfated oligosaccharides". Biochemistry Mosc. 71 (5): 496–504. doi:10.1134/S0006297906050051. PMID 16732727. S2CID 11537303.
Biedermann B, Gil D, Bowen DT, Crocker PR (2007). "Analysis of the CD33-related siglec family reveals that Siglec-9 is an endocytic receptor expressed on subsets of acute myeloid leukemia cells and absent from normal hematopoietic progenitors". Leuk. Res. 31 (2): 211–20. doi:10.1016/j.leukres.2006.05.026. PMID 16828866.

PDB gallery

1nko: Energetic and structural basis of sialylated oligosaccharide recognition by the natural killer cell inhibitory receptor p75/AIRM1 or Siglec-7
1o7s: HIGH RESOLUTION STRUCTURE OF SIGLEC-7
1o7v: HIGH RESOLUTION STRUCTURE OF SIGLEC-7
2df3: The structure of Siglec-7 in complex with alpha(2,3)/alpha(2,6) disialyl lactotetraosyl 2-(trimethylsilyl)ethyl
2g5r: Crystal structure of Siglec-7 in complex with methyl-9-(aminooxalyl-amino)-9-deoxyNeu5Ac (oxamido-Neu5Ac)
2hrl: Siglec-7 in complex with GT1b

External links

SIGLEC7+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50	CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51–100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101–150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151–200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201–250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251–300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301–350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

This membrane protein–related article is a stub. You can help Wikipedia by expanding it.

This page was last edited on 26 August 2023, at 20:55

From Wikipedia, the free encyclopedia

References

Further reading

External links