CD11c

ITGAX

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1N3Y, 2LUV, 3K6S, 3K71, 3K72, 4NEH, 4NEN, 5ES4

Identifiers

Aliases

ITGAX, CD11C, SLEB6, integrin subunit alpha X

External IDs

OMIM: 151510 MGI: 96609 HomoloGene: 55493 GeneCards: ITGAX

Gene ontology
Molecular function	• protein binding • metal ion binding • receptor activity
Cellular component	• integral component of membrane • cell surface • integrin complex • plasma membrane • membrane
Biological process	• animal organ morphogenesis • integrin-mediated signaling pathway • heterotypic cell-cell adhesion • cell adhesion • extracellular matrix organization • leukocyte migration • positive regulation of protein targeting to mitochondrion
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


3687


16411

Ensembl


ENSG00000140678


ENSMUSG00000030789

UniProt


P20702


Q9QXH4

RefSeq (mRNA)


NM_000887 NM_001286375


NM_021334

RefSeq (protein)


NP_000878.2 NP_001273304.1


NP_067309.1

Location (UCSC)

Chr 16: 31.36 – 31.38 Mb

Chr 7: 128.13 – 128.15 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

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CD11c, also known as Integrin, alpha X (complement component 3 receptor 4 subunit) (ITGAX), is a gene that encodes for CD11c .^[3]^[4]

CD11c is an integrin alpha X chain protein. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This protein combines with the beta 2 chain (ITGB2) to form a leukocyte-specific integrin referred to as inactivated-C3b (iC3b) receptor 4 (CR4). The alpha X beta 2 complex seems to overlap the properties of the alpha M beta 2 integrin in the adherence of neutrophils and monocytes to stimulated endothelium cells, and in the phagocytosis of complement coated particles.^[3]

CD11c is a type I transmembrane protein found at high levels on most human dendritic cells, but also on monocytes, macrophages, neutrophils, and some B cells that induces cellular activation and helps trigger neutrophil respiratory burst; expressed in hairy cell leukemias, acute nonlymphocytic leukemias, and some B-cell chronic lymphocytic leukemias.

References

Stewart M, Thiel M, Hogg N (1996). "Leukocyte integrins.". Curr. Opin. Cell Biol. 7 (5): 690–6. doi:10.1016/0955-0674(95)80111-1. PMID 8573344.
Steinman RM, Pack M, Inaba K (1997). "Dendritic cells in the T-cell areas of lymphoid organs.". Immunol. Rev. 156 (1): 25–37. doi:10.1111/j.1600-065X.1997.tb00956.x. PMID 9176697.
Córbi AL, Lopéz-Rodríguez C (1997). "CD11c integrin gene promoter activity during myeloid differentiation.". Leuk. Lymphoma. 25 (5-6): 415–25. doi:10.3109/10428199709039028. PMID 9250811.
Ugarova TP, Yakubenko VP (2001). "Recognition of fibrinogen by leukocyte integrins.". Ann. N. Y. Acad. Sci. 936 (1): 368–85. doi:10.1111/j.1749-6632.2001.tb03523.x. PMID 11460493.
Valentin A, Lundin K, Patarroyo M, Asjö B (1990). "The leukocyte adhesion glycoprotein CD18 participates in HIV-1-induced syncytia formation in monocytoid and T cells.". J. Immunol. 144 (3): 934–7. PMID 1967280.
Gaidano G, Bergui L, Schena M, et al. (1990). "Integrin distribution and cytoskeleton organization in normal and malignant monocytes.". Leukemia. 4 (10): 682–7. PMID 1976870.
Corbi AL, Garcia-Aguilar J, Springer TA (1990). "Genomic structure of an integrin alpha subunit, the leukocyte p150,95 molecule.". J. Biol. Chem. 265 (5): 2782–8. PMID 2303426.
Corbi AL, Larson RS, Kishimoto TK, et al. (1988). "Chromosomal location of the genes encoding the leukocyte adhesion receptors LFA-1, Mac-1 and p150,95. Identification of a gene cluster involved in cell adhesion.". J. Exp. Med. 167 (5): 1597–607. doi:10.1084/jem.167.5.1597. PMC 2188934. PMID 3284962.
Corbi AL, Miller LJ, O'Connor K, et al. (1988). "cDNA cloning and complete primary structure of the alpha subunit of a leukocyte adhesion glycoprotein, p150,95.". EMBO J. 6 (13): 4023–8. PMC 553883. PMID 3327687.
Miller LJ, Wiebe M, Springer TA (1987). "Purification and alpha subunit N-terminal sequences of human Mac-1 and p150,95 leukocyte adhesion proteins.". J. Immunol. 138 (8): 2381–3. PMID 3549901.
Bilsland CA, Diamond MS, Springer TA (1994). "The leukocyte integrin p150,95 (CD11c/CD18) as a receptor for iC3b. Activation by a heterologous beta subunit and localization of a ligand recognition site to the I domain.". J. Immunol. 152 (9): 4582–9. PMID 7512600.
Lecoanet-Henchoz S, Gauchat JF, Aubry JP, et al. (1995). "CD23 regulates monocyte activation through a novel interaction with the adhesion molecules CD11b-CD18 and CD11c-CD18.". Immunity. 3 (1): 119–25. doi:10.1016/1074-7613(95)90164-7. PMID 7621072.
Garcìa-Barcina M, Winnock M, Bidaurrazaga I, et al. (1994). "Detection of cell-adhesion molecules on human liver-associated lymphocytes.". Immunology. 82 (1): 95–8. PMC 1414860. PMID 8045597.
Philippeaux MM, Vesin C, Tacchini-Cottier F, Piguet PF (1996). "Activated human platelets express beta2 integrin.". Eur. J. Haematol. 56 (3): 130–7. doi:10.1111/j.1600-0609.1996.tb01331.x. PMID 8598231.
de Vree WJ, Fontijne-Dorsman AN, Koster JF, Sluiter W (1996). "Photodynamic treatment of human endothelial cells promotes the adherence of neutrophils in vitro.". Br. J. Cancer. 73 (11): 1335–40. doi:10.1038/bjc.1996.255. PMC 2074486. PMID 8645576.
Bernstein CN, Sargent M, Gallatin WM (1998). "Beta2 integrin/ICAM expression in Crohn's disease.". Clin. Immunol. Immunopathol. 86 (2): 147–60. doi:10.1006/clin.1997.4462. PMID 9473377.
Shelley CS, Da Silva N, Georgakis A, et al. (1998). "Mapping of the human CD11c (ITGAX) and CD11d (ITGAD) genes demonstrates that they are arranged in tandem separated by no more than 11.5 kb.". Genomics. 49 (2): 334–6. doi:10.1006/geno.1998.5232. PMID 9598326.

PDB gallery

1n3y: Crystal structure of the alpha-X beta2 integrin I domain

External links

CD11c Antigens at the US National Library of Medicine Medical Subject Headings (MeSH)
Mouse CD Antigen Chart
Human CD Antigen Chart
ITGAX Info with links in the Cell Migration Gateway

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

Proteins: clusters of differentiation (see also list of human clusters of differentiation)

1-50	CD1 a-c 1A 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 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

Cluster of differentiation by lineage

Lymphoid

B cell

plasma cell: CD38
CD138

T/NK

T cell	Pan-T antigens: CD3 CD7 CD1 CD4 CD8 CD13 CD18 CD26 CD27 CD28

NK cell	CD16 CD56/NCAM CD57

All	CD2

All

Myeloid

CFU-GM/
Myelomonocyte

MEP

CFU-Meg	CD34/CD36 CD42 CD41/CD61

CFU-E	CD36 CD71

All (pan-myeloid)

CD13
CD33

Stem cell

CD34

Proteins: complement system (C, L, A)

Activators/enzymes

Early	C: C1Q/C1R/C1S C4 C4a C4b C2 L: MASP1/MASP2 MBL A: Factor B Factor D Factor P/Properdin

Middle	C3 C3a C3b/iC3b C5 C5a C3-convertase C5-convertase

Late	MAC C6 C7 C8 C9

Inhibitors

CL: C4BP

A: Factor H

Complement receptors

Membrane proteins: cell adhesion molecules

Calcium-independent

IgSF CAM	N-CAM (Myelin protein zero) ICAM (1, 5) VCAM-1 PE-CAM L1-CAM Nectin (PVRL1, PVRL2, PVRL3)

Integrins	LFA-1 (CD11a+CD18) Integrin alphaXbeta2 (CD11c+CD18) Macrophage-1 antigen (CD11b+CD18) VLA-4 (CD49d+CD29) Glycoprotein IIb/IIIa (ITGA2B+ITGB3)

Calcium-dependent

Cadherins

Classical	CDH1 CDH2 CDH3

Desmosomal	Desmoglein (DSG1, DSG2, DSG3, DSG4) Desmocollin (DSC1, DSC2, DSC3)

Protocadherin	PCDH1 PCDH15

Unconventional/ungrouped	T-cadherin CDH4 CDH5 CDH6 CDH8 CDH11 CDH12 CDH15 CDH16 CDH17 CDH9 CDH10

Selectins

Other

Integrins

Alpha

Beta

Dimers

Cytoadhesin receptor:	Integrin alpha6beta4 Glycoprotein IIb/IIIa ITGA2B+ITGB3

Fibrinogen receptor:	Macrophage-1 antigen CD11b+CD18

Fibronectin receptor:	Integrin alpha2beta1 Integrin alpha4beta1 Integrin alpha5beta1

Leukocyte-adhesion receptor:	LFA-1 CD11a+CD18 Macrophage-1 antigen CD11b+CD18 Integrin alphaXbeta2 CD11c+CD18

Very late antigen receptor:	Integrin alpha1beta1 Integrin alpha2beta1 Integrin alpha3beta1 VLA-4 CD49d+CD29 Alpha-5 beta-1 Integrin alpha6beta1

Vitronectin receptor:	Alpha-v beta-3 Alpha-v beta-5

see also cell surface receptor deficiencies

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CD11c

See also

References

Further reading

External links