ICAM2

ICAM2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1ZXQ
Identifiers
Aliases	ICAM2, CD102, intercellular adhesion molecule 2
External IDs	OMIM: 146630 MGI: 96394 HomoloGene: 675 GeneCards: ICAM2
Gene location (Human)
Chr.	Chromosome 17 (human)
End	64,020,634 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	106,278,901 bp
RNA expression pattern
	Top expressed in
	spleen; ; vena cava; ; pericardium; ; right lung; ; upper lobe of lung; ; upper lobe of left lung; ; abdominal fat; ; lower lobe of lung; ; blood; ; monocyte;
	Top expressed in
	right lung lobe; ; left lung; ; left lung lobe; ; thymus; ; endocardial cushion; ; atrioventricular valve; ; carotid body; ; dermis; ; external carotid artery; ; renal corpuscle;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	integrin binding;
Cellular component	integral component of membrane; plasma membrane; uropod; extracellular exosome; membrane; cell periphery; integral component of plasma membrane; cleavage furrow; microvillus; cell projection;
Biological process	cell adhesion; stimulatory C-type lectin receptor signaling pathway; extracellular matrix organization; regulation of immune response; cell-cell adhesion;
	Sources:Amigo / QuickGO
Orthologs
	3384
	15896
	ENSG00000108622
	ENSMUSG00000001029
	P13598
	P35330
	NM_001099789; NM_000873; NM_001099786; NM_001099787; NM_001099788
	NM_010494
	NP_000864; NP_001093256; NP_001093257; NP_001093258; NP_001093259
	NP_034624
	Wikidata
View/Edit Human	View/Edit Mouse

Intercellular adhesion molecule 2 (ICAM2), also known as CD102 (Cluster of Differentiation 102), is a human gene, and the protein resulting from it.

Protein structure

The protein encoded by this gene is a member of the intercellular adhesion molecule (ICAM) family. All ICAM proteins are type I transmembrane glycoproteins, contain 2–9 immunoglobulin-like C2-type domains, and bind to the leukocyte adhesion LFA-1 protein.

Protein functions

ICAM-2 molecules regulate spermatid adhesion on Sertoli cell on the apical side of the blood-testis barrier (towards the lumen), thus playing a major role in spermatogenesis.^[5]

This protein may also play a role in lymphocyte recirculation by blocking LFA-1-dependent cell adhesion. It mediates adhesive interactions important for antigen-specific immune response, NK-cell mediated clearance, lymphocyte recirculation, and other cellular interactions important for immune response and surveillance.^[6]

Interactions

ICAM2 has been shown to interact with EZR.^[7] It has also been shown to bind to P9 (Uniprot: B2UM07), a secreted protein from Akkermansia muciniphila.^[8]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000108622 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000001029 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Xiao X, Mruk DD, Cheng CY (2013). "Intercellular adhesion molecules (ICAMs) and spermatogenesis". Human Reproduction Update. 19 (2): 167–86. doi:10.1093/humupd/dms049. PMC 3576004. PMID 23287428.
↑ "Entrez Gene: ICAM2 intercellular adhesion molecule 2".
↑ Heiska L, Alfthan K, Grönholm M, Vilja P, Vaheri A, Carpén O (August 1998). "Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4, 5-bisphosphate". The Journal of Biological Chemistry. 273 (34): 21893–900. doi:10.1074/jbc.273.34.21893. PMID 9705328.
↑ Yoon HS, Cho CH, Yun MS, Jang SJ, You HJ, Kim JH, Han D, Cha KH, Moon SH, Lee K, Kim YJ, Lee SJ, Nam TW, Ko G (May 2021). "Akkermansia muciniphila secretes a glucagon-like peptide-1-inducing protein that improves glucose homeostasis and ameliorates metabolic disease in mice". Nature Microbiology. 6 (5): 563–573. doi:10.1038/s41564-021-00880-5. PMID 33820962. S2CID 233037565.

Simmons DL (1995). "The role of ICAM expression in immunity and disease". Cancer Surveys. 24: 141–55. PMID 7553659.
Hayflick JS, Kilgannon P, Gallatin WM (1998). "The intercellular adhesion molecule (ICAM) family of proteins. New members and novel functions". Immunologic Research. 17 (3): 313–27. doi:10.1007/BF02786454. PMID 9638475. S2CID 19901365.
Lalor PF, Shields P, Grant A, Adams DH (February 2002). "Recruitment of lymphocytes to the human liver". Immunology and Cell Biology. 80 (1): 52–64. doi:10.1046/j.1440-1711.2002.01062.x. PMID 11869363. S2CID 19892941.
Yonekawa K, Harlan JM (February 2005). "Targeting leukocyte integrins in human diseases". Journal of Leukocyte Biology. 77 (2): 129–40. doi:10.1189/jlb.0804460. PMID 15548573. S2CID 44606865.
de Fougerolles AR, Stacker SA, Schwarting R, Springer TA (July 1991). "Characterization of ICAM-2 and evidence for a third counter-receptor for LFA-1". The Journal of Experimental Medicine. 174 (1): 253–67. doi:10.1084/jem.174.1.253. PMC 2118873. PMID 1676048.
Sansom D, Borrow J, Solomon E, Trowsdale J (October 1991). "The human ICAM2 gene maps to 17q23-25". Genomics. 11 (2): 462–4. doi:10.1016/0888-7543(91)90157-A. PMID 1769660.
Staunton DE, Dustin ML, Springer TA (May 1989). "Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1 homologous to ICAM-1". Nature. 339 (6219): 61–4. Bibcode:1989Natur.339...61S. doi:10.1038/339061a0. PMID 2497351. S2CID 4326657.
Bujía J, Holly A, Kim C, Scanady N, Kastenbauer E (1994). "Expression of human intercellular adhesion molecules in middle ear cholesteatoma". American Journal of Otolaryngology. 15 (4): 271–5. doi:10.1016/0196-0709(94)90094-9. PMID 7526720.
de Fougerolles AR, Qin X, Springer TA (February 1994). "Characterization of the function of intercellular adhesion molecule (ICAM)-3 and comparison with ICAM-1 and ICAM-2 in immune responses". The Journal of Experimental Medicine. 179 (2): 619–29. doi:10.1084/jem.179.2.619. PMC 2191386. PMID 7905020.
Butini L, De Fougerolles AR, Vaccarezza M, Graziosi C, Cohen DI, Montroni M, Springer TA, Pantaleo G, Fauci AS (September 1994). "Intercellular adhesion molecules (ICAM)-1 ICAM-2 and ICAM-3 function as counter-receptors for lymphocyte function-associated molecule 1 in human immunodeficiency virus-mediated syncytia formation". European Journal of Immunology. 24 (9): 2191–5. doi:10.1002/eji.1830240939. PMID 7916296. S2CID 24872330.
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Hirao M, Sato N, Kondo T, Yonemura S, Monden M, Sasaki T, Takai Y, Tsukita S, Tsukita S (October 1996). "Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway". The Journal of Cell Biology. 135 (1): 37–51. doi:10.1083/jcb.135.1.37. PMC 2121020. PMID 8858161.
Bernstein CN, Sargent M, Gallatin WM, Wilkins J (October 1996). "Beta 2-integrin/intercellular adhesion molecule (ICAM) expression in the normal human intestine". Clinical and Experimental Immunology. 106 (1): 160–9. PMID 8870715.
Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Casasnovas JM, Springer TA, Liu JH, Harrison SC, Wang JH (May 1997). "Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface". Nature. 387 (6630): 312–5. Bibcode:1997Natur.387..312C. doi:10.1038/387312a0. PMID 9153399. S2CID 4276760.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Sainio M, Zhao F, Heiska L, Turunen O, den Bakker M, Zwarthoff E, Lutchman M, Rouleau GA, Jääskeläinen J, Vaheri A, Carpén O (September 1997). "Neurofibromatosis 2 tumor suppressor protein colocalizes with ezrin and CD44 and associates with actin-containing cytoskeleton". Journal of Cell Science. 110. 110 (18): 2249–60. doi:10.1242/jcs.110.18.2249. PMID 9378774.
Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S, Tsukita S (February 1998). "Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2". The Journal of Cell Biology. 140 (4): 885–95. doi:10.1083/jcb.140.4.885. PMC 2141743. PMID 9472040.
Bernstein CN, Sargent M, Gallatin WM (February 1998). "Beta2 integrin/ICAM expression in Crohn's disease". Clinical Immunology and Immunopathology. 86 (2): 147–60. doi:10.1006/clin.1997.4462. PMID 9473377.

External links

ICAM2+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
PDBe-KB provides an overview of all the structure information available in the PDB for Human Intercellular adhesion molecule 2 (ICAM2)

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

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000108622 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000001029 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[xiao2013-5] Xiao X, Mruk DD, Cheng CY (2013). "Intercellular adhesion molecules (ICAMs) and spermatogenesis". Human Reproduction Update. 19 (2): 167–86. doi:10.1093/humupd/dms049. PMC 3576004. PMID 23287428.

[entrez-6] "Entrez Gene: ICAM2 intercellular adhesion molecule 2".

[pmid9705328-7] Heiska L, Alfthan K, Grönholm M, Vilja P, Vaheri A, Carpén O (August 1998). "Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4, 5-bisphosphate". The Journal of Biological Chemistry. 273 (34): 21893–900. doi:10.1074/jbc.273.34.21893. PMID 9705328.

[pmid33820962-8] Yoon HS, Cho CH, Yun MS, Jang SJ, You HJ, Kim JH, Han D, Cha KH, Moon SH, Lee K, Kim YJ, Lee SJ, Nam TW, Ko G (May 2021). "Akkermansia muciniphila secretes a glucagon-like peptide-1-inducing protein that improves glucose homeostasis and ameliorates metabolic disease in mice". Nature Microbiology. 6 (5): 563–573. doi:10.1038/s41564-021-00880-5. PMID 33820962. S2CID 233037565.

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[3]

[4]

[5]

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[8]

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

Protein structure

Protein functions

Interactions

See also

References

Further reading

External links