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0ICAM3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameICAM3
DescriptionIntercellular adhesion molecule 3 precursor (icam-3) (icam-r) (cdw50) (cd50 antigen).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (TAS)
0005886 plasma membrane (NAS)
0005178 integrin binding (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This entry represents the N-terminal domain of intercellular adhesion molecules (ICAM).uch as ICAM-2.CAM-3 and ICAM-4.ICAM-2 (CD102) has two Ig-like domains. It is expressed on endothelial cells.eucocytes and platelets.nd binds to CD11a./CD18. The protein is refractory to proinflammatory cytokines.nd plays an important role in the adhesion of leucocytes to the uninduced endothelium .ICAM-3 (CD50) contains five Ig-like domains and binds to leucocyte integrinsCD11a./CD18. The protein plays an important role in the immune response andperhaps in signal transduction .ICAM-4 (LW blood group Ag) is red blood cell (RBC) specific and binds to CD11a./CD18. It is associated with the RBC Rh antigens and could be important in retaining immature red cells in the bone marrow.r in the uptake of senescent cells into the spleen .ICAM-5 (telencephalin) has nine Ig-like domains and is confined to the telencephalon of the brain. The role of this CD11a/CD18 binding molecule is not yet known .
  IPR013768:Intercellular adhesion molecule, N-terminal
This entry represents domains with an immunoglobulin-like (Ig-like) fold.hich consists of a beta-sandwich of seven or more strands in two sheets with a Greek-key topology. Ig-like domains are one of the most common protein modules found in animals.ccurring in a variety of different proteins. These domains are often involved in interactions.ommonly with other Ig-like domains via their beta-sheets . Domains within this fold-family share the same structure.ut can diverge with respect to their sequence. Based on sequence.g-like domains can be classified as V-set domains (antibody variable domain-like).1-set domains (antibody constant domain-like).2-set domains.nd I-set domains (antibody intermediate domain-like). Proteins can contain more than one of these types of Ig-like domains. For example.n the human T-cell receptor antigen CD2.omain 1 (D1) is a V-set domain.hile domain 2 (D2) is a C2-set domain.oth domains having the same Ig-like fold .Domains with an Ig-like fold can be found in many.iverse proteins in addition to immunoglobulin molecules. For example.g-like domains occur in several different types of receptors (such as various T-cell antigen receptors).everal cell adhesion molecules.HC class I and II antigens.s well as the hemolymph protein hemolin.nd the muscle proteins titin.elokin and twitchin.
  IPR013783:Immunoglobulin-like fold
This entry is for immunoglobulin-like domains. Studies indicate that the interactions essential for defining the structure of these beta sandwich proteins are also important in nucleation of folding.nd that proteins containing this fold may share similar folding pathways even though the proteins may have low sequence homology. The fold consists of a beta-sandwich formed of 7 strands in 2 sheets with a Greek-key topology. Some members of the fold have additional strands. The Pfam alignments do not include the first and last strand of the immunoglobulin-like domain.
  IPR013151:Immunoglobulin
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This subfamily includes:Cell surface receptors containing an immunoglobin domain.Killer cell inhibitory receptors.Oprin a snake venom metalloproteinase inhibitor from Didelphis marsupialis (Southern opossum) .hich belongs to MEROPS inhibitor family I43.lan I- .Oprin homologues.
  IPR003599:Immunoglobulin subtype
Intercellular adhesion molecules (ICAMs) and vascular cell adhesion molecule-1 (VCAM-1) are part of the immunoglobulin superfamily. They areimportant in inflammation.mmune responses and in intracellular signallingevents . The ICAM family consists of five members.esignated ICAM-1 to ICAM-5. They are known to bind to leucocyte integrins CD11/CD18 during inflammation and in immune responses. In addition.CAMs may exist in soluble forms in human plasma.ue to activation and proteolysis mechanisms at cell surfaces. ICAM-1 (CD54) contains five Ig-like domains. It is expressed on leucocytes.ndothelial and epithelial cells.nd is upregulated in response to bacterial invasion. The protein is a ligand for lymphocyte-function associated (LFA) antigens and also a receptor for CD11a./CD18.ibrinogen.uman rhinoviruses and Plasmodium falciparum-infected erythrocytes. ICAM-1 binding sites for CD11a/CD18 and its other binding partners are located in the first domain and are overlapping. ICAM-1 domain 2 seems to play an important role in maintaining the conformation of domain 1 and particularly the structural integrity of the LFA-1 ligand-binding site .The 3-dimensional atomic structure of the tandem N-terminal Ig-like domains (D1 and D2) of ICAM-1 has been determined to 2.2A resolution and fitted intoa cryoelectron microscopy reconstruction of a rhinovirus-ICAM-1 complex . Extensive charge interactions between ICAM-1 and human rhinoviruses are largely conserved in major and minor receptor groups of rhinoviruses. The interaction of ICAMs with LFA-1 is mediated by a divalent cation bound to the insertion (I)-domain on the alpha chain of LFA-1 and the carboxyl group of a conserved glutamic acid residue on ICAMs. This entry represents the N-terminal domain of both intercellular adhesion molecules (ICAM) and of vascular cell adhesion molecules (VCAM).hich are structurally similar.ICAM-2 (CD102) has two Ig-like domains. It is expressed on endothelialcells.eucocytes and platelets.nd binds to CD11a./CD18. The protein isrefractory to proinflammatory cytokines.nd plays an important role in theadhesion of leucocytes to the uninduced endothelium .ICAM-3 (CD50) contains five Ig-like domains and binds to leucocyte integrinsCD11a./CD18. The protein plays an important role in the immune response andperhaps in signal transduction .ICAM-4 (LW blood group Ag) is red blood cell (RBC) specific and binds to CD11a./CD18. It is associated with the RBC Rh antigens and could be important in retaining immature red cells in the bone marrow.r in the uptake of senescent cells into the spleen .ICAM-5 (telencephalin) has nine Ig-like domains and is confined to the telencephalon of the brain. The role of this CD11a/CD18 binding molecule is not yet known .VCAM-1 was first described as a cytokine-inducible endothelial adhesion molecule. It can bind to leucocyte integrin VL-4 (very late antigen-4) to recruit leucocytes to sites of inflammation . The predominant form of VCAM-1 in vivo has an N-terminal extracellular region comprising seven Ig-like domains . A conserved integrin-binding motif has been identified in domains 1 and 4.ariants of which are present in the N-terminal domain of all members of the integrin-binding subgroup of the immunoglobulin superfamily. The structure of a VLA-4-binding fragment comprising the first two domains of VCAM-1 has been determined to 1.8A resolution. The integrin-binding motif is exposed and forms the N-terminal region of the loop between beta-strands C and D of domain 1 . VCAM-1 domains 1 and 2are structurally similar to ICAM-1 and ICAM-2 .
  IPR003987:Intercellular adhesion molecule/vascular cell adhesion molecule, N-terminal
Intercellular adhesion molecules (ICAMs) and vascular cell adhesion molecule-1 (VCAM-1) are part of the immunoglobulin superfamily. They areimportant in inflammation.mmune responses and in intracellular signallingevents . The ICAM family consists of five members.esignated ICAM-1 to ICAM-5. They are known to bind to leucocyte integrins CD11/CD18 during inflammation and in immune responses. In addition.CAMs may exist in soluble forms in human plasma.ue to activation and proteolysis mechanisms at cell surfaces. ICAM-1 (CD54) contains five Ig-like domains. It is expressed on leucocytes.ndothelial and epithelial cells.nd is upregulated in response to bacterial invasion. The protein is a ligand for lymphocyte-function associated (LFA) antigens and also a receptor for CD11a./CD18.ibrinogen.uman rhinoviruses and Plasmodium falciparum-infected erythrocytes. ICAM-1 binding sites for CD11a/CD18 and its other binding partners are located in the first domain and are overlapping. ICAM-1 domain 2 seems to play an important role in maintaining the conformation of domain 1 and particularly the structural integrity of the LFA-1 ligand-binding site .The 3-dimensional atomic structure of the tandem N-terminal Ig-like domains (D1 and D2) of ICAM-1 has been determined to 2.2A resolution and fitted intoa cryoelectron microscopy reconstruction of a rhinovirus-ICAM-1 complex . Extensive charge interactions between ICAM-1 and human rhinoviruses are largely conserved in major and minor receptor groups of rhinoviruses. The interaction of ICAMs with LFA-1 is mediated by a divalent cation bound to the insertion (I)-domain on the alpha chain of LFA-1 and the carboxyl group of a conserved glutamic acid residue on ICAMs. ICAM-2 (CD102) has two Ig-like domains. It is expressed on endothelialcells.eucocytes and platelets.nd binds to CD11a./CD18. The protein isrefractory to proinflammatory cytokines.nd plays an important role in theadhesion of leucocytes to the uninduced endothelium .ICAM-3 (CD50) contains five Ig-like domains and binds to leucocyte integrinsCD11a./CD18. The protein plays an important role in the immune response andperhaps in signal transduction .ICAM-4 (LW blood group Ag) is red blood cell (RBC) specific and binds to CD11a./CD18. It is associated with the RBC Rh antigens and could be important in retaining immature red cells in the bone marrow.r in the uptake of senescent cells into the spleen .ICAM-5 (telencephalin) has nine Ig-like domains and is confined to the telencephalon of the brain. The role of this CD11a/CD18 binding molecule is not yet known .
  IPR003988:Intercellular adhesion molecule
IPR013768:ICAM_N 
Evalue:-69.4814834594727 
Location:12-119IPR013151:ig 
Evalue:-2.40893530845642 
Location:329-377IPR013783:Ig-like_fold 
Evalue:0 
Location:217-312IPR013783:Ig-like_fold 
Evalue:0 
Location:392-481IPR003987:ICAMVCAM1 
Evalue:0 
Location:146-164IPR003988:ICAM 
Evalue:0 
Location:200-216IPR003988:ICAM 
Evalue:0 
Location:126-139
SequencesProtein: ICAM3_HUMAN (547 aa)
mRNA: BC058903 NM_002162
Local Annotation
Synapse Ontology
the formation of new synapse
sdb:0316 synapse formation  (Evidence:keywords)
KO assignmentK06486
  Level 3 annotation:
    intercellular adhesion molecule 3
  Level 2 annotation:
    Cell adhesion molecules (CAMs)
    CD molecules
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 95 residues, 10305453-10305735Exon2: 85 residues, 10305835-10306084Exon3: 87 residues, 10306203-10306458Exon4: 98 residues, 10306741-10307029Exon5: 104 residues, 10307346-10307652Exon6: 91 residues, 10310357-10310624Exon7: 29 residues, 10311214-10311296Exon8: 2 residues, -Jump to ICAM3_HUMANExon1: 95 residues, 10305453-10305735Exon2: 85 residues, 10305835-10306084Exon3: 87 residues, 10306203-10306458Exon4: 98 residues, 10306741-10307029Exon5: 104 residues, 10307346-10307653Exon6: 90 residues, 10310358-10310624Exon7: 30 residues, 10311214-10311300Exon8: 2 residues, -Jump to ICAM3_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4364 10305453-10311300 ~-6K 17970(ICAM3)(-)Loci: 4365 10544347-10558991 ~-15K 17988(AP1M2)(-)Loci: 3088 10689754-10803579 ~-114K 18002(DNM2)(+)Loci: 3089 10843252-10894447 ~-51K 18009(CARM1)(+)Loci: 3090 11061131-11105490 ~-44K 18013(LDLR)(+)Loci: 4366 11296093-11311321 ~-15K 18027(RAB3D)(-)Loci: 4363 9825394-9908070 ~-83K 17941(OLFM2)(-)Link out to UCSC