Detail Information for IndEnz0002015298
IED ID IndEnz0002015298
Enzyme Type ID protease015298
Protein Name Intercellular adhesion molecule 2
ICAM-2
CD antigen CD102
Gene Name ICAM2
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MSSFGYRTLTVALFTLICCPGSDEKVFEVHVRPKKLAVEPKGSLEVNCSTTCNQPEVGGLETSLDKILLDEQAQWKHYLVSNISHDTVLQCHFTCSGKQESMNSNVSVYQPPRQVILTLQPTLVAVGKSFTIECRVPTVEPLDSLTLFLFRGNETLHYETFGKAAPAPQEATATFNSTADREDGHRNFSCLAVLDLMSRGGNIFHKHSAPKMLEIYEPVSDSQMVIIVTVVSVLLSLFVTSVLLCFIFGQHLRQQRMGTYGVRAAWRRLPQAFRP
Enzyme Length 275
Uniprot Accession Number P13598
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). ICAM2 may 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.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (15); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (6); Helix (3); Natural variant (3); Region (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords 3D-structure;Cell adhesion;Cell projection;Direct protein sequencing;Disulfide bond;Glycoprotein;Immunoglobulin domain;Membrane;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, microvillus {ECO:0000250|UniProtKB:P35330}. Note=Co-localizes with RDX, EZR and MSN in microvilli. {ECO:0000250|UniProtKB:P35330}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..24; /evidence=ECO:0000269|PubMed:19892738
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1ZXQ;
Mapped Pubmed ID 11017109; 11857637; 12097408; 14970226; 15545280; 15548573; 16857989; 16987074; 17059578; 17609265; 18155766; 18768213; 18842965; 18978946; 19175829; 19423540; 19524015; 20237496; 20406964; 20438785; 20711500; 20955708; 21656680; 22190034; 22645275; 23591197; 23714211; 24457076; 24474251; 24704826; 26377944; 26641849; 27556181; 27592383; 29671117; 34484188; 8995416;
Motif
Gene Encoded By
Mass 30,654
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda