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0ITA4_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameITGA4
DescriptionIntegrin alpha-4 precursor (integrin alpha-iv) (vla-4) (cd49d).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This domain is found in integrin alpha and integrin alpha precursors to the C terminus of a number of repeats and to the N terminus of the cytoplasmic region.
  IPR013649:Integrin alpha-2
Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.
  IPR013519:Integrin alpha beta-propellor
This region contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure . The repeat is called the FG-GAP repeat after two conserved motifs in the repeat . The FG-GAP repeats are found in the N terminus of integrin alpha chains. region that has been shown to be important for ligand binding . A putative Ca2+ binding motif is found in some of the repeats.
  IPR013517:FG-GAP
Some alpha subunits are cleaved post-translationally to produce a heavy and a light chain linked by a disulphidebond . Integrin alpha chains share a conserved sequence which is found atthe beginning of the cytoplasmic domain.ust after the end of thetransmembrane region. Within the N-terminal domain of alpha subunits.even sequence repeats.achof approximately 60 amino acids.ave been found . It has been predicted that these repeats assume the beta-propeller fold. The domains contain seven four-stranded beta-sheets arranged in a torus around a pseudosymmetry axis. Integrin ligands and a putative Mg2+ ion are predicted to bind to theupper face of the propeller.n a manner analogous to the way in which thetrimeric G-protein beta subunit (G beta) (which also has a beta-propellerfold) binds the G protein alpha subunit .Integrin cytoplasmic domains are normally less than 50 amino acids in length.ith the beta-subunit sequences exhibiting greater homology to each other than the alpha-subunit sequences . This is consistent with current evidence that the beta subunit is the principal site for binding of cytoskeletal and signalling molecules.hereas the alpha subunit has a regulatory role. The first ten residues of the alpha-subunit cytoplasmic domain appear to form an alpha helix that is terminated by a proline residue. The remainder of the domain is highly acidic in nature and this loops back to contact the membrane-proximal lysine anchor residue.
  IPR013513:Integrin alpha chain, C-terminal cytoplasmic region
Integrins are the major metazoan receptors for cell adhesion to extracellular matrix proteins and.n vertebrates.lso play important roles in certain cell-cell adhesions.ake transmembrane connections to the cytoskeleton and activate many intracellular signaling pathways . Integrins are alpha-beta heterodimers; each subunit crosses the membrane once.ith most of the polypeptide in the extracellular space.nd has two short cytoplasmic domains. Most integrins recognise relatively short peptide motifs.nd in general require an acidic amino acid to be present. Ligand specificity depends on both the alpha and beta subunits. Many integrins are expressed on cell surfaces in an inactive state in which they do not bind ligands and do not signal. Integrins frequently intercommunicate and the engagement of one may lead to the activation or inhibition of another. The structure of unliganded alphaV beta3 showed the molecule to be folded.ith the head bent over towards the C termini of the legs which would normally be inserted into the membrane. The head comprises a beta propeller domain at the end terminus of the alphaV subunit and an I/A domain inserted into a loop on the top of the hybrid domain in the beta subunit. The I/A domain consists of a Rossman fold with a core of beta parallel sheets surrounded by amphipathic alpha helices. Some alpha subunits are cleaved post-translationally to produce a heavy and a light chain linked by a disulphidebond . Integrin alpha chains share a conserved sequence which is found atthe beginning of the cytoplasmic domain.ust after the end of thetransmembrane region. Within the N-terminal domain of alpha subunits.even sequence repeats.achof approximately 60 amino acids.ave been found . It has been predicted that these repeats assume the beta-propeller fold. The domains contain seven four-stranded beta-sheets arranged in a torus around a pseudosymmetry axis. Integrin ligands and a putative Mg2+ ion are predicted to bind to theupper face of the propeller.n a manner analogous to the way in which thetrimeric G-protein beta subunit (G beta) (which also has a beta-propellerfold) binds the G protein alpha subunit .Integrin cytoplasmic domains are normally less than 50 amino acids in length.ith the beta-subunit sequences exhibiting greater homology to each other than the alpha-subunit sequences . This is consistent with current evidence that the beta subunit is the principal site for binding of cytoskeletal and signalling molecules.hereas the alpha subunit has a regulatory role. The first ten residues of the alpha-subunit cytoplasmic domain appear to form an alpha helix that is terminated by a proline residue. The remainder of the domain is highly acidic in nature and this loops back to contact the membrane-proximal lysine anchor residue.
  IPR000413:Integrins alpha chain
IPR013649:Integrin_alpha2 
Evalue:-145.045761108398 
Location:469-908IPR013519:Int_alpha 
Evalue:-14.602059991328 
Location:370-425IPR013519:Int_alpha 
Evalue:-11.568636235841 
Location:308-364IPR013519:Int_alpha 
Evalue:-6.92081875395237 
Location:54-114IPR013519:Int_alpha 
Evalue:-4.4089353929735 
Location:253-306IPR013513:Integrin_alpha 
Evalue:-3.14266753196716 
Location:1007-1021IPR000413:INTEGRINA 
Evalue:0 
Location:436-457
SequencesProtein: ITA4_HUMAN (1038 aa)
mRNA: NM_000885
Local Annotation
Synapse Ontology
A process that increases long-term neuronal synaptic plasticity, the ability of neuronal synapses to change long-term as circumstances require. Long-term neuronal synaptic plasticity generally involves increase or decrease in actual synapse numbers.
sdb:0039 positive regulation of long-term neuronal synaptic plasticity  (Evidence:keywords)
KO assignmentK06483
  Level 3 annotation:
    integrin alpha 4
  Level 2 annotation:
    ECM-receptor interaction
    Cell adhesion molecules (CAMs)
    CD molecules
    Regulation of actin cytoskeleton
    Focal adhesion
    Hematopoietic cell lineage
    Leukocyte transendothelial migration
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 321 residues, 182029863-182030823Exon2: 42 residues, 182031167-182031289Exon3: 37 residues, 182047931-182048038Exon4: 45 residues, 182048130-182048260Exon5: 24 residues, 182051728-182051796Exon6: 45 residues, 182053108-182053238Exon7: 30 residues, 182054569-182054655Exon8: 23 residues, 182055331-182055394Exon9: 48 residues, 182055485-182055623Exon10: 39 residues, 182058852-182058964Exon11: 33 residues, 182066296-182066391Exon12: 32 residues, 182067693-182067784Exon13: 17 residues, 182068342-182068388Exon14: 53 residues, 182068754-182068909Exon15: 53 residues, 182071594-182071749Exon16: 52 residues, 182082629-182082779Exon17: 27 residues, 182084670-182084747Exon18: 52 residues, 182095162-182095313Exon19: 34 residues, 182096408-182096504Exon20: 28 residues, 182097142-182097222Exon21: 32 residues, 182098173-182098263Exon22: 32 residues, 182100268-182100359Exon23: 38 residues, 182102512-182102620Exon24: 44 residues, 182103495-182103621Exon25: 42 residues, 182104628-182104748Exon26: 35 residues, 182107243-182107342Exon27: 42 residues, 182107787-182107907Exon28: 771 residues, 182108403-182110711Exon29: 2 residues, -Jump to ITA4_HUMAN  
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