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0FAT2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameFAT2
DescriptionProtocadherin fat 2 precursor (hfat2) (multiple epidermal growth factor-like domains 1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005509 calcium ion binding (NAS)
Domain Architecture (Details)
InterPro domains assigned to SynO:
Laminins are large heterotrimeric glycoproteins involved in basement membrane function . The laminin globular (G) domain can be found in one to several copies in various laminin family members.ncluding a large number of extracellular proteins. The C-terminus of the laminin alpha chain contains a tandem repeat of five laminin G domains.hich are critical for heparin-binding and cell attachment activity . Laminin alpha4 is distributed in a variety of tissues including peripheral nerves.orsal root ganglion.keletal muscle and capillaries; in the neuromuscular junction.t is required for synaptic specialisation . The structure of the laminin-G domain has been predicted to resemble that of pentraxin .Laminin G domains can vary in their function.nd a variety of binding functions have been ascribed to different LamG modules. For example.he laminin alpha1 and alpha2 chains each have five C-teminal laminin G domains.here only domains LG4 and LG5 contain binding sites for heparin.ulphatides and the cell surface receptor dystroglycan . Laminin G-containing proteins appear to have a wide variety of roles in cell adhesion.ignalling.igration.ssembly and differentiation. Proteins with laminin-G domains include:Laminin.Merosin.Agrin.Neurexins.Vitamin K dependent protein S.Sex steroid binding protein SBP/SHBG.Drosophila proteins Slit.rumbs.at.several proteoglycan precursors.
  IPR001791:Laminin G
InterPro domains unassigned to SynO:
Laminins are large heterotrimeric glycoproteins involved in basement membrane function . The laminin globular (G) domain can be found in one to several copies in various laminin family members.ncluding a large number of extracellular proteins. The C-terminus of the laminin alpha chain contains a tandem repeat of five laminin G domains.hich are critical for heparin-binding and cell attachment activity . Laminin alpha4 is distributed in a variety of tissues including peripheral nerves.orsal root ganglion.keletal muscle and capillaries; in the neuromuscular junction.t is required for synaptic specialisation . The structure of the laminin-G domain has been predicted to resemble that of pentraxin . Laminin G domains can vary in their function.nd a variety of binding functions have been ascribed to different LamG modules. For example.he laminin alpha1 and alpha2 chains each have five C-teminal laminin G domains.here only domains LG4 and LG5 contain binding sites for heparin.ulphatides and the cell surface receptor dystroglycan . Laminin G-containing proteins appear to have a wide variety of roles in cell adhesion.ignalling.igration.ssembly and differentiation. This entry represents one subtype of laminin G domains.hich is sometimes found in association with thrombospondin-type laminin G domains ().
  IPR012680:Laminin G, subdomain 2
A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF)has been shown to be present.n a moreor less conserved form.n a large number of other.ostly animal proteins. The list of proteins currently known tocontain one or more copies of an EGF-like pattern is large and varied. The functional significance of EGF domains inwhat appear to be unrelated proteins is not yet clear. However. common feature is that these repeats are found inthe extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandinG/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphidebonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet.Subdomains between the conserved cysteines vary in length.
  IPR006209:EGF-like
Epidermal growth factors and transforming growth factors belong to a general class of proteins that share a repeat pattern involving a number of conserved Cys residues. Growth factors are involved in cell recognition and division . The repeating pattern.specially of cysteines (the so-called EGF repeat).s thought to be important to the 3D structure of the proteins.nd hence its recognition by receptors and other molecules. The type 1 EGF signature includes six conserved cysteines believed to be involved in disulphide bond formation. The EGF motif is found frequently in nature.articularly in extracellular proteins.
  IPR006210:EGF
Cadherins are a family of adhesion molecules that mediate Ca2+-dependent cell-cell adhesion in all solid tissues of the organism which modulate a wide variety of processes including cell polarisation and migration . Cadherin-mediated cell-cell junctions are formed as a result of interaction between extracellular domains of identical cadherins.hich are located on the membranes of the neighbouring cells. The stability of these adhesive junctions is ensured by binding of the intracellular cadherin domain with the actin cytoskeleton. There are a number of different isoforms distributed in a tissue-specific manner in a wide variety of organisms. Cells containing different cadherins tend to segregate in vitro.hile those that contain the same cadherins tend to preferentially aggregate together. This observation is linked to the finding that cadherin expression causes morphological changes involving the positional segregation of cells into layers.uggesting they may play an important role in the sorting of different cell types during morphogenesis.istogenesis and regeneration. They may also be involved in the regulation of tight and gap junctions.nd in the control of intercellular spacing. Cadherins are evolutionary related to the desmogleins which are component of intercellular desmosome junctions involved in the interaction of plaque proteins.Structurally.adherins comprise a number of domains: classically.hese include a signal sequence; a propeptide of around 130 residues; a single transmembrane domain and five tandemly repeated extracellular cadherin domains. of which are cadherin repeats.nd the fifth contains 4 conserved cysteines and a N-terminal cytoplasmic domain . However.roteins are designated as members of the broadly defined cadherin family if they have one or more cadherin repeats. A cadherin repeat is an independently folding sequence of approximately 110 amino acids that contains motifs with the conserved sequences DRE.XNDNAPXF.nd DXD. Crystal structures have revealed that multiple cadherin domains form Ca2+-dependent rod-like structures with a conserved Ca2+-binding pocket at thedomain-domain interface. Cadherins depend on calcium for their function: calcium ions bind to specific residues in each cadherin repeat to ensure its proper folding.o confer rigidity upon the extracellular domain and is essential for cadherin adhesive function and for protection against protease digestion.
  IPR002126:Cadherin
Lectins and glucanases exhibit the common property of reversibly binding to specific complex carbohydrates. The lectins/glucanases are a diverse group of proteins found in a wide range of species from prokaryotes to humans. The different family members all contain a concanavalin A-like domain.hich consists of a sandwich of 12-14 beta strands in two sheets with a complex topology. Members of this family are diverse.nd include the lectins: legume lectins.ereal lectins.iral lectins.nd animal lectins. Plant lectins function in the storage and transport of carbohydrates in seeds.he binding of nitrogen-fixing bacteria to root hairs.he inhibition of fungal growth or insect feeding.nd in hormonally regulated plant growth . Protein members include concanavalin A (Con A).avin.solectin I.ectin IV.oybean agglutinin and lentil lectin. Animal lectins include the galectins.hich are S-type lactose-binding and IgE-binding proteins such as S-lectin.LC protein.alectin1.alectin2.alectin3 CRD.nd Congerin I . Other members with a Con A-like domain include the glucanases and xylanases. Bacterial and fungal beta-glucanases.uch as Bacillus 1-3.-4-beta-glucanse.arry out the acid catalysis of beta-glucans found in microorganisms and plants . Similarly.appa-Carrageenase degrades kappa-carrageenans from marine red algae cell walls . Xylanase and cellobiohydrolase I degrade hemicellulose and cellulose.espectively . There are many Con A-like domains found in proteins involved in cell recognition and adhesion. For example.everal viral and bacterial toxins carry Con A-like domains. Examples include the Clostridium neurotoxins responsible for the neuroparalytic effects of botulism and tetanus . The Pseudomonas exotoxin A. virulence factor which is highly toxic to eukaryotic cells.ausing the arrest of protein synthesis.ontains a Con A-like domain involved in receptor binding . Cholerae neuraminidase can bind to cell surfaces.ossibly through their Con A-like domains.here they function as part of a mucinase complex to degrade the mucin layer of the gastrointestinal tract . The rotaviral outer capsid protein.P4.as a Con A-like sialic acid binding domain.hich functions in cell attachment and membrane penetration . Con A-like domains also play a role in cell recognition in eukaryotes. Proteins containing a Con A-like domain include the sex hormone-binding globulins which transport sex steroids in blood and regulate their access to target tissues .aminins which are large heterotrimeric glycoproteins involved in basement membrane architecture and function .eurexins which are expressed in hundreds of isoforms on the neuronal cell surface.here they may function as cell recognition molecules and sialidases that are found in both microorganisms and animals.nd function in cell adhesion and signal transduction . Other proteins containing a Con A-like domain include pentraxins and calnexins. The pentraxin PTX3 is a TNFalpha-induced.ecreted protein of adipose cells produced during inflammation . The calnexin family of molecular chaperones is conserved among plants.ungi.nd animals. Family members include Calnexin. type-I integral membrane protein in the endoplasmic reticulum which coordinates the processing of newly synthesized N-linked glycoproteins with their productive folding.almegin. type-I membrane protein expressed mainly in the spermatids of the testis.nd calreticulin. soluble ER lumenal paralog .
  IPR008985:Concanavalin A-like lectin/glucanase
Lectins and glucanases exhibit the common property of reversibly binding to specific complex carbohydrates. The lectins/glucanases are a diverse group of proteins found in a wide range of species from prokaryotes to humans. The different family members all contain a concanavalin A-like domain.hich consists of a sandwich of 12-14 beta strands in two sheets with a complex topology. Members of this family are diverse.nd include the lectins: legume lectins.ereal lectins.iral lectins.nd animal lectins. Plant lectins function in the storage and transport of carbohydrates in seeds.he binding of nitrogen-fixing bacteria to root hairs.he inhibition of fungal growth or insect feeding.nd in hormonally regulated plant growth . Protein members include concanavalin A (Con A).avin.solectin I.ectin IV.oybean agglutinin and lentil lectin. Animal lectins include the galectins.hich are S-type lactose-binding and IgE-binding proteins such as S-lectin.LC protein.alectin1.alectin2.alectin3 CRD.nd Congerin I . Other members with a Con A-like domain include the glucanases. Bacterial and fungal beta-glucanases.uch as Bacillus 1-3.-4-beta-glucanse.arry out the acid catalysis of beta-glucans found in microorganisms and plants . Similarly.appa-Carrageenase degrades kappa-carrageenans from marine red algae cell walls . This entry differs from () by omitting the xylanases and glycosyl hydrolases.
  IPR013320:Concanavalin A-like lectin/glucanase, subgroup
IPR002126:CA 
Evalue:-28.2839966563652 
Location:3033-3111IPR002126:CA 
Evalue:-27.7958800173441 
Location:3343-3424IPR002126:Cadherin 
Evalue:-27.4814853668213 
Location:2277-2370IPR002126:CA 
Evalue:-25.6575773191778 
Location:2819-2904IPR012680:Laminin_G_2 
Evalue:-24.7958793640137 
Location:3800-3921IPR002126:Cadherin 
Evalue:-24.6575775146484 
Location:825-916IPR002126:Cadherin 
Evalue:-23.9586067199707 
Location:720-811IPR002126:CA 
Evalue:-23.2218487496164 
Location:1054-1135IPR002126:CA 
Evalue:-22.568636235841 
Location:1159-1240IPR002126:Cadherin 
Evalue:-22.443696975708 
Location:1560-1651IPR002126:Cadherin 
Evalue:-20.9586067199707 
Location:463-537IPR002126:Cadherin 
Evalue:-20.9208183288574 
Location:3431-3522IPR002126:CA 
Evalue:-19.3187587626244 
Location:2503-2583IPR002126:CA 
Evalue:-18.3467874862247 
Location:2928-3009IPR002126:Cadherin 
Evalue:-18.2441253662109 
Location:2075-2164IPR002126:CA 
Evalue:-16.9208187539524 
Location:3135-3216IPR002126:CA 
Evalue:-16.4685210829577 
Location:1787-1870IPR002126:CA 
Evalue:-15.6777807052661 
Location:2190-2270IPR002126:CA 
Evalue:-15.4948500216801 
Location:1682-1756IPR002126:CA 
Evalue:-14.2757241303992 
Location:1990-2068IPR002126:Cadherin 
Evalue:-14.1135091781616 
Location:3223-3312IPR002126:CA 
Evalue:-14.0555173278498 
Location:947-1028IPR002126:CA 
Evalue:-13.698970004336 
Location:1470-1553IPR002126:CA 
Evalue:-13.537602002101 
Location:2713-2795IPR002126:Cadherin 
Evalue:-10.8239088058472 
Location:2384-2472IPR002126:Cadherin 
Evalue:-10.6020603179932 
Location:153-226IPR002126:Cadherin 
Evalue:-10.0268716812134 
Location:1247-1335IPR002126:Cadherin 
Evalue:-7.95860719680786 
Location:569-659IPR002126:Cadherin 
Evalue:-7.30980396270752 
Location:1354-1438IPR002126:Cadherin 
Evalue:-7.18045616149902 
Location:2590-2682IPR006209:EGF 
Evalue:-6.95860719680786 
Location:3990-4021IPR006209:EGF 
Evalue:-6.69896984100342 
Location:3951-3983IPR002126:Cadherin 
Evalue:-5.46852111816406 
Location:3536-3620IPR002126:CA 
Evalue:-2.45593195564972 
Location:380-456IPR002126:CA 
Evalue:-2.20760831050175 
Location:55-146IPR002126:Cadherin 
Evalue:-1.42021644115448 
Location:1877-1959IPR008985:ConA_like_lec_gl 
Evalue:0 
Location:16-28
SequencesProtein: FAT2_HUMAN (4349 aa)
mRNA: NM_001447
Local Annotation
Synapse Ontology
all
sdb:0004 Presynaptic compartment  (Evidence:keywords,domains)
Any process that modulates the physical form of a synapse, the junction between a neuron and a target (neuron, muscle, or secretory cell).
sdb:0033 regulation of synapse structure  (Evidence:keywords,domains)
The formation of a synapse.
sdb:0034 synaptogenesis  (Evidence:keywords,domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 669 residues, 150863846-150865851Exon2: 154 residues, 150866907-150867365Exon3: 53 residues, 150869774-150869928Exon4: 149 residues, 150871918-150872360Exon5: 50 residues, 150877373-150877519Exon6: 272 residues, 150881029-150881840Exon7: 68 residues, 150885521-150885719Exon8: 50 residues, 150886987-150887131Exon9: 48 residues, 150887749-150887887Exon10: 73 residues, 150888931-150889146Exon11: 130 residues, 150891340-150891724Exon12: 80 residues, 150894162-150894396Exon13: 53 residues, 150897546-150897700Exon14: 67 residues, 150900320-150900517Exon15: 1353 residues, 150902038-150906091Exon16: 72 residues, 150909048-150909259Exon17: 96 residues, 150910343-150910625Exon18: 48 residues, 150911220-150911360Exon19: 72 residues, 150912930-150913141Exon20: 106 residues, 150914115-150914427Exon21: 21 residues, 150916097-150916156Exon22: 107 residues, 150923078-150923393Exon23: 1092 residues, 150925426-150928698Exon24: 2 residues, -Jump to FAT2_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4747 151182360-151284596 ~-102K 29808(GLRA1)(-)Loci: 4746 150863846-150928698 ~-65K 29803(FAT2)(-)Link out to UCSC