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0COBA1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCOL11A1
DescriptionCollagen alpha 1(xi) chain precursor.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005592 collagen type XI (TAS)
0005578 extracellular matrix (sensu Metazoa) (NAS)
0005201 extracellular matrix structural constituent (NAS)
0030674 protein binding, bridging (NAS)
0001502 cartilage condensation (TAS)
0016337 cell-cell adhesion (NAS)
0030198 extracellular matrix organization and bioge... (NAS)
0007601 visual perception (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 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. Laminin G domains can vary in their function.nd a variety of binding functions has 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 the thrombospondin-type laminin G domain found in various laminins.he N-terminus of thrombospondin (TspN) and pentraxins. Both laminin G and TspN-containing proteins belong to an extensive class of multi-domain adhesive proteins in the matrix that surrounds animal cells.cting as molecular bridges between cells and matrix.nd participating in cell-cell communication . Pentraxins include C-reactive proteins (CRP) and serum amyloid protein (SAP).
  IPR003129:Laminin G, Thrombospondin-type, N-terminal
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
Members of this family belong to the collagen superfamily .Collagens are generally extracellular structural proteinsinvolved in formation of connective tissue structure.The sequence is predominantly repeats of the G-X-Y and the polypeptide chainsform a triple helix. The first position of the repeat isglycine.he second and third positions can be any residuebut are frequently proline and hydroxyproline. Collagensare post-translationally modified by proline hydroxylaseto form the hydroxyproline residues. Defectivehydroxylation is the cause of scurvy.Some members of the collagen superfamily are not involvedin connective tissue structure but share the same triplehelical structure.
  IPR008160:Collagen triple helix repeat
Collagens contain a large number of globular domains in between theregions of triple helical repeats .These domains are involved in binding diverse substrates.One of these domains is found at the C terminus of fibrillar collagens.The exact function of this domain is unknown.
  IPR000885:Fibrillar collagen, C-terminal
Members of this family belong to the collagen superfamily . Collagens are generally extracellular structural proteinsinvolved in formation of connective tissue structure. The sequence is predominantly repeats of the G-X-Y and the polypeptide chainsform a triple helix. The first position of the repeat isglycine.he second and third positions can be any residuebut are frequently proline and hydroxyproline. Collagensare post-translationally modified by proline hydroxylaseto form the hydroxyproline residues. Defectivehydroxylation is the cause of scurvy.Some members of the collagen superfamily are not involvedin connective tissue structure but share the same triplehelical structure.
  IPR008161:Collagen helix repeat
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
IPR000885:COLFI 
Evalue:-144.853866577148 
Location:1593-1804IPR003129:TSPN 
Evalue:-67.9586073148418 
Location:38-229IPR008160:Collagen 
Evalue:-14.3010301589966 
Location:583-642IPR008160:Collagen 
Evalue:-14.0222759246826 
Location:1393-1452IPR008160:Collagen 
Evalue:-13.9208183288574 
Location:883-942IPR008160:Collagen 
Evalue:-13.5850267410278 
Location:751-810IPR008160:Collagen 
Evalue:-13.180456161499 
Location:1462-1521IPR008160:Collagen 
Evalue:-12.3098039627075 
Location:643-702IPR008160:Collagen 
Evalue:-12.08092212677 
Location:1066-1125IPR008160:Collagen 
Evalue:-12.0043649673462 
Location:811-870IPR008160:Collagen 
Evalue:-11.8239088058472 
Location:982-1037IPR008160:Collagen 
Evalue:-11.3372421264648 
Location:1156-1215IPR008160:Collagen 
Evalue:-10.8538722991943 
Location:1333-1392IPR008160:Collagen 
Evalue:-10.8239088058472 
Location:1246-1305IPR008160:Collagen 
Evalue:-7.82390880584717 
Location:528-579IPR008160:Collagen 
Evalue:-7.63827228546143 
Location:442-490IPR008160:Collagen 
Evalue:-2.92081880569458 
Location:1522-1542IPR008161:Clg_helix 
Evalue:0 
Location:298-330IPR008161:Clg_helix 
Evalue:0 
Location:265-297
SequencesProtein: COBA1_HUMAN (1806 aa)
mRNA: NM_001854
Local Annotation
Synapse Ontology
A neuromuscular junction is the junction of the axon terminal of a motoneuron with the motor end plate, the highly-excitable region of muscle fiber plasma membrane responsible for initiation of action potentials across the muscle's surface.
sdb:0024 neuromuscular junction  (Evidence:domains)
KO assignmentK06236
  Level 3 annotation:
    collagen, type I/II/III/V/XI, alpha
  Level 2 annotation:
    ECM-receptor interaction
    CAM ligands
    Focal adhesion
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 243 residues, 103115582-103116309Exon2: 80 residues, 103117826-103118060Exon3: 25 residues, 103119840-103119909Exon4: 39 residues, 103121342-103121455Exon5: 85 residues, 103124950-103125200Exon6: 20 residues, 103126720-103126774Exon7: 14 residues, 103126866-103126902Exon8: 20 residues, 103127009-103127063Exon9: 38 residues, 103127598-103127706Exon10: 20 residues, 103128594-103128648Exon11: 20 residues, 103136268-103136322Exon12: 38 residues, 103136809-103136917Exon13: 20 residues, 103137084-103137138Exon14: 20 residues, 103150302-103150356Exon15: 20 residues, 103151780-103151834Exon16: 20 residues, 103152495-103152549Exon17: 38 residues, 103152847-103152955Exon18: 20 residues, 103153774-103153828Exon19: 20 residues, 103158454-103158508Exon20: 20 residues, 103159661-103159715Exon21: 20 residues, 103161479-103161533Exon22: 38 residues, 103172592-103172700Exon23: 20 residues, 103173203-103173257Exon24: 20 residues, 103177178-103177232Exon25: 38 residues, 103178470-103178578Exon26: 38 residues, 103184992-103185100Exon27: 20 residues, 103200009-103200063Exon28: 32 residues, 103200319-103200409Exon29: 38 residues, 103200796-103200904Exon30: 20 residues, 103203630-103203684Exon31: 20 residues, 103208362-103208416Exon32: 20 residues, 103212973-103213027Exon33: 17 residues, 103216851-103216896Exon34: 20 residues, 103217003-103217057Exon35: 17 residues, 103217203-103217248Exon36: 20 residues, 103217525-103217579Exon37: 20 residues, 103222281-103222335Exon38: 38 residues, 103225776-103225884Exon39: 20 residues, 103227661-103227715Exon40: 17 residues, 103234007-103234052Exon41: 20 residues, 103234132-103234186Exon42: 17 residues, 103235223-103235268Exon43: 20 residues, 103236453-103236507Exon44: 17 residues, 103240068-103240113Exon45: 20 residues, 103240571-103240625Exon46: 17 residues, 103240890-103240935Exon47: 20 residues, 103241358-103241412Exon48: 17 residues, 103242587-103242632Exon49: 20 residues, 103242751-103242805Exon50: 20 residues, 103243981-103244035Exon51: 20 residues, 103244211-103244265Exon52: 20 residues, 103244405-103244459Exon53: 20 residues, 103246606-103246660Exon54: 21 residues, 103250556-103250613Exon55: 30 residues, 103252654-103252738Exon56: 27 residues, 103253811-103253886Exon57: 23 residues, 103255963-103256026Exon58: 16 residues, 103256961-103257003Exon59: 23 residues, 103259850-103259913Exon60: 87 residues, 103260885-103261140Exon61: 33 residues, 103263664-103263757Exon62: 41 residues, 103264359-103264476Exon63: 45 residues, 103269259-103269388Exon64: 56 residues, 103312761-103312924Exon65: 73 residues, 103316801-103317015Exon66: 58 residues, 103320948-103321116Exon67: 143 residues, 103346216-103346640Exon68: 2 residues, -Jump to COBA1_HUMAN  
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