Q90584 · COHA1_CHICK

  • Protein
    Collagen alpha-1(XVII) chain
  • Gene
    COL17A1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane.
The 120 kDa linear IgA disease antigen homolog is an anchoring filament component involved in dermal-epidermal cohesion.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentbasement membrane
Cellular Componentcollagen trimer
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentextracellular space
Cellular Componenthemidesmosome
Cellular Componentmembrane
Molecular Functionextracellular matrix structural constituent conferring tensile strength
Molecular Functionheparin binding
Biological Processextracellular matrix organization

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      COL17A1
    • Synonyms
      BP180, BPAG2

Organism names

  • Taxonomic identifier
  • Strain
    • Red jungle fowl
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus

Accessions

  • Primary accession
    Q90584

Proteomes

Organism-specific databases

Subcellular Location

Membrane ; Single-pass type II membrane protein
Note: Localized along the plasma membrane of the hemidesmosome.

120 kDa linear IgA disease antigen homolog

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-435Cytoplasmic
Transmembrane436-456Helical; Signal-anchor for type II membrane protein
Topological domain457-1495Extracellular

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00000594091-1495Collagen alpha-1(XVII) chain
ChainPRO_0000342559497-1495120 kDa linear IgA disease antigen homolog
Glycosylation1424N-linked (GlcNAc...) asparagine

Post-translational modification

The intracellular/endo domain is disulfide-linked.
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
The ectodomain is shedded from the surface of keratinocytes resulting in a 120-kDa soluble form, also named as 120 kDa linear IgA disease antigen homolog. The shedding is mediated by membrane-bound metalloproteases (By similarity).

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Cornea specific.

Gene expression databases

Interaction

Subunit

Homotrimers of alpha 1(XVII)chains.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-138Disordered
Region1-535Nonhelical region (NC16)
Compositional bias15-120Polar residues
Region532-824Disordered
Region536-1482Triple-helical region
Compositional bias785-808Pro residues
Region847-999Disordered
Compositional bias853-885Pro residues
Compositional bias900-914Pro residues
Compositional bias945-959Pro residues
Compositional bias980-994Pro residues
Region1160-1185Disordered
Region1201-1226Disordered
Region1251-1278Disordered
Region1295-1336Disordered
Compositional bias1306-1336Polar residues
Region1396-1416Disordered
Region1435-1495Disordered
Compositional bias1469-1488Basic and acidic residues
Region1483-1495Nonhelical region (NC1)

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,495
  • Mass (Da)
    151,204
  • Last updated
    2008-07-01 v2
  • Checksum
    BE8D8BE3A02BCC0F
MDSVTKKTRQDGSEVTERQGGSSSGLKTSSHTGGSGVEKRSYTHSSGYVTSSGSGRLNSSSSGYRQTQSPSSTLTKSPGSTFERKTYVNRHATYEGSSSANSSPEFPRKEFASASTRGRSQSRESEIRVRLQSASPSGRWTELDDVKRLLKGSRSASCSPTRSSSSTLPIPKKAVVETKMVTESSQSVSGTYDTTILNTTLPPYTWSSTLPAGSSLGGYHNSMGQSSSLINAMSHSTGSVFGVPNNLAPSSHALNTGLSTSSTVFGVQNNLSPSSSALNASAASAAYGMKNTSQTNTMNSTGVSASAGGTILSSQGDDFLHKDCKFLLLEKENAPAKKEMELLVMTKDSGKVFSASSTGLNGGSFAEDTLKKEKQGLSSYAADTGLKSDANGGLKSAPTRDKATYAEIQNGGAGGAIGSAPSWCPCGSCCSWWKWLLGLLLAWLLLLGLLFGLIALAEEVRKLKSRVDNLEKINHSFLTVNQGNPYLEKDVSKVDFLHGVAPSSTFPFENEESVWLMVKSRLNKEIERGYFRGERGEPGMKGDMGLQGPKGDRGLPGVPGIPGPVGHQGPEGPKGQKGSMGDPGMEGPMGQRGREGLPGPRGEPGPPGFGEKGDRGAAGPPGPPGPPGSAGLKGPMGSPGPQGPPGPPGLQGFRGEAGLPGAKGEKGATGPPGPKGDQGEKGARGMTGEQGSRGIPGPPGEPGAKGPAGQAGRDGQPGERGEPGLMGMPGARGPPGPSGDTGEPGLTGPQGPPGLPGNPGRPGAKGEPGAPGKVISAEGSSTIALPGPPGPPGPIGPTGPPGVPGPVGPAGLPGQQGPRGEKGSAGEVVIETIKTEVSSLASQMLSDLQGRAGPPGPPGPPGESVQGLPGPRGPPGLPGPSGPPGRPGSSVSTSETFVSGPPGPPGPPGPKGDQGEPGPRGFTGEPGEPGLPGFSSHGGTVTMQGPPGPPGPPGPKGDAGVPGAPGIPGTSRGGSRQIQGPPGPPGPPGPPGPGGSSSQEIQQYVADYLKSDNVRHYLTGVQGPPGPPGPPGILTTADGKNFDFAELATRVMSYVTSSSDHYQSFASSVSTTSVLYQELLNMLQREEIRQYLVGPRGPPGPPGPGVDGMSLSLDYDELTRRFISYLTSSGMSIGLPGPPGPPGTPGISYSELTAYLRNSEFSGLVGPPGPAGPPGPPGIPGSSGISLEDISAYLQSVGYSSISGIQGPPGPPGPPGPPGFSGTGLLSYADITHSDEFRSELIQYLKSDEVRSYISGPPGPPGPRGPPGPKGDSGLVAGSMSSLYHDSLASERLHGGSIGAEGSHGGSLGASSSYGSSMSSSMSSYSASMGSDGSYGASVGSDGSFDGLLTAEESHRRSAGPGRSYSSSFTGSLDYNELARHVSENLQSRGILQDLMSYTGQGPPGPPGPPGPPGISRVFAAYGNVTEDLMDFFRTHGTVRGPPGEKGERGYPGPKGDPGPMGPPGRHGQRGPKGEKGEKGEQMYSGRRRRRSVGV

Sequence caution

The sequence AAA48703.1 differs from that shown. Reason: Frameshift

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias15-120Polar residues
Sequence conflict384in Ref. 2; AAA48703
Sequence conflict617in Ref. 2; AAA48703
Sequence conflict684in Ref. 2; AAA48703
Sequence conflict728in Ref. 2; AAA48703
Compositional bias785-808Pro residues
Sequence conflict826in Ref. 2; AAA48703
Compositional bias853-885Pro residues
Compositional bias900-914Pro residues
Compositional bias945-959Pro residues
Compositional bias980-994Pro residues
Sequence conflict1185in Ref. 2; AAA48703
Sequence conflict1260in Ref. 2; AAA48703
Sequence conflict1264in Ref. 2; AAA48703
Compositional bias1306-1336Polar residues
Sequence conflict1311in Ref. 2; AAA48703
Sequence conflict1463in Ref. 2; AAA48703
Sequence conflict1469in Ref. 2; AAA48703
Compositional bias1469-1488Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M60172
EMBL· GenBank· DDBJ
AAA48703.1
EMBL· GenBank· DDBJ
mRNA Frameshift

Genome annotation databases

Similar Proteins

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