Q02388 · CO7A1_HUMAN

  • Protein
    Collagen alpha-1(VII) chain
  • Gene
    COL7A1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Stratified squamous epithelial basement membrane protein that forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence by interacting with extracellular matrix (ECM) proteins such as type IV collagen.

Features

Showing features for site.

129442004006008001,0001,2001,4001,6001,8002,0002,2002,4002,6002,800
TypeIDPosition(s)Description
Site2886-2887Reactive bond

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 type VII trimer
Cellular Componentcollagen-containing extracellular matrix
Cellular ComponentCOPII-coated ER to Golgi transport vesicle
Cellular Componentendoplasmic reticulum lumen
Cellular Componentendoplasmic reticulum-Golgi intermediate compartment membrane
Cellular Componentextracellular region
Cellular Componentextracellular space
Molecular Functionextracellular matrix structural constituent conferring tensile strength
Molecular Functionserine-type endopeptidase inhibitor activity
Biological Processcell adhesion
Biological Processendodermal cell differentiation
Biological Processepidermis development
Biological Processextracellular matrix organization

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Collagen alpha-1(VII) chain
  • Alternative names
    • Long-chain collagen (LC collagen)

Gene names

    • Name
      COL7A1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q02388
  • Secondary accessions
    • Q14054
    • Q16507

Proteomes

Organism-specific databases

Disease & Variants

Involvement in disease

  • Epidermolysis bullosa acquisita (EBA) is an autoimmune acquired blistering skin disease resulting from autoantibodies to type VII collagen

Epidermolysis bullosa dystrophica, autosomal dominant (DDEB)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A group of autosomal dominant blistering skin diseases characterized by tissue separation which occurs below the dermal-epidermal basement membrane at the level of the anchoring fibrils. Various clinical types with different severity are recognized, ranging from severe mutilating forms to mild forms with limited and localized scarring, and less frequent extracutaneous manifestations.
  • See also
    MIM:131750
Natural variants in DDEB
Variant IDPosition(s)ChangeDescription
VAR_0111621522G>Ein DDEB; dbSNP:rs387906605
VAR_0018121557G>Rin DDEB
VAR_0111671776G>Rin DDEB
VAR_0018152003G>Rin DDEB; dbSNP:rs121912832
VAR_0111702006G>Ain DDEB
VAR_0111712006G>Din DDEB; interferes with collagen VII folding and secretion; dbSNP:rs121912842
VAR_0111742015G>Ein DDEB; interferes with collagen VII folding and secretion; dbSNP:rs121912843
VAR_0111752028G>Ain DDEB
VAR_0111762028G>Rin DDEB and EBP; dbSNP:rs762162799
VAR_0018182034G>Rin DDEB and EBDSC; interferes with collagen VII folding and secretion; dbSNP:rs121912844
VAR_0111782034G>Win DDEB
VAR_0111792037G>Ein DDEB; dbSNP:rs121912846
VAR_0111802040G>Din DDEB
VAR_0018192040G>Sin DDEB; dbSNP:rs121912829
VAR_0111812040G>Vin DDEB
VAR_0018202043G>Rin DDEB; dbSNP:rs121912836
VAR_0111822043G>Win DDEB; localized type; dbSNP:rs121912836
VAR_0111832046G>Vin DDEB
VAR_0018222055G>Ein DDEB; dbSNP:rs1553854678
VAR_0111842064G>Rin DDEB; dbSNP:rs866061439
VAR_0649972070G>Rin DDEB
VAR_0018262076G>Din DDEB; also in recessive forms; dbSNP:rs121912850
VAR_0018272079G>Ein DDEB
VAR_0111852079G>Rin DDEB
VAR_0111882207G>Rin DDEB
VAR_0111972713G>Din DDEB; dbSNP:rs369591910
VAR_0112012791R>Win DDEB; dbSNP:rs142566193

Epidermolysis bullosa dystrophica, autosomal recessive (RDEB)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A group of autosomal recessive blistering skin diseases characterized by tissue separation which occurs below the dermal-epidermal basement membrane at the level of the anchoring fibrils. Various clinical types with different severity are recognized, ranging from severe mutilating forms, such as epidermolysis bullosa dystrophica Hallopeau-Siemens type, to mild forms with limited localized scarring and less frequent extracutaneous manifestations. Mild forms include epidermolysis bullosa mitis and epidermolysis bullosa localisata.
  • See also
    MIM:226600
Natural variants in RDEB
Variant IDPosition(s)ChangeDescription
VAR_001809142K>Rin RDEB; uncertain significance; may affect exon 3 splicing; dbSNP:rs121912856
VAR_0111601347G>Rin RDEB; localized type; mild; dbSNP:rs121912833
VAR_0111631604G>Rin RDEB; dbSNP:rs1560234201
VAR_0111641652G>Rin RDEB; mitis type; dbSNP:rs1439299333
VAR_0111651703G>Ein RDEB; dbSNP:rs770304825
VAR_0111661772R>Win RDEB; dbSNP:rs1032335328
VAR_0018131782G>Rin RDEB; mitis type; dbSNP:rs374718902
VAR_0111691812G>Rin RDEB
VAR_0649941845G>Rin RDEB
VAR_0649951981K>Rin RDEB; mild form
VAR_0018141982G>Win RDEB
VAR_0111722008R>Cin RDEB; dbSNP:rs1055680335
VAR_0018162008R>Gin RDEB; dbSNP:rs1055680335
VAR_0111732009G>Rin RDEB
VAR_0018172025G>Ain RDEB; mitis type; dbSNP:rs766931219
VAR_0111772031G>Sin RDEB; severe phenotype; dbSNP:rs121912838
VAR_0018212049G>Ein RDEB
VAR_0018232063R>Win RDEB; dbSNP:rs121912849
VAR_0649962069R>Cin RDEB; dbSNP:rs121912855
VAR_0018252073G>Din RDEB; mitis type
VAR_0111862132G>Din RDEB; dbSNP:rs755669902
VAR_0111872192G>Sin RDEB
VAR_0649982221G>Ain RDEB
VAR_0111902263G>Vin RDEB
VAR_0111912287G>Rin RDEB; also found in isolated toenail dystrophy; dbSNP:rs121912839
VAR_0649992296G>Ein RDEB
VAR_0111922316G>Rin RDEB
VAR_0111942366G>Sin RDEB; mitis type; dbSNP:rs1560204600
VAR_0650002557G>Rin RDEB
VAR_0018302569G>Rin RDEB; severe and mitis type
VAR_0018312575G>Rin RDEB; dbSNP:rs760891216
VAR_0650012622R>Win RDEB; dbSNP:rs139318843
VAR_0018332653G>Rin RDEB; mitis type; dbSNP:rs121912851
VAR_0018342671G>Vin RDEB
VAR_0111962674G>Din RDEB
VAR_0018352674G>Rin RDEB; mitis type
VAR_0111992740G>Ain RDEB
VAR_0018362749G>Rin RDEB; dbSNP:rs121912853
VAR_0112002775G>Sin RDEB; mitis type; dbSNP:rs1333259313
VAR_0018372798M>Kin RDEB; dbSNP:rs121912828

Transient bullous dermolysis of the newborn (TBDN)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    TBDN is a neonatal form of dystrophic epidermolysis bullosa characterized by sub-epidermal blisters, reduced or abnormal anchoring fibrils at the dermo-epidermal junction, and electron-dense inclusions in keratinocytes. TBDN heals spontaneously or strongly improves within the first months and years of life.
  • See also
    MIM:131705
Natural variants in TBDN
Variant IDPosition(s)ChangeDescription
VAR_0111611519G>Din TBDN; dbSNP:rs121912835
VAR_0111892251G>Ein TBDN; also found in isolated toenail dystrophy; dbSNP:rs121912834

Epidermolysis bullosa dystrophica, pretibial type (PR-DEB)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A form of dystrophic epidermolysis bullosa characterized by pretibial blisters that develop into prurigo-like hyperkeratotic lesions. It predominantly affects the pretibial areas, sparing the knees and other parts of the skin. Other clinical features include nail dystrophy, albopapuloid skin lesions, and hypertrophic scars without pretibial predominance. The phenotype shows considerable interindividual variability. Inheritance is autosomal dominant.
  • See also
    MIM:131850
Natural variants in PR-DEB
Variant IDPosition(s)ChangeDescription
VAR_0018322623G>Cin PR-DEB; dominant; dbSNP:rs121912831

Epidermolysis bullosa dystrophica, Bart type (B-DEB)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    An autosomal dominant form of dystrophic epidermolysis bullosa characterized by congenital localized absence of skin, skin fragility and deformity of nails.
  • See also
    MIM:132000

Epidermolysis bullosa pruriginosa (EBP)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A distinct clinical subtype of epidermolysis bullosa dystrophica. It is characterized by skin fragility, blistering, scar formation, intense pruritus and excoriated prurigo nodules. Onset is in early childhood, but in some cases is delayed until the second or third decade of life. Inheritance can be autosomal dominant or recessive.
  • See also
    MIM:604129
Natural variants in EBP
Variant IDPosition(s)ChangeDescription
VAR_0111681791G>Ein EBP; dbSNP:rs1575450640
VAR_0111762028G>Rin DDEB and EBP; dbSNP:rs762162799
VAR_0018282242G>Rin EBP; dbSNP:rs121912837
VAR_0111952369G>Sin EBP
VAR_0111982713G>Rin EBP

Nail disorder, non-syndromic congenital, 8 (NDNC8)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A nail disorder characterized by isolated toenail dystrophy. The nail changes are most severe in the great toes and consist of the nail plate being buried in the nail bed with a deformed and narrow free edge.
  • See also
    MIM:607523
Natural variants in NDNC8
Variant IDPosition(s)ChangeDescription
VAR_0155191595G>Rin NDNC8; dbSNP:rs121912840
VAR_0155201815G>Rin NDNC8; dbSNP:rs121912841

Epidermolysis bullosa dystrophica, with subcorneal cleavage (EBDSC)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A bullous skin disorder with variable sized clefts just beneath the level of the stratum corneum. Clinical features include blisters, milia, atrophic scarring, nail dystrophy, and oral and conjunctival involvement, as seen in dystrophic epidermolysis bullosa.
  • See also
    MIM:131750
Natural variants in EBDSC
Variant IDPosition(s)ChangeDescription
VAR_0018182034G>Rin DDEB and EBDSC; interferes with collagen VII folding and secretion; dbSNP:rs121912844

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_035740119in a breast cancer sample; somatic mutation
Natural variantVAR_001809142in RDEB; uncertain significance; may affect exon 3 splicing; dbSNP:rs121912856
Natural variantVAR_001810595in dbSNP:rs2228561
Natural variantVAR_0487661120in dbSNP:rs2228563
Natural variantVAR_0018111277in dbSNP:rs35761247
Natural variantVAR_0111601347in RDEB; localized type; mild; dbSNP:rs121912833
Natural variantVAR_0357411364in a breast cancer sample; somatic mutation
Natural variantVAR_0357421366in a breast cancer sample; somatic mutation; dbSNP:rs147089666
Natural variantVAR_0111611519in TBDN; dbSNP:rs121912835
Natural variantVAR_0111621522in DDEB; dbSNP:rs387906605
Natural variantVAR_0018121557in DDEB
Natural variantVAR_0155191595in NDNC8; dbSNP:rs121912840
Natural variantVAR_0111631604in RDEB; dbSNP:rs1560234201
Natural variantVAR_0111641652in RDEB; mitis type; dbSNP:rs1439299333
Natural variantVAR_0111651703in RDEB; dbSNP:rs770304825
Natural variantVAR_0111661772in RDEB; dbSNP:rs1032335328
Natural variantVAR_0111671776in DDEB
Natural variantVAR_0018131782in RDEB; mitis type; dbSNP:rs374718902
Natural variantVAR_0111681791in EBP; dbSNP:rs1575450640
Natural variantVAR_0111691812in RDEB
Natural variantVAR_0155201815in NDNC8; dbSNP:rs121912841
Natural variantVAR_0649941845in RDEB
Natural variantVAR_0649951981in RDEB; mild form
Natural variantVAR_0018141982in RDEB
Natural variantVAR_0018152003in DDEB; dbSNP:rs121912832
Natural variantVAR_0111702006in DDEB
Natural variantVAR_0111712006in DDEB; interferes with collagen VII folding and secretion; dbSNP:rs121912842
Natural variantVAR_0111722008in RDEB; dbSNP:rs1055680335
Natural variantVAR_0018162008in RDEB; dbSNP:rs1055680335
Natural variantVAR_0111732009in RDEB
Natural variantVAR_0111742015in DDEB; interferes with collagen VII folding and secretion; dbSNP:rs121912843
Natural variantVAR_0018172025in RDEB; mitis type; dbSNP:rs766931219
Natural variantVAR_0111752028in DDEB
Natural variantVAR_0111762028in DDEB and EBP; dbSNP:rs762162799
Natural variantVAR_0111772031in RDEB; severe phenotype; dbSNP:rs121912838
Natural variantVAR_0018182034in DDEB and EBDSC; interferes with collagen VII folding and secretion; dbSNP:rs121912844
Natural variantVAR_0111782034in DDEB
Natural variantVAR_0111792037in DDEB; dbSNP:rs121912846
Natural variantVAR_0111802040in DDEB
Natural variantVAR_0018192040in DDEB; dbSNP:rs121912829
Natural variantVAR_0111812040in DDEB
Natural variantVAR_0018202043in DDEB; dbSNP:rs121912836
Natural variantVAR_0111822043in DDEB; localized type; dbSNP:rs121912836
Natural variantVAR_0111832046in DDEB
Natural variantVAR_0018212049in RDEB
Natural variantVAR_0018222055in DDEB; dbSNP:rs1553854678
Natural variantVAR_0018232063in RDEB; dbSNP:rs121912849
Natural variantVAR_0111842064in DDEB; dbSNP:rs866061439
Natural variantVAR_0649962069in RDEB; dbSNP:rs121912855
Natural variantVAR_0649972070in DDEB
Natural variantVAR_0018252073in RDEB; mitis type
Natural variantVAR_0018262076in DDEB; also in recessive forms; dbSNP:rs121912850
Natural variantVAR_0018272079in DDEB
Natural variantVAR_0111852079in DDEB
Natural variantVAR_0111862132in RDEB; dbSNP:rs755669902
Natural variantVAR_0111872192in RDEB
Natural variantVAR_0111882207in DDEB
Natural variantVAR_0649982221in RDEB
Natural variantVAR_0018282242in EBP; dbSNP:rs121912837
Natural variantVAR_0111892251in TBDN; also found in isolated toenail dystrophy; dbSNP:rs121912834
Natural variantVAR_0111902263in RDEB
Natural variantVAR_0111912287in RDEB; also found in isolated toenail dystrophy; dbSNP:rs121912839
Natural variantVAR_0649992296in RDEB
Natural variantVAR_0111922316in RDEB
Natural variantVAR_0111932348in DDEB/RDEB; mild form
Natural variantVAR_0018292351in a patient with dystrophic epidermolysis bullosa; mitis type; dbSNP:rs1800013
Natural variantVAR_0111942366in RDEB; mitis type; dbSNP:rs1560204600
Natural variantVAR_0111952369in EBP
Natural variantVAR_0337862429in dbSNP:rs2229822
Natural variantVAR_0650002557in RDEB
Natural variantVAR_0018302569in RDEB; severe and mitis type
Natural variantVAR_0018312575in RDEB; dbSNP:rs760891216
Natural variantVAR_0650012622in RDEB; dbSNP:rs139318843
Natural variantVAR_0018322623in PR-DEB; dominant; dbSNP:rs121912831
Natural variantVAR_0018332653in RDEB; mitis type; dbSNP:rs121912851
Natural variantVAR_0018342671in RDEB
Natural variantVAR_0111962674in RDEB
Natural variantVAR_0018352674in RDEB; mitis type
Natural variantVAR_0111972713in DDEB; dbSNP:rs369591910
Natural variantVAR_0111982713in EBP
Natural variantVAR_0111992740in RDEB
Natural variantVAR_0018362749in RDEB; dbSNP:rs121912853
Natural variantVAR_0112002775in RDEB; mitis type; dbSNP:rs1333259313
Natural variantVAR_0112012791in DDEB; dbSNP:rs142566193
Natural variantVAR_0018372798in RDEB; dbSNP:rs121912828

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 3,739 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain, glycosylation, modified residue (large scale data), modified residue, disulfide bond.

TypeIDPosition(s)SourceDescription
Signal1-16UniProt
ChainPRO_000000576117-2944UniProtCollagen alpha-1(VII) chain
Glycosylation337UniProtN-linked (GlcNAc...) asparagine
Glycosylation786UniProtN-linked (GlcNAc...) asparagine
Modified residue (large scale data)828PRIDEPhosphoserine
Glycosylation1109UniProtN-linked (GlcNAc...) asparagine
Modified residue2036UniProt4-hydroxyproline
Modified residue2039UniProt4-hydroxyproline
Modified residue2084UniProt4-hydroxyproline
Modified residue2087UniProt4-hydroxyproline
Modified residue2090UniProt4-hydroxyproline
Modified residue2167UniProt4-hydroxyproline
Modified residue2176UniProt4-hydroxyproline
Modified residue2185UniProt4-hydroxyproline
Modified residue2188UniProt4-hydroxyproline
Modified residue (large scale data)2600PRIDEPhosphoserine
Modified residue2625UniProt5-hydroxylysine; alternate
Glycosylation2625UniProtO-linked (Gal...) hydroxylysine; alternate
Modified residue2631UniProt5-hydroxylysine; alternate
Glycosylation2631UniProtO-linked (Gal...) hydroxylysine; alternate
Disulfide bond2634UniProtInterchain
Modified residue2664UniProt4-hydroxyproline
Modified residue2667UniProt4-hydroxyproline
Modified residue2673UniProt4-hydroxyproline
Disulfide bond2802UniProtInterchain
Disulfide bond2804UniProtInterchain
Disulfide bond2876↔2929UniProt
Disulfide bond2885↔2912UniProt
Disulfide bond2904↔2925UniProt

Post-translational modification

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Homotrimer. Interacts with MIA3/TANGO1; facilitating its loading into transport carriers and subsequent secretion.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q02388MIA3 Q5JRA62EBI-724237, EBI-2291868

Protein-protein interaction databases

Miscellaneous

Structure

3D structure databases

Family & Domains

Features

Showing features for region, domain, motif, compositional bias.

TypeIDPosition(s)Description
Region17-1253Nonhelical region (NC1)
Domain38-211VWFA 1
Domain234-329Fibronectin type-III 1
Domain330-416Fibronectin type-III 2
Domain417-507Fibronectin type-III 3
Domain510-597Fibronectin type-III 4
Domain600-687Fibronectin type-III 5
Region632-651Disordered
Domain688-775Fibronectin type-III 6
Domain778-866Fibronectin type-III 7
Domain869-957Fibronectin type-III 8
Domain958-1051Fibronectin type-III 9
Domain1054-1229VWFA 2
Motif1170-1172Cell attachment site
Region1239-1941Disordered
Region1254-1477Interrupted collagenous region
Region1254-2784Triple-helical region
Motif1334-1336Cell attachment site
Compositional bias1368-1392Pro residues
Compositional bias1425-1439Pro residues
Compositional bias1713-1730Basic and acidic residues
Compositional bias1848-1875Basic and acidic residues
Compositional bias1885-1901Pro residues
Region1963-2782Disordered
Motif2008-2010Cell attachment site
Compositional bias2056-2073Basic and acidic residues
Compositional bias2079-2096Pro residues
Compositional bias2169-2195Pro residues
Compositional bias2278-2292Pro residues
Compositional bias2334-2353Basic and acidic residues
Compositional bias2434-2449Pro residues
Compositional bias2537-2568Basic and acidic residues
Motif2553-2555Cell attachment site
Compositional bias2632-2646Basic and acidic residues
Region2785-2944Nonhelical region (NC2)
Region2837-2872Disordered
Compositional bias2844-2869Acidic residues
Domain2872-2944BPTI/Kunitz inhibitor

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

Q02388-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    2,944
  • Mass (Da)
    295,220
  • Last updated
    1996-02-01 v2
  • Checksum
    96D8BF6D0FD387DB
MTLRLLVAALCAGILAEAPRVRAQHRERVTCTRLYAADIVFLLDGSSSIGRSNFREVRSFLEGLVLPFSGAASAQGVRFATVQYSDDPRTEFGLDALGSGGDVIRAIRELSYKGGNTRTGAAILHVADHVFLPQLARPGVPKVCILITDGKSQDLVDTAAQRLKGQGVKLFAVGIKNADPEELKRVASQPTSDFFFFVNDFSILRTLLPLVSRRVCTTAGGVPVTRPPDDSTSAPRDLVLSEPSSQSLRVQWTAASGPVTGYKVQYTPLTGLGQPLPSERQEVNVPAGETSVRLRGLRPLTEYQVTVIALYANSIGEAVSGTARTTALEGPELTIQNTTAHSLLVAWRSVPGATGYRVTWRVLSGGPTQQQELGPGQGSVLLRDLEPGTDYEVTVSTLFGRSVGPATSLMARTDASVEQTLRPVILGPTSILLSWNLVPEARGYRLEWRRETGLEPPQKVVLPSDVTRYQLDGLQPGTEYRLTLYTLLEGHEVATPATVVPTGPELPVSPVTDLQATELPGQRVRVSWSPVPGATQYRIIVRSTQGVERTLVLPGSQTAFDLDDVQAGLSYTVRVSARVGPREGSASVLTVRREPETPLAVPGLRVVVSDATRVRVAWGPVPGASGFRISWSTGSGPESSQTLPPDSTATDITGLQPGTTYQVAVSVLRGREEGPAAVIVARTDPLGPVRTVHVTQASSSSVTITWTRVPGATGYRVSWHSAHGPEKSQLVSGEATVAELDGLEPDTEYTVHVRAHVAGVDGPPASVVVRTAPEPVGRVSRLQILNASSDVLRITWVGVTGATAYRLAWGRSEGGPMRHQILPGNTDSAEIRGLEGGVSYSVRVTALVGDREGTPVSIVVTTPPEAPPALGTLHVVQRGEHSLRLRWEPVPRAQGFLLHWQPEGGQEQSRVLGPELSSYHLDGLEPATQYRVRLSVLGPAGEGPSAEVTARTESPRVPSIELRVVDTSIDSVTLAWTPVSRASSYILSWRPLRGPGQEVPGSPQTLPGISSSQRVTGLEPGVSYIFSLTPVLDGVRGPEASVTQTPVCPRGLADVVFLPHATQDNAHRAEATRRVLERLVLALGPLGPQAVQVGLLSYSHRPSPLFPLNGSHDLGIILQRIRDMPYMDPSGNNLGTAVVTAHRYMLAPDAPGRRQHVPGVMVLLVDEPLRGDIFSPIREAQASGLNVVMLGMAGADPEQLRRLAPGMDSVQTFFAVDDGPSLDQAVSGLATALCQASFTTQPRPEPCPVYCPKGQKGEPGEMGLRGQVGPPGDPGLPGRTGAPGPQGPPGSATAKGERGFPGADGRPGSPGRAGNPGTPGAPGLKGSPGLPGPRGDPGERGPRGPKGEPGAPGQVIGGEGPGLPGRKGDPGPSGPPGPRGPLGDPGPRGPPGLPGTAMKGDKGDRGERGPPGPGEGGIAPGEPGLPGLPGSPGPQGPVGPPGKKGEKGDSEDGAPGLPGQPGSPGEQGPRGPPGAIGPKGDRGFPGPLGEAGEKGERGPPGPAGSRGLPGVAGRPGAKGPEGPPGPTGRQGEKGEPGRPGDPAVVGPAVAGPKGEKGDVGPAGPRGATGVQGERGPPGLVLPGDPGPKGDPGDRGPIGLTGRAGPPGDSGPPGEKGDPGRPGPPGPVGPRGRDGEVGEKGDEGPPGDPGLPGKAGERGLRGAPGVRGPVGEKGDQGDPGEDGRNGSPGSSGPKGDRGEPGPPGPPGRLVDTGPGAREKGEPGDRGQEGPRGPKGDPGLPGAPGERGIEGFRGPPGPQGDPGVRGPAGEKGDRGPPGLDGRSGLDGKPGAAGPSGPNGAAGKAGDPGRDGLPGLRGEQGLPGPSGPPGLPGKPGEDGKPGLNGKNGEPGDPGEDGRKGEKGDSGASGREGRDGPKGERGAPGILGPQGPPGLPGPVGPPGQGFPGVPGGTGPKGDRGETGSKGEQGLPGERGLRGEPGSVPNVDRLLETAGIKASALREIVETWDESSGSFLPVPERRRGPKGDSGEQGPPGKEGPIGFPGERGLKGDRGDPGPQGPPGLALGERGPPGPSGLAGEPGKPGIPGLPGRAGGVGEAGRPGERGERGEKGERGEQGRDGPPGLPGTPGPPGPPGPKVSVDEPGPGLSGEQGPPGLKGAKGEPGSNGDQGPKGDRGVPGIKGDRGEPGPRGQDGNPGLPGERGMAGPEGKPGLQGPRGPPGPVGGHGDPGPPGAPGLAGPAGPQGPSGLKGEPGETGPPGRGLTGPTGAVGLPGPPGPSGLVGPQGSPGLPGQVGETGKPGAPGRDGASGKDGDRGSPGVPGSPGLPGPVGPKGEPGPTGAPGQAVVGLPGAKGEKGAPGGLAGDLVGEPGAKGDRGLPGPRGEKGEAGRAGEPGDPGEDGQKGAPGPKGFKGDPGVGVPGSPGPPGPPGVKGDLGLPGLPGAPGVVGFPGQTGPRGEMGQPGPSGERGLAGPPGREGIPGPLGPPGPPGSVGPPGASGLKGDKGDPGVGLPGPRGERGEPGIRGEDGRPGQEGPRGLTGPPGSRGERGEKGDVGSAGLKGDKGDSAVILGPPGPRGAKGDMGERGPRGLDGDKGPRGDNGDPGDKGSKGEPGDKGSAGLPGLRGLLGPQGQPGAAGIPGDPGSPGKDGVPGIRGEKGDVGFMGPRGLKGERGVKGACGLDGEKGDKGEAGPPGRPGLAGHKGEMGEPGVPGQSGAPGKEGLIGPKGDRGFDGQPGPKGDQGEKGERGTPGIGGFPGPSGNDGSAGPPGPPGSVGPRGPEGLQGQKGERGPPGERVVGAPGVPGAPGERGEQGRPGPAGPRGEKGEAALTEDDIRGFVRQEMSQHCACQGQFIASGSRPLPSYAADTAGSQLHAVPVLRVSHAEEEERVPPEDDEYSEYSEYSVEEYQDPEAPWDSDDPCSLPLDEGSCTAYTLRWYHRAVTGSTEACHPFVYGGCGGNANRFGTREACERRCPPRVVQSQGTGTAQD

Q02388-2

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
C9JBL3C9JBL3_HUMANCOL7A1173

Sequence caution

The sequence BAA02853.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict, compositional bias, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict195-197in Ref. 4; BAA02853
Sequence conflict369-371in Ref. 5; AAA36357/AAB24637
Sequence conflict518-519in Ref. 5; AAA36357/AAB24637
Sequence conflict529in Ref. 4; BAA02853
Sequence conflict541in Ref. 5; AAA36357/AAB24637
Sequence conflict851in Ref. 4; BAA02853
Sequence conflict893in Ref. 1; AAA58965, 4; BAA02853 and 6; AAA96439
Sequence conflict1122in Ref. 4; BAA02853
Compositional bias1368-1392Pro residues
Compositional bias1425-1439Pro residues
Sequence conflict1463-1464in Ref. 3; AA sequence
Compositional bias1713-1730Basic and acidic residues
Compositional bias1848-1875Basic and acidic residues
Alternative sequenceVSP_0240261869-1900in isoform 2
Compositional bias1885-1901Pro residues
Compositional bias2056-2073Basic and acidic residues
Compositional bias2079-2096Pro residues
Compositional bias2169-2195Pro residues
Compositional bias2278-2292Pro residues
Compositional bias2334-2353Basic and acidic residues
Compositional bias2434-2449Pro residues
Compositional bias2537-2568Basic and acidic residues
Compositional bias2632-2646Basic and acidic residues
Compositional bias2844-2869Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L23982
EMBL· GenBank· DDBJ
AAA58965.1
EMBL· GenBank· DDBJ
Genomic DNA
L02870
EMBL· GenBank· DDBJ
AAA75438.1
EMBL· GenBank· DDBJ
mRNA
D13694
EMBL· GenBank· DDBJ
BAA02853.1
EMBL· GenBank· DDBJ
mRNA Frameshift
M96984
EMBL· GenBank· DDBJ
AAA36357.2
EMBL· GenBank· DDBJ
mRNA
S51236
EMBL· GenBank· DDBJ
AAB24637.1
EMBL· GenBank· DDBJ
mRNA
M65158
EMBL· GenBank· DDBJ
AAA96439.1
EMBL· GenBank· DDBJ
mRNA
L06862
EMBL· GenBank· DDBJ
AAA89196.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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