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Protein

Collagen alpha-1(VII) chain

Gene

COL7A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei2886 – 2887Reactive bondBy similarity2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

BioCyciZFISH:ENSG00000114270-MONOMER.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474244. Extracellular matrix organization.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-2214320. Anchoring fibril formation.
R-HSA-3000157. Laminin interactions.
R-HSA-5694530. Cargo concentration in the ER.

Protein family/group databases

MEROPSiI02.967.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(VII) chain
Alternative name(s):
Long-chain collagen
Short name:
LC collagen
Gene namesi
Name:COL7A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:2214. COL7A1.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: ProtInc
  • collagen type VII trimer Source: ProtInc
  • endoplasmic reticulum-Golgi intermediate compartment membrane Source: Reactome
  • endoplasmic reticulum lumen Source: Reactome
  • ER to Golgi transport vesicle Source: Reactome
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • Golgi membrane Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

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

Epidermolysis bullosa dystrophica, autosomal dominant (DDEB)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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 OMIM:131750
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0111621522G → E in DDEB. Corresponds to variant rs387906605dbSNPEnsembl.1
Natural variantiVAR_0018121557G → R in DDEB. 1
Natural variantiVAR_0111671776G → R in DDEB. 1
Natural variantiVAR_0018152003G → R in DDEB. 1 PublicationCorresponds to variant rs121912832dbSNPEnsembl.1
Natural variantiVAR_0111702006G → A in DDEB. 1
Natural variantiVAR_0111712006G → D in DDEB; interferes with collagen VII folding and secretion. 2 PublicationsCorresponds to variant rs121912842dbSNPEnsembl.1
Natural variantiVAR_0111742015G → E in DDEB; interferes with collagen VII folding and secretion. 2 PublicationsCorresponds to variant rs121912843dbSNPEnsembl.1
Natural variantiVAR_0111752028G → A in DDEB. 1 Publication1
Natural variantiVAR_0111762028G → R in DDEB and EBP. 2 PublicationsCorresponds to variant rs762162799dbSNPEnsembl.1
Natural variantiVAR_0018182034G → R in DDEB and EBDSC; interferes with collagen VII folding and secretion. 4 PublicationsCorresponds to variant rs121912844dbSNPEnsembl.1
Natural variantiVAR_0111782034G → W in DDEB. 2 Publications1
Natural variantiVAR_0111802040G → D in DDEB. 1 Publication1
Natural variantiVAR_0111812040G → V in DDEB. 1 Publication1
Natural variantiVAR_0018202043G → R in DDEB. 5 PublicationsCorresponds to variant rs121912836dbSNPEnsembl.1
Natural variantiVAR_0111822043G → W in DDEB; localized type. 1 Publication1
Natural variantiVAR_0111832046G → V in DDEB. 1
Natural variantiVAR_0018222055G → E in DDEB. 1
Natural variantiVAR_0111842064G → R in DDEB. 2 Publications1
Natural variantiVAR_0649972070G → R in DDEB. 1 Publication1
Natural variantiVAR_0018262076G → D in DDEB; also in recessive forms. 1 PublicationCorresponds to variant rs121912850dbSNPEnsembl.1
Natural variantiVAR_0018272079G → E in DDEB. 1 Publication1
Natural variantiVAR_0111852079G → R in DDEB; associated with squamous cell carcinoma. 1 Publication1
Natural variantiVAR_0111882207G → R in DDEB. 1 Publication1
Natural variantiVAR_0111932348G → R in DDEB/RDEB; mild form. 1 Publication1
Natural variantiVAR_0111972713G → D in DDEB. 1 PublicationCorresponds to variant rs369591910dbSNPEnsembl.1
Natural variantiVAR_0112012791R → W in DDEB. Corresponds to variant rs142566193dbSNPEnsembl.1
Epidermolysis bullosa dystrophica, autosomal recessive (RDEB)10 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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 to mild forms with limited and localized scarring, and less frequent extracutaneous manifestations. Mild forms include epidermolysis bullosa mitis and epidermolysis bullosa localisata.
See also OMIM:226600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001809142K → R in RDEB. Corresponds to variant rs121912856dbSNPEnsembl.1
Natural variantiVAR_001810595P → L in RDEB. Corresponds to variant rs2228561dbSNPEnsembl.1
Natural variantiVAR_0018111277P → L in RDEB. Corresponds to variant rs35761247dbSNPEnsembl.1
Natural variantiVAR_0111601347G → R in RDEB; localized type; mild. 1 PublicationCorresponds to variant rs121912833dbSNPEnsembl.1
Natural variantiVAR_0111631604G → R in RDEB. 1
Natural variantiVAR_0111641652G → R in RDEB; mitis type. 1 Publication1
Natural variantiVAR_0111651703G → E in RDEB. Corresponds to variant rs770304825dbSNPEnsembl.1
Natural variantiVAR_0111661772R → W in RDEB. 1
Natural variantiVAR_0018131782G → R in RDEB; mitis type. 1 PublicationCorresponds to variant rs374718902dbSNPEnsembl.1
Natural variantiVAR_0111691812G → R in RDEB. 1 Publication1
Natural variantiVAR_0649941845G → R in RDEB. 1 Publication1
Natural variantiVAR_0649951981K → R in RDEB; mild form. 1 Publication1
Natural variantiVAR_0111732009G → R in RDEB. 2 Publications1
Natural variantiVAR_0018172025G → A in RDEB; mitis type. 1 PublicationCorresponds to variant rs766931219dbSNPEnsembl.1
Natural variantiVAR_0111772031G → S in RDEB; severe phenotype. 1 PublicationCorresponds to variant rs121912838dbSNPEnsembl.1
Natural variantiVAR_0649962069R → C in RDEB. 1 PublicationCorresponds to variant rs121912855dbSNPEnsembl.1
Natural variantiVAR_0018252073G → D in RDEB; mitis type. 1 Publication1
Natural variantiVAR_0111862132G → D in RDEB. Corresponds to variant rs755669902dbSNPEnsembl.1
Natural variantiVAR_0111872192G → S in RDEB. 1
Natural variantiVAR_0649982221G → A in RDEB. 1 Publication1
Natural variantiVAR_0111902263G → V in RDEB. 1
Natural variantiVAR_0111912287G → R in RDEB; moderately severe phenotype when compound heterozygous with R-2316; leads to isolated toenail dystrophy when heterozygous with a normal allele. 1 PublicationCorresponds to variant rs121912839dbSNPEnsembl.1
Natural variantiVAR_0649992296G → E in RDEB. 1 Publication1
Natural variantiVAR_0111922316G → R in RDEB; moderately severe phenotype when compound heterozygous with R-2287. 1 Publication1
Natural variantiVAR_0111932348G → R in DDEB/RDEB; mild form. 1 Publication1
Natural variantiVAR_0111942366G → S in RDEB; mitis type. 1 Publication1
Natural variantiVAR_0650002557G → R in RDEB. 1 Publication1
Natural variantiVAR_0018302569G → R in RDEB; severe and mitis type. 1
Natural variantiVAR_0650012622R → W in RDEB. 1 PublicationCorresponds to variant rs139318843dbSNPEnsembl.1
Natural variantiVAR_0018332653G → R in RDEB; mitis type. Corresponds to variant rs121912851dbSNPEnsembl.1
Natural variantiVAR_0018342671G → V in RDEB. 1
Natural variantiVAR_0111962674G → D in RDEB. 1
Natural variantiVAR_0018352674G → R in RDEB; mitis type. 1
Natural variantiVAR_0111992740G → A in RDEB. 1
Natural variantiVAR_0112002775G → S in RDEB; mitis type. 1 Publication1
Epidermolysis bullosa dystrophica, Pasini type (P-DEB)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe, dominantly inherited form of dystrophic epidermolysis bullosa characterized by albopapuloid Pasini papule, dorsal extremity blistering, milia formation and red atrophic scarring after recurrent blisters.
See also OMIM:131750
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0111792037G → E in P-DEB. 1 PublicationCorresponds to variant rs121912846dbSNPEnsembl.1
Natural variantiVAR_0018192040G → S in P-DEB. 1 PublicationCorresponds to variant rs121912829dbSNPEnsembl.1
Epidermolysis bullosa dystrophica, Hallopeau-Siemens type (HS-DEB)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionThe most severe recessive form of dystrophic epidermolysis bullosa. It manifests with mutilating scarring, joint contractures, corneal erosions, esophagus structures, and propensity to formation of cutaneous squamous cell carcinomas leading to premature demise of the affected individuals.
See also OMIM:226600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0018141982G → W in HS-DEB. 1 Publication1
Natural variantiVAR_0111722008R → C in HS-DEB; also in a milder localized type. 2 Publications1
Natural variantiVAR_0018162008R → G in HS-DEB. 2 Publications1
Natural variantiVAR_0018212049G → E in HS-DEB. 2 Publications1
Natural variantiVAR_0018232063R → W in HS-DEB; also in a mild form. 3 PublicationsCorresponds to variant rs121912849dbSNPEnsembl.1
Natural variantiVAR_0018312575G → R in HS-DEB; also in a mild form. 2 PublicationsCorresponds to variant rs760891216dbSNPEnsembl.1
Natural variantiVAR_0018362749G → R in HS-DEB; also in a mild form. Corresponds to variant rs121912853dbSNPEnsembl.1
Natural variantiVAR_0018372798M → K in HS-DEB; also in a mild form. 1 PublicationCorresponds to variant rs121912828dbSNPEnsembl.1
Transient bullous dermolysis of the newborn (TBDN)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionTBDN 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 OMIM:131705
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0111611519G → D in TBDN; compound heterozygous with E-2251; clinically silent when heterozygous with a normal allele. 2 PublicationsCorresponds to variant rs121912835dbSNPEnsembl.1
Natural variantiVAR_0111892251G → E in TBDN; compound heterozygous with D-1519; leads to isolated toenail dystrophy when heterozygous with a normal allele. 1 PublicationCorresponds to variant rs121912834dbSNPEnsembl.1
Epidermolysis bullosa dystrophica, pretibial type (PR-DEB)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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 OMIM:131850
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0018322623G → C in PR-DEB; dominant. 1 PublicationCorresponds to variant rs121912831dbSNPEnsembl.1
Epidermolysis bullosa dystrophica, Bart type (B-DEB)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant form of dystrophic epidermolysis bullosa characterized by congenital localized absence of skin, skin fragility and deformity of nails.
See also OMIM:132000
Epidermolysis bullosa pruriginosa (EBP)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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 OMIM:604129
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0111681791G → E in EBP. 1 Publication1
Natural variantiVAR_0111762028G → R in DDEB and EBP. 2 PublicationsCorresponds to variant rs762162799dbSNPEnsembl.1
Natural variantiVAR_0018282242G → R in EBP. 1 PublicationCorresponds to variant rs121912837dbSNPEnsembl.1
Natural variantiVAR_0111952369G → S in EBP. 1 Publication1
Natural variantiVAR_0111982713G → R in EBP. 1 Publication1
Nail disorder, non-syndromic congenital, 8 (NDNC8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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 OMIM:607523
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0155191595G → R in NDNC8. 1 PublicationCorresponds to variant rs121912840dbSNPEnsembl.1
Natural variantiVAR_0155201815G → R in NDNC8. 1 PublicationCorresponds to variant rs121912841dbSNPEnsembl.1
Epidermolysis bullosa dystrophica, with subcorneal cleavage (EBDSC)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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 OMIM:131750
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0018182034G → R in DDEB and EBDSC; interferes with collagen VII folding and secretion. 4 PublicationsCorresponds to variant rs121912844dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Epidermolysis bullosa

Organism-specific databases

DisGeNETi1294.
MalaCardsiCOL7A1.
MIMi131705. phenotype.
131750. phenotype.
131850. phenotype.
132000. phenotype.
226600. phenotype.
604129. phenotype.
607523. phenotype.
OpenTargetsiENSG00000114270.
Orphaneti158673. Acral dystrophic epidermolysis bullosa.
89841. Centripetalis recessive dystrophic epidermolysis bullosa.
89843. Dystrophic epidermolysis bullosa pruriginosa.
158676. Dystrophic epidermolysis bullosa, nails only.
89839. Epidermolysis bullosa simplex superficialis.
231568. Generalized dominant dystrophic epidermolysis bullosa.
79410. Pretibial dystrophic epidermolysis bullosa.
79409. Recessive dystrophic epidermolysis bullosa inversa.
89842. Recessive dystrophic epidermolysis bullosa-generalized other.
79408. Severe generalized recessive dystrophic epidermolysis bullosa.
79411. Transient bullous dermolysis of the newborn.
PharmGKBiPA26730.

Polymorphism and mutation databases

BioMutaiCOL7A1.
DMDMi1345650.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Sequence analysisAdd BLAST16
ChainiPRO_000000576117 – 2944Collagen alpha-1(VII) chainAdd BLAST2928

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi337N-linked (GlcNAc...)Sequence analysis1
Glycosylationi786N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1109N-linked (GlcNAc...)Sequence analysis1
Modified residuei21674-hydroxyproline1 Publication1
Modified residuei21764-hydroxyproline1 Publication1
Modified residuei21854-hydroxyproline1 Publication1
Modified residuei21884-hydroxyproline1 Publication1
Modified residuei26255-hydroxylysine; alternate1 Publication1
Glycosylationi2625O-linked (Gal...); alternate1
Modified residuei26315-hydroxylysine; alternate1 Publication1
Glycosylationi2631O-linked (Gal...); alternate1
Disulfide bondi2634InterchainPROSITE-ProRule annotation
Modified residuei26644-hydroxyproline1 Publication1
Modified residuei26674-hydroxyproline1 Publication1
Modified residuei26734-hydroxyproline1 Publication1
Disulfide bondi2802InterchainPROSITE-ProRule annotation
Disulfide bondi2804InterchainPROSITE-ProRule annotation
Disulfide bondi2876 ↔ 2929PROSITE-ProRule annotation
Disulfide bondi2885 ↔ 2912PROSITE-ProRule annotation
Disulfide bondi2904 ↔ 2925PROSITE-ProRule annotation

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

EPDiQ02388.
MaxQBiQ02388.
PaxDbiQ02388.
PeptideAtlasiQ02388.
PRIDEiQ02388.

PTM databases

iPTMnetiQ02388.
PhosphoSitePlusiQ02388.

Expressioni

Gene expression databases

BgeeiENSG00000114270.
CleanExiHS_COL7A1.
ExpressionAtlasiQ02388. baseline and differential.
GenevisibleiQ02388. HS.

Organism-specific databases

HPAiCAB016357.
HPA042420.

Interactioni

Subunit structurei

Homotrimer. Interacts with MIA3/TANGO1; facilitating its loading into transport carriers and subsequent secretion.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MIA3Q5JRA62EBI-724237,EBI-2291868

Protein-protein interaction databases

BioGridi107691. 17 interactors.
IntActiQ02388. 14 interactors.
MINTiMINT-1390694.
STRINGi9606.ENSP00000332371.

Structurei

3D structure databases

ProteinModelPortaliQ02388.
SMRiQ02388.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini38 – 211VWFA 1PROSITE-ProRule annotationAdd BLAST174
Domaini234 – 329Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST96
Domaini330 – 416Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST87
Domaini417 – 507Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST91
Domaini510 – 597Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST88
Domaini600 – 687Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST88
Domaini688 – 775Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST88
Domaini778 – 866Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST89
Domaini869 – 957Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST89
Domaini958 – 1051Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST94
Domaini1054 – 1229VWFA 2PROSITE-ProRule annotationAdd BLAST176
Domaini2872 – 2944BPTI/Kunitz inhibitorPROSITE-ProRule annotationAdd BLAST73

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni17 – 1253Nonhelical region (NC1)Add BLAST1237
Regioni1254 – 2784Triple-helical regionAdd BLAST1531
Regioni1254 – 1477Interrupted collagenous regionAdd BLAST224
Regioni2785 – 2944Nonhelical region (NC2)Add BLAST160

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1170 – 1172Cell attachment siteSequence analysis3
Motifi1334 – 1336Cell attachment siteSequence analysis3
Motifi2008 – 2010Cell attachment siteSequence analysis3
Motifi2553 – 2555Cell attachment siteSequence analysis3

Sequence similaritiesi

Contains 1 BPTI/Kunitz inhibitor domain.PROSITE-ProRule annotation
Contains 9 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 2 VWFA domains.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00760000119000.
HOGENOMiHOG000111866.
HOVERGENiHBG051053.
InParanoidiQ02388.
KOiK16628.
OMAiDTEYTVH.
OrthoDBiEOG091G008X.
PhylomeDBiQ02388.
TreeFamiTF351645.

Family and domain databases

CDDicd00063. FN3. 9 hits.
Gene3Di2.60.40.10. 9 hits.
3.40.50.410. 2 hits.
4.10.410.10. 1 hit.
InterProiIPR008160. Collagen.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR002223. Kunitz_BPTI.
IPR020901. Prtase_inh_Kunz-CS.
IPR002035. VWF_A.
[Graphical view]
PfamiPF01391. Collagen. 15 hits.
PF00041. fn3. 8 hits.
PF00014. Kunitz_BPTI. 1 hit.
PF00092. VWA. 2 hits.
[Graphical view]
PRINTSiPR00759. BASICPTASE.
SMARTiSM00060. FN3. 9 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 5 hits.
SSF53300. SSF53300. 2 hits.
SSF57362. SSF57362. 1 hit.
PROSITEiPS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
PS50853. FN3. 9 hits.
PS50234. VWFA. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q02388-1) [UniParc]FASTAAdd to basket

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.

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        10         20         30         40         50
MTLRLLVAAL CAGILAEAPR VRAQHRERVT CTRLYAADIV FLLDGSSSIG
60 70 80 90 100
RSNFREVRSF LEGLVLPFSG AASAQGVRFA TVQYSDDPRT EFGLDALGSG
110 120 130 140 150
GDVIRAIREL SYKGGNTRTG AAILHVADHV FLPQLARPGV PKVCILITDG
160 170 180 190 200
KSQDLVDTAA QRLKGQGVKL FAVGIKNADP EELKRVASQP TSDFFFFVND
210 220 230 240 250
FSILRTLLPL VSRRVCTTAG GVPVTRPPDD STSAPRDLVL SEPSSQSLRV
260 270 280 290 300
QWTAASGPVT GYKVQYTPLT GLGQPLPSER QEVNVPAGET SVRLRGLRPL
310 320 330 340 350
TEYQVTVIAL YANSIGEAVS GTARTTALEG PELTIQNTTA HSLLVAWRSV
360 370 380 390 400
PGATGYRVTW RVLSGGPTQQ QELGPGQGSV LLRDLEPGTD YEVTVSTLFG
410 420 430 440 450
RSVGPATSLM ARTDASVEQT LRPVILGPTS ILLSWNLVPE ARGYRLEWRR
460 470 480 490 500
ETGLEPPQKV VLPSDVTRYQ LDGLQPGTEY RLTLYTLLEG HEVATPATVV
510 520 530 540 550
PTGPELPVSP VTDLQATELP GQRVRVSWSP VPGATQYRII VRSTQGVERT
560 570 580 590 600
LVLPGSQTAF DLDDVQAGLS YTVRVSARVG PREGSASVLT VRREPETPLA
610 620 630 640 650
VPGLRVVVSD ATRVRVAWGP VPGASGFRIS WSTGSGPESS QTLPPDSTAT
660 670 680 690 700
DITGLQPGTT YQVAVSVLRG REEGPAAVIV ARTDPLGPVR TVHVTQASSS
710 720 730 740 750
SVTITWTRVP GATGYRVSWH SAHGPEKSQL VSGEATVAEL DGLEPDTEYT
760 770 780 790 800
VHVRAHVAGV DGPPASVVVR TAPEPVGRVS RLQILNASSD VLRITWVGVT
810 820 830 840 850
GATAYRLAWG RSEGGPMRHQ ILPGNTDSAE IRGLEGGVSY SVRVTALVGD
860 870 880 890 900
REGTPVSIVV TTPPEAPPAL GTLHVVQRGE HSLRLRWEPV PRAQGFLLHW
910 920 930 940 950
QPEGGQEQSR VLGPELSSYH LDGLEPATQY RVRLSVLGPA GEGPSAEVTA
960 970 980 990 1000
RTESPRVPSI ELRVVDTSID SVTLAWTPVS RASSYILSWR PLRGPGQEVP
1010 1020 1030 1040 1050
GSPQTLPGIS SSQRVTGLEP GVSYIFSLTP VLDGVRGPEA SVTQTPVCPR
1060 1070 1080 1090 1100
GLADVVFLPH ATQDNAHRAE ATRRVLERLV LALGPLGPQA VQVGLLSYSH
1110 1120 1130 1140 1150
RPSPLFPLNG SHDLGIILQR IRDMPYMDPS GNNLGTAVVT AHRYMLAPDA
1160 1170 1180 1190 1200
PGRRQHVPGV MVLLVDEPLR GDIFSPIREA QASGLNVVML GMAGADPEQL
1210 1220 1230 1240 1250
RRLAPGMDSV QTFFAVDDGP SLDQAVSGLA TALCQASFTT QPRPEPCPVY
1260 1270 1280 1290 1300
CPKGQKGEPG EMGLRGQVGP PGDPGLPGRT GAPGPQGPPG SATAKGERGF
1310 1320 1330 1340 1350
PGADGRPGSP GRAGNPGTPG APGLKGSPGL PGPRGDPGER GPRGPKGEPG
1360 1370 1380 1390 1400
APGQVIGGEG PGLPGRKGDP GPSGPPGPRG PLGDPGPRGP PGLPGTAMKG
1410 1420 1430 1440 1450
DKGDRGERGP PGPGEGGIAP GEPGLPGLPG SPGPQGPVGP PGKKGEKGDS
1460 1470 1480 1490 1500
EDGAPGLPGQ PGSPGEQGPR GPPGAIGPKG DRGFPGPLGE AGEKGERGPP
1510 1520 1530 1540 1550
GPAGSRGLPG VAGRPGAKGP EGPPGPTGRQ GEKGEPGRPG DPAVVGPAVA
1560 1570 1580 1590 1600
GPKGEKGDVG PAGPRGATGV QGERGPPGLV LPGDPGPKGD PGDRGPIGLT
1610 1620 1630 1640 1650
GRAGPPGDSG PPGEKGDPGR PGPPGPVGPR GRDGEVGEKG DEGPPGDPGL
1660 1670 1680 1690 1700
PGKAGERGLR GAPGVRGPVG EKGDQGDPGE DGRNGSPGSS GPKGDRGEPG
1710 1720 1730 1740 1750
PPGPPGRLVD TGPGAREKGE PGDRGQEGPR GPKGDPGLPG APGERGIEGF
1760 1770 1780 1790 1800
RGPPGPQGDP GVRGPAGEKG DRGPPGLDGR SGLDGKPGAA GPSGPNGAAG
1810 1820 1830 1840 1850
KAGDPGRDGL PGLRGEQGLP GPSGPPGLPG KPGEDGKPGL NGKNGEPGDP
1860 1870 1880 1890 1900
GEDGRKGEKG DSGASGREGR DGPKGERGAP GILGPQGPPG LPGPVGPPGQ
1910 1920 1930 1940 1950
GFPGVPGGTG PKGDRGETGS KGEQGLPGER GLRGEPGSVP NVDRLLETAG
1960 1970 1980 1990 2000
IKASALREIV ETWDESSGSF LPVPERRRGP KGDSGEQGPP GKEGPIGFPG
2010 2020 2030 2040 2050
ERGLKGDRGD PGPQGPPGLA LGERGPPGPS GLAGEPGKPG IPGLPGRAGG
2060 2070 2080 2090 2100
VGEAGRPGER GERGEKGERG EQGRDGPPGL PGTPGPPGPP GPKVSVDEPG
2110 2120 2130 2140 2150
PGLSGEQGPP GLKGAKGEPG SNGDQGPKGD RGVPGIKGDR GEPGPRGQDG
2160 2170 2180 2190 2200
NPGLPGERGM AGPEGKPGLQ GPRGPPGPVG GHGDPGPPGA PGLAGPAGPQ
2210 2220 2230 2240 2250
GPSGLKGEPG ETGPPGRGLT GPTGAVGLPG PPGPSGLVGP QGSPGLPGQV
2260 2270 2280 2290 2300
GETGKPGAPG RDGASGKDGD RGSPGVPGSP GLPGPVGPKG EPGPTGAPGQ
2310 2320 2330 2340 2350
AVVGLPGAKG EKGAPGGLAG DLVGEPGAKG DRGLPGPRGE KGEAGRAGEP
2360 2370 2380 2390 2400
GDPGEDGQKG APGPKGFKGD PGVGVPGSPG PPGPPGVKGD LGLPGLPGAP
2410 2420 2430 2440 2450
GVVGFPGQTG PRGEMGQPGP SGERGLAGPP GREGIPGPLG PPGPPGSVGP
2460 2470 2480 2490 2500
PGASGLKGDK GDPGVGLPGP RGERGEPGIR GEDGRPGQEG PRGLTGPPGS
2510 2520 2530 2540 2550
RGERGEKGDV GSAGLKGDKG DSAVILGPPG PRGAKGDMGE RGPRGLDGDK
2560 2570 2580 2590 2600
GPRGDNGDPG DKGSKGEPGD KGSAGLPGLR GLLGPQGQPG AAGIPGDPGS
2610 2620 2630 2640 2650
PGKDGVPGIR GEKGDVGFMG PRGLKGERGV KGACGLDGEK GDKGEAGPPG
2660 2670 2680 2690 2700
RPGLAGHKGE MGEPGVPGQS GAPGKEGLIG PKGDRGFDGQ PGPKGDQGEK
2710 2720 2730 2740 2750
GERGTPGIGG FPGPSGNDGS AGPPGPPGSV GPRGPEGLQG QKGERGPPGE
2760 2770 2780 2790 2800
RVVGAPGVPG APGERGEQGR PGPAGPRGEK GEAALTEDDI RGFVRQEMSQ
2810 2820 2830 2840 2850
HCACQGQFIA SGSRPLPSYA ADTAGSQLHA VPVLRVSHAE EEERVPPEDD
2860 2870 2880 2890 2900
EYSEYSEYSV EEYQDPEAPW DSDDPCSLPL DEGSCTAYTL RWYHRAVTGS
2910 2920 2930 2940
TEACHPFVYG GCGGNANRFG TREACERRCP PRVVQSQGTG TAQD
Length:2,944
Mass (Da):295,220
Last modified:February 1, 1996 - v2
Checksum:i96D8BF6D0FD387DB
GO
Isoform 2 (identifier: Q02388-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1869-1900: Missing.

Show »
Length:2,912
Mass (Da):292,267
Checksum:iC206B8957E4333A2
GO

Sequence cautioni

The sequence BAA02853 differs from that shown. Reason: Frameshift at positions 275, 282, 476, 494, 523, 541 and 543.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti195 – 197FFF → EFR in BAA02853 (PubMed:1567409).Curated3
Sequence conflicti369 – 371QQQ → EFR in AAA36357 (PubMed:1469284).Curated3
Sequence conflicti369 – 371QQQ → EFR in AAB24637 (PubMed:1469284).Curated3
Sequence conflicti518 – 519EL → DV in AAA36357 (PubMed:1469284).Curated2
Sequence conflicti518 – 519EL → DV in AAB24637 (PubMed:1469284).Curated2
Sequence conflicti529S → C in BAA02853 (PubMed:1567409).Curated1
Sequence conflicti541V → W in AAA36357 (PubMed:1469284).Curated1
Sequence conflicti541V → W in AAB24637 (PubMed:1469284).Curated1
Sequence conflicti851R → H in BAA02853 (PubMed:1567409).Curated1
Sequence conflicti893A → E in AAA58965 (PubMed:8088784).Curated1
Sequence conflicti893A → E in BAA02853 (PubMed:1567409).Curated1
Sequence conflicti893A → E in AAA96439 (PubMed:1871109).Curated1
Sequence conflicti1122R → L in BAA02853 (PubMed:1567409).Curated1
Sequence conflicti1463 – 1464SP → LR AA sequence (PubMed:1307247).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035740119T → P in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_001809142K → R in RDEB. Corresponds to variant rs121912856dbSNPEnsembl.1
Natural variantiVAR_048765547V → F.Corresponds to variant rs2229823dbSNPEnsembl.1
Natural variantiVAR_001810595P → L in RDEB. Corresponds to variant rs2228561dbSNPEnsembl.1
Natural variantiVAR_0487661120R → K.Corresponds to variant rs2228563dbSNPEnsembl.1
Natural variantiVAR_0018111277P → L in RDEB. Corresponds to variant rs35761247dbSNPEnsembl.1
Natural variantiVAR_0111601347G → R in RDEB; localized type; mild. 1 PublicationCorresponds to variant rs121912833dbSNPEnsembl.1
Natural variantiVAR_0357411364P → T in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0357421366R → W in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs147089666dbSNPEnsembl.1
Natural variantiVAR_0111611519G → D in TBDN; compound heterozygous with E-2251; clinically silent when heterozygous with a normal allele. 2 PublicationsCorresponds to variant rs121912835dbSNPEnsembl.1
Natural variantiVAR_0111621522G → E in DDEB. Corresponds to variant rs387906605dbSNPEnsembl.1
Natural variantiVAR_0018121557G → R in DDEB. 1
Natural variantiVAR_0155191595G → R in NDNC8. 1 PublicationCorresponds to variant rs121912840dbSNPEnsembl.1
Natural variantiVAR_0111631604G → R in RDEB. 1
Natural variantiVAR_0111641652G → R in RDEB; mitis type. 1 Publication1
Natural variantiVAR_0111651703G → E in RDEB. Corresponds to variant rs770304825dbSNPEnsembl.1
Natural variantiVAR_0111661772R → W in RDEB. 1
Natural variantiVAR_0111671776G → R in DDEB. 1
Natural variantiVAR_0018131782G → R in RDEB; mitis type. 1 PublicationCorresponds to variant rs374718902dbSNPEnsembl.1
Natural variantiVAR_0111681791G → E in EBP. 1 Publication1
Natural variantiVAR_0111691812G → R in RDEB. 1 Publication1
Natural variantiVAR_0155201815G → R in NDNC8. 1 PublicationCorresponds to variant rs121912841dbSNPEnsembl.1
Natural variantiVAR_0649941845G → R in RDEB. 1 Publication1
Natural variantiVAR_0649951981K → R in RDEB; mild form. 1 Publication1
Natural variantiVAR_0018141982G → W in HS-DEB. 1 Publication1
Natural variantiVAR_0018152003G → R in DDEB. 1 PublicationCorresponds to variant rs121912832dbSNPEnsembl.1
Natural variantiVAR_0111702006G → A in DDEB. 1
Natural variantiVAR_0111712006G → D in DDEB; interferes with collagen VII folding and secretion. 2 PublicationsCorresponds to variant rs121912842dbSNPEnsembl.1
Natural variantiVAR_0111722008R → C in HS-DEB; also in a milder localized type. 2 Publications1
Natural variantiVAR_0018162008R → G in HS-DEB. 2 Publications1
Natural variantiVAR_0111732009G → R in RDEB. 2 Publications1
Natural variantiVAR_0111742015G → E in DDEB; interferes with collagen VII folding and secretion. 2 PublicationsCorresponds to variant rs121912843dbSNPEnsembl.1
Natural variantiVAR_0018172025G → A in RDEB; mitis type. 1 PublicationCorresponds to variant rs766931219dbSNPEnsembl.1
Natural variantiVAR_0111752028G → A in DDEB. 1 Publication1
Natural variantiVAR_0111762028G → R in DDEB and EBP. 2 PublicationsCorresponds to variant rs762162799dbSNPEnsembl.1
Natural variantiVAR_0111772031G → S in RDEB; severe phenotype. 1 PublicationCorresponds to variant rs121912838dbSNPEnsembl.1
Natural variantiVAR_0018182034G → R in DDEB and EBDSC; interferes with collagen VII folding and secretion. 4 PublicationsCorresponds to variant rs121912844dbSNPEnsembl.1
Natural variantiVAR_0111782034G → W in DDEB. 2 Publications1
Natural variantiVAR_0111792037G → E in P-DEB. 1 PublicationCorresponds to variant rs121912846dbSNPEnsembl.1
Natural variantiVAR_0111802040G → D in DDEB. 1 Publication1
Natural variantiVAR_0018192040G → S in P-DEB. 1 PublicationCorresponds to variant rs121912829dbSNPEnsembl.1
Natural variantiVAR_0111812040G → V in DDEB. 1 Publication1
Natural variantiVAR_0018202043G → R in DDEB. 5 PublicationsCorresponds to variant rs121912836dbSNPEnsembl.1
Natural variantiVAR_0111822043G → W in DDEB; localized type. 1 Publication1
Natural variantiVAR_0111832046G → V in DDEB. 1
Natural variantiVAR_0018212049G → E in HS-DEB. 2 Publications1
Natural variantiVAR_0018222055G → E in DDEB. 1
Natural variantiVAR_0018232063R → W in HS-DEB; also in a mild form. 3 PublicationsCorresponds to variant rs121912849dbSNPEnsembl.1
Natural variantiVAR_0111842064G → R in DDEB. 2 Publications1
Natural variantiVAR_0649962069R → C in RDEB. 1 PublicationCorresponds to variant rs121912855dbSNPEnsembl.1
Natural variantiVAR_0649972070G → R in DDEB. 1 Publication1
Natural variantiVAR_0018252073G → D in RDEB; mitis type. 1 Publication1
Natural variantiVAR_0018262076G → D in DDEB; also in recessive forms. 1 PublicationCorresponds to variant rs121912850dbSNPEnsembl.1
Natural variantiVAR_0018272079G → E in DDEB. 1 Publication1
Natural variantiVAR_0111852079G → R in DDEB; associated with squamous cell carcinoma. 1 Publication1
Natural variantiVAR_0111862132G → D in RDEB. Corresponds to variant rs755669902dbSNPEnsembl.1
Natural variantiVAR_0111872192G → S in RDEB. 1
Natural variantiVAR_0111882207G → R in DDEB. 1 Publication1
Natural variantiVAR_0649982221G → A in RDEB. 1 Publication1
Natural variantiVAR_0018282242G → R in EBP. 1 PublicationCorresponds to variant rs121912837dbSNPEnsembl.1
Natural variantiVAR_0111892251G → E in TBDN; compound heterozygous with D-1519; leads to isolated toenail dystrophy when heterozygous with a normal allele. 1 PublicationCorresponds to variant rs121912834dbSNPEnsembl.1
Natural variantiVAR_0111902263G → V in RDEB. 1
Natural variantiVAR_0111912287G → R in RDEB; moderately severe phenotype when compound heterozygous with R-2316; leads to isolated toenail dystrophy when heterozygous with a normal allele. 1 PublicationCorresponds to variant rs121912839dbSNPEnsembl.1
Natural variantiVAR_0649992296G → E in RDEB. 1 Publication1
Natural variantiVAR_0111922316G → R in RDEB; moderately severe phenotype when compound heterozygous with R-2287. 1 Publication1
Natural variantiVAR_0111932348G → R in DDEB/RDEB; mild form. 1 Publication1
Natural variantiVAR_0018292351G → R in a patient with dystrophic epidermolysis bullosa; mitis type. Corresponds to variant rs1800013dbSNPEnsembl.1
Natural variantiVAR_0111942366G → S in RDEB; mitis type. 1 Publication1
Natural variantiVAR_0111952369G → S in EBP. 1 Publication1
Natural variantiVAR_0337862429P → L.Corresponds to variant rs2229822dbSNPEnsembl.1
Natural variantiVAR_0650002557G → R in RDEB. 1 Publication1
Natural variantiVAR_0018302569G → R in RDEB; severe and mitis type. 1
Natural variantiVAR_0018312575G → R in HS-DEB; also in a mild form. 2 PublicationsCorresponds to variant rs760891216dbSNPEnsembl.1
Natural variantiVAR_0650012622R → W in RDEB. 1 PublicationCorresponds to variant rs139318843dbSNPEnsembl.1
Natural variantiVAR_0018322623G → C in PR-DEB; dominant. 1 PublicationCorresponds to variant rs121912831dbSNPEnsembl.1
Natural variantiVAR_0018332653G → R in RDEB; mitis type. Corresponds to variant rs121912851dbSNPEnsembl.1
Natural variantiVAR_0018342671G → V in RDEB. 1
Natural variantiVAR_0111962674G → D in RDEB. 1
Natural variantiVAR_0018352674G → R in RDEB; mitis type. 1
Natural variantiVAR_0111972713G → D in DDEB. 1 PublicationCorresponds to variant rs369591910dbSNPEnsembl.1
Natural variantiVAR_0111982713G → R in EBP. 1 Publication1
Natural variantiVAR_0111992740G → A in RDEB. 1
Natural variantiVAR_0018362749G → R in HS-DEB; also in a mild form. Corresponds to variant rs121912853dbSNPEnsembl.1
Natural variantiVAR_0112002775G → S in RDEB; mitis type. 1 Publication1
Natural variantiVAR_0112012791R → W in DDEB. Corresponds to variant rs142566193dbSNPEnsembl.1
Natural variantiVAR_0018372798M → K in HS-DEB; also in a mild form. 1 PublicationCorresponds to variant rs121912828dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0240261869 – 1900Missing in isoform 2. CuratedAdd BLAST32

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23982 Genomic DNA. Translation: AAA58965.1.
L02870 mRNA. Translation: AAA75438.1.
D13694 mRNA. Translation: BAA02853.1. Frameshift.
M96984 mRNA. Translation: AAA36357.2.
S51236 mRNA. Translation: AAB24637.1.
M65158 mRNA. Translation: AAA96439.1.
L06862 mRNA. Translation: AAA89196.1.
CCDSiCCDS2773.1. [Q02388-1]
PIRiA54849.
RefSeqiNP_000085.1. NM_000094.3. [Q02388-1]
XP_011531639.1. XM_011533337.1. [Q02388-1]
UniGeneiHs.476218.

Genome annotation databases

EnsembliENST00000328333; ENSP00000332371; ENSG00000114270. [Q02388-1]
GeneIDi1294.
KEGGihsa:1294.
UCSCiuc003ctz.3. human. [Q02388-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23982 Genomic DNA. Translation: AAA58965.1.
L02870 mRNA. Translation: AAA75438.1.
D13694 mRNA. Translation: BAA02853.1. Frameshift.
M96984 mRNA. Translation: AAA36357.2.
S51236 mRNA. Translation: AAB24637.1.
M65158 mRNA. Translation: AAA96439.1.
L06862 mRNA. Translation: AAA89196.1.
CCDSiCCDS2773.1. [Q02388-1]
PIRiA54849.
RefSeqiNP_000085.1. NM_000094.3. [Q02388-1]
XP_011531639.1. XM_011533337.1. [Q02388-1]
UniGeneiHs.476218.

3D structure databases

ProteinModelPortaliQ02388.
SMRiQ02388.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107691. 17 interactors.
IntActiQ02388. 14 interactors.
MINTiMINT-1390694.
STRINGi9606.ENSP00000332371.

Protein family/group databases

MEROPSiI02.967.

PTM databases

iPTMnetiQ02388.
PhosphoSitePlusiQ02388.

Polymorphism and mutation databases

BioMutaiCOL7A1.
DMDMi1345650.

Proteomic databases

EPDiQ02388.
MaxQBiQ02388.
PaxDbiQ02388.
PeptideAtlasiQ02388.
PRIDEiQ02388.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000328333; ENSP00000332371; ENSG00000114270. [Q02388-1]
GeneIDi1294.
KEGGihsa:1294.
UCSCiuc003ctz.3. human. [Q02388-1]

Organism-specific databases

CTDi1294.
DisGeNETi1294.
GeneCardsiCOL7A1.
GeneReviewsiCOL7A1.
HGNCiHGNC:2214. COL7A1.
HPAiCAB016357.
HPA042420.
MalaCardsiCOL7A1.
MIMi120120. gene.
131705. phenotype.
131750. phenotype.
131850. phenotype.
132000. phenotype.
226600. phenotype.
604129. phenotype.
607523. phenotype.
neXtProtiNX_Q02388.
OpenTargetsiENSG00000114270.
Orphaneti158673. Acral dystrophic epidermolysis bullosa.
89841. Centripetalis recessive dystrophic epidermolysis bullosa.
89843. Dystrophic epidermolysis bullosa pruriginosa.
158676. Dystrophic epidermolysis bullosa, nails only.
89839. Epidermolysis bullosa simplex superficialis.
231568. Generalized dominant dystrophic epidermolysis bullosa.
79410. Pretibial dystrophic epidermolysis bullosa.
79409. Recessive dystrophic epidermolysis bullosa inversa.
89842. Recessive dystrophic epidermolysis bullosa-generalized other.
79408. Severe generalized recessive dystrophic epidermolysis bullosa.
79411. Transient bullous dermolysis of the newborn.
PharmGKBiPA26730.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00760000119000.
HOGENOMiHOG000111866.
HOVERGENiHBG051053.
InParanoidiQ02388.
KOiK16628.
OMAiDTEYTVH.
OrthoDBiEOG091G008X.
PhylomeDBiQ02388.
TreeFamiTF351645.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000114270-MONOMER.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474244. Extracellular matrix organization.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-2214320. Anchoring fibril formation.
R-HSA-3000157. Laminin interactions.
R-HSA-5694530. Cargo concentration in the ER.

Miscellaneous databases

ChiTaRSiCOL7A1. human.
GeneWikiiCollagen,_type_VII,_alpha_1.
GenomeRNAii1294.
PROiQ02388.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000114270.
CleanExiHS_COL7A1.
ExpressionAtlasiQ02388. baseline and differential.
GenevisibleiQ02388. HS.

Family and domain databases

CDDicd00063. FN3. 9 hits.
Gene3Di2.60.40.10. 9 hits.
3.40.50.410. 2 hits.
4.10.410.10. 1 hit.
InterProiIPR008160. Collagen.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR002223. Kunitz_BPTI.
IPR020901. Prtase_inh_Kunz-CS.
IPR002035. VWF_A.
[Graphical view]
PfamiPF01391. Collagen. 15 hits.
PF00041. fn3. 8 hits.
PF00014. Kunitz_BPTI. 1 hit.
PF00092. VWA. 2 hits.
[Graphical view]
PRINTSiPR00759. BASICPTASE.
SMARTiSM00060. FN3. 9 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 5 hits.
SSF53300. SSF53300. 2 hits.
SSF57362. SSF57362. 1 hit.
PROSITEiPS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
PS50853. FN3. 9 hits.
PS50234. VWFA. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO7A1_HUMAN
AccessioniPrimary (citable) accession number: Q02388
Secondary accession number(s): Q14054, Q16507
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 198 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.