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Q02388

- CO7A1_HUMAN

UniProt

Q02388 - CO7A1_HUMAN

Protein

Collagen alpha-1(VII) chain

Gene

COL7A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 174 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Sitei2886 – 28872Reactive bondBy similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. collagen catabolic process Source: Reactome
    3. epidermis development Source: ProtInc
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_118779. Extracellular matrix organization.
    REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13552. Integrin cell surface interactions.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150268. Anchoring fibril formation.
    REACT_150401. Collagen degradation.
    REACT_169262. Laminin interactions.

    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
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:2214. COL7A1.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: ProtInc
    2. collagen type VII trimer Source: ProtInc
    3. endoplasmic reticulum lumen Source: Reactome
    4. extracellular region Source: Reactome
    5. extracellular space Source: UniProt

    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) [MIM:131750]: 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.12 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1522 – 15221G → E in DDEB.
    VAR_011162
    Natural varianti1557 – 15571G → R in DDEB.
    VAR_001812
    Natural varianti1776 – 17761G → R in DDEB.
    VAR_011167
    Natural varianti2003 – 20031G → R in DDEB. 1 Publication
    VAR_001815
    Natural varianti2006 – 20061G → A in DDEB.
    VAR_011170
    Natural varianti2006 – 20061G → D in DDEB; interferes with collagen VII folding and secretion. 2 Publications
    VAR_011171
    Natural varianti2015 – 20151G → E in DDEB; interferes with collagen VII folding and secretion. 2 Publications
    VAR_011174
    Natural varianti2028 – 20281G → A in DDEB. 1 Publication
    VAR_011175
    Natural varianti2028 – 20281G → R in DDEB and EBP. 2 Publications
    VAR_011176
    Natural varianti2034 – 20341G → R in DDEB and EBDSC; interferes with collagen VII folding and secretion. 4 Publications
    VAR_001818
    Natural varianti2034 – 20341G → W in DDEB. 2 Publications
    VAR_011178
    Natural varianti2040 – 20401G → D in DDEB. 1 Publication
    VAR_011180
    Natural varianti2040 – 20401G → V in DDEB. 1 Publication
    VAR_011181
    Natural varianti2043 – 20431G → R in DDEB. 5 Publications
    VAR_001820
    Natural varianti2043 – 20431G → W in DDEB; localized type. 1 Publication
    VAR_011182
    Natural varianti2046 – 20461G → V in DDEB.
    VAR_011183
    Natural varianti2055 – 20551G → E in DDEB.
    VAR_001822
    Natural varianti2064 – 20641G → R in DDEB. 2 Publications
    VAR_011184
    Natural varianti2070 – 20701G → R in DDEB. 1 Publication
    VAR_064997
    Natural varianti2076 – 20761G → D in DDEB; also in recessive forms. 1 Publication
    VAR_001826
    Natural varianti2079 – 20791G → E in DDEB. 1 Publication
    VAR_001827
    Natural varianti2079 – 20791G → R in DDEB; associated with squamous cell carcinoma. 1 Publication
    VAR_011185
    Natural varianti2207 – 22071G → R in DDEB. 1 Publication
    VAR_011188
    Natural varianti2348 – 23481G → R in DDEB/RDEB; mild form. 1 Publication
    VAR_011193
    Natural varianti2713 – 27131G → D in DDEB. 1 Publication
    VAR_011197
    Natural varianti2791 – 27911R → W in DDEB.
    Corresponds to variant rs142566193 [ dbSNP | Ensembl ].
    VAR_011201
    Epidermolysis bullosa dystrophica, autosomal recessive (RDEB) [MIM:226600]: 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 to mild forms with limited and localized scarring, and less frequent extracutaneous manifestations. Mild forms include epidermolysis bullosa mitis and epidermolysis bullosa localisata.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti142 – 1421K → R in RDEB.
    VAR_001809
    Natural varianti595 – 5951P → L in RDEB.
    Corresponds to variant rs2228561 [ dbSNP | Ensembl ].
    VAR_001810
    Natural varianti1277 – 12771P → L in RDEB.
    Corresponds to variant rs35761247 [ dbSNP | Ensembl ].
    VAR_001811
    Natural varianti1347 – 13471G → R in RDEB; localized type; mild. 1 Publication
    VAR_011160
    Natural varianti1604 – 16041G → R in RDEB.
    VAR_011163
    Natural varianti1652 – 16521G → R in RDEB; mitis type. 1 Publication
    VAR_011164
    Natural varianti1703 – 17031G → E in RDEB.
    VAR_011165
    Natural varianti1772 – 17721R → W in RDEB.
    VAR_011166
    Natural varianti1782 – 17821G → R in RDEB; mitis type. 1 Publication
    VAR_001813
    Natural varianti1812 – 18121G → R in RDEB. 1 Publication
    VAR_011169
    Natural varianti1845 – 18451G → R in RDEB. 1 Publication
    VAR_064994
    Natural varianti1981 – 19811K → R in RDEB; mild form. 1 Publication
    VAR_064995
    Natural varianti2009 – 20091G → R in RDEB. 2 Publications
    VAR_011173
    Natural varianti2025 – 20251G → A in RDEB; mitis type. 1 Publication
    VAR_001817
    Natural varianti2031 – 20311G → S in RDEB; severe phenotype. 1 Publication
    VAR_011177
    Natural varianti2069 – 20691R → C in RDEB. 1 Publication
    VAR_064996
    Natural varianti2073 – 20731G → D in RDEB; mitis type. 1 Publication
    VAR_001825
    Natural varianti2132 – 21321G → D in RDEB.
    VAR_011186
    Natural varianti2192 – 21921G → S in RDEB.
    VAR_011187
    Natural varianti2263 – 22631G → V in RDEB.
    VAR_011190
    Natural varianti2296 – 22961G → E in RDEB. 1 Publication
    VAR_064999
    Natural varianti2348 – 23481G → R in DDEB/RDEB; mild form. 1 Publication
    VAR_011193
    Natural varianti2366 – 23661G → S in RDEB; mitis type. 1 Publication
    VAR_011194
    Natural varianti2557 – 25571G → R in RDEB. 1 Publication
    VAR_065000
    Natural varianti2569 – 25691G → R in RDEB; severe and mitis type.
    VAR_001830
    Natural varianti2622 – 26221R → W in RDEB. 1 Publication
    VAR_065001
    Natural varianti2653 – 26531G → R in RDEB; mitis type.
    VAR_001833
    Natural varianti2671 – 26711G → V in RDEB.
    VAR_001834
    Natural varianti2674 – 26741G → D in RDEB.
    VAR_011196
    Natural varianti2674 – 26741G → R in RDEB; mitis type.
    VAR_001835
    Natural varianti2740 – 27401G → A in RDEB.
    VAR_011199
    Natural varianti2775 – 27751G → S in RDEB; mitis type. 1 Publication
    VAR_011200
    Epidermolysis bullosa dystrophica, Pasini type (P-DEB) [MIM:131750]: A 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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2037 – 20371G → E in P-DEB. 1 Publication
    VAR_011179
    Natural varianti2040 – 20401G → S in P-DEB. 1 Publication
    VAR_001819
    Epidermolysis bullosa dystrophica, Hallopeau-Siemens type (HS-DEB) [MIM:226600]: The 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.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1982 – 19821G → W in HS-DEB. 1 Publication
    VAR_001814
    Natural varianti2008 – 20081R → C in HS-DEB; also in a milder localized type. 2 Publications
    VAR_011172
    Natural varianti2008 – 20081R → G in HS-DEB. 2 Publications
    VAR_001816
    Natural varianti2049 – 20491G → E in HS-DEB. 2 Publications
    VAR_001821
    Natural varianti2063 – 20631R → W in HS-DEB; also in a mild form. 3 Publications
    VAR_001823
    Natural varianti2575 – 25751G → R in HS-DEB; also in a mild form. 2 Publications
    VAR_001831
    Natural varianti2749 – 27491G → R in HS-DEB; also in a mild form.
    Corresponds to variant rs121912853 [ dbSNP | Ensembl ].
    VAR_001836
    Natural varianti2798 – 27981M → K in HS-DEB; also in a mild form; the anchoring fibrils may be absent. 1 Publication
    VAR_001837
    Transient bullous dermolysis of the newborn (TBDN) [MIM:131705]: 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1519 – 15191G → D in TBDN; compound heterozygous with E-2251; clinically silent when heterozygous with a normal allele. 2 Publications
    VAR_011161
    Natural varianti2251 – 22511G → E in TBDN; compound heterozygous with D-1519; leads to isolated toenail dystrophy when heterozygous with a normal allele. 1 Publication
    VAR_011189
    Epidermolysis bullosa dystrophica, pretibial type (PR-DEB) [MIM:131850]: 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2623 – 26231G → C in PR-DEB; dominant. 1 Publication
    VAR_001832
    Epidermolysis bullosa dystrophica, Bart type (B-DEB) [MIM:132000]: An autosomal dominant form of dystrophic epidermolysis bullosa characterized by congenital localized absence of skin, skin fragility and deformity of nails.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Epidermolysis bullosa pruriginosa (EBP) [MIM:604129]: 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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1791 – 17911G → E in EBP. 1 Publication
    VAR_011168
    Natural varianti2028 – 20281G → R in DDEB and EBP. 2 Publications
    VAR_011176
    Natural varianti2242 – 22421G → R in EBP. 1 Publication
    VAR_001828
    Natural varianti2369 – 23691G → S in EBP. 1 Publication
    VAR_011195
    Natural varianti2713 – 27131G → R in EBP. 1 Publication
    VAR_011198
    Nail disorder, non-syndromic congenital, 8 (NDNC8) [MIM:607523]: 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1595 – 15951G → R in NDNC8. 1 Publication
    VAR_015519
    Natural varianti1815 – 18151G → R in NDNC8. 1 Publication
    VAR_015520
    Epidermolysis bullosa dystrophica, with subcorneal cleavage (EBDSC) [MIM:131750]: 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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2034 – 20341G → R in DDEB and EBDSC; interferes with collagen VII folding and secretion. 4 Publications
    VAR_001818

    Keywords - Diseasei

    Disease mutation, Epidermolysis bullosa

    Organism-specific databases

    MIMi131705. phenotype.
    131750. phenotype.
    131850. phenotype.
    132000. phenotype.
    226600. phenotype.
    604129. phenotype.
    607523. phenotype.
    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.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 29442928Collagen alpha-1(VII) chainPRO_0000005761Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi786 – 7861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1109 – 11091N-linked (GlcNAc...)Sequence Analysis
    Modified residuei2167 – 216714-hydroxyproline1 Publication
    Modified residuei2176 – 217614-hydroxyproline1 Publication
    Modified residuei2185 – 218514-hydroxyproline1 Publication
    Modified residuei2188 – 218814-hydroxyproline1 Publication
    Modified residuei2625 – 262515-hydroxylysine; alternate1 Publication
    Glycosylationi2625 – 26251O-linked (Gal...); alternate
    Modified residuei2631 – 263115-hydroxylysine; alternate1 Publication
    Glycosylationi2631 – 26311O-linked (Gal...); alternate
    Disulfide bondi2634 – 2634InterchainPROSITE-ProRule annotation
    Modified residuei2664 – 266414-hydroxyproline1 Publication
    Modified residuei2667 – 266714-hydroxyproline1 Publication
    Modified residuei2673 – 267314-hydroxyproline1 Publication
    Disulfide bondi2802 – 2802InterchainPROSITE-ProRule annotation
    Disulfide bondi2804 – 2804InterchainPROSITE-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

    MaxQBiQ02388.
    PaxDbiQ02388.
    PRIDEiQ02388.

    PTM databases

    PhosphoSiteiQ02388.

    Expressioni

    Gene expression databases

    ArrayExpressiQ02388.
    BgeeiQ02388.
    CleanExiHS_COL7A1.
    GenevestigatoriQ02388.

    Organism-specific databases

    HPAiCAB016357.

    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. 8 interactions.
    IntActiQ02388. 6 interactions.
    MINTiMINT-1390694.
    STRINGi9606.ENSP00000332371.

    Structurei

    3D structure databases

    ProteinModelPortaliQ02388.
    SMRiQ02388. Positions 38-215, 233-1041, 1051-1237, 2876-2933.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 211174VWFA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini234 – 32996Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini330 – 41687Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini417 – 50791Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini510 – 59788Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini600 – 68788Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini688 – 77588Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini778 – 86689Fibronectin type-III 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini869 – 95789Fibronectin type-III 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini958 – 105194Fibronectin type-III 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1054 – 1229176VWFA 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2872 – 294473BPTI/Kunitz inhibitorPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni17 – 12531237Nonhelical region (NC1)Add
    BLAST
    Regioni1254 – 27841531Triple-helical regionAdd
    BLAST
    Regioni1254 – 1477224Interrupted collagenous regionAdd
    BLAST
    Regioni2785 – 2944160Nonhelical region (NC2)Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1170 – 11723Cell attachment siteSequence Analysis
    Motifi1334 – 13363Cell attachment siteSequence Analysis
    Motifi2008 – 20103Cell attachment siteSequence Analysis
    Motifi2553 – 25553Cell attachment siteSequence Analysis

    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

    eggNOGiNOG12793.
    HOGENOMiHOG000111866.
    HOVERGENiHBG051053.
    InParanoidiQ02388.
    KOiK16628.
    OMAiWHSGHGP.
    OrthoDBiEOG7CG6Z4.
    PhylomeDBiQ02388.
    TreeFamiTF351645.

    Family and domain databases

    Gene3Di2.60.40.10. 9 hits.
    3.40.50.410. 2 hits.
    4.10.410.10. 1 hit.
    InterProiIPR008160. Collagen.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR002223. Prot_inh_Kunz-m.
    IPR020901. Prtase_inh_Kunz-CS.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF01391. Collagen. 18 hits.
    PF00041. fn3. 9 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. Align

    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.

    « Hide

    MTLRLLVAAL CAGILAEAPR VRAQHRERVT CTRLYAADIV FLLDGSSSIG     50
    RSNFREVRSF LEGLVLPFSG AASAQGVRFA TVQYSDDPRT EFGLDALGSG 100
    GDVIRAIREL SYKGGNTRTG AAILHVADHV FLPQLARPGV PKVCILITDG 150
    KSQDLVDTAA QRLKGQGVKL FAVGIKNADP EELKRVASQP TSDFFFFVND 200
    FSILRTLLPL VSRRVCTTAG GVPVTRPPDD STSAPRDLVL SEPSSQSLRV 250
    QWTAASGPVT GYKVQYTPLT GLGQPLPSER QEVNVPAGET SVRLRGLRPL 300
    TEYQVTVIAL YANSIGEAVS GTARTTALEG PELTIQNTTA HSLLVAWRSV 350
    PGATGYRVTW RVLSGGPTQQ QELGPGQGSV LLRDLEPGTD YEVTVSTLFG 400
    RSVGPATSLM ARTDASVEQT LRPVILGPTS ILLSWNLVPE ARGYRLEWRR 450
    ETGLEPPQKV VLPSDVTRYQ LDGLQPGTEY RLTLYTLLEG HEVATPATVV 500
    PTGPELPVSP VTDLQATELP GQRVRVSWSP VPGATQYRII VRSTQGVERT 550
    LVLPGSQTAF DLDDVQAGLS YTVRVSARVG PREGSASVLT VRREPETPLA 600
    VPGLRVVVSD ATRVRVAWGP VPGASGFRIS WSTGSGPESS QTLPPDSTAT 650
    DITGLQPGTT YQVAVSVLRG REEGPAAVIV ARTDPLGPVR TVHVTQASSS 700
    SVTITWTRVP GATGYRVSWH SAHGPEKSQL VSGEATVAEL DGLEPDTEYT 750
    VHVRAHVAGV DGPPASVVVR TAPEPVGRVS RLQILNASSD VLRITWVGVT 800
    GATAYRLAWG RSEGGPMRHQ ILPGNTDSAE IRGLEGGVSY SVRVTALVGD 850
    REGTPVSIVV TTPPEAPPAL GTLHVVQRGE HSLRLRWEPV PRAQGFLLHW 900
    QPEGGQEQSR VLGPELSSYH LDGLEPATQY RVRLSVLGPA GEGPSAEVTA 950
    RTESPRVPSI ELRVVDTSID SVTLAWTPVS RASSYILSWR PLRGPGQEVP 1000
    GSPQTLPGIS SSQRVTGLEP GVSYIFSLTP VLDGVRGPEA SVTQTPVCPR 1050
    GLADVVFLPH ATQDNAHRAE ATRRVLERLV LALGPLGPQA VQVGLLSYSH 1100
    RPSPLFPLNG SHDLGIILQR IRDMPYMDPS GNNLGTAVVT AHRYMLAPDA 1150
    PGRRQHVPGV MVLLVDEPLR GDIFSPIREA QASGLNVVML GMAGADPEQL 1200
    RRLAPGMDSV QTFFAVDDGP SLDQAVSGLA TALCQASFTT QPRPEPCPVY 1250
    CPKGQKGEPG EMGLRGQVGP PGDPGLPGRT GAPGPQGPPG SATAKGERGF 1300
    PGADGRPGSP GRAGNPGTPG APGLKGSPGL PGPRGDPGER GPRGPKGEPG 1350
    APGQVIGGEG PGLPGRKGDP GPSGPPGPRG PLGDPGPRGP PGLPGTAMKG 1400
    DKGDRGERGP PGPGEGGIAP GEPGLPGLPG SPGPQGPVGP PGKKGEKGDS 1450
    EDGAPGLPGQ PGSPGEQGPR GPPGAIGPKG DRGFPGPLGE AGEKGERGPP 1500
    GPAGSRGLPG VAGRPGAKGP EGPPGPTGRQ GEKGEPGRPG DPAVVGPAVA 1550
    GPKGEKGDVG PAGPRGATGV QGERGPPGLV LPGDPGPKGD PGDRGPIGLT 1600
    GRAGPPGDSG PPGEKGDPGR PGPPGPVGPR GRDGEVGEKG DEGPPGDPGL 1650
    PGKAGERGLR GAPGVRGPVG EKGDQGDPGE DGRNGSPGSS GPKGDRGEPG 1700
    PPGPPGRLVD TGPGAREKGE PGDRGQEGPR GPKGDPGLPG APGERGIEGF 1750
    RGPPGPQGDP GVRGPAGEKG DRGPPGLDGR SGLDGKPGAA GPSGPNGAAG 1800
    KAGDPGRDGL PGLRGEQGLP GPSGPPGLPG KPGEDGKPGL NGKNGEPGDP 1850
    GEDGRKGEKG DSGASGREGR DGPKGERGAP GILGPQGPPG LPGPVGPPGQ 1900
    GFPGVPGGTG PKGDRGETGS KGEQGLPGER GLRGEPGSVP NVDRLLETAG 1950
    IKASALREIV ETWDESSGSF LPVPERRRGP KGDSGEQGPP GKEGPIGFPG 2000
    ERGLKGDRGD PGPQGPPGLA LGERGPPGPS GLAGEPGKPG IPGLPGRAGG 2050
    VGEAGRPGER GERGEKGERG EQGRDGPPGL PGTPGPPGPP GPKVSVDEPG 2100
    PGLSGEQGPP GLKGAKGEPG SNGDQGPKGD RGVPGIKGDR GEPGPRGQDG 2150
    NPGLPGERGM AGPEGKPGLQ GPRGPPGPVG GHGDPGPPGA PGLAGPAGPQ 2200
    GPSGLKGEPG ETGPPGRGLT GPTGAVGLPG PPGPSGLVGP QGSPGLPGQV 2250
    GETGKPGAPG RDGASGKDGD RGSPGVPGSP GLPGPVGPKG EPGPTGAPGQ 2300
    AVVGLPGAKG EKGAPGGLAG DLVGEPGAKG DRGLPGPRGE KGEAGRAGEP 2350
    GDPGEDGQKG APGPKGFKGD PGVGVPGSPG PPGPPGVKGD LGLPGLPGAP 2400
    GVVGFPGQTG PRGEMGQPGP SGERGLAGPP GREGIPGPLG PPGPPGSVGP 2450
    PGASGLKGDK GDPGVGLPGP RGERGEPGIR GEDGRPGQEG PRGLTGPPGS 2500
    RGERGEKGDV GSAGLKGDKG DSAVILGPPG PRGAKGDMGE RGPRGLDGDK 2550
    GPRGDNGDPG DKGSKGEPGD KGSAGLPGLR GLLGPQGQPG AAGIPGDPGS 2600
    PGKDGVPGIR GEKGDVGFMG PRGLKGERGV KGACGLDGEK GDKGEAGPPG 2650
    RPGLAGHKGE MGEPGVPGQS GAPGKEGLIG PKGDRGFDGQ PGPKGDQGEK 2700
    GERGTPGIGG FPGPSGNDGS AGPPGPPGSV GPRGPEGLQG QKGERGPPGE 2750
    RVVGAPGVPG APGERGEQGR PGPAGPRGEK GEAALTEDDI RGFVRQEMSQ 2800
    HCACQGQFIA SGSRPLPSYA ADTAGSQLHA VPVLRVSHAE EEERVPPEDD 2850
    EYSEYSEYSV EEYQDPEAPW DSDDPCSLPL DEGSCTAYTL RWYHRAVTGS 2900
    TEACHPFVYG GCGGNANRFG TREACERRCP PRVVQSQGTG TAQD 2944
    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 BAA02853.1 differs from that shown. Reason: Frameshift at positions 275, 282, 476, 494, 523, 541 and 543.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti195 – 1973FFF → EFR in BAA02853. (PubMed:1567409)Curated
    Sequence conflicti369 – 3713QQQ → EFR in AAA36357. (PubMed:1469284)Curated
    Sequence conflicti369 – 3713QQQ → EFR in AAB24637. (PubMed:1469284)Curated
    Sequence conflicti518 – 5192EL → DV in AAA36357. (PubMed:1469284)Curated
    Sequence conflicti518 – 5192EL → DV in AAB24637. (PubMed:1469284)Curated
    Sequence conflicti529 – 5291S → C in BAA02853. (PubMed:1567409)Curated
    Sequence conflicti541 – 5411V → W in AAA36357. (PubMed:1469284)Curated
    Sequence conflicti541 – 5411V → W in AAB24637. (PubMed:1469284)Curated
    Sequence conflicti851 – 8511R → H in BAA02853. (PubMed:1567409)Curated
    Sequence conflicti893 – 8931A → E in AAA58965. (PubMed:8088784)Curated
    Sequence conflicti893 – 8931A → E in BAA02853. (PubMed:1567409)Curated
    Sequence conflicti893 – 8931A → E in AAA96439. (PubMed:1871109)Curated
    Sequence conflicti1122 – 11221R → L in BAA02853. (PubMed:1567409)Curated
    Sequence conflicti1463 – 14642SP → LR AA sequence (PubMed:1307247)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti119 – 1191T → P in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035740
    Natural varianti142 – 1421K → R in RDEB.
    VAR_001809
    Natural varianti547 – 5471V → F.
    Corresponds to variant rs2229823 [ dbSNP | Ensembl ].
    VAR_048765
    Natural varianti595 – 5951P → L in RDEB.
    Corresponds to variant rs2228561 [ dbSNP | Ensembl ].
    VAR_001810
    Natural varianti1120 – 11201R → K.
    Corresponds to variant rs2228563 [ dbSNP | Ensembl ].
    VAR_048766
    Natural varianti1277 – 12771P → L in RDEB.
    Corresponds to variant rs35761247 [ dbSNP | Ensembl ].
    VAR_001811
    Natural varianti1347 – 13471G → R in RDEB; localized type; mild. 1 Publication
    VAR_011160
    Natural varianti1364 – 13641P → T in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035741
    Natural varianti1366 – 13661R → W in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035742
    Natural varianti1519 – 15191G → D in TBDN; compound heterozygous with E-2251; clinically silent when heterozygous with a normal allele. 2 Publications
    VAR_011161
    Natural varianti1522 – 15221G → E in DDEB.
    VAR_011162
    Natural varianti1557 – 15571G → R in DDEB.
    VAR_001812
    Natural varianti1595 – 15951G → R in NDNC8. 1 Publication
    VAR_015519
    Natural varianti1604 – 16041G → R in RDEB.
    VAR_011163
    Natural varianti1652 – 16521G → R in RDEB; mitis type. 1 Publication
    VAR_011164
    Natural varianti1703 – 17031G → E in RDEB.
    VAR_011165
    Natural varianti1772 – 17721R → W in RDEB.
    VAR_011166
    Natural varianti1776 – 17761G → R in DDEB.
    VAR_011167
    Natural varianti1782 – 17821G → R in RDEB; mitis type. 1 Publication
    VAR_001813
    Natural varianti1791 – 17911G → E in EBP. 1 Publication
    VAR_011168
    Natural varianti1812 – 18121G → R in RDEB. 1 Publication
    VAR_011169
    Natural varianti1815 – 18151G → R in NDNC8. 1 Publication
    VAR_015520
    Natural varianti1845 – 18451G → R in RDEB. 1 Publication
    VAR_064994
    Natural varianti1981 – 19811K → R in RDEB; mild form. 1 Publication
    VAR_064995
    Natural varianti1982 – 19821G → W in HS-DEB. 1 Publication
    VAR_001814
    Natural varianti2003 – 20031G → R in DDEB. 1 Publication
    VAR_001815
    Natural varianti2006 – 20061G → A in DDEB.
    VAR_011170
    Natural varianti2006 – 20061G → D in DDEB; interferes with collagen VII folding and secretion. 2 Publications
    VAR_011171
    Natural varianti2008 – 20081R → C in HS-DEB; also in a milder localized type. 2 Publications
    VAR_011172
    Natural varianti2008 – 20081R → G in HS-DEB. 2 Publications
    VAR_001816
    Natural varianti2009 – 20091G → R in RDEB. 2 Publications
    VAR_011173
    Natural varianti2015 – 20151G → E in DDEB; interferes with collagen VII folding and secretion. 2 Publications
    VAR_011174
    Natural varianti2025 – 20251G → A in RDEB; mitis type. 1 Publication
    VAR_001817
    Natural varianti2028 – 20281G → A in DDEB. 1 Publication
    VAR_011175
    Natural varianti2028 – 20281G → R in DDEB and EBP. 2 Publications
    VAR_011176
    Natural varianti2031 – 20311G → S in RDEB; severe phenotype. 1 Publication
    VAR_011177
    Natural varianti2034 – 20341G → R in DDEB and EBDSC; interferes with collagen VII folding and secretion. 4 Publications
    VAR_001818
    Natural varianti2034 – 20341G → W in DDEB. 2 Publications
    VAR_011178
    Natural varianti2037 – 20371G → E in P-DEB. 1 Publication
    VAR_011179
    Natural varianti2040 – 20401G → D in DDEB. 1 Publication
    VAR_011180
    Natural varianti2040 – 20401G → S in P-DEB. 1 Publication
    VAR_001819
    Natural varianti2040 – 20401G → V in DDEB. 1 Publication
    VAR_011181
    Natural varianti2043 – 20431G → R in DDEB. 5 Publications
    VAR_001820
    Natural varianti2043 – 20431G → W in DDEB; localized type. 1 Publication
    VAR_011182
    Natural varianti2046 – 20461G → V in DDEB.
    VAR_011183
    Natural varianti2049 – 20491G → E in HS-DEB. 2 Publications
    VAR_001821
    Natural varianti2055 – 20551G → E in DDEB.
    VAR_001822
    Natural varianti2063 – 20631R → W in HS-DEB; also in a mild form. 3 Publications
    VAR_001823
    Natural varianti2064 – 20641G → R in DDEB. 2 Publications
    VAR_011184
    Natural varianti2069 – 20691R → C in RDEB. 1 Publication
    VAR_064996
    Natural varianti2070 – 20701G → R in DDEB. 1 Publication
    VAR_064997
    Natural varianti2073 – 20731G → D in RDEB; mitis type. 1 Publication
    VAR_001825
    Natural varianti2076 – 20761G → D in DDEB; also in recessive forms. 1 Publication
    VAR_001826
    Natural varianti2079 – 20791G → E in DDEB. 1 Publication
    VAR_001827
    Natural varianti2079 – 20791G → R in DDEB; associated with squamous cell carcinoma. 1 Publication
    VAR_011185
    Natural varianti2132 – 21321G → D in RDEB.
    VAR_011186
    Natural varianti2192 – 21921G → S in RDEB.
    VAR_011187
    Natural varianti2207 – 22071G → R in DDEB. 1 Publication
    VAR_011188
    Natural varianti2221 – 22211G → A in a patient with recessive dystrophic epidermolysis bullosa. 1 Publication
    VAR_064998
    Natural varianti2242 – 22421G → R in EBP. 1 Publication
    VAR_001828
    Natural varianti2251 – 22511G → E in TBDN; compound heterozygous with D-1519; leads to isolated toenail dystrophy when heterozygous with a normal allele. 1 Publication
    VAR_011189
    Natural varianti2263 – 22631G → V in RDEB.
    VAR_011190
    Natural varianti2287 – 22871G → R in a compound heterozygote affected by moderately severe dystrophic epidermolysis bullosa; in combination with R-2316; leads to isolated toenail dystrophy when heterozygous with a normal allele. 1 Publication
    VAR_011191
    Natural varianti2296 – 22961G → E in RDEB. 1 Publication
    VAR_064999
    Natural varianti2316 – 23161G → R in a compound heterozygote affected by moderately severe dystrophic epidermolysis bullosa; in combination with R-2287. 1 Publication
    VAR_011192
    Natural varianti2348 – 23481G → R in DDEB/RDEB; mild form. 1 Publication
    VAR_011193
    Natural varianti2351 – 23511G → R in a patient with dystrophic epidermolysis bullosa; mitis type.
    Corresponds to variant rs1800013 [ dbSNP | Ensembl ].
    VAR_001829
    Natural varianti2366 – 23661G → S in RDEB; mitis type. 1 Publication
    VAR_011194
    Natural varianti2369 – 23691G → S in EBP. 1 Publication
    VAR_011195
    Natural varianti2429 – 24291P → L.
    Corresponds to variant rs2229822 [ dbSNP | Ensembl ].
    VAR_033786
    Natural varianti2557 – 25571G → R in RDEB. 1 Publication
    VAR_065000
    Natural varianti2569 – 25691G → R in RDEB; severe and mitis type.
    VAR_001830
    Natural varianti2575 – 25751G → R in HS-DEB; also in a mild form. 2 Publications
    VAR_001831
    Natural varianti2622 – 26221R → W in RDEB. 1 Publication
    VAR_065001
    Natural varianti2623 – 26231G → C in PR-DEB; dominant. 1 Publication
    VAR_001832
    Natural varianti2653 – 26531G → R in RDEB; mitis type.
    VAR_001833
    Natural varianti2671 – 26711G → V in RDEB.
    VAR_001834
    Natural varianti2674 – 26741G → D in RDEB.
    VAR_011196
    Natural varianti2674 – 26741G → R in RDEB; mitis type.
    VAR_001835
    Natural varianti2713 – 27131G → D in DDEB. 1 Publication
    VAR_011197
    Natural varianti2713 – 27131G → R in EBP. 1 Publication
    VAR_011198
    Natural varianti2740 – 27401G → A in RDEB.
    VAR_011199
    Natural varianti2749 – 27491G → R in HS-DEB; also in a mild form.
    Corresponds to variant rs121912853 [ dbSNP | Ensembl ].
    VAR_001836
    Natural varianti2775 – 27751G → S in RDEB; mitis type. 1 Publication
    VAR_011200
    Natural varianti2791 – 27911R → W in DDEB.
    Corresponds to variant rs142566193 [ dbSNP | Ensembl ].
    VAR_011201
    Natural varianti2798 – 27981M → K in HS-DEB; also in a mild form; the anchoring fibrils may be absent. 1 Publication
    VAR_001837

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1869 – 190032Missing in isoform 2. CuratedVSP_024026Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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]
    UniGeneiHs.476218.

    Genome annotation databases

    EnsembliENST00000328333; ENSP00000332371; ENSG00000114270. [Q02388-1]
    GeneIDi1294.
    KEGGihsa:1294.
    UCSCiuc003ctz.2. human. [Q02388-1]

    Polymorphism databases

    DMDMi1345650.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS2773.1. [Q02388-1 ]
    PIRi A54849.
    RefSeqi NP_000085.1. NM_000094.3. [Q02388-1 ]
    UniGenei Hs.476218.

    3D structure databases

    ProteinModelPortali Q02388.
    SMRi Q02388. Positions 38-215, 233-1041, 1051-1237, 2876-2933.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107691. 8 interactions.
    IntActi Q02388. 6 interactions.
    MINTi MINT-1390694.
    STRINGi 9606.ENSP00000332371.

    Protein family/group databases

    MEROPSi I02.967.

    PTM databases

    PhosphoSitei Q02388.

    Polymorphism databases

    DMDMi 1345650.

    Proteomic databases

    MaxQBi Q02388.
    PaxDbi Q02388.
    PRIDEi Q02388.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000328333 ; ENSP00000332371 ; ENSG00000114270 . [Q02388-1 ]
    GeneIDi 1294.
    KEGGi hsa:1294.
    UCSCi uc003ctz.2. human. [Q02388-1 ]

    Organism-specific databases

    CTDi 1294.
    GeneCardsi GC03M048576.
    GeneReviewsi COL7A1.
    HGNCi HGNC:2214. COL7A1.
    HPAi CAB016357.
    MIMi 120120. gene.
    131705. phenotype.
    131750. phenotype.
    131850. phenotype.
    132000. phenotype.
    226600. phenotype.
    604129. phenotype.
    607523. phenotype.
    neXtProti NX_Q02388.
    Orphaneti 158673. 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.
    PharmGKBi PA26730.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000111866.
    HOVERGENi HBG051053.
    InParanoidi Q02388.
    KOi K16628.
    OMAi WHSGHGP.
    OrthoDBi EOG7CG6Z4.
    PhylomeDBi Q02388.
    TreeFami TF351645.

    Enzyme and pathway databases

    Reactomei REACT_118779. Extracellular matrix organization.
    REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13552. Integrin cell surface interactions.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150268. Anchoring fibril formation.
    REACT_150401. Collagen degradation.
    REACT_169262. Laminin interactions.

    Miscellaneous databases

    ChiTaRSi COL7A1. human.
    GeneWikii Collagen,_type_VII,_alpha_1.
    GenomeRNAii 1294.
    NextBioi 5251.
    PROi Q02388.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q02388.
    Bgeei Q02388.
    CleanExi HS_COL7A1.
    Genevestigatori Q02388.

    Family and domain databases

    Gene3Di 2.60.40.10. 9 hits.
    3.40.50.410. 2 hits.
    4.10.410.10. 1 hit.
    InterProi IPR008160. Collagen.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR002223. Prot_inh_Kunz-m.
    IPR020901. Prtase_inh_Kunz-CS.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF01391. Collagen. 18 hits.
    PF00041. fn3. 9 hits.
    PF00014. Kunitz_BPTI. 1 hit.
    PF00092. VWA. 2 hits.
    [Graphical view ]
    PRINTSi PR00759. BASICPTASE.
    SMARTi SM00060. FN3. 9 hits.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 5 hits.
    SSF53300. SSF53300. 2 hits.
    SSF57362. SSF57362. 1 hit.
    PROSITEi PS00280. BPTI_KUNITZ_1. 1 hit.
    PS50279. BPTI_KUNITZ_2. 1 hit.
    PS50853. FN3. 9 hits.
    PS50234. VWFA. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structural organization of the human type VII collagen gene (COL7A1), composed of more exons than any previously characterized gene."
      Christiano A.M., Hoffman G.G., Chung-Honet L.C., Lee S., Cheng W., Uitto J., Greenspan D.S.
      Genomics 21:169-179(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
      Tissue: Placenta.
    2. "Cloning of human type VII collagen. Complete primary sequence of the alpha 1(VII) chain and identification of intragenic polymorphisms."
      Christiano A.M., Greenspan D.S., Lee S., Uitto J.
      J. Biol. Chem. 269:20256-20262(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "The large non-collagenous domain (NC-1) of type VII collagen is amino-terminal and chimeric. Homology to cartilage matrix protein, the type III domains of fibronectin and the A domains of von Willebrand factor."
      Christiano A.M., Rosenbaum L.M., Chung-Honet L.C., Parente M.G., Woodley D.T., Pan T.C., Zhang R.Z., Chu M.-L., Burgeson R.E., Uitto J.
      Hum. Mol. Genet. 1:475-481(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 128-1493, PARTIAL PROTEIN SEQUENCE.
    4. "Molecular cloning and characterization of type VII collagen cDNA."
      Tanaka T., Takahashi K., Furukawa F., Imamura S.
      Biochem. Biophys. Res. Commun. 183:958-963(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 195-1275.
      Tissue: Keratinocyte.
    5. "Noncollagenous (NC1) domain of collagen VII resembles multidomain adhesion proteins involved in tissue-specific organization of extracellular matrix."
      Gammon W.R., Abernethy M.L., Padilla K.M., Prisayanh P.S., Cook M.E., Wright J., Briggaman R.A., Hunt S.W. III
      J. Invest. Dermatol. 99:691-696(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 369-1255.
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 815-1439.
    7. "The carboxyl-terminal half of type VII collagen, including the non-collagenous NC-2 domain and intron/exon organization of the corresponding region of the COL7A1 gene."
      Greenspan D.S.
      Hum. Mol. Genet. 2:273-278(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2395-2944.
    8. "Cleavage of type VII collagen by interstitial collagenase and type IV collagenase (gelatinase) derived from human skin."
      Seltzer J.L., Eisen A.Z., Bauer E.A., Morris N.P., Glanville R.W., Burgeson R.E.
      J. Biol. Chem. 264:3822-3826(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, HYDROXYLATION.
    9. "TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites."
      Saito K., Chen M., Bard F., Chen S., Zhou H., Woodley D., Polischuk R., Schekman R., Malhotra V.
      Cell 136:891-902(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MIA3.
    10. "Molecular basis of dystrophic epidermolysis bullosa: mutations in the type VII collagen gene (COL7A1)."
      Jaervikallio A., Pulkkinen L., Uitto J.
      Hum. Mutat. 10:338-347(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Epidermolysis bullosa simplex superficialis. A new variant of epidermolysis bullosa characterized by subcorneal skin cleavage mimicking peeling skin syndrome."
      Fine J.-D., Johnson L., Wright T.
      Arch. Dermatol. 125:633-638(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EBDSC ARG-2034.
    13. "A missense mutation in type VII collagen in two affected siblings with recessive dystrophic epidermolysis bullosa."
      Christiano A.M., Greenspan D.S., Hoffman G.G., Zhang X., Tamai Y., Lin A.N., Dietz H.C., Hovnanian A., Uitto J.
      Nat. Genet. 4:62-66(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HS-DEB LYS-2798.
    14. "Dominant dystrophic epidermolysis bullosa: identification of a Gly-->Ser substitution in the triple-helical domain of type VII collagen."
      Christiano A.M., Ryynaenen M., Uitto J.
      Proc. Natl. Acad. Sci. U.S.A. 91:3549-3553(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT P-DEB SER-2040.
    15. "Pretibial epidermolysis bullosa: genetic linkage to COL7A1 and identification of a glycine-to-cysteine substitution in the triple-helical domain of type VII collagen."
      Christiano A.M., Lee J.Y.-Y., Chen W.J., Laforgia S., Uitto J.
      Hum. Mol. Genet. 4:1579-1583(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PR-DEB CYS-2623.
    16. "A glycine-to-arginine substitution in the triple-helical domain of type VII collagen in a family with dominant dystrophic epidermolysis bullosa."
      Christiano A.M., Morricone A., Paradisi M., Angelo C., Mazzanti C., Cavalieri R., Uitto J.
      J. Invest. Dermatol. 104:438-440(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DDEB ARG-2043.
    17. "Glycine substitutions in the triple-helical region of type VII collagen result in a spectrum of dystrophic epidermolysis bullosa phenotypes and patterns of inheritance."
      Christiano A.M., McGrath J.A., Tan K.C., Uitto J.
      Am. J. Hum. Genet. 58:671-681(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DEB.
    18. "Molecular basis of recessive dystrophic epidermolysis bullosa: genotype/phenotype correlation in a case of moderate clinical severity."
      Shimizu H., McGrath J.A., Christiano A.M., Nishikawa T., Uitto J.
      J. Invest. Dermatol. 106:119-124(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HS-DEB ARG-2575.
    19. "Influence of the second COL7A1 mutation in determining the phenotypic severity of recessive dystrophic epidermolysis bullosa."
      Christiano A.M., McGrath J.A., Uitto J.
      J. Invest. Dermatol. 106:766-770(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RDEB ARG-1782.
    20. "Clinicopathological correlations of compound heterozygous COL7A1 mutations in recessive dystrophic epidermolysis bullosa."
      Dunnill M.G.S., McGrath J.A., Richards A.J., Christiano A.M., Uitto J., Pope F.M., Eady R.A.J.
      J. Invest. Dermatol. 107:171-177(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RDEB ASP-2073.
    21. "Characterization of 18 new mutations in COL7A1 in recessive dystrophic epidermolysis bullosa provides evidence for distinct molecular mechanisms underlying defective anchoring fibril formation."
      Hovnanian A., Rochat A., Bodemer C., Petit E., Rivers C.A., Prost C., Fraitag S., Christiano A.M., Uitto J., Lathrop M., Barrandon Y., de Prost Y.
      Am. J. Hum. Genet. 61:599-610(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HS-DEB TRP-1982; GLY-2008; ALA-2025; GLU-2049; TRP-2063 AND ARG-2575.
    22. "Identification of a glycine substitution and a splice site mutation in the type VII collagen gene in a proband with mitis recessive dystrophic epidermolysis bullosa."
      Cserhalmi-Friedman P.B., Karpati S., Horvath A., Christiano A.M.
      Arch. Dermatol. Res. 289:640-645(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RDEB ARG-1652.
    23. "Modulation of disease severity of dystrophic epidermolysis bullosa by a splice site mutation in combination with a missense mutation in the COL7A1 gene."
      Winberg J.-O., Hammami-Hauasli N., Nilssen O., Anton-Lamprecht I., Naylor S.L., Kerbacher K., Zimmermann M., Krajci P., Gedde-Dahl T. Jr., Bruckner-Tuderman L.
      Hum. Mol. Genet. 6:1125-1135(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RDEB ARG-2009, VARIANT DDEB ARG-2043.
    24. "Some, but not all, glycine substitution mutations in COL7A1 result in intracellular accumulation of collagen VII, loss of anchoring fibrils, and skin blistering."
      Hammami-Hauasli N., Schumann H., Raghunath M., Kilgus O., Luethi U., Luger T., Bruckner-Tuderman L.
      J. Biol. Chem. 273:19228-19234(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DDEB ASP-1519; ASP-2006; GLU-2015 AND ARG-2034.
    25. "Novel COL7A1 mutations in dystrophic forms of epidermolysis bullosa."
      Kon A., Pulkkinen L., Ishida-Yamamoto A., Hashimoto I., Uitto J.
      J. Invest. Dermatol. 111:534-537(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HS-DEB CYS-2008, VARIANT DDEB ARG-2207, VARIANT RDEB SER-2775.
    26. "Compound heterozygosity for a recessive glycine substitution and a splice site mutation in the COL7A1 gene causes an unusually mild form of localized recessive dystrophic epidermolysis bullosa."
      Terracina M., Posteraro P., Schubert M., Sonego G., Atzori F., Zambruno G., Bruckner-Tuderman L., Castiglia D.
      J. Invest. Dermatol. 111:744-750(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RDEB ARG-1347.
    27. "Novel and de novo glycine substitution mutations in the type VII collagen gene (COL7A1) in dystrophic epidermolysis bullosa: implications for genetic counseling."
      Rouan F., Pulkkinen L., Jonkman M.F., Bauer J.W., Cserhalmi-Friedman P.B., Christiano A.M., Uitto J.
      J. Invest. Dermatol. 111:1210-1213(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DDEB TRP-2034; VAL-2040; ARG-2043; ARG-2064 AND ASP-2713.
    28. "Transient bullous dermolysis of the newborn associated with compound heterozygosity for recessive and dominant COL7A1 mutations."
      Hammami-Hauasli N., Raghunath M., Kuester W., Bruckner-Tuderman L.
      J. Invest. Dermatol. 111:1214-1219(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TBDN ASP-1519 AND GLU-2251.
    29. "Diagnostic dilemma of 'sporadic' cases of dystrophic epidermolysis bullosa: a new dominant or mitis recessive mutation?"
      Hashimoto I., Kon A., Tamai K., Uitto J.
      Exp. Dermatol. 8:140-142(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DDEB/RDEB TRP-2063 AND SER-2366, VARIANT DDEB GLU-2079.
    30. "Identification of a de novo glycine substitution in the type VII collagen gene in a proband with mild dystrophic epidermolysis bullosa."
      Cserhalmi-Friedman P.B., Grossman J., Karpati S., Ahmad W., Horvath A., Christiano A.M.
      Exp. Dermatol. 8:143-145(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DDEB/RDEB ARG-2348.
    31. "Squamous cell carcinoma in a family with dominant dystrophic epidermolysis bullosa: a molecular genetic study."
      Christiano A.M., Crollick J., Pincus S., Uitto J.
      Exp. Dermatol. 8:146-152(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DDEB ARG-2079.
    32. "Clustering of COL7A1 mutations in exon 73: implications for mutation analysis in dystrophic epidermolysis bullosa."
      Mecklenbeck S., Hammami-Hauasli N., Hoepfner B., Schumann H., Kramer A., Kuester W., Bruckner-Tuderman L.
      J. Invest. Dermatol. 112:398-400(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DDEB ASP-2006; GLU-2015; ARG-2034; TRP-2034; ARG-2043 AND TRP-2043, VARIANTS HS-DEB CYS-2008 AND GLY-2008, VARIANT RDEB ARG-2009.
    33. "Dominant dystrophic epidermolysis bullosa (Pasini) caused by a novel glycine substitution mutation in the type VII collagen gene (COL7A1)."
      Jonkman M.F., Moreno G., Rouan F., Oranje A.P., Pulkkinen L., Uitto J.
      J. Invest. Dermatol. 112:815-817(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT P-DEB GLU-2037.
    34. Cited for: VARIANTS EBP GLU-1791; ARG-2242; SER-2369 AND ARG-2713.
    35. "Compound heterozygosity for silent and dominant glycine substitution mutations in COL7A1 leads to a marked transient intracytoplasmic retention of procollagen VII and a moderately severe dystrophic epidermolysis bullosa phenotype."
      Shimizu H., Hammami-Hauasli N., Hatta N., Nishikawa T., Bruckner-Tuderman L.
      J. Invest. Dermatol. 113:419-421(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARG-2287 AND ARG-2316.
    36. "Comparative mutation detection screening of the type VII collagen gene (COL7A1) using the protein truncation test, fluorescent chemical cleavage of mismatch, and conformation sensitive gel electrophoresis."
      Whittock N.V., Ashton G.H.S., Mohammedi R., Mellerio J.E., Mathew C.G., Abbs S.J., Eady R.A.J., McGrath J.A.
      J. Invest. Dermatol. 113:673-686(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DEB.
    37. "A de novo glycine substitution mutation in the collagenous domain of COL7A1 in dominant dystrophic epidermolysis bullosa."
      Lee J.Y.-Y., Li C., Chao S.-C., Pulkkinen L., Uitto J.
      Arch. Dermatol. Res. 292:159-163(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DDEB ARG-2028.
    38. "Glycine substitution mutations by different amino acids in the same codon of COL7A1 lead to heterogeneous clinical phenotypes of dominant dystrophic epidermolysis bullosa."
      Murata T., Masunaga T., Shimizu H., Takizawa Y., Ishiko A., Hatta N., Nishikawa T.
      Arch. Dermatol. Res. 292:477-481(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DDEB ALA-2028, VARIANT EBP ARG-2028.
    39. "Combination of novel premature termination codon and glycine substitution mutations in COL7A1 leads to moderately severe recessive dystrophic epidermolysis bullosa."
      Masunaga T., Shimizu H., Takizawa Y., Uitto J., Nishikawa T.
      J. Invest. Dermatol. 114:204-205(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RDEB ARG-1812.
    40. "Generalized dystrophic epidermolysis bullosa: identification of a novel, homozygous glycine substitution, G2031S, in exon 73 of COL7A1 in monozygous triplets."
      Nordal E.J., Mecklenbeck S., Hausser I., Skranes J., Bruckner-Tuderman L., Gedde-Dahl T. Jr.
      Br. J. Dermatol. 144:151-157(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RDEB SER-2031.
    41. "Toenail dystrophy with COL7A1 glycine substitution mutations segregates as an autosomal dominant trait in 2 families with dystrophic epidermolysis bullosa."
      Sato-Matsumura K.C., Yasukawa K., Tomita Y., Shimizu H.
      Arch. Dermatol. 138:269-271(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS NDNC8 ARG-1595 AND ARG-1815.
    42. "EB simplex superficialis resulting from a mutation in the type VII collagen gene."
      Martinez-Mir A., Liu J., Gordon D., Weiner M.S., Ahmad W., Fine J.D., Ott J., Gilliam T.C., Christiano A.M.
      J. Invest. Dermatol. 118:547-549(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EBDSC ARG-2034.
    43. Cited for: VARIANTS [LARGE SCALE ANALYSIS] PRO-119; THR-1364 AND TRP-1366.
    44. "Novel human pathological mutations. Gene symbol: COL7A1. Disease: Epidermolysis bullosa dystrophica."
      Garcia M., Escamez M.J., Cuadrado-Corrales N., Sanchez-Jimeno C., Illera N., Lopez-Martinez M.A., Trujillo-Tiebas M.J., Ayuso C., Del Rio M.
      Hum. Genet. 127:116-117(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ALA-2221.
    45. "Analysis of the COL7A1 gene in Czech patients with dystrophic epidermolysis bullosa reveals novel and recurrent mutations."
      Jerabkova B., Kopeckova L., Buckova H., Vesely K., Valickova J., Fajkusova L.
      J. Dermatol. Sci. 59:136-140(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RDEB ARG-1845; ARG-1981; GLU-2049; TRP-2063; CYS-2069; GLU-2296; ARG-2557 AND TRP-2622, VARIANTS DDEB ARG-2003; ASP-2040; ARG-2043; ARG-2064; ARG-2070 AND ASP-2076.

    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: October 1, 2014
    This is version 174 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

    External Data

    Dasty 3