COHA1_HUMAN
ID COHA1_HUMAN Reviewed; 1497 AA.
AC Q9UMD9; Q02802; Q5JV36; Q99018; Q9NQK9; Q9UC14;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Collagen alpha-1(XVII) chain;
DE AltName: Full=180 kDa bullous pemphigoid antigen 2;
DE AltName: Full=Bullous pemphigoid antigen 2;
DE Contains:
DE RecName: Full=120 kDa linear IgA disease antigen;
DE AltName: Full=120 kDa linear IgA dermatosis antigen;
DE AltName: Full=Linear IgA disease antigen 1;
DE Short=LAD-1;
DE Contains:
DE RecName: Full=97 kDa linear IgA disease antigen;
DE AltName: Full=97 kDa linear IgA bullous dermatosis antigen;
DE Short=97 kDa LAD antigen;
DE Short=97-LAD;
DE AltName: Full=Linear IgA bullous disease antigen of 97 kDa;
DE Short=LABD97;
GN Name=COL17A1; Synonyms=BP180, BPAG2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND VARIANT
RP SER-428.
RC TISSUE=Foreskin;
RX PubMed=1324962; DOI=10.1111/1523-1747.ep12616580;
RA Giudice G.J., Emery D.J., Diaz L.A.;
RT "Cloning and primary structural analysis of the bullous pemphigoid
RT autoantigen, BP180.";
RL J. Invest. Dermatol. 99:243-250(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS ILE-231;
RP THR-238; SER-428; VAL-703 AND GLY-1370.
RX PubMed=9012408;
RA Gatalica B., Pulkkinen L., Li K., Kuokkanen K., Ryynaenen M., McGrath J.A.,
RA Uitto J.;
RT "Cloning of the human type XVII collagen gene (COL17A1), and detection of
RT novel mutations in generalized atrophic benign epidermolysis bullosa.";
RL Am. J. Hum. Genet. 60:352-365(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-390, AND VARIANT MET-210.
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 508-856, AND TISSUE SPECIFICITY.
RX PubMed=1748679; DOI=10.1016/s0021-9258(18)54393-3;
RA Li K.H., Sawamura D., Giudice G.J., Diaz L.A., Mattei M.-G., Chu M.-L.,
RA Uitto J.;
RT "Genomic organization of collagenous domains and chromosomal assignment of
RT human 180-kDa bullous pemphigoid antigen-2, a novel collagen of stratified
RT squamous epithelium.";
RL J. Biol. Chem. 266:24064-24069(1991).
RN [6]
RP PROTEIN SEQUENCE OF 524-535.
RX PubMed=14675210; DOI=10.1046/j.1523-1747.2003.12607.x;
RA Hirako Y., Nishizawa Y., Sitaru C., Opitz A., Marcus K., Meyer H.E.,
RA Butt E., Owaribe K., Zillikens D.;
RT "The 97-kDa (LABD97) and 120-kDa (LAD-1) fragments of bullous pemphigoid
RT antigen 180/type XVII collagen have different N-termini.";
RL J. Invest. Dermatol. 121:1554-1556(2003).
RN [7]
RP PROTEIN SEQUENCE OF 531-546; 554-565; 585-605; 647-666; 680-688; 689-703;
RP 755-765; 842-860; 880-891; 1016-1028; 1062-1069; 1102-1108; 1134-1142;
RP 1227-1247 AND 1248-1260.
RX PubMed=9506436; DOI=10.1046/j.1523-1747.1998.00129.x;
RA Zone J.J., Taylor T.B., Meyer L.J., Petersen M.J.;
RT "The 97 kDa linear IgA bullous disease antigen is identical to a portion of
RT the extracellular domain of the 180 kDa bullous pemphigoid antigen,
RT BPAg2.";
RL J. Invest. Dermatol. 110:207-210(1998).
RN [8]
RP SUBCELLULAR LOCATION, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8618013; DOI=10.1111/1523-1747.ep12345782;
RA Marinkovich M.P., Taylor T.B., Keene D.R., Burgeson R.E., Zone J.J.;
RT "LAD-1, the linear IgA bullous dermatosis autoantigen, is a novel 120-kDa
RT anchoring filament protein synthesized by epidermal cells.";
RL J. Invest. Dermatol. 106:734-738(1996).
RN [9]
RP ERRATUM OF PUBMED:8618013.
RA Marinkovich M.P., Taylor T.B., Keene D.R., Burgeson R.E., Zone J.J.;
RL J. Invest. Dermatol. 106:1343-1343(1996).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=8618014; DOI=10.1111/1523-1747.ep12345793;
RA Ishiko A., Shimizu H., Masunaga T., Hashimoto T., Dmochowski M.,
RA Wojnarowska F., Bhogal B.S., Black M.M., Nishikawa T.;
RT "97-kDa linear IgA bullous dermatosis (LAD) antigen localizes to the lamina
RT lucida of the epidermal basement membrane.";
RL J. Invest. Dermatol. 106:739-743(1996).
RN [11]
RP SUBCELLULAR LOCATION.
RA Limardo M., Arffman A., Aho S., Utto J.;
RT "Evidence that the 180-kD bullous pemphigoid antigen is a transmembrane
RT collagen, type XVII, in a triple-helical conformation and in type II
RT transmembrane topography.";
RL J. Invest. Dermatol. 106:860-860(1996).
RN [12]
RP SUBUNIT, PROTEOLYTIC PROCESSING, GLYCOSYLATION AT ASN-1421, AND DOMAINS.
RX PubMed=9748270; DOI=10.1074/jbc.273.40.25937;
RA Schaecke H., Schumann H., Hammami-Hauasli N., Raghunath M.,
RA Bruckner-Tuderman L.;
RT "Two forms of collagen XVII in keratinocytes. A full-length transmembrane
RT protein and a soluble ectodomain.";
RL J. Biol. Chem. 273:25937-25943(1998).
RN [13]
RP INTERACTION WITH DSP.
RX PubMed=10637308; DOI=10.1091/mbc.11.1.277;
RA Hopkinson S.B., Jones J.C.;
RT "The N terminus of the transmembrane protein BP180 interacts with the N-
RT terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage
RT to the cell surface at the site of the hemidesmosome.";
RL Mol. Biol. Cell 11:277-286(2000).
RN [14]
RP SHEDDING.
RX PubMed=12356719; DOI=10.1093/emboj/cdf532;
RA Franzke C.-W., Tasanen K., Schaecke H., Zhou Z., Tryggvason K., Mauch C.,
RA Zigrino P., Sunnarborg S., Lee D.C., Fahrenholz F., Bruckner-Tuderman L.;
RT "Transmembrane collagen XVII, an epithelial adhesion protein, is shed from
RT the cell surface by ADAMs.";
RL EMBO J. 21:5026-5035(2002).
RN [15]
RP FUNCTION, INTERACTION WITH DSP; DST; ITGB4 AND PLEC, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12482924; DOI=10.1242/jcs.00241;
RA Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.;
RT "Analysis of the interactions between BP180, BP230, plectin and the
RT integrin alpha6beta4 important for hemidesmosome assembly.";
RL J. Cell Sci. 116:387-399(2003).
RN [16]
RP PHOSPHORYLATION AT SER-544.
RX PubMed=17545155; DOI=10.1074/jbc.m701937200;
RA Zimina E.P., Fritsch A., Schermer B., Bakulina A.Y., Bashkurov M.,
RA Benzing T., Bruckner-Tuderman L.;
RT "Extracellular phosphorylation of collagen XVII by ecto-casein kinase 2
RT inhibits ectodomain shedding.";
RL J. Biol. Chem. 282:22737-22746(2007).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP TISSUE SPECIFICITY, INVOLVEMENT IN ERED, AND VARIANT ERED ILE-939.
RX PubMed=25676728; DOI=10.1002/humu.22764;
RA Jonsson F., Bystroem B., Davidson A.E., Backman L.J., Kellgren T.G.,
RA Tuft S.J., Koskela T., Ryden P., Sandgren O., Danielson P.,
RA Hardcastle A.J., Golovleva I.;
RT "Mutations in collagen, type XVII, alpha 1 (COL17A1) cause epithelial
RT recurrent erosion dystrophy (ERED).";
RL Hum. Mutat. 36:463-473(2015).
RN [19]
RP VARIANT JEB4 VAL-627.
RX PubMed=8669466;
RA McGrath J.A., Gatalica B., Li K., Dunnill M.G.S., McMillan J.R.,
RA Christiano A.M., Eady R.A.J., Uitto J.;
RT "Compound heterozygosity for a dominant glycine substitution and a
RT recessive internal duplication mutation in the type XVII collagen gene
RT results in junctional epidermolysis bullosa and abnormal dentition.";
RL Am. J. Pathol. 148:1787-1796(1996).
RN [20]
RP VARIANT JEB4 GLN-1303.
RX PubMed=9199555; DOI=10.1086/515463;
RA Schumann H., Hammami-Hauasli N., Pulkkinen L., Mauviel A., Kuester W.,
RA Luethi U., Owaribe K., Uitto J., Bruckner-Tuderman L.;
RT "Three novel homozygous point mutations and a new polymorphism in the
RT COL17A1 gene: relation to biological and clinical phenotypes of junctional
RT epidermolysis bullosa.";
RL Am. J. Hum. Genet. 60:1344-1353(1997).
RN [21]
RP VARIANT JEB4 VAL-627.
RX PubMed=10652291; DOI=10.1074/jbc.275.5.3093;
RA Tasanen K., Eble J.A., Aumailley M., Schumann H., Baetge J., Tu H.,
RA Bruckner P., Bruckner-Tuderman L.;
RT "Collagen XVII is destabilized by a glycine substitution mutation in the
RT cell adhesion domain Col15.";
RL J. Biol. Chem. 275:3093-3099(2000).
RN [22]
RP VARIANT JEB4 ASP-633.
RX PubMed=10951237; DOI=10.1046/j.1523-1747.2000.00049.x;
RA Tasanen K., Floeth M., Schumann H., Bruckner-Tuderman L.;
RT "Hemizygosity for a glycine substitution in collagen XVII: unfolding and
RT degradation of the ectodomain.";
RL J. Invest. Dermatol. 115:207-212(2000).
RN [23]
RP VARIANT JEB4 CYS-265, AND VARIANT ILE-231.
RX PubMed=11912005; DOI=10.1016/s0923-1811(01)00163-3;
RA Wu Y., Li G., Zhu X.;
RT "A novel homozygous point mutation in the COL17A1 gene in a Chinese family
RT with generalized atrophic benign epidermolysis bullosa.";
RL J. Dermatol. Sci. 28:181-186(2002).
CC -!- FUNCTION: May play a role in the integrity of hemidesmosome and the
CC attachment of basal keratinocytes to the underlying basement membrane.
CC -!- FUNCTION: The 120 kDa linear IgA disease antigen is an anchoring
CC filament component involved in dermal-epidermal cohesion. Is the target
CC of linear IgA bullous dermatosis autoantibodies.
CC -!- SUBUNIT: Homotrimers of alpha 1(XVII)chains. Interacts (via cytoplasmic
CC region) with ITGB4 (via cytoplasmic region). Interacts (via cytoplasmic
CC region) with DST isoform 3 (via N-terminus). Interacts (via N-terminus)
CC with PLEC. Interacts (via cytoplasmic region) with DSP.
CC {ECO:0000269|PubMed:10637308, ECO:0000269|PubMed:12482924,
CC ECO:0000269|PubMed:9748270}.
CC -!- INTERACTION:
CC Q9UMD9; Q9H0L4: CSTF2T; NbExp=3; IntAct=EBI-2528742, EBI-747012;
CC Q9UMD9; O60568: PLOD3; NbExp=3; IntAct=EBI-2528742, EBI-741582;
CC Q9UMD9; Q96T60: PNKP; NbExp=3; IntAct=EBI-2528742, EBI-1045072;
CC Q9UMD9; Q9Y3C6: PPIL1; NbExp=3; IntAct=EBI-2528742, EBI-2557649;
CC Q9UMD9; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2528742, EBI-947187;
CC Q9UMD9; Q9P202: WHRN; NbExp=3; IntAct=EBI-2528742, EBI-310886;
CC -!- SUBCELLULAR LOCATION: Cell junction, hemidesmosome. Membrane; Single-
CC pass type II membrane protein. Note=Localized along the plasma membrane
CC of the hemidesmosome.
CC -!- SUBCELLULAR LOCATION: [120 kDa linear IgA disease antigen]: Secreted,
CC extracellular space, extracellular matrix, basement membrane.
CC Note=Exclusively localized to anchoring filaments. Localized to the
CC epidermal side of split skin.
CC -!- SUBCELLULAR LOCATION: [97 kDa linear IgA disease antigen]: Secreted,
CC extracellular space, extracellular matrix, basement membrane.
CC Note=Localized in the lamina lucida beneath the hemidesmosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UMD9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UMD9-2; Sequence=VSP_024940, VSP_024941;
CC -!- TISSUE SPECIFICITY: Detected in skin (PubMed:8618013). In the cornea,
CC it is detected in the epithelial basement membrane, the epithelial
CC cells, and at a lower level in stromal cells (at protein level)
CC (PubMed:25676728). Stratified squamous epithelia. Found in
CC hemidesmosomes. Expressed in cornea, oral mucosa, esophagus, intestine,
CC kidney collecting ducts, ureter, bladder, urethra and thymus but is
CC absent in lung, blood vessels, skeletal muscle and nerves.
CC {ECO:0000269|PubMed:1748679, ECO:0000269|PubMed:25676728,
CC ECO:0000269|PubMed:8618013}.
CC -!- PTM: The intracellular/endo domain is disulfide-linked.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- PTM: The ectodomain is shedded from the surface of keratinocytes
CC resulting in a 120-kDa soluble form, also named as 120 kDa linear IgA
CC disease antigen. The shedding is mediated by membrane-bound
CC metalloproteases. This cleavage is inhibited by phosphorylation at Ser-
CC 544. {ECO:0000269|PubMed:9748270}.
CC -!- DISEASE: Epidermolysis bullosa, junctional 4, intermediate (JEB4)
CC [MIM:619787]: A form of epidermolysis bullosa, a genodermatosis
CC characterized by recurrent blistering, fragility of the skin and
CC mucosal epithelia, and erosions caused by minor mechanical trauma. JEB4
CC is an autosomal recessive, intermediate form in which blistering
CC lesions occur between the epidermis and the dermis at the lamina lucida
CC level of the basement membrane zone. In intermediate forms of
CC junctional epidermolysis bullosa, blistering does not lead to the
CC formation of chronic granulation tissue and does not affect the
CC lifespan of affected individuals. Nail dystrophy and dental enamel
CC defects are present. Scarring or non-scarring alopecia and diffuse hair
CC loss may occur. JEB4 patients manifest blisters at birth or shortly
CC afterward. Blisters may heal with atrophic scarring and variable
CC hypo- or hyperpigmentation. Oral mucosa may be involved.
CC {ECO:0000269|PubMed:10652291, ECO:0000269|PubMed:10951237,
CC ECO:0000269|PubMed:11912005, ECO:0000269|PubMed:8669466,
CC ECO:0000269|PubMed:9199555}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Epithelial recurrent erosion dystrophy (ERED) [MIM:122400]: A
CC corneal dystrophy characterized by recurrent episodes of epithelial
CC erosions from childhood, with occasional impairment of vision. Most
CC patients have attacks of redness, photophobia, epiphora, and ocular
CC pain. Exposure to sunlight or draught, dust and smoke and lack of sleep
CC can precipitate attacks. {ECO:0000269|PubMed:25676728}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Both the 120 kDa linear IgA disease antigen and the 97
CC kDa linear IgA disease antigen of COL17A1, represent major antigenic
CC targets of autoantibodies in patients with linear IgA disease (LAD).
CC LAD is a subepidermal blistering disorder characterized by tissue-bound
CC and circulating IgA autoantibodies to the dermal-epidermal junction.
CC These IgA autoantibodies preferentially react with 97 and the 120 kDa
CC forms, but not with the full-length COL17A1, suggesting that the
CC cleavage of the ectodomain generates novel autoantigenic epitopes.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35605.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH04478.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; M91669; AAA35605.1; ALT_INIT; mRNA.
DR EMBL; U76604; AAB51499.1; -; Genomic_DNA.
DR EMBL; U76565; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76566; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76567; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76568; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76569; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76570; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76571; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76572; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76573; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76574; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76575; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76576; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76577; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76578; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76579; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76580; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76581; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76582; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76583; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76584; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76585; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76586; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76587; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76588; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76589; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76590; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76591; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76592; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76593; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76594; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76595; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76596; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76597; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76598; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76599; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76600; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76601; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76602; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; U76603; AAB51499.1; JOINED; Genomic_DNA.
DR EMBL; AL138761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004478; AAH04478.1; ALT_SEQ; mRNA.
DR EMBL; M63730; AAA51839.1; -; mRNA.
DR CCDS; CCDS7554.1; -. [Q9UMD9-1]
DR PIR; I56325; A61262.
DR RefSeq; NP_000485.3; NM_000494.3. [Q9UMD9-1]
DR AlphaFoldDB; Q9UMD9; -.
DR BioGRID; 107704; 20.
DR ComplexPortal; CPX-1758; Collagen type XVII trimer.
DR IntAct; Q9UMD9; 10.
DR MINT; Q9UMD9; -.
DR STRING; 9606.ENSP00000340937; -.
DR Allergome; 8213; Hom s BP180.
DR GlyGen; Q9UMD9; 1 site.
DR iPTMnet; Q9UMD9; -.
DR PhosphoSitePlus; Q9UMD9; -.
DR SwissPalm; Q9UMD9; -.
DR BioMuta; COL17A1; -.
DR DMDM; 146345399; -.
DR EPD; Q9UMD9; -.
DR jPOST; Q9UMD9; -.
DR MassIVE; Q9UMD9; -.
DR MaxQB; Q9UMD9; -.
DR PaxDb; Q9UMD9; -.
DR PeptideAtlas; Q9UMD9; -.
DR PRIDE; Q9UMD9; -.
DR ProteomicsDB; 85187; -. [Q9UMD9-1]
DR ProteomicsDB; 85188; -. [Q9UMD9-2]
DR Antibodypedia; 18201; 242 antibodies from 29 providers.
DR DNASU; 1308; -.
DR Ensembl; ENST00000369733.8; ENSP00000358748.3; ENSG00000065618.21. [Q9UMD9-2]
DR Ensembl; ENST00000648076.2; ENSP00000497653.1; ENSG00000065618.21. [Q9UMD9-1]
DR GeneID; 1308; -.
DR KEGG; hsa:1308; -.
DR MANE-Select; ENST00000648076.2; ENSP00000497653.1; NM_000494.4; NP_000485.3.
DR UCSC; uc001kxr.4; human. [Q9UMD9-1]
DR CTD; 1308; -.
DR DisGeNET; 1308; -.
DR GeneCards; COL17A1; -.
DR GeneReviews; COL17A1; -.
DR HGNC; HGNC:2194; COL17A1.
DR HPA; ENSG00000065618; Tissue enriched (skin).
DR MalaCards; COL17A1; -.
DR MIM; 113811; gene.
DR MIM; 122400; phenotype.
DR MIM; 619787; phenotype.
DR neXtProt; NX_Q9UMD9; -.
DR OpenTargets; ENSG00000065618; -.
DR Orphanet; 293381; Epithelial recurrent erosion dystrophy.
DR Orphanet; 79402; Intermediate generalized junctional epidermolysis bullosa.
DR Orphanet; 79406; Late-onset junctional epidermolysis bullosa.
DR Orphanet; 251393; Localized junctional epidermolysis bullosa.
DR PharmGKB; PA26710; -.
DR VEuPathDB; HostDB:ENSG00000065618; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000161242; -.
DR HOGENOM; CLU_004285_0_0_1; -.
DR InParanoid; Q9UMD9; -.
DR OMA; TRVMSYM; -.
DR OrthoDB; 718661at2759; -.
DR PhylomeDB; Q9UMD9; -.
DR TreeFam; TF332289; -.
DR PathwayCommons; Q9UMD9; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-446107; Type I hemidesmosome assembly.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; Q9UMD9; -.
DR BioGRID-ORCS; 1308; 24 hits in 1071 CRISPR screens.
DR ChiTaRS; COL17A1; human.
DR GeneWiki; Collagen,_type_XVII,_alpha_1; -.
DR GenomeRNAi; 1308; -.
DR Pharos; Q9UMD9; Tbio.
DR PRO; PR:Q9UMD9; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9UMD9; protein.
DR Bgee; ENSG00000065618; Expressed in skin of abdomen and 112 other tissues.
DR ExpressionAtlas; Q9UMD9; baseline and differential.
DR Genevisible; Q9UMD9; HS.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; TAS:ProtInc.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL.
DR GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0031581; P:hemidesmosome assembly; IDA:UniProtKB.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Cell junction; Collagen;
KW Direct protein sequencing; Disease variant; Disulfide bond;
KW Epidermolysis bullosa; Extracellular matrix; Glycoprotein; Hydroxylation;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..1497
FT /note="Collagen alpha-1(XVII) chain"
FT /id="PRO_0000059406"
FT CHAIN 524..1497
FT /note="120 kDa linear IgA disease antigen"
FT /id="PRO_0000342555"
FT CHAIN 531..?
FT /note="97 kDa linear IgA disease antigen"
FT /id="PRO_0000342556"
FT TOPO_DOM 1..467
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..1497
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..566
FT /note="Nonhelical region (NC16)"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..230
FT /note="Necessary for interaction with DST and for the
FT recruitment of DST to hemidesmosome"
FT /evidence="ECO:0000269|PubMed:12482924"
FT REGION 167..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..1482
FT /note="Triple-helical region"
FT REGION 1209..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1434..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1483..1497
FT /note="Nonhelical region (NC1)"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..842
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..894
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..921
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1229
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1468
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 544
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:17545155"
FT CARBOHYD 1421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9748270"
FT VAR_SEQ 922..966
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_024940"
FT VAR_SEQ 1170..1207
FT /note="GSEFRGIVGPPGPPGPPGIPGNVWSSISVEDLSSYLHT -> A (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_024941"
FT VARIANT 4
FT /note="T -> A (in dbSNP:rs17116471)"
FT /id="VAR_048781"
FT VARIANT 210
FT /note="T -> M (in dbSNP:rs805708)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_017593"
FT VARIANT 231
FT /note="M -> I (in dbSNP:rs1054113)"
FT /evidence="ECO:0000269|PubMed:11912005,
FT ECO:0000269|PubMed:9012408"
FT /id="VAR_017594"
FT VARIANT 238
FT /note="M -> T"
FT /evidence="ECO:0000269|PubMed:9012408"
FT /id="VAR_017595"
FT VARIANT 265
FT /note="S -> C (in JEB4)"
FT /evidence="ECO:0000269|PubMed:11912005"
FT /id="VAR_017596"
FT VARIANT 428
FT /note="G -> S (in dbSNP:rs805698)"
FT /evidence="ECO:0000269|PubMed:1324962,
FT ECO:0000269|PubMed:9012408"
FT /id="VAR_017597"
FT VARIANT 627
FT /note="G -> V (in JEB4)"
FT /evidence="ECO:0000269|PubMed:10652291,
FT ECO:0000269|PubMed:8669466"
FT /id="VAR_017598"
FT VARIANT 633
FT /note="G -> D (in JEB4; dbSNP:rs121912773)"
FT /evidence="ECO:0000269|PubMed:10951237"
FT /id="VAR_017599"
FT VARIANT 703
FT /note="M -> V (in dbSNP:rs805722)"
FT /evidence="ECO:0000269|PubMed:9012408"
FT /id="VAR_017600"
FT VARIANT 939
FT /note="T -> I (in ERED; dbSNP:rs797045142)"
FT /evidence="ECO:0000269|PubMed:25676728"
FT /id="VAR_074627"
FT VARIANT 1303
FT /note="R -> Q (in JEB4; dbSNP:rs121912771)"
FT /evidence="ECO:0000269|PubMed:9199555"
FT /id="VAR_017601"
FT VARIANT 1370
FT /note="D -> G (in dbSNP:rs17116350)"
FT /evidence="ECO:0000269|PubMed:9012408"
FT /id="VAR_017602"
FT CONFLICT 856
FT /note="Q -> P (in Ref. 5; AAA51839)"
FT /evidence="ECO:0000305"
FT CONFLICT 905
FT /note="S -> F (in Ref. 1; AAA35605 and 2; AAB51499)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1497 AA; 150419 MW; E01027005F3AE843 CRC64;
MDVTKKNKRD GTEVTERIVT ETVTTRLTSL PPKGGTSNGY AKTASLGGGS RLEKQSLTHG
SSGYINSTGS TRGHASTSSY RRAHSPASTL PNSPGSTFER KTHVTRHAYE GSSSGNSSPE
YPRKEFASSS TRGRSQTRES EIRVRLQSAS PSTRWTELDD VKRLLKGSRS ASVSPTRNSS
NTLPIPKKGT VETKIVTASS QSVSGTYDAT ILDANLPSHV WSSTLPAGSS MGTYHNNMTT
QSSSLLNTNA YSAGSVFGVP NNMASCSPTL HPGLSTSSSV FGMQNNLAPS LTTLSHGTTT
TSTAYGVKKN MPQSPAAVNT GVSTSAACTT SVQSDDLLHK DCKFLILEKD NTPAKKEMEL
LIMTKDSGKV FTASPASIAA TSFSEDTLKK EKQAAYNADS GLKAEANGDL KTVSTKGKTT
TADIHSYGSS GGGGSGGGGG VGGAGGGPWG PAPAWCPCGS CCSWWKWLLG LLLTWLLLLG
LLFGLIALAE EVRKLKARVD ELERIRRSIL PYGDSMDRIE KDRLQGMAPA AGADLDKIGL
HSDSQEELWM FVRKKLMMEQ ENGNLRGSPG PKGDMGSPGP KGDRGFPGTP GIPGPLGHPG
PQGPKGQKGS VGDPGMEGPM GQRGREGPMG PRGEAGPPGS GEKGERGAAG EPGPHGPPGV
PGSVGPKGSS GSPGPQGPPG PVGLQGLRGE VGLPGVKGDK GPMGPPGPKG DQGEKGPRGL
TGEPGMRGLP GAVGEPGAKG AMGPAGPDGH QGPRGEQGLT GMPGIRGPPG PSGDPGKPGL
TGPQGPQGLP GTPGRPGIKG EPGAPGKIVT SEGSSMLTVP GPPGPPGAMG PPGPPGAPGP
AGPAGLPGHQ EVLNLQGPPG PPGPRGPPGP SIPGPPGPRG PPGEGLPGPP GPPGSFLSNS
ETFLSGPPGP PGPPGPKGDQ GPPGPRGHQG EQGLPGFSTS GSSSFGLNLQ GPPGPPGPQG
PKGDKGDPGV PGALGIPSGP SEGGSSSTMY VSGPPGPPGP PGPPGSISSS GQEIQQYISE
YMQSDSIRSY LSGVQGPPGP PGPPGPVTTI TGETFDYSEL ASHVVSYLRT SGYGVSLFSS
SISSEDILAV LQRDDVRQYL RQYLMGPRGP PGPPGASGDG SLLSLDYAEL SSRILSYMSS
SGISIGLPGP PGPPGLPGTS YEELLSLLRG SEFRGIVGPP GPPGPPGIPG NVWSSISVED
LSSYLHTAGL SFIPGPPGPP GPPGPRGPPG VSGALATYAA ENSDSFRSEL ISYLTSPDVR
SFIVGPPGPP GPQGPPGDSR LLSTDASHSR GSSSSSHSSS VRRGSSYSSS MSTGGGGAGS
LGAGGAFGEA AGDRGPYGTD IGPGGGYGAA AEGGMYAGNG GLLGADFAGD LDYNELAVRV
SESMQRQGLL QGMAYTVQGP PGQPGPQGPP GISKVFSAYS NVTADLMDFF QTYGAIQGPP
GQKGEMGTPG PKGDRGPAGP PGHPGPPGPR GHKGEKGDKG DQVYAGRRRR RSIAVKP
