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 27-MAR-2024, entry version 196. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 26. DR ComplexPortal; CPX-1758; Collagen type XVII trimer. DR IntAct; Q9UMD9; 11. DR MINT; Q9UMD9; -. DR STRING; 9606.ENSP00000497653; -. DR Allergome; 8213; Hom s BP180. DR GlyCosmos; Q9UMD9; 1 site, No reported glycans. DR GlyGen; Q9UMD9; 3 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000340937; -. DR PeptideAtlas; Q9UMD9; -. DR ProteomicsDB; 85187; -. [Q9UMD9-1] DR ProteomicsDB; 85188; -. [Q9UMD9-2] DR Antibodypedia; 18201; 308 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 AGR; HGNC:2194; -. 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; YRQTQSP; -. DR OrthoDB; 5362506at2759; -. 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; 25 hits in 1152 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 114 other cell types or tissues. DR ExpressionAtlas; Q9UMD9; baseline and differential. 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: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:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL. DR GO; GO:0008201; F:heparin binding; IBA:GO_Central. 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 Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1. DR InterPro; IPR008160; Collagen. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF1100; FIBRILLAR COLLAGEN NC1 DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF01391; Collagen; 3. DR Genevisible; Q9UMD9; HS. 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 //