Q9UMD9 (COHA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-1(XVII) chain

Alternative name(s):
180 kDa bullous pemphigoid antigen 2
Bullous pemphigoid antigen 2

Cleaved into the following 2 chains:

1. 120 kDa linear IgA disease antigen
   Alternative name(s):
   120 kDa linear IgA dermatosis antigen
   Linear IgA disease antigen 1
   Short name=LAD-1
2. 97 kDa linear IgA disease antigen
   Alternative name(s):
   97 kDa linear IgA bullous dermatosis antigen
   Short name=97 kDa LAD antigen
   Short name=97-LAD
   Linear IgA bullous disease antigen of 97 kDa
   Short name=LABD97

Gene names

Name:	COL17A1
Synonyms:	BP180, BPAG2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1497 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane. Ref.8 Ref.15 The 120 kDa linear IgA disease antigen is an anchoring filament component involved in dermal-epidermal cohesion. Is the target of linear IgA bullous dermatosis autoantibodies. Ref.8 Ref.15
Subunit structure	Homotrimers of alpha 1(XVII)chains. Interacts (via cytoplasmic region) with ITGB4 (via cytoplasmic region). Interacts (via cytoplasmic region) with DST isoform 3 (via N-terminus). Interacts (via N-terminus) with PLEC. Interacts (via cytoplasmic region) with DSP. Ref.12 Ref.13 Ref.15
Subcellular location	Cell junction › hemidesmosome. Membrane; Single-pass type II membrane protein. Note: Localized along the plasma membrane of the hemidesmosome. Ref.1 Ref.8 Ref.10 Ref.11 Ref.15 120 kDa linear IgA disease antigen: Secreted › extracellular space › extracellular matrix › basement membrane. Note: Exclusively localized to anchoring filaments. Localized to the epidermal side of split skin. Ref.1 Ref.8 Ref.10 Ref.11 Ref.15 97 kDa linear IgA disease antigen: Secreted › extracellular space › extracellular matrix › basement membrane. Note: Localized in the lamina lucida beneath the hemidesmosomes. Ref.1 Ref.8 Ref.10 Ref.11 Ref.15
Tissue specificity	Stratified squamous epithelia. Found in hemidesmosomes. Expressed in cornea, oral mucosa, esophagus, intestine, kidney collecting ducts, ureter, bladder, urethra and thymus but is absent in lung, blood vessels, skeletal muscle and nerves. Ref.5 Ref.8
Post-translational modification	The intracellular/endo domain is disulfide-linked. Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. The ectodomain is shedded from the surface of keratinocytes resulting in a 120-kDa soluble form, also named as 120 kDa linear IgA disease antigen. The shedding is mediated by membrane-bound metalloproteases. This cleavage is inhibited by phosophorylation at Ser-544.
Involvement in disease	Generalized atrophic benign epidermolysis bullosa (GABEB) [MIM:226650]: A non-lethal, adult form of junctional epidermolysis bullosa characterized by life-long blistering of the skin, associated with hair and tooth abnormalities. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Miscellaneous	Both the 120 kDa linear IgA disease antigen and the 97 kDa linear IgA disease antigen of COL17A1, represent major antigenic targets of autoantibodies in patients with linear IgA disease (LAD). LAD is a subepidermal blistering disorder characterized by tissue-bound and circulating IgA autoantibodies to the dermal-epidermal junction. These IgA autoantibodies preferentially react with 97 and the 120 kDa forms, but not with the full-length COL17A1, suggesting that the cleavage of the ectodomain generates novel autoantigenic epitopes.
Sequence caution	The sequence AAA35605.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAH04478.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Cellular component	Basement membrane Cell junction Extracellular matrix Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Epidermolysis bullosa
Domain	Collagen Repeat Signal-anchor Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Hydroxylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell-matrix adhesion Traceable author statement Ref.2. Source: ProtInc epidermis development Traceable author statement Ref.2. Source: ProtInc extracellular matrix organization Traceable author statement. Source: Reactome hemidesmosome assembly Inferred from direct assay Ref.15. Source: UniProtKB
Cellular_component	basement membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell-cell junction Traceable author statement Ref.2. Source: ProtInc collagen Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum lumen Traceable author statement. Source: Reactome hemidesmosome Inferred from direct assay Ref.15. Source: UniProtKB integral to plasma membrane Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UMD9-1)

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

Isoform 2 (identifier: Q9UMD9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     922-966: Missing.
     1170-1207: GSEFRGIVGPPGPPGPPGIPGNVWSSISVEDLSSYLHT → A

Note: Gene prediction based on EST data.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1497	1497	Collagen alpha-1(XVII) chain		PRO_0000059406
	Chain	524 – 1497	974	120 kDa linear IgA disease antigen		PRO_0000342555
	Chain	531 – ?		97 kDa linear IgA disease antigen		PRO_0000342556
Regions
	Topological domain	1 – 467	467	Cytoplasmic Potential
	Transmembrane	468 – 488	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	489 – 1497	1009	Extracellular Potential
	Region	1 – 566	566	Nonhelical region (NC16)
	Region	145 – 230	86	Necessary for interaction with DST and for the recruitment of DST to hemidesmosome
	Region	567 – 1482	916	Triple-helical region
	Region	1483 – 1497	15	Nonhelical region (NC1)
Amino acid modifications
	Modified residue	85	1	Phosphoserine By similarity
	Modified residue	93	1	Phosphoserine By similarity
	Modified residue	148	1	Phosphoserine By similarity
	Modified residue	544	1	Phosphoserine; by CK2 Ref.16
	Glycosylation	1421	1	N-linked (GlcNAc...) Ref.12
Natural variations
	Alternative sequence	922 – 966	45	Missing in isoform 2.		VSP_024940
	Alternative sequence	1170 – 1207	38	GSEFR…SYLHT → A in isoform 2.		VSP_024941
	Natural variant	4	1	T → A. Corresponds to variant rs17116471 [ dbSNP | Ensembl ].		VAR_048781
	Natural variant	210	1	T → M. Ref.4 Corresponds to variant rs805708 [ dbSNP | Ensembl ].		VAR_017593
	Natural variant	231	1	M → I. Ref.2 Ref.22 Corresponds to variant rs1054113 [ dbSNP | Ensembl ].		VAR_017594
	Natural variant	238	1	M → T. Ref.2		VAR_017595
	Natural variant	265	1	S → C in GABEB. Ref.22		VAR_017596
	Natural variant	428	1	G → S. Ref.1 Ref.2 Corresponds to variant rs805698 [ dbSNP | Ensembl ].		VAR_017597
	Natural variant	627	1	G → V in GABEB. Ref.18 Ref.20		VAR_017598
	Natural variant	633	1	G → D in GABEB. Ref.21		VAR_017599
	Natural variant	703	1	M → V. Ref.2 Corresponds to variant rs805722 [ dbSNP | Ensembl ].		VAR_017600
	Natural variant	1303	1	R → Q in GABEB. Ref.19		VAR_017601
	Natural variant	1370	1	D → G. Ref.2 Corresponds to variant rs17116350 [ dbSNP | Ensembl ].		VAR_017602
Experimental info
	Sequence conflict	856	1	Q → P in AAA51839. Ref.5
	Sequence conflict	905	1	S → F in AAA35605. Ref.1
	Sequence conflict	905	1	S → F in AAB51499. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2007. Version 3. Checksum: E01027005F3AE843	FASTA	1,497	150,419
	10 20 30 40 50 60 MDVTKKNKRD GTEVTERIVT ETVTTRLTSL PPKGGTSNGY AKTASLGGGS RLEKQSLTHG 70 80 90 100 110 120 SSGYINSTGS TRGHASTSSY RRAHSPASTL PNSPGSTFER KTHVTRHAYE GSSSGNSSPE 130 140 150 160 170 180 YPRKEFASSS TRGRSQTRES EIRVRLQSAS PSTRWTELDD VKRLLKGSRS ASVSPTRNSS 190 200 210 220 230 240 NTLPIPKKGT VETKIVTASS QSVSGTYDAT ILDANLPSHV WSSTLPAGSS MGTYHNNMTT 250 260 270 280 290 300 QSSSLLNTNA YSAGSVFGVP NNMASCSPTL HPGLSTSSSV FGMQNNLAPS LTTLSHGTTT 310 320 330 340 350 360 TSTAYGVKKN MPQSPAAVNT GVSTSAACTT SVQSDDLLHK DCKFLILEKD NTPAKKEMEL 370 380 390 400 410 420 LIMTKDSGKV FTASPASIAA TSFSEDTLKK EKQAAYNADS GLKAEANGDL KTVSTKGKTT 430 440 450 460 470 480 TADIHSYGSS GGGGSGGGGG VGGAGGGPWG PAPAWCPCGS CCSWWKWLLG LLLTWLLLLG 490 500 510 520 530 540 LLFGLIALAE EVRKLKARVD ELERIRRSIL PYGDSMDRIE KDRLQGMAPA AGADLDKIGL 550 560 570 580 590 600 HSDSQEELWM FVRKKLMMEQ ENGNLRGSPG PKGDMGSPGP KGDRGFPGTP GIPGPLGHPG 610 620 630 640 650 660 PQGPKGQKGS VGDPGMEGPM GQRGREGPMG PRGEAGPPGS GEKGERGAAG EPGPHGPPGV 670 680 690 700 710 720 PGSVGPKGSS GSPGPQGPPG PVGLQGLRGE VGLPGVKGDK GPMGPPGPKG DQGEKGPRGL 730 740 750 760 770 780 TGEPGMRGLP GAVGEPGAKG AMGPAGPDGH QGPRGEQGLT GMPGIRGPPG PSGDPGKPGL 790 800 810 820 830 840 TGPQGPQGLP GTPGRPGIKG EPGAPGKIVT SEGSSMLTVP GPPGPPGAMG PPGPPGAPGP 850 860 870 880 890 900 AGPAGLPGHQ EVLNLQGPPG PPGPRGPPGP SIPGPPGPRG PPGEGLPGPP GPPGSFLSNS 910 920 930 940 950 960 ETFLSGPPGP PGPPGPKGDQ GPPGPRGHQG EQGLPGFSTS GSSSFGLNLQ GPPGPPGPQG 970 980 990 1000 1010 1020 PKGDKGDPGV PGALGIPSGP SEGGSSSTMY VSGPPGPPGP PGPPGSISSS GQEIQQYISE 1030 1040 1050 1060 1070 1080 YMQSDSIRSY LSGVQGPPGP PGPPGPVTTI TGETFDYSEL ASHVVSYLRT SGYGVSLFSS 1090 1100 1110 1120 1130 1140 SISSEDILAV LQRDDVRQYL RQYLMGPRGP PGPPGASGDG SLLSLDYAEL SSRILSYMSS 1150 1160 1170 1180 1190 1200 SGISIGLPGP PGPPGLPGTS YEELLSLLRG SEFRGIVGPP GPPGPPGIPG NVWSSISVED 1210 1220 1230 1240 1250 1260 LSSYLHTAGL SFIPGPPGPP GPPGPRGPPG VSGALATYAA ENSDSFRSEL ISYLTSPDVR 1270 1280 1290 1300 1310 1320 SFIVGPPGPP GPQGPPGDSR LLSTDASHSR GSSSSSHSSS VRRGSSYSSS MSTGGGGAGS 1330 1340 1350 1360 1370 1380 LGAGGAFGEA AGDRGPYGTD IGPGGGYGAA AEGGMYAGNG GLLGADFAGD LDYNELAVRV 1390 1400 1410 1420 1430 1440 SESMQRQGLL QGMAYTVQGP PGQPGPQGPP GISKVFSAYS NVTADLMDFF QTYGAIQGPP 1450 1460 1470 1480 1490 GQKGEMGTPG PKGDRGPAGP PGHPGPPGPR GHKGEKGDKG DQVYAGRRRR RSIAVKP
	Isoform 2 [UniParc]. Checksum: 51434477730EC017	FASTA	1,415	142,344
	10 20 30 40 50 60 MDVTKKNKRD GTEVTERIVT ETVTTRLTSL PPKGGTSNGY AKTASLGGGS RLEKQSLTHG 70 80 90 100 110 120 SSGYINSTGS TRGHASTSSY RRAHSPASTL PNSPGSTFER KTHVTRHAYE GSSSGNSSPE 130 140 150 160 170 180 YPRKEFASSS TRGRSQTRES EIRVRLQSAS PSTRWTELDD VKRLLKGSRS ASVSPTRNSS 190 200 210 220 230 240 NTLPIPKKGT VETKIVTASS QSVSGTYDAT ILDANLPSHV WSSTLPAGSS MGTYHNNMTT 250 260 270 280 290 300 QSSSLLNTNA YSAGSVFGVP NNMASCSPTL HPGLSTSSSV FGMQNNLAPS LTTLSHGTTT 310 320 330 340 350 360 TSTAYGVKKN MPQSPAAVNT GVSTSAACTT SVQSDDLLHK DCKFLILEKD NTPAKKEMEL 370 380 390 400 410 420 LIMTKDSGKV FTASPASIAA TSFSEDTLKK EKQAAYNADS GLKAEANGDL KTVSTKGKTT 430 440 450 460 470 480 TADIHSYGSS GGGGSGGGGG VGGAGGGPWG PAPAWCPCGS CCSWWKWLLG LLLTWLLLLG 490 500 510 520 530 540 LLFGLIALAE EVRKLKARVD ELERIRRSIL PYGDSMDRIE KDRLQGMAPA AGADLDKIGL 550 560 570 580 590 600 HSDSQEELWM FVRKKLMMEQ ENGNLRGSPG PKGDMGSPGP KGDRGFPGTP GIPGPLGHPG 610 620 630 640 650 660 PQGPKGQKGS VGDPGMEGPM GQRGREGPMG PRGEAGPPGS GEKGERGAAG EPGPHGPPGV 670 680 690 700 710 720 PGSVGPKGSS GSPGPQGPPG PVGLQGLRGE VGLPGVKGDK GPMGPPGPKG DQGEKGPRGL 730 740 750 760 770 780 TGEPGMRGLP GAVGEPGAKG AMGPAGPDGH QGPRGEQGLT GMPGIRGPPG PSGDPGKPGL 790 800 810 820 830 840 TGPQGPQGLP GTPGRPGIKG EPGAPGKIVT SEGSSMLTVP GPPGPPGAMG PPGPPGAPGP 850 860 870 880 890 900 AGPAGLPGHQ EVLNLQGPPG PPGPRGPPGP SIPGPPGPRG PPGEGLPGPP GPPGSFLSNS 910 920 930 940 950 960 ETFLSGPPGP PGPPGPKGDQ GDPGVPGALG IPSGPSEGGS SSTMYVSGPP GPPGPPGPPG 970 980 990 1000 1010 1020 SISSSGQEIQ QYISEYMQSD SIRSYLSGVQ GPPGPPGPPG PVTTITGETF DYSELASHVV 1030 1040 1050 1060 1070 1080 SYLRTSGYGV SLFSSSISSE DILAVLQRDD VRQYLRQYLM GPRGPPGPPG ASGDGSLLSL 1090 1100 1110 1120 1130 1140 DYAELSSRIL SYMSSSGISI GLPGPPGPPG LPGTSYEELL SLLRAAGLSF IPGPPGPPGP 1150 1160 1170 1180 1190 1200 PGPRGPPGVS GALATYAAEN SDSFRSELIS YLTSPDVRSF IVGPPGPPGP QGPPGDSRLL 1210 1220 1230 1240 1250 1260 STDASHSRGS SSSSHSSSVR RGSSYSSSMS TGGGGAGSLG AGGAFGEAAG DRGPYGTDIG 1270 1280 1290 1300 1310 1320 PGGGYGAAAE GGMYAGNGGL LGADFAGDLD YNELAVRVSE SMQRQGLLQG MAYTVQGPPG 1330 1340 1350 1360 1370 1380 QPGPQGPPGI SKVFSAYSNV TADLMDFFQT YGAIQGPPGQ KGEMGTPGPK GDRGPAGPPG 1390 1400 1410 HPGPPGPRGH KGEKGDKGDQ VYAGRRRRRS IAVKP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and primary structural analysis of the bullous pemphigoid autoantigen, BP180." Giudice G.J., Emery D.J., Diaz L.A. J. Invest. Dermatol. 99:243-250(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, VARIANT SER-428. Tissue: Foreskin.
[2]	"Cloning of the human type XVII collagen gene (COL17A1), and detection of novel mutations in generalized atrophic benign epidermolysis bullosa." Gatalica B., Pulkkinen L., Li K., Kuokkanen K., Ryynaenen M., McGrath J.A., Uitto J. Am. J. Hum. Genet. 60:352-365(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS ILE-231; THR-238; SER-428; VAL-703 AND GLY-1370.
[3]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-390, VARIANT MET-210. Tissue: Pancreas.
[5]	"Genomic organization of collagenous domains and chromosomal assignment of human 180-kDa bullous pemphigoid antigen-2, a novel collagen of stratified squamous epithelium." Li K.H., Sawamura D., Giudice G.J., Diaz L.A., Mattei M.-G., Chu M.-L., Uitto J. J. Biol. Chem. 266:24064-24069(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 508-856, TISSUE SPECIFICITY.
[6]	"The 97-kDa (LABD97) and 120-kDa (LAD-1) fragments of bullous pemphigoid antigen 180/type XVII collagen have different N-termini." Hirako Y., Nishizawa Y., Sitaru C., Opitz A., Marcus K., Meyer H.E., Butt E., Owaribe K., Zillikens D. J. Invest. Dermatol. 121:1554-1556(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 524-535.
[7]	"The 97 kDa linear IgA bullous disease antigen is identical to a portion of the extracellular domain of the 180 kDa bullous pemphigoid antigen, BPAg2." Zone J.J., Taylor T.B., Meyer L.J., Petersen M.J. J. Invest. Dermatol. 110:207-210(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 531-546; 554-565; 585-605; 647-666; 680-688; 689-703; 755-765; 842-860; 880-891; 1016-1028; 1062-1069; 1102-1108; 1134-1142; 1227-1247 AND 1248-1260.
[8]	"LAD-1, the linear IgA bullous dermatosis autoantigen, is a novel 120-kDa anchoring filament protein synthesized by epidermal cells." Marinkovich M.P., Taylor T.B., Keene D.R., Burgeson R.E., Zone J.J. J. Invest. Dermatol. 106:734-738(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY.
[9]	Erratum Marinkovich M.P., Taylor T.B., Keene D.R., Burgeson R.E., Zone J.J. J. Invest. Dermatol. 106:1343-1343(1996)
[10]	"97-kDa linear IgA bullous dermatosis (LAD) antigen localizes to the lamina lucida of the epidermal basement membrane." Ishiko A., Shimizu H., Masunaga T., Hashimoto T., Dmochowski M., Wojnarowska F., Bhogal B.S., Black M.M., Nishikawa T. J. Invest. Dermatol. 106:739-743(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[11]	"Evidence that the 180-kD bullous pemphigoid antigen is a transmembrane collagen, type XVII, in a triple-helical conformation and in type II transmembrane topography." Limardo M., Arffman A., Aho S., Utto J. J. Invest. Dermatol. 106:860-860(1996) Cited for: SUBCELLULAR LOCATION.
[12]	"Two forms of collagen XVII in keratinocytes. A full-length transmembrane protein and a soluble ectodomain." Schaecke H., Schumann H., Hammami-Hauasli N., Raghunath M., Bruckner-Tuderman L. J. Biol. Chem. 273:25937-25943(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, PROTEOLYTIC PROCESSING, GLYCOSYLATION AT ASN-1421, DOMAINS.
[13]	"The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell surface at the site of the hemidesmosome." Hopkinson S.B., Jones J.C. Mol. Biol. Cell 11:277-286(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DSP.
[14]	"Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs." Franzke C.-W., Tasanen K., Schaecke H., Zhou Z., Tryggvason K., Mauch C., Zigrino P., Sunnarborg S., Lee D.C., Fahrenholz F., Bruckner-Tuderman L. EMBO J. 21:5026-5035(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SHEDDING.
[15]	"Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly." Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A. J. Cell Sci. 116:387-399(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DSP; DST; ITGB4 AND PLEC, SUBCELLULAR LOCATION.
[16]	"Extracellular phosphorylation of collagen XVII by ecto-casein kinase 2 inhibits ectodomain shedding." Zimina E.P., Fritsch A., Schermer B., Bakulina A.Y., Bashkurov M., Benzing T., Bruckner-Tuderman L. J. Biol. Chem. 282:22737-22746(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-544.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"Compound heterozygosity for a dominant glycine substitution and a recessive internal duplication mutation in the type XVII collagen gene results in junctional epidermolysis bullosa and abnormal dentition." McGrath J.A., Gatalica B., Li K., Dunnill M.G.S., McMillan J.R., Christiano A.M., Eady R.A.J., Uitto J. Am. J. Pathol. 148:1787-1796(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GABEB VAL-627.
[19]	"Three novel homozygous point mutations and a new polymorphism in the COL17A1 gene: relation to biological and clinical phenotypes of junctional epidermolysis bullosa." Schumann H., Hammami-Hauasli N., Pulkkinen L., Mauviel A., Kuester W., Luethi U., Owaribe K., Uitto J., Bruckner-Tuderman L. Am. J. Hum. Genet. 60:1344-1353(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GABEB GLN-1303.
[20]	"Collagen XVII is destabilized by a glycine substitution mutation in the cell adhesion domain Col15." Tasanen K., Eble J.A., Aumailley M., Schumann H., Baetge J., Tu H., Bruckner P., Bruckner-Tuderman L. J. Biol. Chem. 275:3093-3099(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GABEB VAL-627.
[21]	"Hemizygosity for a glycine substitution in collagen XVII: unfolding and degradation of the ectodomain." Tasanen K., Floeth M., Schumann H., Bruckner-Tuderman L. J. Invest. Dermatol. 115:207-212(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GABEB ASP-633.
[22]	"A novel homozygous point mutation in the COL17A1 gene in a Chinese family with generalized atrophic benign epidermolysis bullosa." Wu Y., Li G., Zhu X. J. Dermatol. Sci. 28:181-186(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GABEB CYS-265, VARIANT ILE-231.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	M91669 mRNA. Translation: AAA35605.1. Different initiation. U76604 , U76565, U76566, U76567, U76568, U76569, U76570, U76571, U76572, U76573, U76574, U76575, U76576, U76577, U76578, U76579, U76580, U76581, U76582, U76583, U76584, U76585, U76586, U76587, U76588, U76589, U76590, U76591, U76592, U76593, U76594, U76595, U76596, U76597, U76598, U76599, U76600, U76601, U76602, U76603 Genomic DNA. Translation: AAB51499.1. AL138761 Genomic DNA. Translation: CAC00589.1. AL138761 Genomic DNA. Translation: CAI12398.1. BC004478 mRNA. Translation: AAH04478.1. Sequence problems. M63730 mRNA. Translation: AAA51839.1.
IPI	IPI00398272. IPI00643731.
PIR	A61262. I56325.
RefSeq	NP_000485.3. NM_000494.3.
UniGene	Hs.117938. Hs.732773.
3D structure databases
ProteinModelPortal	Q9UMD9.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000340937.
Protein family/group databases
Allergome	8213. Hom s BP180. 8226. Hom s BP180.0101.
PTM databases
PhosphoSite	Q9UMD9.
Polymorphism databases
DMDM	146345399.
Proteomic databases
PaxDb	Q9UMD9.
PRIDE	Q9UMD9.
Protocols and materials databases
DNASU	1308.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000353479; ENSP00000340937; ENSG00000065618. ENST00000369733; ENSP00000358748; ENSG00000065618.
GeneID	1308.
KEGG	hsa:1308.
UCSC	uc001kxr.3. human.
Organism-specific databases
CTD	1308.
GeneCards	GC10M105781.
H-InvDB	HIX0035327.
HGNC	HGNC:2194. COL17A1.
HPA	HPA043673.
MIM	113811. gene+phenotype. 226650. phenotype.
neXtProt	NX_Q9UMD9.
Orphanet	79402. Generalized junctional epidermolysis bullosa, non-Herlitz type. 251393. Localized junctional epidermolysis bullosa, non-Herlitz type.
PharmGKB	PA26710.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG309396.
HOGENOM	HOG000111885.
HOVERGEN	HBG051065.
InParanoid	Q9UMD9.
KO	K07603.
OMA	LDYAELS.
OrthoDB	EOG4RNB7V.
PhylomeDB	Q9UMD9.
Enzyme and pathway databases
Pathway_Interaction_DB	a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
Reactome	REACT_111155. Cell-Cell communication. REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	Q9UMD9.
Bgee	Q9UMD9.
CleanEx	HS_COL17A1.
Genevestigator	Q9UMD9.
GermOnline	ENSG00000065618. Homo sapiens.
Family and domain databases
InterPro	IPR008160. Collagen. [Graphical view]
Pfam	PF01391. Collagen. 3 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1308.
NextBio	5353.
PMAP-CutDB	Q9UMD9.
SOURCE	Search...

Entry information

Entry name

COHA1_HUMAN

Accession

Primary (citable) accession number: Q9UMD9
Secondary accession number(s): Q02802 , Q5JV36, Q99018, Q9NQK9, Q9UC14

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 2, 2004
Last sequence update:	May 1, 2007
Last modified:	May 1, 2013
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.