COHA1_CANLF
ID COHA1_CANLF Reviewed; 1597 AA.
AC Q9N281;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 118.
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 homolog;
GN Name=COL17A1; Synonyms=BP180, BPAG2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-708, TISSUE SPECIFICITY, AND DISEASE.
RC TISSUE=Squamous cell carcinoma;
RX PubMed=10564722; DOI=10.1016/s0925-4439(99)00092-7;
RA Xu L., O'Toole E.A., Olivry T., Hernandez C., Peng J., Chen M., Chan L.S.;
RT "Molecular cloning of canine bullous pemphigoid antigen 2 cDNA and
RT immunomapping of NC16A domain by canine bullous pemphigoid
RT autoantibodies.";
RL Biochim. Biophys. Acta 1500:97-107(2000).
CC -!- FUNCTION: The 120 kDa linear IgA disease antigen homolog is an
CC anchoring filament component involved in dermal-epidermal cohesion.
CC {ECO:0000250}.
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 (via N-terminus). Interacts (via N-terminus) with
CC PLEC. Interacts (via cytoplasmic region) with DSP (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, hemidesmosome. Membrane; Single-
CC pass type II membrane protein. Note=Localized along the plasma membrane
CC of the hemidesmosome. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [120 kDa linear IgA disease antigen homolog]:
CC Secreted, extracellular space, extracellular matrix, basement membrane
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Upper lamina lucidalhemidesmosome.
CC {ECO:0000269|PubMed:10564722}.
CC -!- PTM: The intracellular/endo domain is disulfide-linked. {ECO:0000250}.
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 homolog. The shedding is mediated by membrane-bound
CC metalloproteases (By similarity). {ECO:0000250}.
CC -!- DISEASE: Note=Defects in COL17A1 are the cause of generalized atrophic
CC benign epidermolysis bullosa. This nonlethal form of junctional
CC epidermolysis bullosa is characterized by life-long blistering of the
CC skin, associated with hair and tooth abnormalities.
CC {ECO:0000269|PubMed:10564722}.
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DR EMBL; AAEX02015518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF016649; AAC27985.2; -; mRNA.
DR AlphaFoldDB; Q9N281; -.
DR STRING; 9615.ENSCAFP00000037321; -.
DR PaxDb; Q9N281; -.
DR PRIDE; Q9N281; -.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; Q9N281; -.
DR OMA; TRVMSYM; -.
DR TreeFam; TF332289; -.
DR Reactome; R-CFA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-CFA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-CFA-446107; Type I hemidesmosome assembly.
DR Reactome; R-CFA-8948216; Collagen chain trimerization.
DR Proteomes; UP000002254; Chromosome 28.
DR Bgee; ENSCAFG00000010547; Expressed in keratinocyte and 38 other tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030056; C:hemidesmosome; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0031581; P:hemidesmosome assembly; ISS:UniProtKB.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 1.
PE 2: Evidence at transcript level;
KW Basement membrane; Cell junction; Collagen; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Membrane;
KW Reference proteome; Repeat; Secreted; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1597
FT /note="Collagen alpha-1(XVII) chain"
FT /id="PRO_0000059405"
FT CHAIN 525..1597
FT /note="120 kDa linear IgA disease antigen homolog"
FT /evidence="ECO:0000250"
FT /id="PRO_0000342554"
FT TOPO_DOM 1..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 490..1597
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..567
FT /note="Nonhelical region (NC16A)"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..231
FT /note="Necessary for interaction with DST and for the
FT recruitment of DST to hemidesmosome"
FT /evidence="ECO:0000250"
FT REGION 168..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..1572
FT /note="Triple-helical region"
FT REGION 907..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1531..1566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1573..1597
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..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..839
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..926
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1036
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1311
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 100
FT /note="R -> G (in Ref. 2; AAC27985)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="N -> D (in Ref. 2; AAC27985)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="G -> EA (in Ref. 2; AAC27985)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="R -> K (in Ref. 2; AAC27985)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1597 AA; 163069 MW; 37BFB47E1FE3E547 CRC64;
MDVTKKNKRD GSEVTERIIT ETVSTRLTSL PPKGGTSNGY AKTGSLSGGS RLEKHSLTHG
SSGYINSSGS TRGNASTSSY RRAHSPASTL PNSPGSTFER KIHITRHGTY EGSSSGNSSP
EYPRKEFASS STRGRSQTRE SEIRVRLQSA SPSTRWTELD DVKRLLKGSR SASVSPTRNS
SNTLPIPKKG TVETKMVTAS SQSVSGTYDA TILDANLPSH MWSSTLPAGS SMGTYHNNVT
TQSSSLLNTN AYSAGSVFGV PNNMTSGSST LHPGVSTCSS VFGMQNNLAP SSSTLSHSTA
TASTAYGMKK NLPQSPAVVS TGVSTSAACT TNVQNEDLLH KDCKFLILEK DNTPAKKEME
LLIMTKDSGK VFTASPASIA ATSFSDDTLK KEKQAAYTAD TCLVSDANGD VKTVSTKGKA
ASAEMHNYNH RGGGSGGGGG GGGGGGGGPW GAAPAWCPCG SCCSWWKWLL GLLLTWLLLL
GLLFGLIALA EEVRALKARV AELEQSRSNV LLFKEEMQRA NKDWLQGEAP SVEAGGKLGL
DGHQQEELWL FVRNRLMAEQ ENGNLRGSPG PKGDMGSQGP KGDRGLPGTP GIPGVLGHPG
PQGPKGQKGS VGEPGMEGPM GQRGREGPMG PRGEPGPPGF GEKGDRGAAG EPGVQGPPGV
PGSVGPKGSG GSPGPRGPPG PMGPQGLRGE VGLPGIKGDK GPLGSPGPKG DQGEKGPRGL
TGEPGLRGLP GAVGEPGAKG AVGPAGPDGH QGPRGEQGLT GMPGTRGPPG PSGDPGKPGF
TGPQGPQGLP GTPGRPGAKG EPGAPGRIMT SEGSSTITVP GPPGPPGAMG PPGPPGAPGP
RGERGLAGES FMGSSSSISE LLSTRSFKEP MQTCHRASFL EARVAKTTPA LSGRHCVLDT
CRKGVDLRGP PGPPGPPGPP DLPFRVRQDP EAPQVKAELP GKRYESIGTQ SLGLALGKSL
PATSPQHRVL ETYFSGPPGP PGPPGPKGDQ GSSSLGLNLQ GPPGPRGPKG DKGGSSSSTM
FMPGPPGPPG PPGPPGSISS SGREIQQYIS EYLQSDSIRS YLSGVQGPPG PPGPPGPVTT
IAGETFDYSE LASRVSSYLQ TSGYSIGSSV SISTEDIVAA LQREYLRRAG GWEPWGLGLP
LPELLRASEE ALVLVPSGQG RPGCGRAVAR EPCGLGGPTP ALPVLAGDDV RQYLRQYVIG
DWSLQSLDYA ELSSRILSYM SSSGISIGLP GPPGPPGLPG TSYEELLSLL QGSEYRGIIG
PPGPPGPPGI PGNAWSSISV EDLSSYLHTA GVSSIPGPPG PPGPPGPRGP PGVSGALATY
AAENSDSFRS ELISYLTSPD VRSFIVGPPG PPGPQGPPGD SRLVSMDGSY SRDSRSSSHS
ASVSRGSSYS SSMGIGGASG GSLGEAGAFG LDMGLGRGYG GAAEGGMYGG EGGPLGAGFA
GGLDYNELAV RVSESLQRQG LLQGMAYTVQ GPPGQPGPQG PPGISKVFSA YSNVTEDLMD
FFRSKSTSVI VFLTPCCPVR GALQDHQVGL GHPALEGTRE KKETKVTKSM RGGEREASPS
SHELPLEEQP LASVLAMAYG VHVKISPKGG SWRLTSY
