COHA1_CHICK
ID COHA1_CHICK Reviewed; 1495 AA.
AC Q90584;
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 384-1495, AND TISSUE SPECIFICITY.
RC TISSUE=Cornea;
RX PubMed=1705041; DOI=10.1073/pnas.88.4.1560;
RA Marchant J.K., Linsenmayer T.F., Gordon M.K.;
RT "cDNA analysis predicts a cornea-specific collagen.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1560-1564(1991).
CC -!- FUNCTION: May play a role in the integrity of hemidesmosome and the
CC attachment of basal keratinocytes to the underlying basement membrane.
CC {ECO:0000250}.
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. {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: Cornea specific. {ECO:0000269|PubMed:1705041}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA48703.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M60172; AAA48703.1; ALT_FRAME; mRNA.
DR PIR; S16501; A38587.
DR RefSeq; NP_001292131.1; NM_001305202.1.
DR AlphaFoldDB; Q90584; -.
DR STRING; 9031.ENSGALP00000038357; -.
DR PRIDE; Q90584; -.
DR Ensembl; ENSGALT00000073791; ENSGALP00000050588; ENSGALG00000029617.
DR GeneID; 396503; -.
DR KEGG; gga:396503; -.
DR CTD; 1308; -.
DR VEuPathDB; HostDB:geneid_396503; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000161242; -.
DR HOGENOM; CLU_004285_0_0_1; -.
DR InParanoid; Q90584; -.
DR OrthoDB; 718661at2759; -.
DR PhylomeDB; Q90584; -.
DR Reactome; R-GGA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-GGA-8948216; Collagen chain trimerization.
DR PRO; PR:Q90584; -.
DR Proteomes; UP000000539; Chromosome 6.
DR Bgee; ENSGALG00000029617; Expressed in colon and 3 other tissues.
DR ExpressionAtlas; Q90584; baseline and differential.
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; IEA:UniProtKB-SubCell.
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 InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 6.
PE 2: Evidence at transcript level;
KW Basement membrane; Cell junction; Collagen; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1495
FT /note="Collagen alpha-1(XVII) chain"
FT /id="PRO_0000059409"
FT CHAIN 497..1495
FT /note="120 kDa linear IgA disease antigen homolog"
FT /evidence="ECO:0000250"
FT /id="PRO_0000342559"
FT TOPO_DOM 1..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..1495
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..535
FT /note="Nonhelical region (NC16)"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..1482
FT /note="Triple-helical region"
FT REGION 847..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1483..1495
FT /note="Nonhelical region (NC1)"
FT COMPBIAS 15..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..808
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..885
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..914
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..959
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..994
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1336
FT /note="Polar 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 CARBOHYD 1424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 384
FT /note="T -> P (in Ref. 2; AAA48703)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="A -> P (in Ref. 2; AAA48703)"
FT /evidence="ECO:0000305"
FT CONFLICT 684
FT /note="R -> H (in Ref. 2; AAA48703)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="M -> I (in Ref. 2; AAA48703)"
FT /evidence="ECO:0000305"
FT CONFLICT 826
FT /note="G -> V (in Ref. 2; AAA48703)"
FT /evidence="ECO:0000305"
FT CONFLICT 1185
FT /note="I -> T (in Ref. 2; AAA48703)"
FT /evidence="ECO:0000305"
FT CONFLICT 1260
FT /note="P -> S (in Ref. 2; AAA48703)"
FT /evidence="ECO:0000305"
FT CONFLICT 1264
FT /note="R -> P (in Ref. 2; AAA48703)"
FT /evidence="ECO:0000305"
FT CONFLICT 1311
FT /note="S -> T (in Ref. 2; AAA48703)"
FT /evidence="ECO:0000305"
FT CONFLICT 1463
FT /note="Missing (in Ref. 2; AAA48703)"
FT /evidence="ECO:0000305"
FT CONFLICT 1469
FT /note="Missing (in Ref. 2; AAA48703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1495 AA; 151204 MW; BE8D8BE3A02BCC0F CRC64;
MDSVTKKTRQ DGSEVTERQG GSSSGLKTSS HTGGSGVEKR SYTHSSGYVT SSGSGRLNSS
SSGYRQTQSP SSTLTKSPGS TFERKTYVNR HATYEGSSSA NSSPEFPRKE FASASTRGRS
QSRESEIRVR LQSASPSGRW TELDDVKRLL KGSRSASCSP TRSSSSTLPI PKKAVVETKM
VTESSQSVSG TYDTTILNTT LPPYTWSSTL PAGSSLGGYH NSMGQSSSLI NAMSHSTGSV
FGVPNNLAPS SHALNTGLST SSTVFGVQNN LSPSSSALNA SAASAAYGMK NTSQTNTMNS
TGVSASAGGT ILSSQGDDFL HKDCKFLLLE KENAPAKKEM ELLVMTKDSG KVFSASSTGL
NGGSFAEDTL KKEKQGLSSY AADTGLKSDA NGGLKSAPTR DKATYAEIQN GGAGGAIGSA
PSWCPCGSCC SWWKWLLGLL LAWLLLLGLL FGLIALAEEV RKLKSRVDNL EKINHSFLTV
NQGNPYLEKD VSKVDFLHGV APSSTFPFEN EESVWLMVKS RLNKEIERGY FRGERGEPGM
KGDMGLQGPK GDRGLPGVPG IPGPVGHQGP EGPKGQKGSM GDPGMEGPMG QRGREGLPGP
RGEPGPPGFG EKGDRGAAGP PGPPGPPGSA GLKGPMGSPG PQGPPGPPGL QGFRGEAGLP
GAKGEKGATG PPGPKGDQGE KGARGMTGEQ GSRGIPGPPG EPGAKGPAGQ AGRDGQPGER
GEPGLMGMPG ARGPPGPSGD TGEPGLTGPQ GPPGLPGNPG RPGAKGEPGA PGKVISAEGS
STIALPGPPG PPGPIGPTGP PGVPGPVGPA GLPGQQGPRG EKGSAGEVVI ETIKTEVSSL
ASQMLSDLQG RAGPPGPPGP PGESVQGLPG PRGPPGLPGP SGPPGRPGSS VSTSETFVSG
PPGPPGPPGP KGDQGEPGPR GFTGEPGEPG LPGFSSHGGT VTMQGPPGPP GPPGPKGDAG
VPGAPGIPGT SRGGSRQIQG PPGPPGPPGP PGPGGSSSQE IQQYVADYLK SDNVRHYLTG
VQGPPGPPGP PGILTTADGK NFDFAELATR VMSYVTSSSD HYQSFASSVS TTSVLYQELL
NMLQREEIRQ YLVGPRGPPG PPGPGVDGMS LSLDYDELTR RFISYLTSSG MSIGLPGPPG
PPGTPGISYS ELTAYLRNSE FSGLVGPPGP AGPPGPPGIP GSSGISLEDI SAYLQSVGYS
SISGIQGPPG PPGPPGPPGF SGTGLLSYAD ITHSDEFRSE LIQYLKSDEV RSYISGPPGP
PGPRGPPGPK GDSGLVAGSM SSLYHDSLAS ERLHGGSIGA EGSHGGSLGA SSSYGSSMSS
SMSSYSASMG SDGSYGASVG SDGSFDGLLT AEESHRRSAG PGRSYSSSFT GSLDYNELAR
HVSENLQSRG ILQDLMSYTG QGPPGPPGPP GPPGISRVFA AYGNVTEDLM DFFRTHGTVR
GPPGEKGERG YPGPKGDPGP MGPPGRHGQR GPKGEKGEKG EQMYSGRRRR RSVGV
