COHA1_BOVIN
ID COHA1_BOVIN Reviewed; 1473 AA.
AC A6QPB3;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION, AND SHEDDING.
RX PubMed=9545306; DOI=10.1074/jbc.273.16.9711;
RA Hirako Y., Usukura J., Uematsu J., Hashimoto T., Kitajima Y., Owaribe K.;
RT "Cleavage of BP180, a 180-kDa bullous pemphigoid antigen, yields a 120-kDa
RT collagenous extracellular polypeptide.";
RL J. Biol. Chem. 273:9711-9717(1998).
RN [3]
RP SHEDDING, AND FUNCTION.
RX PubMed=12761182; DOI=10.1093/jb/mvg024;
RA Hirako Y., Yoshino K., Zillikens D., Owaribe K.;
RT "Extracellular cleavage of bullous pemphigoid antigen 180/type XVII
RT collagen and its involvement in hemidesmosomal disassembly.";
RL J. Biochem. 133:197-206(2003).
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:0000269|PubMed:12761182}.
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
CC {ECO:0000269|PubMed:9545306}. Membrane {ECO:0000269|PubMed:9545306};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:9545306}.
CC Note=Localized along the plasma membrane of the hemidesmosome.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [120 kDa linear IgA disease antigen homolog]:
CC Secreted, extracellular space, extracellular matrix, basement membrane.
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.
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DR EMBL; BC149236; AAI49237.1; -; mRNA.
DR RefSeq; NP_001095450.1; NM_001101980.1.
DR AlphaFoldDB; A6QPB3; -.
DR SMR; A6QPB3; -.
DR STRING; 9913.ENSBTAP00000013271; -.
DR PaxDb; A6QPB3; -.
DR PeptideAtlas; A6QPB3; -.
DR PRIDE; A6QPB3; -.
DR GeneID; 513804; -.
DR KEGG; bta:513804; -.
DR CTD; 1308; -.
DR eggNOG; KOG3544; Eukaryota.
DR HOGENOM; CLU_004285_0_0_1; -.
DR InParanoid; A6QPB3; -.
DR TreeFam; TF332289; -.
DR Proteomes; UP000009136; Unplaced.
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; 5.
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..1473
FT /note="Collagen alpha-1(XVII) chain"
FT /id="PRO_0000342552"
FT CHAIN ?..1473
FT /note="120 kDa linear IgA disease antigen homolog"
FT /id="PRO_0000342553"
FT TOPO_DOM 1..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..1473
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..572
FT /note="Nonhelical region (NC16)"
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 567..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..1459
FT /note="Triple-helical region"
FT REGION 1173..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1460..1473
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 813..836
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..900
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..927
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1210
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 1279..1308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1473 AA; 149154 MW; DAF3B1BAECD28177 CRC64;
MDITQKNKRD GTEVTERIIT ETVTTRLTSL PPKGGTSNGY AKTGSLGGGS RLEKQSLTHG
SSGYINSSGS LRGNASTSSY RRAHSPASTL PNSPGSTFER KTHVTRHGTY EGSSSGNSSP
EYPRKEFASS STRGRSQTRE SEIRVRLQSA SPSTRWTELD DVKRLLKGSR SASVSPTRNS
SNTLPIPKKG TVETKVVTAS SQSVSGTYDT TILDANLPSH VWSSTLPAGS SMGTYHNNIT
TQSSSLLNTN AYSAGSVFGV PNNMASCSAT LQPGISTSSS VFGMQNNLAP SSSTLSHGMA
ATSTAYGVKK NMPQSPTAVS TGVSTSAAST TNVQNDDLLH KDCKFLILEK DNTPAKKEME
LLIMTKDSGK VFTASPASVA ATSFSEDTLK KEKQAAYTDT YLVSEANGDV KTVTAKGNGA
SADIHGYDHR RGGGGGGGSG GALGSGAAGG GGKGSWGAAP TWCPCGSWCS WWKWLLGLLL
TWLLLLGLLF GLIALAEEVR KLKARVEELE KMRGRLSYNE KMERSSQDSV QGVAPRLGEG
LGKSELDDYN LEDVWQFMKV RLMTEQENGN LRGSPGPKGD MGVQGPKGDR GFPGTPGIPG
PLGHQGPEGP KGQKGNVGEP GMEGPMGQRG REGPMGPRGE PGPPGFGEKG DRGDAGKPGI
PGPPGVPGSV GPKGSIGPQG LRGEVGLPGI KGDKGPMGPP GPKGDQGEKG PRGLTGEPGL
KGLPGAVGEP GAKGAMGPAG PDGHQGPRGE QGLPGMPGTR GLPGPSGDPG KPGLTGPQGP
QGIPGTPGRP GVKGEPGAPG KIMTSEGSST ITVPGPPGPP GAMGPPGPPG APGPVGPAGL
PGQQGPRGEP GLAGESFMGS SSSFSEVLST QGIDLRGPPG PPGPPGPPGE GLPGPPGPPG
SLLTSSETFF SGPPGPPGPP GPKGDQGPPG PRGHQGERGF PGLSGSGSSS LGLNLQGPPG
PPGPQGPKGD KGDPGVPGAP GIPGGPSRGG SSSSTTFMQG PPGPPGPPGP PGSLSSSGLE
IQQYISDYMQ SDSIRPYLSG VQGPPGPPGP PGPVTTITGE TFNYSELASL VVSYLQTSGY
NIGTSSTSIS SEDILAALRR DDVRQYLQQY LMPQGAGGDW FLQSLDYAEL SNRILSYMSS
TGVSIGLPGP PGPPGLPGTS YEELLSLLQG SEFRGIVGPP GPPGPPGLPG SSWSSISTED
LSSYLQTAGL SSIPGPPGPP GPPGPRGPPG ISGALATYAA ENSDSFRSEL ISYLTSPDVR
SFIVGPPGPP GPQGPPGDTR LVSTDSSYSR SGSSSSFSRD TSYSSSMGIG GASGGSLGEA
GAFGMDMGRG YGAAAESGMY GGNGRFGTSF AGGLDYNELA VRVSESLQRQ GLLQGMAYTV
QGPPGRPGPQ GPPGISKIFS AYSNVTEDLM DFFRTYGAIP GPPGQKGEMG IPGPKGERGP
AGPPGPRGHK GEKGDKGDQF YIGRRRRSIA VKP
