COHA1_MESAU
ID COHA1_MESAU Reviewed; 1431 AA.
AC Q9JMH4;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 86.
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 Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yamamoto K., Inoue N., Fujimori A., Saito T., Shinkai H., Sakiyama H.;
RT "Mesocricetus auratus mRNA for type XVII collagen.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
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. 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 -!- 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. This cleavage is inhibited by phosphorylation at Ser-
CC 547 (By similarity). {ECO:0000250}.
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DR EMBL; AB027759; BAA94381.1; -; mRNA.
DR RefSeq; NP_001268505.1; NM_001281576.1.
DR AlphaFoldDB; Q9JMH4; -.
DR STRING; 10036.XP_005063541.1; -.
DR PRIDE; Q9JMH4; -.
DR GeneID; 101843802; -.
DR CTD; 1308; -.
DR eggNOG; KOG3544; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030056; C:hemidesmosome; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031581; P:hemidesmosome assembly; ISS:UniProtKB.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 4.
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..1431
FT /note="Collagen alpha-1(XVII) chain"
FT /id="PRO_0000059407"
FT CHAIN 527..1431
FT /note="120 kDa linear IgA disease antigen homolog"
FT /evidence="ECO:0000250"
FT /id="PRO_0000342557"
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..1431
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..569
FT /note="Nonhelical region (NC16)"
FT REGION 25..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 167..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..1417
FT /note="Triple-helical region"
FT REGION 884..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1366..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1418..1431
FT /note="Nonhelical region (NC1)"
FT COMPBIAS 25..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 822..844
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..919
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..950
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 547
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q9UMD9"
FT CARBOHYD 1230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1431 AA; 144580 MW; 4315631FEB2C9A5C CRC64;
MDVTKKNKRD GTEVTERIVT EIVTTRLTSL PPKGSTSNGY AKTGSLGGGS RLEKQSLTHG
SSGYINSSGS IRGNASTSSY RRAHSPASTL PNSPGSTFER KTHMTRHGTY EGSSSGNSSP
EYPRKELASS ATRGRSQTRE SEIRVRLQSA SPSTRWTELD EVKRLLKGSR SASASPTRNT
SSTLPIPKKG TVETKMVTAS SHSVSGTYDT TALDTNLPSH MWSSTLPAGS SMGTYHNNMT
TQSSSLLNTN AYSAGSVFGM PNNMASCSPT LLPGLSSCSS VFGMQNNLAP SSSVPAHGTT
TAPTAYGVKK NVPQPPTVTS TGVSTSATCT TSVQSDDLLH KDCKFLILEK DNVPSKKEME
LLIMTKDSGK VFTASPASVS TTSFSEDTLK KEKQAAYAAD ACLKADINGD LNTVSTKGKA
TSVENHNYDR GGGSGGGARG GGGSGGGGGG GGTWGAAPAW CPCGSCCSWW KWLLGLLLTW
LLLLGLLFGL IALAEEVRKL KARVDELERT RVQYFEDKTE RSSKDRLLGD MPGVGPGLGK
AELDGHSQEA IWLFVRNKLM TEQENGNLRG NPGPKGDMGS QGPKGDRGLP GTAGIPGPLG
HPGPEGPKGQ KGSIGDPGME GPIGQRGLEG PMGPRGEPGP PGSGEKGDRG IAGEQGPRGL
PGVPGSVGPR GPNGSPGPQG PPGSTGPQGL RGEVGLPGVK GDKGLAGPPG PKGDQGEKGP
RGLTGEPGVR GLPGAVGEPG AKGAMGPAGP DGQQGPRGEQ GLTGMPGTRG LPGPSGDPGK
PGVTGPQGPQ GLPGSPGRPG TKGEPGAPGR VMTAEGSSTI TVPGPPGPPG AMGPPGPSGT
PGPAGPAGLP GQTKAQRGEP GLAGDSFISS GSSISEVLAA QGVDLRGPLG PPGPRGPPGP
SIPGPPGPRG PPGEGVPGPP GLPGSFLTDS ETFFSGPPGP PGPPGPKGDQ GDPGVPGTPG
IPGGHSHGES SSTTYRQGPP GPPGPPGPPG SFSSSGQDIQ RYIAEYMQSD SIRTYLSGVQ
GPPGPPGPPG PVITITGETF DYSQLASQVV SYLRTSGYGV SLSSASSEDI LAMLRRNDVW
QFLRQHLVGP PGPPGPPGVG GDGSLLSLDY GELSRHILNY MSSSGISFGH PGPPGPPGLP
GTSYEELLTM LRGSDYRDII GPPGPPGPPG PRGPPGVSAA LATYAAENSD NFRSELIGYL
TSPDVRSFII GPPGPPGPQG PPGDSHLRDN YSWGSSSSAR RGTAYSSSVG MGGANGGSLG
EGRTFGTGDG GPYGTDIGPG GGYGAAAGGI YGTDGDSFRA GFTGDLDYNK LAVRVSESMQ
RQGLLQGMAY TVQGPPGVPG PQGPPGISKV FSAYSNVTQD LMDFFRTHGA IPGPPGQKGE
AGTPGPKGDR GLAGQRGPPG PPGPRGQKGD KGDKGDQVYT GRRRRSIAIK P
