COHA1_MOUSE
ID COHA1_MOUSE Reviewed; 1470 AA.
AC Q07563; Q08AT3; Q3UXX1; Q99LK8;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 167.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ;
RX PubMed=8473327; DOI=10.1016/s0021-9258(18)52948-3;
RA Li K., Tamai K., Tan E.M.L., Uitto J.;
RT "Cloning of type XVII collagen: complementary and genomic DNA sequences of
RT mouse 180-kDa bullous pemphigoid antigen (BPAG2) predict an interrupted
RT collagenous domain, a transmembrane segment, and unusual features in the
RT 5'-end of the gene and the 3' -.";
RL J. Biol. Chem. 268:8825-8834(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1357-1470.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 -!- INTERACTION:
CC Q07563; P08246: ELANE; Xeno; NbExp=2; IntAct=EBI-6251005, EBI-986345;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q07563-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q07563-2; Sequence=VSP_009362;
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 551 (By similarity). {ECO:0000250}.
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DR EMBL; L08407; AAA37443.1; -; mRNA.
DR EMBL; AC131719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003208; AAH03208.1; -; mRNA.
DR EMBL; BC125031; AAI25032.1; -; mRNA.
DR EMBL; BC125032; AAI25033.1; -; mRNA.
DR EMBL; AK135150; BAE22442.1; -; mRNA.
DR CCDS; CCDS38018.1; -. [Q07563-2]
DR CCDS; CCDS70959.1; -. [Q07563-1]
DR PIR; A46053; A46053.
DR RefSeq; NP_001277754.1; NM_001290825.1. [Q07563-1]
DR RefSeq; NP_031758.2; NM_007732.2. [Q07563-2]
DR AlphaFoldDB; Q07563; -.
DR ComplexPortal; CPX-2995; Collagen type XVII trimer.
DR IntAct; Q07563; 1.
DR STRING; 10090.ENSMUSP00000084141; -.
DR GlyGen; Q07563; 2 sites.
DR iPTMnet; Q07563; -.
DR PhosphoSitePlus; Q07563; -.
DR jPOST; Q07563; -.
DR PaxDb; Q07563; -.
DR PRIDE; Q07563; -.
DR ProteomicsDB; 283423; -. [Q07563-1]
DR ProteomicsDB; 283424; -. [Q07563-2]
DR Antibodypedia; 18201; 242 antibodies from 29 providers.
DR DNASU; 12821; -.
DR Ensembl; ENSMUST00000026045; ENSMUSP00000026045; ENSMUSG00000025064. [Q07563-1]
DR Ensembl; ENSMUST00000086923; ENSMUSP00000084141; ENSMUSG00000025064. [Q07563-2]
DR GeneID; 12821; -.
DR KEGG; mmu:12821; -.
DR UCSC; uc008hvi.2; mouse. [Q07563-2]
DR UCSC; uc008hvj.2; mouse. [Q07563-1]
DR CTD; 1308; -.
DR MGI; MGI:88450; Col17a1.
DR VEuPathDB; HostDB:ENSMUSG00000025064; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000161242; -.
DR HOGENOM; CLU_004285_0_0_1; -.
DR InParanoid; Q07563; -.
DR OMA; TRVMSYM; -.
DR OrthoDB; 718661at2759; -.
DR PhylomeDB; Q07563; -.
DR TreeFam; TF332289; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-446107; Type I hemidesmosome assembly.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12821; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Col17a1; mouse.
DR PRO; PR:Q07563; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q07563; protein.
DR Bgee; ENSMUSG00000025064; Expressed in substantia propria of cornea and 103 other tissues.
DR Genevisible; Q07563; MM.
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; IDA:MGI.
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; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Cell junction; Collagen;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..1470
FT /note="Collagen alpha-1(XVII) chain"
FT /id="PRO_0000059408"
FT CHAIN 531..1470
FT /note="120 kDa linear IgA disease antigen homolog"
FT /evidence="ECO:0000250"
FT /id="PRO_0000342558"
FT TOPO_DOM 1..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..1470
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..573
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 167..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..1456
FT /note="Triple-helical region"
FT REGION 885..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1457..1470
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..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..849
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..927
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..953
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1216
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 551
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q9UMD9"
FT CARBOHYD 1273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1157..1194
FT /note="GSDYRNIIGPPGPPGPPGMPGNAWSSISVEDLSSYLHT -> A (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:8473327"
FT /id="VSP_009362"
FT CONFLICT 164
FT /note="R -> S (in Ref. 1; AAA37443)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="A -> G (in Ref. 1; AAA37443)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="S -> C (in Ref. 1; AAA37443)"
FT /evidence="ECO:0000305"
FT CONFLICT 1275
FT /note="S -> G (in Ref. 3; AAH03208)"
FT /evidence="ECO:0000305"
FT CONFLICT 1277
FT /note="N -> S (in Ref. 1; AAA37443 and 3; AAH03208/
FT AAI25032/AAI25033)"
FT /evidence="ECO:0000305"
FT CONFLICT 1292
FT /note="T -> I (in Ref. 1; AAA37443 and 3; AAH03208/
FT AAI25032/AAI25033)"
FT /evidence="ECO:0000305"
FT CONFLICT 1388
FT /note="R -> W (in Ref. 1; AAA37443)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1470 AA; 147975 MW; 7C38356D6ED68347 CRC64;
MDVTKKSKRD GTEVTERIVT ETVTTRLTSL PPKGSTSNGY AKTGSLGGGS RLEKQSLTHG
SSGYINSSGS IRGNASTSSY RRTHSPASTL PNSPGSTFER KAHMTRHGTY EGSSSGNSSP
EYPRKELASS STRGRSQTRE SEIRVRLQSA SPSTRWTELD EVKRLLKGSR SASASPTRNT
SNTLPIPKKG TVETKTVTAS SHSVSGTYDS AILDTNFPPH MWSSTLPAGS SLGTYQNNIT
AQSTSLLNTN AYSTGSVFGV PNNMASCSPT LHPGLSSCSS VFGMQNNLAP SSSVLSHGTT
TASTAYGAKK NVPQPPTVTS TGVSTSATCT TSVQSDDLLH KDCKFLILEK DNTPAKKEME
LLIMTKDSGK VFTASPATIS STSFSEDTLK KEKQAAYAAD TCLKADVNGD LNTVSTKSKM
TSAENHGYDR GGGGGRGKGG GAGGGGGGGG ASGGGGAWGA APAWCPCGSC CSWWKWLLGL
LLTWLLLLGL LFGLIALAEE VRKLKARVEE LEKTKVLYHD VQMDKSNRDR LQAEAPSLGP
GLGKAELDGY SQEAIWLFVR NKLMTEQENG NLRGSPGPKG DMGSQGPKGD RGLPGTPGIP
GPLGHPGPEG PKGQKGSIGD PGMEGPIGQR GLAGPMGPRG EPGPPGSGEK GDRGIAGEQG
PQGLPGVPGP PGLRGHSGSP GPQGPPGAVG PQGLRGDVGL PGVKGDKGLM GPPGPKGDQG
EKGPRGLTGE PGIRGLPGAV GEPGAKGAMG PAGADGQQGS RGEQGLTGMP GTRGPPGPAG
DPGKPGLTGP QGPQGLPGSP GRPGTKGEPG APGRVMTSEG SSTITVPGPP GPPGAMGPPG
PPGTPGPAGP AGLPGQQGPR GEPGLAGDSF LSSGSSISEV LSAQGVDLRG PPGPPGPRGP
PGPSIPGPPG PRGPPGEGVP GPPGPPGSFL TDSETFFTGP PGPPGPPGPK GDQGDPGVPG
TPGISGGLSH GASSSTLYMQ GPPGPPGPPG PPGSLSSSGQ DIQHYIAEYM QSDNIRTYLS
GVQGPPGPPG PPGPVITITG ETFDYSQLAS QVVSYLRSSG YGAGLSSASS SEDILAMLRR
NDVWQYLRQN LVGPPGPPGP PGVSGDGSLL SLDYGELSRH ILNYMSSSGI SFGHPGPPGP
PGLPGTSYEE LLTMLRGSDY RNIIGPPGPP GPPGMPGNAW SSISVEDLSS YLHTAGLSSI
PGPPGPPGPP GPRGPPGVSA ALSTYAAENS DNFRSELISY LTSPDVRSFI VGPPGPPGPQ
GPPGDGHLRE NYNWSSNSSA RRGTSYSSST GTGGTNGGSL GEGGAYGAGD GGPYGTDIGP
GGGYGAAAGG GIYGTNGDSF RDGFTGDLDY NKLAVRVSES MQRQGLLQGM AYTVQGPPGP
QGPPGISRVF SAYSNVTQDL MDFFQTYGTI PGPPGQKGDV GTPGPKGDRG PAGPRGPPGP
PGPRGNKGEK GDKGDQVYTG RRKRSIAIKP
