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   27-MAR-2024, entry version 176.
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.ENSMUSP00000026045; -.
DR   GlyCosmos; Q07563; 2 sites, No reported glycans.
DR   GlyGen; Q07563; 2 sites.
DR   iPTMnet; Q07563; -.
DR   PhosphoSitePlus; Q07563; -.
DR   jPOST; Q07563; -.
DR   PaxDb; 10090-ENSMUSP00000084141; -.
DR   ProteomicsDB; 283423; -. [Q07563-1]
DR   ProteomicsDB; 283424; -. [Q07563-2]
DR   ABCD; Q07563; 24 sequenced antibodies.
DR   Antibodypedia; 18201; 308 antibodies from 29 providers.
DR   DNASU; 12821; -.
DR   Ensembl; ENSMUST00000026045.14; ENSMUSP00000026045.8; ENSMUSG00000025064.16. [Q07563-1]
DR   Ensembl; ENSMUST00000086923.6; ENSMUSP00000084141.6; ENSMUSG00000025064.16. [Q07563-2]
DR   GeneID; 12821; -.
DR   KEGG; mmu:12821; -.
DR   UCSC; uc008hvi.2; mouse. [Q07563-2]
DR   UCSC; uc008hvj.2; mouse. [Q07563-1]
DR   AGR; MGI:88450; -.
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; YRQTQSP; -.
DR   OrthoDB; 5362506at2759; -.
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-446107; Type I hemidesmosome assembly.
DR   Reactome; R-MMU-8948216; Collagen chain trimerization.
DR   BioGRID-ORCS; 12821; 3 hits in 79 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 104 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0062023; C:collagen-containing 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:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR   GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0031581; P:hemidesmosome assembly; ISS:UniProtKB.
DR   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 2.
DR   InterPro; IPR008160; Collagen.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1082; COLLAGEN ALPHA-1(X) CHAIN; 1.
DR   Pfam; PF01391; Collagen; 5.
DR   Genevisible; Q07563; MM.
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;
FT                   AAH03208/AAI25032/AAI25033)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1292
FT                   /note="T -> I (in Ref. 1; AAA37443 and 3;
FT                   AAH03208/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
//