ID   CO7A1_MOUSE             Reviewed;        2944 AA.
AC   Q63870; Q78EC6;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 3.
DT   27-MAR-2024, entry version 169.
DE   RecName: Full=Collagen alpha-1(VII) chain;
DE   AltName: Full=Long-chain collagen;
DE            Short=LC collagen;
DE   Flags: Precursor;
GN   Name=Col7a1 {ECO:0000312|MGI:MGI:88462};
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] {ECO:0000312|EMBL:AAB66593.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8752674; DOI=10.1111/1523-1747.ep12349019;
RA   Kivirikko S., Li K., Christiano A.M., Uitto J.;
RT   "Cloning of mouse type VII collagen reveals evolutionary conservation of
RT   functional protein domains and genomic organization.";
RL   J. Invest. Dermatol. 106:1300-1306(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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] {ECO:0000305, ECO:0000312|EMBL:AAB27492.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1139-2058.
RX   PubMed=8325648; DOI=10.1006/geno.1993.1255;
RA   Li K., Christiano A.M., Copeland N.G., Gilbert D.J., Chu M.-L.,
RA   Jenkins N.A., Uitto J.;
RT   "cDNA cloning and chromosomal mapping of the mouse type VII collagen gene
RT   (Col7a1): evidence for rapid evolutionary divergence of the gene.";
RL   Genomics 16:733-739(1993).
RN   [4] {ECO:0000305}
RP   DISRUPTION PHENOTYPE.
RX   PubMed=10523500; DOI=10.1242/jcs.112.21.3641;
RA   Heinonen S., Mannikko M., Klement J.F., Whitaker-Menezes D., Murphy G.F.,
RA   Uitto J.;
RT   "Targeted inactivation of the type VII collagen gene (Col7a1) in mice
RT   results in severe blistering phenotype: a model for recessive dystrophic
RT   epidermolysis bullosa.";
RL   J. Cell Sci. 112:3641-3648(1999).
RN   [5] {ECO:0000305}
RP   INDUCTION.
RX   PubMed=14675198; DOI=10.1111/j.1523-1747.2003.12640.x;
RA   Naso M., Uitto J., Klement J.F.;
RT   "Transcriptional control of the mouse Col7a1 gene in keratinocytes: basal
RT   and transforming growth factor-beta regulated expression.";
RL   J. Invest. Dermatol. 121:1469-1478(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Stratified squamous epithelial basement membrane protein that
CC       forms anchoring fibrils which may contribute to epithelial basement
CC       membrane organization and adherence by interacting with extracellular
CC       matrix (ECM) proteins such as type IV collagen.
CC       {ECO:0000250|UniProtKB:Q02388, ECO:0000269|PubMed:10523500}.
CC   -!- SUBUNIT: Homotrimer. Interacts with MIA3/TANGO1; facilitating its
CC       loading into transport carriers and subsequent secretion (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q63870; Q63870: Col7a1; NbExp=2; IntAct=EBI-8313134, EBI-8313134;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000250}.
CC   -!- INDUCTION: Transcription of COL7A1 is stimulated by TGFB1 in
CC       keratinocytes and this is possibly dependent on a putative interaction
CC       between SMADS and AP1. {ECO:0000269|PubMed:14675198}.
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. {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Mice do not express type VII collagen in their
CC       skin; they are born with extensive cutaneous blistering and die during
CC       the first two weeks of life, possibly because of complications arising
CC       from blistering; this mouse mutant resembles the autosomal recessive
CC       inherited form of the dystrophic epidermolysis bullosa (DEB) in humans.
CC       Heterozygotes by comparison display a normal phenotype.
CC       {ECO:0000269|PubMed:10523500}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U32107; AAB66593.1; -; mRNA.
DR   EMBL; AC174646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S63654; AAB27492.1; -; mRNA.
DR   CCDS; CCDS40770.1; -.
DR   PIR; A45748; A45748.
DR   RefSeq; NP_031764.2; NM_007738.3.
DR   RefSeq; XP_006511998.1; XM_006511935.3.
DR   PDB; 6S4C; X-ray; 2.00 A; A=1048-1238.
DR   PDBsum; 6S4C; -.
DR   SMR; Q63870; -.
DR   BioGRID; 198826; 2.
DR   ComplexPortal; CPX-2966; Collagen type VII trimer.
DR   MINT; Q63870; -.
DR   STRING; 10090.ENSMUSP00000107701; -.
DR   MEROPS; I02.967; -.
DR   GlyCosmos; Q63870; 3 sites, No reported glycans.
DR   GlyGen; Q63870; 3 sites.
DR   iPTMnet; Q63870; -.
DR   PhosphoSitePlus; Q63870; -.
DR   jPOST; Q63870; -.
DR   MaxQB; Q63870; -.
DR   PaxDb; 10090-ENSMUSP00000107701; -.
DR   PeptideAtlas; Q63870; -.
DR   ProteomicsDB; 283671; -.
DR   DNASU; 12836; -.
DR   Ensembl; ENSMUST00000026740.6; ENSMUSP00000026740.6; ENSMUSG00000025650.14.
DR   Ensembl; ENSMUST00000112070.8; ENSMUSP00000107701.2; ENSMUSG00000025650.14.
DR   GeneID; 12836; -.
DR   KEGG; mmu:12836; -.
DR   UCSC; uc009rrh.1; mouse.
DR   AGR; MGI:88462; -.
DR   CTD; 1294; -.
DR   MGI; MGI:88462; Col7a1.
DR   VEuPathDB; HostDB:ENSMUSG00000025650; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000163668; -.
DR   HOGENOM; CLU_000510_0_0_1; -.
DR   InParanoid; Q63870; -.
DR   OMA; QTFFAVD; -.
DR   OrthoDB; 5353225at2759; -.
DR   PhylomeDB; Q63870; -.
DR   TreeFam; TF351645; -.
DR   Reactome; R-MMU-1442490; Collagen degradation.
DR   Reactome; R-MMU-1474244; Extracellular matrix organization.
DR   Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR   Reactome; R-MMU-216083; Integrin cell surface interactions.
DR   Reactome; R-MMU-2214320; Anchoring fibril formation.
DR   Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR   Reactome; R-MMU-8948216; Collagen chain trimerization.
DR   BioGRID-ORCS; 12836; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Col7a1; mouse.
DR   PRO; PR:Q63870; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q63870; Protein.
DR   Bgee; ENSMUSG00000025650; Expressed in lip and 184 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   CDD; cd00063; FN3; 9.
DR   CDD; cd22627; Kunitz_collagen_alpha1_VII; 1.
DR   CDD; cd01482; vWA_collagen_alphaI-XII-like; 1.
DR   CDD; cd01450; vWFA_subfamily_ECM; 1.
DR   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 9.
DR   Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 2.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1100; FIBRILLAR COLLAGEN NC1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01391; Collagen; 19.
DR   Pfam; PF00041; fn3; 7.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   Pfam; PF00092; VWA; 2.
DR   PRINTS; PR00759; BASICPTASE.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00060; FN3; 9.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF57362; BPTI-like; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 5.
DR   SUPFAM; SSF53300; vWA-like; 2.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR   PROSITE; PS50853; FN3; 9.
DR   PROSITE; PS50234; VWFA; 2.
DR   Genevisible; Q63870; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Basement membrane; Cell adhesion; Collagen; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Hydroxylation; Protease inhibitor;
KW   Reference proteome; Repeat; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..2944
FT                   /note="Collagen alpha-1(VII) chain"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000282951"
FT   DOMAIN          39..212
FT                   /note="VWFA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          235..330
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          331..417
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          418..508
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          511..598
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          601..688
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          689..776
FT                   /note="Fibronectin type-III 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          779..867
FT                   /note="Fibronectin type-III 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          870..957
FT                   /note="Fibronectin type-III 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          959..1053
FT                   /note="Fibronectin type-III 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1055..1230
FT                   /note="VWFA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          2879..2931
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   REGION          18..1254
FT                   /note="Nonhelical region (NC1)"
FT                   /evidence="ECO:0000255"
FT   REGION          1255..2775
FT                   /note="Triple-helical region"
FT                   /evidence="ECO:0000255"
FT   REGION          1255..1475
FT                   /note="Interrupted collagenous region"
FT                   /evidence="ECO:0000255"
FT   REGION          1259..1934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1960..2773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2776..2944
FT                   /note="Nonhelical region (NC2)"
FT                   /evidence="ECO:0000255"
FT   MOTIF           1171..1173
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           2002..2004
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           2063..2065
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           2601..2603
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           2631..2633
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1271..1285
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1366..1390
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1708..1722
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1842..1868
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2014..2030
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2050..2067
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2073..2087
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2172..2186
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2269..2283
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2368..2382
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2425..2439
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2528..2547
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2620..2637
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            2889..2890
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2158
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2167
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2176
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2179
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2616
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2622
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2655
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2658
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2664
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        787
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        2625
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        2793
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        2795
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        2879..2931
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        2888..2914
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        2906..2927
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   CONFLICT        659
FT                   /note="S -> G (in Ref. 1; AAB66593)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1927
FT                   /note="R -> A (in Ref. 1; AAB66593 and 3; AAB27492)"
FT                   /evidence="ECO:0000305"
FT   STRAND          1054..1061
FT                   /evidence="ECO:0007829|PDB:6S4C"
FT   HELIX           1067..1069
FT                   /evidence="ECO:0007829|PDB:6S4C"
FT   HELIX           1070..1082
FT                   /evidence="ECO:0007829|PDB:6S4C"
FT   STRAND          1086..1088
FT                   /evidence="ECO:0007829|PDB:6S4C"
FT   STRAND          1091..1107
FT                   /evidence="ECO:0007829|PDB:6S4C"
FT   HELIX           1115..1123
FT                   /evidence="ECO:0007829|PDB:6S4C"
FT   HELIX           1135..1146
FT                   /evidence="ECO:0007829|PDB:6S4C"
FT   STRAND          1160..1166
FT                   /evidence="ECO:0007829|PDB:6S4C"
FT   HELIX           1175..1183
FT                   /evidence="ECO:0007829|PDB:6S4C"
FT   STRAND          1187..1192
FT                   /evidence="ECO:0007829|PDB:6S4C"
FT   TURN            1198..1202
FT                   /evidence="ECO:0007829|PDB:6S4C"
FT   STRAND          1212..1215
FT                   /evidence="ECO:0007829|PDB:6S4C"
FT   STRAND          1217..1220
FT                   /evidence="ECO:0007829|PDB:6S4C"
FT   HELIX           1221..1237
FT                   /evidence="ECO:0007829|PDB:6S4C"
SQ   SEQUENCE   2944 AA;  295232 MW;  13D01CA7ED36C958 CRC64;
     MRLRLLVAAL CAAEILMGAP EVWAQPRDRV TCTRLYAADI VFLLDGSSSI GRSNFREVRG
     FLEGLVLPFS GAASAQGVRF ATVQYSDDPQ TEFGLDTLGS GSDTIRAIRE LSYKGGNTRT
     GAALHHVSDR VFLPRLTRPG VPKVCILITD GKSQDLVDTA AQKLKGQGVK LFAVGIKNAD
     PEELKRVASQ PTSDFFFFVN DFSILRTLLP LISRRVCTTA GGVPVTLPSD DTPSGPRDLV
     LSEPSSQSLR VQWTAASGPV TGYKVQYTPL TGLGQPLPSE RQEVNIPAGE TSTRLQGLRP
     LTDYQVTVVA LYANSIGEAV SGTARTTAKE GLELSLQNIT SHSLLVAWRR VPGANGYRVT
     WRDLSGGPTQ QQDLSPGQGS VFLDHLEPGT DYEVTVSALF GHSVGPAASL TARTASSVEQ
     TLHPIILSPT SILLSWNLVP EARGYRLEWR RESGLETPQK VELPPDVTRH QLDGLQPGTE
     YRLTLYTLLE GREVATPATV VPTGLEQLVS PVMNLQAIEL PGQRVRVSWN PVPGATEYRF
     TVRTTQGVER TLLLPGSQTT FDLDDVRAGL SYTVRVSARV GAQEGDASIL TIHRDPEAPL
     VVPGLRVVAS DATRIRVAWG LVPGASGFRI SWRTGSGPES SRTLTPDSTV TDILGLQPST
     SYQVAVSALR GREEGPPVVI VARTDPLGPV RRVHLTQAGS SSVSITWTGV PGATGYRVSW
     HSGHGPEKSL LVSGDATVAE IDGLEPDTEY IVRVRTHVAG VDGAPASVVV RTAPEPVGSV
     SKLQILNASS DVLRVTWVGV PGATSYKLAW GRSEGGPMKH RILPGNKESA EIRDLEGGVS
     YSVRVTALVG DREGAPVSIV ITTPPATPAL LETLQVVQSG EHSLRLRWEP VPGAPGFRLH
     WQPEGGQEQS LTLGPESNSY NLVGLEPATK YQVWLTVLGQ TGEGPPRKVT AYTEPSHIPS
     TELRVVDTSI DSVTLTWTPV SGASSYILSW RPLRGTGQEV PRAPQTLPGT SSSHRVTGLE
     PGISYVFSLT PIQSGVRGSE ISVTQTPACS HGPVDVVFLL HATRDNAHNA EAVRRVLERL
     VSALGPLGPQ AAQVGLLTYS HRPSPLFPLN SSHDLGIILR KIRDIPYVDP SGNNLGTAVT
     TAHRYLLASN APGRRQQVPG VMVLLVDEPL RGDILSPIRE AQTSGLKVMA LSLVGADPEQ
     LRRLAPGTDP IQNFFAVDNG PGLDRAVSDL AVALCQAAVT IEPQTGPCAV HCPKGQKGEP
     GVTGLQGQAG PPGPPGLPGR TGAPGPQGPP GSTQAKGERG FPGPEGPPGS PGLPGVPGSP
     GIKGSTGRPG PRGEQGERGP QGPKGEPGEP GQITGGGGPG FPGKKGDPGP SGPPGSRGPV
     GDPGPRGPPG LPGISVKGDK GDRGERGPPG PGIGASEQGD PGLPGLPGSP GPQGPAGRPG
     EKGEKGDCED GGPGLPGQPG PPGEPGLRGA PGMTGPKGDR GLTGTPGEPG VKGERGHPGP
     VGPQGLPGAA GHPGVEGPEG PPGPTGRRGE KGEPGRPGDP AVGPGGAGAK GEKGEAGLPG
     PRGASGSKGE QGAPGLALPG DPGPKGDPGD RGPIGLTGRA GPTGDSGPPG EKGEPGRPGS
     PGPVGPRGRD GEAGEKGDEG IPGEPGLPGK AGERGLRGAP GPRGPVGEKG DQGDPGEDGR
     NGSPGSSGPK GDRGEPGPPG PPGRLVDAGI ESRDKGEPGQ EGPRGPKGDP GPPGVSGERG
     IDGLRGPPGP QGDPGVRGPA GDKGDRGPPG LDGRSGLDGK PGAPGPPGLH GASGKAGDPG
     RDGLPGLRGE HGPPGPPGPP GVPGKAGDDG KPGLNGKNGD PGDPGEDGRK GEKGDSGAPG
     REGPDGPKGE RGAPGNPGLQ GPPGLPGQVG PPGQGFPGVP GITGPKGDRG ETGSKGEQGL
     PGERGLRGEP GSLPNAERLL ETAGIKVSAL REIVDTWDES SGSFLPVPER RPGPKGDPGD
     RGPPGKEGLI GFPGERGLKG ERGDPGPQGP PGLALGERGP PGPPGLAGEP GKPGIPGLPG
     RAGGSGEAGR PGERGERGEK GERGDQGRDG LPGLPGPPGP PGPKVAIEEP GPGLAREQGP
     PGLKGAKGEP GSDGDPGPKG DRGVPGIKGD VGEPGKRGHD GNPGLPGERG VAGPEGKPGL
     QGPRGTPGPV GSHGDPGPPG APGLAGPAGP QGPSGLKGEP GETGPPGRGL PGPVGAVGLP
     GPPGPSGLVG PQGSPGLPGQ VGETGKPGPP GRDGSSGKDG DRGSPGVPGS PGLPGPVGPK
     GEPGPVGAPG QVVVGPPGAK GEKGAPGDLA GALLGEPGAK GDRGLPGPRG EKGEAGRAGG
     PGDPGEDGQK GAPGLKGLKG EPGIGVQGPP GPSGPPGMKG DLGPPGAPGA PGVVGFPGQT
     GPRGETGQPG PVGERGLAGP PGREGAPGPL GPPGPPGSAG APGASGLKGD KGDPGAGLPG
     PRGERGEPGV RGEDGHPGQE GPRGLVGPPG SRGEQGEKGA AGAAGLKGDK GDSAVIEGPP
     GPRGAKGDMG ERGPRGIDGD KGPRGESGNP GDKGSKGEPG DKGSAGSIGV RGLTGPKGEP
     GAAGIPGEPG APGKDGIPGF RGDKGDIGFM GPRGLKGEKG IKGTCGRDGE RGDKGEAGFP
     GRPGLAGKKG DMGEPGLPGQ SGAPGKEGLI GPKGDRGFDG QSGPKGDQGE KGERGPPGVG
     GFPGPRGNDG SSGPPGPPGG VGPKGPEGLQ GQKGERGPPG ESVVGAPGAP GTPGERGEQG
     RPGPAGPRGE KGEAALTEDD IRDFVRQEMS QHCACQGQFI ASGSRPLPGY AADTAGSQLH
     HVPVLRVSHV EEEGQVPPED DDDFSEYSVY SVEDYQEPEV PWDGEAEIKG WDQRGSDLCS
     LPLDEGSCTA YTLRWYHRAV PGGTACHPFV YGGCGGNANR FGTREACERR CPPQGVHSQK
     TGAA
//