CO7A1_MOUSE
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 03-AUG-2022, entry version 160.
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}.
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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 GlyGen; Q63870; 3 sites.
DR iPTMnet; Q63870; -.
DR PhosphoSitePlus; Q63870; -.
DR jPOST; Q63870; -.
DR MaxQB; Q63870; -.
DR PaxDb; Q63870; -.
DR PeptideAtlas; Q63870; -.
DR PRIDE; Q63870; -.
DR ProteomicsDB; 283671; -.
DR DNASU; 12836; -.
DR Ensembl; ENSMUST00000026740; ENSMUSP00000026740; ENSMUSG00000025650.
DR Ensembl; ENSMUST00000112070; ENSMUSP00000107701; ENSMUSG00000025650.
DR GeneID; 12836; -.
DR KEGG; mmu:12836; -.
DR UCSC; uc009rrh.1; mouse.
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; PYMDPSG; -.
DR OrthoDB; 67372at2759; -.
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-2022090; Assembly of collagen fibrils and other multimeric structures.
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-3000157; Laminin interactions.
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 74 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 181 other tissues.
DR Genevisible; Q63870; MM.
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: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 CDD; cd00063; FN3; 9.
DR CDD; cd00109; KU; 1.
DR Gene3D; 2.60.40.10; -; 9.
DR Gene3D; 3.40.50.410; -; 2.
DR Gene3D; 4.10.410.10; -; 1.
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 Pfam; PF01391; Collagen; 20.
DR Pfam; PF00041; fn3; 7.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF00092; VWA; 2.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00060; FN3; 9.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF49265; SSF49265; 5.
DR SUPFAM; SSF53300; SSF53300; 2.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS50853; FN3; 9.
DR PROSITE; PS50234; VWFA; 2.
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
