ID CO1A1_CYNPY Reviewed; 1450 AA. AC Q9YIB4; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 83. DE RecName: Full=Collagen alpha-1(I) chain; DE AltName: Full=Alpha-1 type I collagen; DE Flags: Precursor; GN Name=COL1A1; OS Cynops pyrrhogaster (Japanese fire-bellied newt) (Molge pyrrhogaster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae; Cynops. OX NCBI_TaxID=8330; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Regenerating forelimb blastema; RX PubMed=10474166; RX DOI=10.1002/(sici)1097-0177(199909)216:1<59::aid-dvdy8>3.0.co;2-b; RA Asahina K., Obara M., Yoshizato K.; RT "Expression of genes of type I and type II collagen in the formation and RT development of the blastema of regenerating newt limb."; RL Dev. Dyn. 216:59-71(1999). CC -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar CC forming collagen). {ECO:0000250}. CC -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have CC crucial roles in tissue growth and repair by controlling both the CC intracellular assembly of procollagen molecules and the extracellular CC assembly of collagen fibrils. It binds a calcium ion which is essential CC for its function (By similarity). {ECO:0000250}. CC -!- PTM: Contains mostly 4-hydroxyproline. Proline residues at the third CC position of the tripeptide repeating unit (G-X-Y) are hydroxylated in CC some or all of the chains. {ECO:0000250|UniProtKB:P11087}. CC -!- PTM: Contains 3-hydroxyproline at a few sites. This modification occurs CC on the first proline residue in the sequence motif Gly-Pro-Hyp, where CC Hyp is 4-hydroxyproline. {ECO:0000250|UniProtKB:P11087}. CC -!- PTM: Lysine residues at the third position of the tripeptide repeating CC unit (G-X-Y) are 5-hydroxylated in some or all of the chains. CC {ECO:0000250|UniProtKB:P02457}. CC -!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked CC glycan consists of a Glc-Gal disaccharide. CC {ECO:0000250|UniProtKB:P11087}. CC -!- SIMILARITY: Belongs to the fibrillar collagen family. CC {ECO:0000255|PROSITE-ProRule:PRU00793}. 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; AB015438; BAA36973.1; -; mRNA. DR AlphaFoldDB; Q9YIB4; -. DR SMR; Q9YIB4; -. DR GlyCosmos; Q9YIB4; 3 sites, No reported glycans. DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.1000; -; 1. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR000885; Fib_collagen_C. DR InterPro; IPR001007; VWF_dom. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF1108; ENDOSTATIN DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF01410; COLFI; 1. DR Pfam; PF01391; Collagen; 7. DR Pfam; PF00093; VWC; 1. DR SMART; SM00038; COLFI; 1. DR SMART; SM00214; VWC; 1. DR SUPFAM; SSF57603; FnI-like domain; 1. DR PROSITE; PS51461; NC1_FIB; 1. DR PROSITE; PS01208; VWFC_1; 1. DR PROSITE; PS50184; VWFC_2; 1. PE 2: Evidence at transcript level; KW Calcium; Collagen; Disulfide bond; Extracellular matrix; Glycoprotein; KW Hydroxylation; Metal-binding; Pyrrolidone carboxylic acid; Repeat; KW Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT PROPEP 23..148 FT /note="N-terminal propeptide" FT /evidence="ECO:0000250|UniProtKB:P02452" FT /id="PRO_0000286160" FT CHAIN 149..1204 FT /note="Collagen alpha-1(I) chain" FT /evidence="ECO:0000250|UniProtKB:P02452" FT /id="PRO_0000286161" FT PROPEP 1205..1450 FT /note="C-terminal propeptide" FT /evidence="ECO:0000250|UniProtKB:P02452" FT /id="PRO_0000286162" FT DOMAIN 31..90 FT /note="VWFC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT DOMAIN 1215..1450 FT /note="Fibrillar collagen NC1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT REGION 97..1201 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 124..143 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 168..183 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 978..995 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1162..1181 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1263 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1265 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1266 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1268 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1271 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT MOD_RES 149 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000250|UniProtKB:P02452" FT MOD_RES 157 FT /note="Allysine" FT /evidence="ECO:0000250|UniProtKB:P02452" FT MOD_RES 176 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 182 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 194 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 197 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 212 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 227 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 242 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 248 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 251 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 275 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 278 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 284 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 293 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 299 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 314 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 320 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 329 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 332 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 359 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 362 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 374 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 380 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 389 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 395 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 398 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 413 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 416 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 422 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 437 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 446 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 461 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 467 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 476 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 482 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 491 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 494 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 515 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 521 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 530 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 533 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 551 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 569 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 578 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 590 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 608 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 626 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 632 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 644 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 650 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 656 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 668 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 689 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 704 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 710 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 716 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 725 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 737 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 743 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 758 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 764 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 785 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 791 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 794 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 803 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 809 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 827 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 836 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 845 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 848 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 857 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 863 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 871 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 872 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 881 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 884 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 908 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 914 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 923 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 932 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 950 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 962 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 968 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 983 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 989 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 995 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1004 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1010 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1019 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1031 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1034 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1037 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1082 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1094 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1106 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1109 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1130 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1145 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1150 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1151 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1165 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1166 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1168 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1169 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1171 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1172 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1175 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1178 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1194 FT /note="Allysine" FT /evidence="ECO:0000250|UniProtKB:P02452" FT CARBOHYD 251 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P02457" FT CARBOHYD 1094 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P02457" FT CARBOHYD 1351 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 1245..1277 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1251 FT /note="Interchain (with C-1268)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1268 FT /note="Interchain (with C-1251)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1285..1448 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1356..1401 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" SQ SEQUENCE 1450 AA; 137563 MW; ABF8A74841B87B7C CRC64; MFSFVDNRLL VLLAACVLLV RALDQEDIES GLCHQEGTTY SDKDVWKPEP CVICVCDNGN IMCDDVTCGD YPVDCPNAEI PFGECCPVCP DGDGTSYSEQ TGVEGPKGEV GPKGDRGLPG PPGRDGNPGL PGPPGPPGPP GLGGNFAPQM SYGYDEKSAG ISVPGPMGPM GPRGPPGPSG SPGPQGFQGP SGEPGEPGAA GALGPRGLPG PPGKNGDDGE SGKPGRPGER GPSGPQGARG LPGTAGLPGM KGHRGFNGLD GAKGDNGPAG PKGEPGNPGE NGAPGQAGPR GLPGERGRPG APGPAGARGN DGSPGAAGPP GPTGPTGPPG FPGAVGAKGD AGPQGSRGSE GPQGARGEPG APGPAGAAGP SGNPGTDGQP GGKGATGSPG IAGAPGFPGA RGAPGPQGPA GAPGPKGNNG EPGAQGNKGE PGAKGEPGPA GVQGPPGPSG EEGKRGSRGE PGPAGPPGPA GERGGPGSRG FPGSDGASGP KGAPGERGSV GPAGPKGSTG ESGRPGEPGL PGAKGLTGSP GSPGPDGKTG PAGAAGQDGH PGPPGPSGAR GQSGVMGFPG PKGAAGEPGK SGERGVAGPP GATGAPGKDG EAGAQGPPGP SGPSGERGEQ GPAGSPGFQG LPGSPGPAGE AGKPGEQGAP GDAGGPGPSG PRGERGFPGE RGGQGPAGAQ GPRGSPGSPG NDGAKGEAGA AGAPGGRGPP GLQGMPGERG SAGMPGAKGD RGDAGTKGAD GAPGKDGARG LTGPIGPPGP SGAPGDKGEG GPSGPAGPTG ARGSPGERGE PGAPGPAGIC GPPGADGQPG AKGESGDAGP KGDAGAPGPA GPTGAPGPAG NVGAPGPKGT RGAAGPPGAT GFPGAAGRLG PPGPSGNAGP PGPPGPGGKE GAKGSRGETG PAGRSGEPGP AGPPGPSGEK GSPGSDGPAG APGIPGPQGI AGQRGVVGLP GQRGERGFSG LPGPAGEPGK QGPSGPNGER GPPGPSGPPG LGGPPGEPGR EGSPGSEGAP GRDGSPGPKG DRGENGPSGP PGAPGAPGAP GPVGPAGKNG DRGETGPAGP AGPAGPSGVR GAPGPAGARG DKGEAGEQGE RGMKGHRGFN GMQGPPGPPG SSGEQGAPGP SGPAGPRGPP GSSGSTGKDG VNGLPGPIGP PGPRGRNGDV GPAGPPGPPG PPGPPGPPSG GFDFSFMPQP PEPKSHGDGR YFRADDANVV RDRDLEVDTT LKSLSAQIEN IRSPEGTRKN PARTCRDLKM CHSDWKSGDY WIDPNQGCNL DAIKVHCNME TGETCVYPSQ ASISQKNWYT SKNPREKKHV WFGETMSDGF QFEYGGEGSD PADVNIQLTF LRLMATEASQ NITYHCKNSV AYMDQETGNL KKAVLLQGSN EIEIRAEGNS RFTYGVTEDG CTQHTGEWGK TVIEYKTTKT SRLPIIDIAP MDVGTPDQEF GIDIGPVCFL //