COBA1_RAT
ID COBA1_RAT Reviewed; 1804 AA.
AC P20909; F1LSI4; Q62750; Q63391; Q63392; Q63393; Q8VBY8; Q920Z7; Q920Z8;
AC Q920Z9; Q921A0; Q921A1;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Collagen alpha-1(XI) chain;
DE Flags: Precursor;
GN Name=Col11a1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-556 (ISOFORM 2), PARTIAL NUCLEOTIDE
RP SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5
RP AND 6).
RC STRAIN=Sprague-Dawley; TISSUE=Chondrosarcoma;
RX PubMed=7721875; DOI=10.1074/jbc.270.16.9478;
RA Oxford J.T., Doege K.J., Morris N.P.;
RT "Alternative exon splicing within the amino-terminal nontriple-helical
RT domain of the rat pro-alpha 1(XI) collagen chain generates multiple forms
RT of the mRNA transcript which exhibit tissue-dependent variation.";
RL J. Biol. Chem. 270:9478-9485(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1323-1804.
RX PubMed=3182841; DOI=10.1016/s0021-9258(18)37512-4;
RA Bernard M., Yoshioka H., Rodriguez E., van der Rest M., Kimura T.,
RA Ninomiya Y., Olsen B.R., Ramirez F.;
RT "Cloning and sequencing of pro-alpha 1 (XI) collagen cDNA demonstrates that
RT type XI belongs to the fibrillar class of collagens and reveals that the
RT expression of the gene is not restricted to cartilagenous tissue.";
RL J. Biol. Chem. 263:17159-17166(1988).
RN [4]
RP DISULFIDE BONDS, AND GLYCOSYLATION.
RX PubMed=10753969; DOI=10.1074/jbc.275.15.11498;
RA Gregory K.E., Oxford J.T., Chen Y., Gambee J.E., Gygi S.P., Aebersold R.,
RA Neame P.J., Mechling D.E., Bachinger H.P., Morris N.P.;
RT "Structural organization of distinct domains within the non-collagenous N-
RT terminal region of collagen type XI.";
RL J. Biol. Chem. 275:11498-11506(2000).
CC -!- FUNCTION: May play an important role in fibrillogenesis by controlling
CC lateral growth of collagen II fibrils.
CC -!- SUBUNIT: Trimers composed of three different chains: alpha 1(XI), alpha
CC 2(XI), and alpha 3(XI). Alpha 3(XI) is probably a post-translational
CC modification of alpha 1(II).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=+V1a+V2, p6A+8;
CC IsoId=P20909-1; Sequence=Displayed;
CC Name=2; Synonyms=+V1b+V2, p6B+8;
CC IsoId=P20909-2; Sequence=VSP_042438;
CC Name=3; Synonyms=+V2, p8;
CC IsoId=P20909-3; Sequence=VSP_042439;
CC Name=4; Synonyms=+V1a, p6A;
CC IsoId=P20909-4; Sequence=VSP_042440;
CC Name=5; Synonyms=+V1b, p6B;
CC IsoId=P20909-5; Sequence=VSP_042438, VSP_042440;
CC Name=6; Synonyms=-V1-V2, p0;
CC IsoId=P20909-6; Sequence=VSP_042439, VSP_042440;
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: 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: N-glycosylated. {ECO:0000269|PubMed:10753969}.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; AABR03012126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03013126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03014171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03015382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03015832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03016562; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03017847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03017951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03018245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03019675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03023874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U20116; AAK83682.1; -; Genomic_DNA.
DR EMBL; U20118; AAK83568.2; -; Genomic_DNA.
DR EMBL; U20118; AAK83569.2; -; Genomic_DNA.
DR EMBL; U20118; AAK83570.2; -; Genomic_DNA.
DR EMBL; U20118; AAK83571.2; -; Genomic_DNA.
DR EMBL; U20118; AAA92358.3; -; Genomic_DNA.
DR EMBL; U20118; AAA92359.3; -; Genomic_DNA.
DR EMBL; U20121; AAA92360.1; -; mRNA.
DR PIR; B31795; B31795.
DR RefSeq; NP_037249.1; NM_013117.1. [P20909-1]
DR RefSeq; XP_006233272.1; XM_006233210.3. [P20909-2]
DR AlphaFoldDB; P20909; -.
DR BioGRID; 247683; 1.
DR IntAct; P20909; 33.
DR STRING; 10116.ENSRNOP00000023794; -.
DR CarbonylDB; P20909; -.
DR GlyGen; P20909; 3 sites.
DR iPTMnet; P20909; -.
DR PhosphoSitePlus; P20909; -.
DR jPOST; P20909; -.
DR PaxDb; P20909; -.
DR PRIDE; P20909; -.
DR ABCD; P20909; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000068413; ENSRNOP00000061595; ENSRNOG00000023148. [P20909-1]
DR GeneID; 25654; -.
DR KEGG; rno:25654; -.
DR UCSC; RGD:2372; rat. [P20909-1]
DR CTD; 1301; -.
DR RGD; 2372; Col11a1.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000154535; -.
DR HOGENOM; CLU_001074_2_1_1; -.
DR InParanoid; P20909; -.
DR OMA; CDTPHKD; -.
DR OrthoDB; 199083at2759; -.
DR TreeFam; TF323987; -.
DR Reactome; R-RNO-1442490; Collagen degradation.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-RNO-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-RNO-8874081; MET activates PTK2 signaling.
DR Reactome; R-RNO-8948216; Collagen chain trimerization.
DR PRO; PR:P20909; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000023148; Expressed in ovary and 12 other tissues.
DR Genevisible; P20909; RN.
DR GO; GO:0005581; C:collagen trimer; ISO:RGD.
DR GO; GO:0005592; C:collagen type XI trimer; ISO:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:1904399; F:heparan sulfate binding; IDA:RGD.
DR GO; GO:0008201; F:heparin binding; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001502; P:cartilage condensation; ISO:RGD.
DR GO; GO:0051216; P:cartilage development; ISO:RGD.
DR GO; GO:0002063; P:chondrocyte development; ISO:RGD.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISO:RGD.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0035987; P:endodermal cell differentiation; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0003007; P:heart morphogenesis; ISO:RGD.
DR GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
DR GO; GO:0001503; P:ossification; IEP:RGD.
DR GO; GO:0006029; P:proteoglycan metabolic process; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0048705; P:skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0035989; P:tendon development; ISO:RGD.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:RGD.
DR GO; GO:0007601; P:visual perception; ISO:RGD.
DR CDD; cd00110; LamG; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 7.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Collagen; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT PROPEP 35..511
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000415946"
FT CHAIN 512..1561
FT /note="Collagen alpha-1(XI) chain"
FT /id="PRO_0000005780"
FT PROPEP 1562..1804
FT /note="C-terminal propeptide"
FT /id="PRO_0000005781"
FT DOMAIN 70..242
FT /note="Laminin G-like"
FT DOMAIN 440..488
FT /note="Collagen-like 1"
FT DOMAIN 530..584
FT /note="Collagen-like 2"
FT DOMAIN 581..639
FT /note="Collagen-like 3"
FT DOMAIN 607..664
FT /note="Collagen-like 4"
FT DOMAIN 641..698
FT /note="Collagen-like 5"
FT DOMAIN 746..804
FT /note="Collagen-like 6"
FT DOMAIN 1391..1449
FT /note="Collagen-like 7"
FT DOMAIN 1442..1492
FT /note="Collagen-like 8"
FT DOMAIN 1481..1539
FT /note="Collagen-like 9"
FT DOMAIN 1575..1803
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 229..417
FT /note="Nonhelical region"
FT REGION 418..506
FT /note="Triple-helical region (interrupted)"
FT REGION 437..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..509
FT /note="Short nonhelical segment"
FT REGION 510..527
FT /note="Telopeptide"
FT REGION 525..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..1540
FT /note="Triple-helical region"
FT REGION 1541..1561
FT /note="Nonhelical region (C-terminal)"
FT COMPBIAS 465..482
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..712
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..940
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1229
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1322
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1361
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1507
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1543
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1623
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1625
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1626
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1628
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1631
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 610
FT /note="Allysine"
FT /evidence="ECO:0000250"
FT MOD_RES 1450
FT /note="Allysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793,
FT ECO:0000269|PubMed:10753969"
FT DISULFID 181..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793,
FT ECO:0000269|PubMed:10753969"
FT DISULFID 1605..1637
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1628
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1646..1801
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1712..1755
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT VAR_SEQ 259..297
FT /note="YAPEDIIEYDYEYGETDYKEAESVTEMPTVTEETVAQTE -> KKKSNYTKK
FT KRTLATNSKKKSKMSTTPKSEKFASKKKKRNQATAKAKLGVQ (in isoform 2
FT and isoform 5)"
FT /evidence="ECO:0000303|PubMed:7721875"
FT /id="VSP_042438"
FT VAR_SEQ 259..297
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_042439"
FT VAR_SEQ 329..413
FT /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_042440"
FT CONFLICT 394
FT /note="S -> A (in Ref. 2; AAA92358/AAA92359/AAA92360/
FT AAK83570)"
FT /evidence="ECO:0000305"
FT CONFLICT 1371
FT /note="R -> G (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1702
FT /note="A -> S (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1743
FT /note="E -> D (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1804 AA; 181027 MW; 666A4E0FDCC0BA3B CRC64;
MEPWSRWKTK RWIWDLTIST LVLTFLFQAR EVRGAAPVDI LKALDFHNSP VGISKTTGFC
TSRKNSKDPD IAYRVTEEAQ ISAPTKQLFP GGIFPQDFSI LFTIKPKKGT QAFLLSLYNE
HGIQQLGVEV GRSPVFLFED HTGKPTPENY PLFSTVNIAD GKWHRVAISV EKKTVTMIVD
CKKKITKPLD RSERSIVDTN GIMVFGTRIL ETDVFQGDIQ QFLITGDPKA AYDYCDHYSP
DCDLTSKAAQ AQEPHIDEYA PEDIIEYDYE YGETDYKEAE SVTEMPTVTE ETVAQTEANI
VDDFQDYNYG TMETYQTESP RRVSGSNEPN PVEEGFTEEY LTGEDYDVQR NISEDILYGN
KGIDGRDSDL LVDGDLGEYD FYEYKEYEER TTTSPNEEFG PGVPAETDFT ETSINGHGAY
GEKGQKGEPA VVEPGMLVEG PPGPAGPAGL MGPPGLQGPS GLPGDPGDRG PPGRPGLPGA
DGLPGPPGTM LMLPFRYGGD GSKGPTISAQ EAQAQAILQQ ARIALRGPPG PMGLTGRPGP
VGGPGSAGAK GESGDPGPQG PRGVQGPPGP TGKPGKRGRP GADGGRGMPG EPGSKGDRGF
DGLPGLPGDK GHRGERGPQG PPGLPGDDGM RGEDGEIGPR GLPGEAGPRG LLGPRGTPGP
PGQPGIGGID GPQGPKGNMG PQGEPGPPGQ QGNPGPQGLP GPQGPIGPPG EKGPQGKPGL
AGLPGADGPP GHPGKEGQSG EKGALGPPGP QGPIGYPGPR GVKGADGVRG LKGSKGEKGE
DGFPGFKGDM GLKGDRGEVG QVGPRGEDGP EGPKGRAGPT GDPGPSGQAG EKGKLGVPGL
PGYPGRQGPK GSTGFPGFPG ANGEKGARGI AGKPGPRGQR GPTGPRGSRG ARGPTGKPGP
KGTSGGDGPP GPPGERGPQG PQGPVGFPGP KGPPGPAGKD GLPGHPGQRG ETGFQGKTGP
PGPGGVVGPQ GPTGETGPIG ERGHPGTPGP PGEQGLPGAA GKEGAKGDPG PQGISGKDGP
AGIRGFPGER GLPGAQGAPG LKGGEGPQGP QGPIGSPGER GSAGTAGPIG LPGRPGPQGP
PGPAGEKGAP GEKGPQGPAG RDGVQGPVGL PGPAGPAGSP GEDGDKGEIG EPGQKGSKGD
KGENGPPGPP GLQGPVGAPG IAGGDGEAGP RGQQGMFGQK GDEGARGFPG PPGPIGLQGL
PGPPGEKGEN GDVGPMGPPG PPGPRGPQGP NGADGPQGPP GSIGSVGGVG EKGEPGEAGN
PGPPGEAGSG GPKGERGEKG EAGPPGAAGP PGIKGPPGDD GPKGNPGPVG FPGDPGPPGE
PGPAGQDGVG GDKGEDGDPG QPGPPGPSGE AGPPGPPGKR GPPGASGSEG RQGEKGAKGE
AGAEGPPGKT GPVGPQGPSG KPGPEGLRGI PGPVGEQGLP GAAGQDGPPG PLGPPGLPGL
KGDPGSKGEK GHPGLIGLIG PPGEQGEKGD RGLPGTQGSP GAKGDGGIPG PAGPIGPPGP
PGLPGPAGPK GNKGSSGPTG QKGDSGMPGP PGPPGPPGEV IQPLPILSPK KTRRHTESIQ
ADAGDNILDY SDGMEEIFGS LNSLKQDIEH MKFPMGTQTN PARTCKDLQL SHPDFPDGEY
WIDPNQGCSG DSFKVYCNFT AGGETCIYPD KKSEGVRLSS WPKEKPGSWY SEFKRGKLLS
YLDVEGNSIN MVQMTFLKLL TASARQNFTY NCHQSTAWYD VLSGSYDKAL RFLGSNDEEM
SYENNPHIKA LYDGCASRKG YEKTVIEINT PKIDQVPIID VMINDFGDQN QKFGFEVGPA
CFLG
