CO1A2_CHICK
ID CO1A2_CHICK Reviewed; 1363 AA.
AC P02467; F1P0H9; P87491; P87492; Q90758; Q90792; Q90795; Q90797; Q92014;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Collagen alpha-2(I) chain;
DE AltName: Full=Alpha-2 type I collagen;
DE Flags: Precursor;
GN Name=COL1A2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-245; 263-449 AND 467-1363.
RX PubMed=3868961; DOI=10.1111/j.1749-6632.1985.tb51159.x;
RA Boedtker H., Finer M., Aho S.;
RT "The structure of the chicken alpha 2 collagen gene.";
RL Ann. N. Y. Acad. Sci. 460:85-116(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89.
RX PubMed=6135195; DOI=10.1093/nar/11.1.91;
RA Tate V.E., Finer M.H., Boedtker H., Doty P.;
RT "Chick pro alpha 2 (I) collagen gene: exon location and coding potential
RT for the prepropeptide.";
RL Nucleic Acids Res. 11:91-104(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RX PubMed=6946474; DOI=10.1073/pnas.78.9.5334;
RA Vogeli G., Ohkubo H., Sobel M.E., Yamada Y., Pastan I., de Crombrugghe B.;
RT "Structure of the promoter for chicken alpha 2 type I collagen gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:5334-5338(1981).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RX PubMed=6473103; DOI=10.1093/nar/12.15.6117;
RA Aho S., Tate V.E., Boedtker H.;
RT "Location of the 11 bp exon in the chicken pro alpha 2(I) collagen gene.";
RL Nucleic Acids Res. 12:6117-6125(1984).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-79.
RX PubMed=3678834; DOI=10.1016/0378-1119(87)90159-4;
RA Finer M.H., Boedtker H., Doty P.;
RT "Construction and characterization of cDNA clones encoding the 5' end of
RT the chicken pro alpha 1(I) collagen mRNA.";
RL Gene 56:71-78(1987).
RN [7]
RP PROTEIN SEQUENCE OF 74-92; 264-449 AND 1089-1171.
RX PubMed=5443712; DOI=10.1016/0006-291x(70)90638-8;
RA Vuust J., Lane J.M., Fietzek P.P., Miller E.J., Piez K.A.;
RT "The order of the CNBr peptides from the alpha 2 chain of collagen.";
RL Biochem. Biophys. Res. Commun. 38:703-708(1970).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-91; 264-449 AND 1089-1170.
RX PubMed=6272119; DOI=10.1038/294129a0;
RA Wozney J., Hanahan D., Tate V.E., Boedtker H., Doty P.;
RT "Structure of the pro alpha 2 (I) collagen gene.";
RL Nature 294:129-135(1981).
RN [9]
RP PROTEIN SEQUENCE OF 78-92, ALLYSINE AT LYS-83, AND PYROGLUTAMATE FORMATION
RP AT GLN-78.
RC TISSUE=Skin;
RX PubMed=4313735; DOI=10.1021/bi00806a012;
RA Kang A.H., Gross J.;
RT "Amino acid sequence of cyanogen bromide peptides from the amino-terminal
RT region of chick skicollagen.";
RL Biochemistry 9:796-804(1970).
RN [10]
RP PROTEIN SEQUENCE OF 78-92 AND 416-449, AND PYROGLUTAMATE FORMATION AT
RP GLN-78.
RC TISSUE=Skin;
RX PubMed=5809220; DOI=10.1021/bi00836a011;
RA Kang A.H., Igarashi S., Gross J.;
RT "Characterization of the cyanogen bromide peptides from the alpha-2 chain
RT of chick skin collagen.";
RL Biochemistry 8:3200-3204(1969).
RN [11]
RP PROTEIN SEQUENCE OF 78-92 AND 416-449, AND PYROGLUTAMATE FORMATION AT
RP GLN-78.
RC TISSUE=Bone;
RX PubMed=5785233; DOI=10.1021/bi00833a053;
RA Lane J.M., Miller E.J.;
RT "Isolation and characterization of the peptides derived from the alpha 2
RT chain of chick bone collagen after cyanogen bromide cleavage.";
RL Biochemistry 8:2134-2139(1969).
RN [12]
RP PROTEIN SEQUENCE OF 78-95 AND 416-446.
RX PubMed=5443711; DOI=10.1016/0006-291x(70)90637-6;
RA Igarashi S., Kang A.H., Gross J.;
RT "Renaturation and ordering by electron microscopy of the cyanogen bromide
RT peptides from the alpha 2 chain of chick skin collagen.";
RL Biochem. Biophys. Res. Commun. 38:697-702(1970).
RN [13]
RP PROTEIN SEQUENCE OF 417-445, AND HYDROXYLATION AT PRO-440 AND PRO-443.
RC TISSUE=Skin;
RX PubMed=5544653; DOI=10.1021/bi00780a010;
RA Highberger J.H., Kang A.H., Gross J.;
RT "Comparative studies on the amino acid sequence of the alpha 2-CB2 peptides
RT from chick and rat skin collagens.";
RL Biochemistry 10:610-616(1971).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 567-588.
RX PubMed=364479; DOI=10.1073/pnas.75.11.5417;
RA Lehrach H., Frischauf A.-M., Hanahan D., Wozney J., Fuller F.,
RA Crkvenjakov R., Boedtker H., Doty P.;
RT "Construction and characterization of a 2.5-kilobase procollagen clone.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:5417-5421(1978).
RN [15]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 903-1363.
RX PubMed=6927845; DOI=10.1021/bi00507a054;
RA Fuller F., Boedtker H.;
RT "Sequence determination and analysis of the 3' region of chicken pro-alpha
RT 1(I) and pro-alpha 2(I) collagen messenger ribonucleic acids including the
RT carboxy-terminal propeptide sequences.";
RL Biochemistry 20:996-1006(1981).
RN [16]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 999-1170 AND 1235-1363.
RX PubMed=6267043; DOI=10.1016/s0021-9258(19)68858-7;
RA Dickson L.A., Ninomiya Y., Bernard M.P., Pesciotta D.M., Parsons J.,
RA Green G., Eikenberry E.F., de Crombrugghe B., Vogeli G., Pastan I.,
RA Fietzek P.P., Olsen B.R.;
RT "The exon/intron structure of the 3'-region of the pro alpha 2(I) collagen
RT gene.";
RL J. Biol. Chem. 256:8407-8415(1981).
RN [17]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 933-955 AND 969-981.
RX PubMed=6159982; DOI=10.1016/0092-8674(80)90432-8;
RA Avvedimento V.E., Vogeli G., Yamada Y., Maizel J.V. Jr., Pastan I.,
RA de Crombrugghe B.;
RT "Correlation between splicing sites within an intron and their sequence
RT complementarity with U1 RNA.";
RL Cell 21:689-696(1980).
RN [18]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 126-161; 468-518 AND 927-955.
RX PubMed=7460017; DOI=10.1016/0092-8674(80)90565-6;
RA Yamada Y., Avvedimento V.E., Mudryj M., Ohkubo H., Vogeli G., Irani M.,
RA Pastan I., de Crombrugghe B.;
RT "The collagen gene: evidence for its evolutionary assembly by amplification
RT of a DNA segment containing an exon of 54 bp.";
RL Cell 22:887-892(1980).
CC -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar
CC forming collagen).
CC -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones.
CC In bones the fibrils are mineralized with calcium hydroxyapatite.
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. {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 {ECO:0000269|PubMed:5544653}.
CC -!- PTM: The N-terminus of the mature protein is blocked.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; AADN04000096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M25963; AAA69960.1; -; Genomic_DNA.
DR EMBL; M25956; AAA69960.1; JOINED; Genomic_DNA.
DR EMBL; M25959; AAA69960.1; JOINED; Genomic_DNA.
DR EMBL; M25961; AAA69960.1; JOINED; Genomic_DNA.
DR EMBL; M25962; AAA69960.1; JOINED; Genomic_DNA.
DR EMBL; M25965; AAA69961.1; -; Genomic_DNA.
DR EMBL; M25964; AAA69961.1; JOINED; Genomic_DNA.
DR EMBL; M25984; AAA69962.1; -; Genomic_DNA.
DR EMBL; M25957; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25966; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25967; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25969; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25970; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25971; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25972; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25973; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25974; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25976; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25977; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25978; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25979; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25980; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25981; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25982; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; M25983; AAA69962.1; JOINED; Genomic_DNA.
DR EMBL; J00826; AAA51611.1; -; Genomic_DNA.
DR EMBL; J00821; AAA51611.1; JOINED; Genomic_DNA.
DR EMBL; K00792; AAA51611.1; JOINED; Genomic_DNA.
DR EMBL; J00830; AAA51613.1; -; Genomic_DNA.
DR EMBL; J00829; AAA51613.1; JOINED; Genomic_DNA.
DR EMBL; J00837; AAA51614.1; -; Genomic_DNA.
DR EMBL; J00812; AAA51615.1; -; Genomic_DNA.
DR EMBL; J00811; AAA51615.1; JOINED; Genomic_DNA.
DR EMBL; J00814; AAA51615.1; JOINED; Genomic_DNA.
DR EMBL; J00815; AAA51615.1; JOINED; Genomic_DNA.
DR EMBL; X02657; CAA26493.1; -; mRNA.
DR EMBL; K00794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; V00390; CAA23688.1; -; mRNA.
DR EMBL; M17608; AAA48673.1; -; mRNA.
DR EMBL; M10581; AAA48637.1; -; Genomic_DNA.
DR EMBL; M10540; AAA48638.1; -; Genomic_DNA.
DR EMBL; J00828; AAA51612.1; -; Genomic_DNA.
DR EMBL; J00827; AAA51612.1; JOINED; Genomic_DNA.
DR EMBL; J00832; AAD22117.1; -; Genomic_DNA.
DR EMBL; J00831; AAD22117.1; JOINED; Genomic_DNA.
DR EMBL; J00833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J00822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; I50173; I50173.
DR PIR; I50206; CGCH2S.
DR PIR; S10847; S10847.
DR AlphaFoldDB; P02467; -.
DR SMR; P02467; -.
DR ComplexPortal; CPX-3102; Collagen type I trimer.
DR STRING; 9031.ENSGALP00000015687; -.
DR PaxDb; P02467; -.
DR PRIDE; P02467; -.
DR VEuPathDB; HostDB:geneid_396243; -.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; P02467; -.
DR OrthoDB; 1406711at2759; -.
DR PhylomeDB; P02467; -.
DR TreeFam; TF344135; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005584; C:collagen type I trimer; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005583; C:fibrillar collagen trimer; IDA:AgBase.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 5.
DR SMART; SM00038; COLFI; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 1: Evidence at protein level;
KW Calcium; Collagen; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:P02466"
FT PROPEP 23..77
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT /id="PRO_0000005815"
FT CHAIN 78..1117
FT /note="Collagen alpha-2(I) chain"
FT /id="PRO_0000005816"
FT PROPEP 1118..1363
FT /note="C-terminal propeptide"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT /id="PRO_0000005817"
FT DOMAIN 1128..1363
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 28..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..70
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..116
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..140
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..813
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1061
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1103
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT MOD_RES 78
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:4313735,
FT ECO:0000305|PubMed:5785233, ECO:0000305|PubMed:5809220"
FT MOD_RES 83
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:4313735"
FT MOD_RES 176
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT MOD_RES 440
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:5544653"
FT MOD_RES 443
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:5544653"
FT CARBOHYD 176
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT CARBOHYD 1264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1158..1190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1198..1361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1269..1314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT CONFLICT 428..430
FT /note="VGA -> AGV (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 974
FT /note="P -> L (in Ref. 17; AAA48638)"
FT /evidence="ECO:0000305"
FT CONFLICT 1010
FT /note="P -> H (in Ref. 16; AAA51615)"
FT /evidence="ECO:0000305"
FT CONFLICT 1055
FT /note="P -> H (in Ref. 16; AAA51615)"
FT /evidence="ECO:0000305"
FT CONFLICT 1061
FT /note="P -> H (in Ref. 16; AAA51615)"
FT /evidence="ECO:0000305"
FT CONFLICT 1262
FT /note="S -> P (in Ref. 16; AAA51615)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1363 AA; 128995 MW; 41FFEE5077B428B4 CRC64;
MLSFVDTRIL LLLAVTSYLA TSQHLFQASA GRKGPRGDKG PQGERGPPGP PGRDGEDGPP
GPPGPPGPPG LGGNFAAQYD PSKAADFGPG PMGLMGPRGP PGASGPPGPP GFQGVPGEPG
EPGQTGPQGP RGPPGPPGKA GEDGHPGKPG RPGERGVAGP QGARGFPGTP GLPGFKGIRG
HNGLDGQKGQ PGTPGTKGEP GAPGENGTPG QPGARGLPGE RGRIGAPGPA GARGSDGSAG
PTGPAGPIGA AGPPGFPGAP GAKGEIGPAG NVGPTGPAGP RGEIGLPGSS GPVGPPGNPG
ANGLPGAKGA AGLPGVAGAP GLPGPRGIPG PPGPAGPSGA RGLVGEPGPA GAKGESGNKG
EPGAAGPPGP PGPSGEEGKR GSNGEPGSAG PPGPAGLRGV PGSRGLPGAD GRAGVMGPAG
NRGASGPVGA KGPNGDAGRP GEPGLMGPRG LPGQPGSPGP AGKEGPVGFP GADGRVGPIG
PAGNRGEPGN IGFPGPKGPT GEPGKPGEKG NVGLAGPRGA PGPEGNNGAQ GPPGVTGNQG
AKGETGPAGP PGFQGLPGPS GPAGEAGKPG ERGLHGEFGV PGPAGPRGER GLPGESGAVG
PAGPIGSRGP SGPPGPDGNK GEPGNVGPAG APGPAGPGGI PGERGVAGVP GGKGEKGAPG
LRGDTGATGR DGARGLPGAI GAPGPAGGAG DRGEGGPAGP AGPAGARGIP GERGEPGPVG
PSGFAGPPGA AGQPGAKGER GPKGPKGETG PTGAIGPIGA SGPPGPVGAA GPAGPRGDAG
PPGMTGFPGA AGRVGPPGPA GITGPPGPPG PAGKDGPRGL RGDVGPVGRT GEQGIAGPPG
FAGEKGPSGE AGAAGPPGTP GPQGILGAPG ILGLPGSRGE RGLPGIAGAT GEPGPLGVSG
PPGARGPSGP VGSPGPNGAP GEAGRDGNPG NDGPPGRDGA PGFKGERGAP GNPGPSGALG
APGPHGQVGP SGKPGNRGDP GPVGPVGPAG AFGPRGLAGP QGPRGEKGEP GDKGHRGLPG
LKGHNGLQGL PGLAGQHGDQ GPPGNNGPAG PRGPPGPSGP PGKDGRNGLP GPIGPAGVRG
SHGSQGPAGP PGPPGPPGPP GPNGGGYEVG FDAEYYRADQ PSLRPKDYEV DATLKTLNNQ
IETLLTPEGS KKNPARTCRD LRLSHPEWSS GFYWIDPNQG CTADAIRAYC DFATGETCIH
ASLEDIPTKT WYVSKNPKDK KHIWFGETIN GGTQFEYNGE GVTTKDMATQ LAFMRLLANH
ASQNITYHCK NSIAYMDEET GNLKKAVILQ GSNDVELRAE GNSRFTFSVL VDGCSKKNNK
WGKTIIEYRT NKPSRLPILD IAPLDIGGAD QEFGLHIGPV CFK
