COPA1_HUMAN
ID COPA1_HUMAN Reviewed; 654 AA.
AC Q9BXS0; A8MPZ6; Q9BXR9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Collagen alpha-1(XXV) chain;
DE AltName: Full=Alzheimer disease amyloid-associated protein;
DE Short=AMY;
DE AltName: Full=CLAC-P;
DE Contains:
DE RecName: Full=Collagen-like Alzheimer amyloid plaque component;
DE Short=CLAC;
GN Name=COL25A1 {ECO:0000312|HGNC:HGNC:18603};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK35008.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 131-152
RP AND 156-214, INTERACTION WITH AMYLOID-BETA PEPTIDE, TISSUE SPECIFICITY,
RP CLEAVAGE, HYDROXYLATION, PYROGLUTAMATE FORMATION AT GLU-113, AND
RP MUTAGENESIS OF ARG-109 AND ARG-112.
RX PubMed=11927537; DOI=10.1093/emboj/21.7.1524;
RA Hashimoto T., Wakabayashi T., Watanabe A., Kowa H., Hosoda R., Nakamura A.,
RA Kanazawa I., Arai T., Takio K., Mann D.M.A., Iwatsubo T.;
RT "CLAC: a novel Alzheimer amyloid plaque component derived from a
RT transmembrane precursor, CLAC-P/collagen type XXV.";
RL EMBO J. 21:1524-1534(2002).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=14656069; DOI=10.1093/jnen/62.11.1108;
RA Soederberg L., Zhukareva V., Bogdanovic N., Hashimoto T., Winblad B.,
RA Iwatsubo T., Lee V.M.Y., Trojanowski J.Q., Naeslund J.;
RT "Molecular identification of AMY, an Alzheimer disease amyloid-associated
RT protein.";
RL J. Neuropathol. Exp. Neurol. 62:1108-1117(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF CLAC N-TERMINUS, PROTEIN SEQUENCE OF 182-191 AND
RP 445-452, FUNCTION, SUBUNIT, INTERACTION WITH AMYLOID-BETA PEPTIDE,
RP GLYCOSYLATION, HYDROXYLATION, AND MUTAGENESIS OF 181-LEU--LYS-188.
RX PubMed=15522881; DOI=10.1074/jbc.m403628200;
RA Soederberg L., Kakuyama H., Moeller A., Ito A., Winblad B., Tjernberg L.O.,
RA Naeslund J.;
RT "Characterization of the Alzheimer's disease-associated CLAC protein and
RT identification of an amyloid beta-peptide-binding site.";
RL J. Biol. Chem. 280:1007-1015(2005).
RN [5] {ECO:0000305}
RP INTERACTION WITH AMYLOID-BETA PEPTIDE.
RX PubMed=15215182; DOI=10.1016/s0002-9440(10)63295-6;
RA Kowa H., Sakakura T., Matsuura Y., Wakabayashi T., Mann D.M.A., Duff K.,
RA Tsuji S., Hashimoto T., Iwatsubo T.;
RT "Mostly separate distributions of CLAC- versus Abeta40- or thioflavin S-
RT reactivities in senile plaques reveal two distinct subpopulations of beta-
RT amyloid deposits.";
RL Am. J. Pathol. 165:273-281(2004).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=16300410; DOI=10.1021/bi051263e;
RA Kakuyama H., Soederberg L., Horigome K., Winblad B., Dahlqvist C.,
RA Naeslund J., Tjernberg L.O.;
RT "CLAC binds to aggregated Abeta and Abeta fragments, and attenuates fibril
RT elongation.";
RL Biochemistry 44:15602-15609(2005).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=15853808; DOI=10.1111/j.1742-4658.2005.04647.x;
RA Soederberg L., Dahlqvist C., Kakuyama H., Thyberg J., Ito A., Winblad B.,
RA Naeslund J., Tjernberg L.O.;
RT "Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils
RT into protease resistant aggregates.";
RL FEBS J. 272:2231-2236(2005).
RN [8] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH AMYLOID-BETA PEPTIDE.
RX PubMed=15615705; DOI=10.1074/jbc.m413340200;
RA Osada Y., Hashimoto T., Nishimura A., Matsuo Y., Wakabayashi T.,
RA Iwatsubo T.;
RT "CLAC binds to amyloid beta peptides through the positively charged amino
RT acid cluster within the collagenous domain 1 and inhibits formation of
RT amyloid fibrils.";
RL J. Biol. Chem. 280:8596-8605(2005).
RN [9]
RP ERRATUM OF PUBMED:15615705.
RA Osada Y., Hashimoto T., Nishimura A., Matsuo Y., Wakabayashi T.,
RA Iwatsubo T.;
RL J. Biol. Chem. 280:15484-15484(2005).
RN [10]
RP INVOLVEMENT IN CFEOM5, VARIANT CFEOM5 ARG-382, AND CHARACTERIZATION OF
RP VARIANT CFEOM5 ARG-382.
RX PubMed=25500261; DOI=10.1016/j.ajhg.2014.11.006;
RA Shinwari J.M., Khan A., Awad S., Shinwari Z., Alaiya A., Alanazi M.,
RA Tahir A., Poizat C., Al Tassan N.;
RT "Recessive mutations in COL25A1 are a cause of congenital cranial
RT dysinnervation disorder.";
RL Am. J. Hum. Genet. 96:147-152(2015).
CC -!- FUNCTION: Inhibits fibrillization of amyloid-beta peptide during the
CC elongation phase. Has also been shown to assemble amyloid fibrils into
CC protease-resistant aggregates. Binds heparin.
CC {ECO:0000269|PubMed:15522881, ECO:0000269|PubMed:15615705,
CC ECO:0000269|PubMed:15853808, ECO:0000269|PubMed:16300410}.
CC -!- SUBUNIT: Forms homodimers and homotrimers. Binds to the fibrillized
CC forms of amyloid-beta protein 40 (beta-APP40) and amyloid-beta protein
CC 42 (beta-APP42). Found associated with beta-APP42 more frequently than
CC with beta-APP40. {ECO:0000269|PubMed:11927537,
CC ECO:0000269|PubMed:15215182, ECO:0000269|PubMed:15522881,
CC ECO:0000269|PubMed:15615705}.
CC -!- INTERACTION:
CC Q9BXS0-3; Q9BXS0-3: COL25A1; NbExp=4; IntAct=EBI-11682418, EBI-11682418;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}. Note=After proteolytic cleavage, CLAC
CC is secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:11927537};
CC IsoId=Q9BXS0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11927537};
CC IsoId=Q9BXS0-2; Sequence=VSP_052200;
CC Name=3 {ECO:0000269|PubMed:14656069};
CC IsoId=Q9BXS0-3; Sequence=VSP_052197, VSP_052198, VSP_052199;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in brain. Deposited
CC preferentially in primitive or neuritic amyloid plaques which are
CC typical of Alzheimer disease. {ECO:0000269|PubMed:11927537}.
CC -!- PTM: Undergoes proteolytic cleavage by furin protease to yield the
CC soluble collagen-like Alzheimer amyloid plaque component.
CC {ECO:0000269|PubMed:11927537}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:15522881}.
CC -!- PTM: Hydroxylated on 11% of proline residues and 49% of lysine
CC residues. {ECO:0000269|PubMed:11927537, ECO:0000269|PubMed:15522881}.
CC -!- DISEASE: Fibrosis of extraocular muscles, congenital, 5 (CFEOM5)
CC [MIM:616219]: An ocular motility disorder characterized by congenital
CC dysinnervation of various cranial nerves to ocular muscles. Clinical
CC features are ophthalmoplegia, anchoring of the eyes in downward gaze,
CC ptosis, and backward tilt of the head. {ECO:0000269|PubMed:25500261}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- CAUTION: The pyrrolidone carboxylic acid reported in PubMed:11927537
CC probably formed artifactually from Glu-113 during the extraction
CC procedure in 70% formic acid. In PubMed:15522881, the protein was found
CC to have unblocked Glu at the N-terminus. {ECO:0000305}.
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DR EMBL; AF293340; AAK35008.1; -; mRNA.
DR EMBL; AF293341; AAK35009.1; -; mRNA.
DR EMBL; AC097473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC095066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS43258.1; -. [Q9BXS0-1]
DR CCDS; CCDS43259.1; -. [Q9BXS0-2]
DR RefSeq; NP_115907.2; NM_032518.2. [Q9BXS0-2]
DR RefSeq; NP_942014.1; NM_198721.3. [Q9BXS0-1]
DR AlphaFoldDB; Q9BXS0; -.
DR BioGRID; 124143; 5.
DR ComplexPortal; CPX-1766; Collagen type XXV trimer, variant 1. [Q9BXS0-1]
DR ComplexPortal; CPX-390; Collagen type XXV trimer, variant 2. [Q9BXS0-2]
DR ComplexPortal; CPX-391; Collagen type XXV trimer, variant 3. [Q9BXS0-3]
DR STRING; 9606.ENSP00000382083; -.
DR iPTMnet; Q9BXS0; -.
DR PhosphoSitePlus; Q9BXS0; -.
DR BioMuta; COL25A1; -.
DR DMDM; 296434459; -.
DR MassIVE; Q9BXS0; -.
DR MaxQB; Q9BXS0; -.
DR PaxDb; Q9BXS0; -.
DR PeptideAtlas; Q9BXS0; -.
DR PRIDE; Q9BXS0; -.
DR ProteomicsDB; 79487; -. [Q9BXS0-1]
DR ProteomicsDB; 79488; -. [Q9BXS0-2]
DR ProteomicsDB; 79489; -. [Q9BXS0-3]
DR Antibodypedia; 7049; 180 antibodies from 26 providers.
DR DNASU; 84570; -.
DR Ensembl; ENST00000399126.1; ENSP00000382077.1; ENSG00000188517.17. [Q9BXS0-2]
DR Ensembl; ENST00000399132.6; ENSP00000382083.1; ENSG00000188517.17. [Q9BXS0-1]
DR GeneID; 84570; -.
DR KEGG; hsa:84570; -.
DR MANE-Select; ENST00000399132.6; ENSP00000382083.1; NM_198721.4; NP_942014.1.
DR UCSC; uc062yyf.1; human. [Q9BXS0-1]
DR CTD; 84570; -.
DR DisGeNET; 84570; -.
DR GeneCards; COL25A1; -.
DR HGNC; HGNC:18603; COL25A1.
DR HPA; ENSG00000188517; Tissue enhanced (brain, retina).
DR MalaCards; COL25A1; -.
DR MIM; 610004; gene.
DR MIM; 616219; phenotype.
DR neXtProt; NX_Q9BXS0; -.
DR OpenTargets; ENSG00000188517; -.
DR Orphanet; 91411; Congenital ptosis.
DR PharmGKB; PA134912284; -.
DR VEuPathDB; HostDB:ENSG00000188517; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000159823; -.
DR InParanoid; Q9BXS0; -.
DR OrthoDB; 669310at2759; -.
DR PhylomeDB; Q9BXS0; -.
DR TreeFam; TF338175; -.
DR PathwayCommons; Q9BXS0; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; Q9BXS0; -.
DR BioGRID-ORCS; 84570; 12 hits in 1068 CRISPR screens.
DR ChiTaRS; COL25A1; human.
DR GeneWiki; Collagen,_type_XXV,_alpha_1; -.
DR GenomeRNAi; 84570; -.
DR Pharos; Q9BXS0; Tbio.
DR PRO; PR:Q9BXS0; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9BXS0; protein.
DR Bgee; ENSG00000188517; Expressed in sperm and 102 other tissues.
DR ExpressionAtlas; Q9BXS0; baseline and differential.
DR Genevisible; Q9BXS0; HS.
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:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Amyloid; Collagen; Direct protein sequencing;
KW Disease variant; Glycoprotein; Heparin-binding; Hydroxylation; Membrane;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..654
FT /note="Collagen alpha-1(XXV) chain"
FT /id="PRO_0000259611"
FT CHAIN 113..654
FT /note="Collagen-like Alzheimer amyloid plaque component"
FT /evidence="ECO:0000269|PubMed:11927537,
FT ECO:0000269|PubMed:15522881"
FT /id="PRO_0000259612"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..654
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 121..164
FT /note="Collagen-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 192..247
FT /note="Collagen-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 249..308
FT /note="Collagen-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 311..370
FT /note="Collagen-like 4"
FT /evidence="ECO:0000255"
FT DOMAIN 372..425
FT /note="Collagen-like 5"
FT /evidence="ECO:0000255"
FT DOMAIN 447..505
FT /note="Collagen-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 571..630
FT /note="Collagen-like 7"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..188
FT /note="Interaction with amyloid-beta peptide"
FT /evidence="ECO:0000269|PubMed:15522881"
FT REGION 189..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..210
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..547
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 112..113
FT /note="Cleavage; by furin"
FT MOD_RES 113
FT /note="Pyrrolidone carboxylic acid (Glu)"
FT /evidence="ECO:0000269|PubMed:11927537"
FT VAR_SEQ 141..146
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14656069"
FT /id="VSP_052197"
FT VAR_SEQ 326..340
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14656069"
FT /id="VSP_052198"
FT VAR_SEQ 589..640
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14656069"
FT /id="VSP_052199"
FT VAR_SEQ 616..654
FT /note="GFRGVKGEKGEPGQPGLDGLDAPCQLGPDGLPMPGCWQK -> VTSPSQHVP
FT CLILLLLSALLFSLCDSI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11927537"
FT /id="VSP_052200"
FT VARIANT 382
FT /note="G -> R (in CFEOM5; causes loss of stability; causes
FT incorrect folding; dbSNP:rs780209390)"
FT /evidence="ECO:0000269|PubMed:25500261"
FT /id="VAR_073325"
FT MUTAGEN 109
FT /note="R->A: Not secreted."
FT /evidence="ECO:0000269|PubMed:11927537"
FT MUTAGEN 112
FT /note="R->A: Not secreted."
FT /evidence="ECO:0000269|PubMed:11927537"
FT MUTAGEN 181..188
FT /note="LIKRRLIK->VIKRRTFQ: Reduces binding to amyloid-beta
FT peptide."
FT /evidence="ECO:0000269|PubMed:15522881"
FT MUTAGEN 181..188
FT /note="Missing: Abolishes binding to amyloid-beta peptide."
FT /evidence="ECO:0000269|PubMed:15522881"
FT CONFLICT 28
FT /note="A -> S (in Ref. 1; AAK35008 and 2; AAK35009)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="E -> K (in Ref. 1; AAK35008 and 2; AAK35009)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 654 AA; 64771 MW; D6DFB4FB157C05A2 CRC64;
MLLKKHAGKG GGREPRSEDP TPAEQHCART MPPCAVLAAL LSVVAVVSCL YLGVKTNDLQ
ARIAALESAK GAPSIHLLPD TLDHLKTMVQ EKVERLLAQK SYEHMAKIRI AREAPSECNC
PAGPPGKRGK RGRRGESGPP GQPGPQGPPG PKGDKGEQGD QGPRMVFPKI NHGFLSADQQ
LIKRRLIKGD QGQAGPPGPP GPPGPRGPPG DTGKDGPRGM PGVPGEPGKP GEQGLMGPLG
PPGQKGSIGA PGIPGMNGQK GEPGLPGAVG QNGIPGPKGE PGEQGEKGDA GENGPKGDTG
EKGDPGSSAA GIKGEPGESG RPGQKGEPGL PGLPGLPGIK GEPGFIGPQG EPGLPGLPGT
KGERGEAGPP GRGERGEPGA PGPKGKQGES GTRGPKGSKG DRGEKGDSGA QGPRGPPGQK
GDQGATEIID YNGNLHEALQ RITTLTVTGP PGPPGPQGLQ GPKGEQGSPG IPGMDGEQGL
KGSKGDMGDP GMTGEKGGIG LPGLPGANGM KGEKGDSGMP GPQGPSIIGP PGPPGPHGPP
GPMGPHGLPG PKGTDGPMGP HGPAGPKGER GEKGAMGEPG PRGPYGLPGK DGEPGLDGFP
GPRGEKGDLG EKGEKGFRGV KGEKGEPGQP GLDGLDAPCQ LGPDGLPMPG CWQK
