CORA1_HUMAN
ID CORA1_HUMAN Reviewed; 1860 AA.
AC Q8IZC6; Q66K43; Q96JF7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Collagen alpha-1(XXVII) chain;
DE Flags: Precursor;
GN Name=COL27A1; Synonyms=KIAA1870;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Cartilage;
RX PubMed=12714037; DOI=10.1016/s0945-053x(03)00007-6;
RA Pace J.M., Corrado M., Missero C., Byers P.H.;
RT "Identification, characterization and expression analysis of a new
RT fibrillar collagen gene, COL27A1.";
RL Matrix Biol. 22:3-14(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 238-1860 (ISOFORM 3), AND
RP VARIANTS THR-422; THR-537 AND PHE-611.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=17693149; DOI=10.1016/j.bone.2007.06.024;
RA Hjorten R., Hansen U., Underwood R.A., Telfer H.E., Fernandes R.J.,
RA Krakow D., Sebald E., Wachsmann-Hogiu S., Bruckner P., Jacquet R.,
RA Landis W.J., Byers P.H., Pace J.M.;
RT "Type XXVII collagen at the transition of cartilage to bone during
RT skeletogenesis.";
RL Bone 41:535-542(2007).
RN [6]
RP INVOLVEMENT IN STLS, AND VARIANT STLS ARG-697.
RX PubMed=24986830; DOI=10.1038/ejhg.2014.107;
RA Gonzaga-Jauregui C., Gamble C.N., Yuan B., Penney S., Jhangiani S.,
RA Muzny D.M., Gibbs R.A., Lupski J.R., Hecht J.T.;
RT "Mutations in COL27A1 cause Steel syndrome and suggest a founder mutation
RT effect in the Puerto Rican population.";
RL Eur. J. Hum. Genet. 23:342-346(2015).
CC -!- FUNCTION: Plays a role during the calcification of cartilage and the
CC transition of cartilage to bone. {ECO:0000269|PubMed:17693149}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix. Note=Found on some small banded collagen fibrils and meshworks.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IZC6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZC6-2; Sequence=VSP_030347;
CC Name=3;
CC IsoId=Q8IZC6-3; Sequence=VSP_030348, VSP_030349;
CC -!- DEVELOPMENTAL STAGE: Detected at E67 in the primary ossification center
CC and is tightly restricted to the pericellular region of the
CC hypertrophic chondrocytes and lacunae at the very center of the future
CC diaphysis. At fetal 20-week highly abundant in the hypertrophic zone at
CC the chondroosseous junction. Weakly detected around cells in the
CC resting and proliferative zone of the cartilaginous plate, but the
CC intense detection occurred deep in the hypertrophic zone near the newly
CC formed bone. Detected throughout the extracellular matrix (ECM) in this
CC zone it is also closely situated around hypertrophic chondrocytes.
CC {ECO:0000269|PubMed:17693149}.
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 -!- DISEASE: Steel syndrome (STLS) [MIM:615155]: A syndrome characterized
CC by dislocated hips and radial heads, fusion of carpal bones, short
CC stature, scoliosis, and cervical spine anomalies. Facial features
CC include prominent forehead, long oval-shaped face, hypertelorism and
CC broad nasal bridge. {ECO:0000269|PubMed:24986830}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB47499.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; AY149237; AAN41263.1; -; mRNA.
DR EMBL; AB058773; BAB47499.1; ALT_INIT; mRNA.
DR EMBL; AL356796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC080610; AAH80610.1; -; mRNA.
DR CCDS; CCDS6802.1; -. [Q8IZC6-1]
DR RefSeq; NP_116277.2; NM_032888.3. [Q8IZC6-1]
DR AlphaFoldDB; Q8IZC6; -.
DR BioGRID; 124464; 6.
DR ComplexPortal; CPX-1768; Collagen type XXVII trimer.
DR IntAct; Q8IZC6; 6.
DR MINT; Q8IZC6; -.
DR STRING; 9606.ENSP00000348385; -.
DR ChEMBL; CHEMBL2364188; -.
DR GlyGen; Q8IZC6; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IZC6; -.
DR PhosphoSitePlus; Q8IZC6; -.
DR BioMuta; COL27A1; -.
DR DMDM; 74762504; -.
DR jPOST; Q8IZC6; -.
DR MassIVE; Q8IZC6; -.
DR PaxDb; Q8IZC6; -.
DR PeptideAtlas; Q8IZC6; -.
DR PRIDE; Q8IZC6; -.
DR ProteomicsDB; 71316; -. [Q8IZC6-1]
DR ProteomicsDB; 71318; -. [Q8IZC6-3]
DR Antibodypedia; 65300; 29 antibodies from 15 providers.
DR DNASU; 85301; -.
DR Ensembl; ENST00000356083.8; ENSP00000348385.3; ENSG00000196739.15. [Q8IZC6-1]
DR GeneID; 85301; -.
DR KEGG; hsa:85301; -.
DR MANE-Select; ENST00000356083.8; ENSP00000348385.3; NM_032888.4; NP_116277.2.
DR UCSC; uc011lxl.3; human. [Q8IZC6-1]
DR CTD; 85301; -.
DR DisGeNET; 85301; -.
DR GeneCards; COL27A1; -.
DR HGNC; HGNC:22986; COL27A1.
DR HPA; ENSG00000196739; Tissue enhanced (cervix).
DR MalaCards; COL27A1; -.
DR MIM; 608461; gene.
DR MIM; 615155; phenotype.
DR neXtProt; NX_Q8IZC6; -.
DR OpenTargets; ENSG00000196739; -.
DR Orphanet; 438117; Steel syndrome.
DR PharmGKB; PA134990818; -.
DR VEuPathDB; HostDB:ENSG00000196739; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000163466; -.
DR HOGENOM; CLU_001074_19_1_1; -.
DR InParanoid; Q8IZC6; -.
DR OMA; YSYPDRL; -.
DR OrthoDB; 200318at2759; -.
DR PhylomeDB; Q8IZC6; -.
DR TreeFam; TF344135; -.
DR PathwayCommons; Q8IZC6; -.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; Q8IZC6; -.
DR BioGRID-ORCS; 85301; 9 hits in 1064 CRISPR screens.
DR ChiTaRS; COL27A1; human.
DR GeneWiki; Collagen,_type_XXVII,_alpha_1; -.
DR GenomeRNAi; 85301; -.
DR Pharos; Q8IZC6; Tbio.
DR PRO; PR:Q8IZC6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8IZC6; protein.
DR Bgee; ENSG00000196739; Expressed in tibia and 182 other tissues.
DR ExpressionAtlas; Q8IZC6; baseline and differential.
DR Genevisible; Q8IZC6; HS.
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:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005583; C:fibrillar collagen trimer; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0003431; P:growth plate cartilage chondrocyte development; IEA:Ensembl.
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; 2.
DR Pfam; PF01391; Collagen; 13.
DR SMART; SM00038; COLFI; 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; Disease variant; Disulfide bond;
KW Dwarfism; Extracellular matrix; Glycoprotein; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT PROPEP 42..624
FT /note="N-terminal propeptide"
FT /id="PRO_0000314667"
FT CHAIN 625..1621
FT /note="Collagen alpha-1(XXVII) chain"
FT /id="PRO_5000089163"
FT PROPEP 1622..1860
FT /note="C-terminal propeptide"
FT /id="PRO_0000314668"
FT DOMAIN 71..236
FT /note="Laminin G-like"
FT DOMAIN 625..679
FT /note="Collagen-like 1"
FT DOMAIN 688..747
FT /note="Collagen-like 2"
FT DOMAIN 748..807
FT /note="Collagen-like 3"
FT DOMAIN 808..867
FT /note="Collagen-like 4"
FT DOMAIN 871..930
FT /note="Collagen-like 5"
FT DOMAIN 931..990
FT /note="Collagen-like 6"
FT DOMAIN 1003..1062
FT /note="Collagen-like 7"
FT DOMAIN 1066..1125
FT /note="Collagen-like 8"
FT DOMAIN 1126..1185
FT /note="Collagen-like 9"
FT DOMAIN 1192..1251
FT /note="Collagen-like 10"
FT DOMAIN 1258..1317
FT /note="Collagen-like 11"
FT DOMAIN 1318..1378
FT /note="Collagen-like 12"
FT DOMAIN 1382..1441
FT /note="Collagen-like 13"
FT DOMAIN 1442..1501
FT /note="Collagen-like 14"
FT DOMAIN 1502..1561
FT /note="Collagen-like 15"
FT DOMAIN 1562..1621
FT /note="Collagen-like 16"
FT DOMAIN 1660..1860
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 278..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..1618
FT /note="Triple-helical region"
FT REGION 625..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..1625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..666
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1621
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1708
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1710
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1713
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1716
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1769
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1690..1722
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1696
FT /note="Interchain (with C-1285)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1713
FT /note="Interchain (with C-1268)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1731..1858
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1767..1811
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT VAR_SEQ 1..1033
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11347906"
FT /id="VSP_030347"
FT VAR_SEQ 637..703
FT /note="GPPGLPGLPGIPGARGPRGPPGPYGNPGLPGPPGAKGQKGDPGLSPGKAHDG
FT AKGDMGLPGLSGNPG -> VRLSGVCMLLGAPVGDWGIGQVVAPSKDRKRSSLEQGAGY
FT GYILGSSQAPGSSGSAKCIIAHPAPDS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030348"
FT VAR_SEQ 704..1860
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030349"
FT VARIANT 89
FT /note="V -> I (in dbSNP:rs2567707)"
FT /id="VAR_048784"
FT VARIANT 120
FT /note="Q -> R (in dbSNP:rs2567706)"
FT /id="VAR_048785"
FT VARIANT 265
FT /note="A -> T (in dbSNP:rs34578955)"
FT /id="VAR_048786"
FT VARIANT 349
FT /note="R -> C (in dbSNP:rs34973417)"
FT /id="VAR_048787"
FT VARIANT 422
FT /note="A -> T (in dbSNP:rs2241671)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_048788"
FT VARIANT 537
FT /note="I -> T (in dbSNP:rs2808770)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_048789"
FT VARIANT 611
FT /note="I -> F (in dbSNP:rs2567705)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_048790"
FT VARIANT 697
FT /note="G -> R (in STLS; dbSNP:rs140950220)"
FT /evidence="ECO:0000269|PubMed:24986830"
FT /id="VAR_072564"
FT VARIANT 720
FT /note="P -> R (in dbSNP:rs35446342)"
FT /id="VAR_048791"
FT VARIANT 1116
FT /note="P -> Q (in dbSNP:rs7048607)"
FT /id="VAR_048792"
FT VARIANT 1348
FT /note="R -> Q (in dbSNP:rs1631319)"
FT /id="VAR_048793"
FT VARIANT 1354
FT /note="R -> Q (in dbSNP:rs10982134)"
FT /id="VAR_048794"
FT VARIANT 1808
FT /note="M -> V (in dbSNP:rs3736252)"
FT /id="VAR_048795"
SQ SEQUENCE 1860 AA; 186892 MW; 5F8CDFAF4B6014EC CRC64;
MGAGSARGAR GTAAAAAARG GGFLFSWILV SFACHLASTQ GAPEDVDILQ RLGLSWTKAG
SPAPPGVIPF QSGFIFTQRA RLQAPTGTVI PAALGTELAL VLSLCSHRVN HAFLFAVRSQ
KRKLQLGLQF LPGKTVVHLG SRRSVAFDLD MHDGRWHHLA LELRGRTVTL VTACGQRRVP
VLLPFHRDPA LDPGGSFLFG KMNPHAVQFE GALCQFSIYP VTQVAHNYCT HLRKQCGQAD
TYQSPLGPLF SQDSGRPFTF QSDLALLGLE NLTTATPALG SLPAGRGPRG TVAPATPTKP
QRTSPTNPHQ HMAVGGPAQT PLLPAKLSAS NALDPMLPAS VGGSTRTPRP AAAQPSQKIT
ATKIPKSLPT KPSAPSTSIV PIKSPHPTQK TAPSSFTKSA LPTQKQVPPT SRPVPARVSR
PAEKPIQRNP GMPRPPPPST RPLPPTTSSS KKPIPTLART EAKITSHASK PASARTSTHK
PPPFTALSSS PAPTPGSTRS TRPPATMVPP TSGTSTPRTA PAVPTPGSAP TGSKKPIGSE
ASKKAGPKSS PRKPVPLRPG KAARDVPLSD LTTRPSPRQP QPSQQTTPAL VLAPAQFLSS
SPRPTSSGYS IFHLAGSTPF PLLMGPPGPK GDCGLPGPPG LPGLPGIPGA RGPRGPPGPY
GNPGLPGPPG AKGQKGDPGL SPGKAHDGAK GDMGLPGLSG NPGPPGRKGH KGYPGPAGHP
GEQGQPGPEG SPGAKGYPGR QGLPGPVGDP GPKGSRGYIG LPGLFGLPGS DGERGLPGVP
GKRGKMGMPG FPGVFGERGP PGLDGNPGEL GLPGPPGVPG LIGDLGVLGP IGYPGPKGMK
GLMGSVGEPG LKGDKGEQGV PGVSGDPGFQ GDKGSQGLPG FPGARGKPGP LGKVGDKGSI
GFPGPPGPEG FPGDIGPPGD NGPEGMKGKP GARGLPGPRG QLGPEGDEGP MGPPGAPGLE
GQPGRKGFPG RPGLDGVKGE PGDPGRPGPV GEQGFMGFIG LVGEPGIVGE KGDRGMMGPP
GVPGPKGSMG HPGMPGGMGT PGEPGPQGPP GSRGPPGMRG AKGRRGPRGP DGPAGEQGSR
GLKGPPGPQG RPGRPGQQGV AGERGHLGSR GFPGIPGPSG PPGTKGLPGE PGPQGPQGPI
GPPGEMGPKG PPGAVGEPGL PGEAGMKGDL GPLGTPGEQG LIGQRGEPGL EGDSGPMGPD
GLKGDRGDPG PDGEHGEKGQ EGLMGEDGPP GPPGVTGVRG PEGKSGKQGE KGRTGAKGAK
GYQGQLGEMG VPGDPGPPGT PGPKGSRGSL GPTGAPGRMG AQGEPGLAGY DGHKGIVGPL
GPPGPKGEKG EQGEDGKAEG PPGPPGDRGP VGDRGDRGEP GDPGYPGQEG VQGLRGKPGQ
QGQPGHPGPR GWPGPKGSKG AEGPKGKQGK AGAPGRRGVQ GLQGLPGPRG VVGRQGLEGI
AGPDGLPGRD GQAGQQGEQG DDGDPGPMGP AGKRGNPGVA GLPGAQGPPG FKGESGLPGQ
LGPPGKRGTE GRTGLPGNQG EPGSKGQPGD SGEMGFPGMA GLFGPKGPPG DIGFKGIQGP
RGPPGLMGKE GIVGPLGILG PSGLPGPKGD KGSRGDWGLQ GPRGPPGPRG RPGPPGPPGG
PIQLQQDDLG AAFQTWMDTS GALRPESYSY PDRLVLDQGG EIFKTLHYLS NLIQSIKTPL
GTKENPARVC RDLMDCEQKM VDGTYWVDPN LGCSSDTIEV SCNFTHGGQT CLKPITASKV
EFAISRVQMN FLHLLSSEVT QHITIHCLNM TVWQEGTGQT PAKQAVRFRA WNGQIFEAGG
QFRPEVSMDG CKVQDGRWHQ TLFTFRTQDP QQLPIISVDN LPPASSGKQY RLEVGPACFL
