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   24-JAN-2024, entry version 177.
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 67 dpc in the primary ossification
CC       center 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};
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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   GlyCosmos; Q8IZC6; 3 sites, 1 glycan.
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; 9606-ENSP00000348385; -.
DR   PeptideAtlas; 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   AGR; HGNC:22986; -.
DR   CTD; 85301; -.
DR   DisGeNET; 85301; -.
DR   GeneCards; COL27A1; -.
DR   HGNC; HGNC:22986; COL27A1.
DR   HPA; ENSG00000196739; Tissue enhanced (brain, 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; HQHIAVG; -.
DR   OrthoDB; 2915342at2759; -.
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 1142 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 184 other cell types or tissues.
DR   ExpressionAtlas; Q8IZC6; baseline and differential.
DR   GO; GO:0005581; C:collagen trimer; IBA:GO_Central.
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; 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: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:0001525; P:angiogenesis; IBA:GO_Central.
DR   GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR   GO; GO:0001886; P:endothelial cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0003431; P:growth plate cartilage chondrocyte development; IEA:Ensembl.
DR   GO; GO:0030903; P:notochord development; IBA:GO_Central.
DR   GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR   Gene3D; 2.60.120.1000; -; 2.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000885; Fib_collagen_C.
DR   InterPro; IPR048287; TSPN-like_N.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF844; COLLAGEN ALPHA-1(XXVII) CHAIN; 1.
DR   Pfam; PF01410; COLFI; 2.
DR   Pfam; PF01391; Collagen; 8.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SMART; SM00038; COLFI; 1.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51461; NC1_FIB; 1.
DR   Genevisible; Q8IZC6; HS.
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
//