ID CO9A3_HUMAN Reviewed; 684 AA. AC Q14050; Q13681; Q9H4G9; Q9UPE2; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 27-NOV-2024, entry version 207. DE RecName: Full=Collagen alpha-3(IX) chain; DE Flags: Precursor; GN Name=COL9A3; 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], AND VARIANT GLU-435. RC TISSUE=Cartilage; RX PubMed=8586434; DOI=10.1006/geno.1995.9870; RA Brewton R.G., Wood B.M., Ren Z.-X., Gong Y., Tiller G.E., Warman M.L., RA Lee B., Horton W.A., Olsen B.R., Baker J.R., Mayne R.; RT "Molecular cloning of the alpha 3 chain of human type IX collagen: linkage RT of the gene COL9A3 to chromosome 20q13.3."; RL Genomics 30:329-336(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS 563-GLY--PRO-565 DEL AND RP 564-PRO--GLY-566 DEL. RX PubMed=10428822; DOI=10.1074/jbc.274.32.22469; RA Paassilta P., Pihlajamaa T., Annunen S., Brewton R.G., Wood B.M., RA Johnson C.C., Liu J., Gong Y., Warman M.L., Prockop D.J., Mayne R., RA Ala-Kokko L.; RT "Complete sequence of the 23-kilobase human COL9A3 gene. Detection of Gly- RT X-Y triplet deletions that represent neutral variants."; RL J. Biol. Chem. 274:22469-22475(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 NUCLEOTIDE SEQUENCE [MRNA] OF 522-667. RC TISSUE=Cartilage; RX PubMed=9164858; DOI=10.1042/bj3240209; RA Peraelae M., Savontaus M., Metsaeranta M., Vuorio E.; RT "Developmental regulation of mRNA species for types II, IX and XI collagens RT during mouse embryogenesis."; RL Biochem. J. 324:209-216(1997). RN [6] RP INVOLVEMENT IN EDM3. RX PubMed=10090888; DOI=10.1086/302328; RA Paassilta P., Lohiniva J., Annunen S., Bonaventure J., Le Merrer M., RA Pai L., Ala-Kokko L.; RT "COL9A3: A third locus for multiple epiphyseal dysplasia."; RL Am. J. Hum. Genet. 64:1036-1044(1999). RN [7] RP ERRATUM OF PUBMED:10090888. RA Paassilta P., Lohiniva J., Annunen S., Bonaventure J., Le Merrer M., RA Pai L., Ala-Kokko L.; RL Am. J. Hum. Genet. 65:1214-1214(1999). RN [8] RP INVOLVEMENT IN SUSCEPTIBILITY TO IDD. RX PubMed=11308397; DOI=10.1001/jama.285.14.1843; RA Paassilta P., Lohiniva J., Goring H.H., Perala M., Raina S.S., RA Karppinen J., Hakala M., Palm T., Kroger H., Kaitila I., Vanharanta H., RA Ott J., Ala-Kokko L.; RT "Identification of a novel common genetic risk factor for lumbar disk RT disease."; RL JAMA 285:1843-1849(2001). RN [9] RP INVOLVEMENT IN STL6. RX PubMed=24273071; DOI=10.1002/ajmg.a.36165; RA Faletra F., D'Adamo A.P., Bruno I., Athanasakis E., Biskup S., Esposito L., RA Gasparini P.; RT "Autosomal recessive Stickler syndrome due to a loss of function mutation RT in the COL9A3 gene."; RL Am. J. Med. Genet. A 164A:42-47(2014). RN [10] RP INVOLVEMENT IN STL6. RX PubMed=30450842; DOI=10.1002/ajmg.a.40647; RG University of Washington Center for Mendelian Genomics; RA Hanson-Kahn A., Li B., Cohn D.H., Nickerson D.A., Bamshad M.J., Hudgins L.; RT "Autosomal recessive Stickler syndrome resulting from a COL9A3 mutation."; RL Am. J. Med. Genet. A 176:2887-2891(2018). RN [11] RP VARIANTS GLN-103; TRP-103; LEU-296; GLN-402 AND GLU-435. RX PubMed=11565064; DOI=10.1086/324023; RA Czarny-Ratajczak M., Lohiniva J., Rogala P., Kozlowski K., Peraelae M., RA Carter L., Spector T.D., Kolodziej L., Seppaenen U., Glazar R., RA Krolewski J., Latos-Bielenska A., Ala-Kokko L.; RT "A mutation in COL9A1 causes multiple epiphyseal dysplasia: further RT evidence for locus heterogeneity."; RL Am. J. Hum. Genet. 69:969-980(2001). RN [12] RP VARIANT EDM3 ASP-35. RX PubMed=25381065; DOI=10.1186/1471-2474-15-371; RA Jeong C., Lee J.Y., Kim J., Chae H., Park H.I., Kim M., Kim O.H., Kim P., RA Lee Y.K., Jung J.; RT "Novel COL9A3 mutation in a family diagnosed with multiple epiphyseal RT dysplasia: a case report."; RL BMC Musculoskelet. Disord. 15:371-371(2014). RN [13] RP VARIANT STL6 471-ARG--SER-684 DEL. RX PubMed=31090205; DOI=10.1002/ajmg.a.61191; RA Nixon T.R.W., Alexander P., Richards A., McNinch A., Bearcroft P.W.P., RA Cobben J., Snead M.P.; RT "Homozygous Type IX collagen variants (COL9A1, COL9A2, and COL9A3) causing RT recessive Stickler syndrome-Expanding the phenotype."; RL Am. J. Med. Genet. A 179:1498-1506(2019). RN [14] RP VARIANTS STL6 90-ARG--SER-684 DEL AND 577-ARG--SER-684 DEL. RX PubMed=33570243; DOI=10.1002/mgg3.1620; RA Markova T., Sparber P., Borovikov A., Nagornova T., Dadali E.; RT "Clinical and genetic characterization of autosomal recessive stickler RT syndrome caused by novel compound heterozygous mutations in the COL9A3 RT gene."; RL Mol. Genet. Genomic Med. 9:e1620-e1620(2021). CC -!- FUNCTION: Structural component of hyaline cartilage and vitreous of the CC eye. CC -!- SUBUNIT: Heterotrimer of an alpha 1(IX), an alpha 2(IX) and an alpha CC 3(IX) chain. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000250}. CC -!- PTM: Covalently linked to the telopeptides of type II collagen by CC lysine-derived cross-links. 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 -!- DISEASE: Multiple epiphyseal dysplasia 3 (EDM3) [MIM:600969]: A CC generalized skeletal dysplasia associated with significant morbidity. CC Joint pain, joint deformity, waddling gait, and short stature are the CC main clinical signs and symptoms. Radiological examination of the CC skeleton shows delayed, irregular mineralization of the epiphyseal CC ossification centers and of the centers of the carpal and tarsal bones. CC Multiple epiphyseal dysplasia is broadly categorized into the more CC severe Fairbank and the milder Ribbing types. The Fairbank type is CC characterized by shortness of stature, short and stubby fingers, small CC epiphyses in several joints, including the knee, ankle, hand, and hip. CC The Ribbing type is confined predominantly to the hip joints and is CC characterized by hands that are normal and stature that is normal or CC near-normal. {ECO:0000269|PubMed:10090888, CC ECO:0000269|PubMed:25381065}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Intervertebral disc disease (IDD) [MIM:603932]: A common CC musculo-skeletal disorder caused by degeneration of intervertebral CC disks of the lumbar spine. It results in low-back pain and unilateral CC leg pain. {ECO:0000269|PubMed:11308397, ECO:0000269|PubMed:25381065}. CC Note=Disease susceptibility is associated with variants affecting the CC gene represented in this entry. Susceptibility to intervertebral disk CC disease is conferred by variant p.Arg103Trp (PubMed:11308397). CC {ECO:0000269|PubMed:11308397}. CC -!- DISEASE: Stickler syndrome 6 (STL6) [MIM:620022]: A form of Stickler CC syndrome, an inherited disorder that associates ocular signs with more CC or less complete forms of Pierre Robin sequence, bone disorders and CC sensorineural deafness. Ocular disorders may include juvenile cataract, CC myopia, strabismus, vitreoretinal or chorioretinal degeneration, CC retinal detachment, and chronic uveitis. Pierre Robin sequence includes CC an opening in the roof of the mouth (a cleft palate), a large tongue CC (macroglossia), and a small lower jaw (micrognathia). Bones are CC affected by slight platyspondyly and large, often defective epiphyses. CC Juvenile joint laxity is followed by early signs of arthrosis. The CC degree of hearing loss varies among affected individuals and may become CC more severe over time. STL6 is an autosomal recessive form CC characterized by early-onset progressive hearing loss and progressive CC myopia, with variable manifestation of facial dysmorphism and skeletal CC anomalies. {ECO:0000269|PubMed:24273071, ECO:0000269|PubMed:30450842, CC ECO:0000269|PubMed:31090205, ECO:0000269|PubMed:33570243}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted CC helices (FACIT) family. {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; L41162; AAC41947.1; -; mRNA. DR EMBL; AF026802; AAD47357.1; -; Genomic_DNA. DR EMBL; AF026801; AAD47357.1; JOINED; Genomic_DNA. DR EMBL; AL035669; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC011705; AAH11705.1; -; mRNA. DR EMBL; X91013; CAA62495.1; -; mRNA. DR CCDS; CCDS13505.1; -. DR RefSeq; NP_001844.3; NM_001853.3. DR PDB; 5CTD; X-ray; 1.60 A; C=517-553. DR PDB; 5CTI; X-ray; 1.90 A; C=517-553. DR PDB; 5CVA; X-ray; 2.10 A; C/F=517-553. DR PDB; 5CVB; X-ray; 2.25 A; C/F=517-553. DR PDBsum; 5CTD; -. DR PDBsum; 5CTI; -. DR PDBsum; 5CVA; -. DR PDBsum; 5CVB; -. DR AlphaFoldDB; Q14050; -. DR SMR; Q14050; -. DR BioGRID; 107696; 7. DR ComplexPortal; CPX-1748; Collagen type IX trimer. DR IntAct; Q14050; 5. DR STRING; 9606.ENSP00000496793; -. DR GlyCosmos; Q14050; 1 site, No reported glycans. DR GlyGen; Q14050; 1 site. DR iPTMnet; Q14050; -. DR PhosphoSitePlus; Q14050; -. DR BioMuta; COL9A3; -. DR DMDM; 20137327; -. DR jPOST; Q14050; -. DR MassIVE; Q14050; -. DR PaxDb; 9606-ENSP00000341640; -. DR PeptideAtlas; Q14050; -. DR ProteomicsDB; 59803; -. DR Antibodypedia; 29570; 175 antibodies from 23 providers. DR DNASU; 1299; -. DR Ensembl; ENST00000649368.1; ENSP00000496793.1; ENSG00000092758.18. DR GeneID; 1299; -. DR KEGG; hsa:1299; -. DR MANE-Select; ENST00000649368.1; ENSP00000496793.1; NM_001853.4; NP_001844.3. DR UCSC; uc002ydm.3; human. DR AGR; HGNC:2219; -. DR CTD; 1299; -. DR DisGeNET; 1299; -. DR GeneCards; COL9A3; -. DR GeneReviews; COL9A3; -. DR HGNC; HGNC:2219; COL9A3. DR HPA; ENSG00000092758; Tissue enhanced (brain). DR MalaCards; COL9A3; -. DR MIM; 120270; gene. DR MIM; 600969; phenotype. DR MIM; 603932; phenotype. DR MIM; 620022; phenotype. DR neXtProt; NX_Q14050; -. DR OpenTargets; ENSG00000092758; -. DR Orphanet; 250984; Autosomal recessive Stickler syndrome. DR Orphanet; 166002; Multiple epiphyseal dysplasia due to collagen 9 anomaly. DR PharmGKB; PA26735; -. DR VEuPathDB; HostDB:ENSG00000092758; -. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000163687; -. DR HOGENOM; CLU_001074_18_2_1; -. DR InParanoid; Q14050; -. DR OMA; MINEQIA; -. DR OrthoDB; 5363474at2759; -. DR PhylomeDB; Q14050; -. DR PathwayCommons; Q14050; -. DR Reactome; R-HSA-1442490; Collagen degradation. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR Reactome; R-HSA-186797; Signaling by PDGF. DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR Reactome; R-HSA-419037; NCAM1 interactions. DR Reactome; R-HSA-8948216; Collagen chain trimerization. DR SignaLink; Q14050; -. DR SIGNOR; Q14050; -. DR BioGRID-ORCS; 1299; 16 hits in 1145 CRISPR screens. DR ChiTaRS; COL9A3; human. DR GeneWiki; COL9A3; -. DR GenomeRNAi; 1299; -. DR Pharos; Q14050; Tbio. DR PRO; PR:Q14050; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q14050; protein. DR Bgee; ENSG00000092758; Expressed in tibia and 150 other cell types or tissues. DR ExpressionAtlas; Q14050; baseline and differential. DR GO; GO:0005594; C:collagen type IX trimer; IDA:BHF-UCL. 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:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central. DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR InterPro; IPR008160; Collagen. DR InterPro; IPR050149; Collagen_superfamily. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF958; ZGC:113232; 1. DR Pfam; PF01391; Collagen; 5. PE 1: Evidence at protein level; KW 3D-structure; Collagen; Deafness; Disease variant; Dwarfism; KW Extracellular matrix; Glycoprotein; Hydroxylation; KW Proteomics identification; Reference proteome; Repeat; Secreted; Signal; KW Stickler syndrome. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..684 FT /note="Collagen alpha-3(IX) chain" FT /id="PRO_0000005848" FT REGION 26..521 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 29..519 FT /note="Triple-helical region 3 (COL3)" FT REGION 520..550 FT /note="Nonhelical region 3 (NC3)" FT REGION 548..665 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 551..630 FT /note="Triple-helical region 2 (COL2)" FT REGION 631..632 FT /note="Nonhelical region 2 (NC2)" FT REGION 633..661 FT /note="Triple-helical region 1 (COL1)" FT REGION 662..684 FT /note="Nonhelical region 1 (NC1)" FT MOTIF 423..425 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 601..603 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT COMPBIAS 54..68 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 143..163 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 176..190 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 554..574 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 483 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 35 FT /note="G -> D (in EDM3; dbSNP:rs1390736361)" FT /evidence="ECO:0000269|PubMed:25381065" FT /id="VAR_072736" FT VARIANT 90..684 FT /note="Missing (in STL6)" FT /evidence="ECO:0000269|PubMed:33570243" FT /id="VAR_087540" FT VARIANT 94 FT /note="P -> S (in dbSNP:rs35908728)" FT /id="VAR_048808" FT VARIANT 103 FT /note="R -> Q (in dbSNP:rs142639450)" FT /evidence="ECO:0000269|PubMed:11565064" FT /id="VAR_026467" FT VARIANT 103 FT /note="R -> W (probable risk factor for intervertebral disk FT disease; dbSNP:rs61734651)" FT /evidence="ECO:0000269|PubMed:11565064" FT /id="VAR_026468" FT VARIANT 296 FT /note="P -> L (in dbSNP:rs45628843)" FT /evidence="ECO:0000269|PubMed:11565064" FT /id="VAR_026469" FT VARIANT 402 FT /note="R -> Q (in dbSNP:rs373519549)" FT /evidence="ECO:0000269|PubMed:11565064" FT /id="VAR_026470" FT VARIANT 435 FT /note="A -> E (in dbSNP:rs751557)" FT /evidence="ECO:0000269|PubMed:11565064, FT ECO:0000269|PubMed:8586434" FT /id="VAR_026471" FT VARIANT 471..684 FT /note="Missing (in STL6)" FT /evidence="ECO:0000269|PubMed:31090205" FT /id="VAR_087541" FT VARIANT 563..565 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:10428822" FT /id="VAR_012660" FT VARIANT 564..566 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:10428822" FT /id="VAR_012661" FT VARIANT 577..684 FT /note="Missing (in STL6)" FT /evidence="ECO:0000269|PubMed:33570243" FT /id="VAR_087542" FT CONFLICT 18 FT /note="E -> Q (in Ref. 1; AAC41947 and 2; AAD47357)" FT /evidence="ECO:0000305" FT CONFLICT 39 FT /note="P -> R (in Ref. 1; AAC41947)" FT /evidence="ECO:0000305" FT CONFLICT 144 FT /note="S -> P (in Ref. 1; AAC41947)" FT /evidence="ECO:0000305" FT CONFLICT 524 FT /note="R -> H (in Ref. 5; CAA62495)" FT /evidence="ECO:0000305" FT CONFLICT 576 FT /note="A -> T (in Ref. 5; CAA62495)" FT /evidence="ECO:0000305" FT HELIX 522..543 FT /evidence="ECO:0007829|PDB:5CTD" SQ SEQUENCE 684 AA; 63616 MW; 892F035CF6E06733 CRC64; MAGPRACAPL LLLLLLGELL AAAGAQRVGL PGPPGPPGPP GKPGQDGIDG EAGPPGLPGP PGPKGAPGKP GKPGEAGLPG LPGVDGLTGR DGPPGPKGAP GERGSLGPPG PPGLGGKGLP GPPGEAGVSG PPGGIGLRGP PGPSGLPGLP GPPGPPGPPG HPGVLPEGAT DLQCPSICPP GPPGPPGMPG FKGPTGYKGE QGEVGKDGEK GDPGPPGPAG LPGSVGLQGP RGLRGLPGPL GPPGDRGPIG FRGPPGIPGA PGKAGDRGER GPEGFRGPKG DLGRPGPKGT PGVAGPSGEP GMPGKDGQNG VPGLDGQKGE AGRNGAPGEK GPNGLPGLPG RAGSKGEKGE RGRAGELGEA GPSGEPGVPG DAGMPGERGE AGHRGSAGAL GPQGPPGAPG VRGFQGQKGS MGDPGLPGPQ GLRGDVGDRG PGGAAGPKGD QGIAGSDGLP GDKGELGPSG LVGPKGESGS RGELGPKGTQ GPNGTSGVQG VPGPPGPLGL QGVPGVPGIT GKPGVPGKEA SEQRIRELCG GMISEQIAQL AAHLRKPLAP GSIGRPGPAG PPGPPGPPGS IGHPGARGPP GYRGPTGELG DPGPRGNQGD RGDKGAAGAG LDGPEGDQGP QGPQGVPGTS KDGQDGAPGE PGPPGDPGLP GAIGAQGTPG ICDTSACQGA VLGGVGEKSG SRSS //