ID   CO9A2_HUMAN             Reviewed;         689 AA.
AC   Q14055; B2RMP9;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 2.
DT   27-MAR-2024, entry version 204.
DE   RecName: Full=Collagen alpha-2(IX) chain {ECO:0000305};
DE   Flags: Precursor;
GN   Name=COL9A2 {ECO:0000312|HGNC:HGNC:2218};
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 [GENOMIC DNA].
RC   TISSUE=Foreskin;
RX   PubMed=9707347; DOI=10.1016/s0945-053x(98)90063-4;
RA   Pihlajamaa T., Vuoristo M.M., Annunen S., Peraelae M., Prockop D.J.,
RA   Ala-Kokko L.;
RT   "Human COL9A1 and COL9A2 genes. Two genes of 90 and 15 kb code for similar
RT   polypeptides of the same collagen molecule.";
RL   Matrix Biol. 17:237-241(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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 50-668.
RC   TISSUE=Cartilage;
RX   PubMed=8454052; DOI=10.1016/0014-5793(93)80062-y;
RA   Peraelae M., Haenninen M., Haestbacka J., Elima K., Vuorio E.;
RT   "Molecular cloning of the human alpha 2(IX) collagen cDNA and assignment of
RT   the human COL9A2 gene to chromosome 1.";
RL   FEBS Lett. 319:177-180(1993).
RN   [6]
RP   INVOLVEMENT IN EDM2.
RX   PubMed=10364514; DOI=10.1086/302440;
RA   Holden P., Canty E.G., Mortier G.R., Zabel B., Spranger J., Carr A.,
RA   Grant M.E., Loughlin J.A., Briggs M.D.;
RT   "Identification of novel pro-alpha2(IX) collagen gene mutations in two
RT   families with distinctive oligo-epiphyseal forms of multiple epiphyseal
RT   dysplasia.";
RL   Am. J. Hum. Genet. 65:31-38(1999).
RN   [7]
RP   INVOLVEMENT IN STL5.
RX   PubMed=21671392; DOI=10.1002/ajmg.a.34071;
RA   Baker S., Booth C., Fillman C., Shapiro M., Blair M.P., Hyland J.C.,
RA   Ala-Kokko L.;
RT   "A loss of function mutation in the COL9A2 gene causes autosomal recessive
RT   Stickler syndrome.";
RL   Am. J. Med. Genet. A 155:1668-1672(2011).
RN   [8]
RP   INVOLVEMENT IN STL5.
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   [9]
RP   INVOLVEMENT IN STL5.
RX   PubMed=33356723; DOI=10.1080/13816810.2020.1861309;
RA   Kjellstroem U., Martell S., Brobeck C., Andreasson S.;
RT   "Autosomal recessive Stickler syndrome associated with homozygous mutations
RT   in the COL9A2 gene.";
RL   Ophthalmic Genet. 42:161-169(2021).
RN   [10]
RP   VARIANT IDD TRP-326, AND VARIANT ARG-326.
RX   PubMed=10411504; DOI=10.1126/science.285.5426.409;
RA   Annunen S., Paassilta P., Lohiniva J., Peraelae M., Pihlajamaa T.,
RA   Karppinen J., Tervonen O., Kroeger H., Laehde S., Vanharanta H.,
RA   Ryhaenen L., Goering H.H.H., Ott J., Prockop D.J., Ala-Kokko L.;
RT   "An allele of COL9A2 associated with intervertebral disc disease.";
RL   Science 285:409-412(1999).
RN   [11]
RP   VARIANTS MET-246; ARG-326 AND VAL-335.
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 326-GLN--PRO-689 DEL.
RX   PubMed=28887846; DOI=10.1002/humu.23335;
RA   Zhou X.L., He L.X., Yu L.J., Wang Y., Wang X.J., Wang E.D., Yang T.;
RT   "Mutations in KARS cause early-onset hearing loss and leukoencephalopathy:
RT   Potential pathogenic mechanism.";
RL   Hum. Mutat. 38:1740-1750(2017).
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 (By similarity). The chains are linked to each other by
CC       interchain disulfide bonds (By similarity). Trimers are also cross-
CC       linked via hydroxylysines (By similarity).
CC       {ECO:0000250|UniProtKB:C0HLN2}.
CC   -!- INTERACTION:
CC       Q14055; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-714971, EBI-16439278;
CC       Q14055; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-714971, EBI-741480;
CC       Q14055; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-714971, EBI-947187;
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 2 (EDM2) [MIM:600204]: 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:10364514}. Note=The disease is caused
CC       by variants 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:10411504}. Note=Disease susceptibility is
CC       associated with variants affecting the gene represented in this entry.
CC   -!- DISEASE: Stickler syndrome 5 (STL5) [MIM:614284]: An autosomal
CC       recessive form of Stickler syndrome, an inherited disorder that
CC       associates ocular signs with more or less complete forms of Pierre
CC       Robin sequence, bone disorders and sensorineural deafness. STL5 is
CC       characterized by high myopia, vitreoretinal degeneration, retinal
CC       detachment, mild to moderate sensorineural hearing loss, short stature
CC       in childhood, and absence of cleft palate and Pierre Robin sequence.
CC       {ECO:0000269|PubMed:21671392, ECO:0000269|PubMed:31090205,
CC       ECO:0000269|PubMed:33356723}. Note=The disease is caused by variants
CC       affecting the gene represented in this 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; AF019406; AAC33512.1; -; Genomic_DNA.
DR   EMBL; AL050341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX07229.1; -; Genomic_DNA.
DR   EMBL; BC136326; AAI36327.1; -; mRNA.
DR   EMBL; BC136327; AAI36328.1; -; mRNA.
DR   EMBL; M95610; AAA80977.1; -; mRNA.
DR   CCDS; CCDS450.1; -.
DR   PIR; S32436; S32436.
DR   RefSeq; NP_001843.1; NM_001852.3.
DR   RefSeq; XP_006710428.1; XM_006710365.3.
DR   PDB; 5CTD; X-ray; 1.60 A; B=517-552.
DR   PDB; 5CTI; X-ray; 1.90 A; B=517-552.
DR   PDB; 5CVA; X-ray; 2.10 A; B/E=517-552.
DR   PDB; 5CVB; X-ray; 2.25 A; B/E=517-552.
DR   PDBsum; 5CTD; -.
DR   PDBsum; 5CTI; -.
DR   PDBsum; 5CVA; -.
DR   PDBsum; 5CVB; -.
DR   AlphaFoldDB; Q14055; -.
DR   SMR; Q14055; -.
DR   BioGRID; 107695; 14.
DR   ComplexPortal; CPX-1748; Collagen type IX trimer.
DR   IntAct; Q14055; 8.
DR   STRING; 9606.ENSP00000361834; -.
DR   GlyCosmos; Q14055; 2 sites, No reported glycans.
DR   GlyGen; Q14055; 3 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q14055; -.
DR   PhosphoSitePlus; Q14055; -.
DR   BioMuta; COL9A2; -.
DR   DMDM; 20137328; -.
DR   EPD; Q14055; -.
DR   jPOST; Q14055; -.
DR   MassIVE; Q14055; -.
DR   PaxDb; 9606-ENSP00000361834; -.
DR   PeptideAtlas; Q14055; -.
DR   ProteomicsDB; 59804; -.
DR   Pumba; Q14055; -.
DR   TopDownProteomics; Q14055; -.
DR   Antibodypedia; 64754; 38 antibodies from 13 providers.
DR   DNASU; 1298; -.
DR   Ensembl; ENST00000372748.8; ENSP00000361834.3; ENSG00000049089.15.
DR   GeneID; 1298; -.
DR   KEGG; hsa:1298; -.
DR   MANE-Select; ENST00000372748.8; ENSP00000361834.3; NM_001852.4; NP_001843.1.
DR   UCSC; uc001cfh.2; human.
DR   AGR; HGNC:2218; -.
DR   CTD; 1298; -.
DR   DisGeNET; 1298; -.
DR   GeneCards; COL9A2; -.
DR   GeneReviews; COL9A2; -.
DR   HGNC; HGNC:2218; COL9A2.
DR   HPA; ENSG00000049089; Group enriched (brain, pituitary gland).
DR   MalaCards; COL9A2; -.
DR   MIM; 120260; gene.
DR   MIM; 600204; phenotype.
DR   MIM; 603932; phenotype.
DR   MIM; 614284; phenotype.
DR   neXtProt; NX_Q14055; -.
DR   OpenTargets; ENSG00000049089; -.
DR   Orphanet; 250984; Autosomal recessive Stickler syndrome.
DR   Orphanet; 166002; Multiple epiphyseal dysplasia due to collagen 9 anomaly.
DR   PharmGKB; PA26734; -.
DR   VEuPathDB; HostDB:ENSG00000049089; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000161290; -.
DR   HOGENOM; CLU_001074_18_2_1; -.
DR   InParanoid; Q14055; -.
DR   OMA; MIGGPGQ; -.
DR   OrthoDB; 2970370at2759; -.
DR   PhylomeDB; Q14055; -.
DR   PathwayCommons; Q14055; -.
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; Q14055; -.
DR   SIGNOR; Q14055; -.
DR   BioGRID-ORCS; 1298; 11 hits in 1144 CRISPR screens.
DR   ChiTaRS; COL9A2; human.
DR   GeneWiki; COL9A2; -.
DR   GenomeRNAi; 1298; -.
DR   Pharos; Q14055; Tbio.
DR   PRO; PR:Q14055; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q14055; Protein.
DR   Bgee; ENSG00000049089; Expressed in C1 segment of cervical spinal cord and 137 other cell types or tissues.
DR   ExpressionAtlas; Q14055; 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   GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR   InterPro; IPR008160; Collagen.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF958; ZGC:113232; 1.
DR   Pfam; PF01391; Collagen; 8.
DR   Genevisible; Q14055; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Collagen; Deafness; Disease variant; Disulfide bond;
KW   Dwarfism; Extracellular matrix; Glycoprotein; Hydroxylation; Proteoglycan;
KW   Reference proteome; Repeat; Secreted; Signal; Stickler syndrome.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..689
FT                   /note="Collagen alpha-2(IX) chain"
FT                   /id="PRO_0000005837"
FT   REGION          26..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          27..163
FT                   /note="Triple-helical region 4 (COL4)"
FT   REGION          164..180
FT                   /note="Nonhelical region 4 (NC4)"
FT   REGION          181..519
FT                   /note="Triple-helical region 3 (COL3)"
FT   REGION          520..549
FT                   /note="Nonhelical region 3 (NC3)"
FT   REGION          550..632
FT                   /note="Triple-helical region 2 (COL2)"
FT   REGION          554..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..634
FT                   /note="Nonhelical region 2 (NC2)"
FT   REGION          635..664
FT                   /note="Triple-helical region 1 (COL1)"
FT   REGION          665..689
FT                   /note="Nonhelical region 1 (NC1)"
FT   COMPBIAS        30..44
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..128
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..158
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..571
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         160
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P12108"
FT   MOD_RES         183
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000250|UniProtKB:P12108"
FT   CARBOHYD        169
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P12108"
FT   CARBOHYD        183
FT                   /note="O-linked (Gal...) hydroxylysine"
FT                   /evidence="ECO:0000250|UniProtKB:P12108"
FT   DISULFID        174
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
FT   DISULFID        178
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
FT   VARIANT         246
FT                   /note="T -> M (in dbSNP:rs2228565)"
FT                   /evidence="ECO:0000269|PubMed:11565064"
FT                   /id="VAR_026465"
FT   VARIANT         326..689
FT                   /note="Missing"
FT                   /evidence="ECO:0000269|PubMed:28887846"
FT                   /id="VAR_079749"
FT   VARIANT         326
FT                   /note="Q -> R (in dbSNP:rs2228564)"
FT                   /evidence="ECO:0000269|PubMed:10411504,
FT                   ECO:0000269|PubMed:11565064"
FT                   /id="VAR_012659"
FT   VARIANT         326
FT                   /note="Q -> W (in IDD; requires 2 nucleotide substitutions;
FT                   dbSNP:rs137853213)"
FT                   /evidence="ECO:0000269|PubMed:10411504"
FT                   /id="VAR_012658"
FT   VARIANT         335
FT                   /note="L -> V (in dbSNP:rs2228567)"
FT                   /evidence="ECO:0000269|PubMed:11565064"
FT                   /id="VAR_026466"
FT   VARIANT         581
FT                   /note="V -> I (in dbSNP:rs3737821)"
FT                   /id="VAR_020014"
FT   HELIX           523..549
FT                   /evidence="ECO:0007829|PDB:5CTD"
SQ   SEQUENCE   689 AA;  65131 MW;  EB6106E02F6FA862 CRC64;
     MAAATASPRS LLVLLQVVVL ALAQIRGPPG ERGPPGPPGP PGVPGSDGID GDNGPPGKAG
     PPGPKGEPGK AGPDGPDGKP GIDGLTGAKG EPGPMGIPGV KGQPGLPGPP GLPGPGFAGP
     PGPPGPVGLP GEIGIRGPKG DPGPDGPSGP PGPPGKPGRP GTIQGLEGSA DFLCPTNCPP
     GMKGPPGLQG VKGHAGKRGI LGDPGHQGKP GPKGDVGASG EQGIPGPPGP QGIRGYPGMA
     GPKGETGPHG YKGMVGAIGA TGPPGEEGPR GPPGRAGEKG DEGSPGIRGP QGITGPKGAT
     GPPGINGKDG TPGTPGMKGS AGQAGQPGSP GHQGLAGVPG QPGTKGGPGD QGEPGPQGLP
     GFSGPPGKEG EPGPRGEIGP QGIMGQKGDQ GERGPVGQPG PQGRQGPKGE QGPPGIPGPQ
     GLPGVKGDKG SPGKTGPRGK VGDPGVAGLP GEKGEKGESG EPGPKGQQGV RGEPGYPGPS
     GDAGAPGVQG YPGPPGPRGL AGNRGVPGQP GRQGVEGRDA TDQHIVDVAL KMLQEQLAEV
     AVSAKREALG AVGMMGPPGP PGPPGYPGKQ GPHGHPGPRG VPGIVGAVGQ IGNTGPKGKR
     GEKGDPGEVG RGHPGMPGPP GIPGLPGRPG QAINGKDGDR GSPGAPGEAG RPGLPGPVGL
     PGFCEPAACL GASAYASARL TEPGSIKGP
//