ID CO8A2_HUMAN Reviewed; 703 AA. AC P25067; Q5JV31; Q8TEJ5; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2004, sequence version 2. DT 27-MAR-2024, entry version 206. DE RecName: Full=Collagen alpha-2(VIII) chain; DE AltName: Full=Endothelial collagen; DE Flags: Precursor; GN Name=COL8A2; 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 [LARGE SCALE MRNA]. RC TISSUE=Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). 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 [GENOMIC DNA] OF 66-703. RX PubMed=2019595; DOI=10.1016/s0021-9258(20)89508-8; RA Muragaki Y., Jacenko O., Apte S., Mattei M.-G., Ninomiya Y., Olsen B.R.; RT "The alpha 2(VIII) collagen gene. A novel member of the short chain RT collagen family located on the human chromosome 1."; RL J. Biol. Chem. 266:7721-7727(1991). RN [5] RP PROTEOLYTIC PROCESSING. RX PubMed=1515454; DOI=10.1016/0925-4439(92)90103-t; RA Kittelberger R., Neale T.J., Francky K.T., Greenhill N.S., Gibson G.J.; RT "Cleavage of type VIII collagen by human neutrophil elastase."; RL Biochim. Biophys. Acta 1139:295-299(1992). RN [6] RP TISSUE SPECIFICITY. RX PubMed=10686422; DOI=10.1016/s0945-053x(99)00053-0; RA Greenhill N.S., Ruger B.M., Hasan Q., Davis P.F.; RT "The alpha1(VIII) and alpha2(VIII) collagen chains form two distinct RT homotrimeric proteins in vivo."; RL Matrix Biol. 19:19-28(2000). RN [7] RP SUBUNIT. RX PubMed=14990571; DOI=10.1074/jbc.m305805200; RA Stephan S., Sherratt M.J., Hodson N., Shuttleworth C.A., Kielty C.M.; RT "Expression and supramolecular assembly of recombinant alpha1(viii) and RT alpha2(viii) collagen homotrimers."; RL J. Biol. Chem. 279:21469-21477(2004). RN [8] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=17888087; DOI=10.1111/j.1365-2362.2007.01864.x; RA Gerth J., Cohen C.D., Hopfer U., Lindenmeyer M.T., Sommer M., Grone H.J., RA Wolf G.; RT "Collagen type VIII expression in human diabetic nephropathy."; RL Eur. J. Clin. Invest. 37:767-773(2007). RN [9] RP VARIANTS FECD1 GLN-304; ARG-357; HIS-434; LYS-455 AND LEU-575, VARIANT RP PPCD2 LYS-455, AND VARIANTS ARG-3; GLN-155 AND ILE-645. RX PubMed=11689488; DOI=10.1093/hmg/10.21.2415; RA Biswas S., Munier F.L., Yardley J., Hart-Holden N., Perveen R., Cousin P., RA Sutphin J.E., Noble B., Batterbury M., Kielty C., Hackett A., Bonshek R., RA Ridgway A., McLeod D., Sheffield V.C., Stone E.M., Schorderet D.F., RA Black G.C.M.; RT "Missense mutations in COL8A2, the gene encoding the alpha-2 chain of type RT VIII collagen, cause two forms of corneal endothelial dystrophy."; RL Hum. Mol. Genet. 10:2415-2423(2001). RN [10] RP VARIANTS GLN-155 AND MET-502. RX PubMed=15175909; DOI=10.1007/s10384-003-0063-6; RA Kobayashi A., Fujiki K., Murakami A., Kato T., Chen L.-Z., Onoe H., RA Nakayasu K., Sakurai M., Takahashi M., Sugiyama K., Kanai A.; RT "Analysis of COL8A2 gene mutation in Japanese patients with Fuchs' RT endothelial dystrophy and posterior polymorphous dystrophy."; RL Jpn. J. Ophthalmol. 48:195-198(2004). CC -!- FUNCTION: Macromolecular component of the subendothelium. Major CC component of the Descemet's membrane (basement membrane) of corneal CC endothelial cells. Also a component of the endothelia of blood vessels. CC Necessary for migration and proliferation of vascular smooth muscle CC cells and thus, has a potential role in the maintenance of vessel wall CC integrity and structure, in particular in atherogenesis (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Homotrimers, or heterotrimers in association with alpha CC 2(VIII) type collagens. Four homotrimers can form a tetrahedron CC stabilized by central interacting C-terminal NC1 trimers. CC {ECO:0000269|PubMed:14990571}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane. CC -!- TISSUE SPECIFICITY: Expressed primarily in the subendothelium of large CC blood vessels. Also expressed in arterioles and venules in muscle, CC heart, kidney, spleen, umbilical cord, liver and lung and is also found CC in connective tissue layers around hair follicles, around nerve bundles CC in muscle, in the dura of the optic nerve, in cornea and sclera, and in CC the perichondrium of cartilaginous tissues. In the kidney, expressed in CC mesangial cells, glomerular endothelial cells, and tubular epithelial CC cells. Also expressed in mast cells, and in astrocytes during the CC repair process. Expressed in Descemet's membrane. CC {ECO:0000269|PubMed:10686422, ECO:0000269|PubMed:17888087}. CC -!- INDUCTION: Some up-regulation in diabetic nephropathy. CC {ECO:0000269|PubMed:17888087}. CC -!- PTM: Proteolytically cleaved by neutrophil elastase, in vitro. CC {ECO:0000269|PubMed:1515454}. 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: Corneal dystrophy, Fuchs endothelial, 1 (FECD1) [MIM:136800]: CC A corneal disease caused by loss of endothelium of the central cornea. CC It is characterized by focal wart-like guttata that arise from Descemet CC membrane and develop in the central cornea, epithelial blisters, CC reduced vision and pain. Descemet membrane is thickened by abnormal CC collagenous deposition. {ECO:0000269|PubMed:11689488}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Corneal dystrophy, posterior polymorphous, 2 (PPCD2) CC [MIM:609140]: A rare mild subtype of posterior corneal dystrophy CC characterized by alterations of Descemet membrane presenting as CC vesicles, opacities or band-like lesions on slit-lamp examination and CC specular microscopy. Affected patient typically are asymptomatic. CC {ECO:0000269|PubMed:11689488}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=BAB84955.1; Type=Erroneous initiation; 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; AK074129; BAB84955.1; ALT_INIT; mRNA. DR EMBL; AL138787; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX07388.1; -; Genomic_DNA. DR EMBL; M60832; AAA62822.1; -; Genomic_DNA. DR CCDS; CCDS403.1; -. DR PIR; A57131; A57131. DR RefSeq; NP_001281276.1; NM_001294347.1. DR RefSeq; NP_005193.1; NM_005202.3. DR AlphaFoldDB; P25067; -. DR SMR; P25067; -. DR BioGRID; 107693; 46. DR ComplexPortal; CPX-1745; Collagen type VIII trimer variant 1. DR ComplexPortal; CPX-1747; Collagen type VIII trimer variant 3. DR STRING; 9606.ENSP00000380901; -. DR iPTMnet; P25067; -. DR PhosphoSitePlus; P25067; -. DR BioMuta; COL8A2; -. DR DMDM; 45644957; -. DR jPOST; P25067; -. DR MassIVE; P25067; -. DR PaxDb; 9606-ENSP00000380901; -. DR PeptideAtlas; P25067; -. DR ProteomicsDB; 54250; -. DR Antibodypedia; 56213; 180 antibodies from 24 providers. DR DNASU; 1296; -. DR Ensembl; ENST00000303143.9; ENSP00000305913.4; ENSG00000171812.13. DR Ensembl; ENST00000397799.2; ENSP00000380901.1; ENSG00000171812.13. DR GeneID; 1296; -. DR KEGG; hsa:1296; -. DR MANE-Select; ENST00000397799.2; ENSP00000380901.1; NM_005202.4; NP_005193.1. DR UCSC; uc001bzv.4; human. DR AGR; HGNC:2216; -. DR CTD; 1296; -. DR DisGeNET; 1296; -. DR GeneCards; COL8A2; -. DR HGNC; HGNC:2216; COL8A2. DR HPA; ENSG00000171812; Low tissue specificity. DR MalaCards; COL8A2; -. DR MIM; 120252; gene. DR MIM; 136800; phenotype. DR MIM; 609140; phenotype. DR neXtProt; NX_P25067; -. DR OpenTargets; ENSG00000171812; -. DR Orphanet; 98974; Fuchs endothelial corneal dystrophy. DR Orphanet; 98973; Posterior polymorphous corneal dystrophy. DR PharmGKB; PA26732; -. DR VEuPathDB; HostDB:ENSG00000171812; -. DR eggNOG; ENOG502QRST; Eukaryota. DR GeneTree; ENSGT00940000154317; -. DR InParanoid; P25067; -. DR OMA; IPHMKYM; -. DR OrthoDB; 4272636at2759; -. DR PhylomeDB; P25067; -. DR TreeFam; TF334029; -. DR PathwayCommons; P25067; -. DR Reactome; R-HSA-1442490; Collagen degradation. 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-216083; Integrin cell surface interactions. DR Reactome; R-HSA-8948216; Collagen chain trimerization. DR BioGRID-ORCS; 1296; 19 hits in 1141 CRISPR screens. DR ChiTaRS; COL8A2; human. DR GeneWiki; COL8A2; -. DR GenomeRNAi; 1296; -. DR Pharos; P25067; Tbio. DR PRO; PR:P25067; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P25067; Protein. DR Bgee; ENSG00000171812; Expressed in periodontal ligament and 163 other cell types or tissues. DR ExpressionAtlas; P25067; baseline and differential. DR GO; GO:0005604; C:basement membrane; IBA:GO_Central. 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:0031012; C:extracellular matrix; NAS:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005201; F:extracellular matrix structural constituent; NAS:UniProtKB. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; NAS:UniProtKB. DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl. DR GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB. DR GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR Gene3D; 2.60.120.40; -; 1. DR InterPro; IPR001073; C1q_dom. DR InterPro; IPR008160; Collagen. DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF855; COLLAGEN ALPHA-2(VIII) CHAIN; 1. DR Pfam; PF00386; C1q; 1. DR Pfam; PF01391; Collagen; 3. DR PRINTS; PR00007; COMPLEMNTC1Q. DR SMART; SM00110; C1Q; 1. DR SUPFAM; SSF49842; TNF-like; 1. DR PROSITE; PS50871; C1Q; 1. DR Genevisible; P25067; HS. PE 1: Evidence at protein level; KW Angiogenesis; Basement membrane; Cell adhesion; Collagen; KW Corneal dystrophy; Disease variant; Extracellular matrix; Hydroxylation; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..28 FT /evidence="ECO:0000255" FT CHAIN 29..703 FT /note="Collagen alpha-2(VIII) chain" FT /id="PRO_0000005835" FT DOMAIN 570..703 FT /note="C1q" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368" FT REGION 29..76 FT /note="Nonhelical region (NC2)" FT REGION 70..544 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 77..536 FT /note="Triple-helical region" FT REGION 537..703 FT /note="Nonhelical region (NC1)" FT COMPBIAS 74..100 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 220..234 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 505..533 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 3 FT /note="G -> R (in dbSNP:rs115156902)" FT /evidence="ECO:0000269|PubMed:11689488" FT /id="VAR_017893" FT VARIANT 155 FT /note="R -> Q (in dbSNP:rs75864656)" FT /evidence="ECO:0000269|PubMed:11689488, FT ECO:0000269|PubMed:15175909" FT /id="VAR_017894" FT VARIANT 304 FT /note="R -> Q (in FECD1; dbSNP:rs369487110)" FT /evidence="ECO:0000269|PubMed:11689488" FT /id="VAR_017895" FT VARIANT 357 FT /note="G -> R (in FECD1; uncertain significance; FT dbSNP:rs199786966)" FT /evidence="ECO:0000269|PubMed:11689488" FT /id="VAR_017896" FT VARIANT 434 FT /note="R -> H (in FECD1; dbSNP:rs201235688)" FT /evidence="ECO:0000269|PubMed:11689488" FT /id="VAR_017897" FT VARIANT 455 FT /note="Q -> K (in FECD1 and PPCD2; dbSNP:rs80358191)" FT /evidence="ECO:0000269|PubMed:11689488" FT /id="VAR_017898" FT VARIANT 502 FT /note="T -> M (in dbSNP:rs117860804)" FT /evidence="ECO:0000269|PubMed:15175909" FT /id="VAR_021387" FT VARIANT 575 FT /note="P -> L (in FECD1; uncertain significance; FT dbSNP:rs145553904)" FT /evidence="ECO:0000269|PubMed:11689488" FT /id="VAR_017899" FT VARIANT 645 FT /note="T -> I (in dbSNP:rs200767854)" FT /evidence="ECO:0000269|PubMed:11689488" FT /id="VAR_017900" FT CONFLICT 88 FT /note="R -> W (in Ref. 4; AAA62822)" FT /evidence="ECO:0000305" FT CONFLICT 102 FT /note="M -> H (in Ref. 4; AAA62822)" FT /evidence="ECO:0000305" FT CONFLICT 133 FT /note="K -> N (in Ref. 4; AAA62822)" FT /evidence="ECO:0000305" FT CONFLICT 347 FT /note="E -> D (in Ref. 4; AAA62822)" FT /evidence="ECO:0000305" FT CONFLICT 377..378 FT /note="PK -> LR (in Ref. 4; AAA62822)" FT /evidence="ECO:0000305" FT CONFLICT 506 FT /note="T -> R (in Ref. 4; AAA62822)" FT /evidence="ECO:0000305" FT CONFLICT 523 FT /note="P -> L (in Ref. 4; AAA62822)" FT /evidence="ECO:0000305" FT CONFLICT 529..531 FT /note="Missing (in Ref. 4; AAA62822)" FT /evidence="ECO:0000305" FT CONFLICT 585 FT /note="F -> L (in Ref. 4; AAA62822)" FT /evidence="ECO:0000305" FT CONFLICT 677 FT /note="M -> I (in Ref. 4; AAA62822)" FT /evidence="ECO:0000305" SQ SEQUENCE 703 AA; 67244 MW; 84BD7CBDBDECD466 CRC64; MLGTLTPLSS LLLLLLVLVL GCGPRASSGG GAGGAAGYAP VKYIQPMQKG PVGPPFREGK GQYLEMPLPL LPMDLKGEPG PPGKPGPRGP PGPPGFPGKP GMGKPGLHGQ PGPAGPPGFS RMGKAGPPGL PGKVGPPGQP GLRGEPGIRG DQGLRGPPGP PGLPGPSGIT IPGKPGAQGV PGPPGFQGEP GPQGEPGPPG DRGLKGDNGV GQPGLPGAPG QGGAPGPPGL PGPAGLGKPG LDGLPGAPGD KGESGPPGVP GPRGEPGAVG PKGPPGVDGV GVPGAAGLPG PQGPSGAKGE PGTRGPPGLI GPTGYGMPGL PGPKGDRGPA GVPGLLGDRG EPGEDGEPGE QGPQGLGGPP GLPGSAGLPG RRGPPGPKGE AGPGGPPGVP GIRGDQGPSG LAGKPGVPGE RGLPGAHGPP GPTGPKGEPG FTGRPGGPGV AGALGQKGDL GLPGQPGLRG PSGIPGLQGP AGPIGPQGLP GLKGEPGLPG PPGEGRAGEP GTAGPTGPPG VPGSPGITGP PGPPGPPGPP GAPGAFDETG IAGLHLPNGG VEGAVLGKGG KPQFGLGELS AHATPAFTAV LTSPFPASGM PVKFDRTLYN GHSGYNPATG IFTCPVGGVY YFAYHVHVKG TNVWVALYKN NVPATYTYDE YKKGYLDQAS GGAVLQLRPN DQVWVQMPSD QANGLYSTEY IHSSFSGFLL CPT //