ID CO1A2_HUMAN Reviewed; 1366 AA. AC P08123; P02464; Q13897; Q13997; Q13998; Q14038; Q14057; Q15177; AC Q15947; Q16480; Q16511; Q7Z5S6; Q9UEB6; Q9UEF9; Q9UM83; Q9UMI1; AC Q9UML5; Q9UMM6; Q9UPH0; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 7. DT 09-DEC-2015, entry version 187. DE RecName: Full=Collagen alpha-2(I) chain; DE AltName: Full=Alpha-2 type I collagen; DE Flags: Precursor; GN Name=COL1A2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASN-249; THR-276; VAL-483; RP ALA-549; HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354. RX PubMed=2824475; RA de Wet W.J., Bernard M.P., Benson-Chanda V., Chu M.-L., Dickson L.A., RA Weil D., Ramirez F.; RT "Organization of the human pro-alpha 2(I) collagen gene."; RL J. Biol. Chem. 262:16032-16036(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], REVIEW ON OI VARIANTS, AND VARIANTS RP ALA-549; HIS-678 AND HIS-1354. RX PubMed=9016532; DOI=10.1093/nar/25.1.181; RA Dalgleish R.; RT "The human type I collagen mutation database."; RL Nucleic Acids Res. 25:181-187(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-270; VAL-483; RP HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354. RX PubMed=9443882; DOI=10.1086/301689; RA Korkko J.M., Ala-Kokko L., De Paepe A., Nuytinck L., Earley J.J., RA Prockop D.J.; RT "Analysis of the COL1A1 and COL1A2 genes by PCR amplification and RT scanning by conformation-sensitive gel electrophoresis identifies only RT COL1A1 mutations in 15 patients with osteogenesis imperfecta type I: RT identification of common sequences of null-allele mutations."; RL Am. J. Hum. Genet. 62:98-110(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-549. RC TISSUE=Skin, and Uterus; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-765, AND VARIANTS HIS-678 AND GLY-743. RC TISSUE=Placenta; RX PubMed=3421913; RA Kuivaniemi H., Tromp G., Chu M.-L., Prockop D.J.; RT "Structure of a full-length cDNA clone for the prepro alpha 2(I) chain RT of human type I procollagen. Comparison with the chicken gene confirms RT unusual patterns of gene conservation."; RL Biochem. J. 252:633-640(1988). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-93, AND VARIANT PRO-59. RX PubMed=4011429; DOI=10.1093/nar/13.10.3427; RA Dickson L.A., de Wet W., Di Liberto M., Weil D., Ramirez F.; RT "Analysis of the promoter region and the N-propeptide domain of the RT human pro alpha 2(I) collagen gene."; RL Nucleic Acids Res. 13:3427-3438(1985). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32. RA Akai J., Kimura A., Arai K., Uehara K., Hata R.; RT "Fine structural analysis of the unique 5' region of the human COL1A2 RT gene containing two regions of dinucleotide repeats adjacent to the RT transcriptional start site."; RL Connect. Tissue Res. 30:1-6(1998). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-93, AND VARIANT EDS7B RP 76-ASN--MET-93 DEL. RX PubMed=2394758; RA Weil D., D'Alessio M., Ramirez F., Eyre D.R.; RT "Structural and functional characterization of a splicing mutation in RT the pro-alpha 2(I) collagen gene of an Ehlers-Danlos type VII RT patient."; RL J. Biol. Chem. 265:16007-16011(1990). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-93, AND VARIANT EDS7B RP 76-ASN--MET-93 DEL. RX PubMed=1577745; RA Watson R.B., Wallis G.A., Holmes D.F., Viljoen D., Byers P.H., RA Kadler K.E.; RT "Ehlers Danlos syndrome type VIIB. Incomplete cleavage of abnormal RT type I procollagen by N-proteinase in vitro results in the formation RT of copolymers of collagen and partially cleaved pNcollagen that are RT near circular in cross-section."; RL J. Biol. Chem. 267:9093-9100(1992). RN [10] RP PROTEIN SEQUENCE OF 80-96. RC TISSUE=Skin; RX PubMed=5529814; DOI=10.1021/bi00826a012; RA Click E.M., Bornstein P.; RT "Isolation and characterization of the cyanogen bromide peptides from RT the alpha 1 and alpha 2 chains of human skin collagen."; RL Biochemistry 9:4699-4706(1970). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-198. RX PubMed=3403536; RA Kuivaniemi H., Sabol C., Tromp G., Sippola-Thiele M., Prockop D.J.; RT "A 19-base pair deletion in the pro-alpha 2(I) gene of type I RT procollagen that causes in-frame RNA splicing from exon 10 to exon 12 RT in a proband with atypical osteogenesis imperfecta and in his RT asymptomatic mother."; RL J. Biol. Chem. 263:11407-11413(1988). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 163-213, AND VARIANT OI4 RP 181-GLY--LYS-198 DEL. RX PubMed=1642148; DOI=10.1002/jbmr.5650070709; RA Chipman S.D., Shapiro J.R., McKinstry M.B., Stover M.L., Branson P., RA Rowe D.W.; RT "Expression of mutant alpha (I)-procollagen in osteoblast and RT fibroblast cultures from a proband with osteogenesis imperfecta type RT IV."; RL J. Bone Miner. Res. 7:793-805(1992). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 181-1366. RA Kalicki J., Wamsley P., Gibson A.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [14] RP PROTEIN SEQUENCE OF 417-447, AND HYDROXYLATION AT PRO-420; PRO-441 AND RP PRO-444. RC TISSUE=Skin; RX PubMed=4412529; DOI=10.1111/j.1432-1033.1974.tb03689.x; RA Fietzek P.P., Furthmayr H., Kuehn K.; RT "Comparative sequence studies on alpha2-CB2 from calf, human, rabbit RT and pig-skin collagen."; RL Eur. J. Biochem. 47:257-261(1974). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 520-573, AND VARIANT ALA-549. RX PubMed=2839839; DOI=10.1073/pnas.85.14.5254; RA Tromp G., Prockop D.J.; RT "Single base mutation in the pro alpha 2(I) collagen gene that causes RT efficient splicing of RNA from exon 27 to exon 29 and synthesis of a RT shortened but in-frame pro alpha 2(I) chain."; RL Proc. Natl. Acad. Sci. U.S.A. 85:5254-5258(1988). RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 622-657. RX PubMed=6321602; DOI=10.1111/1523-1747.ep12260213; RA Tajima S., Ting J.P., Pinnell S.R., Kaufman R.E.; RT "Isolation and characterization of a human pro alpha 2(I) collagen RT gene segment."; RL J. Invest. Dermatol. 82:265-269(1984). RN [17] RP NUCLEOTIDE SEQUENCE [MRNA] OF 623-1366, AND VARIANTS HIS-678; RP PHE-1022; GLU-1189; PRO-1198 AND HIS-1354. RX PubMed=6687691; DOI=10.1021/bi00274a023; RA Bernard M.P., Myers J.C., Chu M.-L., Ramirez F., Eikenberry E.F., RA Prockop D.J.; RT "Structure of a cDNA for the pro alpha 2 chain of human type I RT procollagen. Comparison with chick cDNA for pro alpha 2(I) identifies RT structurally conserved features of the protein and the gene."; RL Biochemistry 22:1139-1145(1983). RN [18] RP NUCLEOTIDE SEQUENCE [MRNA] OF 631-864, AND VARIANT OI2 RP 676-GLY--ALA-855 DEL. RX PubMed=1339453; RA Chessler S.D., Byers P.H.; RT "Defective folding and stable association with protein disulfide RT isomerase/prolyl hydroxylase of type I procollagen with a deletion in RT the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern."; RL J. Biol. Chem. 267:7751-7757(1992). RN [19] RP NUCLEOTIDE SEQUENCE [MRNA] OF 663-746, AND VARIANT OI3 VAL-676. RX PubMed=7881420; DOI=10.1093/hmg/3.12.2201; RA Forlino A., Zolezzi F., Valli M., Pignatti P.F., Cetta G., RA Brunelli P.C., Mottes M.; RT "Severe (type III) osteogenesis imperfecta due to glycine RT substitutions in the central domain of the collagen triple helix."; RL Hum. Mol. Genet. 3:2201-2206(1994). RN [20] RP NUCLEOTIDE SEQUENCE [MRNA] OF 960-1356, AND VARIANT HIS-1354. RC TISSUE=Skin; RX PubMed=2364107; RA Maekelae J.K., Vuorio T., Vuorio E.; RT "Growth-dependent modulation of type I collagen production and mRNA RT levels in cultured human skin fibroblasts."; RL Biochim. Biophys. Acta 1049:171-176(1990). RN [21] RP NUCLEOTIDE SEQUENCE [MRNA] OF 964-1019. RX PubMed=6267597; DOI=10.1073/pnas.78.6.3516; RA Myers J.C., Chu M.-L., Faro S.H., Clark W.J., Prockop D.J., RA Ramirez F.; RT "Cloning a cDNA for the pro-alpha 2 chain of human type I collagen."; RL Proc. Natl. Acad. Sci. U.S.A. 78:3516-3520(1981). RN [22] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1090-1107, AND VARIANT OI4 RP ARG-1102. RX PubMed=2897363; RA Wenstrup R.J., Cohn D.H., Cohen T., Byers P.H.; RT "Arginine for glycine substitution in the triple-helical domain of the RT products of one alpha 2(I) collagen allele (COL1A2) produces the RT osteogenesis imperfecta type IV phenotype."; RL J. Biol. Chem. 263:7734-7740(1988). RN [23] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366, AND VARIANT HIS-1354. RX PubMed=6309769; RA Myers J.C., Dickson L.A., de Wet W.J., Bernard M.P., Chu M.-L., RA Di Liberto M., Pepe G., Sangiorgi F.O., Ramirez F.; RT "Analysis of the 3' end of the human pro-alpha 2(I) collagen gene. RT Utilization of multiple polyadenylation sites in cultured RT fibroblasts."; RL J. Biol. Chem. 258:10128-10135(1983). RN [24] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366, AND VARIANT HIS-1354. RC TISSUE=Skin; RX PubMed=6092353; RA Pihlajaniemi T., Dickson L.A., Pope F.M., Korhonen V.R., Nicholls A., RA Prockop D.J., Myers J.C.; RT "Osteogenesis imperfecta: cloning of a pro-alpha 2(I) collagen gene RT with a frameshift mutation."; RL J. Biol. Chem. 259:12941-12944(1984). RN [25] RP REVIEW ON VARIANTS. RX PubMed=2010058; RA Kuivaniemi H., Tromp G., Prockop D.J.; RT "Mutations in collagen genes: causes of rare and some common diseases RT in humans."; RL FASEB J. 5:2052-2060(1991). RN [26] RP REVIEW ON VARIANTS. RX PubMed=9101290; RX DOI=10.1002/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.0.CO;2-9; RA Kuivaniemi H., Tromp G., Prockop D.J.; RT "Mutations in fibrillar collagens (types I, II, III, and XI), fibril- RT associated collagen (type IX), and network-forming collagen (type X) RT cause a spectrum of diseases of bone, cartilage, and blood vessels."; RL Hum. Mutat. 9:300-315(1997). RN [27] RP REVIEW ON OI VARIANTS. RX PubMed=1895312; DOI=10.1136/jmg.28.7.433; RA Byers P.H., Wallis G.A., Willing M.C.; RT "Osteogenesis imperfecta: translation of mutation to phenotype."; RL J. Med. Genet. 28:433-442(1991). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., RA Fischer-Posovszky P., Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion RT profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [29] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [30] RP VARIANT EDS7B 76-ASN--MET-93 DEL. RX PubMed=3680255; RA Wirtz M.K., Glanville R.W., Steinmann B., Rao V.H., Hollister D.W.; RT "Ehlers-Danlos syndrome type VIIB. Deletion of 18 amino acids RT comprising the N-telopeptide region of a pro-alpha 2(I) chain."; RL J. Biol. Chem. 262:16376-16385(1987). RN [31] RP VARIANT OI2 ASP-997. RX PubMed=2914942; RA Baldwin C.T., Constantinou C., Dumars K.W., Prockop D.J.; RT "A single base mutation that converts glycine 907 of the alpha 2(I) RT chain of type I procollagen to aspartate in a lethal variant of RT osteogenesis imperfecta. The single amino acid substitution near the RT carboxyl terminus destabilizes the whole triple helix."; RL J. Biol. Chem. 264:3002-3006(1989). RN [32] RP VARIANT OI2 SER-955. RX PubMed=2777764; RA Lamande S.R., Dahl H.-H.M., Cole W.G., Bateman J.F.; RT "Characterization of point mutations in the collagen COL1A1 and COL1A2 RT genes causing lethal perinatal osteogenesis imperfecta."; RL J. Biol. Chem. 264:15809-15812(1989). RN [33] RP VARIANT OI2 CYS-877. RA Fertala A., Westerhausen A., Morris G.M., Rooney J.E., Prockop D.J.; RT "Two cysteine substitutions in the type I procollagen genes (COL1A1 RT and COL1A2) that cause lethal osteogenesis imperfecta. The location of RT glycine substitutions does not in any simple way predict their effects RT on protein function or phenotype."; RL Am. J. Hum. Genet. 47:A216-A216(1990). RN [34] RP VARIANT OI4 VAL-676. RX PubMed=2064612; RA Bateman J.F., Hannagan M., Chan D., Cole W.G.; RT "Characterization of a type I collagen alpha 2(I) glycine-586 to RT valine substitution in osteogenesis imperfecta type IV. Detection of RT the mutation and prenatal diagnosis by a chemical cleavage method."; RL Biochem. J. 276:765-770(1991). RN [35] RP VARIANT OI3 CYS-349, AND VARIANT OI1 CYS-736. RX PubMed=1990009; RA Wenstrup R.J., Shrago-Howe A.W., Lever L.W., Phillips C.L., RA Byers P.H., Cohn D.H.; RT "The effects of different cysteine for glycine substitutions within RT alpha 2(I) chains. Evidence of distinct structural domains within the RT type I collagen triple helix."; RL J. Biol. Chem. 266:2590-2594(1991). RN [36] RP VARIANT OI2 ARG-784. RX PubMed=1874719; RA Tsuneyoshi T., Westerhausen A., Constantinou C.D., Prockop D.J.; RT "Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type RT I procollagen in lethal osteogenesis imperfecta. The conformational RT strain on the triple helix introduced by a glycine substitution can be RT transmitted along the helix."; RL J. Biol. Chem. 266:15608-15613(1991). RN [37] RP VARIANT OI4 SER-751. RX PubMed=2052622; DOI=10.1073/pnas.88.12.5423; RA Spotila L.D., Constantinou C.D., Sereda L., Ganguly A., Riggs B.L., RA Prockop D.J.; RT "Mutation in a gene for type I procollagen (COL1A2) in a woman with RT postmenopausal osteoporosis: evidence for phenotypic and genotypic RT overlap with mild osteogenesis imperfecta."; RL Proc. Natl. Acad. Sci. U.S.A. 88:5423-5427(1991). RN [38] RP VARIANT OI2 ARG-547. RX PubMed=1284475; DOI=10.1002/humu.1380010109; RA Bateman J.F., Moeller I., Hannagan M., Chan D., Cole W.G.; RT "Lethal perinatal osteogenesis imperfecta due to a type I collagen RT alpha 2(I) Gly to Arg substitution detected by chemical cleavage of an RT mRNA:cDNA sequence mismatch."; RL Hum. Mutat. 1:55-62(1992). RN [39] RP VARIANT OI2 ASP-670. RX PubMed=1385413; RA Niyibizi C., Bonadio J., Byers P.H., Eyre D.R.; RT "Incorporation of type I collagen molecules that contain a mutant RT alpha 2(I) chain (Gly580-->Asp) into bone matrix in a lethal case of RT osteogenesis imperfecta."; RL J. Biol. Chem. 267:23108-23112(1992). RN [40] RP VARIANT OI3 CYS-349, AND VARIANT OI1 CYS-736. RX PubMed=8456807; DOI=10.1002/ajmg.1320450215; RA Wenstrup R.J., Lever L.W., Phillips C.L., Quarles L.D.; RT "Mutations in the COL1A2 gene of type I collagen that result in RT nonlethal forms of osteogenesis imperfecta."; RL Am. J. Med. Genet. 45:228-232(1993). RN [41] RP VARIANT ALA-549. RX PubMed=8456808; DOI=10.1002/ajmg.1320450216; RA Bateman J.F., Lamande S.R., Hannagan M., Moeller I., Dahl H.-H.M., RA Cole W.G.; RT "Chemical cleavage method for the detection of RNA base changes: RT experience in the application to collagen mutations in osteogenesis RT imperfecta."; RL Am. J. Med. Genet. 45:233-240(1993). RN [42] RP VARIANT OI3 VAL-345 DEL. RX PubMed=8444468; DOI=10.1007/BF00202479; RA Molyneux K., Starman B.J., Byers P.H., Dalgleish R.; RT "A single amino acid deletion in the alpha 2(I) chain of type I RT collagen produces osteogenesis imperfecta type III."; RL Hum. Genet. 90:621-628(1993). RN [43] RP VARIANT OI4 VAL-634. RX PubMed=8401517; DOI=10.1093/hmg/2.8.1319; RA Sztrolovics R., Glorieux F.H., van der Rest M., Roughley P.J.; RT "Identification of type I collagen gene (COL1A2) mutations in RT nonlethal osteogenesis imperfecta."; RL Hum. Mol. Genet. 2:1319-1321(1993). RN [44] RP VARIANT OI2 GLU-433. RX PubMed=7906591; DOI=10.1093/hmg/2.12.2175; RA Rose N.J., Mackay K., Byers P.H., Dalgleish R.; RT "A novel glycine to glutamic acid substitution at position 343 in the RT alpha 2 chain of type I collagen in an individual with lethal RT osteogenesis imperfecta."; RL Hum. Mol. Genet. 2:2175-2177(1993). RN [45] RP VARIANT OI4 SER-1012. RX PubMed=8094076; RA Marini J.C., Lewis M.B., Wang Q., Chen K.J., Orrison B.M.; RT "Serine for glycine substitutions in type I collagen in two cases of RT type IV osteogenesis imperfecta (OI). Additional evidence for a RT regional model of OI pathophysiology."; RL J. Biol. Chem. 268:2667-2673(1993). RN [46] RP VARIANT OI4 VAL-766, AND VARIANT OI2 SER-796. RX PubMed=7693712; RA Wang Q., Orrison B.M., Marini J.C.; RT "Two additional cases of osteogenesis imperfecta with substitutions RT for glycine in the alpha 2(I) collagen chain. A regional model RT relating mutation location with phenotype."; RL J. Biol. Chem. 268:25162-25167(1993). RN [47] RP VARIANT OI3 ARG-517. RX PubMed=7520724; DOI=10.1016/8756-3282(94)90295-X; RA Sztrolovics R., Glorieux F.H., Travers R., van der Rest M., RA Roughley P.J.; RT "Osteogenesis imperfecta: comparison of molecular defects with bone RT histological changes."; RL Bone 15:321-328(1994). RN [48] RP VARIANT OI2 SER-592. RX PubMed=7959683; DOI=10.1007/BF00211014; RA Rose N.J., Mackay K., de Paepe A., Steinmann B., Punnett H.H., RA Dalgleish R.; RT "Three unrelated individuals with perinatally lethal osteogenesis RT imperfecta resulting from identical Gly502Ser substitutions in the RT alpha 2-chain of type I collagen."; RL Hum. Genet. 94:497-503(1994). RN [49] RP VARIANT OI3 SER-949. RX PubMed=8081394; DOI=10.1002/humu.1380030411; RA Rose N.J., Mackay K., Byers P.H., Dalgleish R.; RT "A Gly859Ser substitution in the triple helical domain of the alpha 2 RT chain of type I collagen resulting in osteogenesis imperfecta type III RT in two unrelated individuals."; RL Hum. Mutat. 3:391-394(1994). RN [50] RP VARIANT OI2 ASP-790. RX PubMed=8182080; RA Cohen-Solal L., Zylberberg L., Sangalli A., Gomez Lira M., Mottes M.; RT "Substitution of an aspartic acid for glycine 700 in the alpha 2(I) RT chain of type I collagen in a recurrent lethal type II osteogenesis RT imperfecta dramatically affects the mineralization of bone."; RL J. Biol. Chem. 269:14751-14758(1994). RN [51] RP VARIANT OI2 CYS-730. RX PubMed=7891382; DOI=10.1136/jmg.31.12.965; RA Gomez Lira M., Sangalli A., Pignatti P.F., Digilio M.C., Giannotti A., RA Carnevale E., Mottes M.; RT "Determination of a new collagen type I alpha 2 gene point mutation RT which causes a Gly640 Cys substitution in osteogenesis imperfecta and RT prenatal diagnosis by DNA hybridisation."; RL J. Med. Genet. 31:965-968(1994). RN [52] RP VARIANT OI3 SER-778. RX PubMed=7720740; DOI=10.1007/BF01991915; RA Raghunath M., Mackay K., Dalgleish R., Steinmann B.; RT "Genetic counselling on brittle grounds: recurring osteogenesis RT imperfecta due to parental mosaicism for a dominant mutation."; RL Eur. J. Pediatr. 154:123-129(1995). RN [53] RP VARIANT OI3 SER-328. RX PubMed=7860070; DOI=10.1007/BF00209405; RA Rose N.J., Mackay K., Byers P.H., Dalgleish R.; RT "A Gly238Ser substitution in the alpha 2 chain of type I collagen RT results in osteogenesis imperfecta type III."; RL Hum. Genet. 95:215-218(1995). RN [54] RP VARIANT OI3 ALA-1096. RX PubMed=7749416; DOI=10.1002/humu.1380050212; RA Lu J., Costa T., Cole W.G.; RT "A novel G1006A substitution in the alpha 2(I) chain of type I RT collagen produces osteogenesis imperfecta type III."; RL Hum. Mutat. 5:175-178(1995). RN [55] RP VARIANT OI3 ASP-892, AND VARIANT OI4 ASP-892. RX PubMed=8800927; RA Lund A.M., Schwartz M., Raghunath M., Steinmann B., Skovby F.; RT "Gly802Asp substitution in the pro alpha 2(I) collagen chain in a RT family with recurrent osteogenesis imperfecta due to paternal RT mosaicism."; RL Eur. J. Hum. Genet. 4:39-45(1996). RN [56] RP VARIANTS OI1 ASP-211 AND SER-835, VARIANTS OI3 SER-337 AND SER-460, RP AND VARIANT HIS-822. RX PubMed=8829649; RX DOI=10.1002/(SICI)1098-1004(1996)7:2<89::AID-HUMU1>3.0.CO;2-K; RA Zhuang J., Tromp G., Kuivaniemi H., Castells S., Bugge M., RA Prockop D.J.; RT "Direct sequencing of PCR products derived from cDNAs for the pro RT alpha 1 and pro alpha 2 chains of type I procollagen as a screening RT method to detect mutations in patients with osteogenesis imperfecta."; RL Hum. Mutat. 7:89-99(1996). RN [57] RP VARIANT OI3 PRO-1148. RX PubMed=8723681; RX DOI=10.1002/(SICI)1098-1004(1996)7:4<318::AID-HUMU5>3.0.CO;2-4; RA Oliver J.E., Thompson E.M., Pope F.M., Nicholls A.C.; RT "Mutation in the carboxy-terminal propeptide of the Pro alpha 1(I) RT chain of type I collagen in a child with severe osteogenesis RT imperfecta (OI type III): possible implications for protein folding."; RL Hum. Mutat. 7:318-326(1996). RN [58] RP VARIANTS OI2 VAL-409 AND CYS-787. RX PubMed=10627137; RX DOI=10.1002/(SICI)1098-1004(1998)12:1<71::AID-HUMU16>3.0.CO;2-4; RA Mottes M., Gomez Lira M., Zolezzi F., Valli M., Lisi V., Freising P.; RT "Four new cases of lethal osteogenesis imperfecta due to glycine RT substitutions in COL1A1 and genes."; RL Hum. Mutat. 12:71-72(1998). RN [59] RP VARIANTS OI3 ASP-331; CYS-337 AND VAL-973. RX PubMed=10408781; RX DOI=10.1002/(SICI)1098-1004(1999)13:6<503::AID-HUMU11>3.0.CO;2-L; RA Lund A.M., Astroem E., Soederhaell S., Schwartz M., Skovby F.; RT "Osteogenesis imperfecta: mosaicism and refinement of the genotype- RT phenotype map in OI type III."; RL Hum. Mutat. 13:503-503(1999). RN [60] RP CHROMOSOMAL REARRANGEMENT WITH PLAG1. RX PubMed=10987300; RA Hibbard M.K., Kozakewich H.P., Dal Cin P., Sciot R., Tan X., Xiao S., RA Fletcher J.A.; RT "PLAG1 fusion oncogenes in lipoblastoma."; RL Cancer Res. 60:4869-4872(2000). RN [61] RP INVOLVEMENT IN CARDIAC VALVULAR EDS. RX PubMed=15077201; DOI=10.1086/420794; RA Schwarze U., Hata R., McKusick V.A., Shinkai H., Hoyme H.E., RA Pyeritz R.E., Byers P.H.; RT "Rare autosomal recessive cardiac valvular form of Ehlers-Danlos RT syndrome results from mutations in the COL1A2 gene that activate the RT nonsense-mediated RNA decay pathway."; RL Am. J. Hum. Genet. 74:917-930(2004). RN [62] RP INVOLVEMENT IN EDSCV. RX PubMed=16816023; DOI=10.1136/jmg.2005.038224; RA Malfait F., Symoens S., Coucke P., Nunes L., De Almeida S., RA De Paepe A.; RT "Total absence of the alpha2(I) chain of collagen type I causes a rare RT form of Ehlers-Danlos syndrome with hypermobility and propensity to RT cardiac valvular problems."; RL J. Med. Genet. 43:E36-E36(2006). RN [63] RP VARIANTS OI4 SER-193 AND CYS-754, VARIANT OI2 ASP-625, AND VARIANTS RP OI3 CYS-835 AND VAL-991. RX PubMed=16879195; DOI=10.1111/j.1399-0004.2006.00646.x; RA Venturi G., Tedeschi E., Mottes M., Valli M., Camilot M., Viglio S., RA Antoniazzi F., Tato L.; RT "Osteogenesis imperfecta: clinical, biochemical and molecular RT findings."; RL Clin. Genet. 70:131-139(2006). RN [64] RP VARIANTS OI1/OI3/OI4 GLU-325; SER-328; SER-358; SER-601; ASP-676; RP SER-820; ARG-856; SER-1012; PRO-PRO-GLY-811 INS; VAL-GLY-PRO-989 INS RP AND 1094-PRO--GLY-1096 DEL. RX PubMed=16705691; DOI=10.1002/humu.9423; RA Lee K.S., Song H.R., Cho T.J., Kim H.J., Lee T.M., Jin H.S., RA Park H.Y., Kang S., Jung S.C., Koo S.K.; RT "Mutational spectrum of type I collagen genes in Korean patients with RT osteogenesis imperfecta."; RL Hum. Mutat. 27:599-599(2006). RN [65] RP VARIANTS OI4 ARG-202 AND VAL-256, VARIANTS OI1 ARG-247; ARG-319; RP CYS-733 AND TYR-1195, VARIANTS OI2 ASP-253; ASP-982 AND ASP-1003, AND RP VARIANT OI3 ASP-1087. RX PubMed=16786509; DOI=10.1002/humu.9430; RA Pollitt R., McMahon R., Nunn J., Bamford R., Afifi A., Bishop N., RA Dalton A.; RT "Mutation analysis of COL1A1 and COL1A2 in patients diagnosed with RT osteogenesis imperfecta type I-IV."; RL Hum. Mutat. 27:716-716(2006). RN [66] RP VARIANTS SER-528; ALA-549 AND THR-564. RX PubMed=18272325; DOI=10.1016/j.ygeno.2007.12.008; RA Chan T.F., Poon A., Basu A., Addleman N.R., Chen J., Phong A., RA Byers P.H., Klein T.E., Kwok P.Y.; RT "Natural variation in four human collagen genes across an ethnically RT diverse population."; RL Genomics 91:307-314(2008). RN [67] RP VARIANTS OI2 CYS-234; ARG-283; GLU-397; CYS-454; LEU-457; RP 461-PRO--GLY-466 DEL; GLU-526; VAL-562; 705-ALA--PRO-707 DEL; ARG-739; RP VAL-748; ASP-790; PRO-798 INS; 806-PRO--GLY-811 DEL; VAL-856; SER-949; RP ASP-955; GLU-1027 AND 1058-PRO--ALA-1062 DEL, AND VARIANT ALA-549. RX PubMed=18996919; DOI=10.1093/hmg/ddn374; RA Bodian D.L., Chan T.F., Poon A., Schwarze U., Yang K., Byers P.H., RA Kwok P.Y., Klein T.E.; RT "Mutation and polymorphism spectrum in osteogenesis imperfecta type RT II: implications for genotype-phenotype relationships."; RL Hum. Mol. Genet. 18:463-471(2009). RN [68] RP VARIANT THR-1119, AND CHARACTERIZATION OF VARIANT THR-1119. RX PubMed=21344539; DOI=10.1002/humu.21475; RA Lindahl K., Barnes A.M., Fratzl-Zelman N., Whyte M.P., Hefferan T.E., RA Makareeva E., Brusel M., Yaszemski M.J., Rubin C.J., Kindmark A., RA Roschger P., Klaushofer K., McAlister W.H., Mumm S., Leikin S., RA Kessler E., Boskey A.L., Ljunggren O., Marini J.C.; RT "COL1 C-propeptide cleavage site mutations cause high bone mass RT osteogenesis imperfecta."; RL Hum. Mutat. 32:598-609(2011). RN [69] RP VARIANT HIS-1067. RX PubMed=23656646; DOI=10.1056/NEJMoa1215458; RA Laine C.M., Joeng K.S., Campeau P.M., Kiviranta R., Tarkkonen K., RA Grover M., Lu J.T., Pekkinen M., Wessman M., Heino T.J., RA Nieminen-Pihala V., Aronen M., Laine T., Kroeger H., Cole W.G., RA Lehesjoki A.E., Nevarez L., Krakow D., Curry C.J., Cohn D.H., RA Gibbs R.A., Lee B.H., Maekitie O.; RT "WNT1 mutations in early-onset osteoporosis and osteogenesis RT imperfecta."; RL N. Engl. J. Med. 368:1809-1816(2013). CC -!- FUNCTION: Type I collagen is a member of group I collagen CC (fibrillar forming collagen). CC -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains. CC -!- INTERACTION: CC O43765:SGTA; NbExp=3; IntAct=EBI-983038, EBI-347996; CC Q9UMX0:UBQLN1; NbExp=3; IntAct=EBI-983038, EBI-741480; CC Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-983038, EBI-10173939; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and CC bones. In bones the fibrils are mineralized with calcium CC hydroxyapatite. CC -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, CC have crucial roles in tissue growth and repair by controlling both CC the intracellular assembly of procollagen molecules and the CC extracellular assembly of collagen fibrils. It binds a calcium ion CC which is essential for its function (By similarity). CC {ECO:0000250}. CC -!- PTM: Prolines at the third position of the tripeptide repeating CC unit (G-X-Y) are hydroxylated in some or all of the chains. CC {ECO:0000269|PubMed:4412529}. CC -!- DISEASE: Ehlers-Danlos syndrome 7B (EDS7B) [MIM:130060]: A CC connective tissue disorder characterized by hyperextensible skin, CC atrophic cutaneous scars due to tissue fragility and joint CC hyperlaxity. Marked by bilateral congenital hip dislocation, CC hyperlaxity of the joints, and recurrent partial dislocations. CC {ECO:0000269|PubMed:1577745, ECO:0000269|PubMed:2394758, CC ECO:0000269|PubMed:3680255}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Osteogenesis imperfecta 1 (OI1) [MIM:166200]: An CC autosomal dominant form of osteogenesis imperfecta, a connective CC tissue disorder characterized by low bone mass, bone fragility and CC susceptibility to fractures after minimal trauma. Disease severity CC ranges from very mild forms without fractures to intrauterine CC fractures and perinatal lethality. Extraskeletal manifestations, CC which affect a variable number of patients, are dentinogenesis CC imperfecta, hearing loss, and blue sclerae. OI1 is a non-deforming CC form with normal height or mild short stature, and no CC dentinogenesis imperfecta. {ECO:0000269|PubMed:16705691, CC ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:1990009, CC ECO:0000269|PubMed:8456807, ECO:0000269|PubMed:8829649}. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- DISEASE: Osteogenesis imperfecta 2 (OI2) [MIM:166210]: An CC autosomal dominant form of osteogenesis imperfecta, a connective CC tissue disorder characterized by low bone mass, bone fragility and CC susceptibility to fractures after minimal trauma. Disease severity CC ranges from very mild forms without fractures to intrauterine CC fractures and perinatal lethality. Extraskeletal manifestations, CC which affect a variable number of patients, are dentinogenesis CC imperfecta, hearing loss, and blue sclerae. OI2 is characterized CC by bone fragility, with many perinatal fractures, severe bowing of CC long bones, undermineralization, and death in the perinatal period CC due to respiratory insufficiency. {ECO:0000269|PubMed:10627137, CC ECO:0000269|PubMed:1284475, ECO:0000269|PubMed:1339453, CC ECO:0000269|PubMed:1385413, ECO:0000269|PubMed:16786509, CC ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:1874719, CC ECO:0000269|PubMed:18996919, ECO:0000269|PubMed:2777764, CC ECO:0000269|PubMed:2914942, ECO:0000269|PubMed:7693712, CC ECO:0000269|PubMed:7891382, ECO:0000269|PubMed:7906591, CC ECO:0000269|PubMed:7959683, ECO:0000269|PubMed:8182080, CC ECO:0000269|Ref.33}. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC -!- DISEASE: Ehlers-Danlos syndrome, autosomal recessive, cardiac CC valvular form (EDSCV) [MIM:225320]: A connective tissue disorder CC characterized by hyperextensible skin, atrophic cutaneous scars CC due to tissue fragility and joint hyperlaxity. In addition to CC joint laxity, skin hyperextensibility and friability, and abnormal CC scar formation, patients have mitral valve prolapse and CC insufficiency, mitral regurgitation, and aortic insufficiency. CC {ECO:0000269|PubMed:16816023}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Osteogenesis imperfecta 3 (OI3) [MIM:259420]: An CC autosomal dominant form of osteogenesis imperfecta, a connective CC tissue disorder characterized by low bone mass, bone fragility and CC susceptibility to fractures after minimal trauma. Disease severity CC ranges from very mild forms without fractures to intrauterine CC fractures and perinatal lethality. Extraskeletal manifestations, CC which affect a variable number of patients, are dentinogenesis CC imperfecta, hearing loss, and blue sclerae. OI3 is characterized CC by progressively deforming bones, very short stature, a triangular CC face, severe scoliosis, grayish sclera and dentinogenesis CC imperfecta. {ECO:0000269|PubMed:10408781, CC ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:16879195, CC ECO:0000269|PubMed:1990009, ECO:0000269|PubMed:7520724, CC ECO:0000269|PubMed:7720740, ECO:0000269|PubMed:7749416, CC ECO:0000269|PubMed:7860070, ECO:0000269|PubMed:7881420, CC ECO:0000269|PubMed:8081394, ECO:0000269|PubMed:8444468, CC ECO:0000269|PubMed:8456807, ECO:0000269|PubMed:8723681, CC ECO:0000269|PubMed:8800927, ECO:0000269|PubMed:8829649}. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- DISEASE: Osteogenesis imperfecta 4 (OI4) [MIM:166220]: An CC autosomal dominant form of osteogenesis imperfecta, a connective CC tissue disorder characterized by low bone mass, bone fragility and CC susceptibility to fractures after minimal trauma. Disease severity CC ranges from very mild forms without fractures to intrauterine CC fractures and perinatal lethality. Extraskeletal manifestations, CC which affect a variable number of patients, are dentinogenesis CC imperfecta, hearing loss, and blue sclerae. OI4 is characterized CC by moderately short stature, mild to moderate scoliosis, grayish CC or white sclera and dentinogenesis imperfecta. CC {ECO:0000269|PubMed:1642148, ECO:0000269|PubMed:16786509, CC ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:2052622, CC ECO:0000269|PubMed:2064612, ECO:0000269|PubMed:2897363, CC ECO:0000269|PubMed:7693712, ECO:0000269|PubMed:8094076, CC ECO:0000269|PubMed:8401517, ECO:0000269|PubMed:8800927}. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- DISEASE: Note=A chromosomal aberration involving COL1A2 may be a CC cause of lipoblastomas, which are benign tumors resulting from CC transformation of adipocytes, usually diagnosed in children. CC Translocation t(7;8)(p22;q13) with PLAG1. CC -!- SIMILARITY: Belongs to the fibrillar collagen family. CC {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- SIMILARITY: Contains 1 fibrillar collagen NC1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/COL1A2ID411ch7q22.html"; CC -!- WEB RESOURCE: Name=Osteogenesis imperfecta variant database; CC Note=Collagen type I alpha 2 (COL1A2); CC URL="http://oi.gene.le.ac.uk/home.php?select_db=COL1A2"; 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; J03464; AAB59374.1; -; mRNA. DR EMBL; Z74616; CAA98969.1; -; mRNA. DR EMBL; AF004877; AAB93981.1; -; Genomic_DNA. DR EMBL; BC042586; AAH42586.1; -; mRNA. DR EMBL; BC054498; AAH54498.1; -; mRNA. DR EMBL; Y00724; CAA68709.1; -; mRNA. DR EMBL; X02488; CAA26320.1; -; mRNA. DR EMBL; AB004317; BAA25383.1; -; Genomic_DNA. DR EMBL; M35391; AAA60041.1; -; Genomic_DNA. DR EMBL; S98904; AAB22126.1; -; Genomic_DNA. DR EMBL; M21671; AAA59994.1; -; Genomic_DNA. DR EMBL; S41099; AAB22761.1; -; mRNA. DR EMBL; AC002528; AAB69977.1; -; Genomic_DNA. DR EMBL; M21353; AAA52053.1; -; Genomic_DNA. DR EMBL; M28985; AAA60356.1; -; Genomic_DNA. DR EMBL; V00503; CAA23761.1; -; mRNA. DR EMBL; S96821; AAB22020.2; -; mRNA. DR EMBL; L47668; AAB59577.1; -; mRNA. DR EMBL; X55525; CAA39142.1; -; mRNA. DR EMBL; J00114; AAA51996.1; -; mRNA. DR EMBL; M22816; AAA51844.1; -; mRNA. DR EMBL; M22817; AAA51846.1; -; Genomic_DNA. DR EMBL; K01078; AAA51887.1; -; Genomic_DNA. DR EMBL; K02568; AAA51850.1; -; Genomic_DNA. DR CCDS; CCDS34682.1; -. DR PIR; A28500; CGHU2S. DR RefSeq; NP_000080.2; NM_000089.3. DR UniGene; Hs.489142; -. DR ProteinModelPortal; P08123; -. DR SMR; P08123; 1151-1365. DR BioGrid; 107675; 13. DR DIP; DIP-36079N; -. DR IntAct; P08123; 15. DR MINT; MINT-4791958; -. DR STRING; 9606.ENSP00000297268; -. DR ChEMBL; CHEMBL2364188; -. DR DrugBank; DB00048; Collagenase clostridium histolyticum. DR PhosphoSite; P08123; -. DR BioMuta; COL1A2; -. DR DMDM; 296439507; -. DR MaxQB; P08123; -. DR PaxDb; P08123; -. DR PRIDE; P08123; -. DR Ensembl; ENST00000297268; ENSP00000297268; ENSG00000164692. DR GeneID; 1278; -. DR KEGG; hsa:1278; -. DR UCSC; uc003ung.1; human. DR CTD; 1278; -. DR GeneCards; COL1A2; -. DR GeneReviews; COL1A2; -. DR H-InvDB; HIX0006854; -. DR HGNC; HGNC:2198; COL1A2. DR HPA; CAB032650; -. DR MalaCards; COL1A2; -. DR MIM; 120160; gene. DR MIM; 130060; phenotype. DR MIM; 166200; phenotype. DR MIM; 166210; phenotype. DR MIM; 166220; phenotype. DR MIM; 225320; phenotype. DR MIM; 259420; phenotype. DR neXtProt; NX_P08123; -. DR Orphanet; 99876; Ehlers-Danlos syndrome type 7B. DR Orphanet; 230851; Ehlers-Danlos syndrome, cardiac valvular type. DR Orphanet; 230857; Ehlers-Danlos/osteogenesis imperfecta syndrome. DR Orphanet; 314029; High bone mass osteogenesis imperfecta. DR Orphanet; 216796; Osteogenesis imperfecta type 1. DR Orphanet; 216804; Osteogenesis imperfecta type 2. DR Orphanet; 216812; Osteogenesis imperfecta type 3. DR Orphanet; 216820; Osteogenesis imperfecta type 4. DR PharmGKB; PA35042; -. DR eggNOG; KOG3544; Eukaryota. DR eggNOG; ENOG410XNMM; LUCA. DR GeneTree; ENSGT00820000126960; -. DR HOVERGEN; HBG004933; -. DR InParanoid; P08123; -. DR KO; K06236; -. DR OMA; PTGKHGN; -. DR OrthoDB; EOG7TJ3HH; -. DR PhylomeDB; P08123; -. DR TreeFam; TF344135; -. DR Reactome; R-HSA-114604; GPVI-mediated activation cascade. DR Reactome; R-HSA-1442490; Collagen degradation. DR Reactome; R-HSA-1474244; Extracellular matrix organization. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-2214320; Anchoring fibril formation. DR Reactome; R-HSA-2243919; Crosslinking of collagen fibrils. DR Reactome; R-HSA-3000170; Syndecan interactions. DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors. DR Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen. DR ChiTaRS; COL1A2; human. DR GeneWiki; COL1A2; -. DR GenomeRNAi; 1278; -. DR NextBio; 5165; -. DR PRO; PR:P08123; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; P08123; -. DR ExpressionAtlas; P08123; baseline and differential. DR Genevisible; P08123; HS. DR GO; GO:0005584; C:collagen type I trimer; IDA:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005201; F:extracellular matrix structural constituent; NAS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0048407; F:platelet-derived growth factor binding; IDA:MGI. DR GO; GO:0030674; F:protein binding, bridging; IMP:UniProtKB. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0001568; P:blood vessel development; IMP:UniProtKB. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl. DR GO; GO:0030574; P:collagen catabolic process; TAS:Reactome. DR GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB. DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. DR GO; GO:0042476; P:odontogenesis; NAS:UniProtKB. DR GO; GO:0030168; P:platelet activation; TAS:Reactome. DR GO; GO:0070208; P:protein heterotrimerization; IEA:Ensembl. DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome. DR GO; GO:0008217; P:regulation of blood pressure; IMP:UniProtKB. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB. DR GO; GO:0001501; P:skeletal system development; IMP:UniProtKB. DR GO; GO:0043589; P:skin morphogenesis; IMP:UniProtKB. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB. DR InterPro; IPR008160; Collagen. DR InterPro; IPR000885; Fib_collagen_C. DR Pfam; PF01410; COLFI; 1. DR Pfam; PF01391; Collagen; 6. DR ProDom; PD002078; Fib_collagen_C; 1. DR SMART; SM00038; COLFI; 1. DR PROSITE; PS51461; NC1_FIB; 1. PE 1: Evidence at protein level; KW Calcium; Chromosomal rearrangement; Collagen; Complete proteome; KW Direct protein sequencing; Disease mutation; Disulfide bond; Dwarfism; KW Ehlers-Danlos syndrome; Extracellular matrix; Glycoprotein; KW Hydroxylation; Metal-binding; Osteogenesis imperfecta; Polymorphism; KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; KW Signal. FT SIGNAL 1 24 {ECO:0000255}. FT PROPEP 25 79 N-terminal propeptide. FT {ECO:0000269|PubMed:5529814}. FT /FTId=PRO_0000005804. FT CHAIN 80 1102 Collagen alpha-2(I) chain. FT /FTId=PRO_0000005805. FT PROPEP 1103 1366 C-terminal propeptide. FT /FTId=PRO_0000005806. FT DOMAIN 1133 1366 Fibrillar collagen NC1. FT {ECO:0000255|PROSITE-ProRule:PRU00793}. FT METAL 1181 1181 Calcium. {ECO:0000250}. FT METAL 1183 1183 Calcium. {ECO:0000250}. FT METAL 1184 1184 Calcium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 1186 1186 Calcium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 1189 1189 Calcium. {ECO:0000250}. FT MOD_RES 80 80 Pyrrolidone carboxylic acid. FT {ECO:0000250|UniProtKB:P02465}. FT MOD_RES 84 84 Allysine. FT MOD_RES 420 420 Hydroxyproline. FT {ECO:0000269|PubMed:4412529}. FT MOD_RES 441 441 Hydroxyproline. FT {ECO:0000269|PubMed:4412529}. FT MOD_RES 444 444 Hydroxyproline. FT {ECO:0000269|PubMed:4412529}. FT CARBOHYD 1267 1267 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 1163 1195 {ECO:0000255|PROSITE-ProRule:PRU00793}. FT DISULFID 1203 1364 {ECO:0000255|PROSITE-ProRule:PRU00793}. FT DISULFID 1272 1317 {ECO:0000255|PROSITE-ProRule:PRU00793}. FT VARIANT 59 59 T -> P (in dbSNP:rs1800221). FT {ECO:0000269|PubMed:4011429}. FT /FTId=VAR_030116. FT VARIANT 76 93 Missing (in EDS7B). FT {ECO:0000269|PubMed:1577745, FT ECO:0000269|PubMed:2394758, FT ECO:0000269|PubMed:3680255}. FT /FTId=VAR_001851. FT VARIANT 181 198 Missing (in OI4). FT {ECO:0000269|PubMed:1642148}. FT /FTId=VAR_030117. FT VARIANT 193 193 G -> S (in OI4). FT {ECO:0000269|PubMed:16879195}. FT /FTId=VAR_063343. FT VARIANT 202 202 G -> R (in OI4). FT {ECO:0000269|PubMed:16786509}. FT /FTId=VAR_063344. FT VARIANT 211 211 G -> D (in OI1). FT {ECO:0000269|PubMed:8829649}. FT /FTId=VAR_001852. FT VARIANT 234 234 R -> C (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063345. FT VARIANT 247 247 G -> R (in OI1). FT {ECO:0000269|PubMed:16786509}. FT /FTId=VAR_063346. FT VARIANT 249 249 I -> N (in dbSNP:rs1800228). FT {ECO:0000269|PubMed:2824475}. FT /FTId=VAR_001853. FT VARIANT 253 253 G -> D (in OI2). FT {ECO:0000269|PubMed:16786509}. FT /FTId=VAR_063347. FT VARIANT 256 256 G -> V (in OI4). FT {ECO:0000269|PubMed:16786509}. FT /FTId=VAR_063348. FT VARIANT 270 270 V -> I (in dbSNP:rs368468). FT {ECO:0000269|PubMed:9443882}. FT /FTId=VAR_030118. FT VARIANT 276 276 A -> T (in dbSNP:rs1800231). FT {ECO:0000269|PubMed:2824475}. FT /FTId=VAR_001854. FT VARIANT 283 283 G -> R (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063349. FT VARIANT 319 319 G -> R (in OI1). FT {ECO:0000269|PubMed:16786509}. FT /FTId=VAR_063350. FT VARIANT 325 325 G -> E (in OI4). FT {ECO:0000269|PubMed:16705691}. FT /FTId=VAR_063351. FT VARIANT 328 328 G -> S (in OI1, OI3 AND OI4). FT {ECO:0000269|PubMed:16705691, FT ECO:0000269|PubMed:7860070}. FT /FTId=VAR_001855. FT VARIANT 331 331 G -> D (in OI3). FT {ECO:0000269|PubMed:10408781}. FT /FTId=VAR_008119. FT VARIANT 334 334 G -> C (in OI2). FT /FTId=VAR_001856. FT VARIANT 337 337 G -> C (in OI3). FT {ECO:0000269|PubMed:10408781}. FT /FTId=VAR_001857. FT VARIANT 337 337 G -> S (in OI3). FT {ECO:0000269|PubMed:8829649}. FT /FTId=VAR_001858. FT VARIANT 344 344 L -> V (in dbSNP:rs16868573). FT /FTId=VAR_055677. FT VARIANT 345 345 Missing (in OI3). FT {ECO:0000269|PubMed:8444468}. FT /FTId=VAR_001859. FT VARIANT 349 349 G -> C (in OI3). FT {ECO:0000269|PubMed:1990009, FT ECO:0000269|PubMed:8456807}. FT /FTId=VAR_001860. FT VARIANT 358 358 G -> S (in OI3). FT {ECO:0000269|PubMed:16705691}. FT /FTId=VAR_063352. FT VARIANT 397 397 G -> E (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063353. FT VARIANT 409 409 G -> V (in OI2). FT {ECO:0000269|PubMed:10627137}. FT /FTId=VAR_001861. FT VARIANT 433 433 G -> E (in OI2). FT {ECO:0000269|PubMed:7906591}. FT /FTId=VAR_001862. FT VARIANT 454 454 G -> C (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063354. FT VARIANT 457 457 G -> L (in OI2; requires 2 nucleotide FT substitutions). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063355. FT VARIANT 460 460 G -> S (in OI3). FT {ECO:0000269|PubMed:8829649}. FT /FTId=VAR_001863. FT VARIANT 461 466 Missing (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063356. FT VARIANT 483 483 A -> V (in dbSNP:rs414408). FT {ECO:0000269|PubMed:2824475, FT ECO:0000269|PubMed:9443882}. FT /FTId=VAR_030119. FT VARIANT 511 511 G -> D (in OI2). FT /FTId=VAR_001864. FT VARIANT 517 517 G -> R (in OI3). FT {ECO:0000269|PubMed:7520724}. FT /FTId=VAR_001865. FT VARIANT 526 526 G -> E (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063357. FT VARIANT 528 528 N -> S (in dbSNP:rs41317144). FT {ECO:0000269|PubMed:18272325}. FT /FTId=VAR_033040. FT VARIANT 547 547 G -> R (in OI2). FT {ECO:0000269|PubMed:1284475}. FT /FTId=VAR_001866. FT VARIANT 549 549 P -> A (in dbSNP:rs42524). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:18272325, FT ECO:0000269|PubMed:18996919, FT ECO:0000269|PubMed:2824475, FT ECO:0000269|PubMed:2839839, FT ECO:0000269|PubMed:8456808, FT ECO:0000269|PubMed:9016532}. FT /FTId=VAR_001867. FT VARIANT 562 562 G -> C (in OI2). FT /FTId=VAR_001868. FT VARIANT 562 562 G -> V (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063358. FT VARIANT 564 564 A -> T (in dbSNP:rs41317153). FT {ECO:0000269|PubMed:18272325}. FT /FTId=VAR_033041. FT VARIANT 586 586 G -> R (in OI2). FT /FTId=VAR_001869. FT VARIANT 592 592 G -> S (in OI2). FT {ECO:0000269|PubMed:7959683}. FT /FTId=VAR_001870. FT VARIANT 601 601 G -> S (in OI). FT {ECO:0000269|PubMed:16705691}. FT /FTId=VAR_063359. FT VARIANT 625 625 G -> D (in OI2). FT {ECO:0000269|PubMed:16879195}. FT /FTId=VAR_063360. FT VARIANT 634 634 G -> V (in OI4). FT {ECO:0000269|PubMed:8401517}. FT /FTId=VAR_001871. FT VARIANT 637 637 G -> D (in OI2). FT /FTId=VAR_001872. FT VARIANT 640 640 G -> S (in OI2). FT /FTId=VAR_001873. FT VARIANT 670 670 G -> D (in OI2). FT {ECO:0000269|PubMed:1385413}. FT /FTId=VAR_001874. FT VARIANT 676 855 Missing (in OI2). FT {ECO:0000269|PubMed:1339453}. FT /FTId=VAR_030120. FT VARIANT 676 676 G -> D (in OI3). FT {ECO:0000269|PubMed:16705691}. FT /FTId=VAR_063361. FT VARIANT 676 676 G -> V (in OI3 and OI4). FT {ECO:0000269|PubMed:2064612, FT ECO:0000269|PubMed:7881420}. FT /FTId=VAR_001875. FT VARIANT 678 678 P -> H (in dbSNP:rs409108). FT {ECO:0000269|PubMed:2824475, FT ECO:0000269|PubMed:3421913, FT ECO:0000269|PubMed:6687691, FT ECO:0000269|PubMed:9016532, FT ECO:0000269|PubMed:9443882}. FT /FTId=VAR_030121. FT VARIANT 705 707 Missing (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063362. FT VARIANT 708 708 R -> Q (in Marfan syndrome). FT /FTId=VAR_001876. FT VARIANT 715 715 G -> D (in OI2). FT /FTId=VAR_001877. FT VARIANT 730 730 G -> C (in OI2). FT {ECO:0000269|PubMed:7891382}. FT /FTId=VAR_001878. FT VARIANT 733 733 G -> C (in OI1). FT {ECO:0000269|PubMed:16786509}. FT /FTId=VAR_063363. FT VARIANT 736 736 G -> C (in OI1; mild). FT {ECO:0000269|PubMed:1990009, FT ECO:0000269|PubMed:8456807}. FT /FTId=VAR_001879. FT VARIANT 739 739 G -> R (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063364. FT VARIANT 743 743 A -> G (in dbSNP:rs408535). FT {ECO:0000269|PubMed:2824475, FT ECO:0000269|PubMed:3421913, FT ECO:0000269|PubMed:9443882}. FT /FTId=VAR_001880. FT VARIANT 748 748 G -> V (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063365. FT VARIANT 751 751 G -> S (in OI4). FT {ECO:0000269|PubMed:2052622}. FT /FTId=VAR_001881. FT VARIANT 754 754 G -> C (in OI4). FT {ECO:0000269|PubMed:16879195}. FT /FTId=VAR_063366. FT VARIANT 754 754 G -> R (in OI2). FT /FTId=VAR_001882. FT VARIANT 766 766 G -> V (in OI4). FT {ECO:0000269|PubMed:7693712}. FT /FTId=VAR_001883. FT VARIANT 778 778 G -> S (in OI3). FT {ECO:0000269|PubMed:7720740}. FT /FTId=VAR_001884. FT VARIANT 784 784 G -> R (in OI2). FT {ECO:0000269|PubMed:1874719}. FT /FTId=VAR_001885. FT VARIANT 787 787 G -> C (in OI2). FT {ECO:0000269|PubMed:10627137}. FT /FTId=VAR_001886. FT VARIANT 790 790 G -> D (in OI2). FT {ECO:0000269|PubMed:18996919, FT ECO:0000269|PubMed:8182080}. FT /FTId=VAR_001887. FT VARIANT 796 796 G -> S (in OI2). FT {ECO:0000269|PubMed:7693712}. FT /FTId=VAR_001888. FT VARIANT 798 798 P -> PP (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063367. FT VARIANT 806 811 Missing (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063368. FT VARIANT 811 811 G -> GPPG (in OI4). FT /FTId=VAR_063369. FT VARIANT 820 820 G -> S (in OI3). FT {ECO:0000269|PubMed:16705691}. FT /FTId=VAR_063370. FT VARIANT 822 822 R -> H (in dbSNP:rs1800240). FT {ECO:0000269|PubMed:8829649}. FT /FTId=VAR_001889. FT VARIANT 835 835 G -> C (in OI3). FT {ECO:0000269|PubMed:16879195}. FT /FTId=VAR_063371. FT VARIANT 835 835 G -> S (in OI1). FT {ECO:0000269|PubMed:8829649}. FT /FTId=VAR_001890. FT VARIANT 856 856 G -> R (in OI3). FT {ECO:0000269|PubMed:16705691}. FT /FTId=VAR_063372. FT VARIANT 856 856 G -> V (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063373. FT VARIANT 877 877 G -> C (in OI2). {ECO:0000269|Ref.33}. FT /FTId=VAR_001891. FT VARIANT 892 892 G -> D (in OI3 and OI4). FT {ECO:0000269|PubMed:8800927}. FT /FTId=VAR_001892. FT VARIANT 895 895 G -> D (in OI2). FT /FTId=VAR_001893. FT VARIANT 949 949 G -> S (in OI3; moderate). FT {ECO:0000269|PubMed:18996919, FT ECO:0000269|PubMed:8081394}. FT /FTId=VAR_001894. FT VARIANT 955 955 G -> D (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063374. FT VARIANT 955 955 G -> S (in OI2). FT {ECO:0000269|PubMed:2777764}. FT /FTId=VAR_001895. FT VARIANT 973 973 G -> V (in OI3). FT {ECO:0000269|PubMed:10408781}. FT /FTId=VAR_008120. FT VARIANT 982 982 G -> D (in OI2). FT {ECO:0000269|PubMed:16786509}. FT /FTId=VAR_063375. FT VARIANT 989 989 P -> PVGP (in OI4). FT /FTId=VAR_063376. FT VARIANT 991 991 G -> V (in OI3). FT {ECO:0000269|PubMed:16879195}. FT /FTId=VAR_063377. FT VARIANT 997 997 G -> D (in OI2). FT {ECO:0000269|PubMed:2914942}. FT /FTId=VAR_001896. FT VARIANT 1003 1003 G -> D (in OI2). FT {ECO:0000269|PubMed:16786509}. FT /FTId=VAR_063378. FT VARIANT 1012 1012 G -> S (in OI3 and OI4; moderate). FT {ECO:0000269|PubMed:16705691, FT ECO:0000269|PubMed:8094076}. FT /FTId=VAR_001897. FT VARIANT 1022 1022 L -> F (in dbSNP:rs392609). FT {ECO:0000269|PubMed:2824475, FT ECO:0000269|PubMed:6687691, FT ECO:0000269|PubMed:9443882}. FT /FTId=VAR_001898. FT VARIANT 1027 1027 G -> E (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063379. FT VARIANT 1058 1062 Missing (in OI2). FT {ECO:0000269|PubMed:18996919}. FT /FTId=VAR_063380. FT VARIANT 1066 1066 G -> D (in OI2). FT /FTId=VAR_001899. FT VARIANT 1067 1067 R -> H. {ECO:0000269|PubMed:23656646}. FT /FTId=VAR_069633. FT VARIANT 1078 1078 G -> C (in OI2). FT /FTId=VAR_001900. FT VARIANT 1087 1087 G -> D (in OI3). FT {ECO:0000269|PubMed:16786509}. FT /FTId=VAR_063381. FT VARIANT 1094 1096 Missing (in OI4). FT {ECO:0000269|PubMed:16705691}. FT /FTId=VAR_063382. FT VARIANT 1096 1096 G -> A (in OI3). FT {ECO:0000269|PubMed:7749416}. FT /FTId=VAR_001901. FT VARIANT 1101 1101 P -> L. FT /FTId=VAR_001903. FT VARIANT 1102 1102 G -> R (in OI4). FT {ECO:0000269|PubMed:2897363}. FT /FTId=VAR_001902. FT VARIANT 1119 1119 A -> T (found in a patient with mild FT osteogenesis imperfecta associated with FT increased bone mineral density; results FT in defective type I procollagen FT processing; incorporation of the immature FT procollagen into the matrix leads to FT increased bone matrix mineralization and FT altered collagen fibril structure). FT {ECO:0000269|PubMed:21344539}. FT /FTId=VAR_066386. FT VARIANT 1148 1148 T -> P (in OI3; dbSNP:rs1800250). FT {ECO:0000269|PubMed:8723681}. FT /FTId=VAR_001904. FT VARIANT 1189 1189 D -> E (in dbSNP:rs422361). FT {ECO:0000269|PubMed:2824475, FT ECO:0000269|PubMed:6687691, FT ECO:0000269|PubMed:9443882}. FT /FTId=VAR_001905. FT VARIANT 1195 1195 C -> Y (in OI1). FT {ECO:0000269|PubMed:16786509}. FT /FTId=VAR_063383. FT VARIANT 1198 1198 S -> P (in dbSNP:rs384487). FT {ECO:0000269|PubMed:2824475, FT ECO:0000269|PubMed:6687691, FT ECO:0000269|PubMed:9443882}. FT /FTId=VAR_001906. FT VARIANT 1354 1354 Q -> H (in dbSNP:rs418570). FT {ECO:0000269|PubMed:2364107, FT ECO:0000269|PubMed:2824475, FT ECO:0000269|PubMed:6092353, FT ECO:0000269|PubMed:6309769, FT ECO:0000269|PubMed:6687691, FT ECO:0000269|PubMed:9016532, FT ECO:0000269|PubMed:9443882}. FT /FTId=VAR_030122. FT CONFLICT 55 55 E -> G (in Ref. 6; CAA26320). FT {ECO:0000305}. FT CONFLICT 333 333 V -> P (in Ref. 1; AAB59374). FT {ECO:0000305}. FT CONFLICT 338 338 A -> T (in Ref. 1; AAB59374). FT {ECO:0000305}. FT CONFLICT 549 549 P -> D (in Ref. 5; CAA68709). FT {ECO:0000305}. FT CONFLICT 828 828 V -> A (in Ref. 17; CAA23761). FT {ECO:0000305}. FT CONFLICT 831 831 T -> P (in Ref. 17; CAA23761). FT {ECO:0000305}. FT CONFLICT 837 837 V -> P (in Ref. 17; CAA23761). FT {ECO:0000305}. FT CONFLICT 980 980 E -> V (in Ref. 21; AAA51996). FT {ECO:0000305}. FT CONFLICT 1098 1098 P -> L (in Ref. 17; CAA23761). FT {ECO:0000305}. FT CONFLICT 1122 1125 Missing (in Ref. 17; CAA23761). FT {ECO:0000305}. FT CONFLICT 1338 1338 R -> A (in Ref. 23; AAA51887). FT {ECO:0000305}. SQ SEQUENCE 1366 AA; 129314 MW; 1E68A5970FB4210A CRC64; MLSFVDTRTL LLLAVTLCLA TCQSLQEETV RKGPAGDRGP RGERGPPGPP GRDGEDGPTG PPGPPGPPGP PGLGGNFAAQ YDGKGVGLGP GPMGLMGPRG PPGAAGAPGP QGFQGPAGEP GEPGQTGPAG ARGPAGPPGK AGEDGHPGKP GRPGERGVVG PQGARGFPGT PGLPGFKGIR GHNGLDGLKG QPGAPGVKGE PGAPGENGTP GQTGARGLPG ERGRVGAPGP AGARGSDGSV GPVGPAGPIG SAGPPGFPGA PGPKGEIGAV GNAGPAGPAG PRGEVGLPGL SGPVGPPGNP GANGLTGAKG AAGLPGVAGA PGLPGPRGIP GPVGAAGATG ARGLVGEPGP AGSKGESGNK GEPGSAGPQG PPGPSGEEGK RGPNGEAGSA GPPGPPGLRG SPGSRGLPGA DGRAGVMGPP GSRGASGPAG VRGPNGDAGR PGEPGLMGPR GLPGSPGNIG PAGKEGPVGL PGIDGRPGPI GPAGARGEPG NIGFPGPKGP TGDPGKNGDK GHAGLAGARG APGPDGNNGA QGPPGPQGVQ GGKGEQGPPG PPGFQGLPGP SGPAGEVGKP GERGLHGEFG LPGPAGPRGE RGPPGESGAA GPTGPIGSRG PSGPPGPDGN KGEPGVVGAV GTAGPSGPSG LPGERGAAGI PGGKGEKGEP GLRGEIGNPG RDGARGAPGA VGAPGPAGAT GDRGEAGAAG PAGPAGPRGS PGERGEVGPA GPNGFAGPAG AAGQPGAKGE RGAKGPKGEN GVVGPTGPVG AAGPAGPNGP PGPAGSRGDG GPPGMTGFPG AAGRTGPPGP SGISGPPGPP GPAGKEGLRG PRGDQGPVGR TGEVGAVGPP GFAGEKGPSG EAGTAGPPGT PGPQGLLGAP GILGLPGSRG ERGLPGVAGA VGEPGPLGIA GPPGARGPPG AVGSPGVNGA PGEAGRDGNP GNDGPPGRDG QPGHKGERGY PGNIGPVGAA GAPGPHGPVG PAGKHGNRGE TGPSGPVGPA GAVGPRGPSG PQGIRGDKGE PGEKGPRGLP GLKGHNGLQG LPGIAGHHGD QGAPGSVGPA GPRGPAGPSG PAGKDGRTGH PGTVGPAGIR GPQGHQGPAG PPGPPGPPGP PGVSGGGYDF GYDGDFYRAD QPRSAPSLRP KDYEVDATLK SLNNQIETLL TPEGSRKNPA RTCRDLRLSH PEWSSGYYWI DPNQGCTMDA IKVYCDFSTG ETCIRAQPEN IPAKNWYRSS KDKKHVWLGE TINAGSQFEY NVEGVTSKEM ATQLAFMRLL ANYASQNITY HCKNSIAYMD EETGNLKKAV ILQGSNDVEL VAEGNSRFTY TVLVDGCSKK TNEWGKTIIE YKTNKPSRLP FLDIAPLDIG GADQEFFVDI GPVCFK //