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NameCollagen alpha-1(III) chain
Synonyms
  • Collagen alpha-1(III) chain precursor
  • III
Gene NameCOL3A1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0004178|Collagen alpha-1(III) chain
MMSFVQKGSWLLLALLHPTIILAQQEAVEGGCSHLGQSYADRDVWKPEPCQICVCDSGSV
LCDDIICDDQELDCPNPEIPFGECCAVCPQPPTAPTRPPNGQGPQGPKGDPGPPGIPGRN
GDPGIPGQPGSPGSPGPPGICESCPTGPQNYSPQYDSYDVKSGVAVGGLAGYPGPAGPPG
PPGPPGTSGHPGSPGSPGYQGPPGEPGQAGPSGPPGPPGAIGPSGPAGKDGESGRPGRPG
ERGLPGPPGIKGPAGIPGFPGMKGHRGFDGRNGEKGETGAPGLKGENGLPGENGAPGPMG
PRGAPGERGRPGLPGAAGARGNDGARGSDGQPGPPGPPGTAGFPGSPGAKGEVGPAGSPG
SNGAPGQRGEPGPQGHAGAQGPPGPPGINGSPGGKGEMGPAGIPGAPGLMGARGPPGPAG
ANGAPGLRGGAGEPGKNGAKGEPGPRGERGEAGIPGVPGAKGEDGKDGSPGEPGANGLPG
AAGERGAPGFRGPAGPNGIPGEKGPAGERGAPGPAGPRGAAGEPGRDGVPGGPGMRGMPG
SPGGPGSDGKPGPPGSQGESGRPGPPGPSGPRGQPGVMGFPGPKGNDGAPGKNGERGGPG
GPGPQGPPGKNGETGPQGPPGPTGPGGDKGDTGPPGPQGLQGLPGTGGPPGENGKPGEPG
PKGDAGAPGAPGGKGDAGAPGERGPPGLAGAPGLRGGAGPPGPEGGKGAAGPPGPPGAAG
TPGLQGMPGERGGLGSPGPKGDKGEPGGPGADGVPGKDGPRGPTGPIGPPGPAGQPGDKG
EGGAPGLPGIAGPRGSPGERGETGPPGPAGFPGAPGQNGEPGGKGERGAPGEKGEGGPPG
VAGPPGGSGPAGPPGPQGVKGERGSPGGPGAAGFPGARGLPGPPGSNGNPGPPGPSGSPG
KDGPPGPAGNTGAPGSPGVSGPKGDAGQPGEKGSPGAQGPPGAPGPLGIAGITGARGLAG
PPGMPGPRGSPGPQGVKGESGKPGANGLSGERGPPGPQGLPGLAGTAGEPGRDGNPGSDG
LPGRDGSPGGKGDRGENGSPGAPGAPGHPGPPGPVGPAGKSGDRGESGPAGPAGAPGPAG
SRGAPGPQGPRGDKGETGERGAAGIKGHRGFPGNPGAPGSPGPAGQQGAIGSPGPAGPRG
PVGPSGPPGKDGTSGHPGPIGPPGPRGNRGERGSEGSPGHPGQPGPPGPPGAPGPCCGGV
GAAAIAGIGGEKAGGFAPYYGDEPMDFKINTDEIMTSLKSVNGQIESLISPDGSRKNPAR
NCRDLKFCHPELKSGEYWVDPNQGCKLDAIKVFCNMETGETCISANPLNVPRKHWWTDSS
AEKKHVWFGESMDGGFQFSYGNPELPEDVLDVHLAFLRLLSSRASQNITYHCKNSIAYMD
QASGNVKKALKLMGSNEGEFKAEGNSKFTYTVLEDGCTKHTGEWSKTVFEYRTRKAVRLP
IVDIAPYDIGGPDQEFGVDVGPVCFL
Number of residues1466
Molecular Weight138564.005
Theoretical pI6.57
GO Classification
Functions
  • integrin binding
  • extracellular matrix structural constituent
  • metal ion binding
  • platelet-derived growth factor binding
Processes
  • digestive tract development
  • cellular response to amino acid stimulus
  • cerebral cortex development
  • collagen catabolic process
  • positive regulation of Rho protein signal transduction
  • collagen fibril organization
  • extracellular matrix disassembly
  • negative regulation of immune response
  • extracellular matrix organization
  • peptide cross-linking
  • receptor-mediated endocytosis
  • skin development
  • regulation of immune response
  • skeletal system development
  • aorta smooth muscle tissue morphogenesis
  • heart development
  • cell-matrix adhesion
  • negative regulation of neuron migration
  • wound healing
  • integrin-mediated signaling pathway
  • response to radiation
  • response to mechanical stimulus
  • transforming growth factor beta receptor signaling pathway
  • platelet activation
  • aging
  • axon guidance
  • response to cytokine
  • extracellular fibril organization
Components
  • extracellular matrix
  • collagen type III trimer
  • extracellular region
  • extracellular space
  • endoplasmic reticulum lumen
General FunctionPlatelet-derived growth factor binding
Specific FunctionCollagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of GPR56 in the developing brain and binding to GPR56 inhibits neuronal migration and activates the RhoA pathway by coupling GPR56 to GNA13 and possibly GNA12.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID30058
UniProtKB IDP02461
UniProtKB Entry NameCO3A1_HUMAN
Cellular LocationSecreted
Gene sequence
>lcl|BSEQ0011542|Collagen alpha-1(III) chain (COL3A1)
ATGATGAGCTTTGTGCAAAAGGGGAGCTGGCTACTTCTCGCTCTGCTTCATCCCACTATT
ATTTTGGCACAACAGGAAGCTGTTGAAGGAGGATGTTCCCATCTTGGTCAGTCCTATGCG
GATAGAGATGTCTGGAAGCCAGAACCATGCCAAATATGTGTCTGTGACTCAGGATCCGTT
CTCTGCGATGACATAATATGTGACGATCAAGAATTAGACTGCCCCAACCCAGAAATTCCA
TTTGGAGAATGTTGTGCAGTTTGCCCACAGCCTCCAACTGCTCCTACTCGCCCTCCTAAT
GGTCAAGGACCTCAAGGCCCCAAGGGAGATCCAGGCCCTCCTGGTATTCCTGGGAGAAAT
GGTGACCCTGGTATTCCAGGACAACCAGGGTCCCCTGGTTCTCCTGGCCCCCCTGGAATC
TGTGAATCATGCCCTACTGGTCCTCAGAACTATTCTCCCCAGTATGATTCATATGATGTC
AAGTCTGGAGTAGCAGTAGGAGGACTCGCAGGCTATCCTGGACCAGCTGGCCCCCCAGGC
CCTCCCGGTCCCCCTGGTACATCTGGTCATCCTGGTTCCCCTGGATCTCCAGGATACCAA
GGACCCCCTGGTGAACCTGGGCAAGCTGGTCCTTCAGGCCCTCCAGGACCTCCTGGTGCT
ATAGGTCCATCTGGTCCTGCTGGAAAAGATGGAGAATCAGGTAGACCCGGACGACCTGGA
GAGCGAGGATTGCCTGGACCTCCAGGTATCAAAGGTCCAGCTGGGATACCTGGATTCCCT
GGTATGAAAGGACACAGAGGCTTCGATGGACGAAATGGAGAAAAGGGTGAAACAGGTGCT
CCTGGATTAAAGGGTGAAAATGGTCTTCCAGGCGAAAATGGAGCTCCTGGACCCATGGGT
CCAAGAGGGGCTCCTGGTGAGCGAGGACGGCCAGGACTTCCTGGGGCTGCAGGTGCTCGG
GGTAATGACGGTGCTCGAGGCAGTGATGGTCAACCAGGCCCTCCTGGTCCTCCTGGAACT
GCCGGATTCCCTGGATCCCCTGGTGCTAAGGGTGAAGTTGGACCTGCAGGGTCTCCTGGT
TCAAATGGTGCCCCTGGACAAAGAGGAGAACCTGGACCTCAGGGACACGCTGGTGCTCAA
GGTCCTCCTGGCCCTCCTGGGATTAATGGTAGTCCTGGTGGTAAAGGCGAAATGGGTCCC
GCTGGCATTCCTGGAGCTCCTGGACTGATGGGAGCCCGGGGTCCTCCAGGACCAGCCGGT
GCTAATGGTGCTCCTGGACTGCGAGGTGGTGCAGGTGAGCCTGGTAAGAATGGTGCCAAA
GGAGAGCCCGGACCACGTGGTGAACGCGGTGAGGCTGGTATTCCAGGTGTTCCAGGAGCT
AAAGGCGAAGATGGCAAGGATGGATCACCTGGAGAACCTGGTGCAAATGGGCTTCCAGGA
GCTGCAGGAGAAAGGGGTGCCCCTGGGTTCCGAGGACCTGCTGGACCAAATGGCATCCCA
GGAGAAAAGGGTCCTGCTGGAGAGCGTGGTGCTCCAGGCCCTGCAGGGCCCAGAGGAGCT
GCTGGAGAACCTGGCAGAGATGGCGTCCCTGGAGGTCCAGGAATGAGGGGCATGCCCGGA
AGTCCAGGAGGACCAGGAAGTGATGGGAAACCAGGGCCTCCCGGAAGTCAAGGAGAAAGT
GGTCGACCAGGTCCTCCTGGGCCATCTGGTCCCCGAGGTCAGCCTGGTGTCATGGGCTTC
CCCGGTCCTAAAGGAAATGATGGTGCTCCTGGTAAGAATGGAGAACGAGGTGGCCCTGGA
GGACCTGGCCCTCAGGGTCCTCCTGGAAAGAATGGTGAAACTGGACCTCAGGGACCCCCA
GGGCCTACTGGGCCTGGTGGTGACAAAGGAGACACAGGACCCCCTGGTCCACAAGGATTA
CAAGGCTTGCCTGGTACAGGTGGTCCTCCAGGAGAAAATGGAAAACCTGGGGAACCAGGT
CCAAAGGGTGATGCCGGTGCACCTGGAGCTCCAGGAGGCAAGGGTGATGCTGGTGCCCCT
GGTGAACGTGGACCTCCTGGATTGGCAGGGGCCCCAGGACTTAGAGGTGGAGCTGGTCCC
CCTGGTCCCGAAGGAGGAAAGGGTGCTGCTGGTCCTCCTGGGCCACCTGGTGCTGCTGGT
ACTCCTGGTCTGCAAGGAATGCCTGGAGAAAGAGGAGGTCTTGGAAGTCCTGGTCCAAAG
GGTGACAAGGGTGAACCAGGCGGTCCAGGTGCTGATGGTGTCCCAGGGAAAGATGGCCCA
AGGGGTCCTACTGGTCCTATTGGTCCTCCTGGCCCAGCTGGCCAGCCTGGAGATAAGGGT
GAAGGTGGTGCCCCCGGACTTCCAGGTATAGCTGGACCTCGTGGTAGCCCTGGTGAGAGA
GGTGAAACTGGCCCTCCAGGACCTGCTGGTTTCCCTGGTGCTCCTGGACAGAATGGTGAA
CCTGGTGGTAAAGGAGAAAGAGGGGCTCCGGGTGAGAAAGGTGAAGGAGGCCCTCCTGGA
GTTGCAGGACCCCCTGGAGGTTCTGGACCTGCTGGTCCTCCTGGTCCCCAAGGTGTCAAA
GGTGAACGTGGCAGTCCTGGTGGACCTGGTGCTGCTGGCTTCCCTGGTGCTCGTGGTCTT
CCTGGTCCTCCTGGTAGTAATGGTAACCCAGGACCCCCAGGTCCCAGCGGTTCTCCAGGC
AAGGATGGGCCCCCAGGTCCTGCGGGTAACACTGGTGCTCCTGGCAGCCCTGGAGTGTCT
GGACCAAAAGGTGATGCTGGCCAACCAGGAGAGAAGGGATCGCCTGGTGCCCAGGGCCCA
CCAGGAGCTCCAGGCCCACTTGGGATTGCTGGGATCACTGGAGCACGGGGTCTTGCAGGA
CCACCAGGCATGCCAGGTCCTAGGGGAAGCCCTGGCCCTCAGGGTGTCAAGGGTGAAAGT
GGGAAACCAGGAGCTAACGGTCTCAGTGGAGAACGTGGTCCCCCTGGACCCCAGGGTCTT
CCTGGTCTGGCTGGTACAGCTGGTGAACCTGGAAGAGATGGAAACCCTGGATCAGATGGT
CTTCCAGGCCGAGATGGATCTCCTGGTGGCAAGGGTGATCGTGGTGAAAATGGCTCTCCT
GGTGCCCCTGGCGCTCCTGGTCATCCAGGCCCACCTGGTCCTGTCGGTCCAGCTGGAAAG
AGTGGTGACAGAGGAGAAAGTGGCCCTGCTGGCCCTGCTGGTGCTCCCGGTCCTGCTGGT
TCCCGAGGTGCTCCTGGTCCTCAAGGCCCACGTGGTGACAAAGGTGAAACAGGTGAACGT
GGAGCTGCTGGCATCAAAGGACATCGAGGATTCCCTGGTAATCCAGGTGCCCCAGGTTCT
CCAGGCCCTGCTGGTCAGCAGGGTGCAATCGGCAGTCCAGGACCTGCAGGCCCCAGAGGA
CCTGTTGGACCCAGTGGACCTCCTGGCAAAGATGGAACCAGTGGACATCCAGGTCCCATT
GGACCACCAGGGCCTCGAGGTAACAGAGGTGAAAGAGGATCTGAGGGCTCCCCAGGCCAC
CCAGGGCAACCAGGCCCTCCTGGACCTCCTGGTGCCCCTGGTCCTTGCTGTGGTGGTGTT
GGAGCCGCTGCCATTGCTGGGATTGGAGGTGAAAAAGCTGGCGGTTTTGCCCCGTATTAT
GGAGATGAACCAATGGATTTCAAAATCAACACCGATGAGATTATGACTTCACTCAAGTCT
GTTAATGGACAAATAGAAAGCCTCATTAGTCCTGATGGTTCTCGTAAAAACCCCGCTAGA
AACTGCAGAGACCTGAAATTCTGCCATCCTGAACTCAAGAGTGGAGAATACTGGGTTGAC
CCTAACCAAGGATGCAAATTGGATGCTATCAAGGTATTCTGTAATATGGAAACTGGGGAA
ACATGCATAAGTGCCAATCCTTTGAATGTTCCACGGAAACACTGGTGGACAGATTCTAGT
GCTGAGAAGAAACACGTTTGGTTTGGAGAGTCCATGGATGGTGGTTTTCAGTTTAGCTAC
GGCAATCCTGAACTTCCTGAAGATGTCCTTGATGTGCAGCTGGCATTCCTTCGACTTCTC
TCCAGCCGAGCTTCCCAGAACATCACATATCACTGCAAAAATAGCATTGCATACATGGAT
CAGGCCAGTGGAAATGTAAAGAAGGCCCTGAAGCTGATGGGGTCAAATGAAGGTGAATTC
AAGGCTGAAGGAAATAGCAAATTCACCTACACAGTTCTGGAGGATGGTTGCACGAAACAC
ACTGGGGAATGGAGCAAAACAGTCTTTGAATATCGAACACGCAAGGCTGTGAGACTACCT
ATTGTAGATATTGCACCCTATGACATTGGTGGTCCTGATCAAGAATTTGGTGTGGACGTT
GGCCCTGTTTGCTTTTTATAA
GenBank Gene IDX14420
GeneCard IDNot Available
GenAtlas IDCOL3A1
HGNC IDHGNC:2201
Chromosome Location2
Locus2q31
References
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  2. Valkkila M, Melkoniemi M, Kvist L, Kuivaniemi H, Tromp G, Ala-Kokko L: Genomic organization of the human COL3A1 and COL5A2 genes: COL5A2 has evolved differently than the other minor fibrillar collagen genes. Matrix Biol. 2001 Sep;20(5-6):357-66. 11566270
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  5. Benson-Chanda V, Su MW, Weil D, Chu ML, Ramirez F: Cloning and analysis of the 5' portion of the human type-III procollagen gene (COL3A1). Gene. 1989 May 30;78(2):255-65. 2777083
  6. Toman PD, Ricca GA, de Crombrugghe B: Nucleotide sequence of a cDNA coding for the amino-terminal region of human prepro alpha 1(III) collagen. Nucleic Acids Res. 1988 Jul 25;16(14B):7201. 3405773
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  8. Seyer JM, Kang AH: Covalent structure of collagen: amino acid sequence of cyanogen bromide peptides from the amino-terminal segment of type III collagen of human liver. Biochemistry. 1977 Mar 22;16(6):1158-64. 557335
  9. Milewicz DM, Witz AM, Smith AC, Manchester DK, Waldstein G, Byers PH: Parental somatic and germ-line mosaicism for a multiexon deletion with unusual endpoints in a type III collagen (COL3A1) allele produces Ehlers-Danlos syndrome type IV in the heterozygous offspring. Am J Hum Genet. 1993 Jul;53(1):62-70. 8317500
  10. Chiodo AA, Sillence DO, Cole WG, Bateman JF: Abnormal type III collagen produced by an exon-17-skipping mutation of the COL3A1 gene in Ehlers-Danlos syndrome type IV is not incorporated into the extracellular matrix. Biochem J. 1995 Nov 1;311 ( Pt 3):939-43. 7487954
  11. Minafra IP, Andriolo M, Basirico L, Aquino A, Minafra S, Boutillon MM, van der Rest M: Onco-fetal/laminin-binding collagen from colon carcinoma: detection of new sequences. Biochem Biophys Res Commun. 1995 Feb 15;207(2):852-9. 7864881
  12. Seyer JM, Kang AH: Covalent structure of collagen: amino acid sequence of five consecutive CNBr peptides from type III collagen of human liver. Biochemistry. 1978 Aug 8;17(16):3404-11. 687591
  13. Lee B, Vitale E, Superti-Furga A, Steinmann B, Ramirez F: G to T transversion at position +5 of a splice donor site causes skipping of the preceding exon in the type III procollagen transcripts of a patient with Ehlers-Danlos syndrome type IV. J Biol Chem. 1991 Mar 15;266(8):5256-9. 1672129
  14. Seyer JM, Mainardi C, Kang AH: Covalent structure of collagen: amino acid sequence of alpha 1 (III)-CB5 from type III collagen of human liver. Biochemistry. 1980 Apr 15;19(8):1583-9. 6246925
  15. Cole WG, Chiodo AA, Lamande SR, Janeczko R, Ramirez F, Dahl HH, Chan D, Bateman JF: A base substitution at a splice site in the COL3A1 gene causes exon skipping and generates abnormal type III procollagen in a patient with Ehlers-Danlos syndrome type IV. J Biol Chem. 1990 Oct 5;265(28):17070-7. 2145268
  16. Mankoo BS, Dalgleish R: Human pro alpha 1(III) collagen: cDNA sequence for the 3' end. Nucleic Acids Res. 1988 Mar 25;16(5):2337. 3357782
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  19. Loidl HR, Brinker JM, May M, Pihlajaniemi T, Morrow S, Rosenbloom J, Myers JC: Molecular cloning and carboxyl-propeptide analysis of human type III procollagen. Nucleic Acids Res. 1984 Dec 21;12(24):9383-94. 6096827
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  22. Chu ML, Weil D, de Wet W, Bernard M, Sippola M, Ramirez F: Isolation of cDNA and genomic clones encoding human pro-alpha 1 (III) collagen. Partial characterization of the 3' end region of the gene. J Biol Chem. 1985 Apr 10;260(7):4357-63. 2579949
  23. Kuivaniemi H, Tromp G, Prockop DJ: Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels. Hum Mutat. 1997;9(4):300-15. 9101290
  24. Rosenow A, Noben JP, Jocken J, Kallendrusch S, Fischer-Posovszky P, Mariman EC, Renes J: Resveratrol-induced changes of the human adipocyte secretion profile. J Proteome Res. 2012 Sep 7;11(9):4733-43. doi: 10.1021/pr300539b. Epub 2012 Aug 27. 22905912
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  26. Boudko SP, Engel J, Okuyama K, Mizuno K, Bachinger HP, Schumacher MA: Crystal structure of human type III collagen Gly991-Gly1032 cystine knot-containing peptide shows both 7/2 and 10/3 triple helical symmetries. J Biol Chem. 2008 Nov 21;283(47):32580-9. doi: 10.1074/jbc.M805394200. Epub 2008 Sep 19. 18805790
  27. Bourhis JM, Mariano N, Zhao Y, Harlos K, Exposito JY, Jones EY, Moali C, Aghajari N, Hulmes DJ: Structural basis of fibrillar collagen trimerization and related genetic disorders. Nat Struct Mol Biol. 2012 Oct;19(10):1031-6. doi: 10.1038/nsmb.2389. Epub 2012 Sep 23. 23001006
  28. Tromp G, Wu Y, Prockop DJ, Madhatheri SL, Kleinert C, Earley JJ, Zhuang J, Norrgard O, Darling RC, Abbott WM, et al.: Sequencing of cDNA from 50 unrelated patients reveals that mutations in the triple-helical domain of type III procollagen are an infrequent cause of aortic aneurysms. J Clin Invest. 1993 Jun;91(6):2539-45. 8514866
  29. Zafarullah K, Kleinert C, Tromp G, Kuivaniemi H, Kontusaari S, Wu YL, Ganguly A, Prockop DJ: G to A polymorphism in exon 31 of the COL3A1 gene. Nucleic Acids Res. 1990 Oct 25;18(20):6180. 2235526
  30. Kontusaari S, Tromp G, Kuivaniemi H, Romanic AM, Prockop DJ: A mutation in the gene for type III procollagen (COL3A1) in a family with aortic aneurysms. J Clin Invest. 1990 Nov;86(5):1465-73. 2243125
  31. Richards AJ, Lloyd JC, Narcisi P, Ward PN, Nicholls AC, De Paepe A, Pope FM: A 27-bp deletion from one allele of the type III collagen gene (COL3A1) in a large family with Ehlers-Danlos syndrome type IV. Hum Genet. 1992 Jan;88(3):325-30. 1370809
  32. Richards A, Narcisi P, Lloyd J, Ferguson C, Pope FM: The substitution of glycine 661 by arginine in type III collagen produces mutant molecules with different thermal stabilities and causes Ehlers-Danlos syndrome type IV. J Med Genet. 1993 Aug;30(8):690-3. 8411057
  33. Tromp G, Kuivaniemi H, Shikata H, Prockop DJ: A single base mutation that substitutes serine for glycine 790 of the alpha 1 (III) chain of type III procollagen exposes an arginine and causes Ehlers-Danlos syndrome IV. J Biol Chem. 1989 Jan 25;264(3):1349-52. 2492273
  34. Tromp G, De Paepe A, Nuytinck L, Madhatheri S, Kuivaniemi H: Substitution of valine for glycine 793 in type III procollagen in Ehlers-Danlos syndrome type IV. Hum Mutat. 1995;5(2):179-81. 7749417
  35. Richards AJ, Ward PN, Narcisi P, Nicholls AC, Lloyd JC, Pope FM: A single base mutation in the gene for type III collagen (COL3A1) converts glycine 847 to glutamic acid in a family with Ehlers-Danlos syndrome type IV. An unaffected family member is mosaic for the mutation. Hum Genet. 1992 Jun;89(4):414-8. 1352273
  36. Tromp G, Kuivaniemi H, Stolle C, Pope FM, Prockop DJ: Single base mutation in the type III procollagen gene that converts the codon for glycine 883 to aspartate in a mild variant of Ehlers-Danlos syndrome IV. J Biol Chem. 1989 Nov 15;264(32):19313-7. 2808425
  37. Kontusaari S, Tromp G, Kuivaniemi H, Ladda RL, Prockop DJ: Inheritance of an RNA splicing mutation (G+ 1 IVS20) in the type III procollagen gene (COL3A1) in a family having aortic aneurysms and easy bruisability: phenotypic overlap between familial arterial aneurysms and Ehlers-Danlos syndrome type IV. Am J Hum Genet. 1990 Jul;47(1):112-20. 2349939
  38. Richards AJ, Lloyd JC, Ward PN, De Paepe A, Narcisi P, Pope FM: Characterisation of a glycine to valine substitution at amino acid position 910 of the triple helical region of type III collagen in a patient with Ehlers-Danlos syndrome type IV. J Med Genet. 1991 Jul;28(7):458-63. 1895316
  39. Johnson PH, Richards AJ, Pope FM, Hopkinson DA: A COL3A1 glycine 1006 to glutamic acid substitution in a patient with Ehlers-Danlos syndrome type IV detected by denaturing gradient gel electrophoresis. J Inherit Metab Dis. 1992;15(3):426-30. 1357232
  40. Kontusaari S, Tromp G, Kuivaniemi H, Stolle C, Pope FM, Prockop DJ: Substitution of aspartate for glycine 1018 in the type III procollagen (COL3A1) gene causes type IV Ehlers-Danlos syndrome: the mutated allele is present in most blood leukocytes of the asymptomatic and mosaic mother. Am J Hum Genet. 1992 Sep;51(3):497-507. 1496983
  41. Narcisi P, Wu Y, Tromp G, Earley JJ, Richards AJ, Pope FM, Kuivaniemi H: Single base mutation that substitutes glutamic acid for glycine 1021 in the COL3A1 gene and causes Ehlers-Danlos syndrome type IV. Am J Med Genet. 1993 May 15;46(3):278-83. 8098182
  42. Kuivaniemi H, Prockop DJ, Wu Y, Madhatheri SL, Kleinert C, Earley JJ, Jokinen A, Stolle C, Majamaa K, Myllyla VV, et al.: Exclusion of mutations in the gene for type III collagen (COL3A1) as a common cause of intracranial aneurysms or cervical artery dissections: results from sequence analysis of the coding sequences of type III collagen from 55 unrelated patients. Neurology. 1993 Dec;43(12):2652-8. 8255472
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