P02461 (CO3A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-1(III) chain

Gene names

Name:

COL3A1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1466 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Collagen type III occurs in most soft connective tissues along with type I collagen.
Subunit structure	Trimers of identical alpha 1(III) chains. The chains are linked to each other by interchain disulfide bonds. Trimers are also cross-linked via hydroxylysines.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Post-translational modification	Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.
Involvement in disease	Defects in COL3A1 are a cause of Ehlers-Danlos syndrome type 3 (EDS3) [MIM:130020]; also known as benign hypermobility syndrome. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS3 is a form of Ehlers-Danlos syndrome characterized by marked joint hyperextensibility without skeletal deformity. Ref.44 Defects in COL3A1 are the cause of Ehlers-Danlos syndrome type 4 (EDS4) [MIM:130050]. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS4 is the most severe form of the disease. It is characterized by the joint and dermal manifestations as in other forms of the syndrome, characteristic facial features (acrogeria) in most patients, and by proneness to spontaneous rupture of bowel and large arteries. The vascular complications may affect all anatomical areas. Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.43 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.55 Ref.56 Ref.57 Ref.58 Ref.60 Defects in COL3A1 are a cause of susceptibility to aortic aneurysm abdominal (AAA) [MIM:100070]. AAA is a common multifactorial disorder characterized by permanent dilation of the abdominal aorta, usually due to degenerative changes in the aortic wall. Histologically, AAA is characterized by signs of chronic inflammation, destructive remodeling of the extracellular matrix, and depletion of vascular smooth muscle cells. Ref.27 Ref.29 Ref.36
Sequence similarities	Belongs to the fibrillar collagen family. Contains 1 fibrillar collagen NC1 domain. Contains 1 VWFC domain.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Aortic aneurysm Disease mutation Ehlers-Danlos syndrome
Domain	Collagen Repeat Signal
PTM	Disulfide bond Glycoprotein Hydroxylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	axon guidance Traceable author statement. Source: Reactome cell-matrix adhesion Inferred from direct assay. Source: UniProtKB collagen biosynthetic process Inferred from mutant phenotype Ref.52. Source: UniProtKB collagen fibril organization Inferred from mutant phenotype Ref.52. Source: UniProtKB fibril organization Inferred from mutant phenotype. Source: UniProtKB heart development Inferred from mutant phenotype. Source: UniProtKB integrin-mediated signaling pathway Inferred from mutant phenotype. Source: UniProtKB negative regulation of immune response Inferred from mutant phenotype. Source: UniProtKB peptide cross-linking Inferred from direct assay. Source: UniProtKB platelet activation Non-traceable author statement. Source: UniProtKB response to cytokine stimulus Inferred from direct assay. Source: UniProtKB response to radiation Inferred from direct assay. Source: UniProtKB skin development Inferred from mutant phenotype Ref.52. Source: UniProtKB transforming growth factor beta receptor signaling pathway Inferred from direct assay. Source: UniProtKB
Cellular component	collagen type III Inferred from mutant phenotype Ref.12. Source: UniProtKB extracellular space Inferred from direct assay Ref.12. Source: UniProtKB
Molecular function	extracellular matrix structural constituent Inferred from mutant phenotype Ref.12Ref.52. Source: UniProtKB integrin binding Inferred from mutant phenotype. Source: UniProtKB platelet-derived growth factor binding Inferred from direct assay. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P02461-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P02461-2)

The sequence of this isoform differs from the canonical sequence as follows:
     847-1149: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23
	Propeptide	24 – 153	130	N-terminal propeptide		PRO_0000005740
	Chain	154 – 1221	1068	Collagen alpha-1(III) chain		PRO_0000005741
	Propeptide	1222 – 1466	245	C-terminal propeptide		PRO_0000005742
Regions
	Domain	30 – 89	60	VWFC
	Domain	1232 – 1466	235	Fibrillar collagen NC1
	Region	149 – 167	19	Nonhelical region (N-terminal)
	Region	168 – 1196	1029	Triple-helical region
	Region	1197 – 1205	9	Nonhelical region (C-terminal)
Amino acid modifications
	Modified residue	263	1	5-hydroxylysine
	Modified residue	284	1	5-hydroxylysine
	Modified residue	860	1	5-hydroxylysine
	Modified residue	977	1	5-hydroxylysine
	Modified residue	1094	1	5-hydroxylysine; partial
	Modified residue	1106	1	5-hydroxylysine
	Modified residue	1378	1	Phosphotyrosine Ref.26
	Modified residue	1383	1	Phosphoserine Ref.26
	Glycosylation	263	1	O-linked (Gal...) Ref.9
	Disulfide bond	1196		Interchain
	Disulfide bond	1197		Interchain
Natural variations
	Alternative sequence	847 – 1149	303	Missing in isoform 2.		VSP_022502
	Natural variant	169	1	L → F in AAA.		VAR_001767
	Natural variant	183	1	G → C in EDS4. Ref.46 Ref.52		VAR_001768
	Natural variant	183	1	G → D in EDS4.		VAR_011095
	Natural variant	183	1	G → S in EDS4.		VAR_011096
	Natural variant	192	1	G → V in EDS4.		VAR_011097
	Natural variant	201	1	G → R in EDS4. Ref.46 Ref.52		VAR_001769
	Natural variant	204	1	G → D in EDS4. Ref.55		VAR_011098
	Natural variant	204	1	G → S in EDS4.		VAR_011099
	Natural variant	210	1	G → D in EDS4. Ref.55		VAR_011100
	Natural variant	219	1	G → C in EDS4.		VAR_011101
	Natural variant	225	1	G → V in EDS4.		VAR_011102
	Natural variant	228	1	G → E in EDS4. Ref.46 Ref.52		VAR_001770
	Natural variant	240	1	G → R in EDS4.		VAR_011103
	Natural variant	243	1	G → V in EDS4.		VAR_011104
	Natural variant	249	1	G → D in EDS4.		VAR_011105
	Natural variant	249	1	G → V in EDS4.		VAR_011106
	Natural variant	252	1	G → D in EDS4.		VAR_011107
	Natural variant	252	1	G → R in EDS4.		VAR_011108
	Natural variant	252	1	G → V in EDS4.		VAR_011109
	Natural variant	255	1	G → V in EDS4.		VAR_011110
	Natural variant	264	1	G → R in EDS4. Ref.55		VAR_011111
	Natural variant	267	1	G → V in EDS4.		VAR_011112
	Natural variant	297	1	G → R in EDS4. Ref.58		VAR_037007
	Natural variant	303	1	G → R in fibromuscular dysplasia and aortic aneurysm. Ref.27		VAR_001771
	Natural variant	321	1	G → V in EDS4.		VAR_011113
	Natural variant	327	1	G → D in EDS4. Ref.55		VAR_011114
	Natural variant	345	1	G → R in EDS4.		VAR_011115
	Natural variant	417	1	G → R in EDS4.		VAR_011116
	Natural variant	420	1	G → S in a colorectal cancer sample; somatic mutation. Ref.61		VAR_035738
	Natural variant	444	1	G → R in EDS4.		VAR_011117
	Natural variant	489	1	G → E in EDS4.		VAR_011118
	Natural variant	501	1	G → R in EDS4.		VAR_011119
	Natural variant	519	1	G → V in EDS4.		VAR_011120
	Natural variant	534	1	G → E. Corresponds to variant rs41263744 [ dbSNP | Ensembl ].		VAR_055665
	Natural variant	540	1	G → R in EDS4. Ref.46 Ref.52		VAR_001772
	Natural variant	549	1	G → E in EDS4.		VAR_011121
	Natural variant	552	1	G → E in EDS4.		VAR_011122
	Natural variant	567	1	G → E in EDS4. Ref.48		VAR_001773
	Natural variant	582	1	G → S in EDS4. Ref.51		VAR_001774
	Natural variant	588	1	G → D in EDS4.		VAR_011123
	Natural variant	602	1	P → T. Ref.42 Corresponds to variant rs35795890 [ dbSNP | Ensembl ].		VAR_001775
	Natural variant	635	1	P → L. Ref.42		VAR_001776
	Natural variant	636	1	G → R in EDS4.		VAR_011124
	Natural variant	657	1	G → E in EDS4.		VAR_011125
	Natural variant	660	1	G → D in EDS4.		VAR_011126
	Natural variant	666	1	G → D in EDS4. Ref.50		VAR_001777
	Natural variant	668	1	P → T. Ref.27 Corresponds to variant rs1801183 [ dbSNP | Ensembl ].		VAR_011127
	Natural variant	679	1	A → T. Ref.62 Corresponds to variant rs41263773 [ dbSNP | Ensembl ].		VAR_055666
	Natural variant	686	1	P → A. Corresponds to variant rs41263775 [ dbSNP | Ensembl ].		VAR_055667
	Natural variant	698	1	A → T. Ref.28 Ref.62 Corresponds to variant rs1800255 [ dbSNP | Ensembl ].		VAR_001778
	Natural variant	699	1	G → R in EDS4.		VAR_011128
	Natural variant	726	1	G → R in EDS4. Ref.53		VAR_001779
	Natural variant	738	1	G → S in EDS4.		VAR_011129
	Natural variant	738	1	G → V in EDS4.		VAR_011130
	Natural variant	744	1	G → V in EDS4.		VAR_011131
	Natural variant	756	1	G → E in EDS4. Ref.43		VAR_001780
	Natural variant	762	1	G → C in EDS4. Ref.48		VAR_001781
	Natural variant	786	1	G → R in AAA. Ref.29 Ref.36		VAR_001782
	Natural variant	804	1	G → S in EDS3. Ref.44		VAR_001783
	Natural variant	828	1	G → R in EDS4. Ref.31		VAR_001784
	Natural variant	828	1	G → W in EDS4.		VAR_011132
	Natural variant	830 – 838	9	Missing in EDS4.		VAR_037008
	Natural variant	852	1	G → C in EDS4.		VAR_011133
	Natural variant	879	1	G → V in EDS4.		VAR_011134
	Natural variant	882	1	G → D in EDS4.		VAR_011135
	Natural variant	900	1	G → D in EDS4.		VAR_011136
	Natural variant	903	1	G → E in EDS4.		VAR_011137
	Natural variant	909	1	G → D in EDS4. Ref.47		VAR_001785
	Natural variant	909	1	G → V in EDS4.		VAR_011138
	Natural variant	918	1	G → E in EDS4.		VAR_011139
	Natural variant	924	1	G → C in EDS4.		VAR_011140
	Natural variant	936	1	G → R in EDS4. Ref.46 Ref.52		VAR_001786
	Natural variant	936	1	G → S in EDS4.		VAR_001787
	Natural variant	939	1	G → D in EDS4. Ref.47		VAR_001788
	Natural variant	942	1	G → E in EDS4.		VAR_011141
	Natural variant	957	1	G → S in EDS4; severe variant. Ref.32		VAR_001789
	Natural variant	960	1	G → V in EDS4; severe variant. Ref.33		VAR_001790
	Natural variant	966	1	G → V in EDS4.		VAR_011142
	Natural variant	972	1	G → A in EDS4.		VAR_011143
	Natural variant	984	1	G → T in EDS4; requires 2 nucleotide substitutions.		VAR_011144
	Natural variant	996	1	G → E in EDS4. Ref.46		VAR_001791
	Natural variant	999	1	G → R in EDS4.		VAR_011145
	Natural variant	1011	1	G → E in EDS4.		VAR_011146
	Natural variant	1014	1	G → E in EDS4. Ref.34		VAR_001792
	Natural variant	1032	1	G → V in EDS4.		VAR_011147
	Natural variant	1035	1	G → C in EDS4.		VAR_011148
	Natural variant	1044	1	G → D in EDS4. Ref.57		VAR_011149
	Natural variant	1050	1	G → D in EDS4; mild variant. Ref.35		VAR_001793
	Natural variant	1050	1	G → V in EDS4. Ref.60		VAR_011150
	Natural variant	1071	1	G → V in EDS4. Ref.46		VAR_001794
	Natural variant	1077	1	G → V in EDS4. Ref.37		VAR_001795
	Natural variant	1089	1	G → D in EDS4.		VAR_011151
	Natural variant	1098	1	G → D in EDS4. Ref.55		VAR_011152
	Natural variant	1098	1	G → V in EDS4.		VAR_011153
	Natural variant	1101	1	G → E in EDS4. Ref.49		VAR_001796
	Natural variant	1104	1	G → A in EDS4. Ref.46		VAR_001797
	Natural variant	1161	1	G → V in EDS4.		VAR_011154
	Natural variant	1164	1	G → E in EDS4.		VAR_011155
	Natural variant	1164	1	G → R in EDS4.		VAR_011156
	Natural variant	1164	1	G → S in spondyloepiphyseal dysplasia.		VAR_001798
	Natural variant	1167	1	G → V in EDS4. Ref.41		VAR_001799
	Natural variant	1170	1	G → D in EDS4. Ref.41 Ref.48		VAR_001800
	Natural variant	1170	1	G → V in EDS4.		VAR_011157
	Natural variant	1173	1	G → E in EDS4. Ref.38 Ref.41 Ref.55		VAR_001801
	Natural variant	1173	1	G → R in EDS4; Gottron type acrogeria. Ref.54		VAR_011158
	Natural variant	1176	1	G → V in EDS4; severe. Ref.45		VAR_001802
	Natural variant	1179	1	G → R in EDS4.		VAR_011159
	Natural variant	1182	1	G → E in EDS4. Ref.46		VAR_001803
	Natural variant	1185	1	G → D in EDS4; severe variant. Ref.39		VAR_001804
	Natural variant	1185	1	G → V in EDS4. Ref.46		VAR_001805
	Natural variant	1188	1	G → E in EDS4; severe variant. Ref.40 Ref.46		VAR_001806
	Natural variant	1188	1	G → R in EDS4. Ref.46		VAR_001807
	Natural variant	1205	1	I → V. Ref.62 Corresponds to variant rs2271683 [ dbSNP | Ensembl ].		VAR_020012
	Natural variant	1353	1	H → Q. Ref.1 Ref.2 Ref.5 Ref.18 Ref.41 Ref.62 Corresponds to variant rs1516446 [ dbSNP | Ensembl ].		VAR_030115
	Natural variant	1434	1	R → C in a colorectal cancer sample; somatic mutation. Ref.61		VAR_035739
Experimental info
	Sequence conflict	163	1	G → GG in CAA33387. Ref.8
	Sequence conflict	168	1	G → V AA sequence Ref.9
	Sequence conflict	226 – 228	3	Missing AA sequence Ref.9
	Sequence conflict	241	1	E → D in CAA33387. Ref.8
	Sequence conflict	278	1	T → A AA sequence Ref.9
	Sequence conflict	293 – 295	3	NGA → DGS AA sequence Ref.9
	Sequence conflict	401	1	A → L AA sequence Ref.13
	Sequence conflict	409	1	L → P AA sequence Ref.13
	Sequence conflict	472	1	E → D in CAA33387. Ref.8
	Sequence conflict	488 – 490	3	PGF → LGS in CAA33387. Ref.8
	Sequence conflict	589	1	A → E AA sequence Ref.13
	Sequence conflict	614	1	T → Y in CAA33387. Ref.8
	Sequence conflict	635	1	P → R in CAA33387. Ref.8
	Sequence conflict	664	1	D → E in CAA33387. Ref.8
	Sequence conflict	676	1	D → N AA sequence Ref.14
	Sequence conflict	803	1	T → P AA sequence Ref.13
	Sequence conflict	896	1	S → A AA sequence Ref.16
	Sequence conflict	980	1	S → A AA sequence Ref.20
	Sequence conflict	985 – 989	5	ANGLS → PSGQN AA sequence Ref.20
	Sequence conflict	1019	1	D → Y in CAA29886. Ref.18
	Sequence conflict	1067	1	S → P AA sequence Ref.13
	Sequence conflict	1070	1	A → P AA sequence Ref.13
	Sequence conflict	1097	1	T → P AA sequence Ref.20
	Sequence conflict	1153 – 1154	2	TS → AT AA sequence Ref.20
	Sequence conflict	1156	1	H → S AA sequence Ref.20
	Sequence conflict	1184	1	P → S in CAA33387. Ref.8
	Sequence conflict	1203	1	A → P in CAA33387. Ref.8
	Sequence conflict	1210	1	G → A in CAA33387. Ref.8
	Sequence conflict	1241	1	V → A in CAA29886. Ref.18
	Sequence conflict	1241	1	V → A in CAA25879. Ref.21
	Sequence conflict	1357	1	L → P no nucleotide entry Ref.24

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: B904B4E05E17D339	FASTA	1,466	138,564
	10 20 30 40 50 60 MMSFVQKGSW LLLALLHPTI ILAQQEAVEG GCSHLGQSYA DRDVWKPEPC QICVCDSGSV 70 80 90 100 110 120 LCDDIICDDQ ELDCPNPEIP FGECCAVCPQ PPTAPTRPPN GQGPQGPKGD PGPPGIPGRN 130 140 150 160 170 180 GDPGIPGQPG SPGSPGPPGI CESCPTGPQN YSPQYDSYDV KSGVAVGGLA GYPGPAGPPG 190 200 210 220 230 240 PPGPPGTSGH PGSPGSPGYQ GPPGEPGQAG PSGPPGPPGA IGPSGPAGKD GESGRPGRPG 250 260 270 280 290 300 ERGLPGPPGI KGPAGIPGFP GMKGHRGFDG RNGEKGETGA PGLKGENGLP GENGAPGPMG 310 320 330 340 350 360 PRGAPGERGR PGLPGAAGAR GNDGARGSDG QPGPPGPPGT AGFPGSPGAK GEVGPAGSPG 370 380 390 400 410 420 SNGAPGQRGE PGPQGHAGAQ GPPGPPGING SPGGKGEMGP AGIPGAPGLM GARGPPGPAG 430 440 450 460 470 480 ANGAPGLRGG AGEPGKNGAK GEPGPRGERG EAGIPGVPGA KGEDGKDGSP GEPGANGLPG 490 500 510 520 530 540 AAGERGAPGF RGPAGPNGIP GEKGPAGERG APGPAGPRGA AGEPGRDGVP GGPGMRGMPG 550 560 570 580 590 600 SPGGPGSDGK PGPPGSQGES GRPGPPGPSG PRGQPGVMGF PGPKGNDGAP GKNGERGGPG 610 620 630 640 650 660 GPGPQGPPGK NGETGPQGPP GPTGPGGDKG DTGPPGPQGL QGLPGTGGPP GENGKPGEPG 670 680 690 700 710 720 PKGDAGAPGA PGGKGDAGAP GERGPPGLAG APGLRGGAGP PGPEGGKGAA GPPGPPGAAG 730 740 750 760 770 780 TPGLQGMPGE RGGLGSPGPK GDKGEPGGPG ADGVPGKDGP RGPTGPIGPP GPAGQPGDKG 790 800 810 820 830 840 EGGAPGLPGI AGPRGSPGER GETGPPGPAG FPGAPGQNGE PGGKGERGAP GEKGEGGPPG 850 860 870 880 890 900 VAGPPGGSGP AGPPGPQGVK GERGSPGGPG AAGFPGARGL PGPPGSNGNP GPPGPSGSPG 910 920 930 940 950 960 KDGPPGPAGN TGAPGSPGVS GPKGDAGQPG EKGSPGAQGP PGAPGPLGIA GITGARGLAG 970 980 990 1000 1010 1020 PPGMPGPRGS PGPQGVKGES GKPGANGLSG ERGPPGPQGL PGLAGTAGEP GRDGNPGSDG 1030 1040 1050 1060 1070 1080 LPGRDGSPGG KGDRGENGSP GAPGAPGHPG PPGPVGPAGK SGDRGESGPA GPAGAPGPAG 1090 1100 1110 1120 1130 1140 SRGAPGPQGP RGDKGETGER GAAGIKGHRG FPGNPGAPGS PGPAGQQGAI GSPGPAGPRG 1150 1160 1170 1180 1190 1200 PVGPSGPPGK DGTSGHPGPI GPPGPRGNRG ERGSEGSPGH PGQPGPPGPP GAPGPCCGGV 1210 1220 1230 1240 1250 1260 GAAAIAGIGG EKAGGFAPYY GDEPMDFKIN TDEIMTSLKS VNGQIESLIS PDGSRKNPAR 1270 1280 1290 1300 1310 1320 NCRDLKFCHP ELKSGEYWVD PNQGCKLDAI KVFCNMETGE TCISANPLNV PRKHWWTDSS 1330 1340 1350 1360 1370 1380 AEKKHVWFGE SMDGGFQFSY GNPELPEDVL DVHLAFLRLL SSRASQNITY HCKNSIAYMD 1390 1400 1410 1420 1430 1440 QASGNVKKAL KLMGSNEGEF KAEGNSKFTY TVLEDGCTKH TGEWSKTVFE YRTRKAVRLP 1450 1460 IVDIAPYDIG GPDQEFGVDV GPVCFL
	Isoform 2 [UniParc]. Checksum: BE06E5CA84FBB829	FASTA	1,163	111,907
	10 20 30 40 50 60 MMSFVQKGSW LLLALLHPTI ILAQQEAVEG GCSHLGQSYA DRDVWKPEPC QICVCDSGSV 70 80 90 100 110 120 LCDDIICDDQ ELDCPNPEIP FGECCAVCPQ PPTAPTRPPN GQGPQGPKGD PGPPGIPGRN 130 140 150 160 170 180 GDPGIPGQPG SPGSPGPPGI CESCPTGPQN YSPQYDSYDV KSGVAVGGLA GYPGPAGPPG 190 200 210 220 230 240 PPGPPGTSGH PGSPGSPGYQ GPPGEPGQAG PSGPPGPPGA IGPSGPAGKD GESGRPGRPG 250 260 270 280 290 300 ERGLPGPPGI KGPAGIPGFP GMKGHRGFDG RNGEKGETGA PGLKGENGLP GENGAPGPMG 310 320 330 340 350 360 PRGAPGERGR PGLPGAAGAR GNDGARGSDG QPGPPGPPGT AGFPGSPGAK GEVGPAGSPG 370 380 390 400 410 420 SNGAPGQRGE PGPQGHAGAQ GPPGPPGING SPGGKGEMGP AGIPGAPGLM GARGPPGPAG 430 440 450 460 470 480 ANGAPGLRGG AGEPGKNGAK GEPGPRGERG EAGIPGVPGA KGEDGKDGSP GEPGANGLPG 490 500 510 520 530 540 AAGERGAPGF RGPAGPNGIP GEKGPAGERG APGPAGPRGA AGEPGRDGVP GGPGMRGMPG 550 560 570 580 590 600 SPGGPGSDGK PGPPGSQGES GRPGPPGPSG PRGQPGVMGF PGPKGNDGAP GKNGERGGPG 610 620 630 640 650 660 GPGPQGPPGK NGETGPQGPP GPTGPGGDKG DTGPPGPQGL QGLPGTGGPP GENGKPGEPG 670 680 690 700 710 720 PKGDAGAPGA PGGKGDAGAP GERGPPGLAG APGLRGGAGP PGPEGGKGAA GPPGPPGAAG 730 740 750 760 770 780 TPGLQGMPGE RGGLGSPGPK GDKGEPGGPG ADGVPGKDGP RGPTGPIGPP GPAGQPGDKG 790 800 810 820 830 840 EGGAPGLPGI AGPRGSPGER GETGPPGPAG FPGAPGQNGE PGGKGERGAP GEKGEGGPPG 850 860 870 880 890 900 VAGPPGKDGT SGHPGPIGPP GPRGNRGERG SEGSPGHPGQ PGPPGPPGAP GPCCGGVGAA 910 920 930 940 950 960 AIAGIGGEKA GGFAPYYGDE PMDFKINTDE IMTSLKSVNG QIESLISPDG SRKNPARNCR 970 980 990 1000 1010 1020 DLKFCHPELK SGEYWVDPNQ GCKLDAIKVF CNMETGETCI SANPLNVPRK HWWTDSSAEK 1030 1040 1050 1060 1070 1080 KHVWFGESMD GGFQFSYGNP ELPEDVLDVH LAFLRLLSSR ASQNITYHCK NSIAYMDQAS 1090 1100 1110 1120 1130 1140 GNVKKALKLM GSNEGEFKAE GNSKFTYTVL EDGCTKHTGE WSKTVFEYRT RKAVRLPIVD 1150 1160 IAPYDIGGPD QEFGVDVGPV CFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of cDNA clones coding for the entire prepro alpha 1 (III) chain of human type III procollagen. Differences in protein structure from type I procollagen and conservation of codon preferences." Ala-Kokko L., Kontusaari S., Baldwin C.T., Kuivaniemi H., Prockop D.J. Biochem. J. 260:509-516(1989) [PubMed: 2764886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-1353. Tissue: Skin fibroblast.
[2]	"Genomic organization of the human COL3A1 and COL5A2 genes: COL5A2 has evolved differently than the other minor fibrillar collagen genes." Valkkila M., Melkoniemi M., Kvist L., Kuivaniemi H., Tromp G., Ala-Kokko L. Matrix Biol. 20:357-366(2001) [PubMed: 11566270] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT GLN-1353.
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-1353.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLN-1353. Tissue: Liver.
[6]	"Cloning and analysis of the 5' portion of the human type-III procollagen gene (COL3A1)." Benson-Chanda V., Su M.W., Weil D., Chu M.-L., Ramirez F. Gene 78:255-265(1989) [PubMed: 2777083] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176.
[7]	"Nucleotide sequence of a cDNA coding for the amino-terminal region of human prepro alpha 1(III) collagen." Toman D., Ricca G., de Crombrugghe B. Nucleic Acids Res. 16:7201-7201(1988) [PubMed: 3405773] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-170 (ISOFORMS 1/2). Tissue: Placenta.
[8]	"Nucleotide and amino acid sequences of the entire human alpha 1 (III) collagen." Janeczko R.A., Ramirez F. Nucleic Acids Res. 17:6742-6742(1989) [PubMed: 2780304] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 149-1225 (ISOFORM 1).
[9]	"Covalent structure of collagen: amino acid sequence of cyanogen bromide peptides from the amino-terminal segment of type III collagen of human liver." Seyer J.M., Kang A.H. Biochemistry 16:1158-1164(1977) [PubMed: 557335] [Abstract] Cited for: PROTEIN SEQUENCE OF 168-398.
[10]	Seyer J.M. Submitted (DEC-1977) to the PIR data bank Cited for: SEQUENCE REVISION.
[11]	"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." Milewicz D.M., Witz A.M., Smith A.C., Manchester D.K., Waldstein G., Byers P.H. Am. J. Hum. Genet. 53:62-70(1993) [PubMed: 8317500] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 186-194 (ISOFORMS 1/2).
[12]	"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." Chiodo A.A., Sillence D.O., Cole W.G., Bateman J.F. Biochem. J. 311:939-943(1995) [PubMed: 7487954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 302-423 (ISOFORMS 1/2).
[13]	"Onco-fetal/laminin-binding collagen from colon carcinoma: detection of new sequences." Minafra I.P., Andriolo M., Basirico L., Aquino A., Minafra S., Boutillon M.-M., van der Rest M. Biochem. Biophys. Res. Commun. 207:852-859(1995) [PubMed: 7864881] [Abstract] Cited for: PROTEIN SEQUENCE OF 395-416; 579-595; 800-814 AND 1064-1079. Tissue: Colon carcinoma.
[14]	"Covalent structure of collagen: amino acid sequence of five consecutive CNBr peptides from type III collagen of human liver." Seyer J.M., Kang A.H. Biochemistry 17:3404-3411(1978) [PubMed: 687591] [Abstract] Cited for: PROTEIN SEQUENCE OF 399-727.
[15]	"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." Lee B., Vitale E., Superti-Furga A., Steinmann B., Ramirez F. J. Biol. Chem. 266:5256-5259(1991) [PubMed: 1672129] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 537-605.
[16]	"Covalent structure of collagen: amino acid sequence of alpha 1 (III)-CB5 from type III collagen of human liver." Seyer J.M., Mainardi C., Kang A.H. Biochemistry 19:1583-1589(1980) [PubMed: 6246925] [Abstract] Cited for: PROTEIN SEQUENCE OF 728-964.
[17]	"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." Cole W.G., Chiodo A.A., Lamande S.R., Janeczko R., Ramirez F., Dahl H.-H.M., Chan D., Bateman J.F. J. Biol. Chem. 265:17070-17077(1990) [PubMed: 2145268] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 861-1015 (ISOFORM 1).
[18]	"Human pro alpha 1(III) collagen: cDNA sequence for the 3' end." Mankoo B.S., Dalgleish R. Nucleic Acids Res. 16:2337-2337(1988) [PubMed: 3357782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 950-1466 (ISOFORM 1), VARIANT GLN-1353.
[19]	"Human type III collagen 'variant' is a cDNA cloning artefact." Molyneux K., Dalgleish R. Nucleic Acids Res. 16:11833-11833(1988) [PubMed: 3211760] [Abstract] Cited for: SEQUENCE REVISION TO 1184.
[20]	"Covalent structure of collagen: amino acid sequence of alpha 1(III)-CB9 from type III collagen of human liver." Seyer J.M., Kang A.H. Biochemistry 20:2621-2627(1981) [PubMed: 7016180] [Abstract] Cited for: PROTEIN SEQUENCE OF 965-1200.
[21]	"Molecular cloning and carboxyl-propeptide analysis of human type III procollagen." Loidl H.R., Brinker J.M., May M., Pihlajaniemi T., Morrow S., Rosenbloom J., Myers J.C. Nucleic Acids Res. 12:9383-9394(1984) [PubMed: 6096827] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1065-1466 (ISOFORM 1).
[22]	"Human type III collagen gene expression is coordinately modulated with the type I collagen genes during fibroblast growth." Miskulin M., Dalgleish R., Kluve-Beckerman B., Rennard S.I., Tolstoshev P., Brantly M., Crystal R.G. Biochemistry 25:1408-1413(1986) [PubMed: 3754462] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1161-1200 (ISOFORMS 1/2).
[23]	"Human alpha 1(III) and alpha 2(V) procollagen genes are located on the long arm of chromosome 2." Emanuel B.S., Cannizzaro L.A., Seyer J.M., Myers J.C. Proc. Natl. Acad. Sci. U.S.A. 82:3385-3389(1985) [PubMed: 3858826] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1165-1196 (ISOFORMS 1/2).
[24]	"Isolation of cDNA and genomic clones encoding human pro-alpha 1 (III) collagen. Partial characterization of the 3' end region of the gene." Chu M.-L., Weil D., de Wet W.J., Bernard M.P., Sippola M., Ramirez F. J. Biol. Chem. 260:4357-4363(1985) [PubMed: 2579949] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1176-1466 (ISOFORMS 1/2).
[25]	"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." Kuivaniemi H., Tromp G., Prockop D.J. Hum. Mutat. 9:300-315(1997) [PubMed: 9101290] [Abstract] Cited for: REVIEW ON VARIANTS.
[26]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1378 AND SER-1383, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[27]	"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." Tromp G., Wu Y., Prockop D.J., Madhatheri S.L., Kleinert C., Earley J.J., Zhuang J., Noerrgaard O., Darling R.C., Abbott W.M., Cole C.W., Jaakkola P., Ryynaenen M., Pearce W.H., Yao J.S.T., Majamaa K., Smullens S.N., Gatalica Z. , Ferrell R.E., Jimenez S.A., Jackson C.E., Michels V.V., Kaye M., Kuivaniemi H. J. Clin. Invest. 91:2539-2545(1993) [PubMed: 8514866] [Abstract] Cited for: VARIANT AAA ARG-303, VARIANT THR-668.
[28]	"G to A polymorphism in exon 31 of the COL3A1 gene." Zafarullah K., Kleinert C., Tromp G., Kuivaniemi H., Kontusaari S., Wu Y., Ganguly A., Prockop D.J. Nucleic Acids Res. 18:6180-6180(1990) [PubMed: 2235526] [Abstract] Cited for: VARIANT THR-698.
[29]	"A mutation in the gene for type III procollagen (COL3A1) in a family with aortic aneurysms." Kontusaari S., Tromp G., Kuivaniemi H., Romanic A.M., Prockop D.J. J. Clin. Invest. 86:1465-1473(1990) [PubMed: 2243125] [Abstract] Cited for: VARIANT AAA ARG-786.
[30]	"A 27-bp deletion from one allele of the type III collagen gene (COL3A1) in a large family with Ehlers-Danlos syndrome type IV." Richards A.J., Lloyd J.C., Narcisi P., Ward P.N., Nicholls A.C., De Paepe A., Pope F.M. Hum. Genet. 88:325-330(1992) [PubMed: 1370809] [Abstract] Cited for: VARIANT EDS4 830-PRO--PRO-838 DEL.
[31]	"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." Richards A.J., Narcisi P., Lloyd J.C., Ferguson C., Pope F.M. J. Med. Genet. 30:690-693(1993) [PubMed: 8411057] [Abstract] Cited for: VARIANT EDS4 ARG-828.
[32]	"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." Tromp G., Kuivaniemi H., Shikata H., Prockop D.J. J. Biol. Chem. 264:1349-1352(1989) [PubMed: 2492273] [Abstract] Cited for: VARIANT EDS4 SER-957.
[33]	"Substitution of valine for glycine 793 in type III procollagen in Ehlers-Danlos syndrome type IV." Tromp G., de Paepe A., Nuytinck L., Madhatheri S.L., Kuivaniemi H. Hum. Mutat. 5:179-181(1995) [PubMed: 7749417] [Abstract] Cited for: VARIANT EDS4 VAL-960.
[34]	"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." Richards A.J., Ward P.N., Narcisi P., Nicholls A.C., Lloyd J.C., Pope F.M. Hum. Genet. 89:414-418(1992) [PubMed: 1352273] [Abstract] Cited for: VARIANT EDS4 GLU-1014.
[35]	"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." Tromp G., Kuivaniemi H., Stolle C.A., Pope F.M., Prockop D.J. J. Biol. Chem. 264:19313-19317(1989) [PubMed: 2808425] [Abstract] Cited for: VARIANT EDS4 ASP-1050.
[36]	"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." Kontusaari S., Tromp G., Kuivaniemi H., Ladda R.L., Prockop D.J. Am. J. Hum. Genet. 47:112-120(1990) [PubMed: 2349939] [Abstract] Cited for: VARIANT AAA ARG-786.
[37]	"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." Richards A.J., Lloyd J.C., Ward P.N., de Paepe A., Narcisi P., Pope F.M. J. Med. Genet. 28:458-463(1991) [PubMed: 1895316] [Abstract] Cited for: VARIANT EDS4 VAL-1077.
[38]	"A COL3A1 glycine 1006 to glutamic acid substitution in a patient with Ehlers-Danlos syndrome type IV detected by denaturing gradient gel electrophoresis." Johnson P.H., Richards A.J., Pope F.M., Hopkinson D.A. J. Inherit. Metab. Dis. 15:426-430(1992) [PubMed: 1357232] [Abstract] Cited for: VARIANT EDS4 GLU-1173.
[39]	"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." Kontusaari S., Tromp G., Kuivaniemi H., Stolle C.A., Pope F.M., Prockop D.J. Am. J. Hum. Genet. 51:497-507(1992) [PubMed: 1496983] [Abstract] Cited for: VARIANT EDS4 ASP-1185.
[40]	"Single base mutation that substitutes glutamic acid for glycine 1021 in the COL3A1 gene and causes Ehlers-Danlos syndrome type IV." Narcisi P., Wu Y., Tromp G., Earley J.J., Richards A.J., Pope F.M., Kuivaniemi H. Am. J. Med. Genet. 46:278-283(1993) [PubMed: 8098182] [Abstract] Cited for: VARIANT EDS4 GLU-1188.
[41]	"Substitution of glycines 1000, 1003 and 1006 in type III collagen all cause the acrogeric form of EDS-IV, and destabilise the collagen triple helix." Richards A.J., Narcisi P., Lloyd J.C., Johnson P.H., Hopkinson D.A., Pope F.M. Matrix 13:47-47(1993) Cited for: VARIANTS EDS4 VAL-1167; ASP-1170 AND GLU-1173.
[42]	"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." Kuivaniemi H., Prockop D.J., Wu Y., Madhatheri S.L., Kleinert C., Earley J.J., Jokinen A., Stolle C.A., Majamaa K., Mylllylae V.V., Noerrgaard O., Schievink W.I., Mokri B., Fukawa O., Ter Berg J.W.M., de Paepe A., Lozano A.M., Leblanc R. , Ryynaenen M., Baxter B.T., Shikata H., Ferrell R.E., Tromp G. Neurology 43:2652-2658(1993) [PubMed: 8255472] [Abstract] Cited for: VARIANTS THR-602 AND LEU-635.
[43]	"Substitution of glutamic acid for glycine 589 in the triple-helical domain of type III procollagen (COL3A1) in a family with variable phenotype of the Ehlers-Danlos syndrome type IV." Madhatheri S.L., Tromp G., Gustavson K.H., Kuivaniemi H. Hum. Mol. Genet. 3:511-512(1994) [PubMed: 7912131] [Abstract] Cited for: VARIANT EDS4 GLU-756.
[44]	"A family with Ehlers-Danlos syndrome type III/articular hypermobility syndrome has a glycine 637-to-serine substitution in type III collagen." Narcisi P., Richards A.J., Ferguson S.D., Pope F.M. Hum. Mol. Genet. 3:1617-1620(1994) [PubMed: 7833919] [Abstract] Cited for: VARIANT EDS3 SER-804.
[45]	"Single-strand conformation polymorphism (SSCP) analysis of the COL3A1 gene detects a mutation that results in the substitution of glycine 1009 to valine and causes severe Ehlers-Danlos syndrome type IV." Nuytinck L., De Paepe A., Renard J.P., Adriaens F., Leroy J. Hum. Mutat. 3:268-274(1994) [PubMed: 8019562] [Abstract] Cited for: VARIANT EDS4 VAL-1176.
[46]	"Marked heterogeneity in COL3A1 mutations that produce the EDS type IV phenotype." Goldstein J.A., Schwarze U., Witz A., Byers P.H. Matrix Biol. 14:392-393(1994) Cited for: VARIANTS EDS4 CYS-183; ARG-201; GLU-228; ARG-540; ARG-936; GLU-996; VAL-1071; ALA-1104; GLU-1182; VAL-1185; GLU-1188 AND ARG-1188.
[47]	"Efficient strategy for the detection of mutations in acrogeric Ehlers-Danlos syndrome type IV." Johnson P.H., Richards A.J., Lloyd J.C., Pope F.M., Hopkinson D.A. Hum. Mutat. 6:336-342(1995) [PubMed: 8680408] [Abstract] Cited for: VARIANTS EDS4 ASP-909 AND ASP-939.
[48]	"Ehlers-Danlos syndrome type IV caused by Gly400Glu, Gly595Cys and Gly1003Asp substitutions in collagen III: clinical features, biochemical screening, and molecular confirmation." Mackay K., Raghunath M., Superti-Furga A., Steinmann B., Dalgleish R. Clin. Genet. 49:286-295(1996) [PubMed: 8884076] [Abstract] Cited for: VARIANTS EDS4 GLU-567; CYS-762 AND ASP-1170.
[49]	"Abnormal extracellular matrix in Ehlers-Danlos syndrome type IV due to the substitution of glycine 934 by glutamic acid in the triple helical domain of type III collagen." McGrory J., Weksberg R., Thorner P., Cole W.G. Clin. Genet. 50:442-445(1996) [PubMed: 9147870] [Abstract] Cited for: VARIANT EDS4 GLU-1101.
[50]	"A novel G499D substitution in the alpha 1(III) chain of type III collagen produces variable forms of Ehlers-Danlos syndrome type IV." McGrory J., Costa T., Cole W.G. Hum. Mutat. 7:59-60(1996) [PubMed: 8664902] [Abstract] Cited for: VARIANT EDS4 ASP-666.
[51]	"A glycine (415)-to-serine substitution results in impaired secretion and decreased thermal stability of type III procollagen in a patient with Ehlers-Danlos syndrome type IV." Anderson D.W., Thakker-Varia S., Tromp G., Kuivaniemi H., Stolle C.A. Hum. Mutat. 9:62-63(1997) [PubMed: 8990011] [Abstract] Cited for: VARIANT EDS4 SER-582.
[52]	"Mutations in the COL3A1 gene result in the Ehlers-Danlos syndrome type IV and alterations in the size and distribution of the major collagen fibrils of the dermis." Smith L.T., Schwarze U., Goldstein J., Byers P.H. J. Invest. Dermatol. 108:241-247(1997) [PubMed: 9036918] [Abstract] Cited for: VARIANTS EDS4 CYS-183; ARG-201; GLU-228; ARG-540 AND ARG-936.
[53]	"A type III collagen Gly559 to Arg helix mutation in Ehler's-Danlos syndrome type IV." Bateman J.F., Chiodo A.A., Weng Y.M., Chan D., Haan E. Hum. Mutat. Suppl. 1:S257-S259(1998) [PubMed: 9452103] [Abstract] Cited for: VARIANT EDS4 ARG-726.
[54]	"COL3A1 mutation leading to acrogeria (Gottron Type)." Jansen T., de Paepe A., Luytinck N., Plewig G. Br. J. Dermatol. 142:178-180(2000) [PubMed: 10819545] [Abstract] Cited for: VARIANT EDS-IV ARG-1173.
[55]	"Characterization of 11 new mutations in COL3A1 of individuals with Ehlers-Danlos syndrome type IV: preliminary comparison of RNase cleavage, EMC and DHPLC assays." Giunta C., Steinmann B. Hum. Mutat. 16:176-177(2000) [PubMed: 10923041] [Abstract] Cited for: VARIANTS EDS4 ASP-204; ASP-210; ARG-264; ASP-327; ASP-1098 AND GLU-1173.
[56]	"Clinical and genetic features of Ehlers-Danlos syndrome type IV, the vascular type." Pepin M., Schwarze U., Superti-Furga A., Byers P.H. N. Engl. J. Med. 342:673-680(2000) [PubMed: 10706896] [Abstract] Cited for: VARIANTS EDS4.
[57]	"Ehlers-Danlos syndrome type IV with a unique point mutation in COL3A1 and familial phenotype of myocardial infarction without organic coronary stenosis." Nishiyama Y., Nejima J., Watanabe A., Kotani E., Sakai N., Hatamochi A., Shinkai H., Kiuchi K., Tamura K., Shimada T., Takano T., Katayama Y. J. Intern. Med. 249:103-108(2001) [PubMed: 11168790] [Abstract] Cited for: VARIANT EDS4 ASP-1044.
[58]	"Ehlers-Danlos syndrome type IV: unusual congenital anomalies in a mother and son with a COL3A1 mutation and a normal collagen III protein profile." Kroes H.Y., Pals G., van Essen A.J. Clin. Genet. 63:224-227(2003) [PubMed: 12694234] [Abstract] Cited for: VARIANT EDS4 ARG-297.
[59]	Erratum Kroes H.Y., Pals G., van Essen A.J. Clin. Genet. 64:375-375(2003)
[60]	"Neurological presentation of Ehlers-Danlos syndrome type IV in a family with parental mosaicism." Palmeri S., Mari F., Meloni I., Malandrini A., Ariani F., Villanova M., Pompilio A., Schwarze U., Byers P.H., Renieri A. Clin. Genet. 63:510-515(2003) [PubMed: 12786757] [Abstract] Cited for: VARIANT EDS4 VAL-1050.
[61]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-420 AND CYS-1434.
[62]	"Natural variation in four human collagen genes across an ethnically diverse population." Chan T.F., Poon A., Basu A., Addleman N.R., Chen J., Phong A., Byers P.H., Klein T.E., Kwok P.Y. Genomics 91:307-314(2008) [PubMed: 18272325] [Abstract] Cited for: VARIANTS THR-679; THR-698; VAL-1205 AND GLN-1353.
+	Additional computationally mapped references.

Web resources

COL3A1

Collagen type III alpha-1 chain mutations

GeneReviews

Wikipedia

Type-III collagen entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X14420 mRNA. Translation: CAA32583.1.
AY054301, AY016295 Genomic DNA. Translation: AAL13167.1.
AC066694 Genomic DNA. Translation: AAY24164.1.
CH471058 Genomic DNA. Translation: EAX10910.1.
CH471058 Genomic DNA. Translation: EAX10911.1.
BC028178 mRNA. Translation: AAH28178.1.
M26939 Genomic DNA. Translation: AAA52040.1.
X07240 mRNA. Translation: CAA30229.1.
X15332 mRNA. Translation: CAA33387.1.
S62925 Genomic DNA. Translation: AAD13937.1.
S79877 mRNA. Translation: AAB35615.1.
M59312 Genomic DNA. Translation: AAA52041.1.
M59227 mRNA. Translation: AAB59383.1.
M55603 Genomic DNA. No translation available.
X06700 mRNA. Translation: CAA29886.1.
X01655 mRNA. Translation: CAA25821.1.
X01742 mRNA. Translation: CAA25879.1.
M13146 mRNA. Translation: AAA52003.1.
M11134 mRNA. Translation: AAA52004.1.

IPI

IPI00021033.
IPI00167087.

PIR

CGHU7L. S05272.

RefSeq

NP_000081.1. NM_000090.3.

UniGene

Hs.443625.
Hs.708235.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V53	X-ray	3.20	B/C/D	563-590	[»]
3DMW	X-ray	2.30	A/B/C	1158-1199	[»]

ProteinModelPortal

P02461.

SMR

P02461. Positions 28-94.

ModBase

Search...

Protein-protein interaction databases

IntAct

P02461. 17 interactions.

STRING

P02461.

PTM databases

PhosphoSite

P02461.

Polymorphism databases

DMDM

124056490.

2D gel databases

Siena-2DPAGE

P02461.

Proteomic databases

PRIDE

P02461.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000304636; ENSP00000304408; ENSG00000168542.

GeneID

1281.

KEGG

hsa:1281.

NMPDR

fig|9606.3.peg.19042.

UCSC

uc002uqj.1. human.

Organism-specific databases

CTD

1281.

GeneCards

GC02P189803.

HGNC

HGNC:2201. COL3A1.

HPA

CAB016766.
HPA007583.

MIM

100070. phenotype.
120180. gene.
130020. phenotype.
130050. phenotype.

neXtProt

NX_P02461.

Orphanet

2500. Acrogeria.
285. Ehlers-Danlos syndrome, hypermobile type.
286. Ehlers-Danlos syndrome, vascular type.
86. Familial abdominal aortic aneurysm.

PharmGKB

PA26716.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13929.

HOVERGEN

HBG004933.

InParanoid

P02461.

OMA

MSFVQKG.

OrthoDB

EOG4FTW1C.

PhylomeDB

P02461.

Enzyme and pathway databases

Pathway_Interaction_DB

endothelinpathway. Endothelins.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P02461.

Bgee

P02461.

Genevestigator

P02461.

GermOnline

ENSG00000168542. Homo sapiens.

Family and domain databases

InterPro

IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]

KO

K06236.

Pfam

PF01410. COLFI. 1 hit.
PF01391. Collagen. 10 hits.
PF00093. VWC. 1 hit.
[Graphical view]

ProDom

PD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]

PROSITE

PS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00048. Collagenase.
DB00039. Palifermin.

NextBio

5177.

SOURCE

Search...

Entry information

Entry name

CO3A1_HUMAN

Accession

Primary (citable) accession number: P02461
Secondary accession number(s): D3DPH4 , P78429, Q15112, Q16403, Q53S91, Q541P8, Q6LDB3, Q6LDJ2, Q6LDJ3, Q7KZ56, Q8N6U4, Q9UC88, Q9UC89, Q9UC90, Q9UC91

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 144 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.