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P02461 (CO3A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(III) chain
Gene names
Name:COL3A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Collagen 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.

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

Secretedextracellular spaceextracellular matrix By similarity.

Domain

The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function.

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

Ehlers-Danlos syndrome 3 (EDS3) [MIM:130020]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. It is a form of Ehlers-Danlos syndrome characterized by marked joint hyperextensibility without skeletal deformity.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.44

Ehlers-Danlos syndrome 4 (EDS4) [MIM:130050]: The most severe form of Ehlers-Danlos syndrome, a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. 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

Aortic aneurysm, familial abdominal (AAA) [MIM:100070]: 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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. 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 componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAortic aneurysm
Disease mutation
Ehlers-Danlos syndrome
   DomainCollagen
Repeat
Signal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

axon guidance

Traceable author statement. Source: Reactome

blood vessel development

Inferred from electronic annotation. Source: Ensembl

cell-matrix adhesion

Inferred from direct assay PubMed 16912226. Source: UniProtKB

cellular response to amino acid stimulus

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from sequence or structural similarity. Source: UniProtKB

collagen catabolic process

Traceable author statement. Source: Reactome

collagen fibril organization

Inferred from mutant phenotype PubMed 7546986Ref.52. Source: UniProtKB

digestive tract development

Inferred from electronic annotation. Source: Ensembl

extracellular fibril organization

Inferred from mutant phenotype PubMed 14970208. Source: UniProtKB

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

heart development

Inferred from mutant phenotype PubMed 7546986. Source: UniProtKB

integrin-mediated signaling pathway

Inferred from mutant phenotype PubMed 14970208. Source: UniProtKB

negative regulation of immune response

Inferred from mutant phenotype PubMed 16754721. Source: UniProtKB

negative regulation of neuron migration

Inferred from sequence or structural similarity. Source: UniProtKB

peptide cross-linking

Inferred from direct assay PubMed 16754721. Source: UniProtKB

platelet activation

Non-traceable author statement PubMed 9573018. Source: UniProtKB

positive regulation of Rho protein signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

response to cytokine

Inferred from direct assay PubMed 16360482PubMed 9076960. Source: UniProtKB

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to radiation

Inferred from direct assay PubMed 14736764. Source: UniProtKB

skeletal system development

Inferred from electronic annotation. Source: Ensembl

skin development

Inferred from mutant phenotype Ref.52. Source: UniProtKB

transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 16360482. Source: UniProtKB

wound healing

Inferred from direct assay PubMed 1466622. Source: UniProtKB

   Cellular_componentcollagen type III

Inferred from mutant phenotype PubMed 17576241Ref.12. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular matrix

Inferred from mutant phenotype PubMed 14970208Ref.12. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functionextracellular matrix structural constituent

Inferred from mutant phenotype Ref.12Ref.52. Source: UniProtKB

integrin binding

Inferred from mutant phenotype PubMed 9573018. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

platelet-derived growth factor binding

Inferred from direct assay PubMed 8900172. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AAEL010235O019492EBI-2431491,EBI-7685554From a different organism.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Propeptide24 – 153130N-terminal propeptide
PRO_0000005740
Chain154 – 12211068Collagen alpha-1(III) chain
PRO_0000005741
Propeptide1222 – 1466245C-terminal propeptide
PRO_0000005742

Regions

Domain30 – 8960VWFC
Domain1232 – 1466235Fibrillar collagen NC1
Region149 – 16719Nonhelical region (N-terminal)
Region168 – 11961029Triple-helical region
Region1197 – 12059Nonhelical region (C-terminal)

Sites

Metal binding12801Calcium
Metal binding12821Calcium
Metal binding12831Calcium; via carbonyl oxygen
Metal binding12851Calcium; via carbonyl oxygen
Metal binding12881Calcium

Amino acid modifications

Modified residue26315-hydroxylysine; alternate
Modified residue28415-hydroxylysine
Modified residue86015-hydroxylysine
Modified residue97715-hydroxylysine
Modified residue109415-hydroxylysine; partial
Modified residue110615-hydroxylysine
Glycosylation2631O-linked (Gal...); alternate
Disulfide bond1196Interchain Ref.26
Disulfide bond1197Interchain Ref.26
Disulfide bond1262 ↔ 1294 Ref.26
Disulfide bond1268Interchain (with C-1285) Ref.26
Disulfide bond1285Interchain (with C-1268) Ref.26
Disulfide bond1302 ↔ 1464 Ref.26
Disulfide bond1372 ↔ 1417 Ref.26

Natural variations

Alternative sequence847 – 1149303Missing in isoform 2.
VSP_022502
Natural variant1691L → F in AAA.
VAR_001767
Natural variant1831G → C in EDS4. Ref.46 Ref.52
VAR_001768
Natural variant1831G → D in EDS4.
VAR_011095
Natural variant1831G → S in EDS4.
VAR_011096
Natural variant1921G → V in EDS4.
VAR_011097
Natural variant2011G → R in EDS4. Ref.46 Ref.52
VAR_001769
Natural variant2041G → D in EDS4. Ref.55
VAR_011098
Natural variant2041G → S in EDS4.
VAR_011099
Natural variant2101G → D in EDS4. Ref.55
VAR_011100
Natural variant2191G → C in EDS4.
VAR_011101
Natural variant2251G → V in EDS4.
VAR_011102
Natural variant2281G → E in EDS4. Ref.46 Ref.52
VAR_001770
Natural variant2401G → R in EDS4.
VAR_011103
Natural variant2431G → V in EDS4.
VAR_011104
Natural variant2491G → D in EDS4.
VAR_011105
Natural variant2491G → V in EDS4.
VAR_011106
Natural variant2521G → D in EDS4.
VAR_011107
Natural variant2521G → R in EDS4.
VAR_011108
Natural variant2521G → V in EDS4.
VAR_011109
Natural variant2551G → V in EDS4.
VAR_011110
Natural variant2641G → R in EDS4. Ref.55
VAR_011111
Natural variant2671G → V in EDS4.
VAR_011112
Natural variant2971G → R in EDS4. Ref.58
VAR_037007
Natural variant3031G → R in fibromuscular dysplasia and aortic aneurysm. Ref.27
VAR_001771
Natural variant3211G → V in EDS4.
VAR_011113
Natural variant3271G → D in EDS4. Ref.55
VAR_011114
Natural variant3451G → R in EDS4.
VAR_011115
Natural variant4171G → R in EDS4.
VAR_011116
Natural variant4201G → S in a colorectal cancer sample; somatic mutation. Ref.61
VAR_035738
Natural variant4441G → R in EDS4.
VAR_011117
Natural variant4891G → E in EDS4.
VAR_011118
Natural variant5011G → R in EDS4.
VAR_011119
Natural variant5191G → V in EDS4.
VAR_011120
Natural variant5341G → E.
Corresponds to variant rs41263744 [ dbSNP | Ensembl ].
VAR_055665
Natural variant5401G → R in EDS4. Ref.46 Ref.52
VAR_001772
Natural variant5491G → E in EDS4.
VAR_011121
Natural variant5521G → E in EDS4.
VAR_011122
Natural variant5671G → E in EDS4. Ref.48
VAR_001773
Natural variant5821G → S in EDS4. Ref.51
VAR_001774
Natural variant5881G → D in EDS4.
VAR_011123
Natural variant6021P → T. Ref.42
Corresponds to variant rs35795890 [ dbSNP | Ensembl ].
VAR_001775
Natural variant6351P → L. Ref.42
VAR_001776
Natural variant6361G → R in EDS4.
VAR_011124
Natural variant6571G → E in EDS4.
VAR_011125
Natural variant6601G → D in EDS4.
VAR_011126
Natural variant6661G → D in EDS4. Ref.50
VAR_001777
Natural variant6681P → T. Ref.27
Corresponds to variant rs1801183 [ dbSNP | Ensembl ].
VAR_011127
Natural variant6791A → T. Ref.62
Corresponds to variant rs41263773 [ dbSNP | Ensembl ].
VAR_055666
Natural variant6861P → A.
Corresponds to variant rs41263775 [ dbSNP | Ensembl ].
VAR_055667
Natural variant6981A → T. Ref.28 Ref.62
Corresponds to variant rs1800255 [ dbSNP | Ensembl ].
VAR_001778
Natural variant6991G → R in EDS4.
VAR_011128
Natural variant7261G → R in EDS4. Ref.53
VAR_001779
Natural variant7381G → S in EDS4.
VAR_011129
Natural variant7381G → V in EDS4.
VAR_011130
Natural variant7441G → V in EDS4.
VAR_011131
Natural variant7561G → E in EDS4. Ref.43
VAR_001780
Natural variant7621G → C in EDS4. Ref.48
VAR_001781
Natural variant7861G → R in AAA. Ref.29 Ref.36
VAR_001782
Natural variant8041G → S in EDS3. Ref.44
VAR_001783
Natural variant8281G → R in EDS4. Ref.31
VAR_001784
Natural variant8281G → W in EDS4.
VAR_011132
Natural variant830 – 8389Missing in EDS4.
VAR_037008
Natural variant8521G → C in EDS4.
VAR_011133
Natural variant8791G → V in EDS4.
VAR_011134
Natural variant8821G → D in EDS4.
VAR_011135
Natural variant9001G → D in EDS4.
VAR_011136
Natural variant9031G → E in EDS4.
VAR_011137
Natural variant9091G → D in EDS4. Ref.47
VAR_001785
Natural variant9091G → V in EDS4.
VAR_011138
Natural variant9181G → E in EDS4.
VAR_011139
Natural variant9241G → C in EDS4.
VAR_011140
Natural variant9361G → R in EDS4. Ref.46 Ref.52
VAR_001786
Natural variant9361G → S in EDS4.
VAR_001787
Natural variant9391G → D in EDS4. Ref.47
VAR_001788
Natural variant9421G → E in EDS4.
VAR_011141
Natural variant9571G → S in EDS4; severe variant. Ref.32
VAR_001789
Natural variant9601G → V in EDS4; severe variant. Ref.33
VAR_001790
Natural variant9661G → V in EDS4.
VAR_011142
Natural variant9721G → A in EDS4.
VAR_011143
Natural variant9841G → T in EDS4; requires 2 nucleotide substitutions.
VAR_011144
Natural variant9961G → E in EDS4. Ref.46
VAR_001791
Natural variant9991G → R in EDS4.
VAR_011145
Natural variant10111G → E in EDS4.
VAR_011146
Natural variant10141G → E in EDS4. Ref.34
VAR_001792
Natural variant10321G → V in EDS4.
VAR_011147
Natural variant10351G → C in EDS4.
VAR_011148
Natural variant10441G → D in EDS4. Ref.57
VAR_011149
Natural variant10501G → D in EDS4; mild variant. Ref.35
VAR_001793
Natural variant10501G → V in EDS4. Ref.60
VAR_011150
Natural variant10711G → V in EDS4. Ref.46
VAR_001794
Natural variant10771G → V in EDS4. Ref.37
VAR_001795
Natural variant10891G → D in EDS4.
VAR_011151
Natural variant10981G → D in EDS4. Ref.55
VAR_011152
Natural variant10981G → V in EDS4.
VAR_011153
Natural variant11011G → E in EDS4. Ref.49
VAR_001796
Natural variant11041G → A in EDS4. Ref.46
VAR_001797
Natural variant11611G → V in EDS4.
VAR_011154
Natural variant11641G → E in EDS4.
VAR_011155
Natural variant11641G → R in EDS4.
VAR_011156
Natural variant11641G → S in spondyloepiphyseal dysplasia.
VAR_001798
Natural variant11671G → V in EDS4. Ref.41
VAR_001799
Natural variant11701G → D in EDS4. Ref.41 Ref.48
VAR_001800
Natural variant11701G → V in EDS4.
VAR_011157
Natural variant11731G → E in EDS4. Ref.38 Ref.41 Ref.55
VAR_001801
Natural variant11731G → R in EDS4; Gottron type acrogeria. Ref.54
VAR_011158
Natural variant11761G → V in EDS4; severe. Ref.45
VAR_001802
Natural variant11791G → R in EDS4.
VAR_011159
Natural variant11821G → E in EDS4. Ref.46
VAR_001803
Natural variant11851G → D in EDS4; severe variant. Ref.39
VAR_001804
Natural variant11851G → V in EDS4. Ref.46
VAR_001805
Natural variant11881G → E in EDS4; severe variant. Ref.40 Ref.46
VAR_001806
Natural variant11881G → R in EDS4. Ref.46
VAR_001807
Natural variant12051I → V. Ref.62
Corresponds to variant rs2271683 [ dbSNP | Ensembl ].
VAR_020012
Natural variant13531H → Q. Ref.1 Ref.2 Ref.5 Ref.18 Ref.41 Ref.62
Corresponds to variant rs1516446 [ dbSNP | Ensembl ].
VAR_030115
Natural variant14341R → C in a colorectal cancer sample; somatic mutation. Ref.61
VAR_035739

Experimental info

Sequence conflict1631G → GG in CAA33387. Ref.8
Sequence conflict1681G → V AA sequence Ref.9
Sequence conflict226 – 2283Missing AA sequence Ref.9
Sequence conflict2411E → D in CAA33387. Ref.8
Sequence conflict2781T → A AA sequence Ref.9
Sequence conflict293 – 2953NGA → DGS AA sequence Ref.9
Sequence conflict4011A → L AA sequence Ref.13
Sequence conflict4091L → P AA sequence Ref.13
Sequence conflict4721E → D in CAA33387. Ref.8
Sequence conflict488 – 4903PGF → LGS in CAA33387. Ref.8
Sequence conflict5891A → E AA sequence Ref.13
Sequence conflict6141T → Y in CAA33387. Ref.8
Sequence conflict6351P → R in CAA33387. Ref.8
Sequence conflict6641D → E in CAA33387. Ref.8
Sequence conflict6761D → N AA sequence Ref.14
Sequence conflict8031T → P AA sequence Ref.13
Sequence conflict8961S → A AA sequence Ref.16
Sequence conflict9801S → A AA sequence Ref.20
Sequence conflict985 – 9895ANGLS → PSGQN AA sequence Ref.20
Sequence conflict10191D → Y in CAA29886. Ref.18
Sequence conflict10671S → P AA sequence Ref.13
Sequence conflict10701A → P AA sequence Ref.13
Sequence conflict10971T → P AA sequence Ref.20
Sequence conflict1153 – 11542TS → AT AA sequence Ref.20
Sequence conflict11561H → S AA sequence Ref.20
Sequence conflict11841P → S in CAA33387. Ref.8
Sequence conflict12031A → P in CAA33387. Ref.8
Sequence conflict12101G → A in CAA33387. Ref.8
Sequence conflict12411V → A in CAA29886. Ref.18
Sequence conflict12411V → A in CAA25879. Ref.21
Sequence conflict13571L → P no nucleotide entry Ref.24

Secondary structure

................................................... 1466
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: B904B4E05E17D339

FASTA1,466138,564
        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 

« Hide

Isoform 2 [UniParc].

Checksum: BE06E5CA84FBB829
Show »

FASTA1,163111,907

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[26]"Structural basis of fibrillar collagen trimerization and related genetic disorders."
Bourhis J.M., Mariano N., Zhao Y., Harlos K., Exposito J.Y., Jones E.Y., Moali C., Aghajari N., Hulmes D.J.
Nat. Struct. Mol. Biol. 19:1031-1036(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1222-1466, PROPEPTIDE, DISULFIDE BONDS, CALCIUM-BINDING SITES.
[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. expand/collapse author list , Ferrell R.E., Jimenez S.A., Jackson C.E., Michels V.V., Kaye M., Kuivaniemi H.
J. Clin. Invest. 91:2539-2545(1993) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , Ryynaenen M., Baxter B.T., Shikata H., Ferrell R.E., Tromp G.
Neurology 43:2652-2658(1993) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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.
PIRCGHU7L. S05272.
RefSeqNP_000081.1. NM_000090.3.
UniGeneHs.443625.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V53X-ray3.20B/C/D563-590[»]
3DMWX-ray2.30A/B/C1158-1199[»]
4AE2X-ray1.68A/B/C1222-1466[»]
4AEJX-ray2.21A/B/C1222-1466[»]
4AK3X-ray3.50A1222-1466[»]
4GYXX-ray1.49A/B/C564-897[»]
ProteinModelPortalP02461.
SMRP02461. Positions 28-94, 240-278, 1249-1466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107678. 8 interactions.
DIPDIP-57177N.
IntActP02461. 19 interactions.
MINTMINT-7299332.

Chemistry

ChEMBLCHEMBL2364188.
DrugBankDB00048. Collagenase.
DB00039. Palifermin.

PTM databases

PhosphoSiteP02461.

Polymorphism databases

DMDM124056490.

Proteomic databases

PaxDbP02461.
PRIDEP02461.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304636; ENSP00000304408; ENSG00000168542. [P02461-1]
GeneID1281.
KEGGhsa:1281.
UCSCuc002uqj.1. human. [P02461-1]

Organism-specific databases

CTD1281.
GeneCardsGC02P189803.
HGNCHGNC:2201. COL3A1.
HPACAB016766.
HPA007583.
MIM100070. phenotype.
120180. gene.
130020. phenotype.
130050. phenotype.
neXtProtNX_P02461.
Orphanet2500. Acrogeria.
286. Ehlers-Danlos syndrome, vascular type.
86. Familial abdominal aortic aneurysm.
231160. Familial cerebral saccular aneurysm.
PharmGKBPA26716.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG004933.
InParanoidP02461.
KOK06236.
OMAPGPSGHQ.
OrthoDBEOG7TJ3HH.
PhylomeDBP02461.
TreeFamTF344135.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

ArrayExpressP02461.
BgeeP02461.
GenevestigatorP02461.

Family and domain databases

InterProIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 10 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL3A1. human.
EvolutionaryTraceP02461.
GeneWikiCollagen,_type_III,_alpha_1.
GenomeRNAi1281.
NextBio5177.
PROP02461.
SOURCESearch...

Entry information

Entry nameCO3A1_HUMAN
AccessionPrimary (citable) accession number: P02461
Secondary accession number(s): D3DPH4 expand/collapse secondary AC list , 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: April 16, 2014
This is version 166 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM