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P12105 (CO3A1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(III) chain
Gene names
Name:COL3A1
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length1262 AA.
Sequence statusFragments.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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

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 By similarity.

Post-translational modification

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

Sequence similarities

Belongs to the fibrillar collagen family.

Contains 1 fibrillar collagen NC1 domain.

Contains 1 VWFC domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 150127N-terminal propeptide By similarity
PRO_0000005737
Chain151 – 1017867Collagen alpha-1(III) chain
PRO_0000005738
Propeptide1018 – 1262245C-terminal propeptide By similarity
PRO_0000005739

Regions

Domain29 – 8860VWFC
Domain1028 – 1262235Fibrillar collagen NC1
Region145 – 16420Nonhelical region (N-terminal)
Region165 – 994830Triple-helical region
Region995 – 10039Nonhelical region (C-terminal)

Sites

Metal binding10761Calcium By similarity
Metal binding10781Calcium By similarity
Metal binding10791Calcium; via carbonyl oxygen By similarity
Metal binding10811Calcium; via carbonyl oxygen By similarity
Metal binding10841Calcium By similarity

Amino acid modifications

Modified residue26215-hydroxylysine By similarity
Modified residue28315-hydroxylysine By similarity
Modified residue85915-hydroxylysine By similarity
Glycosylation11631N-linked (GlcNAc...) Potential
Disulfide bond994Interchain By similarity
Disulfide bond995Interchain By similarity
Disulfide bond1058 ↔ 1090 By similarity
Disulfide bond1064Interchain (with C-1285) By similarity
Disulfide bond1081Interchain (with C-1268) By similarity
Disulfide bond1098 ↔ 1260 By similarity
Disulfide bond1168 ↔ 1213 By similarity

Experimental info

Sequence conflict961E → K Ref.2
Sequence conflict8811G → R in CAA23689. Ref.3
Sequence conflict8841G → V in CAA23689. Ref.3
Sequence conflict9841L → V in CAA23690. Ref.3
Sequence conflict11321F → S in AAA18519. Ref.4
Non-adjacent residues886 – 8872
Non-adjacent residues922 – 9232

Sequences

Sequence LengthMass (Da)Tools
P12105 [UniParc].

Last modified August 29, 2001. Version 2.
Checksum: 96ABE7B2E9DEB43D

FASTA1,262121,249
        10         20         30         40         50         60 
MMSFVQKVSL FILAVFQPSV ILAQQDALGG CTHLGQEYAD RDVWKPEPCQ ICVCDSGSVL 

        70         80         90        100        110        120 
CDDIICDDQE LDCPNPEIPL GECCPVCPQT TPQPTELPYT QGPKGDPGSP GSPGRTGAPG 

       130        140        150        160        170        180 
PPGQPGSPGA PGPPGICQSC PSISGGSFSP QYDSYDVKAG SVGMGYPPQP ISGFPGPPGP 

       190        200        210        220        230        240 
SGPPGPPGHA GPPGSNGYQG PPGEPGQPGP SGPPGPAGMI GPAGPPGKDG EPGRPGRNGD 

       250        260        270        280        290        300 
RGIPGLPGHK GHPGMPGMPG MKGARGFDGK DGAKGDSGAP GPKGEAGQPG ANGSPGQPGP 

       310        320        330        340        350        360 
GGPTGERGRP GNPGGPGAHG KDGAPGTAGP LGPPGPPGTA GFPGSPGFKG EAGPPGPAGA 

       370        380        390        400        410        420 
SGNPGERGEP GPQGQAGPPG PQGPPGRAGS PGGKGEMGPS GIPGGPGPPG GRGLPGPPGT 

       430        440        450        460        470        480 
SGNPGAKGTP GEPGKNGAKG DPGPKGERGE NGTPGARGPP GEEGKRGANG EPGQNGVPGT 

       490        500        510        520        530        540 
PGERGSPGFR GLPGSNGLPG EKGPAGERGS PGPPGPSGPA GDRGQDGGPG LPGMRGLPGI 

       550        560        570        580        590        600 
PGSPGSDGKP GPPGNQGEPG RSGPPGPAGP RGQPGVMGFP GPKGNEGAPG KNGERGPGGP 

       610        620        630        640        650        660 
PGTPGPAGKN GDVGLPGPPG PAGPAGDRGE PGPSGSPGLQ GLPGGPGPAG ENGKPGEPGP 

       670        680        690        700        710        720 
KGDIGGPGFP GPKGENGIPG ERGPQGPPGP TGARGGPGPA GSEGAKGPPG PPGAPGGTGL 

       730        740        750        760        770        780 
PGLQGMPGER GASGSPGPKG DKGEPGGKGA DGLPGARGER GNVGPIGPPG PAGPPGDKGE 

       790        800        810        820        830        840 
TGPAGAPGPA GSRGGPGERG EQGLPGPAGF PGAPGQNGEP GGKGERGPPG LRGEAGPPGA 

       850        860        870        880        890        900 
AGPQGGPGAP GPPGPQGVKG ERGSPGGPGA AGFPGARGPP GPPGNNGDRG ESGPPGVPGP 

       910        920        930        940        950        960 
PGHPGPAGNN GAPGKAGERG FQGPLGPQGA IGSPGASGAR GPPGPAGPPG KDGRGGYPGP 

       970        980        990       1000       1010       1020 
IGPPGPRGNR GESGPAGPPG QPGLPGPSGP PGPCCGGGVA SLGAGEKGPV GYGYEYRDEP 

      1030       1040       1050       1060       1070       1080 
KENEINLGEI MSSMKSINNQ IENILSPDGS RKNPARNCRD LKFCHPELKS GEYWIDPNQG 

      1090       1100       1110       1120       1130       1140 
CKMDAIKVYC NMETGETCLS ANPATVPRKN WWTTESSGKK HVWFGESMKG GFQFSYGDPD 

      1150       1160       1170       1180       1190       1200 
LPEDVSEVQL AFLRILSSRA SQNITYHCKN SIAYMNQASG NVKKALKLMS SVETDIKAEG 

      1210       1220       1230       1240       1250       1260 
NSKYMYAVLE DGCTKHTGEW GKTVFEYRTR KTMRLPVVDI APIDIGGPDQ EFGVDVGPVC 


FL 

« Hide

References

[1]"An alternative transcript of the chick type III collagen gene that does not encode type III collagen."
Nah H.-D., Niu Z., Adams S.L.
J. Biol. Chem. 269:16443-16448(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-886.
Tissue: Kidney.
[2]"Conservation of the sizes for one but not another class of exons in two chick collagen genes."
Yamada Y., Liau G., Mudryj M., Obici S., de Crombrugghe B.
Nature 310:333-337(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-96; 332-397; 431-484; 503-535 AND 869-976.
[3]"Isolation and characterization of a genomic clone encoding chick alpha-1 type III collagen."
Yamada Y., Mudryj M., Sullivan M., de Crombrugghe B.
J. Biol. Chem. 258:2758-2761(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 869-886 AND 977-994.
[4]"A conserved nucleotide sequence, coding for a segment of the C-propeptide, is found at the same location in different collagen genes."
Yamada Y., Kuhn K., de Crombrugghe B.
Nucleic Acids Res. 11:2733-2744(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 977-1262.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U07973 mRNA. Translation: AAA83407.1.
X00822, X00823 Genomic DNA. Translation: CAB52686.1.
X00826, X00825 Genomic DNA. Translation: CAA25397.1. Sequence problems.
X00827 Genomic DNA. Translation: CAA25398.1.
X00828 Genomic DNA. Translation: CAA25399.1.
X00830 Genomic DNA. Translation: CAA25401.1.
X00831 Genomic DNA. Translation: CAA25402.1.
K02302 Genomic DNA. Translation: AAD15299.1.
K02301 Genomic DNA. Translation: AAD15298.1.
V00391 Genomic DNA. Translation: CAA23689.1.
V00392 Genomic DNA. Translation: CAA23690.1.
M36662 Unassigned DNA. Translation: AAA18519.1. Sequence problems.
PIRA05269.
I50694.
UniGeneGga.42140.

3D structure databases

ProteinModelPortalP12105.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbP12105.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG004933.

Enzyme and pathway databases

ReactomeREACT_196873. Extracellular matrix organization.

Family and domain databases

InterProIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 7 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

PROP12105.

Entry information

Entry nameCO3A1_CHICK
AccessionPrimary (citable) accession number: P12105
Secondary accession number(s): P79758 expand/collapse secondary AC list , P79759, Q90790, Q90791, Q90794, Q92029
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: August 29, 2001
Last modified: July 9, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families