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P12105

- CO3A1_CHICK

UniProt

P12105 - CO3A1_CHICK

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Protein

Collagen alpha-1(III) chain

Gene

COL3A1

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Collagen type III occurs in most soft connective tissues along with type I collagen.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1076 – 10761CalciumBy similarity
Metal bindingi1078 – 10781CalciumBy similarity
Metal bindingi1079 – 10791Calcium; via carbonyl oxygenBy similarity
Metal bindingi1081 – 10811Calcium; via carbonyl oxygenBy similarity
Metal bindingi1084 – 10841CalciumBy similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: InterPro
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(III) chain
Gene namesi
Name:COL3A1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. extracellular region Source: Reactome
  3. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Propeptidei24 – 150127N-terminal propeptideBy similarityPRO_0000005737Add
BLAST
Chaini151 – 1017867Collagen alpha-1(III) chainPRO_0000005738Add
BLAST
Propeptidei1018 – 1262245C-terminal propeptideBy similarityPRO_0000005739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei262 – 26215-hydroxylysineBy similarity
Modified residuei283 – 28315-hydroxylysineBy similarity
Modified residuei859 – 85915-hydroxylysineBy similarity
Disulfide bondi994 – 994InterchainPROSITE-ProRule annotation
Disulfide bondi995 – 995InterchainPROSITE-ProRule annotation
Disulfide bondi1058 ↔ 1090PROSITE-ProRule annotation
Disulfide bondi1064 – 1064Interchain (with C-1285)PROSITE-ProRule annotation
Disulfide bondi1081 – 1081Interchain (with C-1268)PROSITE-ProRule annotation
Disulfide bondi1098 ↔ 1260PROSITE-ProRule annotation
Glycosylationi1163 – 11631N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1168 ↔ 1213PROSITE-ProRule annotation

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP12105.

Interactioni

Subunit structurei

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.

Structurei

3D structure databases

ProteinModelPortaliP12105.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 8860VWFCPROSITE-ProRule annotationAdd
BLAST
Domaini1028 – 1262235Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni145 – 16420Nonhelical region (N-terminal)Add
BLAST
Regioni165 – 994830Triple-helical regionAdd
BLAST
Regioni995 – 10039Nonhelical region (C-terminal)

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOVERGENiHBG004933.
InParanoidiP12105.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 7 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragments.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12105-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMSFVQKVSL FILAVFQPSV ILAQQDALGG CTHLGQEYAD RDVWKPEPCQ
60 70 80 90 100
ICVCDSGSVL CDDIICDDQE LDCPNPEIPL GECCPVCPQT TPQPTELPYT
110 120 130 140 150
QGPKGDPGSP GSPGRTGAPG PPGQPGSPGA PGPPGICQSC PSISGGSFSP
160 170 180 190 200
QYDSYDVKAG SVGMGYPPQP ISGFPGPPGP SGPPGPPGHA GPPGSNGYQG
210 220 230 240 250
PPGEPGQPGP SGPPGPAGMI GPAGPPGKDG EPGRPGRNGD RGIPGLPGHK
260 270 280 290 300
GHPGMPGMPG MKGARGFDGK DGAKGDSGAP GPKGEAGQPG ANGSPGQPGP
310 320 330 340 350
GGPTGERGRP GNPGGPGAHG KDGAPGTAGP LGPPGPPGTA GFPGSPGFKG
360 370 380 390 400
EAGPPGPAGA SGNPGERGEP GPQGQAGPPG PQGPPGRAGS PGGKGEMGPS
410 420 430 440 450
GIPGGPGPPG GRGLPGPPGT SGNPGAKGTP GEPGKNGAKG DPGPKGERGE
460 470 480 490 500
NGTPGARGPP GEEGKRGANG EPGQNGVPGT PGERGSPGFR GLPGSNGLPG
510 520 530 540 550
EKGPAGERGS PGPPGPSGPA GDRGQDGGPG LPGMRGLPGI PGSPGSDGKP
560 570 580 590 600
GPPGNQGEPG RSGPPGPAGP RGQPGVMGFP GPKGNEGAPG KNGERGPGGP
610 620 630 640 650
PGTPGPAGKN GDVGLPGPPG PAGPAGDRGE PGPSGSPGLQ GLPGGPGPAG
660 670 680 690 700
ENGKPGEPGP KGDIGGPGFP GPKGENGIPG ERGPQGPPGP TGARGGPGPA
710 720 730 740 750
GSEGAKGPPG PPGAPGGTGL PGLQGMPGER GASGSPGPKG DKGEPGGKGA
760 770 780 790 800
DGLPGARGER GNVGPIGPPG PAGPPGDKGE TGPAGAPGPA GSRGGPGERG
810 820 830 840 850
EQGLPGPAGF PGAPGQNGEP GGKGERGPPG LRGEAGPPGA AGPQGGPGAP
860 870 880 890 900
GPPGPQGVKG ERGSPGGPGA AGFPGARGPP GPPGNNGDRG ESGPPGVPGP
910 920 930 940 950
PGHPGPAGNN GAPGKAGERG FQGPLGPQGA IGSPGASGAR GPPGPAGPPG
960 970 980 990 1000
KDGRGGYPGP IGPPGPRGNR GESGPAGPPG QPGLPGPSGP PGPCCGGGVA
1010 1020 1030 1040 1050
SLGAGEKGPV GYGYEYRDEP KENEINLGEI MSSMKSINNQ IENILSPDGS
1060 1070 1080 1090 1100
RKNPARNCRD LKFCHPELKS GEYWIDPNQG CKMDAIKVYC NMETGETCLS
1110 1120 1130 1140 1150
ANPATVPRKN WWTTESSGKK HVWFGESMKG GFQFSYGDPD LPEDVSEVQL
1160 1170 1180 1190 1200
AFLRILSSRA SQNITYHCKN SIAYMNQASG NVKKALKLMS SVETDIKAEG
1210 1220 1230 1240 1250
NSKYMYAVLE DGCTKHTGEW GKTVFEYRTR KTMRLPVVDI APIDIGGPDQ
1260
EFGVDVGPVC FL
Length:1,262
Mass (Da):121,249
Last modified:August 29, 2001 - v2
Checksum:i96ABE7B2E9DEB43D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961E → K(PubMed:6547770)Curated
Sequence conflicti881 – 8811G → R in CAA23689. (PubMed:6298201)Curated
Sequence conflicti884 – 8841G → V in CAA23689. (PubMed:6298201)Curated
Non-adjacent residuesi886 – 8872Curated
Non-adjacent residuesi922 – 9232Curated
Sequence conflicti984 – 9841L → V in CAA23690. (PubMed:6298201)Curated
Sequence conflicti1132 – 11321F → S in AAA18519. (PubMed:6856474)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA05269.
I50694.
UniGeneiGga.42140.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRi A05269.
I50694.
UniGenei Gga.42140.

3D structure databases

ProteinModelPortali P12105.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi P12105.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG12793.
HOVERGENi HBG004933.
InParanoidi P12105.

Miscellaneous databases

PROi P12105.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 7 hits.
PF00093. VWC. 1 hit.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view ]
PROSITEi PS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCO3A1_CHICK
AccessioniPrimary (citable) accession number: P12105
Secondary accession number(s): P79758
, P79759, Q90790, Q90791, Q90794, Q92029
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: August 29, 2001
Last modified: November 26, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3