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P02453

- CO1A1_BOVIN

UniProt

P02453 - CO1A1_BOVIN

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Protein
Collagen alpha-1(I) chain
Gene
COL1A1
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Type I collagen is a member of group I collagen (fibrillar forming collagen).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1276 – 12761Calcium By similarity
Metal bindingi1278 – 12781Calcium By similarity
Metal bindingi1279 – 12791Calcium; via carbonyl oxygen By similarity
Metal bindingi1281 – 12811Calcium; via carbonyl oxygen By similarity
Metal bindingi1284 – 12841Calcium By similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: Ensembl
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. blood vessel development Source: Ensembl
  2. bone trabecula formation Source: Ensembl
  3. cartilage development involved in endochondral bone morphogenesis Source: Ensembl
  4. cellular response to amino acid stimulus Source: Ensembl
  5. cellular response to mechanical stimulus Source: Ensembl
  6. collagen biosynthetic process Source: Ensembl
  7. collagen fibril organization Source: Ensembl
  8. embryonic skeletal system development Source: Ensembl
  9. endochondral ossification Source: Ensembl
  10. face morphogenesis Source: Ensembl
  11. intramembranous ossification Source: Ensembl
  12. negative regulation of cell-substrate adhesion Source: Ensembl
  13. osteoblast differentiation Source: Ensembl
  14. positive regulation of canonical Wnt signaling pathway Source: Ensembl
  15. positive regulation of cell migration Source: Ensembl
  16. positive regulation of epithelial to mesenchymal transition Source: Ensembl
  17. positive regulation of transcription, DNA-templated Source: Ensembl
  18. protein heterotrimerization Source: Ensembl
  19. protein localization to nucleus Source: Ensembl
  20. protein transport Source: Ensembl
  21. sensory perception of sound Source: Ensembl
  22. skin morphogenesis Source: Ensembl
  23. tooth mineralization Source: Ensembl
  24. visual perception Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_204848. Syndecan interactions.
REACT_207047. Integrin cell surface interactions.
REACT_208597. Cell surface interactions at the vascular wall.
REACT_215758. Collagen biosynthesis and modifying enzymes.
REACT_215983. Anchoring fibril formation.
REACT_219098. GPVI-mediated activation cascade.
REACT_219927. Non-integrin membrane-ECM interactions.
REACT_220688. Platelet Adhesion to exposed collagen.
REACT_222217. ECM proteoglycans.
REACT_222620. Collagen degradation.
REACT_223425. Extracellular matrix organization.
REACT_224259. Crosslinking of collagen fibrils.
REACT_226104. Assembly of collagen fibrils and other multimeric structures.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(I) chain
Alternative name(s):
Alpha-1 type I collagen
Gene namesi
Name:COL1A1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 19

Subcellular locationi

GO - Cellular componenti

  1. collagen type I trimer Source: Ensembl
  2. cytoplasm Source: Ensembl
  3. extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 Reviewed prediction
Add
BLAST
Propeptidei23 – 161139N-terminal propeptide
PRO_0000236804Add
BLAST
Chaini162 – 12151054Collagen alpha-1(I) chain
PRO_0000059396Add
BLAST
Propeptidei1216 – 1463248C-terminal propeptide
PRO_0000236805Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei162 – 1621Pyrrolidone carboxylic acid1 Publication
Modified residuei170 – 1701Allysine
Modified residuei264 – 26415-hydroxylysine
Glycosylationi264 – 2641O-linked (Gal...)
Modified residuei276 – 27615-hydroxylysine Reviewed prediction
Modified residuei285 – 28515-hydroxylysine Reviewed prediction
Modified residuei708 – 70815-hydroxylysine Reviewed prediction
Modified residuei780 – 78015-hydroxylysine Reviewed prediction
Modified residuei861 – 86115-hydroxylysine Reviewed prediction
Modified residuei933 – 93315-hydroxylysine Reviewed prediction
Modified residuei1095 – 109515-hydroxylysine Reviewed prediction
Modified residuei1107 – 110715-hydroxylysine Reviewed prediction
Modified residuei1163 – 116313-hydroxyproline
Disulfide bondi1258 ↔ 1290 By similarity
Disulfide bondi1264 – 1264Interchain (with C-1281) By similarity
Disulfide bondi1281 – 1281Interchain (with C-1264) By similarity
Disulfide bondi1298 ↔ 1461 By similarity
Disulfide bondi1369 ↔ 1414 By similarity

Post-translational modificationi

Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. Pro-1163 is the only 3-hydroxyproline and the only hydroxylated proline in position X.
O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP02453.
PRIDEiP02453.

Miscellaneous databases

PMAP-CutDBP02453.

Expressioni

Tissue specificityi

Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.

Interactioni

Subunit structurei

Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2 By similarity. Interacts with TRAM2 By similarity.

Protein-protein interaction databases

IntActiP02453. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP02453.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 9659VWFC
Add
BLAST
Domaini1228 – 1463236Fibrillar collagen NC1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni162 – 17716Nonhelical region (N-terminal)
Add
BLAST
Regioni178 – 11911014Triple-helical region
Add
BLAST
Regioni1192 – 121524Nonhelical region (C-terminal)
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi744 – 7463Cell attachment site Reviewed prediction
Motifi1092 – 10943Cell attachment site Reviewed prediction

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.

Sequence similaritiesi

Contains 1 VWFC domain.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00740000114967.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP02453.
KOiK06236.
OMAiKEKRHVW.
OrthoDBiEOG7TJ3HH.
TreeFamiTF344135.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 11 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: Complete.

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

P02453-1 [UniParc]FASTAAdd to Basket

« Hide

MFSFVDLRLL LLLAATALLT HGQEEGQEEG QEEDIPPVTC VQNGLRYHDR     50
DVWKPVPCQI CVCDNGNVLC DDVICDELKD CPNAKVPTDE CCPVCPEGQE 100
SPTDQETTGV EGPKGDTGPR GPRGPAGPPG RDGIPGQPGL PGPPGPPGPP 150
GPPGLGGNFA PQLSYGYDEK STGISVPGPM GPSGPRGLPG PPGAPGPQGF 200
QGPPGEPGEP GASGPMGPRG PPGPPGKNGD DGEAGKPGRP GERGPPGPQG 250
ARGLPGTAGL PGMKGHRGFS GLDGAKGDAG PAGPKGEPGS PGENGAPGQM 300
GPRGLPGERG RPGAPGPAGA RGNDGATGAA GPPGPTGPAG PPGFPGAVGA 350
KGEGGPQGPR GSEGPQGVRG EPGPPGPAGA AGPAGNPGAD GQPGAKGANG 400
APGIAGAPGF PGARGPSGPQ GPSGPPGPKG NSGEPGAPGS KGDTGAKGEP 450
GPTGIQGPPG PAGEEGKRGA RGEPGPAGLP GPPGERGGPG SRGFPGADGV 500
AGPKGPAGER GAPGPAGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG 550
KTGPPGPAGQ DGRPGPPGPP GARGQAGVMG FPGPKGAAGE PGKAGERGVP 600
GPPGAVGPAG KDGEAGAQGP PGPAGPAGER GEQGPAGSPG FQGLPGPAGP 650
PGEAGKPGEQ GVPGDLGAPG PSGARGERGF PGERGVQGPP GPAGPRGANG 700
APGNDGAKGD AGAPGAPGSQ GAPGLQGMPG ERGAAGLPGP KGDRGDAGPK 750
GADGAPGKDG VRGLTGPIGP PGPAGAPGDK GEAGPSGPAG PTGARGAPGD 800
RGEPGPPGPA GFAGPPGADG QPGAKGEPGD AGAKGDAGPP GPAGPAGPPG 850
PIGNVGAPGP KGARGSAGPP GATGFPGAAG RVGPPGPSGN AGPPGPPGPA 900
GKEGSKGPRG ETGPAGRPGE VGPPGPPGPA GEKGAPGADG PAGAPGTPGP 950
QGIAGQRGVV GLPGQRGERG FPGLPGPSGE PGKQGPSGAS GERGPPGPMG 1000
PPGLAGPPGE SGREGAPGAE GSPGRDGSPG AKGDRGETGP AGPPGAPGAP 1050
GAPGPVGPAG KSGDRGETGP AGPAGPIGPV GARGPAGPQG PRGDKGETGE 1100
QGDRGIKGHR GFSGLQGPPG PPGSPGEQGP SGASGPAGPR GPPGSAGSPG 1150
KDGLNGLPGP IGPPGPRGRT GDAGPAGPPG PPGPPGPPGP PSGGYDLSFL 1200
PQPPQEKAHD GGRYYRADDA NVVRDRDLEV DTTLKSLSQQ IENIRSPEGS 1250
RKNPARTCRD LKMCHSDWKS GEYWIDPNQG CNLDAIKVFC NMETGETCVY 1300
PTQPSVAQKN WYISKNPKEK RHVWYGESMT GGFQFEYGGQ GSDPADVAIQ 1350
LTFLRLMSTE ASQNITYHCK NSVAYMDQQT GNLKKALLLQ GSNEIEIRAE 1400
GNSRFTYSVT YDGCTSHTGA WGKTVIEYKT TKTSRLPIID VAPLDVGAPD 1450
QEFGFDVGPA CFL 1463
Length:1,463
Mass (Da):138,938
Last modified:May 30, 2006 - v3
Checksum:i8A6E17F276C4C6FA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti687 – 6871Q → E AA sequence 1 Publication
Sequence conflicti790 – 7923Missing AA sequence 1 Publication
Sequence conflicti794 – 7941A → T AA sequence 1 Publication
Sequence conflicti1043 – 10431P → A AA sequence 1 Publication
Sequence conflicti1046 – 10461A → P AA sequence 1 Publication
Sequence conflicti1074 – 10741A → I AA sequence 1 Publication
Sequence conflicti1077 – 10771I → V AA sequence 1 Publication
Sequence conflicti1080 – 10801V → A AA sequence 1 Publication
Sequence conflicti1206 – 12061E → QZ AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC105184 mRNA. Translation: AAI05185.1.
PIRiA91193. CGBO1S.
RefSeqiNP_001029211.1. NM_001034039.2.
UniGeneiBt.23316.

Genome annotation databases

EnsembliENSBTAT00000017420; ENSBTAP00000017420; ENSBTAG00000013103.
GeneIDi282187.
KEGGibta:282187.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC105184 mRNA. Translation: AAI05185.1 .
PIRi A91193. CGBO1S.
RefSeqi NP_001029211.1. NM_001034039.2.
UniGenei Bt.23316.

3D structure databases

ProteinModelPortali P02453.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P02453. 1 interaction.

Proteomic databases

PaxDbi P02453.
PRIDEi P02453.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000017420 ; ENSBTAP00000017420 ; ENSBTAG00000013103 .
GeneIDi 282187.
KEGGi bta:282187.

Organism-specific databases

CTDi 1277.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00740000114967.
HOGENOMi HOG000085654.
HOVERGENi HBG004933.
InParanoidi P02453.
KOi K06236.
OMAi KEKRHVW.
OrthoDBi EOG7TJ3HH.
TreeFami TF344135.

Enzyme and pathway databases

Reactomei REACT_204848. Syndecan interactions.
REACT_207047. Integrin cell surface interactions.
REACT_208597. Cell surface interactions at the vascular wall.
REACT_215758. Collagen biosynthesis and modifying enzymes.
REACT_215983. Anchoring fibril formation.
REACT_219098. GPVI-mediated activation cascade.
REACT_219927. Non-integrin membrane-ECM interactions.
REACT_220688. Platelet Adhesion to exposed collagen.
REACT_222217. ECM proteoglycans.
REACT_222620. Collagen degradation.
REACT_223425. Extracellular matrix organization.
REACT_224259. Crosslinking of collagen fibrils.
REACT_226104. Assembly of collagen fibrils and other multimeric structures.

Miscellaneous databases

NextBioi 20806015.
PMAP-CutDB P02453.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 11 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

« Hide 'large scale' publications
  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal liver.
  2. "Structural characterization of N-terminal antigenic determinants in calf and human collagen."
    Rauterberg J., Timpl R., Furthmayr H.
    Eur. J. Biochem. 27:231-237(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 162-180.
  3. "The covalent structure of collagen: amino-acid sequence of the cyanogen-bromide peptides alpha-1-CB2, alpha-1-CB4 and alpha-1-CB5 from calf-skin collagen."
    Fietzek P.P., Kuehn K.
    Eur. J. Biochem. 52:77-82(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 181-306, HYDROXYLATION AT LYS-264.
  4. "The covalent structure of collagen: amino acid sequence of alpha-1-CB3 from calf skin collagen."
    Fietzek P.P., Wendt P., Kell I., Kuehn K.
    FEBS Lett. 26:74-76(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 580-728.
  5. "The covalent structure of collagen. 2. The amino-acid sequence of alpha-1-CB7 from calf-skin collagen."
    Fietzek P.P., Rexrodt F.W., Hopper K.E., Kuehn K.
    Eur. J. Biochem. 38:396-400(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 729-999.
  6. "The covalent structure of collagen. The amino-acid sequence of the 112-residues. Amino-terminal part of peptide alpha-1-CB6 from calf-skin collagen."
    Wendt P., Mark K.V.D., Rexrodt F., Kuehn K.
    Eur. J. Biochem. 30:169-183(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1000-1112.
  7. "The covalent structure of collagen. Amino-acid sequence of peptide alpha-1-CB6-C2."
    Fietzek P.P., Rexrodt F.W., Wendt P., Stark M., Kuehn K.
    Eur. J. Biochem. 30:163-168(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1113-1188.
  8. "The amino acid sequence of the carboxyterminal nonhelical cross link region of the alpha 1 chain of calf skin collagen."
    Rauterberg J., Fietzek P., Rexrodt F., Becker U., Stark M., Kuehn K.
    FEBS Lett. 21:75-79(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1196-1215, HYDROXYLATION AT PRO-1163.

Entry informationi

Entry nameiCO1A1_BOVIN
AccessioniPrimary (citable) accession number: P02453
Secondary accession number(s): Q3MHM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 30, 2006
Last modified: September 3, 2014
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi