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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 – 12761CalciumBy similarity
Metal bindingi1278 – 12781CalciumBy similarity
Metal bindingi1279 – 12791Calcium; via carbonyl oxygenBy similarity
Metal bindingi1281 – 12811Calcium; via carbonyl oxygenBy similarity
Metal bindingi1284 – 12841CalciumBy 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

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

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 – 2222Sequence AnalysisAdd
BLAST
Propeptidei23 – 161139N-terminal propeptide1 PublicationPRO_0000236804Add
BLAST
Chaini162 – 12151054Collagen alpha-1(I) chainPRO_0000059396Add
BLAST
Propeptidei1216 – 1463248C-terminal propeptidePRO_0000236805Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei162 – 1621Pyrrolidone carboxylic acid1 Publication
Modified residuei170 – 1701Allysine
Modified residuei264 – 26415-hydroxylysine1 Publication
Glycosylationi264 – 2641O-linked (Gal...)
Modified residuei276 – 27615-hydroxylysineSequence Analysis
Modified residuei285 – 28515-hydroxylysineSequence Analysis
Modified residuei708 – 70815-hydroxylysineSequence Analysis
Modified residuei780 – 78015-hydroxylysineSequence Analysis
Modified residuei861 – 86115-hydroxylysineSequence Analysis
Modified residuei933 – 93315-hydroxylysineSequence Analysis
Modified residuei1095 – 109515-hydroxylysineSequence Analysis
Modified residuei1107 – 110715-hydroxylysineSequence Analysis
Modified residuei1163 – 116313-hydroxyproline1 Publication
Disulfide bondi1258 ↔ 1290PROSITE-ProRule annotation
Disulfide bondi1264 – 1264Interchain (with C-1281)PROSITE-ProRule annotation
Disulfide bondi1281 – 1281Interchain (with C-1264)PROSITE-ProRule annotation
Disulfide bondi1298 ↔ 1461PROSITE-ProRule annotation
Disulfide bondi1369 ↔ 1414PROSITE-ProRule annotation

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.2 Publications
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.

Gene expression databases

ExpressionAtlasiP02453. baseline and differential.

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).By similarity

Protein-protein interaction databases

IntActiP02453. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP02453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 9659VWFCPROSITE-ProRule annotationAdd
BLAST
Domaini1228 – 1463236Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi744 – 7463Cell attachment siteSequence Analysis
Motifi1092 – 10943Cell attachment siteSequence Analysis

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.
GeneTreeiENSGT00760000118776.
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

        10         20         30         40         50
MFSFVDLRLL LLLAATALLT HGQEEGQEEG QEEDIPPVTC VQNGLRYHDR
60 70 80 90 100
DVWKPVPCQI CVCDNGNVLC DDVICDELKD CPNAKVPTDE CCPVCPEGQE
110 120 130 140 150
SPTDQETTGV EGPKGDTGPR GPRGPAGPPG RDGIPGQPGL PGPPGPPGPP
160 170 180 190 200
GPPGLGGNFA PQLSYGYDEK STGISVPGPM GPSGPRGLPG PPGAPGPQGF
210 220 230 240 250
QGPPGEPGEP GASGPMGPRG PPGPPGKNGD DGEAGKPGRP GERGPPGPQG
260 270 280 290 300
ARGLPGTAGL PGMKGHRGFS GLDGAKGDAG PAGPKGEPGS PGENGAPGQM
310 320 330 340 350
GPRGLPGERG RPGAPGPAGA RGNDGATGAA GPPGPTGPAG PPGFPGAVGA
360 370 380 390 400
KGEGGPQGPR GSEGPQGVRG EPGPPGPAGA AGPAGNPGAD GQPGAKGANG
410 420 430 440 450
APGIAGAPGF PGARGPSGPQ GPSGPPGPKG NSGEPGAPGS KGDTGAKGEP
460 470 480 490 500
GPTGIQGPPG PAGEEGKRGA RGEPGPAGLP GPPGERGGPG SRGFPGADGV
510 520 530 540 550
AGPKGPAGER GAPGPAGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG
560 570 580 590 600
KTGPPGPAGQ DGRPGPPGPP GARGQAGVMG FPGPKGAAGE PGKAGERGVP
610 620 630 640 650
GPPGAVGPAG KDGEAGAQGP PGPAGPAGER GEQGPAGSPG FQGLPGPAGP
660 670 680 690 700
PGEAGKPGEQ GVPGDLGAPG PSGARGERGF PGERGVQGPP GPAGPRGANG
710 720 730 740 750
APGNDGAKGD AGAPGAPGSQ GAPGLQGMPG ERGAAGLPGP KGDRGDAGPK
760 770 780 790 800
GADGAPGKDG VRGLTGPIGP PGPAGAPGDK GEAGPSGPAG PTGARGAPGD
810 820 830 840 850
RGEPGPPGPA GFAGPPGADG QPGAKGEPGD AGAKGDAGPP GPAGPAGPPG
860 870 880 890 900
PIGNVGAPGP KGARGSAGPP GATGFPGAAG RVGPPGPSGN AGPPGPPGPA
910 920 930 940 950
GKEGSKGPRG ETGPAGRPGE VGPPGPPGPA GEKGAPGADG PAGAPGTPGP
960 970 980 990 1000
QGIAGQRGVV GLPGQRGERG FPGLPGPSGE PGKQGPSGAS GERGPPGPMG
1010 1020 1030 1040 1050
PPGLAGPPGE SGREGAPGAE GSPGRDGSPG AKGDRGETGP AGPPGAPGAP
1060 1070 1080 1090 1100
GAPGPVGPAG KSGDRGETGP AGPAGPIGPV GARGPAGPQG PRGDKGETGE
1110 1120 1130 1140 1150
QGDRGIKGHR GFSGLQGPPG PPGSPGEQGP SGASGPAGPR GPPGSAGSPG
1160 1170 1180 1190 1200
KDGLNGLPGP IGPPGPRGRT GDAGPAGPPG PPGPPGPPGP PSGGYDLSFL
1210 1220 1230 1240 1250
PQPPQEKAHD GGRYYRADDA NVVRDRDLEV DTTLKSLSQQ IENIRSPEGS
1260 1270 1280 1290 1300
RKNPARTCRD LKMCHSDWKS GEYWIDPNQG CNLDAIKVFC NMETGETCVY
1310 1320 1330 1340 1350
PTQPSVAQKN WYISKNPKEK RHVWYGESMT GGFQFEYGGQ GSDPADVAIQ
1360 1370 1380 1390 1400
LTFLRLMSTE ASQNITYHCK NSVAYMDQQT GNLKKALLLQ GSNEIEIRAE
1410 1420 1430 1440 1450
GNSRFTYSVT YDGCTSHTGA WGKTVIEYKT TKTSRLPIID VAPLDVGAPD
1460
QEFGFDVGPA CFL
Length:1,463
Mass (Da):138,938
Last modified:May 30, 2006 - v3
Checksum:i8A6E17F276C4C6FA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti687 – 6871Q → E AA sequence (PubMed:4673951)Curated
Sequence conflicti790 – 7923Missing AA sequence (PubMed:4359390)Curated
Sequence conflicti794 – 7941A → T AA sequence (PubMed:4359390)Curated
Sequence conflicti1043 – 10431P → A AA sequence (PubMed:4343808)Curated
Sequence conflicti1046 – 10461A → P AA sequence (PubMed:4343808)Curated
Sequence conflicti1074 – 10741A → I AA sequence (PubMed:4343808)Curated
Sequence conflicti1077 – 10771I → V AA sequence (PubMed:4343808)Curated
Sequence conflicti1080 – 10801V → A AA sequence (PubMed:4343808)Curated
Sequence conflicti1206 – 12061E → QZ AA sequence (PubMed:11946479)Curated

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 ENSGT00760000118776.
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.

Gene expression databases

ExpressionAtlasi P02453. baseline and differential.

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: October 29, 2014
This is version 119 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