Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P02453

- CO1A1_BOVIN

UniProt

P02453 - CO1A1_BOVIN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 3 (30 May 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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.

    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.
    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

    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 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

    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 1, 2014
    This is version 118 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