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P02454

- CO1A1_RAT

UniProt

P02454 - CO1A1_RAT

Protein

Collagen alpha-1(I) chain

Gene

Col1a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 5 (22 Sep 2009)
      Previous versions | rss
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    Functioni

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1266 – 12661CalciumBy similarity
    Metal bindingi1268 – 12681CalciumBy similarity
    Metal bindingi1269 – 12691Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1271 – 12711Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1274 – 12741CalciumBy similarity

    GO - Molecular functioni

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

    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 epidermal growth factor stimulus Source: RGD
    6. cellular response to fibroblast growth factor stimulus Source: RGD
    7. cellular response to fluoride Source: RGD
    8. cellular response to mechanical stimulus Source: RGD
    9. cellular response to retinoic acid Source: RGD
    10. cellular response to transforming growth factor beta stimulus Source: UniProtKB
    11. cellular response to tumor necrosis factor Source: RGD
    12. cellular response to vitamin E Source: RGD
    13. collagen biosynthetic process Source: Ensembl
    14. collagen fibril organization Source: Ensembl
    15. embryonic skeletal system development Source: Ensembl
    16. endochondral ossification Source: Ensembl
    17. face morphogenesis Source: Ensembl
    18. intramembranous ossification Source: Ensembl
    19. negative regulation of cell-substrate adhesion Source: Ensembl
    20. ossification Source: RGD
    21. osteoblast differentiation Source: Ensembl
    22. positive regulation of canonical Wnt signaling pathway Source: Ensembl
    23. positive regulation of cell migration Source: Ensembl
    24. positive regulation of epithelial to mesenchymal transition Source: Ensembl
    25. positive regulation of transcription, DNA-templated Source: Ensembl
    26. protein heterotrimerization Source: Ensembl
    27. protein localization to nucleus Source: Ensembl
    28. protein transport Source: Ensembl
    29. response to cAMP Source: RGD
    30. response to corticosteroid Source: RGD
    31. response to drug Source: RGD
    32. response to estradiol Source: RGD
    33. response to fluoride Source: RGD
    34. response to hydrogen peroxide Source: RGD
    35. response to hyperoxia Source: RGD
    36. response to mechanical stimulus Source: RGD
    37. response to nutrient Source: RGD
    38. response to nutrient levels Source: RGD
    39. response to peptide hormone Source: RGD
    40. response to steroid hormone Source: RGD
    41. sensory perception of sound Source: Ensembl
    42. skin morphogenesis Source: Ensembl
    43. tooth eruption Source: RGD
    44. tooth mineralization Source: Ensembl
    45. visual perception Source: Ensembl
    46. wound healing Source: RGD

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_195275. Extracellular matrix organization.
    REACT_197897. Syndecan interactions.
    REACT_198300. Syndecan interactions.
    REACT_198584. Collagen biosynthesis and modifying enzymes.
    REACT_198718. Anchoring fibril formation.
    REACT_198733. Scavenging by Class A Receptors.
    REACT_198756. Non-integrin membrane-ECM interactions.
    REACT_198757. ECM proteoglycans.
    REACT_198792. Crosslinking of collagen fibrils.
    REACT_199129. Assembly of collagen fibrils and other multimeric structures.
    REACT_199177. Collagen degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(I) chain
    Alternative name(s):
    Alpha-1 type I collagen
    Gene namesi
    Name:Col1a1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 10

    Organism-specific databases

    RGDi61817. Col1a1.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

    GO - Cellular componenti

    1. collagen type I trimer Source: Ensembl
    2. endoplasmic reticulum Source: RGD
    3. extracellular region Source: Reactome
    4. extracellular space Source: RGD
    5. Golgi apparatus Source: RGD
    6. secretory granule Source: RGD

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 151129N-terminal propeptide1 PublicationPRO_0000043358Add
    BLAST
    Chaini152 – 12071056Collagen alpha-1(I) chainPRO_0000043359Add
    BLAST
    Propeptidei1208 – 1453246C-terminal propeptideBy similarityPRO_0000043360Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi56 – 561N-linked (GlcNAc...)Sequence Analysis
    Modified residuei152 – 1521Pyrrolidone carboxylic acidCurated
    Modified residuei160 – 1601Allysine
    Modified residuei179 – 17914-hydroxyprolineCurated
    Modified residuei182 – 18214-hydroxyprolineCurated
    Modified residuei185 – 18514-hydroxyprolineCurated
    Modified residuei194 – 19414-hydroxyprolineCurated
    Modified residuei197 – 19714-hydroxyprolineCurated
    Modified residuei200 – 20014-hydroxyprolineCurated
    Modified residuei254 – 25415-hydroxylysine1 Publication
    Glycosylationi254 – 2541O-linked (Gal...)1 Publication
    Modified residuei575 – 57515-hydroxylysineCurated
    Modified residuei698 – 69815-hydroxylysineCurated
    Modified residuei1153 – 115313-hydroxyprolineBy similarity
    Disulfide bondi1248 ↔ 1280PROSITE-ProRule annotation
    Disulfide bondi1254 – 1254Interchain (with C-1271)PROSITE-ProRule annotation
    Disulfide bondi1271 – 1271Interchain (with C-1254)PROSITE-ProRule annotation
    Disulfide bondi1288 ↔ 1451PROSITE-ProRule annotation
    Glycosylationi1354 – 13541N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1359 ↔ 1404PROSITE-ProRule annotation

    Post-translational modificationi

    Proline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains.1 Publication
    O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.1 Publication
    Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

    Proteomic databases

    PaxDbiP02454.
    PRIDEiP02454.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    GenevestigatoriP02454.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiP02454. 2 interactions.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HQVfiber diffraction5.16A/C152-1207[»]
    3HR2fiber diffraction5.16A/C152-1207[»]
    ProteinModelPortaliP02454.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02454.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 8759VWFCPROSITE-ProRule annotationAdd
    BLAST
    Domaini1218 – 1453236Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni152 – 16716Nonhelical region (N-terminal)Add
    BLAST
    Regioni168 – 11811014Triple-helical regionAdd
    BLAST
    Regioni1176 – 118611Major antigenic determinant (of neutral salt-extracted rat skin collagen)Add
    BLAST
    Regioni1182 – 120726Nonhelical region (C-terminal)Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi734 – 7363Cell attachment siteSequence Analysis
    Motifi1082 – 10843Cell 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.
    InParanoidiA3KNA1.
    KOiK06236.
    OMAiYGVIEDG.
    OrthoDBiEOG7TJ3HH.
    PhylomeDBiP02454.
    TreeFamiTF344135.

    Family and domain databases

    InterProiIPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view]
    PfamiPF01410. COLFI. 1 hit.
    PF01391. Collagen. 12 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.

    P02454-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFSFVDLRLL LLLGATALLT HGQEDIPEVS CIHNGLRVPN GETWKPDVCL     50
    ICICHNGTAV CDGVLCKEDL DCPNPQKREG ECCPFCPEEY VSPDAEVIGV 100
    EGPKGDPGPQ GPRGPVGPPG QDGIPGQPGL PGPPGPPGPP GPPGLGGNFA 150
    SQMSYGYDEK SAGVSVPGPM GPSGPRGLPG PPGAPGPQGF QGPPGEPGEP 200
    GASGPMGPRG PPGPPGKNGD DGEAGKPGRP GERGPPGPQG ARGLPGTAGL 250
    PGMKGHRGFS GLDGAKGDTG PAGPKGEPGS PGENGAPGQM GPRGLPGERG 300
    RPGPPGSAGA RGNDGAVGAA GPPGPTGPTG PPGFPGAAGA KGEAGPQGAR 350
    GSEGPQGVRG EPGPPGPAGA AGPAGNPGAD GQPGAKGANG APGIAGAPGF 400
    PGARGPSGPQ GPSGAPGPKG NSGEPGAPGN KGDTGAKGEP GPAGVQGPPG 450
    PAGEEGKRGA RGEPGPSGLP GPPGERGGPG SRGFPGADGV AGPKGPAGER 500
    GSPGPAGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG KTGPPGPAGQ 550
    DGRPGPAGPP GARGQAGVMG FPGPKGTAGE PGKAGERGVP GPPGAVGPAG 600
    KDGEAGAQGA PGPAGPAGER GEQGPAGSPG FQGLPGPAGP PGEAGKPGEQ 650
    GVPGDLGAPG PSGARGERGF PGERGVQGPP GPAGPRGNNG APGNDGAKGD 700
    TGAPGAPGSQ GAPGLQGMPG ERGAAGLPGP KGDRGDAGPK GADGSPGKDG 750
    VRGLTGPIGP PGPAGAPGDK GETGPSGPAG PTGARGAPGD RGEPGPPGPA 800
    GFAGPPGADG QPGAKGEPGD TGVKGDAGPP GPAGPAGPPG PIGNVGAPGP 850
    KGSRGAAGPP GATGFPGAAG RVGPPGPSGN AGPPGPPGPV GKEGGKGPRG 900
    ETGPAGRPGE VGPPGPPGPA GEKGSPGADG PAGSPGTPGP QGIAGQRGVV 950
    GLPGQRGERG FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE 1000
    SGREGSPGAE GSPGRDGAPG AKGDRGETGP AGPPGAPGAP GAPGPVGPAG 1050
    KNGDRGETGP AGPAGPIGPA GARGPAGPQG PRGDKGETGE QGDRGIKGHR 1100
    GFSGLQGPPG SPGSPGEQGP SGASGPAGPR GPPGSAGSPG KDGLNGLPGP 1150
    IGPPGPRGRT GDSGPAGPPG PPGPPGPPGP PSGGYDFSFL PQPPQEKSQD 1200
    GGRYYRADDA NVVRDRDLEV DTTLKSLSQQ IENIRSPEGS RKNPARTCRD 1250
    LKMCHSDWKS GEYWIDPNQG CNLDAIKVYC NMETGQTCVF PTQPSVPQKN 1300
    WYISPNPKEK KHVWFGESMT DGFQFEYGSE GSDPADVAIQ LTFLRLMSTE 1350
    ASQNITYHCK NSVAYMDQQT GNLKKSLLLQ GSNEIELRGE GNSRFTYSTL 1400
    VDGCTSHTGT WGKTVIEYKT TKTSRLPIID VAPLDIGAPD QEFGMDIGPA 1450
    CFV 1453
    Length:1,453
    Mass (Da):137,953
    Last modified:September 22, 2009 - v5
    Checksum:iBCDDC40C3167AE59
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti143 – 1431P → L in CAB01633. (PubMed:10065941)Curated
    Sequence conflicti202 – 2021A → G in CAB01633. (PubMed:10065941)Curated
    Sequence conflicti209 – 2091R → P in CAB01633. (PubMed:10065941)Curated
    Sequence conflicti232 – 2321E → Q AA sequence (PubMed:4327399)Curated
    Sequence conflicti268 – 2681D → N AA sequence (PubMed:5411206)Curated
    Sequence conflicti286 – 2861A → T in CAB01633. (PubMed:10065941)Curated
    Sequence conflicti307 – 3071S → T in CAB01633. (PubMed:10065941)Curated
    Sequence conflicti313 – 3131N → D AA sequence (PubMed:4335087)Curated
    Sequence conflicti421 – 4211N → T in CAB01633. (PubMed:10065941)Curated
    Sequence conflicti497 – 4971A → S in CAB01633. (PubMed:10065941)Curated
    Sequence conflicti773 – 7731T → A in CAB01633. (PubMed:10065941)Curated
    Sequence conflicti794 – 7941P → A in CAB01633. (PubMed:10065941)Curated
    Sequence conflicti958 – 9581E → K in CAB01633. (PubMed:10065941)Curated
    Sequence conflicti1111 – 11111S → P AA sequence (PubMed:4126850)Curated
    Sequence conflicti1163 – 11631S → A AA sequence (PubMed:4126850)Curated
    Sequence conflicti1166 – 11661A → S AA sequence (PubMed:4126850)Curated
    Sequence conflicti1187 – 11871F → L AA sequence (PubMed:4636751)Curated
    Sequence conflicti1190 – 11901L → F AA sequence (PubMed:4636751)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z78279 mRNA. Translation: CAB01633.1.
    CH473948 Genomic DNA. Translation: EDM05727.1.
    BC133728 mRNA. Translation: AAI33729.1.
    M11432 mRNA. Translation: AAA40832.1. Sequence problems.
    PIRiA90559. CGRT1S.
    RefSeqiNP_445756.1. NM_053304.1.
    UniGeneiRn.2953.

    Genome annotation databases

    EnsembliENSRNOT00000005311; ENSRNOP00000005311; ENSRNOG00000003897.
    GeneIDi29393.
    KEGGirno:29393.
    UCSCiRGD:61817. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z78279 mRNA. Translation: CAB01633.1 .
    CH473948 Genomic DNA. Translation: EDM05727.1 .
    BC133728 mRNA. Translation: AAI33729.1 .
    M11432 mRNA. Translation: AAA40832.1 . Sequence problems.
    PIRi A90559. CGRT1S.
    RefSeqi NP_445756.1. NM_053304.1.
    UniGenei Rn.2953.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HQV fiber diffraction 5.16 A/C 152-1207 [» ]
    3HR2 fiber diffraction 5.16 A/C 152-1207 [» ]
    ProteinModelPortali P02454.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P02454. 2 interactions.

    Proteomic databases

    PaxDbi P02454.
    PRIDEi P02454.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000005311 ; ENSRNOP00000005311 ; ENSRNOG00000003897 .
    GeneIDi 29393.
    KEGGi rno:29393.
    UCSCi RGD:61817. rat.

    Organism-specific databases

    CTDi 1277.
    RGDi 61817. Col1a1.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00740000114967.
    HOGENOMi HOG000085654.
    HOVERGENi HBG004933.
    InParanoidi A3KNA1.
    KOi K06236.
    OMAi YGVIEDG.
    OrthoDBi EOG7TJ3HH.
    PhylomeDBi P02454.
    TreeFami TF344135.

    Enzyme and pathway databases

    Reactomei REACT_195275. Extracellular matrix organization.
    REACT_197897. Syndecan interactions.
    REACT_198300. Syndecan interactions.
    REACT_198584. Collagen biosynthesis and modifying enzymes.
    REACT_198718. Anchoring fibril formation.
    REACT_198733. Scavenging by Class A Receptors.
    REACT_198756. Non-integrin membrane-ECM interactions.
    REACT_198757. ECM proteoglycans.
    REACT_198792. Crosslinking of collagen fibrils.
    REACT_199129. Assembly of collagen fibrils and other multimeric structures.
    REACT_199177. Collagen degradation.

    Miscellaneous databases

    EvolutionaryTracei P02454.
    NextBioi 609017.
    PROi P02454.

    Gene expression databases

    Genevestigatori P02454.

    Family and domain databases

    InterProi IPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view ]
    Pfami PF01410. COLFI. 1 hit.
    PF01391. Collagen. 12 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. "Expression of collagen alpha1(I) mRNA variants during tooth and bone formation in the rat."
      Brandsten C., Lundmark C., Christersson C., Hammarstroem L., Wurtz T.
      J. Dent. Res. 78:11-19(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Bone and Tooth.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Brown Norway.
      Tissue: Lung.
    4. "Comparative sequence studies of rat skin and tendon collagen. II. The absence of a short sequence at the amino terminus of the skin alpha-1 chain."
      Bornstein P.
      Biochemistry 8:63-71(1969) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 152-170.
    5. "The amino acid sequence of peptides from the cross-linking region of rat skin collagen."
      Kang A.H., Bornstein P., Piez K.A.
      Biochemistry 6:788-795(1967) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 156-170.
    6. "The incomplete hydroxylation of individual prolyl residues in collagen."
      Bornstein P.
      J. Biol. Chem. 242:2572-2574(1967) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 171-206.
    7. "Chemical studies on the cyanogen bromide peptides of rat skin collagen. Amino acid sequence of alpha 1-CB4."
      Butler W.T., Ponds S.L.
      Biochemistry 10:2076-2081(1971) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 207-253.
    8. "Chemical studies on the cyanogen bromide peptides of rat skin collagen. The covalent structure of alpha 1-CB5, the major hexose-containing cyanogen bromide peptide of alpha 1."
      Butler W.T.
      Biochemistry 9:44-50(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 254-290, HYDROXYLATION AT LYS-254, GLYCOSYLATION AT LYS-254.
    9. "Structure of rat skin collagen alpha 1-CB8. Amino acid sequence of the hydroxylamine-produced fragment HA1."
      Balian G., Click E.M., Bornstein P.
      Biochemistry 10:4470-4478(1971) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 291-389.
    10. "Structure of rat skin collagen alpha 1-CBB. Amino acid sequence of the hydroxyl amine-produced fragment HA2."
      Balian G., Click E.M., Hermodson M.A., Bornstein P.
      Biochemistry 11:3798-3806(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 390-569.
    11. "Chemical studies on the cyanogen bromide peptides of rat skin collagen. Amino acid sequence of alpha 1-CB3."
      Butler W.T., Underwood S.P., Finch J.E. Jr.
      Biochemistry 13:2946-2953(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 570-718.
    12. "Construction of DNA sequences complementary to rat alpha 1 and alpha 2 collagen mRNA and their use in studying the regulation of type I collagen synthesis by 1,25-dihydroxyvitamin D."
      Genovese C., Rowe D., Kream B.
      Biochemistry 23:6210-6216(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 680-718.
    13. "Structural and immunogenic properties of a major antigenic determinant in neutral salt-extracted rat-skin collagen."
      Stoltz M., Timpl R., Furthmayr H., Kuehn K.
      Eur. J. Biochem. 37:287-294(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1103-1186.
    14. "Non-helical regions in rat collagen alpha 1-chain."
      Stoltz M., Timpl R., Kuehn K.
      FEBS Lett. 26:61-65(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1186-1206.
    15. "Endo180 binds to the C-terminal region of type I collagen."
      Thomas E.K., Nakamura M., Wienke D., Isacke C.M., Pozzi A., Liang P.
      J. Biol. Chem. 280:22596-22605(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MRC2.
      Strain: Sprague-Dawley.
    16. "A new procedure for rapid, high yield purification of Type I collagen for tissue engineering."
      Xiong X., Ghosh R., Hiller E., Drepper F., Knapp B., Brunner H., Rupp S.
      Process Biochem. 44:1200-1212(2009)
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (5.16 ANGSTROMS) OF 152-1207.

    Entry informationi

    Entry nameiCO1A1_RAT
    AccessioniPrimary (citable) accession number: P02454
    Secondary accession number(s): A3KNA1, P02455, Q63079
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 130 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3