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P02454

- CO1A1_RAT

UniProt

P02454 - CO1A1_RAT

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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

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

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
Complete GO annotation...

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
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 – 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.
GeneTreeiENSGT00760000118776.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP02454.
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

        10         20         30         40         50
MFSFVDLRLL LLLGATALLT HGQEDIPEVS CIHNGLRVPN GETWKPDVCL
60 70 80 90 100
ICICHNGTAV CDGVLCKEDL DCPNPQKREG ECCPFCPEEY VSPDAEVIGV
110 120 130 140 150
EGPKGDPGPQ GPRGPVGPPG QDGIPGQPGL PGPPGPPGPP GPPGLGGNFA
160 170 180 190 200
SQMSYGYDEK SAGVSVPGPM GPSGPRGLPG PPGAPGPQGF QGPPGEPGEP
210 220 230 240 250
GASGPMGPRG PPGPPGKNGD DGEAGKPGRP GERGPPGPQG ARGLPGTAGL
260 270 280 290 300
PGMKGHRGFS GLDGAKGDTG PAGPKGEPGS PGENGAPGQM GPRGLPGERG
310 320 330 340 350
RPGPPGSAGA RGNDGAVGAA GPPGPTGPTG PPGFPGAAGA KGEAGPQGAR
360 370 380 390 400
GSEGPQGVRG EPGPPGPAGA AGPAGNPGAD GQPGAKGANG APGIAGAPGF
410 420 430 440 450
PGARGPSGPQ GPSGAPGPKG NSGEPGAPGN KGDTGAKGEP GPAGVQGPPG
460 470 480 490 500
PAGEEGKRGA RGEPGPSGLP GPPGERGGPG SRGFPGADGV AGPKGPAGER
510 520 530 540 550
GSPGPAGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG KTGPPGPAGQ
560 570 580 590 600
DGRPGPAGPP GARGQAGVMG FPGPKGTAGE PGKAGERGVP GPPGAVGPAG
610 620 630 640 650
KDGEAGAQGA PGPAGPAGER GEQGPAGSPG FQGLPGPAGP PGEAGKPGEQ
660 670 680 690 700
GVPGDLGAPG PSGARGERGF PGERGVQGPP GPAGPRGNNG APGNDGAKGD
710 720 730 740 750
TGAPGAPGSQ GAPGLQGMPG ERGAAGLPGP KGDRGDAGPK GADGSPGKDG
760 770 780 790 800
VRGLTGPIGP PGPAGAPGDK GETGPSGPAG PTGARGAPGD RGEPGPPGPA
810 820 830 840 850
GFAGPPGADG QPGAKGEPGD TGVKGDAGPP GPAGPAGPPG PIGNVGAPGP
860 870 880 890 900
KGSRGAAGPP GATGFPGAAG RVGPPGPSGN AGPPGPPGPV GKEGGKGPRG
910 920 930 940 950
ETGPAGRPGE VGPPGPPGPA GEKGSPGADG PAGSPGTPGP QGIAGQRGVV
960 970 980 990 1000
GLPGQRGERG FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE
1010 1020 1030 1040 1050
SGREGSPGAE GSPGRDGAPG AKGDRGETGP AGPPGAPGAP GAPGPVGPAG
1060 1070 1080 1090 1100
KNGDRGETGP AGPAGPIGPA GARGPAGPQG PRGDKGETGE QGDRGIKGHR
1110 1120 1130 1140 1150
GFSGLQGPPG SPGSPGEQGP SGASGPAGPR GPPGSAGSPG KDGLNGLPGP
1160 1170 1180 1190 1200
IGPPGPRGRT GDSGPAGPPG PPGPPGPPGP PSGGYDFSFL PQPPQEKSQD
1210 1220 1230 1240 1250
GGRYYRADDA NVVRDRDLEV DTTLKSLSQQ IENIRSPEGS RKNPARTCRD
1260 1270 1280 1290 1300
LKMCHSDWKS GEYWIDPNQG CNLDAIKVYC NMETGQTCVF PTQPSVPQKN
1310 1320 1330 1340 1350
WYISPNPKEK KHVWFGESMT DGFQFEYGSE GSDPADVAIQ LTFLRLMSTE
1360 1370 1380 1390 1400
ASQNITYHCK NSVAYMDQQT GNLKKSLLLQ GSNEIELRGE GNSRFTYSTL
1410 1420 1430 1440 1450
VDGCTSHTGT WGKTVIEYKT TKTSRLPIID VAPLDIGAPD QEFGMDIGPA

CFV
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 ENSGT00760000118776.
HOGENOMi HOG000085654.
HOVERGENi HBG004933.
InParanoidi P02454.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 131 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