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P02453 (CO1A1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(I) chain
Alternative name(s):
Alpha-1 type I collagen
Gene names
Name:COL1A1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length1463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

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

Domain

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.

Post-translational modification

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.

Sequence similarities

Belongs to the fibrillar collagen family.

Contains 1 fibrillar collagen NC1 domain.

Contains 1 VWFC domain.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   DomainCollagen
Repeat
Signal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
Hydroxylation
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood vessel development

Inferred from electronic annotation. Source: Ensembl

bone trabecula formation

Inferred from electronic annotation. Source: Ensembl

cartilage development involved in endochondral bone morphogenesis

Inferred from electronic annotation. Source: Ensembl

cellular response to amino acid stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

collagen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

collagen fibril organization

Inferred from electronic annotation. Source: Ensembl

embryonic skeletal system development

Inferred from electronic annotation. Source: Ensembl

endochondral ossification

Inferred from electronic annotation. Source: Ensembl

face morphogenesis

Inferred from electronic annotation. Source: Ensembl

intramembranous ossification

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell-substrate adhesion

Inferred from electronic annotation. Source: Ensembl

osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial to mesenchymal transition

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

protein heterotrimerization

Inferred from electronic annotation. Source: Ensembl

protein localization to nucleus

Inferred from electronic annotation. Source: Ensembl

protein transport

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Inferred from electronic annotation. Source: Ensembl

skin morphogenesis

Inferred from electronic annotation. Source: Ensembl

tooth mineralization

Inferred from electronic annotation. Source: Ensembl

visual perception

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcollagen type I trimer

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionextracellular matrix structural constituent

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 161139N-terminal propeptide
PRO_0000236804
Chain162 – 12151054Collagen alpha-1(I) chain
PRO_0000059396
Propeptide1216 – 1463248C-terminal propeptide
PRO_0000236805

Regions

Domain38 – 9659VWFC
Domain1228 – 1463236Fibrillar collagen NC1
Region162 – 17716Nonhelical region (N-terminal)
Region178 – 11911014Triple-helical region
Region1192 – 121524Nonhelical region (C-terminal)
Motif744 – 7463Cell attachment site Potential
Motif1092 – 10943Cell attachment site Potential

Sites

Metal binding12761Calcium By similarity
Metal binding12781Calcium By similarity
Metal binding12791Calcium; via carbonyl oxygen By similarity
Metal binding12811Calcium; via carbonyl oxygen By similarity
Metal binding12841Calcium By similarity

Amino acid modifications

Modified residue1621Pyrrolidone carboxylic acid Ref.2
Modified residue1701Allysine
Modified residue26415-hydroxylysine
Modified residue27615-hydroxylysine Potential
Modified residue28515-hydroxylysine Potential
Modified residue70815-hydroxylysine Potential
Modified residue78015-hydroxylysine Potential
Modified residue86115-hydroxylysine Potential
Modified residue93315-hydroxylysine Potential
Modified residue109515-hydroxylysine Potential
Modified residue110715-hydroxylysine Potential
Modified residue116313-hydroxyproline
Glycosylation2641O-linked (Gal...)
Disulfide bond1258 ↔ 1290 By similarity
Disulfide bond1264Interchain (with C-1281) By similarity
Disulfide bond1281Interchain (with C-1264) By similarity
Disulfide bond1298 ↔ 1461 By similarity
Disulfide bond1369 ↔ 1414 By similarity

Experimental info

Sequence conflict6871Q → E AA sequence Ref.4
Sequence conflict790 – 7923Missing AA sequence Ref.5
Sequence conflict7941A → T AA sequence Ref.5
Sequence conflict10431P → A AA sequence Ref.6
Sequence conflict10461A → P AA sequence Ref.6
Sequence conflict10741A → I AA sequence Ref.6
Sequence conflict10771I → V AA sequence Ref.6
Sequence conflict10801V → A AA sequence Ref.6
Sequence conflict12061E → QZ AA sequence Ref.8

Sequences

Sequence LengthMass (Da)Tools
P02453 [UniParc].

Last modified May 30, 2006. Version 3.
Checksum: 8A6E17F276C4C6FA

FASTA1,463138,938
        10         20         30         40         50         60 
MFSFVDLRLL LLLAATALLT HGQEEGQEEG QEEDIPPVTC VQNGLRYHDR DVWKPVPCQI 

        70         80         90        100        110        120 
CVCDNGNVLC DDVICDELKD CPNAKVPTDE CCPVCPEGQE SPTDQETTGV EGPKGDTGPR 

       130        140        150        160        170        180 
GPRGPAGPPG RDGIPGQPGL PGPPGPPGPP GPPGLGGNFA PQLSYGYDEK STGISVPGPM 

       190        200        210        220        230        240 
GPSGPRGLPG PPGAPGPQGF QGPPGEPGEP GASGPMGPRG PPGPPGKNGD DGEAGKPGRP 

       250        260        270        280        290        300 
GERGPPGPQG ARGLPGTAGL PGMKGHRGFS GLDGAKGDAG PAGPKGEPGS PGENGAPGQM 

       310        320        330        340        350        360 
GPRGLPGERG RPGAPGPAGA RGNDGATGAA GPPGPTGPAG PPGFPGAVGA KGEGGPQGPR 

       370        380        390        400        410        420 
GSEGPQGVRG EPGPPGPAGA AGPAGNPGAD GQPGAKGANG APGIAGAPGF PGARGPSGPQ 

       430        440        450        460        470        480 
GPSGPPGPKG NSGEPGAPGS KGDTGAKGEP GPTGIQGPPG PAGEEGKRGA RGEPGPAGLP 

       490        500        510        520        530        540 
GPPGERGGPG SRGFPGADGV AGPKGPAGER GAPGPAGPKG SPGEAGRPGE AGLPGAKGLT 

       550        560        570        580        590        600 
GSPGSPGPDG KTGPPGPAGQ DGRPGPPGPP GARGQAGVMG FPGPKGAAGE PGKAGERGVP 

       610        620        630        640        650        660 
GPPGAVGPAG KDGEAGAQGP PGPAGPAGER GEQGPAGSPG FQGLPGPAGP PGEAGKPGEQ 

       670        680        690        700        710        720 
GVPGDLGAPG PSGARGERGF PGERGVQGPP GPAGPRGANG APGNDGAKGD AGAPGAPGSQ 

       730        740        750        760        770        780 
GAPGLQGMPG ERGAAGLPGP KGDRGDAGPK GADGAPGKDG VRGLTGPIGP PGPAGAPGDK 

       790        800        810        820        830        840 
GEAGPSGPAG PTGARGAPGD RGEPGPPGPA GFAGPPGADG QPGAKGEPGD AGAKGDAGPP 

       850        860        870        880        890        900 
GPAGPAGPPG PIGNVGAPGP KGARGSAGPP GATGFPGAAG RVGPPGPSGN AGPPGPPGPA 

       910        920        930        940        950        960 
GKEGSKGPRG ETGPAGRPGE VGPPGPPGPA GEKGAPGADG PAGAPGTPGP QGIAGQRGVV 

       970        980        990       1000       1010       1020 
GLPGQRGERG FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE SGREGAPGAE 

      1030       1040       1050       1060       1070       1080 
GSPGRDGSPG AKGDRGETGP AGPPGAPGAP GAPGPVGPAG KSGDRGETGP AGPAGPIGPV 

      1090       1100       1110       1120       1130       1140 
GARGPAGPQG PRGDKGETGE QGDRGIKGHR GFSGLQGPPG PPGSPGEQGP SGASGPAGPR 

      1150       1160       1170       1180       1190       1200 
GPPGSAGSPG KDGLNGLPGP IGPPGPRGRT GDAGPAGPPG PPGPPGPPGP PSGGYDLSFL 

      1210       1220       1230       1240       1250       1260 
PQPPQEKAHD GGRYYRADDA NVVRDRDLEV DTTLKSLSQQ IENIRSPEGS RKNPARTCRD 

      1270       1280       1290       1300       1310       1320 
LKMCHSDWKS GEYWIDPNQG CNLDAIKVFC NMETGETCVY PTQPSVAQKN WYISKNPKEK 

      1330       1340       1350       1360       1370       1380 
RHVWYGESMT GGFQFEYGGQ GSDPADVAIQ LTFLRLMSTE ASQNITYHCK NSVAYMDQQT 

      1390       1400       1410       1420       1430       1440 
GNLKKALLLQ GSNEIEIRAE GNSRFTYSVT YDGCTSHTGA WGKTVIEYKT TKTSRLPIID 

      1450       1460 
VAPLDVGAPD QEFGFDVGPA CFL 

« Hide

References

« Hide 'large scale' references
[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.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC105184 mRNA. Translation: AAI05185.1.
PIRCGBO1S. A91193.
RefSeqNP_001029211.1. NM_001034039.2.
UniGeneBt.23316.

3D structure databases

ProteinModelPortalP02453.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP02453. 1 interaction.

Proteomic databases

PaxDbP02453.
PRIDEP02453.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000017420; ENSBTAP00000017420; ENSBTAG00000013103.
GeneID282187.
KEGGbta:282187.

Organism-specific databases

CTD1277.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00740000114967.
HOGENOMHOG000085654.
HOVERGENHBG004933.
InParanoidP02453.
KOK06236.
OMAKEKRHVW.
OrthoDBEOG7TJ3HH.
TreeFamTF344135.

Family and domain databases

InterProIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 11 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20806015.
PMAP-CutDBP02453.

Entry information

Entry nameCO1A1_BOVIN
AccessionPrimary (citable) accession number: P02453
Secondary accession number(s): Q3MHM2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 30, 2006
Last modified: July 9, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families