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Protein

Collagen alpha-1(I) chain

Gene

COL1A1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1276CalciumBy similarity1
Metal bindingi1278CalciumBy similarity1
Metal bindingi1279Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1281Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1284CalciumBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-BTA-114604 GPVI-mediated activation cascade
R-BTA-1442490 Collagen degradation
R-BTA-1474244 Extracellular matrix organization
R-BTA-1650814 Collagen biosynthesis and modifying enzymes
R-BTA-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-BTA-2022090 Assembly of collagen fibrils and other multimeric structures
R-BTA-202733 Cell surface interactions at the vascular wall
R-BTA-216083 Integrin cell surface interactions
R-BTA-2214320 Anchoring fibril formation
R-BTA-2243919 Crosslinking of collagen fibrils
R-BTA-3000171 Non-integrin membrane-ECM interactions
R-BTA-3000178 ECM proteoglycans
R-BTA-430116 GP1b-IX-V activation signalling
R-BTA-75892 Platelet Adhesion to exposed collagen
R-BTA-76009 Platelet Aggregation (Plug Formation)
R-BTA-8874081 MET activates PTK2 signaling
R-BTA-8948216 Collagen chain trimerization

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
Proteomesi
  • UP000009136 Componenti: Chromosome 19

Organism-specific databases

VGNCiVGNC:27560 COL1A1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000023680423 – 161N-terminal propeptide1 PublicationAdd BLAST139
ChainiPRO_0000059396162 – 1217Collagen alpha-1(I) chain1 PublicationAdd BLAST1056
PropeptideiPRO_00002368051218 – 1463C-terminal propeptide1 PublicationAdd BLAST246

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei162Pyrrolidone carboxylic acid1 Publication1
Modified residuei170Allysine1 Publication1
Modified residuei171PhosphoserineBy similarity1
Modified residuei1894-hydroxyprolineBy similarity1
Modified residuei1924-hydroxyprolineBy similarity1
Modified residuei1954-hydroxyprolineBy similarity1
Modified residuei2044-hydroxyprolineBy similarity1
Modified residuei2074-hydroxyprolineBy similarity1
Modified residuei2104-hydroxyprolineBy similarity1
Modified residuei2254-hydroxyprolineBy similarity1
Modified residuei2404-hydroxyprolineBy similarity1
Modified residuei2464-hydroxyprolineBy similarity1
Modified residuei2554-hydroxyprolineBy similarity1
Modified residuei2614-hydroxyprolineBy similarity1
Modified residuei2645-hydroxylysine; alternate1 Publication1
Glycosylationi264O-linked (Gal...) hydroxylysine; alternateBy similarity1
Modified residuei270PhosphoserineBy similarity1
Modified residuei2765-hydroxylysineSequence analysis1
Modified residuei2855-hydroxylysineSequence analysis1
Modified residuei2884-hydroxyprolineBy similarity1
Modified residuei2914-hydroxyprolineBy similarity1
Modified residuei2974-hydroxyprolineBy similarity1
Modified residuei3064-hydroxyprolineBy similarity1
Modified residuei3124-hydroxyprolineBy similarity1
Modified residuei3334-hydroxyprolineBy similarity1
Modified residuei3424-hydroxyprolineBy similarity1
Modified residuei3454-hydroxyprolineBy similarity1
Modified residuei3724-hydroxyprolineBy similarity1
Modified residuei3754-hydroxyprolineBy similarity1
Modified residuei3874-hydroxyprolineBy similarity1
Modified residuei3934-hydroxyprolineBy similarity1
Modified residuei4024-hydroxyprolineBy similarity1
Modified residuei4084-hydroxyprolineBy similarity1
Modified residuei4114-hydroxyprolineBy similarity1
Modified residuei4264-hydroxyprolineBy similarity1
Modified residuei4295-hydroxylysineBy similarity1
Modified residuei4354-hydroxyprolineBy similarity1
Modified residuei4384-hydroxyprolineBy similarity1
Modified residuei4504-hydroxyprolineBy similarity1
Modified residuei4594-hydroxyprolineBy similarity1
Modified residuei4744-hydroxyprolineBy similarity1
Modified residuei4804-hydroxyprolineBy similarity1
Modified residuei4894-hydroxyprolineBy similarity1
Modified residuei4954-hydroxyprolineBy similarity1
Modified residuei5045-hydroxylysineBy similarity1
Modified residuei5134-hydroxyprolineBy similarity1
Modified residuei5224-hydroxyprolineBy similarity1
Modified residuei5284-hydroxyprolineBy similarity1
Modified residuei5344-hydroxyprolineBy similarity1
Modified residuei5434-hydroxyprolineBy similarity1
Modified residuei5464-hydroxyprolineBy similarity1
Modified residuei5554-hydroxyprolineBy similarity1
Modified residuei5644-hydroxyprolineBy similarity1
Modified residuei5704-hydroxyprolineBy similarity1
Modified residuei5824-hydroxyprolineBy similarity1
Modified residuei5914-hydroxyprolineBy similarity1
Modified residuei6004-hydroxyprolineBy similarity1
Modified residuei6034-hydroxyprolineBy similarity1
Modified residuei6214-hydroxyprolineBy similarity1
Modified residuei6394-hydroxyprolineBy similarity1
Modified residuei6454-hydroxyprolineBy similarity1
Modified residuei6514-hydroxyprolineBy similarity1
Modified residuei6574-hydroxyprolineBy similarity1
Modified residuei6634-hydroxyprolineBy similarity1
Modified residuei6694-hydroxyprolineBy similarity1
Modified residuei6814-hydroxyprolineBy similarity1
Modified residuei6904-hydroxyprolineBy similarity1
Modified residuei7024-hydroxyprolineBy similarity1
Modified residuei7144-hydroxyprolineBy similarity1
Modified residuei7174-hydroxyprolineBy similarity1
Modified residuei7234-hydroxyprolineBy similarity1
Modified residuei7294-hydroxyprolineBy similarity1
Modified residuei7384-hydroxyprolineBy similarity1
Modified residuei7505-hydroxylysineBy similarity1
Modified residuei7564-hydroxyprolineBy similarity1
Modified residuei7714-hydroxyprolineBy similarity1
Modified residuei7774-hydroxyprolineBy similarity1
Modified residuei786PhosphoserineBy similarity1
Modified residuei7984-hydroxyprolineBy similarity1
Modified residuei8044-hydroxyprolineBy similarity1
Modified residuei8074-hydroxyprolineBy similarity1
Modified residuei8164-hydroxyprolineBy similarity1
Modified residuei8224-hydroxyprolineBy similarity1
Modified residuei8404-hydroxyprolineBy similarity1
Modified residuei8494-hydroxyprolineBy similarity1
Modified residuei8584-hydroxyprolineBy similarity1
Modified residuei8615-hydroxylysineBy similarity1
Modified residuei8704-hydroxyprolineBy similarity1
Modified residuei8764-hydroxyprolineBy similarity1
Modified residuei8843-hydroxyprolineBy similarity1
Modified residuei8854-hydroxyprolineBy similarity1
Modified residuei8944-hydroxyprolineBy similarity1
Modified residuei8974-hydroxyprolineBy similarity1
Modified residuei9184-hydroxyprolineBy similarity1
Modified residuei9274-hydroxyprolineBy similarity1
Modified residuei9364-hydroxyprolineBy similarity1
Modified residuei9454-hydroxyprolineBy similarity1
Modified residuei9634-hydroxyprolineBy similarity1
Modified residuei9724-hydroxyprolineBy similarity1
Modified residuei9754-hydroxyprolineBy similarity1
Modified residuei9814-hydroxyprolineBy similarity1
Modified residuei9964-hydroxyprolineBy similarity1
Modified residuei10024-hydroxyprolineBy similarity1
Modified residuei10084-hydroxyprolineBy similarity1
Modified residuei10174-hydroxyprolineBy similarity1
Modified residuei10234-hydroxyprolineBy similarity1
Modified residuei10325-hydroxylysineBy similarity1
Modified residuei10444-hydroxyprolineBy similarity1
Modified residuei10474-hydroxyprolineBy similarity1
Modified residuei10504-hydroxyprolineBy similarity1
Modified residuei10955-hydroxylysineBy similarity1
Modified residuei11075-hydroxylysine; alternateBy similarity1
Glycosylationi1107O-linked (Gal...) hydroxylysine; alternateBy similarity1
Modified residuei11194-hydroxyprolineBy similarity1
Modified residuei11224-hydroxyprolineBy similarity1
Modified residuei11254-hydroxyprolineBy similarity1
Modified residuei11434-hydroxyprolineBy similarity1
Modified residuei11584-hydroxyprolineBy similarity1
Modified residuei11633-hydroxyproline1 Publication1
Modified residuei11644-hydroxyprolineBy similarity1
Modified residuei11783-hydroxyproline1 Publication1
Modified residuei11794-hydroxyproline1 Publication1
Modified residuei11813-hydroxyproline1 Publication1
Modified residuei11824-hydroxyproline1 Publication1
Modified residuei11843-hydroxyprolineBy similarity1
Modified residuei11854-hydroxyproline1 Publication1
Modified residuei11884-hydroxyproline1 Publication1
Modified residuei11914-hydroxyprolineBy similarity1
Modified residuei1207Allysine1 Publication1
Disulfide bondi1258 ↔ 1290PROSITE-ProRule annotation
Disulfide bondi1264Interchain (with C-1281)PROSITE-ProRule annotation
Disulfide bondi1281Interchain (with C-1264)PROSITE-ProRule annotation
Disulfide bondi1298 ↔ 1461PROSITE-ProRule annotation
Disulfide bondi1369 ↔ 1414PROSITE-ProRule annotation

Post-translational modificationi

Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.2 Publications
Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline.1 Publication
Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains.By similarity
O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP02453
PeptideAtlasiP02453
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

BgeeiENSBTAG00000013103

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). Interacts with MFAP4 in a Ca (2+)-dependent manner (PubMed:26601954).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiP02453, 1 interactor
STRINGi9913.ENSBTAP00000017420

Structurei

3D structure databases

ProteinModelPortaliP02453
SMRiP02453
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini38 – 96VWFCPROSITE-ProRule annotationAdd BLAST59
Domaini1228 – 1463Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST236

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni162 – 177Nonhelical region (N-terminal)Add BLAST16
Regioni178 – 1191Triple-helical regionAdd BLAST1014
Regioni1192 – 1215Nonhelical region (C-terminal)Add BLAST24

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi744 – 746Cell attachment siteSequence analysis3
Motifi1092 – 1094Cell attachment siteSequence analysis3

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

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG410XNMM LUCA
GeneTreeiENSGT00900000140789
HOGENOMiHOG000085654
HOVERGENiHBG004933
InParanoidiP02453
KOiK06236
OMAiYDGCTSH
OrthoDBiEOG091G03LV
TreeFamiTF344135

Family and domain databases

InterProiView protein in InterPro
IPR008160 Collagen
IPR000885 Fib_collagen_C
IPR001007 VWF_dom
PfamiView protein in Pfam
PF01410 COLFI, 1 hit
PF01391 Collagen, 10 hits
PF00093 VWC, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002078 Fib_collagen_C, 1 hit
SMARTiView protein in SMART
SM00038 COLFI, 1 hit
SM00214 VWC, 1 hit
PROSITEiView protein in PROSITE
PS51461 NC1_FIB, 1 hit
PS01208 VWFC_1, 1 hit
PS50184 VWFC_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti687Q → E AA sequence (PubMed:4673951).Curated1
Sequence conflicti790 – 792Missing AA sequence (PubMed:4359390).Curated3
Sequence conflicti794A → T AA sequence (PubMed:4359390).Curated1
Sequence conflicti1043P → A AA sequence (PubMed:4343808).Curated1
Sequence conflicti1046A → P AA sequence (PubMed:4343808).Curated1
Sequence conflicti1074A → I AA sequence (PubMed:4343808).Curated1
Sequence conflicti1077I → V AA sequence (PubMed:4343808).Curated1
Sequence conflicti1080V → A AA sequence (PubMed:4343808).Curated1
Sequence conflicti1206E → QZ AA sequence (PubMed:11946479).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiCO1A1_BOVIN
AccessioniPrimary (citable) accession number: P02453
Secondary accession number(s): Q3MHM2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 30, 2006
Last modified: April 25, 2018
This is version 145 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health