Col1a1

Functionⁱ

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

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	1266	CalciumBy similarity	1
Metal bindingⁱ	1268	CalciumBy similarity	1
Metal bindingⁱ	1269	Calcium; via carbonyl oxygenBy similarity	1
Metal bindingⁱ	1271	Calcium; via carbonyl oxygenBy similarity	1
Metal bindingⁱ	1274	CalciumBy similarity	1

GO - Molecular functionⁱ

extracellular matrix structural constituent
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
identical protein binding Source: Ensembl
metal ion binding Source: UniProtKB-KW
platelet-derived growth factor binding Source: Ensembl
protease binding Source: Ensembl

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

blood vessel development
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
bone trabecula formation Source: Ensembl
cartilage development involved in endochondral bone morphogenesis Source: Ensembl
cellular response to amino acid stimulus Source: Ensembl
cellular response to epidermal growth factor stimulus
Source: RGD
Inferred from expression patternⁱ
- 2016852
cellular response to fibroblast growth factor stimulus
Source: RGD
Inferred from expression patternⁱ
- 16972247
cellular response to fluoride
Source: RGD
Inferred from expression patternⁱ
- 21093551
cellular response to mechanical stimulus
Source: RGD
Inferred from expression patternⁱ
- 22615126
cellular response to retinoic acid
Source: RGD
Inferred from expression patternⁱ
- 1921334
- 21181362
cellular response to transforming growth factor beta stimulus
Source: UniProtKB
Inferred from expression patternⁱ
- 19362560
cellular response to tumor necrosis factor
Source: RGD
Inferred from expression patternⁱ
- 17485223
cellular response to vitamin E
Source: RGD
Inferred from expression patternⁱ
- 23722449
collagen-activated tyrosine kinase receptor signaling pathway
Source: MGI
Inferred from direct assayⁱ
- 10970885
collagen biosynthetic process Source: Ensembl
collagen fibril organization Source: Ensembl
embryonic skeletal system development Source: Ensembl
endochondral ossification Source: Ensembl
extracellular matrix organization
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
face morphogenesis Source: Ensembl
intramembranous ossification Source: Ensembl
negative regulation of cell-substrate adhesion Source: Ensembl
ossification
Source: RGD
Inferred from expression patternⁱ
- 14595530
osteoblast differentiation Source: Ensembl
positive regulation of canonical Wnt signaling pathway Source: Ensembl
positive regulation of cell migration Source: Ensembl
positive regulation of epithelial to mesenchymal transition Source: Ensembl
positive regulation of transcription, DNA-templated Source: Ensembl
protein heterotrimerization Source: Ensembl
protein localization to nucleus Source: Ensembl
protein transport Source: Ensembl
response to cAMP
Source: RGD
Inferred from expression patternⁱ
- 10679825
response to corticosteroid
Source: RGD
Inferred from expression patternⁱ
- 14993121
response to drug
Source: RGD
Inferred from expression patternⁱ
- 23069578
response to estradiol
Source: RGD
Inferred from expression patternⁱ
- 2456904
response to fluoride
Source: RGD
Inferred from expression patternⁱ
- 15552839
response to hydrogen peroxide
Source: RGD
Inferred from expression patternⁱ
- 10051504
response to hyperoxia
Source: RGD
Inferred from expression patternⁱ
- 11918316
response to mechanical stimulus
Source: RGD
Inferred from expression patternⁱ
- 11748224
- 18988763
response to nutrient
Source: RGD
Inferred from expression patternⁱ
- 15042712
response to nutrient levels
Source: RGD
Inferred from expression patternⁱ
- 20397200
response to peptide hormone
Source: RGD
Inferred from expression patternⁱ
- 10679825
response to steroid hormone
Source: RGD
Inferred from expression patternⁱ
- 21842416
sensory perception of sound Source: Ensembl
skeletal system development
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
skin development
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
skin morphogenesis Source: Ensembl
tooth eruption
Source: RGD
Inferred from expression patternⁱ
- 12351664
tooth mineralization Source: Ensembl
visual perception Source: Ensembl
wound healing
Source: RGD
Inferred from mutant phenotypeⁱ
- 20647009

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Ligand	Calcium, Metal-binding

Ligand

Calcium, Metal-binding

Enzyme and pathway databases

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

Reactomeⁱ

R-RNO-114604 GPVI-mediated activation cascade
R-RNO-1442490 Collagen degradation
R-RNO-1474244 Extracellular matrix organization
R-RNO-1650814 Collagen biosynthesis and modifying enzymes
R-RNO-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-RNO-2022090 Assembly of collagen fibrils and other multimeric structures
R-RNO-202733 Cell surface interactions at the vascular wall
R-RNO-216083 Integrin cell surface interactions
R-RNO-2214320 Anchoring fibril formation
R-RNO-2243919 Crosslinking of collagen fibrils
R-RNO-3000171 Non-integrin membrane-ECM interactions
R-RNO-3000178 ECM proteoglycans
R-RNO-430116 GP1b-IX-V activation signalling
R-RNO-75892 Platelet Adhesion to exposed collagen
R-RNO-76009 Platelet Aggregation (Plug Formation)
R-RNO-8874081 MET activates PTK2 signaling
R-RNO-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
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Chromosome 10

Organism-specific databases

Rat genome database More...RGDⁱ	61817 Col1a1

RGDⁱ

61817 Col1a1

Keywords - Cellular componentⁱ

Extracellular matrix, Secreted

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Signal peptideⁱ	1 – 22	Sequence analysisAdd BLAST	22
PropeptideⁱPRO_0000043358	23 – 151	N-terminal propeptide1 PublicationAdd BLAST	129
ChainⁱPRO_0000043359	152 – 1207	Collagen alpha-1(I) chainAdd BLAST	1056
PropeptideⁱPRO_0000043360	1208 – 1453	C-terminal propeptideBy similarityAdd BLAST	246

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	56	N-linked (GlcNAc...) asparagineSequence analysis	1
Modified residueⁱ	152	Pyrrolidone carboxylic acid1 Publication	1
Modified residueⁱ	160	Allysine1 Publication	1
Modified residueⁱ	161	PhosphoserineCombined sources	1
Modified residueⁱ	179	4-hydroxyproline1 Publication	1
Modified residueⁱ	182	4-hydroxyproline1 Publication	1
Modified residueⁱ	185	4-hydroxyproline1 Publication	1
Modified residueⁱ	194	4-hydroxyproline1 Publication	1
Modified residueⁱ	197	4-hydroxyproline1 Publication	1
Modified residueⁱ	200	4-hydroxyproline1 Publication	1
Modified residueⁱ	215	4-hydroxyprolineBy similarity	1
Modified residueⁱ	230	4-hydroxyprolineBy similarity	1
Modified residueⁱ	236	4-hydroxyprolineBy similarity	1
Modified residueⁱ	245	4-hydroxyprolineBy similarity	1
Modified residueⁱ	251	4-hydroxyprolineBy similarity	1
Modified residueⁱ	254	5-hydroxylysine; alternate1 Publication	1
Glycosylationⁱ	254	O-linked (Gal...) hydroxylysine; alternate1 Publication	1
Modified residueⁱ	260	PhosphoserineCombined sources	1
Modified residueⁱ	278	4-hydroxyprolineBy similarity	1
Modified residueⁱ	281	4-hydroxyprolineBy similarity	1
Modified residueⁱ	287	4-hydroxyprolineBy similarity	1
Modified residueⁱ	296	4-hydroxyprolineBy similarity	1
Modified residueⁱ	302	4-hydroxyprolineBy similarity	1
Modified residueⁱ	323	4-hydroxyprolineBy similarity	1
Modified residueⁱ	332	4-hydroxyprolineBy similarity	1
Modified residueⁱ	335	4-hydroxyprolineBy similarity	1
Modified residueⁱ	362	4-hydroxyprolineBy similarity	1
Modified residueⁱ	365	4-hydroxyprolineBy similarity	1
Modified residueⁱ	377	4-hydroxyprolineBy similarity	1
Modified residueⁱ	383	4-hydroxyprolineBy similarity	1
Modified residueⁱ	392	4-hydroxyprolineBy similarity	1
Modified residueⁱ	398	4-hydroxyprolineBy similarity	1
Modified residueⁱ	401	4-hydroxyprolineBy similarity	1
Modified residueⁱ	416	4-hydroxyprolineBy similarity	1
Modified residueⁱ	419	5-hydroxylysineBy similarity	1
Modified residueⁱ	425	4-hydroxyprolineBy similarity	1
Modified residueⁱ	428	4-hydroxyprolineBy similarity	1
Modified residueⁱ	440	4-hydroxyprolineBy similarity	1
Modified residueⁱ	449	4-hydroxyprolineBy similarity	1
Modified residueⁱ	464	4-hydroxyprolineBy similarity	1
Modified residueⁱ	470	4-hydroxyprolineBy similarity	1
Modified residueⁱ	479	4-hydroxyprolineBy similarity	1
Modified residueⁱ	485	4-hydroxyprolineBy similarity	1
Modified residueⁱ	494	5-hydroxylysineBy similarity	1
Modified residueⁱ	503	4-hydroxyprolineBy similarity	1
Modified residueⁱ	512	4-hydroxyprolineBy similarity	1
Modified residueⁱ	518	4-hydroxyprolineBy similarity	1
Modified residueⁱ	524	4-hydroxyprolineBy similarity	1
Modified residueⁱ	533	4-hydroxyprolineBy similarity	1
Modified residueⁱ	536	4-hydroxyprolineBy similarity	1
Modified residueⁱ	545	4-hydroxyprolineBy similarity	1
Modified residueⁱ	554	4-hydroxyprolineBy similarity	1
Modified residueⁱ	560	4-hydroxyprolineBy similarity	1
Modified residueⁱ	572	4-hydroxyprolineBy similarity	1
Modified residueⁱ	581	4-hydroxyprolineBy similarity	1
Modified residueⁱ	590	4-hydroxyprolineBy similarity	1
Modified residueⁱ	593	4-hydroxyprolineBy similarity	1
Modified residueⁱ	611	4-hydroxyprolineBy similarity	1
Modified residueⁱ	629	4-hydroxyprolineBy similarity	1
Modified residueⁱ	635	4-hydroxyprolineBy similarity	1
Modified residueⁱ	641	4-hydroxyprolineBy similarity	1
Modified residueⁱ	647	4-hydroxyprolineBy similarity	1
Modified residueⁱ	653	4-hydroxyprolineBy similarity	1
Modified residueⁱ	659	4-hydroxyprolineBy similarity	1
Modified residueⁱ	671	4-hydroxyprolineBy similarity	1
Modified residueⁱ	680	4-hydroxyprolineBy similarity	1
Modified residueⁱ	692	4-hydroxyprolineBy similarity	1
Modified residueⁱ	704	4-hydroxyprolineBy similarity	1
Modified residueⁱ	707	4-hydroxyprolineBy similarity	1
Modified residueⁱ	713	4-hydroxyprolineBy similarity	1
Modified residueⁱ	719	4-hydroxyprolineBy similarity	1
Modified residueⁱ	728	4-hydroxyprolineBy similarity	1
Modified residueⁱ	740	5-hydroxylysineBy similarity	1
Modified residueⁱ	746	4-hydroxyprolineBy similarity	1
Modified residueⁱ	761	4-hydroxyprolineBy similarity	1
Modified residueⁱ	767	4-hydroxyprolineBy similarity	1
Modified residueⁱ	776	PhosphoserineCombined sources	1
Modified residueⁱ	788	4-hydroxyprolineBy similarity	1
Modified residueⁱ	794	4-hydroxyprolineBy similarity	1
Modified residueⁱ	797	4-hydroxyprolineBy similarity	1
Modified residueⁱ	806	4-hydroxyprolineBy similarity	1
Modified residueⁱ	812	4-hydroxyprolineBy similarity	1
Modified residueⁱ	830	4-hydroxyprolineBy similarity	1
Modified residueⁱ	839	4-hydroxyprolineBy similarity	1
Modified residueⁱ	848	4-hydroxyprolineBy similarity	1
Modified residueⁱ	851	5-hydroxylysineBy similarity	1
Modified residueⁱ	860	4-hydroxyprolineBy similarity	1
Modified residueⁱ	866	4-hydroxyprolineBy similarity	1
Modified residueⁱ	874	3-hydroxyprolineBy similarity	1
Modified residueⁱ	875	4-hydroxyprolineBy similarity	1
Modified residueⁱ	884	4-hydroxyprolineBy similarity	1
Modified residueⁱ	887	4-hydroxyprolineBy similarity	1
Modified residueⁱ	908	4-hydroxyprolineBy similarity	1
Modified residueⁱ	917	4-hydroxyprolineBy similarity	1
Modified residueⁱ	926	4-hydroxyprolineBy similarity	1
Modified residueⁱ	935	4-hydroxyprolineBy similarity	1
Modified residueⁱ	953	4-hydroxyprolineBy similarity	1
Modified residueⁱ	962	4-hydroxyprolineBy similarity	1
Modified residueⁱ	965	4-hydroxyprolineBy similarity	1
Modified residueⁱ	971	4-hydroxyprolineBy similarity	1
Modified residueⁱ	986	4-hydroxyprolineBy similarity	1
Modified residueⁱ	992	4-hydroxyprolineBy similarity	1
Modified residueⁱ	998	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1007	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1013	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1022	5-hydroxylysineBy similarity	1
Modified residueⁱ	1034	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1037	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1040	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1085	5-hydroxylysineBy similarity	1
Modified residueⁱ	1097	5-hydroxylysine; alternateBy similarity	1
Glycosylationⁱ	1097	O-linked (Gal...) hydroxylysine; alternateBy similarity	1
Modified residueⁱ	1109	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1112	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1115	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1133	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1148	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1153	3-hydroxyprolineBy similarity	1
Modified residueⁱ	1154	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1168	3-hydroxyprolineBy similarity	1
Modified residueⁱ	1169	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1171	3-hydroxyprolineBy similarity	1
Modified residueⁱ	1172	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1174	3-hydroxyprolineBy similarity	1
Modified residueⁱ	1175	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1178	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1181	4-hydroxyprolineBy similarity	1
Modified residueⁱ	1197	AllysineBy similarity	1
Disulfide bondⁱ	1248 ↔ 1280	PROSITE-ProRule annotation
Disulfide bondⁱ	1254	Interchain (with C-1271)PROSITE-ProRule annotation
Disulfide bondⁱ	1271	Interchain (with C-1254)PROSITE-ProRule annotation
Disulfide bondⁱ	1288 ↔ 1451	PROSITE-ProRule annotation
Glycosylationⁱ	1354	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	1359 ↔ 1404	PROSITE-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.1 Publication

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.By similarity

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.1 Publication

Keywords - PTMⁱ

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

Proteomic databases

PaxDbⁱ	P02454
PRIDEⁱ	P02454

PTM databases

iPTMnetⁱ	P02454
PhosphoSitePlusⁱ	P02454

Expressionⁱ

Tissue specificityⁱ

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

Gene expression databases

Bgeeⁱ	ENSRNOG00000003897 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue
Genevisibleⁱ	P02454 RN

Interactionⁱ

Subunit structureⁱ

Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2 (PubMed:15817460). Interacts with TRAM2. Interacts with MFAP4 in a Ca (2+)-dependent manner.By similarity1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
MRC2	Q9UBG0	2	EBI-915744,EBI-1104992	From Homo sapiens.

With

Entry

#Exp.

IntAct

Notes

MRC2

Q9UBG0

2

EBI-915744,EBI-1104992

From Homo sapiens.

GO - Molecular functionⁱ

identical protein binding Source: Ensembl
platelet-derived growth factor binding Source: Ensembl
protease binding Source: Ensembl

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	248045, 1 interactor
ComplexPortalⁱ	CPX-3104 Collagen type I trimer
Database of interacting proteins More...DIPⁱ	DIP-36887N
IntActⁱ	P02454, 4 interactors
STRINGⁱ	10116.ENSRNOP00000005311

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P02454
SMRⁱ	P02454
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P02454

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	29 – 87	VWFCPROSITE-ProRule annotationAdd BLAST		59
Domainⁱ	1218 – 1453	Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST		236

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	152 – 167	Nonhelical region (N-terminal)Add BLAST	16
Regionⁱ	168 – 1181	Triple-helical regionAdd BLAST	1014
Regionⁱ	1176 – 1186	Major antigenic determinant (of neutral salt-extracted rat skin collagen)Add BLAST	11
Regionⁱ	1182 – 1207	Nonhelical region (C-terminal)Add BLAST	26

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	734 – 736	Cell attachment siteSequence analysis		3
Motifⁱ	1082 – 1084	Cell attachment siteSequence analysis		3

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

Sequence similaritiesⁱ

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation

Keywords - Domainⁱ

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGⁱ	KOG3544 Eukaryota ENOG410XNMM LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00900000140789
HOGENOMⁱ	HOG000085654
HOVERGENⁱ	HBG004933
InParanoidⁱ	P02454
KEGG Orthology (KO) More...KOⁱ	K06236
OMAⁱ	YDGCTSH
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G03LV
PhylomeDBⁱ	P02454
TreeFamⁱ	TF344135

Family and domain databases

InterProⁱ	View protein in InterPro IPR008160 Collagen IPR000885 Fib_collagen_C IPR001007 VWF_dom
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01410 COLFI, 1 hit PF01391 Collagen, 12 hits PF00093 VWC, 1 hit
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD002078 Fib_collagen_C, 1 hit
SMARTⁱ	View protein in SMART SM00038 COLFI, 1 hit SM00214 VWC, 1 hit
PROSITEⁱ	View 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.

P02454-1 [UniParc]FASTA Add 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 key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	143	P → L in CAB01633 (PubMed:10065941).Curated	1
Sequence conflictⁱ	202	A → G in CAB01633 (PubMed:10065941).Curated	1
Sequence conflictⁱ	209	R → P in CAB01633 (PubMed:10065941).Curated	1
Sequence conflictⁱ	232	E → Q AA sequence (PubMed:4327399).Curated	1
Sequence conflictⁱ	268	D → N AA sequence (PubMed:5411206).Curated	1
Sequence conflictⁱ	286	A → T in CAB01633 (PubMed:10065941).Curated	1
Sequence conflictⁱ	307	S → T in CAB01633 (PubMed:10065941).Curated	1
Sequence conflictⁱ	313	N → D AA sequence (PubMed:4335087).Curated	1
Sequence conflictⁱ	421	N → T in CAB01633 (PubMed:10065941).Curated	1
Sequence conflictⁱ	497	A → S in CAB01633 (PubMed:10065941).Curated	1
Sequence conflictⁱ	773	T → A in CAB01633 (PubMed:10065941).Curated	1
Sequence conflictⁱ	794	P → A in CAB01633 (PubMed:10065941).Curated	1
Sequence conflictⁱ	958	E → K in CAB01633 (PubMed:10065941).Curated	1
Sequence conflictⁱ	1111	S → P AA sequence (PubMed:4126850).Curated	1
Sequence conflictⁱ	1163	S → A AA sequence (PubMed:4126850).Curated	1
Sequence conflictⁱ	1166	A → S AA sequence (PubMed:4126850).Curated	1
Sequence conflictⁱ	1187	F → L AA sequence (PubMed:4636751).Curated	1
Sequence conflictⁱ	1190	L → F AA sequence (PubMed:4636751).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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
NCBI Reference Sequences More...RefSeqⁱ	NP_445756.1, NM_053304.1
UniGeneⁱ	Rn.2953

Genome annotation databases

Ensemblⁱ	ENSRNOT00000005311; ENSRNOP00000005311; ENSRNOG00000003897
GeneIDⁱ	29393
KEGGⁱ	rno:29393
UCSC genome browser More...UCSCⁱ	RGD:61817 rat

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P02454	Type I-alpha 1 collagen (Fragment)		RAT		233	UniRef100_P02454
Uncharacterized protein (Fragment)		Phenylobacterium kunshanense		180

Protein	Similar proteins		Species	Score	Length	Source
P02454	Collagen alpha-1(I) chain	)	HUMAN		1464	UniRef90_P02452
Collagen alpha-1(I) chain		BOVIN		1463
Collagen alpha-1(I) chain		CANLF		1460
COL1A1 isoform 4		PONAB		1467
Uncharacterized protein		PIG		1466
+87

Protein	Similar proteins		Species	Score	Length	Source
P02454	Collagen alpha-1(I) chain	)	HUMAN		1464	UniRef50_P02452
Collagen alpha-1(I) chain		BOVIN		1463
Collagen alpha-1(I) chain		CANLF		1460
Collagen alpha-2(I) chain		ONCMY		1356
Collagen alpha-2(I) chain	)	RAT		1372
+1844

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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
SMRⁱ	P02454
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	248045, 1 interactor
ComplexPortalⁱ	CPX-3104 Collagen type I trimer
DIPⁱ	DIP-36887N
IntActⁱ	P02454, 4 interactors
STRINGⁱ	10116.ENSRNOP00000005311

PTM databases

iPTMnetⁱ	P02454
PhosphoSitePlusⁱ	P02454

Proteomic databases

PaxDbⁱ	P02454
PRIDEⁱ	P02454

Protocols and materials databases

Structural Biology Knowledgebase	Search...

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	KOG3544 Eukaryota ENOG410XNMM LUCA
GeneTreeⁱ	ENSGT00900000140789
HOGENOMⁱ	HOG000085654
HOVERGENⁱ	HBG004933
InParanoidⁱ	P02454
KOⁱ	K06236
OMAⁱ	YDGCTSH
OrthoDBⁱ	EOG091G03LV
PhylomeDBⁱ	P02454
TreeFamⁱ	TF344135

Enzyme and pathway databases

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

Reactomeⁱ

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

Miscellaneous databases

EvolutionaryTraceⁱ	P02454
Protein Ontology More...PROⁱ	PR:P02454

Gene expression databases

Bgeeⁱ	ENSRNOG00000003897 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue
Genevisibleⁱ	P02454 RN

Family and domain databases

InterProⁱ	View protein in InterPro IPR008160 Collagen IPR000885 Fib_collagen_C IPR001007 VWF_dom
Pfamⁱ	View protein in Pfam PF01410 COLFI, 1 hit PF01391 Collagen, 12 hits PF00093 VWC, 1 hit
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD002078 Fib_collagen_C, 1 hit
SMARTⁱ	View protein in SMART SM00038 COLFI, 1 hit SM00214 VWC, 1 hit
PROSITEⁱ	View protein in PROSITE PS51461 NC1_FIB, 1 hit PS01208 VWFC_1, 1 hit PS50184 VWFC_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CO1A1_RAT
Accessionⁱ	P02454Primary (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:	November 7, 2018
	This is version 166 of the entry and version 5 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

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UniProtKB - P02454 (CO1A1_RAT)

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Collagen alpha-1(I) chain

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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Functionⁱ

GO - Molecular functionⁱ

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Names & Taxonomyⁱ

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Keywords - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

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Keywords - Domainⁱ

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Keywords - Technical termⁱ