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UniProtKB - P02454 (CO1A1_RAT)
Protein
Collagen alpha-1(I) chain
Gene
Col1a1
Organism
Rattus norvegicus (Rat)
Status
Functioni
Type I collagen is a member of group I collagen (fibrillar forming collagen).
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | 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: RGD
- identical protein binding Source: RGD
- metal ion binding Source: UniProtKB-KW
- platelet-derived growth factor binding Source: RGD
- protease binding Source: RGD
GO - Biological processi
- blood vessel development Source: RGD
- bone trabecula formation Source: RGD
- cartilage development involved in endochondral bone morphogenesis Source: RGD
- cellular response to amino acid stimulus Source: RGD
- cellular response to epidermal growth factor stimulus Source: RGD
- cellular response to fibroblast growth factor stimulus Source: RGD
- cellular response to fluoride Source: RGD
- cellular response to mechanical stimulus Source: RGD
- cellular response to retinoic acid Source: RGD
- cellular response to transforming growth factor beta stimulus Source: UniProtKB
- cellular response to tumor necrosis factor Source: RGD
- cellular response to vitamin E Source: RGD
- collagen-activated tyrosine kinase receptor signaling pathway Source: MGI
- collagen biosynthetic process Source: RGD
- collagen fibril organization Source: RGD
- embryonic skeletal system development Source: RGD
- endochondral ossification Source: RGD
- extracellular matrix organization Source: GO_Central
- face morphogenesis Source: RGD
- intramembranous ossification Source: RGD
- negative regulation of cell-substrate adhesion Source: RGD
- ossification Source: RGD
- osteoblast differentiation Source: RGD
- positive regulation of canonical Wnt signaling pathway Source: RGD
- positive regulation of cell migration Source: RGD
- positive regulation of epithelial to mesenchymal transition Source: RGD
- positive regulation of transcription, DNA-templated Source: RGD
- protein localization to nucleus Source: RGD
- protein transport Source: RGD
- response to cAMP Source: RGD
- response to corticosteroid Source: RGD
- response to estradiol Source: RGD
- response to fluoride Source: RGD
- response to hydrogen peroxide Source: RGD
- response to hyperoxia Source: RGD
- response to mechanical stimulus Source: RGD
- response to nutrient Source: RGD
- response to nutrient levels Source: RGD
- response to peptide hormone Source: RGD
- response to steroid hormone Source: RGD
- response to xenobiotic stimulus Source: RGD
- sensory perception of sound Source: RGD
- skeletal system development Source: RGD
- skeletal system morphogenesis Source: RGD
- skin development Source: RGD
- skin morphogenesis Source: RGD
- tooth eruption Source: RGD
- tooth mineralization Source: RGD
- visual perception Source: RGD
- wound healing Source: RGD
Keywordsi
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-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) chainAlternative name(s): Alpha-1 type I collagen |
Gene namesi | Name:Col1a1 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 61817, Col1a1 |
Subcellular locationi
Extracellular region or secreted
- extracellular matrix PROSITE-ProRule annotation
Endoplasmic reticulum
- endoplasmic reticulum Source: RGD
Extracellular region or secreted
- extracellular region Source: Reactome
- extracellular space Source: RGD
Golgi apparatus
- Golgi apparatus Source: RGD
Other locations
- collagen trimer Source: RGD
- collagen type I trimer Source: RGD
- cytoplasm Source: RGD
- extracellular matrix Source: RGD
- secretory granule Source: RGD
Keywords - Cellular componenti
Extracellular matrix, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | 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 | Graphical view | 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 acidProteomic databases
jPOSTi | P02454 |
PaxDbi | P02454 |
PRIDEi | P02454 |
PTM databases
GlyGeni | P02454, 4 sites |
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 skeletal muscle tissue and 21 other tissues |
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 PublicationBinary interactionsi
P02454
With | #Exp. | IntAct |
---|---|---|
MRC2 [Q9UBG0] from Homo sapiens. | 2 | EBI-915744,EBI-1104992 |
GO - Molecular functioni
- identical protein binding Source: RGD
- platelet-derived growth factor binding Source: RGD
- protease binding Source: RGD
Protein-protein interaction databases
BioGRIDi | 248045, 4 interactors |
ComplexPortali | CPX-3104, Collagen type I trimer |
DIPi | DIP-36887N |
IntActi | P02454, 5 interactors |
STRINGi | 10116.ENSRNOP00000005311 |
Structurei
3D structure databases
AlphaFoldDBi | P02454 |
SMRi | P02454 |
ModBasei | Search... |
PDBe-KBi | 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 | Graphical view | Length |
---|---|---|---|---|
Regioni | 97 – 1206 | DisorderedSequence analysisAdd BLAST | 1110 | |
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 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 108 – 144 | Pro residuesSequence analysisAdd BLAST | 37 | |
Compositional biasi | 172 – 215 | Pro residuesSequence analysisAdd BLAST | 44 | |
Compositional biasi | 538 – 554 | Pro residuesSequence analysisAdd BLAST | 17 | |
Compositional biasi | 831 – 845 | Pro residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 877 – 891 | Pro residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 1165 – 1184 | Pro residuesSequence analysisAdd BLAST | 20 |
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, SignalPhylogenomic databases
eggNOGi | KOG3544, Eukaryota |
GeneTreei | ENSGT00940000156584 |
HOGENOMi | CLU_001074_2_3_1 |
InParanoidi | P02454 |
OMAi | YYDRDVW |
OrthoDBi | 337699at2759 |
PhylomeDBi | P02454 |
TreeFami | TF344135 |
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 |
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 |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All
P02454-1 [UniParc]FASTAAdd to basket
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
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A8I5ZRN2 | A0A8I5ZRN2_RAT | Collagen alpha-1(I) chain | Col1a1 | 1,369 | Annotation score: | ||
A0A8I6G8P4 | A0A8I6G8P4_RAT | Collagen alpha-1(I) chain | Col1a1 | 1,444 | Annotation score: | ||
A0A8I6GG08 | A0A8I6GG08_RAT | Collagen alpha-1(I) chain | Col1a1 | 1,388 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | 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 |
RefSeqi | NP_445756.1, NM_053304.1 |
Genome annotation databases
Ensembli | ENSRNOT00000005311; ENSRNOP00000005311; ENSRNOG00000003897 |
GeneIDi | 29393 |
KEGGi | rno:29393 |
UCSCi | RGD:61817, rat |
Similar proteinsi
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 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi 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 | [»] | |
AlphaFoldDBi | P02454 | |||||
SMRi | P02454 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 248045, 4 interactors |
ComplexPortali | CPX-3104, Collagen type I trimer |
DIPi | DIP-36887N |
IntActi | P02454, 5 interactors |
STRINGi | 10116.ENSRNOP00000005311 |
PTM databases
GlyGeni | P02454, 4 sites |
iPTMneti | P02454 |
PhosphoSitePlusi | P02454 |
Proteomic databases
jPOSTi | P02454 |
PaxDbi | P02454 |
PRIDEi | P02454 |
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 |
GeneTreei | ENSGT00940000156584 |
HOGENOMi | CLU_001074_2_3_1 |
InParanoidi | P02454 |
OMAi | YYDRDVW |
OrthoDBi | 337699at2759 |
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-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 |
PROi | PR:P02454 |
Gene expression databases
Bgeei | ENSRNOG00000003897, Expressed in skeletal muscle tissue and 21 other tissues |
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 |
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 |
MobiDBi | 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: | May 25, 2022 | |
This is version 184 of the entry and version 5 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families