UniProtKB - P13941 (CO3A1_RAT)
Protein
Collagen alpha-1(III) chain
Gene
Col3a1
Organism
Rattus norvegicus (Rat)
Status
Functioni
Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12 (By similarity).By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 1277 | CalciumBy similarity | 1 | |
Metal bindingi | 1279 | CalciumBy similarity | 1 | |
Metal bindingi | 1280 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 1282 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 1285 | CalciumBy similarity | 1 |
GO - Molecular functioni
- extracellular matrix structural constituent Source: RGD
- integrin binding Source: RGD
- metal ion binding Source: UniProtKB-KW
- platelet-derived growth factor binding Source: RGD
- protease binding Source: RGD
- SMAD binding Source: RGD
GO - Biological processi
- aorta smooth muscle tissue morphogenesis Source: RGD
- blood vessel development Source: RGD
- cell-matrix adhesion Source: RGD
- cellular response to amino acid stimulus Source: RGD
- cerebral cortex development Source: UniProtKB
- collagen fibril organization Source: RGD
- digestive tract development Source: RGD
- extracellular matrix organization Source: GO_Central
- heart development Source: RGD
- integrin-mediated signaling pathway Source: RGD
- negative regulation of immune response Source: RGD
- negative regulation of neuron migration Source: UniProtKB
- peptide cross-linking Source: RGD
- positive regulation of Rho protein signal transduction Source: UniProtKB
- response to cytokine Source: RGD
- response to mechanical stimulus Source: RGD
- response to radiation Source: RGD
- skeletal system development Source: RGD
- skin development Source: RGD
- supramolecular fiber organization Source: RGD
- transforming growth factor beta receptor signaling pathway Source: RGD
- wound healing Source: RGD
Keywordsi
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
Reactomei | R-RNO-1442490, Collagen degradation R-RNO-1474244, Extracellular matrix organization R-RNO-1650814, Collagen biosynthesis and modifying enzymes R-RNO-186797, Signaling by PDGF 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-216083, Integrin cell surface interactions R-RNO-3000171, Non-integrin membrane-ECM interactions R-RNO-3000178, ECM proteoglycans R-RNO-419037, NCAM1 interactions R-RNO-8874081, MET activates PTK2 signaling R-RNO-8948216, Collagen chain trimerization |
Names & Taxonomyi
Protein namesi | Recommended name: Collagen alpha-1(III) chain |
Gene namesi | Name:Col3a1 |
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 | 71029, Col3a1 |
Subcellular locationi
Extracellular region or secreted
- extracellular matrix PROSITE-ProRule annotation
Extracellular region or secreted
- extracellular space Source: RGD
Other locations
- collagen trimer Source: RGD
- collagen type III trimer Source: RGD
- collagen-containing extracellular matrix Source: RGD
- extracellular matrix Source: RGD
Keywords - Cellular componenti
Extracellular matrix, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 23 | By similarityAdd BLAST | 23 | |
PropeptideiPRO_0000005746 | 24 – 154 | N-terminal propeptideBy similarityAdd BLAST | 131 | |
ChainiPRO_0000005747 | 155 – 1218 | Collagen alpha-1(III) chainAdd BLAST | 1064 | |
PropeptideiPRO_0000043408 | 1219 – 1463 | C-terminal propeptideBy similarityAdd BLAST | 245 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 262 | 5-hydroxylysine; alternateBy similarity | 1 | |
Glycosylationi | 262 | O-linked (Gal...) hydroxylysine; alternateBy similarity | 1 | |
Modified residuei | 283 | 5-hydroxylysineBy similarity | 1 | |
Modified residuei | 859 | 5-hydroxylysineBy similarity | 1 | |
Modified residuei | 976 | 5-hydroxylysineBy similarity | 1 | |
Modified residuei | 1093 | 5-hydroxylysineBy similarity | 1 | |
Modified residuei | 1105 | 5-hydroxylysineBy similarity | 1 | |
Disulfide bondi | 1195 | InterchainPROSITE-ProRule annotation | ||
Disulfide bondi | 1196 | InterchainPROSITE-ProRule annotation | ||
Disulfide bondi | 1259 ↔ 1291 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1265 | Interchain (with C-1282)PROSITE-ProRule annotation | ||
Disulfide bondi | 1282 | Interchain (with C-1265)PROSITE-ProRule annotation | ||
Disulfide bondi | 1299 ↔ 1461 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1369 ↔ 1414 | PROSITE-ProRule annotation |
Post-translational modificationi
O-glycosylated.By similarity
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Keywords - PTMi
Disulfide bond, Glycoprotein, HydroxylationProteomic databases
PaxDbi | P13941 |
PRIDEi | P13941 |
PTM databases
GlyGeni | P13941, 1 site |
iPTMneti | P13941 |
PhosphoSitePlusi | P13941 |
Expressioni
Gene expression databases
Bgeei | ENSRNOG00000003357, Expressed in esophagus and 21 other tissues |
Genevisiblei | P13941, RN |
Interactioni
Subunit structurei
Trimers of identical alpha 1(III) chains. The chains are linked to each other by interchain disulfide bonds. Trimers are also cross-linked via hydroxylysines.
Interacts with ADGRG1 (By similarity).
By similarityGO - Molecular functioni
- integrin binding Source: RGD
- platelet-derived growth factor binding Source: RGD
- protease binding Source: RGD
- SMAD binding Source: RGD
Protein-protein interaction databases
BioGRIDi | 249898, 1 interactor |
IntActi | P13941, 2 interactors |
STRINGi | 10116.ENSRNOP00000004956 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 31 – 90 | VWFCPROSITE-ProRule annotationAdd BLAST | 60 | |
Domaini | 1229 – 1463 | Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST | 235 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 155 – 169 | Nonhelical region (N-terminal)Add BLAST | 15 | |
Regioni | 170 – 1195 | Triple-helical regionAdd BLAST | 1026 |
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, SignalPhylogenomic databases
eggNOGi | KOG3544, Eukaryota |
GeneTreei | ENSGT00940000161229 |
HOGENOMi | CLU_001074_2_3_1 |
InParanoidi | P13941 |
OMAi | SPQFESY |
OrthoDBi | 1406711at2759 |
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, 4 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 |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P13941-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MMSFVQCGTW FLLTLLHPSL ILAQQSNVDE LGCNYLGQSY ESRDVWKPEP
60 70 80 90 100
CQICVCDSGS VLCDDIMCDD EPLDCPNPEI PFGECCAICP QPSTPAPVIP
110 120 130 140 150
DGNRPQGPKG DPGPPGIPGR NGDPGLPGQP GLPGPPGSPG ICESCPTGGQ
160 170 180 190 200
NYSPQFDSYD VKSGVGGMGG YPGPAGPPGP PGPPGSSGHP GSPGSPGYQG
210 220 230 240 250
PPGEPGQAGP AGPPGPPGAI GPSGPAGKDG ESGRPGRPGE RGLPGPPGIK
260 270 280 290 300
GPAGIPGFPG MKGHRGFDGR NGEKGETGAP GLKGENGLPG DNGAPGPMGP
310 320 330 340 350
RGAPGERGRP GLPGAAGARG NDGARGSDGQ PGPPGPPGTA GFPGSPGAKG
360 370 380 390 400
EVGPAGSPGS NGSPGQRGEP GPQGHAGAQG PPGPPGNNGS PGGKGEMGPA
410 420 430 440 450
GIPGAPGLLG ARGPPGPAGA NGAPGQRGPS GEPGKNGAKG EPGARGERGE
460 470 480 490 500
AGSPGIPGPK GEDGKDGSPG EPGANGVPGN PGERGAPGFR GPAGPNGAPG
510 520 530 540 550
EKGPAGERGG PGPAGPRGVA GEPGRDGTPG GPGIRGMPGS PGGPGNDGKP
560 570 580 590 600
GPPGSQGESG RPGPPGPSGP RGQPGVMGFP GPKGNDGAPG KNGERGGPGG
610 620 630 640 650
PGLPGPAGKN GETGPQGPPG PTGAPGDKGD AGPPGPQGLQ GIPGTSGPPG
660 670 680 690 700
ENGKPGEPGP KGEAGAPGVP GGKGDSGAPG ERGPPGTAGT PGLRGGAGPP
710 720 730 740 750
GPEGGKGPAG PPGPPGTSGP PGLQGMPGER GGPGSPGPKG EKGEPGGAGA
760 770 780 790 800
DGVPGKDGPR GPAGPIGPPG PAGQPGDKGE GGAPGLPGIA GPRGGPGERG
810 820 830 840 850
EHGPPGPAGF PGAPGQNGEP GAKGERGAPG EKGEGGPPGA AGPPGGSGPA
860 870 880 890 900
GPPGPQGVKG ERGSPGGPGA AGFPGGRGLP GPPGNNGNPG PPGPSGAPGK
910 920 930 940 950
DGPPGPAGNS GSPGNPGVAG PKGDAGQPGE KGPPGAQGPP GSPGPLGIAG
960 970 980 990 1000
LTGARGLAGP PGMPGPRGSP GPQGIKGESG KPGASGHNGE RGPPGPQGLP
1010 1020 1030 1040 1050
GQPGTAGEPG RDGNPGSDGQ PGRDGSPGGK GDRGENGSPG APGAPGHPGP
1060 1070 1080 1090 1100
PGPVGPSGKN GDRGETGPAG PSGAPGPAGA RGAPGPQGPR GDKGETGERG
1110 1120 1130 1140 1150
SNGIKGHRGF PGNPGPPGSP GAAGHQGAVG SPGPAGPRGP VGPHGPPGKD
1160 1170 1180 1190 1200
GSSGHPGPIG PPGPRGNRGE RGSEGSPGHP GQPGPPGPPG APGPCCGGGA
1210 1220 1230 1240 1250
AIAGVGGEKS GGFSPYYGDD PMDFKINTEE IMSSLKSVNG QIESLISPDG
1260 1270 1280 1290 1300
SRKNPARNCR DLKFCHPELK SGEYWVDPNQ GCKMDAIKVF CNMETGETCI
1310 1320 1330 1340 1350
NASPMTVPRK HWWTDAGAEK KHVWFGESMN GGFQFSYGNP DLPEDVLDVQ
1360 1370 1380 1390 1400
LAFLRLLSSR ASQNITYHCK NSIAYMDQAN GNVKKSLKLM GSNEGEFKAE
1410 1420 1430 1440 1450
GNSKFTYTVL EDGCTKHTGE WSKTVFEYQT RKAMRLPIID IAPYDIGGPD
1460
QEFGVDIGPV CFL
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 1167 | N → D in CAA06510 (Ref. 3) Curated | 1 | |
Sequence conflicti | 1256 | A → G in CAA06510 (Ref. 3) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC087039 mRNA Translation: AAH87039.1 X70369 mRNA Translation: CAA49832.1 AJ005395 mRNA Translation: CAA06510.1 M21354 mRNA Translation: AAA40942.1 |
PIRi | S41067 |
RefSeqi | NP_114474.1, NM_032085.1 |
Genome annotation databases
Ensembli | ENSRNOT00000004956; ENSRNOP00000004956; ENSRNOG00000003357 |
GeneIDi | 84032 |
KEGGi | rno:84032 |
UCSCi | RGD:71029, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC087039 mRNA Translation: AAH87039.1 X70369 mRNA Translation: CAA49832.1 AJ005395 mRNA Translation: CAA06510.1 M21354 mRNA Translation: AAA40942.1 |
PIRi | S41067 |
RefSeqi | NP_114474.1, NM_032085.1 |
3D structure databases
SMRi | P13941 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 249898, 1 interactor |
IntActi | P13941, 2 interactors |
STRINGi | 10116.ENSRNOP00000004956 |
PTM databases
GlyGeni | P13941, 1 site |
iPTMneti | P13941 |
PhosphoSitePlusi | P13941 |
Proteomic databases
PaxDbi | P13941 |
PRIDEi | P13941 |
Genome annotation databases
Ensembli | ENSRNOT00000004956; ENSRNOP00000004956; ENSRNOG00000003357 |
GeneIDi | 84032 |
KEGGi | rno:84032 |
UCSCi | RGD:71029, rat |
Organism-specific databases
CTDi | 1281 |
RGDi | 71029, Col3a1 |
Phylogenomic databases
eggNOGi | KOG3544, Eukaryota |
GeneTreei | ENSGT00940000161229 |
HOGENOMi | CLU_001074_2_3_1 |
InParanoidi | P13941 |
OMAi | SPQFESY |
OrthoDBi | 1406711at2759 |
TreeFami | TF344135 |
Enzyme and pathway databases
Reactomei | R-RNO-1442490, Collagen degradation R-RNO-1474244, Extracellular matrix organization R-RNO-1650814, Collagen biosynthesis and modifying enzymes R-RNO-186797, Signaling by PDGF 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-216083, Integrin cell surface interactions R-RNO-3000171, Non-integrin membrane-ECM interactions R-RNO-3000178, ECM proteoglycans R-RNO-419037, NCAM1 interactions R-RNO-8874081, MET activates PTK2 signaling R-RNO-8948216, Collagen chain trimerization |
Miscellaneous databases
PROi | PR:P13941 |
Gene expression databases
Bgeei | ENSRNOG00000003357, Expressed in esophagus and 21 other tissues |
Genevisiblei | P13941, 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, 4 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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CO3A1_RAT | |
Accessioni | P13941Primary (citable) accession number: P13941 Secondary accession number(s): O70604, Q5PQT6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1990 |
Last sequence update: | December 6, 2005 | |
Last modified: | April 7, 2021 | |
This is version 166 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families