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Protein

Collagen alpha-1(III) chain

Gene

Col3a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

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 keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1277CalciumBy similarity1
Metal bindingi1279CalciumBy similarity1
Metal bindingi1280Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1282Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1285CalciumBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-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.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(III) chain
Gene namesi
Name:Col3a1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi71029. Col3a1.

Subcellular locationi

GO - Cellular componenti

  • collagen type III trimer Source: Ensembl
  • extracellular matrix Source: RGD
  • extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23By similarityAdd BLAST23
PropeptideiPRO_000000574624 – 154N-terminal propeptideBy similarityAdd BLAST131
ChainiPRO_0000005747155 – 1218Collagen alpha-1(III) chainAdd BLAST1064
PropeptideiPRO_00000434081219 – 1463C-terminal propeptideBy similarityAdd BLAST245

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2625-hydroxylysine; alternateBy similarity1
Glycosylationi262O-linked (Gal...); alternateBy similarity1
Modified residuei2835-hydroxylysineBy similarity1
Modified residuei8595-hydroxylysineBy similarity1
Modified residuei9765-hydroxylysineBy similarity1
Modified residuei10935-hydroxylysineBy similarity1
Modified residuei11055-hydroxylysineBy similarity1
Disulfide bondi1195InterchainPROSITE-ProRule annotation
Disulfide bondi1196InterchainPROSITE-ProRule annotation
Disulfide bondi1259 ↔ 1291PROSITE-ProRule annotation
Disulfide bondi1265Interchain (with C-1282)PROSITE-ProRule annotation
Disulfide bondi1282Interchain (with C-1265)PROSITE-ProRule annotation
Disulfide bondi1299 ↔ 1461PROSITE-ProRule annotation
Disulfide bondi1369 ↔ 1414PROSITE-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, Hydroxylation

Proteomic databases

PaxDbiP13941.
PRIDEiP13941.

PTM databases

iPTMnetiP13941.
PhosphoSitePlusiP13941.

Expressioni

Gene expression databases

BgeeiENSRNOG00000003357.
GenevisibleiP13941. 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.

Protein-protein interaction databases

IntActiP13941. 1 interactor.
STRINGi10116.ENSRNOP00000004956.

Structurei

3D structure databases

ProteinModelPortaliP13941.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 90VWFCPROSITE-ProRule annotationAdd BLAST60
Domaini1229 – 1463Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST235

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni155 – 169Nonhelical region (N-terminal)Add BLAST15
Regioni170 – 1195Triple-helical regionAdd BLAST1026

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
Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP13941.
KOiK19720.
OMAiAEKKHVW.
OrthoDBiEOG091G03LV.
TreeFamiTF344135.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 4 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13941-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:1,463
Mass (Da):138,936
Last modified:December 6, 2005 - v3
Checksum:i63C218CD2BCA47B6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1167N → D in CAA06510 (Ref. 3) Curated1
Sequence conflicti1256A → G in CAA06510 (Ref. 3) Curated1

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.
PIRiS41067.
RefSeqiNP_114474.1. NM_032085.1.
UniGeneiRn.3247.

Genome annotation databases

EnsembliENSRNOT00000004956; ENSRNOP00000004956; ENSRNOG00000003357.
GeneIDi84032.
KEGGirno:84032.
UCSCiRGD:71029. rat.

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.
PIRiS41067.
RefSeqiNP_114474.1. NM_032085.1.
UniGeneiRn.3247.

3D structure databases

ProteinModelPortaliP13941.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP13941. 1 interactor.
STRINGi10116.ENSRNOP00000004956.

PTM databases

iPTMnetiP13941.
PhosphoSitePlusiP13941.

Proteomic databases

PaxDbiP13941.
PRIDEiP13941.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004956; ENSRNOP00000004956; ENSRNOG00000003357.
GeneIDi84032.
KEGGirno:84032.
UCSCiRGD:71029. rat.

Organism-specific databases

CTDi1281.
RGDi71029. Col3a1.

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP13941.
KOiK19720.
OMAiAEKKHVW.
OrthoDBiEOG091G03LV.
TreeFamiTF344135.

Enzyme and pathway databases

ReactomeiR-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.

Miscellaneous databases

PROiP13941.

Gene expression databases

BgeeiENSRNOG00000003357.
GenevisibleiP13941. RN.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 4 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO3A1_RAT
AccessioniPrimary (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: November 30, 2016
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.