CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001963
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Collagen alpha-1(III) chain 
Protein Synonyms/Alias
  
Gene Name
 COL3A1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1387DQASGNVKKALKLMGacetylation[1]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 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 GPR56 in the developing brain and binding to GPR56 inhibits neuronal migration and activates the RhoA pathway by coupling GPR56 to GNA13 and possibly GNA12. 
Sequence Annotation
 DOMAIN 30 89 VWFC.
 DOMAIN 1232 1466 Fibrillar collagen NC1.
 REGION 149 167 Nonhelical region (N-terminal).
 REGION 168 1196 Triple-helical region.
 REGION 1197 1205 Nonhelical region (C-terminal).
 METAL 1280 1280 Calcium.
 METAL 1282 1282 Calcium.
 METAL 1283 1283 Calcium; via carbonyl oxygen.
 METAL 1285 1285 Calcium; via carbonyl oxygen.
 METAL 1288 1288 Calcium.
 MOD_RES 263 263 5-hydroxylysine; alternate.
 MOD_RES 284 284 5-hydroxylysine.
 MOD_RES 860 860 5-hydroxylysine.
 MOD_RES 977 977 5-hydroxylysine.
 MOD_RES 1094 1094 5-hydroxylysine; partial.
 MOD_RES 1106 1106 5-hydroxylysine.
 CARBOHYD 263 263 O-linked (Gal...); alternate.
 DISULFID 1196 1196 Interchain.
 DISULFID 1197 1197 Interchain.
 DISULFID 1262 1294
 DISULFID 1268 1268 Interchain (with C-1285).
 DISULFID 1285 1285 Interchain (with C-1268).
 DISULFID 1302 1464
 DISULFID 1372 1417  
Keyword
 3D-structure; Alternative splicing; Aortic aneurysm; Calcium; Collagen; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Ehlers-Danlos syndrome; Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding; Polymorphism; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1466 AA 
Protein Sequence
MMSFVQKGSW LLLALLHPTI ILAQQEAVEG GCSHLGQSYA DRDVWKPEPC QICVCDSGSV 60
LCDDIICDDQ ELDCPNPEIP FGECCAVCPQ PPTAPTRPPN GQGPQGPKGD PGPPGIPGRN 120
GDPGIPGQPG SPGSPGPPGI CESCPTGPQN YSPQYDSYDV KSGVAVGGLA GYPGPAGPPG 180
PPGPPGTSGH PGSPGSPGYQ GPPGEPGQAG PSGPPGPPGA IGPSGPAGKD GESGRPGRPG 240
ERGLPGPPGI KGPAGIPGFP GMKGHRGFDG RNGEKGETGA PGLKGENGLP GENGAPGPMG 300
PRGAPGERGR PGLPGAAGAR GNDGARGSDG QPGPPGPPGT AGFPGSPGAK GEVGPAGSPG 360
SNGAPGQRGE PGPQGHAGAQ GPPGPPGING SPGGKGEMGP AGIPGAPGLM GARGPPGPAG 420
ANGAPGLRGG AGEPGKNGAK GEPGPRGERG EAGIPGVPGA KGEDGKDGSP GEPGANGLPG 480
AAGERGAPGF RGPAGPNGIP GEKGPAGERG APGPAGPRGA AGEPGRDGVP GGPGMRGMPG 540
SPGGPGSDGK PGPPGSQGES GRPGPPGPSG PRGQPGVMGF PGPKGNDGAP GKNGERGGPG 600
GPGPQGPPGK NGETGPQGPP GPTGPGGDKG DTGPPGPQGL QGLPGTGGPP GENGKPGEPG 660
PKGDAGAPGA PGGKGDAGAP GERGPPGLAG APGLRGGAGP PGPEGGKGAA GPPGPPGAAG 720
TPGLQGMPGE RGGLGSPGPK GDKGEPGGPG ADGVPGKDGP RGPTGPIGPP GPAGQPGDKG 780
EGGAPGLPGI AGPRGSPGER GETGPPGPAG FPGAPGQNGE PGGKGERGAP GEKGEGGPPG 840
VAGPPGGSGP AGPPGPQGVK GERGSPGGPG AAGFPGARGL PGPPGSNGNP GPPGPSGSPG 900
KDGPPGPAGN TGAPGSPGVS GPKGDAGQPG EKGSPGAQGP PGAPGPLGIA GITGARGLAG 960
PPGMPGPRGS PGPQGVKGES GKPGANGLSG ERGPPGPQGL PGLAGTAGEP GRDGNPGSDG 1020
LPGRDGSPGG KGDRGENGSP GAPGAPGHPG PPGPVGPAGK SGDRGESGPA GPAGAPGPAG 1080
SRGAPGPQGP RGDKGETGER GAAGIKGHRG FPGNPGAPGS PGPAGQQGAI GSPGPAGPRG 1140
PVGPSGPPGK DGTSGHPGPI GPPGPRGNRG ERGSEGSPGH PGQPGPPGPP GAPGPCCGGV 1200
GAAAIAGIGG EKAGGFAPYY GDEPMDFKIN TDEIMTSLKS VNGQIESLIS PDGSRKNPAR 1260
NCRDLKFCHP ELKSGEYWVD PNQGCKLDAI KVFCNMETGE TCISANPLNV PRKHWWTDSS 1320
AEKKHVWFGE SMDGGFQFSY GNPELPEDVL DVHLAFLRLL SSRASQNITY HCKNSIAYMD 1380
QASGNVKKAL KLMGSNEGEF KAEGNSKFTY TVLEDGCTKH TGEWSKTVFE YRTRKAVRLP 1440
IVDIAPYDIG GPDQEFGVDV GPVCFL 1466 
Gene Ontology
 GO:0005586; C:collagen type III; IMP:UniProtKB.
 GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
 GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO:0005201; F:extracellular matrix structural constituent; IMP:UniProtKB.
 GO:0005178; F:integrin binding; IMP:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0048407; F:platelet-derived growth factor binding; IDA:MGI.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0001568; P:blood vessel development; IEA:Compara.
 GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
 GO:0071230; P:cellular response to amino acid stimulus; IEA:Compara.
 GO:0032964; P:collagen biosynthetic process; IMP:UniProtKB.
 GO:0030574; P:collagen catabolic process; TAS:Reactome.
 GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
 GO:0048565; P:digestive tract development; IEA:Compara.
 GO:0043206; P:extracellular fibril organization; IMP:UniProtKB.
 GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
 GO:0007507; P:heart development; IMP:UniProtKB.
 GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
 GO:0050777; P:negative regulation of immune response; IMP:UniProtKB.
 GO:0018149; P:peptide cross-linking; IDA:UniProtKB.
 GO:0030168; P:platelet activation; NAS:UniProtKB.
 GO:0034097; P:response to cytokine stimulus; IDA:UniProtKB.
 GO:0009314; P:response to radiation; IDA:UniProtKB.
 GO:0001501; P:skeletal system development; IEA:Compara.
 GO:0043588; P:skin development; IMP:UniProtKB.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB. 
Interpro
 IPR008160; Collagen.
 IPR000885; Fib_collagen_C.
 IPR001007; VWF_C. 
Pfam
 PF01410; COLFI
 PF01391; Collagen
 PF00093; VWC 
SMART
 SM00038; COLFI
 SM00214; VWC 
PROSITE
 PS51461; NC1_FIB
 PS01208; VWFC_1
 PS50184; VWFC_2 
PRINTS