Tag | Content |
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CPLM ID | CPLM-002066 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Interstitial collagenase |
Protein Synonyms/Alias | Fibroblast collagenase; Matrix metalloproteinase-1; MMP-1; 22 kDa interstitial collagenase; 27 kDa interstitial collagenase |
Gene Name | MMP1 |
Gene Synonyms/Alias | CLG |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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450 | RQYKFDPKTKRILTL | ubiquitination | [1, 2] |
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Reference | [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C. Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [ PMID: 21890473] [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties. Chen Z, Zhou Y, Song J, Zhang Z. Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [ PMID: 23603789] |
Functional Description | Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity. |
Sequence Annotation | REPEAT 275 324 Hemopexin 1. REPEAT 325 371 Hemopexin 2. REPEAT 374 422 Hemopexin 3. REPEAT 423 466 Hemopexin 4. REGION 98 276 Metalloprotease. MOTIF 90 97 Cysteine switch (By similarity). ACT_SITE 219 219 METAL 92 92 Zinc 2; in inhibited form. METAL 124 124 Calcium 1. METAL 158 158 Calcium 2. METAL 168 168 Zinc 1. METAL 170 170 Zinc 1. METAL 175 175 Calcium 3. METAL 176 176 Calcium 3; via carbonyl oxygen. METAL 178 178 Calcium 3; via carbonyl oxygen. METAL 180 180 Calcium 3; via carbonyl oxygen. METAL 183 183 Zinc 1. METAL 190 190 Calcium 2; via carbonyl oxygen. METAL 192 192 Calcium 2; via carbonyl oxygen. METAL 194 194 Calcium 2. METAL 196 196 Zinc 1. METAL 198 198 Calcium 3. METAL 199 199 Calcium 1. METAL 201 201 Calcium 3. METAL 218 218 Zinc 2; catalytic. METAL 222 222 Zinc 2; catalytic. METAL 228 228 Zinc 2; catalytic. METAL 285 285 Calcium 4; via carbonyl oxygen (By METAL 329 329 Calcium 4; via carbonyl oxygen (By METAL 378 378 Calcium 4; via carbonyl oxygen (By METAL 427 427 Calcium 4; via carbonyl oxygen (By CARBOHYD 120 120 N-linked (GlcNAc...). DISULFID 278 466 By similarity. |
Keyword | 3D-structure; Autocatalytic cleavage; Calcium; Collagen degradation; Complete proteome; Direct protein sequencing; Disulfide bond; Extracellular matrix; Glycoprotein; Host-virus interaction; Hydrolase; Metal-binding; Metalloprotease; Polymorphism; Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 469 AA |
Protein Sequence | MHSFPPLLLL LFWGVVSHSF PATLETQEQD VDLVQKYLEK YYNLKNDGRQ VEKRRNSGPV 60 VEKLKQMQEF FGLKVTGKPD AETLKVMKQP RCGVPDVAQF VLTEGNPRWE QTHLTYRIEN 120 YTPDLPRADV DHAIEKAFQL WSNVTPLTFT KVSEGQADIM ISFVRGDHRD NSPFDGPGGN 180 LAHAFQPGPG IGGDAHFDED ERWTNNFREY NLHRVAAHEL GHSLGLSHST DIGALMYPSY 240 TFSGDVQLAQ DDIDGIQAIY GRSQNPVQPI GPQTPKACDS KLTFDAITTI RGEVMFFKDR 300 FYMRTNPFYP EVELNFISVF WPQLPNGLEA AYEFADRDEV RFFKGNKYWA VQGQNVLHGY 360 PKDIYSSFGF PRTVKHIDAA LSEENTGKTY FFVANKYWRY DEYKRSMDPG YPKMIAHDFP 420 GIGHKVDAVF MKDGFFYFFH GTRQYKFDPK TKRILTLQKA NSWFNCRKN 469 |
Gene Ontology | GO:0005576; C:extracellular region; TAS:Reactome. GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell. GO:0005509; F:calcium ion binding; IEA:InterPro. GO:0004222; F:metalloendopeptidase activity; IDA:BHF-UCL. GO:0008270; F:zinc ion binding; TAS:ProtInc. GO:0007596; P:blood coagulation; TAS:Reactome. GO:0044267; P:cellular protein metabolic process; TAS:Reactome. GO:0030574; P:collagen catabolic process; TAS:Reactome. GO:0022617; P:extracellular matrix disassembly; TAS:Reactome. GO:0050900; P:leukocyte migration; TAS:Reactome. GO:0006508; P:proteolysis; TAS:ProtInc. GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. |
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PRINTS | |