ID MMP3_HUMAN Reviewed; 477 AA. AC P08254; B2R8B8; Q3B7S0; Q6GRF8; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 2. DT 03-APR-2013, entry version 150. DE RecName: Full=Stromelysin-1; DE Short=SL-1; DE EC=3.4.24.17; DE AltName: Full=Matrix metalloproteinase-3; DE Short=MMP-3; DE AltName: Full=Transin-1; DE Flags: Precursor; GN Name=MMP3; Synonyms=STMY1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-24. RX PubMed=3360803; RA Saus J., Quinones S., Otani Y., Nagase H., Harris E.D. Jr., RA Kurkinen M.; RT "The complete primary structure of human matrix metalloproteinase-3. RT Identity with stromelysin."; RL J. Biol. Chem. 263:6742-6745(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fibroblast; RX PubMed=3030290; RA Whitham S.E., Murphy G., Angel P., Rahmsdorf H.J., Smith B., Lyons A., RA Harris T.J.R., Reynolds J.J., Herrlich P., Docherty A.J.P.; RT "Comparison of human stromelysin and collagenase by cloning and RT sequence analysis."; RL Biochem. J. 240:913-916(1986). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3477804; DOI=10.1073/pnas.84.19.6725; RA Wilhelm S.M., Collier I.E., Kronberger A., Eisen A.Z., Marmer B.L., RA Grant G.A., Bauer E.A., Goldberg G.I.; RT "Human skin fibroblast stromelysin: structure, glycosylation, RT substrate specificity, and differential expression in normal and RT tumorigenic cells."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6725-6729(1987). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Lin D., Duncan M., Allen E., Araujo R., Aparicio A., Chai A., RA Chung E., Davis K., Federspiel N., Hyman R., Kalman S., Komp C., RA Kurdi O., Lashkari D., Lew H., Namath A., Oefner P., Roberts D., RA Heller R., Davis R.W.; RT "Three matrix metalloproteinases on 81kb of P1 insert."; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Synovium; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-45. RC TISSUE=Synovium; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-45. RG SeattleSNPs variation discovery resource; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-45. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP ZYMOGEN ACTIVATION. RX PubMed=2383557; DOI=10.1021/bi00476a020; RA Nagase H., Enghild J.J., Suzuki K., Salvesen G.; RT "Stepwise activation mechanisms of the precursor of matrix RT metalloproteinase 3 (stromelysin) by proteinases and (4- RT aminophenyl)mercuric acetate."; RL Biochemistry 29:5783-5789(1990). RN [11] RP INVOLVEMENT IN CHDS6. RX PubMed=8662692; DOI=10.1074/jbc.271.22.13244; RA Ye S., Eriksson P., Hamsten A., Kurkinen M., Humphries S.E., RA Henney A.M.; RT "Progression of coronary atherosclerosis is associated with a common RT genetic variant of the human stromelysin-1 promoter which results in RT reduced gene expression."; RL J. Biol. Chem. 271:13055-13060(1996). RN [12] RP INVOLVEMENT IN CHDS6. RX PubMed=12477941; DOI=10.1056/NEJMoa021445; RA Yamada Y., Izawa H., Ichihara S., Takatsu F., Ishihara H., RA Hirayama H., Sone T., Tanaka M., Yokota M.; RT "Prediction of the risk of myocardial infarction from polymorphisms in RT candidate genes."; RL N. Engl. J. Med. 347:1916-1923(2002). RN [13] RP STRUCTURE BY NMR OF CATALYTIC DOMAIN. RX PubMed=7656014; DOI=10.1038/nsb0294-111; RA Gooley P.R., O'Connell J.F., Marcy A.I., Cuca G.C., Salowe S.P., RA Bush B.L., Hermes J.D., Esser C.K., Hagmann W.K., Springer J.P., RA Johnson B.A.; RT "The NMR structure of the inhibited catalytic domain of human RT stromelysin-1."; RL Nat. Struct. Biol. 1:111-118(1994). RN [14] RP STRUCTURE BY NMR OF 100-267. RX PubMed=9827994; RA Stockman B.J., Waldon D.J., Gates J.A., Scahill T.A., RA Kloosterman D.A., Mizsak S.A., Jacobsen E.J., Belonga K.L., RA Mitchell M.A., Mao B., Petke J.D., Goodman L., Powers E.A., RA Ledbetter S.R., Kaytes P.S., Vogeli G., Marshall V.P., Petzold G.L., RA Poorman R.A.; RT "Solution structures of stromelysin complexed to thiadiazole RT inhibitors."; RL Protein Sci. 7:2281-2286(1998). RN [15] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 18-272. RX PubMed=8535233; RA Becker J.W., Marcy A.I., Rokosz L.L., Axel M.G., Burbaum J.J., RA Fitzgerald P.M.D., Cameron P.M., Esser C.K., Hagmann W.K., RA Hermes J.D., Springer J.P.; RT "Stromelysin-1: three-dimensional structure of the inhibited catalytic RT domain and of the C-truncated proenzyme."; RL Protein Sci. 4:1966-1976(1995). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-266. RX PubMed=8740360; DOI=10.1016/S0969-2126(96)00043-3; RA Dhanaraj V., Ye Q.-Z., Johnson L.L., Hupe D.J., Otwine D.F., RA Dunbar J.B. Jr., Rubin J.R., Pavlovsky A., Humblet C., Blundell T.L.; RT "X-ray structure of a hydroxamate inhibitor complex of stromelysin RT catalytic domain and its comparison with members of the zinc RT metalloproteinase superfamily."; RL Structure 4:375-386(1996). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 105-264. RX PubMed=9083493; DOI=10.1021/jm960465t; RA Esser C.K., Bugianesi R.L., Caldwell C.G., Chapman K.T., Durette P.L., RA Girotra N.N., Kopka I.E., Lanza T.J., Levorse D.A., Maccoss M., RA Owens K.A., Ponpipom M.M., Simeone J.P., Harrison R.K., RA Niedzwiecki L., Becker J.W., Marcy A.I., Axel M.G., Christen A.J., RA McDonnell J., Moore V.L., Olszewski J.M., Saphos C., Visco D.M., RA Shen F., Colletti A., Kriter P.A., Hagmann W.K.; RT "Inhibition of stromelysin-1 (MMP-3) by P1'-biphenylylethyl RT carboxyalkyl dipeptides."; RL J. Med. Chem. 40:1026-1040(1997). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 100-267 IN COMPLEX WITH RP TIMP1. RX PubMed=9288970; DOI=10.1038/37995; RA Gomis-Rueth F.-X., Maskos K., Betz M., Bergner A., Huber R., RA Suzuki K., Yoshida N., Nagase H., Brew K., Bourenkov G.P., RA Bartunik H., Bode W.; RT "Mechanism of inhibition of the human matrix metalloproteinase RT stromelysin-1 by TIMP-1."; RL Nature 389:77-81(1997). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 100-264. RX PubMed=9792098; RA Finzel B.C., Baldwin E.T., Bryant G.L. Jr., Hess G.F., Wilks J.W., RA Trepod C.M., Mott J.E., Marshall V.P., Petzold G.L., Poorman R.A., RA O'Sullivan T.J., Schostarez H.J., Mitchell M.A.; RT "Structural characterizations of nonpeptidic thiadiazole inhibitors of RT matrix metalloproteinases reveal the basis for stromelysin RT selectivity."; RL Protein Sci. 7:2118-2126(1998). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-272. RX PubMed=10543949; DOI=10.1006/jmbi.1999.3147; RA Chen L., Rydel T.J., Gu F., Dunaway C.M., Pikul S., Dunham K.M., RA Barnett B.L.; RT "Crystal structure of the stromelysin catalytic domain at 2.0-A RT resolution: inhibitor-induced conformational changes."; RL J. Mol. Biol. 293:545-557(1999). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 100-267. RX PubMed=10422833; RA Pavlovsky A.G., Williams M.G., Ye Q.-Z., Ortwine D.F., RA Purchase C.F. II, White A.D., Dhanaraj V., Roth B.D., Johnson L.L., RA Hupe D., Humblet C., Blundell T.L.; RT "X-ray structure of human stromelysin catalytic domain complexed with RT nonpeptide inhibitors: implications for inhibitor selectivity."; RL Protein Sci. 8:1455-1462(1999). RN [22] RP STRUCTURE BY NMR OF 100-272. RX PubMed=9760240; DOI=10.1021/bi981328w; RA Li Y.C., Zhang X., Melton R., Ganu V., Gonnella N.C.; RT "Solution structure of the catalytic domain of human stromelysin-1 RT complexed to a potent, nonpeptidic inhibitor."; RL Biochemistry 37:14048-14056(1998). CC -!- FUNCTION: Can degrade fibronectin, laminin, gelatins of type I, CC III, IV, and V; collagens III, IV, X, and IX, and cartilage CC proteoglycans. Activates procollagenase. CC -!- CATALYTIC ACTIVITY: Preferential cleavage where P1', P2' and P3' CC are hydrophobic residues. CC -!- COFACTOR: Binds 4 calcium ions per subunit. CC -!- COFACTOR: Binds 2 zinc ions per subunit. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix (Probable). CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch CC motif binds the catalytic zinc ion, thus inhibiting the enzyme. CC The dissociation of the cysteine from the zinc ion upon the CC activation-peptide release activates the enzyme. CC -!- DISEASE: Defects in MMP3 are the cause of susceptibility to CC coronary heart disease type 6 (CHDS6) [MIM:614466]. A CC multifactorial disease characterized by an imbalance between CC myocardial functional requirements and the capacity of the CC coronary vessels to supply sufficient blood flow. Decreased CC capacity of the coronary vessels is often associated with CC thickening and loss of elasticity of the coronary arteries. Note=A CC polymorphism in the MMP3 promoter region is associated with the CC risk of coronary heart disease and myocardial infarction, due to CC lower MMP3 proteolytic activity and higher extracellular matrix CC deposition in atherosclerotic lesions. CC -!- SIMILARITY: Belongs to the peptidase M10A family. CC -!- SIMILARITY: Contains 4 hemopexin-like domains. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/mmp3/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X05232; CAA28859.1; -; mRNA. DR EMBL; J03209; AAA36321.1; -; mRNA. DR EMBL; U78045; AAB36942.1; -; Genomic_DNA. DR EMBL; AK223283; BAD97003.1; -; mRNA. DR EMBL; AK223291; BAD97011.1; -; mRNA. DR EMBL; AK313310; BAG36115.1; -; mRNA. DR EMBL; AF405705; AAK95247.1; -; Genomic_DNA. DR EMBL; CH471065; EAW67032.1; -; Genomic_DNA. DR EMBL; BC069676; AAH69676.1; -; mRNA. DR EMBL; BC069716; AAH69716.1; -; mRNA. DR EMBL; BC074815; AAH74815.1; -; mRNA. DR EMBL; BC074869; AAH74869.1; -; mRNA. DR EMBL; BC105954; AAI05955.1; -; mRNA. DR EMBL; BC107490; AAI07491.1; -; mRNA. DR EMBL; BC107491; AAI07492.1; -; mRNA. DR IPI; IPI00027782; -. DR PIR; A28156; KCHUS1. DR RefSeq; NP_002413.1; NM_002422.3. DR UniGene; Hs.375129; -. DR PDB; 1B3D; X-ray; 2.30 A; A/B=100-272. DR PDB; 1B8Y; X-ray; 2.00 A; A=100-266. DR PDB; 1BIW; X-ray; 2.50 A; A/B=100-272. DR PDB; 1BM6; NMR; -; A=100-272. DR PDB; 1BQO; X-ray; 2.30 A; A/B=100-272. DR PDB; 1C3I; X-ray; 1.83 A; A/B=100-272. DR PDB; 1C8T; X-ray; 2.60 A; A/B=103-268. DR PDB; 1CAQ; X-ray; 1.80 A; A=100-267. DR PDB; 1CIZ; X-ray; 1.64 A; A=100-267. DR PDB; 1CQR; X-ray; 2.00 A; A/B=100-272. DR PDB; 1D5J; X-ray; 2.60 A; A/B=100-272. DR PDB; 1D7X; X-ray; 2.00 A; A/B=100-272. DR PDB; 1D8F; X-ray; 2.40 A; A/B=100-272. DR PDB; 1D8M; X-ray; 2.44 A; A/B=100-272. DR PDB; 1G05; X-ray; 2.45 A; A/B=100-272. DR PDB; 1G49; X-ray; 1.90 A; A/B=100-272. DR PDB; 1G4K; X-ray; 2.00 A; A/B/C=100-267. DR PDB; 1HFS; X-ray; 1.70 A; A=105-264. DR PDB; 1HY7; X-ray; 1.50 A; A/B=100-272. DR PDB; 1M1W; Model; -; A=100-268. DR PDB; 1OO9; NMR; -; A=100-267. DR PDB; 1QIA; X-ray; 2.00 A; A/B/C/D=106-267. DR PDB; 1QIC; X-ray; 2.00 A; A/B/C/D=106-266. DR PDB; 1SLM; X-ray; 1.90 A; A=18-272. DR PDB; 1SLN; X-ray; 2.27 A; A=100-272. DR PDB; 1UEA; X-ray; 2.80 A; A/C=100-272. DR PDB; 1UMS; NMR; -; A=100-273. DR PDB; 1UMT; NMR; -; A=100-273. DR PDB; 1USN; X-ray; 1.80 A; A=100-264. DR PDB; 2D1O; X-ray; 2.02 A; A/B=100-270. DR PDB; 2JNP; NMR; -; A=105-265. DR PDB; 2JT5; NMR; -; A=105-265. DR PDB; 2JT6; NMR; -; A=105-265. DR PDB; 2SRT; NMR; -; A=100-272. DR PDB; 2USN; X-ray; 2.20 A; A=100-264. DR PDB; 3OHL; X-ray; 2.36 A; A=100-266. DR PDB; 3OHO; X-ray; 2.50 A; A=100-268. DR PDB; 3USN; NMR; -; A=100-267. DR PDBsum; 1B3D; -. DR PDBsum; 1B8Y; -. DR PDBsum; 1BIW; -. DR PDBsum; 1BM6; -. DR PDBsum; 1BQO; -. DR PDBsum; 1C3I; -. DR PDBsum; 1C8T; -. DR PDBsum; 1CAQ; -. DR PDBsum; 1CIZ; -. DR PDBsum; 1CQR; -. DR PDBsum; 1D5J; -. DR PDBsum; 1D7X; -. DR PDBsum; 1D8F; -. DR PDBsum; 1D8M; -. DR PDBsum; 1G05; -. DR PDBsum; 1G49; -. DR PDBsum; 1G4K; -. DR PDBsum; 1HFS; -. DR PDBsum; 1HY7; -. DR PDBsum; 1M1W; -. DR PDBsum; 1OO9; -. DR PDBsum; 1QIA; -. DR PDBsum; 1QIC; -. DR PDBsum; 1SLM; -. DR PDBsum; 1SLN; -. DR PDBsum; 1UEA; -. DR PDBsum; 1UMS; -. DR PDBsum; 1UMT; -. DR PDBsum; 1USN; -. DR PDBsum; 2D1O; -. DR PDBsum; 2JNP; -. DR PDBsum; 2JT5; -. DR PDBsum; 2JT6; -. DR PDBsum; 2SRT; -. DR PDBsum; 2USN; -. DR PDBsum; 3OHL; -. DR PDBsum; 3OHO; -. DR PDBsum; 3USN; -. DR ProteinModelPortal; P08254; -. DR SMR; P08254; 31-476. DR MINT; MINT-269333; -. DR STRING; 9606.ENSP00000299855; -. DR MEROPS; M10.005; -. DR PhosphoSite; P08254; -. DR DMDM; 116857; -. DR PaxDb; P08254; -. DR PRIDE; P08254; -. DR DNASU; 4314; -. DR Ensembl; ENST00000299855; ENSP00000299855; ENSG00000149968. DR Ensembl; ENST00000572537; ENSP00000458496; ENSG00000263313. DR GeneID; 4314; -. DR KEGG; hsa:4314; -. DR UCSC; uc001phj.1; human. DR CTD; 4314; -. DR GeneCards; GC11M102706; -. DR HGNC; HGNC:7173; MMP3. DR HPA; CAB016139; -. DR HPA; HPA007875; -. DR MIM; 185250; gene. DR MIM; 614466; phenotype. DR neXtProt; NX_P08254; -. DR PharmGKB; PA30886; -. DR eggNOG; NOG258253; -. DR HOGENOM; HOG000217927; -. DR HOVERGEN; HBG052484; -. DR InParanoid; P08254; -. DR KO; K01394; -. DR OMA; AVCSAYP; -. DR OrthoDB; EOG4KKZ2X; -. DR PhylomeDB; P08254; -. DR Pathway_Interaction_DB; p75ntrpathway; p75(NTR)-mediated signaling. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_118779; Extracellular matrix organization. DR Reactome; REACT_133391; Extracellular matrix organization. DR BindingDB; P08254; -. DR ChEMBL; CHEMBL283; -. DR ChiTaRS; MMP3; human. DR DrugBank; DB00786; Marimastat. DR DrugBank; DB00641; Simvastatin. DR EvolutionaryTrace; P08254; -. DR GenomeRNAi; 4314; -. DR NextBio; 16977; -. DR PMAP-CutDB; P08254; -. DR ArrayExpress; P08254; -. DR Bgee; P08254; -. DR CleanEx; HS_MMP3; -. DR Genevestigator; P08254; -. DR GermOnline; ENSG00000149968; Homo sapiens. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004222; F:metalloendopeptidase activity; TAS:ProtInc. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Compara. DR GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW. DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome. DR GO; GO:0006508; P:proteolysis; TAS:ProtInc. DR GO; GO:0030334; P:regulation of cell migration; IEA:Compara. DR Gene3D; 2.110.10.10; -; 1. DR Gene3D; 3.40.390.10; -; 1. DR InterPro; IPR000585; Hemopexin/matrixin. DR InterPro; IPR018486; Hemopexin/matrixin_CS. DR InterPro; IPR018487; Hemopexin/matrixin_repeat. DR InterPro; IPR024079; MetalloPept_cat_dom. DR InterPro; IPR001818; Pept_M10_metallopeptidase. DR InterPro; IPR016293; Pept_M10A_matrix_strom. DR InterPro; IPR021190; Pept_M10A_matrixin. DR InterPro; IPR021158; Pept_M10A_Zn_BS. DR InterPro; IPR006026; Peptidase_Metallo. DR InterPro; IPR002477; Peptidoglycan-bd-like. DR Pfam; PF00045; Hemopexin; 4. DR Pfam; PF00413; Peptidase_M10; 1. DR Pfam; PF01471; PG_binding_1; 1. DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1. DR PRINTS; PR00138; MATRIXIN. DR SMART; SM00120; HX; 4. DR SMART; SM00235; ZnMc; 1. DR SUPFAM; SSF50923; Hemopexin; 1. DR SUPFAM; SSF47090; PGBD_like; 1. DR PROSITE; PS00546; CYSTEINE_SWITCH; 1. DR PROSITE; PS00024; HEMOPEXIN; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Collagen degradation; Complete proteome; KW Direct protein sequencing; Disulfide bond; Extracellular matrix; KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Polymorphism; KW Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen. FT SIGNAL 1 17 Probable. FT PROPEP 18 99 Activation peptide. FT /FTId=PRO_0000028728. FT CHAIN 100 477 Stromelysin-1. FT /FTId=PRO_0000028729. FT DOMAIN 296 338 Hemopexin-like 1. FT DOMAIN 340 383 Hemopexin-like 2. FT DOMAIN 388 435 Hemopexin-like 3. FT DOMAIN 437 477 Hemopexin-like 4. FT MOTIF 90 97 Cysteine switch (By similarity). FT ACT_SITE 219 219 FT METAL 92 92 Zinc 2; in inhibited form. FT METAL 124 124 Calcium 1. FT METAL 158 158 Calcium 2. FT METAL 168 168 Zinc 1. FT METAL 170 170 Zinc 1. FT METAL 175 175 Calcium 3. FT METAL 176 176 Calcium 3; via carbonyl oxygen. FT METAL 178 178 Calcium 3; via carbonyl oxygen. FT METAL 180 180 Calcium 3; via carbonyl oxygen. FT METAL 183 183 Zinc 1. FT METAL 190 190 Calcium 2; via carbonyl oxygen. FT METAL 192 192 Calcium 2; via carbonyl oxygen. FT METAL 194 194 Calcium 2. FT METAL 196 196 Zinc 1. FT METAL 198 198 Calcium 3. FT METAL 199 199 Calcium 1. FT METAL 201 201 Calcium 1. FT METAL 201 201 Calcium 3. FT METAL 218 218 Zinc 2; catalytic. FT METAL 222 222 Zinc 2; catalytic. FT METAL 228 228 Zinc 2; catalytic. FT METAL 297 297 Calcium 4; via carbonyl oxygen (By FT similarity). FT METAL 389 389 Calcium 4; via carbonyl oxygen (By FT similarity). FT METAL 438 438 Calcium 4; via carbonyl oxygen (By FT similarity). FT CARBOHYD 120 120 N-linked (GlcNAc...) (Potential). FT DISULFID 290 477 By similarity. FT VARIANT 45 45 K -> E (in dbSNP:rs679620). FT /FTId=VAR_013090. FT CONFLICT 420 420 P -> L (in Ref. 3). FT HELIX 34 41 FT HELIX 58 70 FT HELIX 81 86 FT STRAND 96 98 FT STRAND 102 104 FT STRAND 110 118 FT STRAND 123 125 FT HELIX 127 142 FT STRAND 144 146 FT STRAND 148 151 FT STRAND 153 155 FT STRAND 158 164 FT STRAND 169 171 FT STRAND 176 179 FT STRAND 182 184 FT STRAND 187 189 FT TURN 190 193 FT STRAND 195 198 FT STRAND 199 201 FT STRAND 203 211 FT HELIX 212 223 FT TURN 231 233 FT STRAND 237 239 FT HELIX 240 243 FT HELIX 246 248 FT HELIX 253 263 SQ SEQUENCE 477 AA; 53977 MW; 96194833B907668D CRC64; MKSLPILLLL CVAVCSAYPL DGAARGEDTS MNLVQKYLEN YYDLKKDVKQ FVRRKDSGPV VKKIREMQKF LGLEVTGKLD SDTLEVMRKP RCGVPDVGHF RTFPGIPKWR KTHLTYRIVN YTPDLPKDAV DSAVEKALKV WEEVTPLTFS RLYEGEADIM ISFAVREHGD FYPFDGPGNV LAHAYAPGPG INGDAHFDDD EQWTKDTTGT NLFLVAAHEI GHSLGLFHSA NTEALMYPLY HSLTDLTRFR LSQDDINGIQ SLYGPPPDSP ETPLVPTEPV PPEPGTPANC DPALSFDAVS TLRGEILIFK DRHFWRKSLR KLEPELHLIS SFWPSLPSGV DAAYEVTSKD LVFIFKGNQF WAIRGNEVRA GYPRGIHTLG FPPTVRKIDA AISDKEKNKT YFFVEDKYWR FDEKRNSMEP GFPKQIAEDF PGIDSKIDAV FEEFGFFYFF TGSSQLEFDP NAKKVTHTLK SNSWLNC //