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Macrophage metalloelastase (MME) (EC 3.4.24.65) (Macrophage elastase) (ME) (hME) (Matrix metalloproteinase-12) (MMP-12)

 MMP12_HUMAN             Reviewed;         470 AA.
P39900; B2R9X8; B7ZLF6; Q2M1L9;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
20-JUN-2018, entry version 189.
RecName: Full=Macrophage metalloelastase;
Short=MME;
EC=3.4.24.65;
AltName: Full=Macrophage elastase;
Short=ME;
Short=hME;
AltName: Full=Matrix metalloproteinase-12;
Short=MMP-12;
Flags: Precursor;
Name=MMP12; Synonyms=HME;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Alveolar macrophage;
PubMed=8226919;
Shapiro S.D., Kobayashi D.K., Ley T.J.;
"Cloning and characterization of a unique elastolytic
metalloproteinase produced by human alveolar macrophages.";
J. Biol. Chem. 268:23824-23829(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-357 AND ARG-469.
NIEHS SNPs program;
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Esophagus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-357.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
CHARACTERIZATION.
PubMed=9115292; DOI=10.1074/jbc.272.18.12189;
Gronski T.J. Jr., Martin R.L., Kobayashi D.K., Walsh B.C.,
Holman M.C., Huber M., Van Wart H.E., Shapiro S.D.;
"Hydrolysis of a broad spectrum of extracellular matrix proteins by
human macrophage elastase.";
J. Biol. Chem. 272:12189-12194(1997).
[7]
X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS) OF 106-263.
PubMed=11575928; DOI=10.1006/jmbi.2001.4954;
Lang R., Kocourek A., Braun M., Tschesche H., Huber R., Bode W.,
Maskos K.;
"Substrate specificity determinants of human macrophage elastase (MMP-
12) based on the 1.1 A crystal structure.";
J. Mol. Biol. 312:731-742(2001).
[8]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 100-280.
PubMed=11575929; DOI=10.1006/jmbi.2001.4953;
Nar H., Werle K., Bauer M.M.T., Dollinger H., Jung B.;
"Crystal structure of human macrophage elastase (MMP-12) in complex
with a hydroxamic acid inhibitor.";
J. Mol. Biol. 312:743-751(2001).
-!- FUNCTION: May be involved in tissue injury and remodeling. Has
significant elastolytic activity. Can accept large and small amino
acids at the P1' site, but has a preference for leucine. Aromatic
or hydrophobic residues are preferred at the P1 site, with small
hydrophobic residues (preferably alanine) occupying P3.
-!- CATALYTIC ACTIVITY: Hydrolysis of soluble and insoluble elastin.
Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-
Tyr-|-Leu-17 in the B chain of insulin.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 4 Ca(2+) ions per subunit.;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 2 Zn(2+) ions per subunit.;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000305}.
-!- TISSUE SPECIFICITY: Found in alveolar macrophages but not in
peripheral blood monocytes.
-!- INDUCTION: By exposure to bacterial lipopolysaccharides (LPS).
Inhibited by dexamethasone.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mmp12/";
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EMBL; L23808; AAA58658.1; ALT_SEQ; mRNA.
EMBL; AY856072; AAW29944.1; -; Genomic_DNA.
EMBL; AK313959; BAG36675.1; -; mRNA.
EMBL; CH471065; EAW67033.1; -; Genomic_DNA.
EMBL; BC112301; AAI12302.1; -; mRNA.
EMBL; BC143773; AAI43774.1; -; mRNA.
CCDS; CCDS73375.1; -.
PIR; A49499; A49499.
RefSeq; NP_002417.2; NM_002426.5.
UniGene; Hs.1695; -.
UniGene; Hs.709832; -.
PDB; 1JIZ; X-ray; 2.60 A; A/B=100-264.
PDB; 1JK3; X-ray; 1.09 A; A=106-263.
PDB; 1OS2; X-ray; 2.15 A; A/B/C/D/E/F=106-268.
PDB; 1OS9; X-ray; 1.85 A; A/B/C/D/E/F=106-268.
PDB; 1RMZ; X-ray; 1.34 A; A=106-263.
PDB; 1ROS; X-ray; 2.00 A; A/B=106-268.
PDB; 1UTT; X-ray; 2.20 A; A=106-264.
PDB; 1UTZ; X-ray; 2.50 A; A/B=106-264.
PDB; 1Y93; X-ray; 1.03 A; A=106-263.
PDB; 1YCM; NMR; -; A=106-263.
PDB; 1Z3J; NMR; -; A=106-263.
PDB; 2HU6; X-ray; 1.32 A; A=106-263.
PDB; 2JXY; NMR; -; A=278-470.
PDB; 2K2G; NMR; -; A=100-263.
PDB; 2K9C; NMR; -; A=112-263.
PDB; 2KRJ; NMR; -; A=112-263.
PDB; 2MLR; NMR; -; A=100-263.
PDB; 2MLS; NMR; -; A=100-263.
PDB; 2N8R; NMR; -; A=100-263.
PDB; 2OXU; X-ray; 1.24 A; A=106-263.
PDB; 2OXW; X-ray; 1.15 A; A=106-263.
PDB; 2OXZ; X-ray; 1.90 A; A=106-263.
PDB; 2POJ; NMR; -; A=100-263.
PDB; 2W0D; X-ray; 2.00 A; A/B/C/D=106-263.
PDB; 2WO8; X-ray; 2.00 A; A/B/C/D=106-268.
PDB; 2WO9; X-ray; 1.70 A; A/B/C/D=106-268.
PDB; 2WOA; X-ray; 2.30 A; A/B/C/D=106-268.
PDB; 2Z2D; NMR; -; A=100-263.
PDB; 3BA0; X-ray; 3.00 A; A=106-470.
PDB; 3EHX; X-ray; 1.90 A; A=106-263.
PDB; 3EHY; X-ray; 1.90 A; A=106-263.
PDB; 3F15; X-ray; 1.70 A; A=106-263.
PDB; 3F16; X-ray; 1.16 A; A=106-263.
PDB; 3F17; X-ray; 1.10 A; A=106-263.
PDB; 3F18; X-ray; 1.13 A; A=106-263.
PDB; 3F19; X-ray; 1.13 A; A=106-263.
PDB; 3F1A; X-ray; 1.25 A; A=106-263.
PDB; 3LIK; X-ray; 1.80 A; A=106-263.
PDB; 3LIL; X-ray; 1.80 A; A=106-263.
PDB; 3LIR; X-ray; 1.90 A; A=106-263.
PDB; 3LJG; X-ray; 1.31 A; A=106-263.
PDB; 3LK8; X-ray; 1.80 A; A=106-263.
PDB; 3LKA; X-ray; 1.80 A; A=106-263.
PDB; 3N2U; X-ray; 1.81 A; A=106-263.
PDB; 3N2V; X-ray; 1.55 A; A=106-263.
PDB; 3NX7; X-ray; 1.80 A; A=106-263.
PDB; 3RTS; X-ray; 1.81 A; A=106-263.
PDB; 3RTT; X-ray; 1.82 A; A=106-263.
PDB; 3TS4; X-ray; 1.59 A; A=106-263.
PDB; 3TSK; X-ray; 2.00 A; A=106-263.
PDB; 3UVC; X-ray; 1.30 A; A/B=106-263.
PDB; 4EFS; X-ray; 1.63 A; A=106-263.
PDB; 4GQL; X-ray; 1.15 A; A=106-263.
PDB; 4GR0; X-ray; 1.50 A; A=106-263.
PDB; 4GR3; X-ray; 1.49 A; A=106-263.
PDB; 4GR8; X-ray; 1.30 A; A=111-262.
PDB; 4GUY; X-ray; 2.00 A; A=106-263.
PDB; 4H30; X-ray; 1.43 A; A/B=106-263.
PDB; 4H49; X-ray; 2.16 A; A/B/C/D=106-263.
PDB; 4H76; X-ray; 1.50 A; A=106-263.
PDB; 4H84; X-ray; 1.59 A; A/B=106-263.
PDB; 4I03; X-ray; 1.70 A; A=106-263.
PDB; 4IJO; X-ray; 1.90 A; A=106-263.
PDB; 5CXA; X-ray; 1.30 A; A=106-263.
PDB; 5CZM; X-ray; 1.30 A; A=106-263.
PDB; 5D2B; X-ray; 1.20 A; A=106-263.
PDB; 5D3C; X-ray; 1.31 A; A=106-263.
PDB; 5I0L; X-ray; 2.45 A; A/B=106-263.
PDB; 5I2Z; X-ray; 2.30 A; A/B/C/D=106-263.
PDB; 5I3M; X-ray; 2.17 A; A/B/C/D=106-263.
PDB; 5I43; X-ray; 1.95 A; A/B/C/D=106-263.
PDB; 5I4O; X-ray; 2.05 A; A/B/C/D=106-263.
PDB; 5L79; X-ray; 2.07 A; A=106-263.
PDB; 5L7F; X-ray; 1.80 A; A/B=106-263.
PDB; 5LAB; X-ray; 1.34 A; A=106-263.
PDB; 5N5J; X-ray; 1.80 A; A=106-263.
PDB; 5N5K; X-ray; 1.80 A; A=108-263.
PDBsum; 1JIZ; -.
PDBsum; 1JK3; -.
PDBsum; 1OS2; -.
PDBsum; 1OS9; -.
PDBsum; 1RMZ; -.
PDBsum; 1ROS; -.
PDBsum; 1UTT; -.
PDBsum; 1UTZ; -.
PDBsum; 1Y93; -.
PDBsum; 1YCM; -.
PDBsum; 1Z3J; -.
PDBsum; 2HU6; -.
PDBsum; 2JXY; -.
PDBsum; 2K2G; -.
PDBsum; 2K9C; -.
PDBsum; 2KRJ; -.
PDBsum; 2MLR; -.
PDBsum; 2MLS; -.
PDBsum; 2N8R; -.
PDBsum; 2OXU; -.
PDBsum; 2OXW; -.
PDBsum; 2OXZ; -.
PDBsum; 2POJ; -.
PDBsum; 2W0D; -.
PDBsum; 2WO8; -.
PDBsum; 2WO9; -.
PDBsum; 2WOA; -.
PDBsum; 2Z2D; -.
PDBsum; 3BA0; -.
PDBsum; 3EHX; -.
PDBsum; 3EHY; -.
PDBsum; 3F15; -.
PDBsum; 3F16; -.
PDBsum; 3F17; -.
PDBsum; 3F18; -.
PDBsum; 3F19; -.
PDBsum; 3F1A; -.
PDBsum; 3LIK; -.
PDBsum; 3LIL; -.
PDBsum; 3LIR; -.
PDBsum; 3LJG; -.
PDBsum; 3LK8; -.
PDBsum; 3LKA; -.
PDBsum; 3N2U; -.
PDBsum; 3N2V; -.
PDBsum; 3NX7; -.
PDBsum; 3RTS; -.
PDBsum; 3RTT; -.
PDBsum; 3TS4; -.
PDBsum; 3TSK; -.
PDBsum; 3UVC; -.
PDBsum; 4EFS; -.
PDBsum; 4GQL; -.
PDBsum; 4GR0; -.
PDBsum; 4GR3; -.
PDBsum; 4GR8; -.
PDBsum; 4GUY; -.
PDBsum; 4H30; -.
PDBsum; 4H49; -.
PDBsum; 4H76; -.
PDBsum; 4H84; -.
PDBsum; 4I03; -.
PDBsum; 4IJO; -.
PDBsum; 5CXA; -.
PDBsum; 5CZM; -.
PDBsum; 5D2B; -.
PDBsum; 5D3C; -.
PDBsum; 5I0L; -.
PDBsum; 5I2Z; -.
PDBsum; 5I3M; -.
PDBsum; 5I43; -.
PDBsum; 5I4O; -.
PDBsum; 5L79; -.
PDBsum; 5L7F; -.
PDBsum; 5LAB; -.
PDBsum; 5N5J; -.
PDBsum; 5N5K; -.
DisProt; DP00571; -.
ProteinModelPortal; P39900; -.
SMR; P39900; -.
BioGrid; 110464; 1.
IntAct; P39900; 1.
MINT; P39900; -.
BindingDB; P39900; -.
ChEMBL; CHEMBL4393; -.
DrugBank; DB07921; 2-[(4-fluorophenyl)sulfonylamino]-N-oxo-ethanamide.
DrugBank; DB00551; Acetohydroxamic Acid.
DrugBank; DB05387; AE-941.
DrugBank; DB03880; Batimastat.
DrugBank; DB02118; CP-271485.
DrugBank; DB00786; Marimastat.
DrugBank; DB07446; N-(biphenyl-4-ylsulfonyl)-D-leucine.
DrugBank; DB08599; N-[(4-methoxyphenyl)sulfonyl]-D-alanine.
DrugBank; DB07556; N-HYDROXY-2(R)-[[(4-METHOXYPHENYL)SULFONYL](3-PICOLYL)AMINO]-3-METHYLBUTANAMIDE HYDROCHLORIDE.
DrugBank; DB08271; N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID.
DrugBank; DB07922; N-oxo-2-(phenylsulfonylamino)ethanamide.
DrugBank; DB07920; N-oxo-2-[(4-phenylphenyl)sulfonylamino]ethanamide.
DrugBank; DB03367; PF-00356231.
GuidetoPHARMACOLOGY; 1636; -.
MEROPS; M10.009; -.
iPTMnet; P39900; -.
PhosphoSitePlus; P39900; -.
BioMuta; MMP12; -.
DMDM; 729179; -.
PeptideAtlas; P39900; -.
PRIDE; P39900; -.
ProteomicsDB; 55327; -.
TopDownProteomics; P39900; -.
DNASU; 4321; -.
Ensembl; ENST00000571244; ENSP00000458585; ENSG00000262406.
GeneID; 4321; -.
KEGG; hsa:4321; -.
UCSC; uc031yde.2; human.
CTD; 4321; -.
DisGeNET; 4321; -.
EuPathDB; HostDB:ENSG00000262406.2; -.
GeneCards; MMP12; -.
HGNC; HGNC:7158; MMP12.
MIM; 601046; gene.
neXtProt; NX_P39900; -.
OpenTargets; ENSG00000262406; -.
PharmGKB; PA30870; -.
GeneTree; ENSGT00760000118870; -.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; P39900; -.
KO; K01413; -.
OMA; FLFKDDK; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; P39900; -.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
ChiTaRS; MMP12; human.
EvolutionaryTrace; P39900; -.
GeneWiki; Matrix_metallopeptidase_12; -.
GenomeRNAi; 4321; -.
PRO; PR:P39900; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000262406; -.
CleanEx; HS_MMP12; -.
Genevisible; P39900; HS.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IMP:CAFA.
GO; GO:0005634; C:nucleus; IMP:CAFA.
GO; GO:0005509; F:calcium ion binding; IMP:CAFA.
GO; GO:0005518; F:collagen binding; IPI:CAFA.
GO; GO:0001047; F:core promoter binding; IMP:CAFA.
GO; GO:0004175; F:endopeptidase activity; TAS:UniProtKB.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:CAFA.
GO; GO:0043565; F:sequence-specific DNA binding; IMP:CAFA.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IMP:CAFA.
GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IDA:BHF-UCL.
GO; GO:1902741; P:positive regulation of interferon-alpha secretion; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:CAFA.
GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
GO; GO:0006606; P:protein import into nucleus; IMP:CAFA.
GO; GO:0006508; P:proteolysis; IDA:CAFA.
GO; GO:0050691; P:regulation of defense response to virus by host; IEA:Ensembl.
GO; GO:0035313; P:wound healing, spreading of epidermal cells; IDA:BHF-UCL.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 1.10.101.10; -; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 2.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR028718; MMP12.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR021158; Pept_M10A_Zn_BS.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
InterPro; IPR036366; PGBDSf.
PANTHER; PTHR10201:SF32; PTHR10201:SF32; 1.
Pfam; PF00045; Hemopexin; 4.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PROSITE; PS00024; HEMOPEXIN; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Disulfide bond;
Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
Metalloprotease; Polymorphism; Protease; Reference proteome; Repeat;
Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 16 {ECO:0000305}.
PROPEP 17 105 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000028776.
CHAIN 106 470 Macrophage metalloelastase.
/FTId=PRO_0000028777.
REPEAT 279 328 Hemopexin 1.
REPEAT 329 375 Hemopexin 2.
REPEAT 377 425 Hemopexin 3.
REPEAT 426 470 Hemopexin 4.
MOTIF 90 97 Cysteine switch. {ECO:0000250}.
ACT_SITE 219 219
METAL 92 92 Zinc 2; in inhibited form. {ECO:0000250}.
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 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 289 289 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 333 333 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 381 381 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 430 430 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
CARBOHYD 20 20 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 282 470 {ECO:0000250}.
VARIANT 357 357 N -> S (in dbSNP:rs652438).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2}.
/FTId=VAR_021343.
VARIANT 469 469 G -> R (in dbSNP:rs28381701).
{ECO:0000269|Ref.2}.
/FTId=VAR_021344.
STRAND 106 108 {ECO:0000244|PDB:2K2G}.
STRAND 110 118 {ECO:0000244|PDB:1Y93}.
STRAND 123 125 {ECO:0000244|PDB:2W0D}.
HELIX 127 142 {ECO:0000244|PDB:1Y93}.
STRAND 144 146 {ECO:0000244|PDB:4H84}.
STRAND 148 151 {ECO:0000244|PDB:1Y93}.
STRAND 153 155 {ECO:0000244|PDB:1Y93}.
STRAND 158 164 {ECO:0000244|PDB:1Y93}.
STRAND 169 171 {ECO:0000244|PDB:1Y93}.
STRAND 176 179 {ECO:0000244|PDB:1Y93}.
STRAND 182 184 {ECO:0000244|PDB:1Y93}.
STRAND 187 189 {ECO:0000244|PDB:1JK3}.
TURN 190 193 {ECO:0000244|PDB:1Y93}.
STRAND 195 198 {ECO:0000244|PDB:1Y93}.
STRAND 203 211 {ECO:0000244|PDB:1Y93}.
HELIX 212 223 {ECO:0000244|PDB:1Y93}.
TURN 232 236 {ECO:0000244|PDB:3BA0}.
STRAND 237 239 {ECO:0000244|PDB:1Y93}.
HELIX 245 247 {ECO:0000244|PDB:1Y93}.
HELIX 252 259 {ECO:0000244|PDB:1Y93}.
STRAND 260 262 {ECO:0000244|PDB:3BA0}.
STRAND 266 268 {ECO:0000244|PDB:3BA0}.
STRAND 281 284 {ECO:0000244|PDB:2JXY}.
STRAND 291 294 {ECO:0000244|PDB:3BA0}.
STRAND 297 302 {ECO:0000244|PDB:3BA0}.
STRAND 305 308 {ECO:0000244|PDB:3BA0}.
STRAND 318 320 {ECO:0000244|PDB:3BA0}.
HELIX 321 324 {ECO:0000244|PDB:3BA0}.
STRAND 334 338 {ECO:0000244|PDB:3BA0}.
HELIX 339 341 {ECO:0000244|PDB:3BA0}.
STRAND 343 348 {ECO:0000244|PDB:3BA0}.
STRAND 351 354 {ECO:0000244|PDB:3BA0}.
STRAND 357 360 {ECO:0000244|PDB:2JXY}.
TURN 361 363 {ECO:0000244|PDB:3BA0}.
STRAND 365 367 {ECO:0000244|PDB:3BA0}.
TURN 368 372 {ECO:0000244|PDB:3BA0}.
STRAND 382 386 {ECO:0000244|PDB:3BA0}.
TURN 387 390 {ECO:0000244|PDB:3BA0}.
STRAND 391 396 {ECO:0000244|PDB:3BA0}.
STRAND 399 404 {ECO:0000244|PDB:3BA0}.
TURN 405 408 {ECO:0000244|PDB:3BA0}.
HELIX 418 421 {ECO:0000244|PDB:3BA0}.
STRAND 430 435 {ECO:0000244|PDB:3BA0}.
TURN 436 438 {ECO:0000244|PDB:3BA0}.
STRAND 439 444 {ECO:0000244|PDB:3BA0}.
STRAND 447 452 {ECO:0000244|PDB:3BA0}.
TURN 453 456 {ECO:0000244|PDB:3BA0}.
STRAND 457 463 {ECO:0000244|PDB:3BA0}.
TURN 464 469 {ECO:0000244|PDB:3BA0}.
SEQUENCE 470 AA; 54002 MW; 8C745EEA8C0EA216 CRC64;
MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFGERYLEKF YGLEINKLPV TKMKYSGNLM
KEKIQEMQHF LGLKVTGQLD TSTLEMMHAP RCGVPDVHHF REMPGGPVWR KHYITYRINN
YTPDMNREDV DYAIRKAFQV WSNVTPLKFS KINTGMADIL VVFARGAHGD FHAFDGKGGI
LAHAFGPGSG IGGDAHFDED EFWTTHSGGT NLFLTAVHEI GHSLGLGHSS DPKAVMFPTY
KYVDINTFRL SADDIRGIQS LYGDPKENQR LPNPDNSEPA LCDPNLSFDA VTTVGNKIFF
FKDRFFWLKV SERPKTSVNL ISSLWPTLPS GIEAAYEIEA RNQVFLFKDD KYWLISNLRP
EPNYPKSIHS FGFPNFVKKI DAAVFNPRFY RTYFFVDNQY WRYDERRQMM DPGYPKLITK
NFQGIGPKID AVFYSKNKYY YFFQGSNQFE YDFLLQRITK TLKSNSWFGC


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