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Protein

Macrophage metalloelastase

Gene

MMP12

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 4 Ca2+ ions per subunit.
  • Zn2+Note: Binds 2 Zn2+ ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi92 – 921Zinc 2; in inhibited formBy similarity
Metal bindingi124 – 1241Calcium 1
Metal bindingi158 – 1581Calcium 2
Metal bindingi168 – 1681Zinc 1
Metal bindingi170 – 1701Zinc 1
Metal bindingi175 – 1751Calcium 3
Metal bindingi176 – 1761Calcium 3; via carbonyl oxygen
Metal bindingi178 – 1781Calcium 3; via carbonyl oxygen
Metal bindingi180 – 1801Calcium 3; via carbonyl oxygen
Metal bindingi183 – 1831Zinc 1
Metal bindingi190 – 1901Calcium 2; via carbonyl oxygen
Metal bindingi192 – 1921Calcium 2; via carbonyl oxygen
Metal bindingi194 – 1941Calcium 2
Metal bindingi196 – 1961Zinc 1
Metal bindingi198 – 1981Calcium 3
Metal bindingi199 – 1991Calcium 1
Metal bindingi201 – 2011Calcium 1
Metal bindingi201 – 2011Calcium 3
Metal bindingi218 – 2181Zinc 2; catalytic
Active sitei219 – 2191
Metal bindingi222 – 2221Zinc 2; catalytic
Metal bindingi228 – 2281Zinc 2; catalytic
Metal bindingi289 – 2891Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi333 – 3331Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi381 – 3811Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi430 – 4301Calcium 4; via carbonyl oxygenBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. endopeptidase activity Source: UniProtKB
  3. metalloendopeptidase activity Source: UniProtKB
  4. zinc ion binding Source: ProtInc

GO - Biological processi

  1. collagen catabolic process Source: Reactome
  2. extracellular matrix disassembly Source: Reactome
  3. extracellular matrix organization Source: Reactome
  4. positive regulation of epithelial cell proliferation involved in wound healing Source: BHF-UCL
  5. proteolysis Source: ProtInc
  6. wound healing, spreading of epidermal cells Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_150401. Collagen degradation.

Protein family/group databases

MEROPSiM10.009.

Names & Taxonomyi

Protein namesi
Recommended name:
Macrophage metalloelastase (EC:3.4.24.65)
Short name:
MME
Alternative name(s):
Macrophage elastase
Short name:
ME
Short name:
hME
Matrix metalloproteinase-12
Short name:
MMP-12
Gene namesi
Name:MMP12
Synonyms:HME
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7158. MMP12.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30870.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616CuratedAdd
BLAST
Propeptidei17 – 10589Activation peptideBy similarityPRO_0000028776Add
BLAST
Chaini106 – 470365Macrophage metalloelastasePRO_0000028777Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi20 – 201N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi282 ↔ 470By similarity
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP39900.
PRIDEiP39900.

PTM databases

PhosphoSiteiP39900.

Expressioni

Tissue specificityi

Found in alveolar macrophages but not in peripheral blood monocytes.

Inductioni

By exposure to bacterial lipopolysaccharides (LPS). Inhibited by dexamethasone.

Gene expression databases

CleanExiHS_MMP12.
GenevestigatoriP39900.

Interactioni

Protein-protein interaction databases

BioGridi110464. 1 interaction.
IntActiP39900. 1 interaction.
MINTiMINT-7709562.
STRINGi9606.ENSP00000320664.

Structurei

Secondary structure

1
470
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi106 – 1083Combined sources
Beta strandi110 – 1189Combined sources
Beta strandi123 – 1253Combined sources
Helixi127 – 14216Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi148 – 1514Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi158 – 1647Combined sources
Beta strandi169 – 1713Combined sources
Beta strandi176 – 1794Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi187 – 1893Combined sources
Turni190 – 1934Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi203 – 2119Combined sources
Helixi212 – 22312Combined sources
Turni232 – 2365Combined sources
Beta strandi237 – 2393Combined sources
Helixi245 – 2473Combined sources
Helixi252 – 2598Combined sources
Beta strandi260 – 2623Combined sources
Beta strandi266 – 2683Combined sources
Beta strandi281 – 2844Combined sources
Beta strandi291 – 2944Combined sources
Beta strandi297 – 3026Combined sources
Beta strandi305 – 3084Combined sources
Beta strandi318 – 3203Combined sources
Helixi321 – 3244Combined sources
Beta strandi334 – 3385Combined sources
Helixi339 – 3413Combined sources
Beta strandi343 – 3486Combined sources
Beta strandi351 – 3544Combined sources
Beta strandi357 – 3604Combined sources
Turni361 – 3633Combined sources
Beta strandi365 – 3673Combined sources
Turni368 – 3725Combined sources
Beta strandi382 – 3865Combined sources
Turni387 – 3904Combined sources
Beta strandi391 – 3966Combined sources
Beta strandi399 – 4046Combined sources
Turni405 – 4084Combined sources
Helixi418 – 4214Combined sources
Beta strandi430 – 4356Combined sources
Turni436 – 4383Combined sources
Beta strandi439 – 4446Combined sources
Beta strandi447 – 4526Combined sources
Turni453 – 4564Combined sources
Beta strandi457 – 4637Combined sources
Turni464 – 4696Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JIZX-ray2.60A/B100-264[»]
1JK3X-ray1.09A106-263[»]
1OS2X-ray2.15A/B/C/D/E/F106-268[»]
1OS9X-ray1.85A/B/C/D/E/F106-268[»]
1RMZX-ray1.34A106-263[»]
1ROSX-ray2.00A/B106-268[»]
1UTTX-ray2.20A106-264[»]
1UTZX-ray2.50A/B106-264[»]
1Y93X-ray1.03A106-263[»]
1YCMNMR-A106-263[»]
1Z3JNMR-A106-263[»]
2HU6X-ray1.32A106-263[»]
2JXYNMR-A278-470[»]
2K2GNMR-A100-263[»]
2K9CNMR-A112-263[»]
2KRJNMR-A112-263[»]
2MLRNMR-A100-263[»]
2MLSNMR-A100-263[»]
2OXUX-ray1.24A106-263[»]
2OXWX-ray1.15A106-263[»]
2OXZX-ray1.90A106-263[»]
2POJNMR-A100-263[»]
2W0DX-ray2.00A/B/C/D106-263[»]
2WO8X-ray2.00A/B/C/D106-268[»]
2WO9X-ray1.70A/B/C/D106-268[»]
2WOAX-ray2.30A/B/C/D106-268[»]
2Z2DNMR-A100-263[»]
3BA0X-ray3.00A106-470[»]
3EHXX-ray1.90A106-263[»]
3EHYX-ray1.90A106-263[»]
3F15X-ray1.70A106-263[»]
3F16X-ray1.16A106-263[»]
3F17X-ray1.10A106-263[»]
3F18X-ray1.13A106-263[»]
3F19X-ray1.13A106-263[»]
3F1AX-ray1.25A106-263[»]
3LIKX-ray1.80A106-263[»]
3LILX-ray1.80A106-263[»]
3LIRX-ray1.90A106-263[»]
3LJGX-ray1.31A106-263[»]
3LK8X-ray1.80A106-263[»]
3LKAX-ray1.80A106-263[»]
3N2UX-ray1.81A106-263[»]
3N2VX-ray1.55A106-263[»]
3NX7X-ray1.80A106-263[»]
3RTSX-ray1.81A106-263[»]
3RTTX-ray1.82A106-263[»]
3TS4X-ray1.59A106-263[»]
3TSKX-ray2.00A106-263[»]
3UVCX-ray1.30A/B106-263[»]
4EFSX-ray1.63A106-263[»]
4GQLX-ray1.15A106-263[»]
4GR0X-ray1.50A106-263[»]
4GR3X-ray1.49A106-263[»]
4GR8X-ray1.30A111-262[»]
4GUYX-ray2.00A106-263[»]
4H30X-ray1.43A/B106-263[»]
4H49X-ray2.16A/B/C/D106-263[»]
4H76X-ray1.50A106-263[»]
4H84X-ray1.59A/B106-263[»]
4I03X-ray1.70A106-263[»]
4IJOX-ray1.90A106-263[»]
DisProtiDP00571.
ProteinModelPortaliP39900.
SMRiP39900. Positions 34-470.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39900.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati279 – 32850Hemopexin 1Add
BLAST
Repeati329 – 37547Hemopexin 2Add
BLAST
Repeati377 – 42549Hemopexin 3Add
BLAST
Repeati426 – 47045Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi90 – 978Cysteine switchBy similarity

Domaini

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.

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG323958.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP39900.
KOiK01413.
OMAiRKHYITY.
OrthoDBiEOG7XPZ57.
PhylomeDBiP39900.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR028718. MMP12.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF32. PTHR10201:SF32. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P39900-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFGERYLEKF YGLEINKLPV
60 70 80 90 100
TKMKYSGNLM KEKIQEMQHF LGLKVTGQLD TSTLEMMHAP RCGVPDVHHF
110 120 130 140 150
REMPGGPVWR KHYITYRINN YTPDMNREDV DYAIRKAFQV WSNVTPLKFS
160 170 180 190 200
KINTGMADIL VVFARGAHGD FHAFDGKGGI LAHAFGPGSG IGGDAHFDED
210 220 230 240 250
EFWTTHSGGT NLFLTAVHEI GHSLGLGHSS DPKAVMFPTY KYVDINTFRL
260 270 280 290 300
SADDIRGIQS LYGDPKENQR LPNPDNSEPA LCDPNLSFDA VTTVGNKIFF
310 320 330 340 350
FKDRFFWLKV SERPKTSVNL ISSLWPTLPS GIEAAYEIEA RNQVFLFKDD
360 370 380 390 400
KYWLISNLRP EPNYPKSIHS FGFPNFVKKI DAAVFNPRFY RTYFFVDNQY
410 420 430 440 450
WRYDERRQMM DPGYPKLITK NFQGIGPKID AVFYSKNKYY YFFQGSNQFE
460 470
YDFLLQRITK TLKSNSWFGC
Length:470
Mass (Da):54,002
Last modified:February 1, 1995 - v1
Checksum:i8C745EEA8C0EA216
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti357 – 3571N → S.2 Publications
Corresponds to variant rs652438 [ dbSNP | Ensembl ].
VAR_021343
Natural varianti469 – 4691G → R.1 Publication
Corresponds to variant rs28381701 [ dbSNP | Ensembl ].
VAR_021344

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23808 mRNA. Translation: AAA58658.1. Sequence problems.
AY856072 Genomic DNA. Translation: AAW29944.1.
AK313959 mRNA. Translation: BAG36675.1.
CH471065 Genomic DNA. Translation: EAW67033.1.
BC112301 mRNA. Translation: AAI12302.1.
BC143773 mRNA. Translation: AAI43774.1.
CCDSiCCDS73375.1.
PIRiA49499.
RefSeqiNP_002417.2. NM_002426.4.
UniGeneiHs.1695.
Hs.709832.

Genome annotation databases

EnsembliENST00000571244; ENSP00000458585; ENSG00000262406.
GeneIDi4321.
KEGGihsa:4321.
UCSCiuc001phk.3. human.

Polymorphism databases

DMDMi729179.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23808 mRNA. Translation: AAA58658.1. Sequence problems.
AY856072 Genomic DNA. Translation: AAW29944.1.
AK313959 mRNA. Translation: BAG36675.1.
CH471065 Genomic DNA. Translation: EAW67033.1.
BC112301 mRNA. Translation: AAI12302.1.
BC143773 mRNA. Translation: AAI43774.1.
CCDSiCCDS73375.1.
PIRiA49499.
RefSeqiNP_002417.2. NM_002426.4.
UniGeneiHs.1695.
Hs.709832.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JIZX-ray2.60A/B100-264[»]
1JK3X-ray1.09A106-263[»]
1OS2X-ray2.15A/B/C/D/E/F106-268[»]
1OS9X-ray1.85A/B/C/D/E/F106-268[»]
1RMZX-ray1.34A106-263[»]
1ROSX-ray2.00A/B106-268[»]
1UTTX-ray2.20A106-264[»]
1UTZX-ray2.50A/B106-264[»]
1Y93X-ray1.03A106-263[»]
1YCMNMR-A106-263[»]
1Z3JNMR-A106-263[»]
2HU6X-ray1.32A106-263[»]
2JXYNMR-A278-470[»]
2K2GNMR-A100-263[»]
2K9CNMR-A112-263[»]
2KRJNMR-A112-263[»]
2MLRNMR-A100-263[»]
2MLSNMR-A100-263[»]
2OXUX-ray1.24A106-263[»]
2OXWX-ray1.15A106-263[»]
2OXZX-ray1.90A106-263[»]
2POJNMR-A100-263[»]
2W0DX-ray2.00A/B/C/D106-263[»]
2WO8X-ray2.00A/B/C/D106-268[»]
2WO9X-ray1.70A/B/C/D106-268[»]
2WOAX-ray2.30A/B/C/D106-268[»]
2Z2DNMR-A100-263[»]
3BA0X-ray3.00A106-470[»]
3EHXX-ray1.90A106-263[»]
3EHYX-ray1.90A106-263[»]
3F15X-ray1.70A106-263[»]
3F16X-ray1.16A106-263[»]
3F17X-ray1.10A106-263[»]
3F18X-ray1.13A106-263[»]
3F19X-ray1.13A106-263[»]
3F1AX-ray1.25A106-263[»]
3LIKX-ray1.80A106-263[»]
3LILX-ray1.80A106-263[»]
3LIRX-ray1.90A106-263[»]
3LJGX-ray1.31A106-263[»]
3LK8X-ray1.80A106-263[»]
3LKAX-ray1.80A106-263[»]
3N2UX-ray1.81A106-263[»]
3N2VX-ray1.55A106-263[»]
3NX7X-ray1.80A106-263[»]
3RTSX-ray1.81A106-263[»]
3RTTX-ray1.82A106-263[»]
3TS4X-ray1.59A106-263[»]
3TSKX-ray2.00A106-263[»]
3UVCX-ray1.30A/B106-263[»]
4EFSX-ray1.63A106-263[»]
4GQLX-ray1.15A106-263[»]
4GR0X-ray1.50A106-263[»]
4GR3X-ray1.49A106-263[»]
4GR8X-ray1.30A111-262[»]
4GUYX-ray2.00A106-263[»]
4H30X-ray1.43A/B106-263[»]
4H49X-ray2.16A/B/C/D106-263[»]
4H76X-ray1.50A106-263[»]
4H84X-ray1.59A/B106-263[»]
4I03X-ray1.70A106-263[»]
4IJOX-ray1.90A106-263[»]
DisProtiDP00571.
ProteinModelPortaliP39900.
SMRiP39900. Positions 34-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110464. 1 interaction.
IntActiP39900. 1 interaction.
MINTiMINT-7709562.
STRINGi9606.ENSP00000320664.

Chemistry

BindingDBiP39900.
ChEMBLiCHEMBL4393.
DrugBankiDB00551. Acetohydroxamic Acid.
DB00786. Marimastat.
GuidetoPHARMACOLOGYi1636.

Protein family/group databases

MEROPSiM10.009.

PTM databases

PhosphoSiteiP39900.

Polymorphism databases

DMDMi729179.

Proteomic databases

PaxDbiP39900.
PRIDEiP39900.

Protocols and materials databases

DNASUi4321.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000571244; ENSP00000458585; ENSG00000262406.
GeneIDi4321.
KEGGihsa:4321.
UCSCiuc001phk.3. human.

Organism-specific databases

CTDi4321.
GeneCardsiGC11M102767.
HGNCiHGNC:7158. MMP12.
MIMi601046. gene.
neXtProtiNX_P39900.
PharmGKBiPA30870.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG323958.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP39900.
KOiK01413.
OMAiRKHYITY.
OrthoDBiEOG7XPZ57.
PhylomeDBiP39900.

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_150401. Collagen degradation.

Miscellaneous databases

ChiTaRSiMMP12. human.
EvolutionaryTraceiP39900.
GeneWikiiMatrix_metallopeptidase_12.
GenomeRNAii4321.
NextBioi17001.
PROiP39900.
SOURCEiSearch...

Gene expression databases

CleanExiHS_MMP12.
GenevestigatoriP39900.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR028718. MMP12.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF32. PTHR10201:SF32. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages."
    Shapiro S.D., Kobayashi D.K., Ley T.J.
    J. Biol. Chem. 268:23824-23829(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Alveolar macrophage.
  2. NIEHS SNPs program
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-357 AND ARG-469.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Esophagus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-357.
  6. "Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase."
    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.
    J. Biol. Chem. 272:12189-12194(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 A crystal structure."
    Lang R., Kocourek A., Braun M., Tschesche H., Huber R., Bode W., Maskos K.
    J. Mol. Biol. 312:731-742(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS) OF 106-263.
  8. "Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor."
    Nar H., Werle K., Bauer M.M.T., Dollinger H., Jung B.
    J. Mol. Biol. 312:743-751(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 100-280.

Entry informationi

Entry nameiMMP12_HUMAN
AccessioniPrimary (citable) accession number: P39900
Secondary accession number(s): B2R9X8, B7ZLF6, Q2M1L9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 4, 2015
This is version 162 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.