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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)DescriptionActionsGraphical viewLength
Metal bindingi92Zinc 2; in inhibited formBy similarity1
Metal bindingi124Calcium 11
Metal bindingi158Calcium 21
Metal bindingi168Zinc 11
Metal bindingi170Zinc 11
Metal bindingi175Calcium 31
Metal bindingi176Calcium 3; via carbonyl oxygen1
Metal bindingi178Calcium 3; via carbonyl oxygen1
Metal bindingi180Calcium 3; via carbonyl oxygen1
Metal bindingi183Zinc 11
Metal bindingi190Calcium 2; via carbonyl oxygen1
Metal bindingi192Calcium 2; via carbonyl oxygen1
Metal bindingi194Calcium 21
Metal bindingi196Zinc 11
Metal bindingi198Calcium 31
Metal bindingi199Calcium 11
Metal bindingi201Calcium 11
Metal bindingi201Calcium 31
Metal bindingi218Zinc 2; catalytic1
Active sitei2191
Metal bindingi222Zinc 2; catalytic1
Metal bindingi228Zinc 2; catalytic1
Metal bindingi289Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi333Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi381Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi430Calcium 4; via carbonyl oxygenBy similarity1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • endopeptidase activity Source: UniProtKB
  • metalloendopeptidase activity Source: UniProtKB
  • serine-type endopeptidase activity Source: Reactome
  • zinc ion binding Source: ProtInc

GO - Biological processi

  • collagen catabolic process Source: Reactome
  • extracellular matrix disassembly Source: Reactome
  • positive regulation of epithelial cell proliferation involved in wound healing Source: BHF-UCL
  • proteolysis Source: ProtInc
  • 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

BioCyciZFISH:HS03303-MONOMER.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474228. Degradation of the extracellular matrix.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7158. MMP12.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi4321.
OpenTargetsiENSG00000262406.
PharmGKBiPA30870.

Chemistry databases

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

Polymorphism and mutation databases

BioMutaiMMP12.
DMDMi729179.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16CuratedAdd BLAST16
PropeptideiPRO_000002877617 – 105Activation peptideBy similarityAdd BLAST89
ChainiPRO_0000028777106 – 470Macrophage metalloelastaseAdd BLAST365

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi20N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi282 ↔ 470By similarity
Glycosylationi285N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PeptideAtlasiP39900.
PRIDEiP39900.
TopDownProteomicsiP39900.

PTM databases

iPTMnetiP39900.
PhosphoSitePlusiP39900.

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

BgeeiENSG00000262406.
CleanExiHS_MMP12.
GenevisibleiP39900. HS.

Interactioni

Protein-protein interaction databases

BioGridi110464. 1 interactor.
IntActiP39900. 1 interactor.
MINTiMINT-7709562.

Chemistry databases

BindingDBiP39900.

Structurei

Secondary structure

1470
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi106 – 108Combined sources3
Beta strandi110 – 118Combined sources9
Beta strandi123 – 125Combined sources3
Helixi127 – 142Combined sources16
Beta strandi144 – 146Combined sources3
Beta strandi148 – 151Combined sources4
Beta strandi153 – 155Combined sources3
Beta strandi158 – 164Combined sources7
Beta strandi169 – 171Combined sources3
Beta strandi176 – 179Combined sources4
Beta strandi182 – 184Combined sources3
Beta strandi187 – 189Combined sources3
Turni190 – 193Combined sources4
Beta strandi195 – 198Combined sources4
Beta strandi203 – 211Combined sources9
Helixi212 – 223Combined sources12
Turni232 – 236Combined sources5
Beta strandi237 – 239Combined sources3
Helixi245 – 247Combined sources3
Helixi252 – 259Combined sources8
Beta strandi260 – 262Combined sources3
Beta strandi266 – 268Combined sources3
Beta strandi281 – 284Combined sources4
Beta strandi291 – 294Combined sources4
Beta strandi297 – 302Combined sources6
Beta strandi305 – 308Combined sources4
Beta strandi318 – 320Combined sources3
Helixi321 – 324Combined sources4
Beta strandi334 – 338Combined sources5
Helixi339 – 341Combined sources3
Beta strandi343 – 348Combined sources6
Beta strandi351 – 354Combined sources4
Beta strandi357 – 360Combined sources4
Turni361 – 363Combined sources3
Beta strandi365 – 367Combined sources3
Turni368 – 372Combined sources5
Beta strandi382 – 386Combined sources5
Turni387 – 390Combined sources4
Beta strandi391 – 396Combined sources6
Beta strandi399 – 404Combined sources6
Turni405 – 408Combined sources4
Helixi418 – 421Combined sources4
Beta strandi430 – 435Combined sources6
Turni436 – 438Combined sources3
Beta strandi439 – 444Combined sources6
Beta strandi447 – 452Combined sources6
Turni453 – 456Combined sources4
Beta strandi457 – 463Combined sources7
Turni464 – 469Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2N8RNMR-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[»]
5CXAX-ray1.30A106-263[»]
5CZMX-ray1.30A106-263[»]
5D2BX-ray1.20A106-263[»]
5D3CX-ray1.31A106-263[»]
5I0LX-ray2.45A/B106-263[»]
5I2ZX-ray2.30A/B/C/D106-263[»]
5I3MX-ray2.17A/B/C/D106-263[»]
5I43X-ray1.95A/B/C/D106-263[»]
5I4OX-ray2.05A/B/C/D106-263[»]
5L79X-ray2.07A106-263[»]
5L7FX-ray1.80A/B106-263[»]
5LABX-ray1.34A106-263[»]
DisProtiDP00571.
ProteinModelPortaliP39900.
SMRiP39900.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39900.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati279 – 328Hemopexin 1Add BLAST50
Repeati329 – 375Hemopexin 2Add BLAST47
Repeati377 – 425Hemopexin 3Add BLAST49
Repeati426 – 470Hemopexin 4Add BLAST45

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi90 – 97Cysteine switchBy similarity8

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

GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP39900.
KOiK01413.
OMAiQFEYDFL.
OrthoDBiEOG091G03DP.
PhylomeDBiP39900.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_021343357N → S.2 PublicationsCorresponds to variant rs652438dbSNPEnsembl.1
Natural variantiVAR_021344469G → R.1 PublicationCorresponds to variant rs28381701dbSNPEnsembl.1

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_002426.5.
UniGeneiHs.1695.
Hs.709832.

Genome annotation databases

EnsembliENST00000571244; ENSP00000458585; ENSG00000262406.
GeneIDi4321.
KEGGihsa:4321.
UCSCiuc031yde.2. human.

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_002426.5.
UniGeneiHs.1695.
Hs.709832.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2N8RNMR-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[»]
5CXAX-ray1.30A106-263[»]
5CZMX-ray1.30A106-263[»]
5D2BX-ray1.20A106-263[»]
5D3CX-ray1.31A106-263[»]
5I0LX-ray2.45A/B106-263[»]
5I2ZX-ray2.30A/B/C/D106-263[»]
5I3MX-ray2.17A/B/C/D106-263[»]
5I43X-ray1.95A/B/C/D106-263[»]
5I4OX-ray2.05A/B/C/D106-263[»]
5L79X-ray2.07A106-263[»]
5L7FX-ray1.80A/B106-263[»]
5LABX-ray1.34A106-263[»]
DisProtiDP00571.
ProteinModelPortaliP39900.
SMRiP39900.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110464. 1 interactor.
IntActiP39900. 1 interactor.
MINTiMINT-7709562.

Chemistry databases

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

Protein family/group databases

MEROPSiM10.009.

PTM databases

iPTMnetiP39900.
PhosphoSitePlusiP39900.

Polymorphism and mutation databases

BioMutaiMMP12.
DMDMi729179.

Proteomic databases

PeptideAtlasiP39900.
PRIDEiP39900.
TopDownProteomicsiP39900.

Protocols and materials databases

DNASUi4321.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000571244; ENSP00000458585; ENSG00000262406.
GeneIDi4321.
KEGGihsa:4321.
UCSCiuc031yde.2. human.

Organism-specific databases

CTDi4321.
DisGeNETi4321.
GeneCardsiMMP12.
HGNCiHGNC:7158. MMP12.
MIMi601046. gene.
neXtProtiNX_P39900.
OpenTargetsiENSG00000262406.
PharmGKBiPA30870.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP39900.
KOiK01413.
OMAiQFEYDFL.
OrthoDBiEOG091G03DP.
PhylomeDBiP39900.

Enzyme and pathway databases

BioCyciZFISH:HS03303-MONOMER.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474228. Degradation of the extracellular matrix.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000262406.
CleanExiHS_MMP12.
GenevisibleiP39900. HS.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
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...

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: November 30, 2016
This is version 176 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

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 one 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.