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Protein

Macrophage metalloelastase

Gene

Mmp12

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript 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 (By similarity).By similarity

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+By similarityNote: Binds 4 Ca2+ ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi88Zinc 2; in inhibited formBy similarity1
Metal bindingi120Calcium 1By similarity1
Metal bindingi154Calcium 2By similarity1
Metal bindingi164Zinc 1By similarity1
Metal bindingi166Zinc 1By similarity1
Metal bindingi171Calcium 3By similarity1
Metal bindingi172Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi174Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi176Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi179Zinc 1By similarity1
Metal bindingi186Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi190Calcium 2By similarity1
Metal bindingi192Zinc 1By similarity1
Metal bindingi194Calcium 3By similarity1
Metal bindingi195Calcium 1By similarity1
Metal bindingi197Calcium 1By similarity1
Metal bindingi197Calcium 3By similarity1
Metal bindingi214Zinc 2; catalyticBy similarity1
Active sitei215PROSITE-ProRule annotation1
Metal bindingi218Zinc 2; catalyticBy similarity1
Metal bindingi224Zinc 2; catalyticBy similarity1
Metal bindingi285Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi377Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi426Calcium 4; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

  • positive regulation of epithelial cell proliferation Source: RGD
  • regulation of trophoblast cell migration Source: RGD
  • response to drug Source: RGD
  • response to hypoxia Source: RGD
  • response to organic cyclic compound Source: RGD
  • wound healing Source: InterPro

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
LigandCalcium, Metal-binding, Zinc

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):
Matrix metalloproteinase-12
Short name:
MMP-12
Gene namesi
Name:Mmp12
Synonyms:Mmel
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620195 Mmp12

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5506

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21CuratedAdd BLAST21
PropeptideiPRO_000002878222 – 101Activation peptideBy similarityAdd BLAST80
ChainiPRO_0000028783102 – 465Macrophage metalloelastaseAdd BLAST364

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi278 ↔ 465By similarity
Glycosylationi313N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ63341
PRIDEiQ63341

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011727

Chemistry databases

BindingDBiQ63341

Structurei

3D structure databases

ProteinModelPortaliQ63341
SMRiQ63341
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati281 – 324Hemopexin 1Add BLAST44
Repeati325 – 371Hemopexin 2Add BLAST47
Repeati373 – 421Hemopexin 3Add BLAST49
Repeati422 – 465Hemopexin 4Add BLAST44

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi86 – 93Cysteine 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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1565 Eukaryota
ENOG410XQ5D LUCA
HOGENOMiHOG000217927
HOVERGENiHBG052484
InParanoidiQ63341
KOiK01413
PhylomeDBiQ63341
TreeFamiTF315428

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
InterProiView protein in InterPro
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028718 MMP12
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
PANTHERiPTHR10201:SF32 PTHR10201:SF32, 1 hit
PfamiView protein in Pfam
PF00045 Hemopexin, 4 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PIRSFiPIRSF001191 Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138 MATRIXIN
SMARTiView protein in SMART
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
PROSITEiView protein in PROSITE
PS00024 HEMOPEXIN, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q63341-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFLLVLVLL VSLQVSACGA APMNESEFAE WYLSRFFDYQ GDRIPMTKTK
60 70 80 90 100
TNRNLLEEKL QEMQQFFGLE VTGQLDTSTL KIMHTSRCGV PDVQHLRAVP
110 120 130 140 150
QRSRWMKRYL TYRIYNYTPD MKRADVDYIF QKAFQVWSDV TPLRFRKIHK
160 170 180 190 200
GEADITILFA FGDHGDFYDF DGKGGTLAHA FYPGPGIQGD AHFDEAETWT
210 220 230 240 250
KSFQGTNLFL VAVHELGHSL GLRHSNNPKS IMYPTYRYLH PNTFRLSADD
260 270 280 290 300
IHSIQSLYGA PVKNPSLTNP GSPPSTVCHQ SLSFDAVTTV GDKIFFFKDW
310 320 330 340 350
FFWWRLPGSP ATNITSISSM WPTIPSGIQA AYEIGGRNQL FLFKDEKYWL
360 370 380 390 400
INNLVPEPHY PRSIHSLGFP ASVKKIDAAV FDPLRQKVYF FVDKQYWRYD
410 420 430 440 450
VRQELMDAAY PKLISTHFPG IRPKIDAVLY FKRHYYIFQG AYQLEYDPLL
460
DRVTKTLSST SWFGC
Length:465
Mass (Da):53,738
Last modified:November 1, 1996 - v1
Checksum:iE779B6014EC6FF68
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti223R → P in AAH88120 (PubMed:15489334).Curated1
Sequence conflicti451D → H in AAH88120 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98517 mRNA Translation: CAA67142.1
BC088120 mRNA Translation: AAH88120.1
RefSeqiNP_446415.2, NM_053963.2
UniGeneiRn.33193

Genome annotation databases

GeneIDi117033
KEGGirno:117033
UCSCiRGD:620195 rat

Similar proteinsi

Entry informationi

Entry nameiMMP12_RAT
AccessioniPrimary (citable) accession number: Q63341
Secondary accession number(s): Q5I0P0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 148 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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