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Protein

Macrophage metalloelastase

Gene

Mmp12

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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
  • response to drug Source: RGD
  • response to organic cyclic compound Source: RGD
  • wound healing Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620195. Mmp12.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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...)Sequence 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.
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
Contains 4 hemopexin repeats.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.
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.
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.
PROSITEiPS00024. 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.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ63341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011727.

Chemistry databases

BindingDBiQ63341.
ChEMBLiCHEMBL5506.

Protein family/group databases

MEROPSiM10.009.

Proteomic databases

PaxDbiQ63341.
PRIDEiQ63341.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi117033.
KEGGirno:117033.
UCSCiRGD:620195. rat.

Organism-specific databases

CTDi4321.
RGDi620195. Mmp12.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ63341.
KOiK01413.
PhylomeDBiQ63341.
TreeFamiTF315428.

Miscellaneous databases

PROiQ63341.

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.
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.
PROSITEiPS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMMP12_RAT
AccessioniPrimary (citable) accession number: Q63341
Secondary accession number(s): Q5I0P0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 138 of the entry and version 1 of the sequence. [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

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.