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Q63341 (MMP12_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Macrophage metalloelastase

Short name=MME
EC=3.4.24.65
Alternative name(s):
Matrix metalloproteinase-12
Short name=MMP-12
Gene names
Name:Mmp12
Synonyms:Mmel
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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 By similarity.

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

Binds 4 calcium ions per subunit By similarity.

Binds 2 zinc ions per subunit By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

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.

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Probable
Propeptide22 – 10180Activation peptide By similarity
PRO_0000028782
Chain102 – 465364Macrophage metalloelastase
PRO_0000028783

Regions

Repeat281 – 32444Hemopexin 1
Repeat325 – 37147Hemopexin 2
Repeat373 – 42149Hemopexin 3
Repeat422 – 46544Hemopexin 4
Motif86 – 938Cysteine switch By similarity

Sites

Active site2151 By similarity
Metal binding881Zinc 2; in inhibited form By similarity
Metal binding1201Calcium 1 By similarity
Metal binding1541Calcium 2 By similarity
Metal binding1641Zinc 1 By similarity
Metal binding1661Zinc 1 By similarity
Metal binding1711Calcium 3 By similarity
Metal binding1721Calcium 3; via carbonyl oxygen By similarity
Metal binding1741Calcium 3; via carbonyl oxygen By similarity
Metal binding1761Calcium 3; via carbonyl oxygen By similarity
Metal binding1791Zinc 1 By similarity
Metal binding1861Calcium 2; via carbonyl oxygen By similarity
Metal binding1901Calcium 2 By similarity
Metal binding1921Zinc 1 By similarity
Metal binding1941Calcium 3 By similarity
Metal binding1951Calcium 1 By similarity
Metal binding1971Calcium 1 By similarity
Metal binding1971Calcium 3 By similarity
Metal binding2141Zinc 2; catalytic By similarity
Metal binding2181Zinc 2; catalytic By similarity
Metal binding2241Zinc 2; catalytic By similarity
Metal binding2851Calcium 4; via carbonyl oxygen By similarity
Metal binding3771Calcium 4; via carbonyl oxygen By similarity
Metal binding4261Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation3131N-linked (GlcNAc...) Potential
Disulfide bond278 ↔ 465 By similarity

Experimental info

Sequence conflict2231R → P in AAH88120. Ref.2
Sequence conflict4511D → H in AAH88120. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q63341 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E779B6014EC6FF68

FASTA46553,738
        10         20         30         40         50         60 
MKFLLVLVLL VSLQVSACGA APMNESEFAE WYLSRFFDYQ GDRIPMTKTK TNRNLLEEKL 

        70         80         90        100        110        120 
QEMQQFFGLE VTGQLDTSTL KIMHTSRCGV PDVQHLRAVP QRSRWMKRYL TYRIYNYTPD 

       130        140        150        160        170        180 
MKRADVDYIF QKAFQVWSDV TPLRFRKIHK GEADITILFA FGDHGDFYDF DGKGGTLAHA 

       190        200        210        220        230        240 
FYPGPGIQGD AHFDEAETWT KSFQGTNLFL VAVHELGHSL GLRHSNNPKS IMYPTYRYLH 

       250        260        270        280        290        300 
PNTFRLSADD IHSIQSLYGA PVKNPSLTNP GSPPSTVCHQ SLSFDAVTTV GDKIFFFKDW 

       310        320        330        340        350        360 
FFWWRLPGSP ATNITSISSM WPTIPSGIQA AYEIGGRNQL FLFKDEKYWL INNLVPEPHY 

       370        380        390        400        410        420 
PRSIHSLGFP ASVKKIDAAV FDPLRQKVYF FVDKQYWRYD VRQELMDAAY PKLISTHFPG 

       430        440        450        460 
IRPKIDAVLY FKRHYYIFQG AYQLEYDPLL DRVTKTLSST SWFGC 

« Hide

References

« Hide 'large scale' references
[1]Cossins J., Clements J., Catlin G.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
[2]"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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thymus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98517 mRNA. Translation: CAA67142.1.
BC088120 mRNA. Translation: AAH88120.1.
RefSeqNP_446415.2. NM_053963.2.
UniGeneRn.33193.

3D structure databases

ProteinModelPortalQ63341.
SMRQ63341. Positions 105-465.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ63341.
ChEMBLCHEMBL5506.

Protein family/group databases

MEROPSM10.009.

Proteomic databases

PRIDEQ63341.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID117033.
KEGGrno:117033.
UCSCRGD:620195. rat.

Organism-specific databases

CTD4321.
RGD620195. Mmp12.

Phylogenomic databases

eggNOGNOG323958.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidQ63341.
KOK01413.
PhylomeDBQ63341.
TreeFamTF315428.

Gene expression databases

GenevestigatorQ63341.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. 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.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERPTHR10201:SF32. PTHR10201:SF32. 1 hit.
PfamPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio619817.
PROQ63341.

Entry information

Entry nameMMP12_RAT
AccessionPrimary (citable) accession number: Q63341
Secondary accession number(s): Q5I0P0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries