Skip Header

Contribute Send feedback
Read comments (?) or add your own

P34960 (MMP12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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:Mme, Mmel
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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

Secreted › extracellular space › extracellular 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-like domains.

Sequence caution

The sequence AAA39526.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC40889.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Probable
Propeptide29 – 10981Activation peptide
PRO_0000028778
Chain110 – 473364Macrophage metalloelastase
PRO_0000028779

Regions

Domain292 – 33443Hemopexin-like 1
Domain336 – 37944Hemopexin-like 2
Domain384 – 43148Hemopexin-like 3
Domain433 – 47341Hemopexin-like 4
Motif94 – 1018Cysteine switch By similarity

Sites

Active site2231 By similarity
Metal binding961Zinc 2; in inhibited form By similarity
Metal binding1281Calcium 1 By similarity
Metal binding1621Calcium 2 By similarity
Metal binding1721Zinc 1 By similarity
Metal binding1741Zinc 1 By similarity
Metal binding1791Calcium 3 By similarity
Metal binding1801Calcium 3; via carbonyl oxygen By similarity
Metal binding1821Calcium 3; via carbonyl oxygen By similarity
Metal binding1841Calcium 3; via carbonyl oxygen By similarity
Metal binding1871Zinc 1 By similarity
Metal binding1941Calcium 2; via carbonyl oxygen By similarity
Metal binding1981Calcium 2 By similarity
Metal binding2001Zinc 1 By similarity
Metal binding2021Calcium 3 By similarity
Metal binding2031Calcium 1 By similarity
Metal binding2051Calcium 1 By similarity
Metal binding2051Calcium 3 By similarity
Metal binding2221Zinc 2; catalytic By similarity
Metal binding2261Zinc 2; catalytic By similarity
Metal binding2321Zinc 2; catalytic By similarity
Metal binding2931Calcium 4; via carbonyl oxygen By similarity
Metal binding3851Calcium 4; via carbonyl oxygen By similarity
Metal binding4341Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation321N-linked (GlcNAc...) Potential
Glycosylation851N-linked (GlcNAc...) Potential
Glycosylation3211N-linked (GlcNAc...) Potential
Disulfide bond286 ↔ 473 By similarity

Experimental info

Sequence conflict651K → E in AAH19135. Ref.3
Sequence conflict651K → E in CAJ18584. Ref.4
Sequence conflict781E → V in BAE30809. Ref.2
Sequence conflict781E → V in BAE30260. Ref.2
Sequence conflict781E → V in BAE30039. Ref.2
Sequence conflict781E → V in BAE29689. Ref.2
Sequence conflict801T → N in BAE33415. Ref.2
Sequence conflict871T → A in BAE42486. Ref.2
Sequence conflict1721H → N in BAE42198. Ref.2
Sequence conflict1881A → V in AAA39526. Ref.1
Sequence conflict1991A → T in BAC40836. Ref.2
Sequence conflict2411Y → D in AAH19135. Ref.3
Sequence conflict2411Y → D in CAJ18584. Ref.4
Sequence conflict2471L → F in BAE33072. Ref.2
Sequence conflict2501S → N in AAH19135. Ref.3
Sequence conflict2501S → N in CAJ18584. Ref.4
Sequence conflict2681A → P in BAC40846. Ref.2
Sequence conflict2721P → T in AAH19135. Ref.3
Sequence conflict2721P → T in CAJ18584. Ref.4
Sequence conflict3031F → L in AAA39526. Ref.1
Sequence conflict3031F → Y in BAC40889. Ref.2
Sequence conflict3031F → Y in BAC40913. Ref.2
Sequence conflict3191A → D in BAE33415. Ref.2
Sequence conflict3231T → I in AAH19135. Ref.3
Sequence conflict3231T → I in CAJ18584. Ref.4
Sequence conflict3281I → T in BAE41743. Ref.2
Sequence conflict3351G → A in AAA39526. Ref.1
Sequence conflict4031H → Q in AAH19135. Ref.3
Sequence conflict4031H → Q in CAJ18584. Ref.4
Sequence conflict4321K → R in BAC40836. Ref.2
Sequence conflict4671S → G in BAE42201. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P34960 [UniParc].

Last modified July 10, 2007. Version 3.
Checksum: D377250610BA249E

FASTA47354,971
        10         20         30         40         50         60 
MSCTLLKGVC TMKFLMMIVF LQVSACGAAP MNDSEFAEWY LSRFYDYGKD RIPMTKTKTN 

        70         80         90        100        110        120 
RNFLKEKLQE MQQFFGLEAT GQLDNSTLAI MHIPRCGVPD VQHLRAVPQR SRWMKRYLTY 

       130        140        150        160        170        180 
RIYNYTPDMK REDVDYIFQK AFQVWSDVTP LRFRKLHKDE ADIMILFAFG AHGDFNYFDG 

       190        200        210        220        230        240 
KGGTLAHAFY PGPGIQGDAH FDEAETWTKS FQGTNLFLVA VHELGHSLGL QHSNNPKSIM 

       250        260        270        280        290        300 
YPTYRYLNPS TFRLSADDIR NIQSLYGAPV KPPSLTKPSS PPSTFCHQSL SFDAVTTVGE 

       310        320        330        340        350        360 
KIFFFKDWFF WWKLPGSPAT NITSISSIWP SIPSGIQAAY EIESRNQLFL FKDEKYWLIN 

       370        380        390        400        410        420 
NLVPEPHYPR SIYSLGFSAS VKKVDAAVFD PLRQKVYFFV DKHYWRYDVR QELMDPAYPK 

       430        440        450        460        470 
LISTHFPGIK PKIDAVLYFK RHYYIFQGAY QLEYDPLFRR VTKTLKSTSW FGC

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, chromosomal localization, and bacterial expression of a murine macrophage metalloelastase."
Shapiro S.D., Griffin G.L., Gilbert D.J., Jenkins N.A., Copeland N.G., Welgus H.G., Senior R.M., Ley T.J.
J. Biol. Chem. 267:4664-4671(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 110-136.
Tissue: Macrophage.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: BALB/c, C57BL/6J and NOD.
Tissue: B-cell, Dendritic cell and Macrophage.
[3]"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].
Strain: Czech II.
Tissue: Mammary gland.
[4]"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-473.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M82831 mRNA. Translation: AAA39526.1. Different initiation.
AK089309 mRNA. Translation: BAC40836.1.
AK089335 mRNA. Translation: BAC40846.1.
AK089452 mRNA. Translation: BAC40889.1. Different initiation.
AK089523 mRNA. Translation: BAC40913.1.
AK090051 mRNA. Translation: BAC41067.1.
AK150596 mRNA. Translation: BAE29689.1.
AK151021 mRNA. Translation: BAE30039.1.
AK151273 mRNA. Translation: BAE30260.1.
AK151933 mRNA. Translation: BAE30809.1.
AK155139 mRNA. Translation: BAE33072.1.
AK155743 mRNA. Translation: BAE33411.1.
AK155747 mRNA. Translation: BAE33414.1.
AK155748 mRNA. Translation: BAE33415.1.
AK155865 mRNA. Translation: BAE33469.1.
AK170360 mRNA. Translation: BAE41743.1.
AK170364 mRNA. Translation: BAE41746.1.
AK170798 mRNA. Translation: BAE42035.1.
AK170804 mRNA. Translation: BAE42039.1.
AK170976 mRNA. Translation: BAE42154.1.
AK171006 mRNA. Translation: BAE42177.1.
AK171032 mRNA. Translation: BAE42198.1.
AK171036 mRNA. Translation: BAE42201.1.
AK171176 mRNA. Translation: BAE42294.1.
AK171428 mRNA. Translation: BAE42446.1.
AK171447 mRNA. Translation: BAE42457.1.
AK171448 mRNA. Translation: BAE42458.1.
AK171449 mRNA. Translation: BAE42459.1.
AK171450 mRNA. Translation: BAE42460.1.
AK171466 mRNA. Translation: BAE42472.1.
AK171468 mRNA. Translation: BAE42474.1.
AK171470 mRNA. Translation: BAE42476.1.
AK171472 mRNA. Translation: BAE42478.1.
AK171485 mRNA. Translation: BAE42486.1.
AK171518 mRNA. Translation: BAE42502.1.
AK171542 mRNA. Translation: BAE42516.1.
AK171570 mRNA. Translation: BAE42531.1.
BC019135 mRNA. Translation: AAH19135.2.
CT010377 mRNA. Translation: CAJ18584.1.
IPIIPI00321648.
PIRA42401.
RefSeqNP_032631.3. NM_008605.3.
UniGeneMm.2055.

3D structure databases

ProteinModelPortalP34960.
SMRP34960. Positions 40-473.
ModBaseSearch...

Protein family/group databases

MEROPSM10.009.

PTM databases

PhosphoSiteP34960.

Proteomic databases

PRIDEP34960.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005950; ENSMUSP00000005950; ENSMUSG00000049723.
GeneID17381.
KEGGmmu:17381.
UCSCuc009och.1. mouse.

Organism-specific databases

CTD4321.
MGIMGI:97005. Mmp12.

Phylogenomic databases

eggNOGNOG323958.
GeneTreeENSGT00630000089491.
HOVERGENHBG052484.
InParanoidP34960.
KOK01413.
OMAPKLISTH.
OrthoDBEOG4TXBRN.

Gene expression databases

ArrayExpressP34960.
BgeeP34960.
CleanExMM_MME.
MM_MMP12.
GenevestigatorP34960.
GermOnlineENSMUSG00000049723. Mus musculus.

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.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_Metazoans.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
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]
SUPFAMSSF50923. Hemopexin. 1 hit.
SSF47090. PGBD_like. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP34960.
ChEMBLCHEMBL2594.
NextBio291984.
SOURCESearch...

Entry information

Entry nameMMP12_MOUSE
AccessionPrimary (citable) accession number: P34960
Secondary accession number(s): Q3TB28 expand/collapse secondary AC list , Q3TBV6, Q3TBV9, Q3TD61, Q3U1S8, Q3U1S9, Q3U2R8, Q3UBC5, Q4FJM7, Q8BJ92, Q8BJB3, Q8BJB6, Q8BJB8, Q8BJB9, Q8VED6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: July 10, 2007
Last modified: May 29, 2013
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents