Macrophage metalloelastase precursor - Rattus norvegicus (Rat)

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Q63341 (MMP12_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 115. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	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.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Domain	Repeat Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of epithelial cell proliferation Inferred from expression pattern PubMed 15802269. Source: RGD proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to drug Inferred from expression pattern PubMed 12783419. Source: RGD
Cellular_component	proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

Probable

Propeptide

22 – 101

Activation peptide By similarity

PRO_0000028782

Chain

102 – 465

364

Macrophage metalloelastase

PRO_0000028783

Regions

Domain

284 – 326

Hemopexin-like 1

Domain

328 – 371

Hemopexin-like 2

Domain

376 – 423

Hemopexin-like 3

Domain

425 – 465

Hemopexin-like 4

Motif

86 – 93

Cysteine switch By similarity

Sites

Active site

215

By similarity

Metal binding

Zinc 2; in inhibited form By similarity

Metal binding

120

Calcium 1 By similarity

Metal binding

154

Calcium 2 By similarity

Metal binding

164

Zinc 1 By similarity

Metal binding

166

Zinc 1 By similarity

Metal binding

171

Calcium 3 By similarity

Metal binding

172

Calcium 3; via carbonyl oxygen By similarity

Metal binding

174

Calcium 3; via carbonyl oxygen By similarity

Metal binding

176

Calcium 3; via carbonyl oxygen By similarity

Metal binding

179

Zinc 1 By similarity

Metal binding

186

Calcium 2; via carbonyl oxygen By similarity

Metal binding

190

Calcium 2 By similarity

Metal binding

192

Zinc 1 By similarity

Metal binding

194

Calcium 3 By similarity

Metal binding

195

Calcium 1 By similarity

Metal binding

197

Calcium 1 By similarity

Metal binding

197

Calcium 3 By similarity

Metal binding

214

Zinc 2; catalytic By similarity

Metal binding

218

Zinc 2; catalytic By similarity

Metal binding

224

Zinc 2; catalytic By similarity

Metal binding

285

Calcium 4; via carbonyl oxygen By similarity

Metal binding

377

Calcium 4; via carbonyl oxygen By similarity

Metal binding

426

Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation

313

N-linked (GlcNAc...) Potential

Disulfide bond

278 ↔ 465

By similarity

Experimental info

Sequence conflict

223

R → P in AAH88120. Ref.2

Sequence conflict

451

D → H in AAH88120. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q63341 [UniParc].

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

465

53,738

        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' referencesShow '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.
IPI	IPI00475653.
RefSeq	NP_446415.2. NM_053963.2.
UniGene	Rn.33193.
3D structure databases
ProteinModelPortal	Q63341.
SMR	Q63341. Positions 105-465.
ModBase	Search...
Protein family/group databases
MEROPS	M10.009.
Proteomic databases
PRIDE	Q63341.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	117033.
KEGG	rno:117033.
UCSC	RGD:620195. rat.
Organism-specific databases
CTD	4321.
RGD	620195. Mmp12.
Phylogenomic databases
eggNOG	NOG323958.
HOGENOM	HOG000217927.
HOVERGEN	HBG052484.
InParanoid	Q63341.
KO	K01413.
Gene expression databases
ArrayExpress	Q63341.
Genevestigator	Q63341.
GermOnline	ENSRNOG00000030187. Rattus norvegicus.
Family and domain databases
Gene3D	2.110.10.10. 1 hit. 3.40.390.10. 1 hit.
InterPro	IPR000585. 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. IPR006026. Peptidase_Metallo. IPR002477. Peptidoglycan-bd-like. [Graphical view]
Pfam	PF00045. Hemopexin. 4 hits. PF00413. Peptidase_M10. 1 hit. PF01471. PG_binding_1. 1 hit. [Graphical view]
PIRSF	PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTS	PR00138. MATRIXIN.
SMART	SM00120. HX. 4 hits. SM00235. ZnMc. 1 hit. [Graphical view]
SUPFAM	SSF50923. Hemopexin. 1 hit. SSF47090. PGBD_like. 1 hit.
PROSITE	PS00546. CYSTEINE_SWITCH. False negative. PS00024. HEMOPEXIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q63341.
ChEMBL	CHEMBL5506.
NextBio	619817.

Entry information

Entry name

MMP12_RAT

Accession

Primary (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:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents