Matrix metalloproteinase-14 precursor

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Reviewed, UniProtKB/Swiss-Prot P53690 (MMP14_MOUSE)

Last modified February 9, 2010. Version 95. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Matrix metalloproteinase-14
      Short name=MMP-14
    EC=3.4.24.80
Alternative name(s):
    Membrane-type matrix metalloproteinase 1
      Short name=MT-MMP 1
      Short name=MTMMP1
    Membrane-type-1 matrix metalloproteinase
      Short name=MT1-MMP
      Short name=MT1MMP
    MMP-X1
    MT-MMP

Gene names

Name:	Mmp14
Synonyms:	Mtmmp

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	582 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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General annotation (Comments)

Function	Endopeptidase that degrades various components of the extracellular matrix, such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development. Ref.5
Catalytic activity	Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-\|-Leu-38. Other bonds hydrolyzed include 35-Gly-\|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-\|-Phe-342, 441-Asp-\|-Leu-442 and 354-Gln-\|-Thr-355 in the aggrecan interglobular domain.
Cofactor	Binds 1 zinc ion per subunit By similarity. Calcium By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein; Extracellular side Potential. Melanosome By similarity.
Tissue specificity	Highly expressed in placenta, kidney, heart, lung, embryonic skeletal and periskeletal tissues.
Developmental stage	Not detected before day 10.5. At day 12.5, prominently expressed in large arteries and the umbilical arteries, expressed at lower levels in the myocardium, craniofacial mesenchyme, nasal epithelium and liver capsule. At days 14.5 and 17.5, expressed in the musculoskeletal system, and ossification areas, with continued expression in the arterial tunica media.
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.
Post-translational modification	The precursor is cleaved by a furin endopeptidase By similarity.
Sequence similarities	Belongs to the peptidase M10A family. Contains 4 hemopexin-like domains.

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Ontologies

Keywords
Biological process	Collagen degradation
Cellular component	Membrane
Domain	Repeat Signal Transmembrane
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Zymogen
Gene Ontology (GO)
Biological process	branching morphogenesis of a tube Inferred from mutant phenotype. Source: MGI collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW lung development Inferred from mutant phenotype. Source: MGI proteolysis Inferred from electronic annotation. Source: InterPro zymogen activation Inferred from mutant phenotype. Source: MGI
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell proteinaceous extracellular matrix Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro transcription factor activity Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Potential

Propeptide

21 – 111

By similarity

PRO_0000028800

Chain

112 – 582

471

Matrix metalloproteinase-14

PRO_0000028801

Regions

Topological domain

112 – 541

430

Extracellular Potential

Transmembrane

542 – 562

Potential

Topological domain

563 – 582

Cytoplasmic Potential

Domain

323 – 366

Hemopexin-like 1

Domain

368 – 412

Hemopexin-like 2

Domain

415 – 461

Hemopexin-like 3

Domain

463 – 508

Hemopexin-like 4

Motif

91 – 98

Cysteine switch By similarity

Sites

Active site

240

By similarity

Metal binding

Zinc; in inhibited form By similarity

Metal binding

239

Zinc; catalytic By similarity

Metal binding

243

Zinc; catalytic By similarity

Metal binding

249

Zinc; catalytic By similarity

Amino acid modifications

Disulfide bond

319 ↔ 508

By similarity

Experimental info

Sequence conflict

133

P → S in AAB86602. Ref.3

Sequence conflict

255

A → D in CAA58520. Ref.1

Sequence conflict

258

S → A in AAB86602. Ref.3

Sequence conflict

341

F → L in CAA58520. Ref.1

Sequence conflict

346

N → P in AAB86602. Ref.3

Sequence conflict

378

K → T in CAA58520. Ref.1

Sequence conflict

390 – 391

FD → CV in CAA58520. Ref.1

Sequence conflict

400 – 401

PK → AN in CAA58520. Ref.1

Sequence conflict

407

G → V in CAA58520. Ref.1

Sequence conflict

412

T → S in CAA58520. Ref.1

Sequence conflict

417

A → T in CAA58520. Ref.1

Sequence conflict

512

G → R in AAB51753. Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

P53690-1 [UniParc].

Last modified January 24, 2001. Version 2.
Checksum: 3AB355158D4DD175
Show »

FASTA

582

65,935

        10         20         30         40         50         60 
MSPAPRPSRS LLLPLLTLGT ALASLGWAQG SNFSPEAWLQ QYGYLPPGDL RTHTQRSPQS 

        70         80         90        100        110        120 
LSAAIAAMQK FYGLQVTGKA DLATMMAMRR PRCGVPDKFG TEIKANVRRK RYAIQGLKWQ 

       130        140        150        160        170        180 
HNEITFCIQN YTPKVGEYAT FEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIL 

       190        200        210        220        230        240 
FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVQNEDLNG NDIFLVAVHE 

       250        260        270        280        290        300 
LGHALGLEHS NDPSAIMSPF YQWMDTENFV LPDDDRRGIQ QLYGSKSGSP TKMPPQPRTT 

       310        320        330        340        350        360 
SRPSVPDKPK NPAYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM DGYPMPIGQF 

       370        380        390        400        410        420 
WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP KHIKELGRGL PTDKIDAALF 

       430        440        450        460        470        480 
WMPNGKTYFF RGNKYYRFNE EFRAVDSEYP KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG 

       490        500        510        520        530        540 
NKYWKFNNQK LKVEPGYPKS ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGSGAVSAA 

       550        560        570        580 
AVVLPVLLLL LVLAVGLAVF FFRRHGTPKR LLYCQRSLLD KV

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References

[1]	"Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas." Okada A., Bellocq J.-P., Rouyer N., Chenard M.P., Rio M.C., Chambon P., Basset P. Proc. Natl. Acad. Sci. U.S.A. 92:2730-2734(1995) [PubMed: 7708715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Odaka A. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"The matrix metalloproteinase-14 (MMP-14) gene is structurally distinct from other MMP genes and is co-expressed with the TIMP-2 gene during mouse embryogenesis." Apte S.S., Fukai N., Beier D.R., Olsen B.R. J. Biol. Chem. 272:25511-25517(1997) [PubMed: 9325265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 129/Sv.
[4]	"Cloning of murine membrane-type-1-matrix metalloproteinase (MT-1-MMP) and its metanephric developmental regulation with respect to MMP-2 and its inhibitor." Ota K., Stetler-Stevenson W.G., Yang Q., Kumar A., Wada J., Kashihara N., Wallner E.I., Kanwar Y.S. Kidney Int. 54:131-142(1998) [PubMed: 9648071] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: CD-1. Tissue: Kidney.
[5]	"MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover." Holmbeck K., Bianco P., Caterina J., Yamada S., Kromer M., Kuznetsov S.A., Mankani M., Robey P.G., Poole A.R., Pidoux I., Ward J.M., Birkedal-Hansen H. Cell 99:81-92(1999) [PubMed: 10520996] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	X83536 mRNA. Translation: CAA58520.2. AF022432 AF022431 Genomic DNA. Translation: AAB86602.1. U54984 mRNA. Translation: AAB51753.1.
IPI	IPI00133725.
PIR	I48673.
UniGene	Mm.280175
3D structure databases
SMR	P53690. Positions 114-287, 315-508.
ModBase	Search...
Protein-protein interaction databases
STRING	P53690.
Protein family/group databases
MEROPS	M10.014.
PTM databases
PhosphoSite	P53690.
Proteomic databases
PRIDE	P53690.
Genome annotation databases
Ensembl	ENSMUST00000089688; ENSMUSP00000087119; ENSMUSG00000000957; Mus musculus. [Genome view]
Organism-specific databases
MGI	MGI:101900. Mmp14.
Phylogenomic databases
eggNOG	maNOG06003.
HOGENOM	HBG747685.
HOVERGEN	P53690.
InParanoid	P53690.
Enzyme and pathway databases
BRENDA	3.4.24.80. 244.
Gene expression databases
ArrayExpress	P53690.
Bgee	P53690.
CleanEx	MM_MMP14.
Genevestigator	P53690.
GermOnline	ENSMUSG00000000957. Mus musculus.
Family and domain databases
InterPro	IPR000585. Hemopexin/matrixin. IPR018486. Hemopexin/matrixin_CS. IPR018487. Hemopexin/matrixin_repeat. IPR001818. Pept_M10A_M12B. IPR016293. Pept_M10A_matrix. IPR006026. Peptidase_M. IPR002477. Peptidoglycan-bd-like. [Graphical view]
Gene3D	G3DSA:2.110.10.10. Hemopexin. 1 hit.
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]
PROSITE	PS00546. CYSTEINE_SWITCH. 1 hit. PS00024. HEMOPEXIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

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Entry information

Entry name

MMP14_MOUSE

Accession

Primary (citable) accession number: P53690
Secondary accession number(s): O08645, O35369

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 24, 2001
Last modified:	February 9, 2010
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents