Reviewed, UniProtKB/Swiss-Prot Q10739 (MMP14_RAT)

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
      Short name=MT-MMP

Gene names

Name:	Mmp14
Synonyms:	Mtmmp

Organism

Rattus norvegicus (Rat)

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	582 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	Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface.
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 Potential. Melanosome 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	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	angiogenesis Inferred from expression pattern. Source: RGD astrocyte cell migration Inferred from expression pattern. Source: RGD endothelial cell proliferation Inferred from expression pattern. Source: RGD negative regulation of focal adhesion formation Inferred from direct assay. Source: RGD ossification Inferred from expression pattern. Source: RGD ovarian follicle development Inferred from expression pattern. Source: RGD proteolysis Inferred from electronic annotation. Source: InterPro response to estrogen stimulus Inferred from expression pattern. Source: RGD response to hypoxia Inferred from expression pattern. Source: RGD response to mechanical stimulus Inferred from expression pattern. Source: RGD response to oxidative stress Inferred from expression pattern. Source: RGD tissue remodeling Inferred from direct assay. Source: RGD
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 peptidase activator activity Inferred from mutant phenotype. Source: RGD zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Propeptide	21 – 111	91	Activation peptide		PRO_0000028806
	Chain	112 – 582	471	Matrix metalloproteinase-14		PRO_0000028807
Regions
	Topological domain	112 – 541	430	Extracellular Potential
	Transmembrane	542 – 562	21	Potential
	Topological domain	563 – 582	20	Cytoplasmic Potential
	Domain	323 – 366	44	Hemopexin-like 1
	Domain	368 – 412	45	Hemopexin-like 2
	Domain	415 – 461	47	Hemopexin-like 3
	Domain	463 – 508	46	Hemopexin-like 4
	Motif	91 – 98	8	Cysteine switch By similarity
Sites
	Active site	240	1	By similarity
	Metal binding	93	1	Zinc; in inhibited form By similarity
	Metal binding	239	1	Zinc; catalytic By similarity
	Metal binding	243	1	Zinc; catalytic By similarity
	Metal binding	249	1	Zinc; catalytic By similarity
Amino acid modifications
	Disulfide bond	319 ↔ 508		By similarity
Experimental info
	Sequence conflict	68	1	M → I in CAA58521. Ref.1
	Sequence conflict	255	1	A → D in CAA58521. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q10739-1 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 48F1A8E3065E1AE8	FASTA	582	66,080
	10 20 30 40 50 60 MSPAPRPSRS LLLPLLTLGT TLASLGWAQS SNFSPEAWLQ QYGYLPPGDL RTHTQRSPQS 70 80 90 100 110 120 LSAAIAAMQR FYGLQVTGKA DSDTMKAMRR 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 NDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGSKSGSP TKMPPQPRTT 310 320 330 340 350 360 SRPSVPDKPR NPTYGPNICD 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

References

	« Hide 'large scale' referencesShow 'large scale' 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]	"Expression and function of MT-MMP in glial cells." Cossins J., Clements J., Catlin G., Wells G. Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X83537 mRNA. Translation: CAA58521.1. X91785 mRNA. Translation: CAA62897.1. BC072509 mRNA. Translation: AAH72509.1.
IPI	IPI00327562.
PIR	I84471.
RefSeq	NP_112318.1.
UniGene	Rn.10371
3D structure databases
HSSP	HSSP built from PDB template 1BQQ based on UniProtKB P50281.
SMR	Q10739. Positions 114-287.
ModBase	Search...
Protein-protein interaction databases
STRING	Q10739.
Protein family/group databases
MEROPS	M10.014.
PTM databases
PhosphoSite	Q10739.
Genome annotation databases
Ensembl	ENSRNOT00000015101; ENSRNOP00000015101; ENSRNOG00000010947; Rattus norvegicus. [Genome view] ENSRNOT00000042938; ENSRNOP00000049168; ENSRNOG00000010947; Rattus norvegicus. [Genome view]
GeneID	81707.
KEGG	rno:81707.
UCSC	NM_031056. rat.
Organism-specific databases
CTD	81707.
RGD	620198. Mmp14.
Phylogenomic databases
HOVERGEN	Q10739.
Enzyme and pathway databases
BRENDA	3.4.24.80. 248.
Gene expression databases
ArrayExpress	Q10739.
Genevestigator	Q10739.
GermOnline	ENSRNOG00000010947. Rattus norvegicus.
Family and domain databases
InterPro	IPR000585. Hemopexin/matrixin. IPR018486. Hemopexin/matrixin_CS. IPR018487. Hemopexin/matrixin_repeat. IPR001818. Pept_M10A_M12B. IPR016293. Pept_M10A_matrix. IPR006025. Pept_M_Zn_BS. 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
NextBio	615328.

Entry information

Entry name

MMP14_RAT

Accession

Primary (citable) accession number: Q10739
Secondary accession number(s): Q6IN06

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 1, 2007
Last modified:	October 13, 2009
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)