Q9R0S3 (MMP17_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Matrix metalloproteinase-17
Short name=MMP-17
EC=3.4.24.-

Alternative name(s):
Membrane-type matrix metalloproteinase 4
Short name=MT-MMP 4
Short name=MTMMP4
Membrane-type-4 matrix metalloproteinase
Short name=MT4-MMP
Short name=MT4MMP

Gene names

Name:	Mmp17
Synonyms:	Mt4mmp

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	578 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin. Ref.3
Catalytic activity	Cleaves pro-TNF-alpha at the 74-Ala-|-Gln-75 site.
Cofactor	Binds 1 zinc ion per subunit By similarity. Calcium By similarity.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor; Extracellular side. Secreted › extracellular space › extracellular matrix Ref.6.
Tissue specificity	Expressed by monocytes and macrophages.
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.

Ontologies

Keywords
Cellular component	Cell membrane Extracellular matrix Membrane Secreted
Domain	Repeat Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond GPI-anchor Glycoprotein Lipoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell 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 – 39	39	Potential
	Propeptide	40 – 124	85	By similarity		PRO_0000028821
	Chain	125 – 558	434	Matrix metalloproteinase-17		PRO_0000028822
	Propeptide	559 – 578	20	Removed in mature form Potential		PRO_0000028823
Regions
	Domain	340 – 384	45	Hemopexin-like 1
	Domain	389 – 432	44	Hemopexin-like 2
	Domain	435 – 481	47	Hemopexin-like 3
	Domain	483 – 527	45	Hemopexin-like 4
	Motif	107 – 114	8	Cysteine switch By similarity
Sites
	Active site	248	1
	Metal binding	109	1	Zinc; in inhibited form By similarity
	Metal binding	247	1	Zinc; catalytic By similarity
	Metal binding	251	1	Zinc; catalytic By similarity
	Metal binding	257	1	Zinc; catalytic By similarity
Amino acid modifications
	Lipidation	558	1	GPI-anchor amidated serine Potential
	Glycosylation	136	1	N-linked (GlcNAc...) Potential
	Glycosylation	322	1	N-linked (GlcNAc...) Potential
	Disulfide bond	336 ↔ 527		By similarity
Experimental info
	Mutagenesis	248	1	E → A: Loss of activity. Ref.6
	Sequence conflict	45	1	A → G in CAB92315. Ref.3
	Sequence conflict	277	1	L → V in BAA82708. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9R0S3 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 168C933B63A1EB7B	FASTA	578	64,333
	10 20 30 40 50 60 MGRRPRGPGS PRGPGPPRPG PGLPPLLLVL ALAAHGGCAA PAPRAEDLSL GVEWLSRFGY 70 80 90 100 110 120 LPPADPASGQ LQTQEELSKA ITAMQQFGGL ETTGILDEAT LALMKTPRCS LPDLPPGAQS 130 140 150 160 170 180 RRKRQTPPPT KWSKRNLSWR VRTFPRDSPL GRDTVRALMY YALKVWSDIT PLNFHEVAGN 190 200 210 220 230 240 AADIQIDFSK ADHNDGYPFD GPGGTVAHAF FPGDHHTAGD THFDDDEPWT FRSSDAHGMD 250 260 270 280 290 300 LFAVAVHEFG HAIGLSHVAA PSSIMQPYYQ GPVGDPLRYG LPYEDRVRVW QLYGVRESVS 310 320 330 340 350 360 PTAQLDTPEP EEPPLLPEPP NNRSSTPPQK DVPHRCTAHF DAVAQIRGEA FFFKGKYFWR 370 380 390 400 410 420 LTRDRHLVSL QPAQMHRFWR GLPLHLDSVD AVYERTSDHK IVFFKGDRYW VFKDNNVEEG 430 440 450 460 470 480 YPRPVSDFSL PPGGIDAVFS WAHNDRTYFF KDQLYWRYDD HTRRMDPGYP AQGPLWRGVP 490 500 510 520 530 540 SMLDDAMRWS DGASYFFRGQ EYWKVLDGEL EAAPGYPQST ARDWLVCGEP LADAEDVGPG 550 560 570 PQGRSGAQDG LAVCSCTSDA HRLALPSLLL LTPLLWGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human membrane type-4 matrix metalloproteinase (MT4-MMP) is encoded by a novel major transcript: isolation of complementary DNA clones for human and mouse mt4-mmp transcripts." Kajita M., Kinoh H., Ito N., Takamura A., Itoh Y., Okada A., Sato H., Seiki M. FEBS Lett. 457:353-356(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Embryonic brain.
[2]	Seiki M. Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO C-TERMINUS.
[3]	"Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha convertase activity but does not activate pro-MMP2." English W.R., Puente X.S., Freije J.M.P., Knaeuper V., Amour A., Merryweather A., Lopez-Otin C., Murphy G. J. Biol. Chem. 275:14046-14055(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Tissue: Brain.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: C57BL/6. Tissue: Embryonic brain.
[6]	"Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase." Itoh Y., Kajita M., Kinoh H., Mori H., Okada A., Seiki M. J. Biol. Chem. 274:34260-34266(1999) [PubMed] [Europe PMC] [Abstract] Cited for: GPI-ANCHOR, MUTAGENESIS OF GLU-248.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB021224 mRNA. Translation: BAA82708.2. AJ010731 mRNA. Translation: CAB92315.1. CH466529 Genomic DNA. Translation: EDL19513.1. BC051917 mRNA. Translation: AAH51917.1.
IPI	IPI00330325.
RefSeq	NP_035976.3. NM_011846.4.
UniGene	Mm.42047.
3D structure databases
ProteinModelPortal	Q9R0S3.
SMR	Q9R0S3. Positions 47-559.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000031390.
Protein family/group databases
MEROPS	M10.017.
PTM databases
PhosphoSite	Q9R0S3.
2D gel databases
REPRODUCTION-2DPAGE	Q9R0S3.
Proteomic databases
PaxDb	Q9R0S3.
PRIDE	Q9R0S3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000031390; ENSMUSP00000031390; ENSMUSG00000029436.
GeneID	23948.
KEGG	mmu:23948.
Organism-specific databases
CTD	4326.
MGI	MGI:1346076. Mmp17.
Phylogenomic databases
eggNOG	NOG295915.
GeneTree	ENSGT00700000104196.
HOGENOM	HOG000217928.
HOVERGEN	HBG052484.
InParanoid	Q80UM9.
KO	K07997.
OMA	WRGLPLH.
OrthoDB	EOG40VVPC.
Gene expression databases
Bgee	Q9R0S3.
CleanEx	MM_MMP17.
Genevestigator	Q9R0S3.
GermOnline	ENSMUSG00000029436. Mus musculus.
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. 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. False negative. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	303765.
SOURCE	Search...

Entry information

Entry name

MMP17_MOUSE

Accession

Primary (citable) accession number: Q9R0S3
Secondary accession number(s): Q80UM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 116 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program