Matrix metalloproteinase-16 precursor

Contribute

Send feedback

Read comments (?) or add your own

Q9WTR0 (MMP16_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 119. History...

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

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

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

Names and origin

Protein names

Recommended name:
Matrix metalloproteinase-16
Short name=MMP-16
EC=3.4.24.-

Alternative name(s):
Membrane-type matrix metalloproteinase 3
Short name=MT-MMP 3
Short name=MTMMP3
Membrane-type-3 matrix metalloproteinase
Short name=MT3-MMP
Short name=MT3MMP

Gene names

Name:

Mmp16

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	607 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	Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells By similarity.
Cofactor	Binds 1 zinc ion per subunit By similarity. Calcium By similarity.
Subunit structure	Interacts with CSPG4 through CSPG4 chondroitin sulfate glycosaminoglycan By similarity.
Subcellular location	Cell membrane; Single-pass type I membrane protein; Extracellular side Potential. Note: Localized at the cell surface of melanoma cells 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.
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
Biological process	Collagen degradation
Cellular component	Cell membrane Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular matrix Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane 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 – 31

Potential

Propeptide

32 – 119

By similarity

PRO_0000028814

Chain

120 – 607

488

Matrix metalloproteinase-16

PRO_0000028815

Regions

Topological domain

120 – 564

445

Extracellular Potential

Transmembrane

565 – 585

Helical; Potential

Topological domain

586 – 607

Cytoplasmic Potential

Domain

347 – 390

Hemopexin-like 1

Domain

392 – 436

Hemopexin-like 2

Domain

439 – 485

Hemopexin-like 3

Domain

487 – 532

Hemopexin-like 4

Motif

99 – 106

Cysteine switch By similarity

Sites

Active site

247

By similarity

Metal binding

101

Zinc 1; in inhibited form By similarity

Metal binding

183

Calcium 1; via carbonyl oxygen By similarity

Metal binding

193

Zinc 1 By similarity

Metal binding

195

Zinc 1 By similarity

Metal binding

200

Calcium 2 By similarity

Metal binding

201

Calcium 2; via carbonyl oxygen By similarity

Metal binding

203

Calcium 2; via carbonyl oxygen By similarity

Metal binding

205

Calcium 2; via carbonyl oxygen By similarity

Metal binding

215

Calcium 1; via carbonyl oxygen By similarity

Metal binding

217

Calcium 1; via carbonyl oxygen By similarity

Metal binding

219

Calcium 1 By similarity

Metal binding

223

Calcium 2 By similarity

Metal binding

226

Calcium 2 By similarity

Metal binding

246

Zinc 2; catalytic By similarity

Metal binding

250

Zinc 2; catalytic By similarity

Metal binding

256

Zinc 2; catalytic By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Disulfide bond

343 ↔ 532

By similarity

Experimental info

Sequence conflict

R → H in BAA78420. Ref.1

Sequence conflict

G → V in AAG17704. Ref.2

Sequence conflict

196

S → R in AAG17704. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q9WTR0 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: C4CB54F75B26A296
Show »

FASTA

607

69,571

        10         20         30         40         50         60 
MILLAFSSGR RLDFVHRSGV FFLQTLLWIL CATVCGTEQY FNVEVWLQKY GYLPPTDPRM 

        70         80         90        100        110        120 
SVLRSAETMQ SALAAMQQFY GINMTGKVDR NTIDWMKKPR CGVPDQTRGS SKFNIRRKRY 

       130        140        150        160        170        180 
ALTGQKWQHK HITYSIKNVT PKVGDPETRR AIRRAFDVWQ NVTPLTFEEV PYSELENGKR 

       190        200        210        220        230        240 
DVDITIIFAS GFHGDSSPFD GEGGFLAHAY FPGPGIGGDT HFDSDEPWTL GNPNHDGNDL 

       250        260        270        280        290        300 
FLVAVHELGH ALGLEHSNDP TAIMAPFYQY METDNFKLPN DDLQGIQKIY GPPDKIPPPT 

       310        320        330        340        350        360 
RPLPTVPPHR SVPPADPRRH DRPKPPRPPT GRPSYPGAKP NICDGNFNTL AILRREMFVF 

       370        380        390        400        410        420 
KDQWFWRVRN NRVMDGYPMQ ITYFWRGLPP SIDAVYENSD GNFVFFKGNK YWVFKDTTLQ 

       430        440        450        460        470        480 
PGYPHDLITL GNGIPPHGID SAIWWEDVGK TYFFKGDRYW RYSEEMKTMD PGYPKPITIW 

       490        500        510        520        530        540 
KGIPESPQGA FVHKENGFTY FYKGKEYWKF NNQILKVEPG YPRSILKDFM GCDGPTDRDK 

       550        560        570        580        590        600 
EGLSPPDDVD IVIKLDNTAS TVKAIAIVIP CILALCLLVL VYTVFQFKRK GTPRHILYCK 


RSMQEWV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Seiki M., Kinoh H. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Differential localization and Triton X-100 solubility of membrane-type matrix metalloproteinases 1-3." Budde P., Gatsios P., Nienaber N.T., Li H., Staege M.S., Graeve L., Heinrich P.C., Frey J. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6. Tissue: Brain.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-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: 129. Tissue: Mammary tumor.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB021228 mRNA. Translation: BAA78420.1. AF282844 mRNA. Translation: AAG17704.1. AL683877, AL805957 Genomic DNA. Translation: CAM13981.1. AL805957, AL683877 Genomic DNA. Translation: CAM18851.1. CH466538 Genomic DNA. Translation: EDL05585.1. CH466538 Genomic DNA. Translation: EDL05587.1. BC057926 mRNA. Translation: AAH57926.1.
IPI	IPI00322697.
RefSeq	NP_062698.2. NM_019724.3.
UniGene	Mm.187315.
3D structure databases
ProteinModelPortal	Q9WTR0.
SMR	Q9WTR0. Positions 85-561.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000029881.
Protein family/group databases
MEROPS	M10.016.
PTM databases
PhosphoSite	Q9WTR0.
Proteomic databases
PRIDE	Q9WTR0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000029881; ENSMUSP00000029881; ENSMUSG00000028226.
GeneID	17389.
KEGG	mmu:17389.
Organism-specific databases
CTD	4325.
MGI	MGI:1276107. Mmp16.
Phylogenomic databases
eggNOG	NOG295915.
GeneTree	ENSGT00700000104046.
HOGENOM	HOG000217928.
HOVERGEN	HBG052484.
InParanoid	Q6PEQ6.
KO	K07996.
OMA	GPTDRDK.
OrthoDB	EOG4R5029.
Gene expression databases
ArrayExpress	Q9WTR0.
Bgee	Q9WTR0.
CleanEx	MM_MMP16.
Genevestigator	Q9WTR0.
GermOnline	ENSMUSG00000028226. 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. IPR018486. Hemopexin_CS. IPR024079. MetalloPept_cat_dom. IPR001818. Pept_M10_metallopeptidase. IPR021190. Pept_M10A. IPR021805. Pept_M10A_metallopeptidase_C. IPR016293. Pept_M10A_Metazoans. IPR021158. Pept_M10A_Zn_BS. IPR006026. Peptidase_Metallo. IPR002477. Peptidoglycan-bd-like. [Graphical view]
Pfam	PF11857. DUF3377. 1 hit. 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. 1 hit. PS00024. HEMOPEXIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MMP16. mouse.
NextBio	292008.
SOURCE	Search...

Entry information

Entry name

MMP16_MOUSE

Accession

Primary (citable) accession number: Q9WTR0
Secondary accession number(s): Q6PEQ6, Q9ERT6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 119 of the entry and version 3 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

MGD cross-references

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

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-protein interaction databases

Protein family/group databases

PTM 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