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O35548 (MMP16_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length607 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. The short isoform efficientlyconverts progelatinase A to the intermediate form but not to the mature one. 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.

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.

Isoform Short: Secretedextracellular spaceextracellular matrix.

Tissue specificity

Strongly expressed in the lung, brain and smooth muscle cells. Weakly detectable in the spleen and liver and indetectable in the heart, skeletal muscle and kidney.

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 repeats.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: O35548-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: O35548-2)

Also known as: MT3-MMP-del;

The sequence of this isoform differs from the canonical sequence as follows:
     547-607: DDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV → P

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Propeptide32 – 11988 By similarity
PRO_0000028816
Chain120 – 607488Matrix metalloproteinase-16
PRO_0000028817

Regions

Topological domain120 – 564445Extracellular Potential
Transmembrane565 – 58521Helical; Potential
Topological domain586 – 60722Cytoplasmic Potential
Repeat340 – 38849Hemopexin 1
Repeat389 – 43446Hemopexin 2
Repeat436 – 48449Hemopexin 3
Repeat485 – 53248Hemopexin 4
Motif99 – 1068Cysteine switch By similarity

Sites

Active site2471 By similarity
Metal binding1011Zinc 1; in inhibited form By similarity
Metal binding1831Calcium 1; via carbonyl oxygen By similarity
Metal binding1931Zinc 1 By similarity
Metal binding1951Zinc 1 By similarity
Metal binding2001Calcium 2 By similarity
Metal binding2011Calcium 2; via carbonyl oxygen By similarity
Metal binding2031Calcium 2; via carbonyl oxygen By similarity
Metal binding2051Calcium 2; via carbonyl oxygen By similarity
Metal binding2151Calcium 1; via carbonyl oxygen By similarity
Metal binding2171Calcium 1; via carbonyl oxygen By similarity
Metal binding2191Calcium 1 By similarity
Metal binding2231Calcium 2 By similarity
Metal binding2261Calcium 2 By similarity
Metal binding2461Zinc 2; catalytic By similarity
Metal binding2501Zinc 2; catalytic By similarity
Metal binding2561Zinc 2; catalytic By similarity

Amino acid modifications

Glycosylation831N-linked (GlcNAc...) Potential
Disulfide bond343 ↔ 532 By similarity

Natural variations

Alternative sequence547 – 60761DDVDI…MQEWV → P in isoform Short.
VSP_005455

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 86BBCF8063441653

FASTA60769,624
        10         20         30         40         50         60 
MILLAFSSGR RLDFVHRSGV FFFQTLLWIL 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 GFHGDRSPFD GEGGFLAHAY FPGPGIGGDT HFDSDEPWTL GNPNHDGNDL 

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

       310        320        330        340        350        360 
RPLPTVPPHR SVPPADPRKN 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

Isoform Short (MT3-MMP-del) [UniParc].

Checksum: 61CE63C123C3B9A5
Show »

FASTA54762,775

References

[1]"Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain."
Shofuda K., Yasumitsu H., Nishihashi A., Miki K., Miyazaki K.
J. Biol. Chem. 272:9749-9754(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
Tissue: Smooth muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D85509 mRNA. Translation: BAA22224.1.
D63886 mRNA. Translation: BAA22223.1.
RefSeqNP_542954.1. NM_080776.1.
UniGeneRn.208361.

3D structure databases

ProteinModelPortalO35548.
SMRO35548. Positions 124-292.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM10.016.

PTM databases

PhosphoSiteO35548.

Proteomic databases

PaxDbO35548.
PRIDEO35548.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID65205.
KEGGrno:65205.
UCSCRGD:620199. rat. [O35548-1]

Organism-specific databases

CTD4325.
RGD620199. Mmp16.

Phylogenomic databases

eggNOGNOG295915.
HOGENOMHOG000217928.
HOVERGENHBG052484.
KOK07996.
PhylomeDBO35548.

Gene expression databases

GenevestigatorO35548.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR028697. MMP16.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021805. Pept_M10A_metallopeptidase_C.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF26. PTHR10201:SF26. 1 hit.
PfamPF11857. DUF3377. 1 hit.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio614169.
PROO35548.

Entry information

Entry nameMMP16_RAT
AccessionPrimary (citable) accession number: O35548
Secondary accession number(s): O35541
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries