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Matrix metalloproteinase-16 (MMP-16) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 3) (MT-MMP 3) (MTMMP3) (Membrane-type-3 matrix metalloproteinase) (MT3-MMP) (MT3MMP)

 MMP16_RAT               Reviewed;         607 AA.
O35548; O35541;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
05-DEC-2018, entry version 153.
RecName: Full=Matrix metalloproteinase-16;
Short=MMP-16;
EC=3.4.24.-;
AltName: Full=Membrane-type matrix metalloproteinase 3;
Short=MT-MMP 3;
Short=MTMMP3;
AltName: Full=Membrane-type-3 matrix metalloproteinase;
Short=MT3-MMP;
Short=MT3MMP;
Flags: Precursor;
Name=Mmp16;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Smooth muscle;
PubMed=9092507; DOI=10.1074/jbc.272.15.9749;
Shofuda K., Yasumitsu H., Nishihashi A., Miki K., Miyazaki K.;
"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.";
J. Biol. Chem. 272:9749-9754(1997).
-!- 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 efficiently converts
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:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts with CSPG4 through CSPG4 chondroitin sulfate
glycosaminoglycan. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
type I membrane protein {ECO:0000305}; Extracellular side
{ECO:0000305}. Note=Localized at the cell surface of melanoma
cells. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform Short: Secreted, extracellular
space, extracellular matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=O35548-1; Sequence=Displayed;
Name=Short; Synonyms=MT3-MMP-del;
IsoId=O35548-2; Sequence=VSP_005455;
-!- 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.
-!- PTM: The precursor is cleaved by a furin endopeptidase.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D85509; BAA22224.1; -; mRNA.
EMBL; D63886; BAA22223.1; -; mRNA.
RefSeq; NP_542954.1; NM_080776.1. [O35548-2]
UniGene; Rn.208361; -.
ProteinModelPortal; O35548; -.
SMR; O35548; -.
STRING; 10116.ENSRNOP00000040229; -.
MEROPS; M10.016; -.
iPTMnet; O35548; -.
PhosphoSitePlus; O35548; -.
PaxDb; O35548; -.
PRIDE; O35548; -.
GeneID; 65205; -.
KEGG; rno:65205; -.
UCSC; RGD:620199; rat. [O35548-1]
CTD; 4325; -.
RGD; 620199; Mmp16.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
HOGENOM; HOG000217928; -.
HOVERGEN; HBG052484; -.
InParanoid; O35548; -.
KO; K07996; -.
PhylomeDB; O35548; -.
PRO; PR:O35548; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
GO; GO:1990834; P:response to odorant; IEP:RGD.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR028697; MMP16.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR021805; Pept_M10A_metallopeptidase_C.
InterPro; IPR021158; Pept_M10A_Zn_BS.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
PANTHER; PTHR10201:SF26; PTHR10201:SF26; 1.
Pfam; PF11857; DUF3377; 1.
Pfam; PF00045; Hemopexin; 4.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PROSITE; PS00024; HEMOPEXIN; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Alternative splicing; Calcium; Cell membrane;
Cleavage on pair of basic residues; Collagen degradation;
Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein;
Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix; Zinc; Zymogen.
SIGNAL 1 31 {ECO:0000255}.
PROPEP 32 119 {ECO:0000250}.
/FTId=PRO_0000028816.
CHAIN 120 607 Matrix metalloproteinase-16.
/FTId=PRO_0000028817.
TOPO_DOM 120 564 Extracellular. {ECO:0000255}.
TRANSMEM 565 585 Helical. {ECO:0000255}.
TOPO_DOM 586 607 Cytoplasmic. {ECO:0000255}.
REPEAT 340 388 Hemopexin 1.
REPEAT 389 434 Hemopexin 2.
REPEAT 436 484 Hemopexin 3.
REPEAT 485 532 Hemopexin 4.
MOTIF 99 106 Cysteine switch. {ECO:0000250}.
ACT_SITE 247 247 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 101 101 Zinc 1; in inhibited form. {ECO:0000250}.
METAL 183 183 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 193 193 Zinc 1. {ECO:0000250}.
METAL 195 195 Zinc 1. {ECO:0000250}.
METAL 200 200 Calcium 2. {ECO:0000250}.
METAL 201 201 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 203 203 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 205 205 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 215 215 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 217 217 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 219 219 Calcium 1. {ECO:0000250}.
METAL 223 223 Calcium 2. {ECO:0000250}.
METAL 226 226 Calcium 2. {ECO:0000250}.
METAL 246 246 Zinc 2; catalytic. {ECO:0000250}.
METAL 250 250 Zinc 2; catalytic. {ECO:0000250}.
METAL 256 256 Zinc 2; catalytic. {ECO:0000250}.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 343 532 {ECO:0000250}.
VAR_SEQ 547 607 DDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQF
KRKGTPRHILYCKRSMQEWV -> P (in isoform
Short). {ECO:0000305}.
/FTId=VSP_005455.
SEQUENCE 607 AA; 69624 MW; 86BBCF8063441653 CRC64;
MILLAFSSGR RLDFVHRSGV FFFQTLLWIL CATVCGTEQY FNVEVWLQKY GYLPPTDPRM
SVLRSAETMQ SALAAMQQFY GINMTGKVDR NTIDWMKKPR CGVPDQTRGS SKFNIRRKRY
ALTGQKWQHK HITYSIKNVT PKVGDPETRR AIRRAFDVWQ NVTPLTFEEV PYSELENGKR
DVDITIIFAS GFHGDRSPFD GEGGFLAHAY FPGPGIGGDT HFDSDEPWTL GNPNHDGNDL
FLVAVHELGH ALGLEHSNDP TAIMAPFYQY METDNFKLPN DDLQGIQKIY GPPDKIPPPT
RPLPTVPPHR SVPPADPRKN DRPKPPRPPT GRPSYPGAKP NICDGNFNTL AILRREMFVF
KDQWFWRVRN NRVMDGYPMQ ITYFWRGLPP SIDAVYENSD GNFVFFKGNK YWVFKDTTLQ
PGYPHDLITL GNGIPPHGID SAIWWEDVGK TYFFKGDRYW RYSEEMKTMD PGYPKPITIW
KGIPESPQGA FVHKENGFTY FYKGKEYWKF NNQILKVEPG YPRSILKDFM GCDGPTDRDK
EGLSPPDDVD IVIKLDNTAS TVKAIAIVIP CILALCLLVL VYTVFQFKRK GTPRHILYCK
RSMQEWV


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