SpermatogenesisOnline 1.0
 

Tag Content
SG ID
SG00001921 
UniProt Accession
Theoretical PI
5.86  
Molecular Weight
66080 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Mmp14 
Gene Synonyms/Alias
Mtmmp 
Protein Name
Matrix metalloproteinase-14 
Protein Synonyms/Alias
MMP-14EC=3.4.24.80 Membrane-type matrix metalloproteinase 1;MT-MMP 1MTMMP1 Membrane-type-1 matrix metalloproteinase;MT-MMPMT1-MMPMT1MMPFlags: Precursor 
Organism
Rattus norvegicus (Rat) 
NCBI Taxonomy ID
10116 
Chromosome Location
chr:15;32493821-32503066;1
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Description
Temporarily unavailable 
The information of related literatures
1. M. L. Slongo, M. Zampieri and M. Onisto (2002) Expression of matrix metalloproteases (MMP-2, MT1 -MMP) and their tissue inhibitor (TIMP-2) by rat sertoli cells in culture. Biol Chem 383(1): 235-9. 

Abstract
During testicular development and maturation, extracellular matrix (ECM) remodelling is a fundamental process which requires the presence of several proteases and protease inhibitors. Among the proteases, a pivotal role has been proposed for matrix metalloproteases (MMPs) and their tissue inhibitors (TIMPs). Here we report an analysis of MMP-2, MT1-MMP and TIMP-2 expression by rat Sertoli cells in culture using RT-PCR and zymographic techniques. Stimulating Sertoli cells with follicle-stimulating hormone (FSH) in vitro induced evident changes in the level of their mRNA in a time-dependent manner. In the case of TIMP-2 and MT1-MMP, the respective transcripts were augmented up to three-fold after 24 h of treatment, and MMP-2 transcripts increased by four times in the same period. MMP-2 activity determined by gelatin zymography showed an increase in enzyme secretion after FSH stimulation. The results of this study suggest that PMID: [11928819] 

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Figures for illustrating the function of this protein/gene
Function
Seems to specifically activate progelatinase A. May thustrigger invasion by tumor cells by activating progelatinase A onthe tumor cell surface. May be involved in actin cytoskeletonreorganization by cleaving PTK7 (By similarity). Acts as apositive regulator of cell growth and migration via activation ofMMP15 (By similarity). 
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Subcellular Location
Membrane; Single-pass type I membraneprotein (Potential). Melanosome (By similarity). Cytoplasm (Bysimilarity). Note=Forms a complex with BST2 and localizes to thecytoplasm (By similarity). 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0005737 C:cytoplasm IDA:RGD.
GO:0031012 C:extracellular matrix IEA:InterPro.
GO:0016021 C:integral to membrane IEA:UniProtKB-KW.
GO:0042470 C:melanosome IEA:UniProtKB-SubCell.
GO:0005509 F:calcium ion binding IEA:InterPro.
GO:0004222 F:metalloendopeptidase activity IEA:InterPro.
GO:0016504 F:peptidase activator activity IMP:RGD.
GO:0003700 F:sequence-specific DNA binding transcription factor activity IEA:Compara.
GO:0008270 F:zinc ion binding IEA:InterPro.
GO:0001525 P:angiogenesis IEP:RGD.
GO:0043615 P:astrocyte cell migration IEP:RGD.
GO:0048754 P:branching morphogenesis of a tube IEA:Compara.
GO:0001935 P:endothelial cell proliferation IEP:RGD.
GO:0030324 P:lung development IEA:Compara.
GO:0051895 P:negative regulation of focal adhesion assembly IDA:RGD.
GO:0001503 P:ossification IEP:RGD.
GO:0001541 P:ovarian follicle development IEP:RGD.
GO:0006508 P:proteolysis IEA:UniProtKB-KW.
GO:0043627 P:response to estrogen stimulus IEP:RGD.
GO:0001666 P:response to hypoxia IEP:RGD.
GO:0009612 P:response to mechanical stimulus IEP:RGD.
GO:0014070 P:response to organic cyclic compound IEP:RGD.
GO:0006979 P:response to oxidative stress IEP:RGD.
GO:0048771 P:tissue remodeling IDA:RGD.
GO:0031638 P:zymogen activation IEA:Compara.
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Interpro
IPR000585;    Hemopexin/matrixin.
IPR018486;    Hemopexin/matrixin_CS.
IPR018487;    Hemopexin/matrixin_repeat.
IPR024079;    MetalloPept_cat_dom.
IPR001818;    Pept_M10_metallopeptidase.
IPR016293;    Pept_M10A_matrix_strom.
IPR021190;    Pept_M10A_matrixin.
IPR021805;    Pept_M10A_metallopeptidase_C.
IPR021158;    Pept_M10A_Zn_BS.
IPR006026;    Peptidase_Metallo.
IPR002477;    Peptidoglycan-bd-like.
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Pfam
PF11857;    DUF3377;    1.
PF00045;    Hemopexin;    4.
PF00413;    Peptidase_M10;    1.
PF01471;    PG_binding_1;    1.
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SMART
SM00120;    HX;    4.
SM00235;    ZnMc;    1.
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PROSITE
PS00546;    CYSTEINE_SWITCH;    1.
PS00024;    HEMOPEXIN;    1.
PS00142;    ZINC_PROTEASE;    1.
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PRINTS
PR00138;    MATRIXIN.;   
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Created Date
18-Oct-2012 
Record Type
Experiment identified 
Protein sequence Annotation
SIGNAL        1     20       Potential.
PROPEP       21    111       Activation peptide.
                             /FTId=PRO_0000028806.
CHAIN       112    582       Matrix metalloproteinase-14.
                             /FTId=PRO_0000028807.
TOPO_DOM    112    541       Extracellular (Potential).
TRANSMEM    542    562       Helical; (Potential).
TOPO_DOM    563    582       Cytoplasmic (Potential).
DOMAIN      323    366       Hemopexin-like 1.
DOMAIN      368    412       Hemopexin-like 2.
DOMAIN      415    461       Hemopexin-like 3.
DOMAIN      463    508       Hemopexin-like 4.
MOTIF        91     98       Cysteine switch (By similarity).
ACT_SITE    240    240       By similarity.
METAL        93     93       Zinc; in inhibited form (By similarity).
METAL       239    239       Zinc; catalytic (By similarity).
METAL       243    243       Zinc; catalytic (By similarity).
METAL       249    249       Zinc; catalytic (By similarity).
DISULFID    319    508       By similarity.
CONFLICT     68     68       M -> I (in Ref. 1; CAA58521).
CONFLICT    255    255       A -> D (in Ref. 1; CAA58521).
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Nucleotide Sequence
Length: 2412 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 582 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
Other Protein-Protein interaction resources
String database  
View Microarray data
Temporarily unavailable 
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