Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q10739

- MMP14_RAT

UniProt

Q10739 - MMP14_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Matrix metalloproteinase-14

Gene

Mmp14

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7 (By similarity). Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues (By similarity).By similarity

Catalytic activityi

Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.

Cofactori

Binds 1 zinc ion per subunit.By similarity
Calcium.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi93 – 931Zinc; in inhibited formBy similarity
Metal bindingi239 – 2391Zinc; catalyticPROSITE-ProRule annotation
Active sitei240 – 2401PROSITE-ProRule annotation
Metal bindingi243 – 2431Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi249 – 2491Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. integrin binding Source: RGD
  3. metalloendopeptidase activity Source: InterPro
  4. peptidase activator activity Source: RGD
  5. sequence-specific DNA binding transcription factor activity Source: Ensembl
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. angiogenesis Source: RGD
  2. astrocyte cell migration Source: RGD
  3. branching morphogenesis of an epithelial tube Source: Ensembl
  4. chondrocyte proliferation Source: Ensembl
  5. collagen catabolic process Source: Ensembl
  6. craniofacial suture morphogenesis Source: Ensembl
  7. embryonic cranial skeleton morphogenesis Source: Ensembl
  8. endochondral ossification Source: Ensembl
  9. endothelial cell proliferation Source: RGD
  10. lung development Source: Ensembl
  11. male gonad development Source: RGD
  12. negative regulation of focal adhesion assembly Source: RGD
  13. ossification Source: RGD
  14. ovarian follicle development Source: RGD
  15. positive regulation of cell growth Source: Ensembl
  16. positive regulation of cell migration Source: Ensembl
  17. positive regulation of peptidase activity Source: GOC
  18. response to estrogen Source: RGD
  19. response to hormone Source: RGD
  20. response to hypoxia Source: RGD
  21. response to mechanical stimulus Source: RGD
  22. response to organic cyclic compound Source: RGD
  23. response to oxidative stress Source: RGD
  24. tissue remodeling Source: RGD
  25. zymogen activation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_198590. Activation of Matrix Metalloproteinases.
REACT_199177. Collagen degradation.
REACT_199178. Degradation of the extracellular matrix.

Protein family/group databases

MEROPSiM10.014.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-14 (EC:3.4.24.80)
Short name:
MMP-14
Alternative name(s):
Membrane-type matrix metalloproteinase 1
Short name:
MT-MMP 1
Short name:
MTMMP1
Membrane-type-1 matrix metalloproteinase
Short name:
MT-MMP
Short name:
MT1-MMP
Short name:
MT1MMP
Gene namesi
Name:Mmp14
Synonyms:Mtmmp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 15

Organism-specific databases

RGDi620198. Mmp14.

Subcellular locationi

Membrane Curated; Single-pass type I membrane protein Curated. Melanosome By similarity. Cytoplasm By similarity
Note: Forms a complex with BST2 and localizes to the cytoplasm.By similarity

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. extracellular matrix Source: InterPro
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 11191Activation peptidePRO_0000028806Add
BLAST
Chaini112 – 582471Matrix metalloproteinase-14PRO_0000028807Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi319 ↔ 508By similarity
Modified residuei399 – 3991Phosphotyrosine; by PKDCCBy similarity

Post-translational modificationi

Tyrosine phosphorylated by PKDCC/VLK.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Phosphoprotein, Zymogen

Proteomic databases

PRIDEiQ10739.

PTM databases

PhosphoSiteiQ10739.

Expressioni

Gene expression databases

GenevestigatoriQ10739.

Interactioni

Subunit structurei

Interacts (via C-terminal cytoplasmic tail) with BST2.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000049168.

Structurei

3D structure databases

ProteinModelPortaliQ10739.
SMRiQ10739. Positions 114-287.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini112 – 541430ExtracellularSequence AnalysisAdd
BLAST
Topological domaini563 – 58220CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei542 – 56221HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati316 – 36449Hemopexin 1Add
BLAST
Repeati365 – 41046Hemopexin 2Add
BLAST
Repeati412 – 46049Hemopexin 3Add
BLAST
Repeati461 – 50848Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi91 – 988Cysteine switchBy similarity

Domaini

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.

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG295915.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ10739.
KOiK07763.
OMAiWMGCPSG.
OrthoDBiEOG7XPZ57.
PhylomeDBiQ10739.
TreeFamiTF352396.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR028693. MMP14.
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]
PANTHERiPTHR10201:SF24. PTHR10201:SF24. 1 hit.
PfamiPF11857. DUF3377. 1 hit.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q10739-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSPAPRPSRS LLLPLLTLGT TLASLGWAQS SNFSPEAWLQ QYGYLPPGDL
60 70 80 90 100
RTHTQRSPQS LSAAIAAMQR FYGLQVTGKA DSDTMKAMRR PRCGVPDKFG
110 120 130 140 150
TEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT FEAIRKAFRV
160 170 180 190 200
WESATPLRFR EVPYAYIREG HEKQADIMIL FAEGFHGDST PFDGEGGFLA
210 220 230 240 250
HAYFPGPNIG GDTHFDSAEP WTVQNEDLNG NDIFLVAVHE LGHALGLEHS
260 270 280 290 300
NDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGSKSGSP TKMPPQPRTT
310 320 330 340 350
SRPSVPDKPR NPTYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM
360 370 380 390 400
DGYPMPIGQF WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP
410 420 430 440 450
KHIKELGRGL PTDKIDAALF WMPNGKTYFF RGNKYYRFNE EFRAVDSEYP
460 470 480 490 500
KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG NKYWKFNNQK LKVEPGYPKS
510 520 530 540 550
ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGSGAVSAA AVVLPVLLLL
560 570 580
LVLAVGLAVF FFRRHGTPKR LLYCQRSLLD KV
Length:582
Mass (Da):66,080
Last modified:May 1, 2007 - v2
Checksum:i48F1A8E3065E1AE8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681M → I in CAA58521. (PubMed:7708715)Curated
Sequence conflicti255 – 2551A → D in CAA58521. (PubMed:7708715)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83537 mRNA. Translation: CAA58521.1.
X91785 mRNA. Translation: CAA62897.1.
BC072509 mRNA. Translation: AAH72509.1.
PIRiI84471.
RefSeqiNP_112318.1. NM_031056.1.
UniGeneiRn.10371.

Genome annotation databases

EnsembliENSRNOT00000042938; ENSRNOP00000049168; ENSRNOG00000010947.
ENSRNOT00000075610; ENSRNOP00000065434; ENSRNOG00000010947.
GeneIDi81707.
KEGGirno:81707.
UCSCiRGD:620198. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83537 mRNA. Translation: CAA58521.1 .
X91785 mRNA. Translation: CAA62897.1 .
BC072509 mRNA. Translation: AAH72509.1 .
PIRi I84471.
RefSeqi NP_112318.1. NM_031056.1.
UniGenei Rn.10371.

3D structure databases

ProteinModelPortali Q10739.
SMRi Q10739. Positions 114-287.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000049168.

Protein family/group databases

MEROPSi M10.014.

PTM databases

PhosphoSitei Q10739.

Proteomic databases

PRIDEi Q10739.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000042938 ; ENSRNOP00000049168 ; ENSRNOG00000010947 .
ENSRNOT00000075610 ; ENSRNOP00000065434 ; ENSRNOG00000010947 .
GeneIDi 81707.
KEGGi rno:81707.
UCSCi RGD:620198. rat.

Organism-specific databases

CTDi 4323.
RGDi 620198. Mmp14.

Phylogenomic databases

eggNOGi NOG295915.
GeneTreei ENSGT00760000118870.
HOGENOMi HOG000217928.
HOVERGENi HBG052484.
InParanoidi Q10739.
KOi K07763.
OMAi WMGCPSG.
OrthoDBi EOG7XPZ57.
PhylomeDBi Q10739.
TreeFami TF352396.

Enzyme and pathway databases

Reactomei REACT_198590. Activation of Matrix Metalloproteinases.
REACT_199177. Collagen degradation.
REACT_199178. Degradation of the extracellular matrix.

Miscellaneous databases

NextBioi 615328.
PROi Q10739.

Gene expression databases

Genevestigatori Q10739.

Family and domain databases

Gene3Di 2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR028693. MMP14.
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 ]
PANTHERi PTHR10201:SF24. PTHR10201:SF24. 1 hit.
Pfami PF11857. DUF3377. 1 hit.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSi PR00138. MATRIXIN.
SMARTi SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas."
    Okada A., Bellocq J.-P., Rouyer N., Chenard M.P., Rio M.C., Chambon P., Basset P.
    Proc. Natl. Acad. Sci. U.S.A. 92:2730-2734(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Expression and function of MT-MMP in glial cells."
    Cossins J., Clements J., Catlin G., Wells G.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
    Tissue: Heart.

Entry informationi

Entry nameiMMP14_RAT
AccessioniPrimary (citable) accession number: Q10739
Secondary accession number(s): Q6IN06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 1, 2007
Last modified: October 29, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3