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Protein

Matrix metalloproteinase-14

Gene

MMP14

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: 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 (By similarity). May play a role in the biomineralization of enamel and dentin. 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

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • Ca2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi91 – 911Zinc; in inhibited formBy similarity
Metal bindingi237 – 2371Zinc; catalyticPROSITE-ProRule annotation
Active sitei238 – 2381PROSITE-ProRule annotation
Metal bindingi241 – 2411Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi247 – 2471Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

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:
MT1-MMP
Short name:
MT1MMP
Gene namesi
Name:MMP14
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini110 – 539430ExtracellularSequence analysisAdd
BLAST
Transmembranei540 – 56021HelicalSequence analysisAdd
BLAST
Topological domaini561 – 58020CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Propeptidei29 – 10981Activation peptidePRO_0000028802Add
BLAST
Chaini110 – 580471Matrix metalloproteinase-14PRO_0000028803Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi317 ↔ 506By similarity
Modified residuei397 – 3971Phosphotyrosine; 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

PaxDbiQ9XT90.

Expressioni

Tissue specificityi

Highly expressed in developing tooth tissues.

Interactioni

Subunit structurei

Interacts (via C-terminal cytoplasmic tail) with BST2. Interacts with DLL1; inhibits DLL1-induced Notch signaling.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000002229.

Structurei

3D structure databases

ProteinModelPortaliQ9XT90.
SMRiQ9XT90. Positions 112-285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati314 – 36249Hemopexin 1Add
BLAST
Repeati363 – 40846Hemopexin 2Add
BLAST
Repeati410 – 45849Hemopexin 3Add
BLAST
Repeati459 – 50648Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi89 – 968Cysteine 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

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ9XT90.
KOiK07763.

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.

Q9XT90-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPAPRPVRS LLLPLLTLAS ALASLSSAQS FSPEAWLQQY GYLPPGDLRT
60 70 80 90 100
HTQRSPQSLS AAIAAMQRFY GLRVTGKADA DTMKAMRRPR CGVPDKFGAE
110 120 130 140 150
IKANVRRKRY AIQGLKWQHN EITFCIQNYT PKVGEYATFE AIRKAFRVWE
160 170 180 190 200
SATPLRFREV PYAYIREGHE KQADIMIFFA EGFHGDSTPF DGEGGFLAHA
210 220 230 240 250
YFPGPNIGGD THFDSAEPWT VRNEDLNGND IFLVAVHELG HALGLEHSND
260 270 280 290 300
PSAIMAPFYQ WMDTENFVLP DDDRRGIQQL YGSESGFPTK MPPQPRTTSK
310 320 330 340 350
PSVPDKPKNP TYGPNICDGN FDTVAMLRGE MFVFKERWFW RVRKNQVMDG
360 370 380 390 400
YPMPIGQFWR GLPASINTAY ERKDGKFVFF KGDKHWVFDE ASLEPGYPKH
410 420 430 440 450
IKELGRRLPT DKIDAALFWM PNGKDYFFRG NKYYRFNEEL RAVDSEYPKN
460 470 480 490 500
IKVWEGIPES PRGSFMGSDE VFTYFYKGNK YWKFNNQKLK VEPGYPKSAL
510 520 530 540 550
RDWMGCPSGG RPDEGTEEET EVIIIEVDEE GSGAVSAAAV VLPVLLLLLV
560 570 580
LAVGLAVFFF RRHGTPKRLL YCQRSLLDKV
Length:580
Mass (Da):65,934
Last modified:November 1, 1999 - v1
Checksum:iB7B2C2C569A96CAC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF067419 mRNA. Translation: AAD38324.1.
RefSeqiNP_999404.1. NM_214239.1.
UniGeneiSsc.734.

Genome annotation databases

GeneIDi397471.
KEGGissc:397471.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF067419 mRNA. Translation: AAD38324.1.
RefSeqiNP_999404.1. NM_214239.1.
UniGeneiSsc.734.

3D structure databases

ProteinModelPortaliQ9XT90.
SMRiQ9XT90. Positions 112-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000002229.

Protein family/group databases

MEROPSiM10.014.

Proteomic databases

PaxDbiQ9XT90.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397471.
KEGGissc:397471.

Organism-specific databases

CTDi4323.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ9XT90.
KOiK07763.

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]
ProtoNetiSearch...

Publicationsi

  1. "Expression and localization of membrane type 1 matrix metalloproteinase in tooth tissues."
    Caron C., Xue J., Bartlett J.D.
    Matrix Biol. 17:501-511(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiMMP14_PIG
AccessioniPrimary (citable) accession number: Q9XT90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: December 9, 2015
This is version 117 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.