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Protein

Matrix metalloproteinase-14

Gene

MMP14

Organism
Oryctolagus cuniculus (Rabbit)
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 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 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

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini112 – 541430ExtracellularSequence analysisAdd
BLAST
Transmembranei542 – 56221HelicalSequence analysisAdd
BLAST
Topological domaini563 – 58220CytoplasmicSequence 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 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 11191Activation peptidePRO_0000028804Add
BLAST
Chaini112 – 582471Matrix metalloproteinase-14PRO_0000028805Add
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

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

STRINGi9986.ENSOCUP00000008835.

Structurei

3D structure databases

ProteinModelPortaliQ95220.
SMRiQ95220. Positions 114-287.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ95220.
KOiK07763.

Family and domain databases

CDDicd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
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.
IPR006311. TAT_signal.
[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.

Q95220-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPAPRPSRR LLLPLLTLGT ALASLGSAQS NSFSPEAWLQ QYGYLPPGDL
60 70 80 90 100
RTHTQRSPQS LSAAIAAMQR FYGLRVTGKA DTDTMKAMRR PRCGVPDKFG
110 120 130 140 150
AEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT FEAIRKAFRV
160 170 180 190 200
WESATPLRFR EVHYAYIRDG REKQADIMIF FAEGFHGDST PFDGEGGFLA
210 220 230 240 250
HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS
260 270 280 290 300
NDPSAIMAPF YQWMDTEKFL LPDDERRGIQ QLYGSQSGSP TRCLLNPGQP
310 320 330 340 350
SGLLFRISPG NPTYGPKICD GNFDTVAVFR GEMFVFKERW FWRVRNNQVM
360 370 380 390 400
DGYPMPIGQL WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP
410 420 430 440 450
KHIKELGRGL PTDKIDAALF WMPNGKTYFF RGNKYYRFNE ELRAVDSEYP
460 470 480 490 500
KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG NKYWKFNNQK LKVEPGYPKS
510 520 530 540 550
ALRDWMGCPA GGRPDEGTEE ETEVIIIEVD EEGSGAVSAA AVVLPVLLLL
560 570 580
LVLAVGLAVF FFRRHGTPKR LLYCQRSLLD KV
Length:582
Mass (Da):65,963
Last modified:July 15, 1998 - v2
Checksum:i844624B0AF1B6812
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291Q → K in AAD13803 (Ref. 2) Curated
Sequence conflicti268 – 2681K → N (Ref. 2) Curated
Sequence conflicti270 – 2701L → V (Ref. 2) Curated
Sequence conflicti275 – 2751E → D in AAD13803 (Ref. 2) Curated
Sequence conflicti292 – 2965RCLLN → KMPPP (Ref. 2) Curated
Sequence conflicti298 – 3003GQP → RTT (Ref. 2) Curated
Sequence conflicti302 – 3087GLLFRIS → RTFIPDK (Ref. 2) Curated
Sequence conflicti310 – 3101G → R (Ref. 2) Curated
Sequence conflicti317 – 3171K → N in AAD13803 (Ref. 2) Curated
Sequence conflicti329 – 3291F → L in AAD13803 (Ref. 2) Curated
Sequence conflicti360 – 3601L → F in AAD13803 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U83918 mRNA. Translation: AAB41500.1.
U73940 Genomic DNA. Translation: AAD13803.1.
RefSeqiNP_001076262.1. NM_001082793.1.
UniGeneiOcu.6250.

Genome annotation databases

GeneIDi100009598.
KEGGiocu:100009598.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U83918 mRNA. Translation: AAB41500.1.
U73940 Genomic DNA. Translation: AAD13803.1.
RefSeqiNP_001076262.1. NM_001082793.1.
UniGeneiOcu.6250.

3D structure databases

ProteinModelPortaliQ95220.
SMRiQ95220. Positions 114-287.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000008835.

Protein family/group databases

MEROPSiM10.014.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009598.
KEGGiocu:100009598.

Organism-specific databases

CTDi4323.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ95220.
KOiK07763.

Family and domain databases

CDDicd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
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.
IPR006311. TAT_signal.
[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...

Entry informationi

Entry nameiMMP14_RABIT
AccessioniPrimary (citable) accession number: Q95220
Secondary accession number(s): P79225
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: September 7, 2016
This is version 119 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

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.