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Protein

Matrix metalloproteinase-14

Gene

Mmp14

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Endopeptidase that degrades various components of the extracellular matrix, such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development. 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

  • angiogenesis Source: Ensembl
  • astrocyte cell migration Source: Ensembl
  • bone development Source: MGI
  • branching morphogenesis of an epithelial tube Source: MGI
  • cell migration Source: MGI
  • chondrocyte proliferation Source: MGI
  • collagen catabolic process Source: MGI
  • craniofacial suture morphogenesis Source: MGI
  • embryonic cranial skeleton morphogenesis Source: MGI
  • endochondral ossification Source: MGI
  • endodermal cell differentiation Source: Ensembl
  • endothelial cell proliferation Source: Ensembl
  • lung development Source: MGI
  • male gonad development Source: Ensembl
  • negative regulation of focal adhesion assembly Source: Ensembl
  • ossification Source: MGI
  • ovarian follicle development Source: Ensembl
  • positive regulation of cell growth Source: MGI
  • positive regulation of cell migration Source: MGI
  • proteolysis Source: MGI
  • regulation of transcription, DNA-templated Source: GOC
  • response to estrogen Source: Ensembl
  • response to hypoxia Source: Ensembl
  • response to mechanical stimulus Source: Ensembl
  • response to oxidative stress Source: Ensembl
  • tissue remodeling Source: Ensembl
  • zymogen activation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_275864. Degradation of the extracellular matrix.
REACT_313067. Collagen degradation.
REACT_332323. Activation of Matrix Metalloproteinases.

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):
MMP-X1
MT-MMP
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
Synonyms:Mtmmp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:101900. Mmp14.

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 – 11191By similarityPRO_0000028800Add
BLAST
Chaini112 – 582471Matrix metalloproteinase-14PRO_0000028801Add
BLAST

Amino acid modifications

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

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity
Tyrosine phosphorylated by PKDCC/VLK.By similarity

Keywords - PTMi

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

Proteomic databases

MaxQBiP53690.
PRIDEiP53690.

PTM databases

PhosphoSiteiP53690.

Expressioni

Tissue specificityi

Highly expressed in placenta, kidney, heart, lung, embryonic skeletal and periskeletal tissues.

Developmental stagei

Not detected before day 10.5. At day 12.5, prominently expressed in large arteries and the umbilical arteries, expressed at lower levels in the myocardium, craniofacial mesenchyme, nasal epithelium and liver capsule. At days 14.5 and 17.5, expressed in the musculoskeletal system, and ossification areas, with continued expression in the arterial tunica media.

Gene expression databases

BgeeiP53690.
CleanExiMM_MMP14.
ExpressionAtlasiP53690. baseline and differential.
GenevestigatoriP53690.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP53690. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP53690.
SMRiP53690. Positions 65-511.
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

eggNOGiNOG295915.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiP53690.
KOiK07763.
OMAiMKAMKRP.
OrthoDBiEOG7XPZ57.
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.

P53690-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPAPRPSRS LLLPLLTLGT ALASLGWAQG SNFSPEAWLQ QYGYLPPGDL
60 70 80 90 100
RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DLATMMAMRR 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
SRPSVPDKPK NPAYGPNICD 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):65,919
Last modified:July 27, 2011 - v3
Checksum:i6CA95CFD5811B093
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331P → S in AAB86602 (PubMed:9325265).Curated
Sequence conflicti255 – 2551A → D in CAA58520 (PubMed:7708715).Curated
Sequence conflicti258 – 2581A → S in CAA58520 (PubMed:7708715).Curated
Sequence conflicti258 – 2581A → S in AAB51753 (PubMed:9648071).Curated
Sequence conflicti341 – 3411F → L in CAA58520 (PubMed:7708715).Curated
Sequence conflicti346 – 3461N → P in AAB86602 (PubMed:9325265).Curated
Sequence conflicti378 – 3781K → T in CAA58520 (PubMed:7708715).Curated
Sequence conflicti390 – 3912FD → CV in CAA58520 (PubMed:7708715).Curated
Sequence conflicti400 – 4012PK → AN in CAA58520 (PubMed:7708715).Curated
Sequence conflicti407 – 4071G → V in CAA58520 (PubMed:7708715).Curated
Sequence conflicti412 – 4121T → S in CAA58520 (PubMed:7708715).Curated
Sequence conflicti417 – 4171A → T in CAA58520 (PubMed:7708715).Curated
Sequence conflicti512 – 5121G → R in AAB51753 (PubMed:9648071).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83536 mRNA. Translation: CAA58520.2.
AF022432
, AF022424, AF022425, AF022426, AF022427, AF022428, AF022429, AF022430, AF022431 Genomic DNA. Translation: AAB86602.1.
U54984 mRNA. Translation: AAB51753.1.
DQ249870 mRNA. Translation: ABB45784.1.
AK088476 mRNA. Translation: BAC40377.1.
AK138611 mRNA. Translation: BAE23719.1.
AK149907 mRNA. Translation: BAE29158.1.
AK149988 mRNA. Translation: BAE29216.1.
AK165014 mRNA. Translation: BAE38000.1.
CH466535 Genomic DNA. Translation: EDL36348.1.
CCDSiCCDS36922.1.
PIRiI48673.
RefSeqiNP_032634.3. NM_008608.3.
UniGeneiMm.280175.
Mm.486486.

Genome annotation databases

EnsembliENSMUST00000089688; ENSMUSP00000087119; ENSMUSG00000000957.
GeneIDi17387.
KEGGimmu:17387.
UCSCiuc007twc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83536 mRNA. Translation: CAA58520.2.
AF022432
, AF022424, AF022425, AF022426, AF022427, AF022428, AF022429, AF022430, AF022431 Genomic DNA. Translation: AAB86602.1.
U54984 mRNA. Translation: AAB51753.1.
DQ249870 mRNA. Translation: ABB45784.1.
AK088476 mRNA. Translation: BAC40377.1.
AK138611 mRNA. Translation: BAE23719.1.
AK149907 mRNA. Translation: BAE29158.1.
AK149988 mRNA. Translation: BAE29216.1.
AK165014 mRNA. Translation: BAE38000.1.
CH466535 Genomic DNA. Translation: EDL36348.1.
CCDSiCCDS36922.1.
PIRiI48673.
RefSeqiNP_032634.3. NM_008608.3.
UniGeneiMm.280175.
Mm.486486.

3D structure databases

ProteinModelPortaliP53690.
SMRiP53690. Positions 65-511.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP53690. 1 interaction.

Protein family/group databases

MEROPSiM10.014.

PTM databases

PhosphoSiteiP53690.

Proteomic databases

MaxQBiP53690.
PRIDEiP53690.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000089688; ENSMUSP00000087119; ENSMUSG00000000957.
GeneIDi17387.
KEGGimmu:17387.
UCSCiuc007twc.2. mouse.

Organism-specific databases

CTDi4323.
MGIiMGI:101900. Mmp14.

Phylogenomic databases

eggNOGiNOG295915.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiP53690.
KOiK07763.
OMAiMKAMKRP.
OrthoDBiEOG7XPZ57.
TreeFamiTF352396.

Enzyme and pathway databases

ReactomeiREACT_275864. Degradation of the extracellular matrix.
REACT_313067. Collagen degradation.
REACT_332323. Activation of Matrix Metalloproteinases.

Miscellaneous databases

ChiTaRSiMmp14. mouse.
NextBioi292000.
PROiP53690.
SOURCEiSearch...

Gene expression databases

BgeeiP53690.
CleanExiMM_MMP14.
ExpressionAtlasiP53690. baseline and differential.
GenevestigatoriP53690.

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

« 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. Odaka A.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "The matrix metalloproteinase-14 (MMP-14) gene is structurally distinct from other MMP genes and is co-expressed with the TIMP-2 gene during mouse embryogenesis."
    Apte S.S., Fukai N., Beier D.R., Olsen B.R.
    J. Biol. Chem. 272:25511-25517(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  4. "Cloning of murine membrane-type-1-matrix metalloproteinase (MT-1-MMP) and its metanephric developmental regulation with respect to MMP-2 and its inhibitor."
    Ota K., Stetler-Stevenson W.G., Yang Q., Kumar A., Wada J., Kashihara N., Wallner E.I., Kanwar Y.S.
    Kidney Int. 54:131-142(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CD-1.
    Tissue: Kidney.
  5. "Interference with the complement system by tumor cell membrane type-1 matrix metalloproteinase plays a significant role in promoting metastasis in mice."
    Rozanov D.V., Savinov A.Y., Golubkov V.S., Tomlinson S., Strongin A.Y.
    Cancer Res. 66:6258-6263(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: FVB/N.
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Eye, Spinal cord and Thymus.
  7. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover."
    Holmbeck K., Bianco P., Caterina J., Yamada S., Kromer M., Kuznetsov S.A., Mankani M., Robey P.G., Poole A.R., Pidoux I., Ward J.M., Birkedal-Hansen H.
    Cell 99:81-92(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiMMP14_MOUSE
AccessioniPrimary (citable) accession number: P53690
Secondary accession number(s): O08645, O35369, Q8BTX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: May 27, 2015
This is version 146 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.