UniProt:P50281 MMP14

chain
  • signal peptide:1-20
  • propeptide:21-111
  • chain:112-582
checksum 3722DE286A4BBCDE
comment
  • FUNCTION Endopeptidase that degrades various components of the extracellular matrix such as collagen (PubMed:8015608). Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (By similarity). Activates progelatinase A/MMP2, thereby acting as a positive regulator of cell growth and migration (PubMed:22065321, PubMed:8015608). Involved in the formation of the fibrovascular tissues in association with pro-MMP2 (PubMed:12714657, PubMed:22065321). May be involved in actin cytoskeleton reorganization by cleaving PTK7 (PubMed:20837484). Acts as a regulator of Notch signaling by mediating cleavage and inhibition of DLL1 (PubMed:21572390). Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis (PubMed:22330140). Acts as a negative regulator of the GDF15-GFRAL aversive response by mediating cleavage and inactivation of GFRAL (PubMed:35177851).CATALYTIC ACTIVITY 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.COFACTOR Binds 1 zinc ion per subunit.COFACTOR Interacts (via C-terminal cytoplasmic tail) with BST2.INTERACTION Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Forms a complex with BST2 and localizes to the cytoplasm (PubMed:17081065).TISSUE SPECIFICITY Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors.INDUCTION Up-regulated by NANOS1.DOMAIN 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.PTM The precursor is cleaved by a furin endopeptidase.PTM Tyrosine phosphorylated by PKDCC/VLK.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the peptidase M10A family.
crossReference
databaseName UniProt
dbId 59405
description
  • recommendedName: Matrix metalloproteinase-14 shortName: MMP-14 ecNumber evidence="18 22"3.4.24.80 alternativeName: MMP-X1 alternativeName: Membrane-type matrix metalloproteinase 1 shortName: MT-MMP 1 shortName: MTMMP1 alternativeName: fullName evidence="27"Membrane-type-1 matrix metalloproteinase shortName evidence="27"MT1-MMP shortName evidence="27"MT1MMP
displayName UniProt:P50281 MMP14
geneName
  • MMP14
identifier P50281
isSequenceChanged false
keyword
  • 3D-structure
  • Calcium
  • Cell membrane
  • Cleavage on pair of basic residues
  • Cytoplasm
  • Direct protein sequencing
  • Disease variant
  • Disulfide bond
  • Hydrolase
  • Membrane
  • Metal-binding
  • Metalloprotease
  • Osteoporosis
  • Phosphoprotein
  • Protease
  • Proteomics identification
  • Reference proteome
  • Repeat
  • Signal
  • Transmembrane
  • Transmembrane helix
  • Zinc
  • Zymogen
modified [InstanceEdit:9926675] Weiser, Joel, 2024-11-03
moleculeType Protein
name
  • MMP14
otherIdentifier
  • 11725987_a_at
  • 11725988_at
  • 11725989_x_at
  • 11747717_a_at
  • 1301_s_at
  • 160020_PM_at
  • 160020_at
  • 16782187
  • 202827_PM_s_at
  • 202827_s_at
  • 202828_PM_s_at
  • 202828_s_at
  • 217279_3p_x_at
  • 217279_PM_x_at
  • 217279_x_at
  • 34747_at
  • 3528865
  • 3528866
  • 3528867
  • 3528868
  • 3528870
  • 3528871
  • 3528872
  • 3528873
  • 3528874
  • 3528875
  • 3528876
  • 3528877
  • 3528878
  • 3528879
  • 3528880
  • 3528881
  • 3528882
  • 3528883
  • 3528884
  • 3528885
  • 3528886
  • 3528887
  • 3528888
  • 3528890
  • 3528892
  • 4323
  • 4870053_3p_s_at
  • 73002_at
  • 7973336
  • A_14_P114314
  • A_24_P82106
  • GE60414
  • GO:0001501
  • GO:0001503
  • GO:0001525
  • GO:0001541
  • GO:0001666
  • GO:0001935
  • GO:0001958
  • GO:0004175
  • GO:0004222
  • GO:0004252
  • GO:0005178
  • GO:0005515
  • GO:0005615
  • GO:0005634
  • GO:0005737
  • GO:0005768
  • GO:0005796
  • GO:0005829
  • GO:0005856
  • GO:0005886
  • GO:0005925
  • GO:0006508
  • GO:0006979
  • GO:0008233
  • GO:0008237
  • GO:0008270
  • GO:0008584
  • GO:0009612
  • GO:0009653
  • GO:0009725
  • GO:0010831
  • GO:0010954
  • GO:0016020
  • GO:0016477
  • GO:0016485
  • GO:0016787
  • GO:0022617
  • GO:0030154
  • GO:0030163
  • GO:0030198
  • GO:0030307
  • GO:0030312
  • GO:0030324
  • GO:0030335
  • GO:0030574
  • GO:0031012
  • GO:0031410
  • GO:0031638
  • GO:0035987
  • GO:0035988
  • GO:0042470
  • GO:0043615
  • GO:0043627
  • GO:0044354
  • GO:0045111
  • GO:0045579
  • GO:0045746
  • GO:0046872
  • GO:0048701
  • GO:0048754
  • GO:0048771
  • GO:0048856
  • GO:0048870
  • GO:0051895
  • GO:0060322
  • GO:0060348
  • GO:0070006
  • GO:0071412
  • GO:0097094
  • GO:0160144
  • GO:0160145
  • GO:1903076
  • GO:1905523
  • GO:1990834
  • HMNXSV003041452
  • Hs.2399.0.S2_3p_s_at
  • Hs.2399.1.S1_3p_a_at
  • Hs.2399.1.S1_3p_s_at
  • ILMN_1774739
  • PH_hs_0000323
  • TC14000133.hg
  • X83535_s_at
  • Z48481_at
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • MMP14_HUMAN
  • A8K5L0
  • Q6GSF3
  • Q92678
sequenceLength 582
species [Species:48887] Homo sapiens
stId uniprot:P50281
url http://purl.uniprot.org/uniprot/P50281

Referrals

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