Matrix metalloproteinase-14 precursor

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9XT90 (MMP14_PIG)

Last modified October 13, 2009. Version 73. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Matrix metalloproteinase-14
      Short name=MMP-14
    EC=3.4.24.80
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 names

Name:

MMP14

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Hide | Top

Protein attributes

Sequence length	580 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

Hide | Top

General annotation (Comments)

Function	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.
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 By similarity. Calcium By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein Potential. Melanosome By similarity.
Tissue specificity	Highly expressed in developing tooth tissues.
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.
Sequence similarities	Belongs to the peptidase M10A family. Contains 4 hemopexin-like domains.

Hide | Top

Ontologies

Keywords
Cellular component	Membrane
Domain	Repeat Signal Transmembrane
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Zymogen
Gene Ontology (GO)
Biological process	branching morphogenesis of a tube Inferred from sequence or structural similarity. Source: AgBase cell migration Inferred from sequence or structural similarity. Source: AgBase lung development Inferred from sequence or structural similarity. Source: AgBase proteolysis Inferred from electronic annotation. Source: InterPro zymogen activation Inferred from sequence or structural similarity. Source: AgBase
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell proteinaceous extracellular matrix Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

Potential

Propeptide

29 – 109

Activation peptide

PRO_0000028802

Chain

110 – 580

471

Matrix metalloproteinase-14

PRO_0000028803

Regions

Topological domain

110 – 539

430

Extracellular Potential

Transmembrane

540 – 560

Potential

Topological domain

561 – 580

Cytoplasmic Potential

Domain

321 – 364

Hemopexin-like 1

Domain

366 – 410

Hemopexin-like 2

Domain

413 – 459

Hemopexin-like 3

Domain

461 – 506

Hemopexin-like 4

Motif

89 – 96

Cysteine switch By similarity

Sites

Active site

238

By similarity

Metal binding

Zinc; in inhibited form By similarity

Metal binding

237

Zinc; catalytic By similarity

Metal binding

241

Zinc; catalytic By similarity

Metal binding

247

Zinc; catalytic By similarity

Amino acid modifications

Disulfide bond

317 ↔ 506

By similarity

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q9XT90-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: B7B2C2C569A96CAC
Show »

FASTA

580

65,934

        10         20         30         40         50         60 
MSPAPRPVRS LLLPLLTLAS ALASLSSAQS FSPEAWLQQY GYLPPGDLRT HTQRSPQSLS 

        70         80         90        100        110        120 
AAIAAMQRFY GLRVTGKADA DTMKAMRRPR CGVPDKFGAE IKANVRRKRY AIQGLKWQHN 

       130        140        150        160        170        180 
EITFCIQNYT PKVGEYATFE AIRKAFRVWE SATPLRFREV PYAYIREGHE KQADIMIFFA 

       190        200        210        220        230        240 
EGFHGDSTPF DGEGGFLAHA YFPGPNIGGD THFDSAEPWT VRNEDLNGND IFLVAVHELG 

       250        260        270        280        290        300 
HALGLEHSND PSAIMAPFYQ WMDTENFVLP DDDRRGIQQL YGSESGFPTK MPPQPRTTSK 

       310        320        330        340        350        360 
PSVPDKPKNP TYGPNICDGN FDTVAMLRGE MFVFKERWFW RVRKNQVMDG YPMPIGQFWR 

       370        380        390        400        410        420 
GLPASINTAY ERKDGKFVFF KGDKHWVFDE ASLEPGYPKH IKELGRRLPT DKIDAALFWM 

       430        440        450        460        470        480 
PNGKDYFFRG NKYYRFNEEL RAVDSEYPKN IKVWEGIPES PRGSFMGSDE VFTYFYKGNK 

       490        500        510        520        530        540 
YWKFNNQKLK VEPGYPKSAL RDWMGCPSGG RPDEGTEEET EVIIIEVDEE GSGAVSAAAV 

       550        560        570        580 
VLPVLLLLLV LAVGLAVFFF RRHGTPKRLL YCQRSLLDKV

« Hide

Hide | Top

References

[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: 9881602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Hide | Top

Cross-references

Sequence databases
	AF067419 mRNA. Translation: AAD38324.1.
RefSeq	NP_999404.1.
UniGene	Ssc.734
3D structure databases
HSSP	HSSP built from PDB template 1BQQ based on UniProtKB P50281.
SMR	Q9XT90. Positions 112-285.
ModBase	Search...
Protein family/group databases
MEROPS	M10.014.
Genome annotation databases
GeneID	397471.
KEGG	ssc:397471.
Organism-specific databases
CTD	397471.
Phylogenomic databases
HOVERGEN	Q9XT90.
Enzyme and pathway databases
BRENDA	3.4.24.80. 249.
Family and domain databases
InterPro	IPR000585. Hemopexin/matrixin. IPR018486. Hemopexin/matrixin_CS. IPR018487. Hemopexin/matrixin_repeat. IPR001818. Pept_M10A_M12B. IPR016293. Pept_M10A_matrix. IPR006025. Pept_M_Zn_BS. IPR006026. Peptidase_M. IPR002477. Peptidoglycan-bd-like. [Graphical view]
Gene3D	G3DSA:2.110.10.10. Hemopexin. 1 hit.
Pfam	PF00045. Hemopexin. 4 hits. PF00413. Peptidase_M10. 1 hit. PF01471. PG_binding_1. 1 hit. [Graphical view]
PIRSF	PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTS	PR00138. MATRIXIN.
SMART	SM00120. HX. 4 hits. SM00235. ZnMc. 1 hit. [Graphical view]
PROSITE	PS00546. CYSTEINE_SWITCH. 1 hit. PS00024. HEMOPEXIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Hide | Top

Entry information

Entry name

MMP14_PIG

Accession

Primary (citable) accession number: Q9XT90

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	October 13, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents