Matrix metalloproteinase-14 precursor - Oryctolagus cuniculus (Rabbit)

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Q95220 (MMP14_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 93. History...

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

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Oryctolagus cuniculus (Rabbit) [Complete proteome]

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	582 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

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 be involved in actin cytoskeleton reorganization by cleaving PTK7 By similarity.
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.
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.

Ontologies

Keywords
Cellular component	Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Zymogen
Technical term	Complete proteome
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: UniProtKB-KW zymogen activation Inferred from sequence or structural similarity. Source: AgBase
Cellular component	extracellular matrix Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Potential

Propeptide

21 – 111

Activation peptide

PRO_0000028804

Chain

112 – 582

471

Matrix metalloproteinase-14

PRO_0000028805

Regions

Topological domain

112 – 541

430

Extracellular Potential

Transmembrane

542 – 562

Helical; Potential

Topological domain

563 – 582

Cytoplasmic Potential

Domain

323 – 366

Hemopexin-like 1

Domain

368 – 412

Hemopexin-like 2

Domain

415 – 461

Hemopexin-like 3

Domain

463 – 508

Hemopexin-like 4

Motif

91 – 98

Cysteine switch By similarity

Sites

Active site

240

By similarity

Metal binding

Zinc; in inhibited form By similarity

Metal binding

239

Zinc; catalytic By similarity

Metal binding

243

Zinc; catalytic By similarity

Metal binding

249

Zinc; catalytic By similarity

Amino acid modifications

Disulfide bond

319 ↔ 508

By similarity

Experimental info

Sequence conflict

Q → K in AAD13803. Ref.2

Sequence conflict

268

K → N Ref.2

Sequence conflict

270

L → V Ref.2

Sequence conflict

275

E → D in AAD13803. Ref.2

Sequence conflict

292 – 296

RCLLN → KMPPP Ref.2

Sequence conflict

298 – 300

GQP → RTT Ref.2

Sequence conflict

302 – 308

GLLFRIS → RTFIPDK Ref.2

Sequence conflict

310

G → R Ref.2

Sequence conflict

317

K → N in AAD13803. Ref.2

Sequence conflict

329

F → L in AAD13803. Ref.2

Sequence conflict

360

L → F in AAD13803. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q95220 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 844624B0AF1B6812
Show »

FASTA

582

65,963

        10         20         30         40         50         60 
MSPAPRPSRR LLLPLLTLGT ALASLGSAQS NSFSPEAWLQ QYGYLPPGDL RTHTQRSPQS 

        70         80         90        100        110        120 
LSAAIAAMQR FYGLRVTGKA DTDTMKAMRR PRCGVPDKFG AEIKANVRRK RYAIQGLKWQ 

       130        140        150        160        170        180 
HNEITFCIQN YTPKVGEYAT FEAIRKAFRV WESATPLRFR EVHYAYIRDG REKQADIMIF 

       190        200        210        220        230        240 
FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE 

       250        260        270        280        290        300 
LGHALGLEHS NDPSAIMAPF YQWMDTEKFL LPDDERRGIQ QLYGSQSGSP TRCLLNPGQP 

       310        320        330        340        350        360 
SGLLFRISPG NPTYGPKICD GNFDTVAVFR GEMFVFKERW FWRVRNNQVM DGYPMPIGQL 

       370        380        390        400        410        420 
WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP KHIKELGRGL PTDKIDAALF 

       430        440        450        460        470        480 
WMPNGKTYFF RGNKYYRFNE ELRAVDSEYP KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG 

       490        500        510        520        530        540 
NKYWKFNNQK LKVEPGYPKS ALRDWMGCPA GGRPDEGTEE ETEVIIIEVD EEGSGAVSAA 

       550        560        570        580 
AVVLPVLLLL LVLAVGLAVF FFRRHGTPKR LLYCQRSLLD KV

« Hide

References

[1]	Wang H., Keiser J. Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: New Zealand white. Tissue: Vascular smooth muscle.
[2]	Sato T. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-572. Strain: New Zealand white.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U83918 mRNA. Translation: AAB41500.1. U73940 Genomic DNA. Translation: AAD13803.1.
RefSeq	NP_001076262.1. NM_001082793.1.
UniGene	Ocu.6250.
3D structure databases
ProteinModelPortal	Q95220.
SMR	Q95220. Positions 114-287.
ModBase	Search...
Protein-protein interaction databases
STRING	Q95220.
Protein family/group databases
MEROPS	M10.014.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100009598.
Organism-specific databases
CTD	4323.
Phylogenomic databases
GeneTree	ENSGT00580000081226.
HOVERGEN	HBG052484.
Family and domain databases
InterPro	IPR000585. Hemopexin/matrixin. IPR018486. Hemopexin/matrixin_CS. IPR018487. Hemopexin/matrixin_repeat. IPR024079. MetalloPept_cat_dom. IPR001818. Pept_M10_metallopeptidase. IPR016293. Pept_M10A_matrix_strom. IPR021190. Pept_M10A_matrixin. IPR021805. Pept_M10A_metallopeptidase_C. IPR021158. Pept_M10A_Zn_BS. IPR006026. Peptidase_Metallo. IPR002477. Peptidoglycan-bd-like. IPR006311. TAT_signal. [Graphical view]
Gene3D	G3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit. G3DSA:2.110.10.10. Hemopexin. 1 hit.
Pfam	PF11857. DUF3377. 1 hit. 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]
SUPFAM	SSF50923. Hemopexin. 1 hit. SSF47090. PGBD_like. 1 hit.
PROSITE	PS00546. CYSTEINE_SWITCH. 1 hit. PS00024. HEMOPEXIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MMP14_RABIT

Accession

Primary (citable) accession number: Q95220
Secondary accession number(s): P79225

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 15, 1998
Last modified:	November 16, 2011
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents