Annotation for this protein is in progress - please check future releases for more complete information


DP00571: Macrophage metalloelastaseFASTA viewXML view

General information
DisProt:DP00571
Name:Macrophage metalloelastase
Synonym(s):MMP12_HUMAN
HME
EC=3.4.24.65
Matrix metalloproteinase-12
MMP-12
Macrophage elastase
ME
First appeared in release:Release 4.1 (07/10/2008)
UniProt:P39900
UniGene:Hs.1695
SwissProt: MMP12_HUMAN
TrEMBL:  
NCBI (GI): 729179
Source organism:Homo sapiens (Human)
Sequence length:470
Percent disordered:4%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFGERYLEKF YGLEINKLPV TKMKYSGNLM - 60
KEKIQEMQHF LGLKVTGQLD TSTLEMMHAP RCGVPDVHHF REMPGGPVWR KHYITYRINN - 120
YTPDMNREDV DYAIRKAFQV WSNVTPLKFS KINTGMADIL VVFARGAHGD FHAFDGKGGI - 180
LAHAFGPGSG IGGDAHFDED EFWTTHSGGT NLFLTAVHEI GHSLGLGHSS DPKAVMFPTY - 240
KYVDINTFRL SADDIRGIQS LYGDPKENQR LPNPDNSEPA LCDPNLSFDA VTTVGNKIFF - 300
FKDRFFWLKV SERPKTSVNL ISSLWPTLPS GIEAAYEIEA RNQVFLFKDD KYWLISNLRP - 360
EPNYPKSIHS FGFPNFVKKI DAAVFNPRFY RTYFFVDNQY WRYDERRQMM DPGYPKLITK - 420
NFQGIGPKID AVFYSKNKYY YFFQGSNQFE YDFLLQRITK TLKSNSWFGC



Functional narrative    

May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.

Region 1: 110-116 Region 2: 146-157

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:110 - 116
Length:7
Region sequence:

RKHYITY

Modification type: Native
PDB: 1JK3:A, 1OS2:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Modification site
Molecular assembly
Functional subclasses: Flexible linkers/spacers
Substrate/ligand binding
Detection methods:
 
References:
  1. Bertini I, Calderone V, Cosenza M, Fragai M, Lee YM, Luchinat C, Mangani S, Terni B, Turano P. "Conformational variability of matrix metalloproteinases: beyond a single 3D structure." Proc Natl Acad Sci U S A. 2005; 102(15): 5334-9. PubMed: 15809432
Comments:
 



Region 2
Type:Disordered
Name: 
Location:146 - 157
Length:12
Region sequence:

PLKFSKINTGMA

Modification type: Native
PDB: 1JK3:A, 1OS2:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Modification site
Molecular assembly
Functional subclasses: Flexible linkers/spacers
Substrate/ligand binding
Detection methods:
 
References:
  1. Bertini I, Calderone V, Cosenza M, Fragai M, Lee YM, Luchinat C, Mangani S, Terni B, Turano P. "Conformational variability of matrix metalloproteinases: beyond a single 3D structure." Proc Natl Acad Sci U S A. 2005; 102(15): 5334-9. PubMed: 15809432
Comments:
 



References

  1. Bertini I, Calderone V, Cosenza M, Fragai M, Lee YM, Luchinat C, Mangani S, Terni B, Turano P. "Conformational variability of matrix metalloproteinases: beyond a single 3D structure." Proc Natl Acad Sci U S A. 2005; 102(15): 5334-9. PubMed: 15809432

  2. Bertini I, Calderone V, Fragai M, Luchinat C, Mangani S, Terni B. "X-ray structures of binary and ternary enzyme-product-inhibitor complexes of matrix metalloproteinases." Angew Chem Int Ed Engl. 2003; 42(23): 2673-6. PubMed: 12813751

  3. Lang R, Kocourek A, Braun M, Tschesche H, Huber R, Bode W, Maskos K. "Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 A crystal structure." J Mol Biol. 2001; 312(4): 731-42. PubMed: 11575928


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