PMID- 10644717
OWN - NLM
STAT- MEDLINE
DCOM- 20000229
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 4
DP  - 2000 Jan 28
TI  - Characterization of a novel human serine protease that has extensive homology to 
      bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia.
PG  - 2581-8
AB  - We report the isolation and characterization of a cDNA encoding the novel
      mammalian serine protease Omi. Omi protein consists of 458 amino acids and has
      homology to bacterial HtrA endoprotease, which acts as a chaperone at low
      temperatures and as a proteolytic enzyme that removes denatured or damaged
      substrates at elevated temperatures. The carboxyl terminus of Omi has extensive
      homology to a mammalian protein called L56 (human HtrA), but unlike L56, which is
      secreted, Omi is localized in the endoplasmic reticulum. Omi has several novel
      putative protein-protein interaction motifs, as well as a PDZ domain and a Src
      homology 3-binding domain. Omi mRNA is expressed ubiquitously, and the gene is
      localized on human chromosome 2p12. Omi interacts with Mxi2, an alternatively
      spliced form of the p38 stress-activated kinase. Omi protein, when made in a
      heterologous system, shows proteolytic activity against a nonspecific substrate
      beta-casein. The proteolytic activity of Omi is markedly up-regulated in the
      mouse kidney following ischemia/reperfusion.
FAU - Faccio, L
AU  - Faccio L
AD  - Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown,
      Massachusetts 02129, USA.
FAU - Fusco, C
AU  - Fusco C
FAU - Chen, A
AU  - Chen A
FAU - Martinotti, S
AU  - Martinotti S
FAU - Bonventre, J V
AU  - Bonventre JV
FAU - Zervos, A S
AU  - Zervos AS
LA  - eng
SI  - GENBANK/AF020760
GR  - R01 DK55734-01/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Bacterial Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (Heat-Shock Proteins)
RN  - 0 (Mitochondrial Proteins)
RN  - 0 (Periplasmic Proteins)
RN  - 0 (Recombinant Proteins)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
RN  - EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases)
RN  - EC 3.4.21.- (DegP protease)
RN  - EC 3.4.21.- (Serine Endopeptidases)
RN  - EC 3.4.21.108 (HTRA2 protein, human)
RN  - EC 3.4.21.108 (High-Temperature Requirement A Serine Peptidase 2)
RN  - EC 3.4.21.108 (Htra2 protein, mouse)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Bacterial Proteins/chemistry/genetics
MH  - Base Sequence
MH  - Catalytic Domain
MH  - DNA, Complementary
MH  - *Gene Expression Regulation, Enzymologic
MH  - Heat-Shock Proteins/chemistry/genetics
MH  - High-Temperature Requirement A Serine Peptidase 2
MH  - Humans
MH  - Hydrolysis
MH  - Ischemia/*genetics
MH  - Kidney/*blood supply
MH  - Mice
MH  - Mitochondrial Proteins
MH  - Mitogen-Activated Protein Kinases/metabolism
MH  - Molecular Sequence Data
MH  - *Periplasmic Proteins
MH  - Recombinant Proteins/chemistry/genetics
MH  - Sequence Homology, Amino Acid
MH  - Serine Endopeptidases/chemistry/*genetics/metabolism
MH  - p38 Mitogen-Activated Protein Kinases
EDAT- 2000/01/25 09:00
MHDA- 2000/03/04 09:00
CRDT- 2000/01/25 09:00
PHST- 2000/01/25 09:00 [pubmed]
PHST- 2000/03/04 09:00 [medline]
PHST- 2000/01/25 09:00 [entrez]
AID - 10.1074/jbc.275.4.2581 [doi]
AID - S0021-9258(18)31012-3 [pii]
PST - ppublish
SO  - J Biol Chem. 2000 Jan 28;275(4):2581-8. doi: 10.1074/jbc.275.4.2581.