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Search results 201 to 246 out of 246 for Vkorc1

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0.019s

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Hits by Strain

Type Details Score
Protein
A0A7T0LYD5
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: false
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Protein
A0A7T8I144
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: false
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Protein
A0A7T0Q2L1
Organism: Mus musculus/domesticus
Length: 88  
Fragment?: true
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Protein
A0A7T8CZF5
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: false
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Protein
A0A0U1RP21
Organism: Mus musculus/domesticus
Length: 112  
Fragment?: false
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Protein
A0A7T8CZX5
Organism: Mus musculus/domesticus
Length: 61  
Fragment?: true
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Protein
A0A7T8D077
Organism: Mus musculus/domesticus
Length: 66  
Fragment?: false
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Protein
A0A7T0Q304
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: false
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Protein
A0A7T8D066
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: false
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Protein
A0A7T0LYF5
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: true
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Protein
A0A7T8D0E1
Organism: Mus musculus/domesticus
Length: 66  
Fragment?: false
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Protein
A0A7T0Q407
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: true
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Protein
A0A7T8I110
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: false
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Protein
A0A7T8CZQ2
Organism: Mus musculus/domesticus
Length: 66  
Fragment?: false
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Protein
A0A7T8D0G3
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: false
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Protein
A0A7T8CZE0
Organism: Mus musculus/domesticus
Length: 94  
Fragment?: true
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Protein
A0A7T8CZS5
Organism: Mus musculus/domesticus
Length: 66  
Fragment?: false
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Protein
A0A7T8CZQ0
Organism: Mus musculus/domesticus
Length: 103  
Fragment?: false
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Protein
A0A7T8CZQ8
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: false
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Protein
G3CE17
Organism: Mus musculus/domesticus
Length: 58  
Fragment?: true
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Protein
A0A7T0Q274
Organism: Mus musculus/domesticus
Length: 54  
Fragment?: true
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Protein
A0A7T8I121
Organism: Mus musculus/domesticus
Length: 58  
Fragment?: true
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Protein
G3CE70
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: false
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Protein
A0A7T8I0U4
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: false
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Protein
A0A7T8I109
Organism: Mus musculus/domesticus
Length: 66  
Fragment?: false
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Protein
A0A7T8CZX1
Organism: Mus musculus/domesticus
Length: 60  
Fragment?: true
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Protein
G3CE58
Organism: Mus musculus/domesticus
Length: 58  
Fragment?: true
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Protein
A0A7T8CZJ9
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: false
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Protein
A0A7T0LYE7
Organism: Mus musculus/domesticus
Length: 156  
Fragment?: false
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Protein
A0A7T8I0T3
Organism: Mus musculus/domesticus
Length: 66  
Fragment?: false
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Protein
A0A7T0LZ78
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: false
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Protein
G3CE24
Organism: Mus musculus/domesticus
Length: 57  
Fragment?: true
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Protein
A0A7T0LZ52
Organism: Mus musculus/domesticus
Length: 36  
Fragment?: true
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Protein
Q0VGU5
Organism: Mus musculus/domesticus
Length: 127  
Fragment?: false
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Publication
16677080 | -
First Author: Oldenburg J
Year: 2006
Journal: Antioxid Redox Signal
Title: Vitamin K epoxide reductase complex subunit 1 (VKORC1): the key protein of the vitamin K cycle.
Volume: 8
Issue: 3-4
Pages: 347-53
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Publication
16270630 | -
First Author: Rost S
Year: 2005
Journal: Thromb Haemost
Title: Site-directed mutagenesis of coumarin-type anticoagulant-sensitive VKORC1: evidence that highly conserved amino acids define structural requirements for enzymatic activity and inhibition by warfarin.
Volume: 94
Issue: 4
Pages: 780-6
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Publication
30050002 | -
 
First Author: Lacombe J
Year: 2018
Journal: Nutrients
Title: VKORC1L1, An Enzyme Mediating the Effect of Vitamin K in Liver and Extrahepatic Tissues.
Volume: 10
Issue: 8
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Publication
24532791 | -
First Author: Tie JK
Year: 2014
Journal: J Biol Chem
Title: Conserved loop cysteines of vitamin K epoxide reductase complex subunit 1-like 1 (VKORC1L1) are involved in its active site regeneration.
Volume: 289
Issue: 13
Pages: 9396-407
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Protein Domain
IPR042406 | VKORC1/VKORC1L1
Type: Family
Description: This entry represents the vitamin K epoxide reductase complex subunit VKORC1 and VKORC1L1 mostly from animals.VKORC1 is an integral membrane protein that catalyzes the reduction of vitamin K 2,3-epoxide and vitamin K to vitamin K hydroquinone, an essential co-factor subsequently used in the γ-carboxylation of glutamic acid residues in blood coagulation enzymes [, ]. All homologues of VKOR contain an active site CXXC motif, which is switched between reduced and disulfide-bonded states during the reaction cycle []. Warfarin, a widely used oral anticoagulant used in medicine as well as rodenticides, inhibits the activity of VKOR, resulting in decreased levels of reduced vitamin K, which is required for the function of several clotting factors []. However, anticoagulation effect of warfarin is significantly associated with polymorphism of certain genes, including VKORC1. Interestingly, in rodents, an adaptive trait appears to have evolved convergently by selection on new or standing genetic polymorphisms in VKORC1 as well as by adaptive introgressive hybridization between species, likely brought about by human-mediated dispersal []. VKORC1L1, a paralogue of VKORC1, is a vitamin K oxidoreductase, which can support γ-carboxylation in vivo [, ].
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Protein Domain
IPR012932 | VKOR
Type: Domain
Description: Vitamin K epoxide reductase (VKOR) recycles vitamin K 2,3-epoxide to vitamin K hydroquinone, a co-factor that is essential for the posttranslational γ-carboxylation of several blood coagulation factors []. VKORC1, the catalytic subunit of the VKOR complex, is a member of a large family of predicted enzymes that are present in vertebrates, Drosophila, plants, bacteria and archaea [, ]. Bacterial VKOR homologues catalyse disulphide bridge formation in secreted proteins by cooperating with a periplasmic, Trx-like redox partner [, ]. In fact, in some plant and bacterial homologues the VKORC1 homologous domain is fused with domains of the thioredoxin family of oxidoreductases []. VKOR is part of a disulphide bond formation pathway that uses electrons from cysteines of newly synthesized proteins to reduce a quinone [].
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Protein Domain
IPR038354 | VKOR_sf
Type: Homologous_superfamily
Description: Vitamin K epoxide reductase (VKOR) recycles vitamin K 2,3-epoxide to vitamin K hydroquinone, a co-factor that is essential for the posttranslational γ-carboxylation of several blood coagulation factors []. VKORC1, the catalytic subunit of the VKOR complex, is a member of a large family of predicted enzymes that are present in vertebrates, Drosophila, plants, bacteria and archaea [, ]. Bacterial VKOR homologues catalyse disulphide bridge formation in secreted proteins by cooperating with a periplasmic, Trx-like redox partner [, ]. In fact, in some plant and bacterial homologues the VKORC1 homologous domain is fused with domains of the thioredoxin family of oxidoreductases []. VKOR is part of a disulphide bond formation pathway that uses electrons from cysteines of newly synthesized proteins to reduce a quinone [].
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Publication
20110994 | -
First Author: Li W
Year: 2010
Journal: Nature
Title: Structure of a bacterial homologue of vitamin K epoxide reductase.
Volume: 463
Issue: 7280
Pages: 507-12
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Publication
18413314 | -
First Author: Singh AK
Year: 2008
Journal: J Biol Chem
Title: Identification of an atypical membrane protein involved in the formation of protein disulfide bonds in oxygenic photosynthetic organisms.
Volume: 283
Issue: 23
Pages: 15762-70
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Publication
18695247 | -
First Author: Dutton RJ
Year: 2008
Journal: Proc Natl Acad Sci U S A
Title: Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation.
Volume: 105
Issue: 33
Pages: 11933-8
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Publication
24477003 | -
 
First Author: Liu S
Year: 2014
Journal: Nat Commun
Title: Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer.
Volume: 5
Pages: 3110
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Publication
15276181 | -
First Author: Goodstadt L
Year: 2004
Journal: Trends Biochem Sci
Title: Vitamin K epoxide reductase: homology, active site and catalytic mechanism.
Volume: 29
Issue: 6
Pages: 289-92
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