Gene

KWMTBOMO15852  Validated by peptides from experiments

Pre Gene Modal

BGIBMGA000064

Annotation

thioredoxin_peroxidase_[Bombyx_mori]

Location

Bomo_Chr26(+):11465913-11468810      View in EpiBrowser

Full name

Thioredoxin-dependent peroxide reductase, mitochondrial      

Alternative Name

Peroxiredoxin-3

Location in the cell

Cytoplasmic   Reliability : 1.294 Mitochondrial   Reliability : 1.457

CDS

ATGTCGTTCATTGTGAAGCAACTAAGTCGAAGTGTACTGTCGCCGGCTTTCAAAGTAGCAAAAAGGATTAATTTTTCTACGACCAGCACTACAAGAGCTCCTAAAGTTCAGAAGCCTGCTCCAGACTTCAGTGCGACAGCAGTTGTCAATGGAGAGTTCAATCAACTTAAACTTTCAGATTTCACGGGAAAATACGTAGTTCTGTTCTTCTATCCATTGGATTTCACATTTGTATGTCCGACAGAGCTCATAGCGTTCAGTGATAAAGCTAAAGACTTTGCTGGAATCGATTGTCAGGTGATTGGAGTGTCCACAGACTCTGAGTTCAGTCATCTCGCATGGATCAACACTCCTAGGAAGGACGGTGGATTGGGAAAAATGGAAATTCCTCTGCTTGCTGATTACAAAAAACAGATTTCAAAAGATTATGATGTATTACTTGATGATGGGTTTGCATTAAGAGGTTTGTTCATAATCGACCGTAATGGCACCCTGCGTCACATGTCGGTGAACGATCTGCCCGTGGGCCGCTCCGTGGACGAGACGCTCCGCCTGGTCAAGGCCTTCCAGTTCGCCGACAAGCACGGAGAGGTGTGCCCGGCCGGCTGGAACCCGGACACCAACGCCGACACCATCAAGCCGAACCCCAAGGACAGTAAAGAATACTTTCAAAAAGCTAATTAA

Protein

MSFIVKQLSRSVLSPAFKVAKRINFSTTSTTRAPKVQKPAPDFSATAVVNGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAWINTPRKDGGLGKMEIPLLADYKKQISKDYDVLLDDGFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQFADKHGEVCPAGWNPDTNADTIKPNPKDSKEYFQKAN

Description

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.

Catalytic Activity

[protein]-dithiol + a hydroperoxide = [protein]-disulfide + an alcohol + H2O

Subunit

Homodimer; disulfide-linked, upon oxidation. 6 homodimers assemble to form a ring-like dodecamer. Interacts with NEK6. Interacts with LRRK2. Interacts with RPS6KC1 (via PX domain).

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.

Similarity

Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.

Keywords

Acetylation   Antioxidant   Complete proteome   Cytoplasm   Disulfide bond   Endosome   Mitochondrion   Oxidoreductase   Peroxidase   Phosphoprotein   Redox-active center   Reference proteome   Transit peptide  

Feature

chain  Thioredoxin-dependent peroxide reductase, mitochondrial

Uniprot

Q1HPQ1   H9IS38   A0A2A4K9S7   A0A2S0RQP8   M1F678   A0A2H1V0P5   + More
A0A212F982   A0A2S0RQQ3   A0A0N1IFB5   I4DJN9   S4PMG0   A0A182IPM1   A0A182M5S1   A0A182W5M8   A0A182RHL3   A0A182UTB3   A0A336MA65   G0T334   Q7QFB6   G1PLH3   A0A182PSV3   A0A182XJX5   A0A182IAV5   A0A336LF43   B0WSI8   A0A1Q3FGF5   A0A084VFR5   A0A3B3C971   A0A2U9CE55   A0A182TU64   A0A3Q1HLD1   A0A1S3AGG9   A0A3B4Z194   A0A1S3WQS8   A0A182K6H4   A0A182YH76   A0A3P8RJW4   A0A3B4YFT6   A0A3P8VR89   A0A146YCT1   A0A3Q2QY50   A0A1L3KPW7   T1T097   A0A0F8BJP3   A0A146PKI7   A0A3B4V6Z5   A0A3Q2ULJ0   G3NFN1   A0A3Q3MEP0   A0A0B4UEZ5   A0A3Q2GBR6   C3KJR7   A0A1U7UMM6   H2MGZ4   A0A1A8FVA5   A0A3P9IFG1   I3JVX4   C1BLW7   A0A2U3V6N3   A0A1A7WPS3   A0A0K2A1S9   A0A1A8KM25   A0A3B4F5Q4   A0A3Q3CQZ2   A0A3P8QIJ0   A0A3P9C177   A0A1A8R9X6   A0A1B0EX70   A0A1A8M8A9   A0A1A8SF65   A0A250XX54   A0A3P9K1U7   A0A3Q1CNI6   A0A3Q3B464   A0A1A8AT07   A0A1A8D6H3   H2V8X4   A0A2J8W6R9   Q5REY3   A0A2I3FZZ1   L5JZR9   A0A3N0XWM8   A0A3B3YF82   A0A087XP21   A0A3B3TJV1   G3WNV4   A0A3P9MZF7   Q16IW1   A0A0S7JIY8   A0A2K6GGM8   A0A2Y9MPW1   A0A286XCF9   A0A3Q3W904   A0A3Q3GGU8   A0A2Y9DIA9   A0A0N9HLK3   M4A0M2   B5X6K7   A0A2K5NHP3   F7H938  

EC Number

1.11.1.15

Pubmed

19121390    22118469    26354079    22651552    23622113    21640832    + More
12364791    14747013    17210077    21993624    24438588    29451363    25244985    24487278    24378678    25835551    25542382    17554307    25186727    28087693    21551351    23258410    21709235    17510324    23542700    17431167   

EMBL

DQ443351    ABF51440.1    BABH01035692    NWSH01000019    PCG80726.1    MF805701    + More
AWA45766.1    JQ285933    AFO67940.1    ODYU01000131    SOQ34389.1    AGBW02009638    OWR50269.1    MF979107    AWA45970.1    KQ461111    KPJ08942.1    AK401507    KQ459144    BAM18129.1    KPJ03608.1    GAIX01003570    JAA88990.1    AXCM01002712    UFQT01000555    SSX25257.1    GQ252681    ADI78066.1    AAAB01008846    EAA06406.3    AAPE02042232    APCN01001346    UFQS01004076    UFQT01004076    SSX16159.1    SSX35485.1    DS232072    EDS33918.1    GFDL01008412    JAV26633.1    ATLV01012458    KE524793    KFB36809.1    CP026257    AWP14350.1    GCES01034363    JAR51960.1    KU207097    APG79659.1    KC990696    KF270681    AGT56738.1    AGW80514.1    KQ042804    KKF10455.1    GCES01141934    JAQ44388.1    KM370333    AJC98155.1    BT083182    ACQ58889.1    HAEB01015527    HAEC01001294    SBQ62054.1    AERX01006552    AERX01006553    BT075596    ACO10020.1    HADW01006134    HADX01009574    SBP07534.1    KR905163    AKZ42351.1    HAEE01013405    SBR33455.1    HAEH01015333    SBS02477.1    AJVK01000890    HAEF01012036    HAEG01011003    SBR53195.1    HAEI01013736    SBS16205.1    GFFV01003995    JAV35950.1    HADY01019343    HAEJ01003748    SBP57828.1    HADZ01020705    HAEA01001370    SBQ29850.1    NDHI03003398    PNJ65458.1    CR857380    ADFV01164449    ADFV01164450    ADFV01164451    KB031059    ELK04914.1    RJVU01057857    ROK15673.1    AYCK01011665    AEFK01004544    CH478048    EAT34216.1    GBYX01237987    JAO65174.1    AAKN02003057    KR086406    ALG02339.1    BT046676    ACI66477.1    JSUE03044428   

Proteomes

UP000005204    UP000218220    UP000007151    UP000053240    UP000053268    UP000075880    + More
UP000075883    UP000075920    UP000075900    UP000075903    UP000007062    UP000001074    UP000075885    UP000076407    UP000075840    UP000002320    UP000030765    UP000261560    UP000246464    UP000075902    UP000257200    UP000079721    UP000261400    UP000075881    UP000076408    UP000265080    UP000261360    UP000265120    UP000265000    UP000261420    UP000007635    UP000261640    UP000265020    UP000189704    UP000001038    UP000265200    UP000005207    UP000245320    UP000261460    UP000264840    UP000265100    UP000265160    UP000092462    UP000265180    UP000257160    UP000264800    UP000005226    UP000001595    UP000001073    UP000010552    UP000261480    UP000028760    UP000261500    UP000007648    UP000242638    UP000008820    UP000233160    UP000248483    UP000005447    UP000261620    UP000261660    UP000248480    UP000002852    UP000087266    UP000233060    UP000006718   

PRIDE

Q1HPQ1    H9IS38    I3JVX4    Q5REY3   

Pfam

PF10417   1-cysPrx_C        + More
PF00578   AhpC-TSA

Interpro

IPR036249   Thioredoxin-like_sf        + More
IPR024706   Peroxiredoxin_AhpC-typ       
IPR000866   AhpC/TSA       
IPR013766   Thioredoxin_domain       
IPR019479   Peroxiredoxin_C       

SUPFAM

SSF52833   SSF52833       

ProteinModelPortal

Q1HPQ1   H9IS38   A0A2A4K9S7   A0A2S0RQP8   M1F678   A0A2H1V0P5   + More
A0A212F982   A0A2S0RQQ3   A0A0N1IFB5   I4DJN9   S4PMG0   A0A182IPM1   A0A182M5S1   A0A182W5M8   A0A182RHL3   A0A182UTB3   A0A336MA65   G0T334   Q7QFB6   G1PLH3   A0A182PSV3   A0A182XJX5   A0A182IAV5   A0A336LF43   B0WSI8   A0A1Q3FGF5   A0A084VFR5   A0A3B3C971   A0A2U9CE55   A0A182TU64   A0A3Q1HLD1   A0A1S3AGG9   A0A3B4Z194   A0A1S3WQS8   A0A182K6H4   A0A182YH76   A0A3P8RJW4   A0A3B4YFT6   A0A3P8VR89   A0A146YCT1   A0A3Q2QY50   A0A1L3KPW7   T1T097   A0A0F8BJP3   A0A146PKI7   A0A3B4V6Z5   A0A3Q2ULJ0   G3NFN1   A0A3Q3MEP0   A0A0B4UEZ5   A0A3Q2GBR6   C3KJR7   A0A1U7UMM6   H2MGZ4   A0A1A8FVA5   A0A3P9IFG1   I3JVX4   C1BLW7   A0A2U3V6N3   A0A1A7WPS3   A0A0K2A1S9   A0A1A8KM25   A0A3B4F5Q4   A0A3Q3CQZ2   A0A3P8QIJ0   A0A3P9C177   A0A1A8R9X6   A0A1B0EX70   A0A1A8M8A9   A0A1A8SF65   A0A250XX54   A0A3P9K1U7   A0A3Q1CNI6   A0A3Q3B464   A0A1A8AT07   A0A1A8D6H3   H2V8X4   A0A2J8W6R9   Q5REY3   A0A2I3FZZ1   L5JZR9   A0A3N0XWM8   A0A3B3YF82   A0A087XP21   A0A3B3TJV1   G3WNV4   A0A3P9MZF7   Q16IW1   A0A0S7JIY8   A0A2K6GGM8   A0A2Y9MPW1   A0A286XCF9   A0A3Q3W904   A0A3Q3GGU8   A0A2Y9DIA9   A0A0N9HLK3   M4A0M2   B5X6K7   A0A2K5NHP3   F7H938  

PDB

5JCG     E-value=1.51793e-77,     Score=734

KEGG

733003    K20011 peroxiredoxin 3 [EC:1.11.1.15] | (RefSeq) thioredoxin peroxidase

GO

GO:0045454   GO:0051920   GO:0005623   GO:0004601   GO:0008379   GO:0034599   GO:0005737   GO:0005739   GO:0001893   GO:0051881   GO:0051092   GO:0042802   GO:0008022   GO:0042744   GO:0043027   GO:0005829   GO:0008284   GO:0019901   GO:0018171   GO:0032496   GO:0033673   GO:0005769   GO:0042542   GO:0030099   GO:0034614   GO:0032991   GO:0007005   GO:0045321   GO:0006979   GO:0016209   GO:0016491   GO:0005215   GO:0006270   GO:0042555   GO:0003707   GO:0006281   GO:0006259   GO:0055114  

Subcellular location

Mitochondrion   Localizes to early endosomes in a RPS6KC1-dependent manner.   With evidence from 2 publications.
Cytoplasm   Localizes to early endosomes in a RPS6KC1-dependent manner.   With evidence from 2 publications.
Early endosome   Localizes to early endosomes in a RPS6KC1-dependent manner.   With evidence from 2 publications.

Length:

227

Number of predicted TMHs:

0

Exp number of AAs in TMHs:

2.73881

Exp number, first 60 AAs:

0.00064

Total prob of N-in:

0.15869

outside

1  -  227

 

 

Pi

61.996218

Theta

136.911751

Tajima's D

-0.575414

CLR

50.226635

CSRT

0.222288885555722

Interpretation

Uncertain