ID M7BXM1_CHEMY Unreviewed; 371 AA.
AC M7BXM1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Ferroptosis suppressor protein 1 {ECO:0000256|ARBA:ARBA00040253};
DE AltName: Full=Apoptosis-inducing factor homologous mitochondrion-associated inducer of death {ECO:0000256|ARBA:ARBA00041541};
DE AltName: Full=p53-responsive gene 3 protein {ECO:0000256|ARBA:ARBA00042318};
DE Flags: Fragment;
GN ORFNames=UY3_02185 {ECO:0000313|EMBL:EMP40585.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP40585.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + phylloquinone = NAD(+) + phylloquinol;
CC Xref=Rhea:RHEA:74075, ChEBI:CHEBI:15378, ChEBI:CHEBI:18067,
CC ChEBI:CHEBI:28433, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000256|ARBA:ARBA00036360};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74076;
CC Evidence={ECO:0000256|ARBA:ARBA00036360};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + ubiquinone-10 = NAD(+) + ubiquinol-10;
CC Xref=Rhea:RHEA:61984, ChEBI:CHEBI:15378, ChEBI:CHEBI:46245,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:64183;
CC Evidence={ECO:0000256|ARBA:ARBA00036802};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61985;
CC Evidence={ECO:0000256|ARBA:ARBA00036802};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + menadione + NADH = menadiol + NAD(+);
CC Xref=Rhea:RHEA:69695, ChEBI:CHEBI:6746, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28869, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000256|ARBA:ARBA00036047};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69696;
CC Evidence={ECO:0000256|ARBA:ARBA00036047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + menaquinone-4 + NADH = menaquinol-4 + NAD(+);
CC Xref=Rhea:RHEA:74079, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:78277, ChEBI:CHEBI:193091;
CC Evidence={ECO:0000256|ARBA:ARBA00036254};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74080;
CC Evidence={ECO:0000256|ARBA:ARBA00036254};
CC -!- COFACTOR:
CC Name=6-hydroxy-FAD; Xref=ChEBI:CHEBI:60470;
CC Evidence={ECO:0000256|ARBA:ARBA00037027};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Lipid droplet
CC {ECO:0000256|ARBA:ARBA00004502}. Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004325}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006442}.
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DR EMBL; KB508622; EMP40585.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BXM1; -.
DR STRING; 8469.M7BXM1; -.
DR eggNOG; KOG1336; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.100; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR PANTHER; PTHR43735; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43735:SF3; FERROPTOSIS SUPPRESSOR PROTEIN 1; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443}.
FT DOMAIN 12..296
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMP40585.1"
SQ SEQUENCE 371 AA; 40492 MW; 05F297D56B143201 CRC64;
MGSKLSVDDS VRVVIVGGGF GGIAAARQLK SWGIPFVLVD MRDAFHHNVG ALRASVESGF
AKKTFISYSV TFEESFRQAK VVGIDLLRQK VLLNDNEELF YSHLILATGS DGPFPGKFNQ
IIDMETAIQT YEDMVKEKSP RIVIVGGGAA GVEMAAEIKT EYPAKEVTLI HSKIALADVE
LLPSVRQVVK EILLRKEVHL LLSDRVSNLH MLTLNRFQEN MAVKTEKGIE VAADMVILCT
GIKINSSAYS SAFGDKLAGN GALKVNQYLQ VEGYDNIYAI GDCADVKEPK MAYHAGLHAN
IVVTNIINSL TQKPLKTYQP GSLTFLLSMG RNDGVGQING CYVGRLLVTI AKSRDLFVSK
SWETMGQTMP C
//
