ID C1BHM4_ONCMY Unreviewed; 371 AA.
AC C1BHM4;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 39.
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};
GN Name=AMID {ECO:0000313|EMBL:ACO08527.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:ACO08527.1};
RN [1] {ECO:0000313|EMBL:ACO08527.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=White blood cell {ECO:0000313|EMBL:ACO08527.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Yasuike M., von Schalburg K., Cooper G., Leong J., Davidson W.S.,
RA Koop B.F.;
RT "Oncorhynchus mykiss ESTs and full-length cDNAs from White Blood Cells.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; BT074103; ACO08527.1; -; mRNA.
DR RefSeq; NP_001158717.1; NM_001165245.1.
DR AlphaFoldDB; C1BHM4; -.
DR GeneID; 100305340; -.
DR KEGG; omy:100305340; -.
DR CTD; 84883; -.
DR OrthoDB; 5348355at2759; -.
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 2: Evidence at transcript level;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 11..297
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 371 AA; 39789 MW; 8146D28196E5ABD7 CRC64;
MGSQVSVDNV HVVVVGGGFG GTAAAQQLKS RGIPFTLIDL RDAFHHNVAA LRAAVQSGFA
QQTFIPYLKT FGENFLQGRV IWVDPVSQTV ALDGGKEVHY SHLILCTGTD GPFPGKYNMV
ASYQTAIQKY EDIVKEVQAA GSVLVVGGGS TGVEMAAEIK TEYPDKKVIL IHSRVGLADP
ELLPSVRQQA KEVLLEKGVE LLLGQKVSNL SVLELNVTNK NMVIMTDKDT EITADLVICC
TGMKINSDAY SSTLNGCLAE NGSLKVNVHL QVEGYDNVYA VGDCANVNEP KMAYHAGLHA
GVAVANITNS LMGKHLESYH PGSVTMLLAM GHNDGVGQFN GLRLPRCLVT QGKSKNLLLW
KGWKEMGQKA P
//
