ID C3ZD98_BRAFL Unreviewed; 353 AA.
AC C3ZD98;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=BRAFLDRAFT_206673 {ECO:0000313|EMBL:EEN49453.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN49453.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN49453.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN49453.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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: 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; GG666612; EEN49453.1; -; Genomic_DNA.
DR RefSeq; XP_002593442.1; XM_002593396.1.
DR AlphaFoldDB; C3ZD98; -.
DR STRING; 7739.C3ZD98; -.
DR eggNOG; KOG1336; Eukaryota.
DR InParanoid; C3ZD98; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
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; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 2..279
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEN49453.1"
SQ SEQUENCE 353 AA; 39045 MW; 3A9936F2C9AAA4CE CRC64;
YAGIAIARKL QGKINFTLID PKECFHHHIG ALRSAVRTDF AKKTFIPYDA TFGKRFKQGR
VKDVNTSDRT IILETGETIS YTHLVIATGC TGPFPGRVDD TITTDEAISR YNNLAEQIET
ADKIVIVGGG VAGIELTGEI LSAHKNKNVT LIHAHQHLIN DDVLPGMRTK LHEKLARYGV
TFILDERVKN LEEVATNVSK PTTVKTDAGT EVSADLVIRC TGVKPNTAVF TNNLGGKLDD
SGRLKVNELF EVDGLEHVYA IGECNDVAEV KMPRHSTAQG ELLAENIVRK LDNKEMKPHT
HGQLMMEISL GPNAGVSQVK GLILGSFLTK YRKSKDLFVH RFWKKVMKQE VPH
//
