ID G1KUD7_ANOCA Unreviewed; 373 AA.
AC G1KUD7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Ferroptosis suppressor protein 1 {ECO:0000256|ARBA:ARBA00040253};
DE EC=1.4.3.2 {ECO:0000256|ARBA:ARBA00012806};
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=aifm2 {ECO:0000313|Ensembl:ENSACAP00000017515.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000017515.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000017515.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000017515.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000017515.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000256|ARBA:ARBA00005465}.
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DR RefSeq; XP_003218521.1; XM_003218473.3.
DR AlphaFoldDB; G1KUD7; -.
DR STRING; 28377.ENSACAP00000017515; -.
DR Ensembl; ENSACAT00000017860.4; ENSACAP00000017515.3; ENSACAG00000017786.4.
DR GeneID; 100551529; -.
DR KEGG; acs:100551529; -.
DR CTD; 84883; -.
DR eggNOG; KOG1336; Eukaryota.
DR GeneTree; ENSGT00390000004582; -.
DR HOGENOM; CLU_019845_2_1_1; -.
DR InParanoid; G1KUD7; -.
DR OrthoDB; 5348355at2759; -.
DR TreeFam; TF329369; -.
DR Proteomes; UP000001646; Chromosome 3.
DR Bgee; ENSACAG00000017786; Expressed in adrenal gland and 12 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
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:0001716; F:L-amino-acid oxidase activity; IEA:UniProtKB-EC.
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; PR00469; PNDRDTASEII.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 12..298
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 373 AA; 40682 MW; ABC42D369EA68806 CRC64;
MGSKVSVDAS VRVVIVGGGF GGIEAALQLH SWEIPFLLVD MRDAFHHNVA ALRASVDSGF
AKKTFISFSV TFKDSFRQGT VVGIDLDKQH VLLNDGEEIF FSHLILATGS DGPFPGKFNQ
VIDMQAAIQT YEDMAKEVQK APRIVIVGGG SAGVEMAAEV KTMYPTKEVA LIHSKIALAD
EELLPRVRQE VKETLIHEGV NLFLGQRVDN LHELTLHQFK ENMVVKTDKG TEMVTDMVIL
CTGIKVNSSA YRSSFINKLA SNGALKVNDH LQVEGYDNIY AIGDCADVKE PKMAYHAGLH
ADVAVTNIIN SLTQKPLKIY TPGSLTFLIS MGSNDGVGQI SGIYIGHFLV TVAKSKDLFV
SKSWKKMGQH MPC
//
