ID A0A455B3Y6_PHYMC Unreviewed; 579 AA.
AC A0A455B3Y6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Apoptosis-inducing factor 1, mitochondrial isoform X3 {ECO:0000313|RefSeq:XP_028338731.1};
GN Name=AIFM1 {ECO:0000313|RefSeq:XP_028338731.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028338731.1};
RN [1] {ECO:0000313|RefSeq:XP_028338731.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028338731.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H(+) + NADH = AH2 + NAD(+); Xref=Rhea:RHEA:11356,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000256|ARBA:ARBA00000272};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006442}.
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DR RefSeq; XP_007103107.1; XM_007103045.1.
DR RefSeq; XP_028338731.1; XM_028482930.2.
DR AlphaFoldDB; A0A455B3Y6; -.
DR Proteomes; UP000248484; Chromosome 21.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR029324; AIF_C.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF4; APOPTOSIS-INDUCING FACTOR 1, MITOCHONDRIAL; 1.
DR Pfam; PF14721; AIF_C; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM01353; AIF_C; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 102..427
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 431..560
FT /note="Mitochondrial apoptosis-inducing factor C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14721"
FT REGION 66..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 63076 MW; B138FCA1A60DF2C0 CRC64;
MCNLFQRWHV PLELQMTRQM TSSGASGGKI DNSVLVLIVG LSTIGAGAYA YKTIKDDQKR
YNERISGLGL TPEEKQKRAT SSAPEGEPVP EVRVPSHIPF LLIGGGTAAF AAARSIRARD
PGARVLIVSE DPELPYMRPP LSKELWFSDD PNVTKTLRFK QWNGKERSIY FQPPSFYVSA
QELPHIENGG VAVLTGKKVV QLDVRGNVAK LNDGSQITYE KCLIATGGTP RSLSAIDRAG
AEVKSRTTLF RKIGDFRTLE KISREVKSIT IIGGGFLGSE LACALGRKAR ASGTEVIQLF
PEKGNMGKIL PEYLSNWTME KVRQEGVKVL PSAIVQSVGV SGGRLLIKLK DGRKVETDHI
VAAVGLEPNV ELAKTGGLEI DSDFGGFRVN AELQARSNIW VAGDAACFYD IKLGRRRVEH
HDHAVVSGRL AGENMTGAAK PYWHQSMFWS DLGPDVGYEA IGLVDSSLPT VGVFAKATAQ
DNPKSATEQS GTGIRSESET ESEASEITLP PSSPVVPQAP AQGEDYGKGV IFYLRDKVVV
GIVLWNIFNR MPIARKIIKD GEEHEDLNEV AKLFNIHED
//