ID A0A3Q4HFR8_NEOBR Unreviewed; 534 AA.
AC A0A3Q4HFR8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Apoptosis-inducing factor 1, mitochondrial-like {ECO:0000313|Ensembl:ENSNBRP00000019283.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000019283.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000019283.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3Q4HFR8; -.
DR Ensembl; ENSNBRT00000019795.1; ENSNBRP00000019283.1; ENSNBRG00000014809.1.
DR GeneTree; ENSGT00940000156455; -.
DR OMA; EVRYERC; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000014809; Expressed in muscle tissue and 9 other cell types or tissues.
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:UP000261580};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 59..385
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 389..515
FT /note="Mitochondrial apoptosis-inducing factor C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14721"
FT REGION 438..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 58083 MW; 2D8C62B7F8D6725B CRC64;
PTHVPTAHMS SGLPGGGGDN LKYALLVGAA SIAGVAYVSK LTVGITPASL KLPSHAPYLL
IGGGTASFAA ARSIRARDPG AKVLIVTDEP DLPYMRPPLS KELWFSDDPS VTETLRFKQW
NGKERSIYFQ PPSFYINPEE LDSVENGGVA VLTGKKVIHM DVRGNKVKLD DDTEISYDKC
LIATGGVPRN LQVIERAGEE VMMRTTLFRK IEDFRSLDKV SRDVKSITII GGGFLGSELA
CALGRRSTES DLEVIQMFPE KGNMGKVLPE YLSNWTTEKV KKEGVKVISE ALVKSVTCND
DKLEIHLKDG RLVKTDHIVT AVGLEPNVDL AKSGGLEVDS DFGGYRVNAE LQARSNIWVA
GDAACFYDIR LGRRRVEHHD HAVVSGRLAG ENMTGANKPY WHQSMFWSDL GPDVGYEAIG
IVDSSLPTVG VFAKATAKDT PKAATEESGT GIRSESETED TATSAVASVT PAPVVENKDD
YGKGVIFYLR DKVVVGIILW NVFNRMPVAR KIIKDGEEHA DLNEVAKLFN IHED
//