ID   AFG1L_RAT               Reviewed;         480 AA.
AC   Q32PX9;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=AFG1-like ATPase {ECO:0000312|RGD:1561501};
DE            EC=3.6.-.- {ECO:0000305};
DE   AltName: Full=Lactation elevated protein 1 {ECO:0000312|RGD:1561501};
GN   Name=Afg1l {ECO:0000312|RGD:1561501};
GN   Synonyms=Lace1 {ECO:0000312|RGD:1561501};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Putative mitochondrial ATPase. Plays a role in mitochondrial
CC       morphology and mitochondrial protein metabolism. Promotes degradation
CC       of excess nuclear-encoded complex IV subunits (COX4I1, COX5A and
CC       COX6A1) and normal activity of complexes III and IV of the respiratory
CC       chain. Mediates mitochondrial translocation of TP53 and its
CC       transcription-independent apoptosis in response to genotoxic stress.
CC       {ECO:0000250|UniProtKB:Q8WV93}.
CC   -!- SUBUNIT: Found in several complexes of 140-500 kDa. Interacts with
CC       YME1L1. Interacts with COX4I1. Interacts with COX5A. Interacts with
CC       TP53; mediates mitochondrial translocation of TP53 in response to
CC       genotoxic stress such as mitomycin C treatment.
CC       {ECO:0000250|UniProtKB:Q8WV93}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000250|UniProtKB:Q8WV93}.
CC   -!- SIMILARITY: Belongs to the AFG1 ATPase family. {ECO:0000305}.
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DR   EMBL; BC107937; AAI07938.1; -; mRNA.
DR   RefSeq; NP_001032745.1; NM_001037656.1.
DR   AlphaFoldDB; Q32PX9; -.
DR   PRIDE; Q32PX9; -.
DR   GeneID; 502479; -.
DR   KEGG; rno:502479; -.
DR   CTD; 246269; -.
DR   RGD; 1561501; Afg1l.
DR   InParanoid; Q32PX9; -.
DR   OrthoDB; 702840at2759; -.
DR   PhylomeDB; Q32PX9; -.
DR   PRO; PR:Q32PX9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; ISO:RGD.
DR   GO; GO:0035694; P:mitochondrial protein catabolic process; ISO:RGD.
DR   GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR005654; ATPase_AFG1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12169; PTHR12169; 1.
DR   Pfam; PF03969; AFG1_ATPase; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Hydrolase; Membrane; Mitochondrion; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..480
FT                   /note="AFG1-like ATPase"
FT                   /id="PRO_0000279523"
FT   BINDING         136..143
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WV93"
FT   BINDING         209..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WV93"
SQ   SEQUENCE   480 AA;  54503 MW;  8DC00876D759A1E0 CRC64;
     MAASWSPLVT LRSAARSRLT GRGVGCGARV IAIFPPAPGP RKPLWKAYTV QTLEGVRPTA
     ASEAHSRALA VCHGPLAHYD FLIKAQELKN DEHQRRVVQC LQKLQEDLKG YNIEEGGLFS
     KLFSRNKPPK GLYVYGDVGT GKTMVMDMFY EYVEVKSKRR VHFHGFMLDV HKRIHRLKQS
     LPKRKVGFMA KSYDPIAPIA EEISQEASLL CFDEFQVTDI ADAMILKQLF ENLFKNGVVV
     VATSNRPPED LYKNGLQRAN FVPFIAVLKE YCNTVQLDSG VDYRKRELTP AGKLYYLTSE
     ADVGTVMDKL FDELAQKQND LTSPRILKVQ GRELRLNKAC GTVADCTFEE LCERPLGASD
     YLELSKNFDT VIIRNIPQFS LAKRTQVRRF ITLIDNFYDF KVRIICSASV PISSLFVYQH
     QDSESDQSRV LMDDLGLSQD SAGLSMFTGE EEIFSFQRTL SRLTEMQTEQ YWIEGDRSRK