AFG3_CAEEL
ID AFG3_CAEEL Reviewed; 782 AA.
AC Q9N3T5;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=AFG3-like protein spg-7 {ECO:0000305};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:Q9Y4W6};
GN Name=spg-7 {ECO:0000312|WormBase:Y47G6A.10};
GN ORFNames=Y47G6A.10 {ECO:0000312|WormBase:Y47G6A.10};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21408209; DOI=10.1371/journal.pgen.1002010;
RA Nelson M.D., Zhou E., Kiontke K., Fradin H., Maldonado G., Martin D.,
RA Shah K., Fitch D.H.;
RT "A bow-tie genetic architecture for morphogenesis suggested by a genome-
RT wide RNAi screen in Caenorhabditis elegans.";
RL PLoS Genet. 7:E1002010-E1002010(2011).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22700657; DOI=10.1126/science.1223560;
RA Nargund A.M., Pellegrino M.W., Fiorese C.J., Baker B.M., Haynes C.M.;
RT "Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR
RT activation.";
RL Science 337:587-590(2012).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25274306; DOI=10.1038/nature13818;
RA Pellegrino M.W., Nargund A.M., Kirienko N.V., Gillis R., Fiorese C.J.,
RA Haynes C.M.;
RT "Mitochondrial UPR-regulated innate immunity provides resistance to
RT pathogen infection.";
RL Nature 516:414-417(2014).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25773600; DOI=10.1016/j.molcel.2015.02.008;
RA Nargund A.M., Fiorese C.J., Pellegrino M.W., Deng P., Haynes C.M.;
RT "Mitochondrial and nuclear accumulation of the transcription factor ATFS-1
RT promotes OXPHOS recovery during the UPR(mt).";
RL Mol. Cell 58:123-133(2015).
CC -!- FUNCTION: Acts as a component of the m-AAA protease complex which is an
CC ATP-dependent metalloprotease mediating degradation of non-assembled
CC mitochondrial inner membrane proteins (By similarity). The complex is
CC necessary for the assembly of mitochondrial respiratory chain and
CC ATPase complexes (By similarity). Functions both in post-translational
CC assembly and in the turnover of mistranslated or misfolded polypeptides
CC (PubMed:22700657, PubMed:25274306, PubMed:25773600). Plays a role in
CC male tail tip morphogenesis (PubMed:21408209).
CC {ECO:0000250|UniProtKB:P39925, ECO:0000269|PubMed:21408209,
CC ECO:0000305|PubMed:22700657, ECO:0000305|PubMed:25274306,
CC ECO:0000305|PubMed:25773600}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9WZ49};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9WZ49};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P39925}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P39925}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown disrupts tail tip
CC morphogenesis resulting in retention of the pointed larval tail tip in
CC adult males (also known as the Lep phenotype) (PubMed:21408209). RNAi-
CC mediated knockdown induces nuclear and mitochondrial transcription of
CC mitochondrial protective genes including chaperone hsp-60 as part of
CC the mitochondrial unfolded protein response (PubMed:25773600,
CC PubMed:25274306, PubMed:22700657). RNAi-mediated knockdown causes
CC nuclear accumulation of transcription factor atfs-1 in intestinal cells
CC (PubMed:22700657). RNAi-mediated knockdown results in mitochondria in
CC intestinal cells which are abnormally elongated (PubMed:25274306).
CC RNAi-mediated knockdown reduces oxygen consumption (PubMed:25773600).
CC RNAi-mediated knockdown also induces the transcription of innate
CC immunity-related genes such as lys-2, abf-2, clec-65 and clec-4 which
CC results in resistance to P.aeruginosa-mediated infection
CC (PubMed:25274306). RNAi-mediated knockdown abolishes transcription up-
CC regulation in an atfs-1 (tm4919) mutant background (PubMed:22700657,
CC PubMed:25274306, PubMed:25773600). {ECO:0000269|PubMed:21408209,
CC ECO:0000269|PubMed:22700657, ECO:0000269|PubMed:25274306,
CC ECO:0000269|PubMed:25773600}.
CC -!- MISCELLANEOUS: Despite its gene name, this protein is an ortholog of
CC human AFG3L2 and yeast AFG3 and not of human SPG7 and yeast YTA12
CC (C.elegans ortholog is actually ppgn-1). {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000305}.
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DR EMBL; BX284601; CCD72555.1; -; Genomic_DNA.
DR RefSeq; NP_491165.2; NM_058764.4.
DR AlphaFoldDB; Q9N3T5; -.
DR SMR; Q9N3T5; -.
DR STRING; 6239.Y47G6A.10; -.
DR MEROPS; M41.A10; -.
DR TCDB; 3.A.29.1.2; the mitochondrial inner membrane i-aaa protease complex (mimp) familly.
DR EPD; Q9N3T5; -.
DR PaxDb; Q9N3T5; -.
DR PeptideAtlas; Q9N3T5; -.
DR EnsemblMetazoa; Y47G6A.10.1; Y47G6A.10.1; WBGene00004978.
DR GeneID; 171915; -.
DR KEGG; cel:CELE_Y47G6A.10; -.
DR UCSC; Y47G6A.10; c. elegans.
DR CTD; 171915; -.
DR WormBase; Y47G6A.10; CE34400; WBGene00004978; spg-7.
DR eggNOG; KOG0731; Eukaryota.
DR GeneTree; ENSGT00940000173525; -.
DR HOGENOM; CLU_000688_23_0_1; -.
DR InParanoid; Q9N3T5; -.
DR OMA; DEAYKQC; -.
DR OrthoDB; 217929at2759; -.
DR PhylomeDB; Q9N3T5; -.
DR Reactome; R-CEL-8949664; Processing of SMDT1.
DR PRO; PR:Q9N3T5; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004978; Expressed in adult organism and 5 other tissues.
DR GO; GO:0005745; C:m-AAA complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:WormBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0034982; P:mitochondrial protein processing; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:UniProtKB.
DR GO; GO:0110039; P:positive regulation of nematode male tail tip morphogenesis; IMP:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IGI:UniProtKB.
DR Gene3D; 1.20.58.760; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; SSF140990; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..782
FT /note="AFG3-like protein spg-7"
FT /id="PRO_0000442515"
FT TOPO_DOM 1..118
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P39925"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..230
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P39925"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..782
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P39925"
FT REGION 88..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 560
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
FT BINDING 333..340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT BINDING 559
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
FT BINDING 563
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
FT BINDING 634
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
SQ SEQUENCE 782 AA; 87469 MW; 5F24C34488EFA87A CRC64;
MWRLYRKTPK QLRNSVESCF KSVNSRQFSV SSFSAVAKDD KSVLKQQEVL HLLAKDQRFE
ERFFNQVQQT IRYFASKPND LKKFFRKEAS TDNKESSSSS DKKDSKGNKG EDNNPFNQFP
GGWQQIAVSV GILLALYAFM DYQSYREISW KEFYSDFLEA GLVERLEVVD KRWVRIVSSS
GKYAGQTCYF NIGSVDSFER SLGAAQHHLQ YDADRQIPVL YKSEFNFKRE IPNLISVAFP
LLFGYYIYRM LKGGGAAGGA GRAGGGGLGG MFGGFGQSTA RVINREDIKV KFADVAGCEE
AKIEIMEFVN FLKNPQQYKD LGAKIPKGAI LTGPPGTGKT LLAKATAGEA NVPFITVSGS
EFLEMFVGVG PARVRDMFSM ARKNSPCILF IDEIDAVGRK RGGKGGMGGH SEQENTLNQL
LVEMDGFTTD ESSVIVIAAT NRVDILDSAL LRPGRFDRQI YVPVPDIKGR ASIFRVHLGP
LRTSLDKTVL SRKLAAHTPG FSGADISNVC NEAALIAARD ANHEISNKHF EQAIERVVAG
MEKKTQVLQK EEKKTVAYHE AGHAIAGWFL QHADPLLKVS IIPRGKGLGY AQYLPKEQYL
YSKDQLLDRM CMTLGGRVAE EIFFGRITTG AQDDLQKVTQ MAYSQVVKFG MSEKVGPLSF
ETPAPGEMAF DKPYSEATAQ LIDQEVRDLV MNALRRTRDL LLEKRSDIER VALRLLEKEI
LNREDMIELV GKRPFVEKNT YEEMVSGTGG LDENVELPKG LENWNKESEK KKKDEEKKKN
DE
