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Mitochondrial respiratory chain complexes assembly protein AFG3 (EC 3.4.24.-) (ATPase family gene 3 protein) (Tat-binding homolog 10)

 AFG3_YEAST              Reviewed;         761 AA.
P39925; D3DLR5;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
05-DEC-2018, entry version 184.
RecName: Full=Mitochondrial respiratory chain complexes assembly protein AFG3;
EC=3.4.24.-;
AltName: Full=ATPase family gene 3 protein;
AltName: Full=Tat-binding homolog 10;
Name=AFG3; Synonyms=YTA10; OrderedLocusNames=YER017C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7754704; DOI=10.1002/yea.320100903;
Schnall R., Mannhaupt G., Stucka R., Tauer R., Ehnle S.,
Schwarzlose C., Vetter I., Feldmann H.;
"Identification of a set of yeast genes coding for a novel family of
putative ATPases with high similarity to constituents of the 26S
protease complex.";
Yeast 10:1141-1155(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=S288c / YPH1;
PubMed=7900428; DOI=10.1002/yea.320101016;
Guelin E.J.M., Rep M., Grivell L.A.;
"Sequence of the AFG3 gene encoding a new member of the FtsH/Yme1/Tma
subfamily of the AAA-protein family.";
Yeast 10:1389-1394(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169868;
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
IDENTIFICATION IN THE M-AAA PROTEASE COMPLEX, FUNCTION OF THE M-AAA
PROTEASE COMPLEX, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=8681382; DOI=10.1016/S0092-8674(00)81271-4;
Arlt H., Tauer R., Feldmann H., Neupert W., Langer T.;
"The YTA10-12 complex, an AAA protease with chaperone-like activity in
the inner membrane of mitochondria.";
Cell 85:875-885(1996).
[6]
FUNCTION OF THE M-AAA PROTEASE COMPLEX, AND MUTAGENESIS OF GLU-559.
PubMed=9707443; DOI=10.1093/emboj/17.16.4837;
Arlt H., Steglich G., Perryman R., Guiard B., Neupert W., Langer T.;
"The formation of respiratory chain complexes in mitochondria is under
the proteolytic control of the m-AAA protease.";
EMBO J. 17:4837-4847(1998).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
-!- FUNCTION: Acts as a component of the m-AAA protease complex which
is a ATP-dependent metalloprotease mediating degradation of non-
assembled mitochondrial inner membrane proteins. The complex is
necessary for the assembly of mitochondrial respiratory chain and
ATPase complexes. Function both in post-translational assembly and
in the turnover of mistranslated or misfolded polypeptides.
{ECO:0000269|PubMed:8681382, ECO:0000269|PubMed:9707443}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
Note=Binds 1 zinc ion per subunit. {ECO:0000305};
-!- SUBUNIT: Component of the 850 kDa m-AAA protease complex (YTA10-
12) which consists of multiple copies of RCA1 AND AFG3.
{ECO:0000269|PubMed:8681382}.
-!- INTERACTION:
P40341:YTA12; NbExp=3; IntAct=EBI-2317, EBI-14858;
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:8681382}; Multi-pass membrane protein
{ECO:0000269|PubMed:8681382}.
-!- MISCELLANEOUS: Present with 3870 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the peptidase
M41 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X81066; CAA56953.1; -; Genomic_DNA.
EMBL; X76643; CAA54091.1; -; Genomic_DNA.
EMBL; U18778; AAB64550.1; -; Genomic_DNA.
EMBL; BK006939; DAA07669.1; -; Genomic_DNA.
PIR; S46611; S46611.
RefSeq; NP_010933.1; NM_001178908.1.
ProteinModelPortal; P39925; -.
SMR; P39925; -.
BioGrid; 36750; 179.
ComplexPortal; CPX-1654; m-AAA complex.
DIP; DIP-802N; -.
IntAct; P39925; 23.
MINT; P39925; -.
STRING; 4932.YER017C; -.
MEROPS; M41.002; -.
TCDB; 3.A.29.1.1; the mitochondrial inner membrane i-aaa protease complex (mimp) familly.
MaxQB; P39925; -.
PaxDb; P39925; -.
PRIDE; P39925; -.
EnsemblFungi; YER017C_mRNA; YER017C_mRNA; YER017C.
GeneID; 856737; -.
KEGG; sce:YER017C; -.
SGD; S000000819; AFG3.
GeneTree; ENSGT00940000173525; -.
HOGENOM; HOG000217277; -.
InParanoid; P39925; -.
KO; K08956; -.
OMA; MNKRWRN; -.
OrthoDB; EOG092C147V; -.
BioCyc; YEAST:G3O-30202-MONOMER; -.
PRO; PR:P39925; -.
Proteomes; UP000002311; Chromosome V.
GO; GO:0005745; C:m-AAA complex; IDA:SGD.
GO; GO:0097002; C:mitochondrial inner boundary membrane; IDA:SGD.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:SGD.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008237; F:metallopeptidase activity; IMP:SGD.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0034622; P:cellular protein-containing complex assembly; IMP:SGD.
GO; GO:0042407; P:cristae formation; IBA:GO_Central.
GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
GO; GO:0008053; P:mitochondrial fusion; IBA:GO_Central.
GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:SGD.
GO; GO:0006508; P:proteolysis; IMP:SGD.
GO; GO:0001302; P:replicative cell aging; IMP:SGD.
GO; GO:0006465; P:signal peptide processing; IMP:SGD.
HAMAP; MF_01458; FtsH; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR005936; FtsH.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR011546; Pept_M41_FtsH_extracell.
InterPro; IPR000642; Peptidase_M41.
InterPro; IPR037219; Peptidase_M41-like.
Pfam; PF00004; AAA; 1.
Pfam; PF06480; FtsH_ext; 1.
Pfam; PF01434; Peptidase_M41; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF140990; SSF140990; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01241; FtsH_fam; 1.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Mitochondrion; Mitochondrion inner membrane;
Nucleotide-binding; Protease; Reference proteome; Transmembrane;
Transmembrane helix; Zinc.
CHAIN 1 761 Mitochondrial respiratory chain complexes
assembly protein AFG3.
/FTId=PRO_0000084670.
TOPO_DOM 1 115 Mitochondrial matrix.
{ECO:0000269|PubMed:8681382}.
TRANSMEM 116 136 Helical. {ECO:0000255}.
TOPO_DOM 137 223 Mitochondrial intermembrane.
{ECO:0000269|PubMed:8681382}.
TRANSMEM 224 244 Helical. {ECO:0000255}.
TOPO_DOM 245 761 Mitochondrial matrix.
{ECO:0000269|PubMed:8681382}.
NP_BIND 328 335 ATP. {ECO:0000255}.
ACT_SITE 559 559 {ECO:0000250|UniProtKB:Q9WZ49}.
METAL 558 558 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q9WZ49}.
METAL 562 562 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q9WZ49}.
METAL 634 634 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q9WZ49}.
MUTAGEN 559 559 E->Q: Abolishes proteolytic activity;
impairs synthesis of respiratory chain
proteins COB and COX1. No effect on m-AAA
protease assembly.
{ECO:0000269|PubMed:9707443}.
CONFLICT 411 411 A -> R (in Ref. 1; CAA54091).
{ECO:0000305}.
SEQUENCE 761 AA; 84544 MW; 517C1F0E81ABE841 CRC64;
MMMWQRYARG APRSLTSLSF GKASRISTVK PVLRSRMPVH QRLQTLSGLA TRNTIHRSTQ
IRSFHISWTR LNENRPNKEG EGKNNGNKDN NSNKEDGKDK RNEFGSLSEY FRSKEFANTM
FLTIGFTIIF TLLTPSSNNS GDDSNRVLTF QDFKTKYLEK GLVSKIYVVN KFLVEAELVN
TKQVVSFTIG SVDIFEEQMD QIQDLLNIPP RDRIPIKYIE RSSPFTFLFP FLPTIILLGG
LYFITRKINS SPPNANGGGG GGLGGMFNVG KSRAKLFNKE TDIKISFKNV AGCDEAKQEI
MEFVHFLKNP GKYTKLGAKI PRGAILSGPP GTGKTLLAKA TAGEANVPFL SVSGSEFVEM
FVGVGASRVR DLFTQARSMA PSIIFIDEID AIGKERGKGG ALGGANDERE ATLNQLLVEM
DGFTTSDQVV VLAGTNRPDV LDNALMRPGR FDRHIQIDSP DVNGRQQIYL VHLKRLNLDP
LLTDDMNNLS GKLATLTPGF TGADIANACN EAALIAARHN DPYITIHHFE QAIERVIAGL
EKKTRVLSKE EKRSVAYHEA GHAVCGWFLK YADPLLKVSI IPRGQGALGY AQYLPPDQYL
ISEEQFRHRM IMALGGRVSE ELHFPSVTSG AHDDFKKVTQ MANAMVTSLG MSPKIGYLSF
DQNDGNFKVN KPFSNKTART IDLEVKSIVD DAHRACTELL TKNLDKVDLV AKELLRKEAI
TREDMIRLLG PRPFKERNEA FEKYLDPKSN TEPPEAPAAT N


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