FTSH3_ARATH
ID FTSH3_ARATH Reviewed; 809 AA.
AC Q84WU8; O81076; Q0WWR8; Q8VZR5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 3, mitochondrial;
DE Short=AtFTSH3;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=FTSH3; OrderedLocusNames=At2g29080; ORFNames=T9I4.16;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 471-796.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11299370; DOI=10.1104/pp.125.4.1912;
RA Adam Z., Adamska I., Nakabayashi K., Ostersetzer O., Haussuhl K.,
RA Manuell A., Zheng B., Vallon O., Rodermel S.R., Shinozaki K., Clarke A.K.;
RT "Chloroplast and mitochondrial proteases in Arabidopsis. A proposed
RT nomenclature.";
RL Plant Physiol. 125:1912-1918(2001).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=14630971; DOI=10.1105/tpc.017319;
RA Sakamoto W., Zaltsman A., Adam Z., Takahashi Y.;
RT "Coordinated regulation and complex formation of yellow variegated1 and
RT yellow variegated2, chloroplastic FtsH metalloproteases involved in the
RT repair cycle of photosystem II in Arabidopsis thylakoid membranes.";
RL Plant Cell 15:2843-2855(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14996218; DOI=10.1111/j.1365-313x.2003.02014.x;
RA Yu F., Park S., Rodermel S.R.;
RT "The Arabidopsis FtsH metalloprotease gene family: interchangeability of
RT subunits in chloroplast oligomeric complexes.";
RL Plant J. 37:864-876(2004).
RN [9]
RP INDUCTION BY HEAT AND HIGH LIGHT.
RX PubMed=15266057; DOI=10.1104/pp.104.043299;
RA Sinvany-Villalobo G., Davydov O., Ben-Ari G., Zaltsman A., Raskind A.,
RA Adam Z.;
RT "Expression in multigene families. Analysis of chloroplast and
RT mitochondrial proteases.";
RL Plant Physiol. 135:1336-1345(2004).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RA Kolodziejczak M., Gibala M., Urantowka A., Janska H.;
RT "The significance of Arabidopsis AAA proteases for activity and
RT assembly/stability of mitochondrial OXPHOS complexes.";
RL Physiol. Plantarum 129:135-142(2007).
CC -!- FUNCTION: Probable ATP-dependent zinc metallopeptidase. Involved in the
CC assembly and/or stability of the complexes I and V of the mitochondrial
CC oxidative phosphorylation system. {ECO:0000269|Ref.10}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:14671022,
CC ECO:0000269|Ref.10}; Single-pass membrane protein
CC {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:14671022,
CC ECO:0000269|Ref.10}; Matrix side {ECO:0000269|PubMed:14630971,
CC ECO:0000269|PubMed:14671022, ECO:0000269|Ref.10}.
CC -!- INDUCTION: By heat and high light. {ECO:0000269|PubMed:15266057}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC33234.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC005315; AAC33234.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC08208.1; -; Genomic_DNA.
DR EMBL; BT002743; AAO22572.1; -; mRNA.
DR EMBL; AY063914; AAL36270.1; -; mRNA.
DR EMBL; AK226271; BAE98430.1; -; mRNA.
DR PIR; T02738; T02738.
DR RefSeq; NP_850129.1; NM_179798.2.
DR AlphaFoldDB; Q84WU8; -.
DR SMR; Q84WU8; -.
DR BioGRID; 2806; 3.
DR STRING; 3702.AT2G29080.1; -.
DR MEROPS; M41.022; -.
DR SwissPalm; Q84WU8; -.
DR PaxDb; Q84WU8; -.
DR PRIDE; Q84WU8; -.
DR ProteomicsDB; 228919; -.
DR EnsemblPlants; AT2G29080.1; AT2G29080.1; AT2G29080.
DR GeneID; 817456; -.
DR Gramene; AT2G29080.1; AT2G29080.1; AT2G29080.
DR KEGG; ath:AT2G29080; -.
DR Araport; AT2G29080; -.
DR TAIR; locus:2066128; AT2G29080.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_23_2_1; -.
DR InParanoid; Q84WU8; -.
DR OMA; GFHNDER; -.
DR OrthoDB; 217929at2759; -.
DR PhylomeDB; Q84WU8; -.
DR BRENDA; 3.4.24.B20; 399.
DR PRO; PR:Q84WU8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q84WU8; baseline and differential.
DR Genevisible; Q84WU8; AT.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005745; C:m-AAA complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
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; ISS:TAIR.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Protease;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Zinc.
FT TRANSIT 1..83
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 84..809
FT /note="ATP-dependent zinc metalloprotease FTSH 3,
FT mitochondrial"
FT /id="PRO_0000341329"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 93..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..809
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 587
FT /evidence="ECO:0000250"
FT BINDING 362..369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 586
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 590
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 662
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 155
FT /note="E -> D (in Ref. 3; AAL36270)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="T -> A (in Ref. 4; BAE98430)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="A -> P (in Ref. 3; AAL36270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 809 AA; 89353 MW; 2A54BBC8F8786429 CRC64;
MTMIFFSKLN RSISRSKGFL YGGGVRSAAR LLTSPGLEAA SVNEVEGGLG FIRRHFASLA
SRKGLVNNDL IGVFANPRLR RFFSDEAPKK KNYENYFPKD KQEPKSDQKS EHKEGSEKNE
NENVGDMFMN RFQNLLIPLL ALAVFFSTFS FGSGEQQQIS FQEFKNKLLE PGLVDHIDVS
NKSVAKVYVR STPKDQQTTD VVHGNGNGIP AKRTGGQYKY YFNIGSVDSF EEKLEEAQEA
LGVDRHEYVP VTYVSEMVWY QEFMRFAPTL LLLGTLIYGA RRMQGGLGVG GTGGKNGRGI
FNIGKATITR ADKHSKNKIY FKDVAGCDEA KQEIMEFVHF LKNPKKYEDL GAKIPKGALL
VGPPGTGKTL LAKATAGESG VPFLSISGSD FMEMFVGVGP SRVRHLFQEA RQAAPSIIFI
DEIDAIGRAR GRGGLGGNDE RESTLNQLLV EMDGFGTTAG VVVLAGTNRP DILDKALLRP
GRFDRQITID KPDIKGRDQI FKIYLKKIKL DHEPSYYSQR LAALTPGFAG ADIANVCNEA
ALIAARHEGA TVTMAHFESA IDRVIGGLEK KNRVISKLER RTVAYHESGH AVVGWFLEHA
EPLLKVTIVP RGTAALGFAQ YVPNENLLMT KEQLFDMTCM TLGGRAAEQV LIGKISTGAQ
NDLEKVTKMT YAQVAVYGFS DKVGLLSFPP RDDGYDFSKP YSNKTGAIID EEVRDWVAKA
YERTVELVEE HKVKVAEIAE LLLEKEVLHQ DDLLKILGER PFKSAEVTNY DRFKSGFEET
EKDSAATPTV EPVVDDGAPP PFEPQVVPT
