LONM_ORYSI
ID LONM_ORYSI Reviewed; 1002 AA.
AC A2YQ56; Q4ZJ72;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Lon protease homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03120};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
GN ORFNames=OsI_27415;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Lin C.-F., Su W., Yang J.-S.;
RT "Molecular cloning and characterization of OsLON1, a novel LON protease
RT gene from Oryza sativa.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of misfolded, unassembled or oxidatively damaged
CC polypeptides as well as certain short-lived regulatory proteins in the
CC mitochondrial matrix. May also have a chaperone function in the
CC assembly of inner membrane protein complexes. Participates in the
CC regulation of mitochondrial gene expression and in the maintenance of
CC the integrity of the mitochondrial genome. Binds to mitochondrial DNA
CC in a site-specific manner. {ECO:0000255|HAMAP-Rule:MF_03120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03120};
CC -!- SUBUNIT: Homohexamer or homoheptamer. Organized in a ring with a
CC central cavity. {ECO:0000255|HAMAP-Rule:MF_03120}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2YQ56-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2YQ56-2; Sequence=VSP_039540;
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
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DR EMBL; DQ004688; AAY21162.1; -; mRNA.
DR EMBL; CM000132; EAZ05217.1; -; Genomic_DNA.
DR AlphaFoldDB; A2YQ56; -.
DR SMR; A2YQ56; -.
DR STRING; 39946.A2YQ56; -.
DR EnsemblPlants; BGIOSGA023678-TA; BGIOSGA023678-PA; BGIOSGA023678. [A2YQ56-1]
DR Gramene; BGIOSGA023678-TA; BGIOSGA023678-PA; BGIOSGA023678. [A2YQ56-1]
DR HOGENOM; CLU_004109_2_0_1; -.
DR OMA; YVGPPIY; -.
DR Proteomes; UP000007015; Chromosome 7.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0070407; P:oxidation-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03120; lonm_euk; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR004815; Lon_bac/euk-typ.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027503; Lonm_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR43718; PTHR43718; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00763; lon; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; DNA-binding; Hydrolase; Mitochondrion;
KW Nucleotide-binding; Protease; Reference proteome; Serine protease.
FT CHAIN 1..1002
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000395766"
FT DOMAIN 102..311
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 811..995
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 901
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 944
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 468..475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT VAR_SEQ 742..767
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039540"
FT CONFLICT 735
FT /note="K -> N (in Ref. 1; AAY21162)"
FT /evidence="ECO:0000305"
FT CONFLICT 848
FT /note="L -> M (in Ref. 1; AAY21162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1002 AA; 109539 MW; 6B1BF2FD47B4541D CRC64;
MLRAAAAAAA VFPSRFAAAP AVAAVEEVRS PLLRVLGALR GGRVSTLGRR ARFCSNSAGS
DSEAAAAEAK AEDAVAAEGE ADGKASSAIV PTVLRPEDCL SVIALPLPHR PLFPGFYMPI
YVKDQKLLQA LVENRKRSIP YAGAFLVKDE EGTDPNIVTS SDSDKSIDDL KGKELLQRLN
EVGTLAQITS IQGDQVVLLG HRRLKITEMV QEDPLTVKVD HLKEKPYDKD DDVIKATSFE
VISTLREVLK ASSLWKDHVQ TYTQHMGDFN YPRLADFGAA ISGANKFLCQ EVLEELDVYK
RLKLTLELVK KEMEISKLQQ SIAKAIEEKI SGDQRRYLLN EQLKAIKKEL GLETDDKTAL
SAKFRERIEA KKEKCPAHVL QVIEEELTKL QLLEASSSEF NVTRNYLDWL TVLPWGNYSD
ENFDVHHAQQ ILDEDHYGLS DVKERILEFI AVGKLRGTSQ GKIICLSGPP GVGKTSIGRS
IARALNRKFY RFSVGGLADV AEIKGHRRTY VGAMPGKMVQ CLKSVGTANP LVLIDEIDKL
GRGHSGDPAS ALLELLDPEQ NVNFLDHYLD VPIDLSKVLF VCTANVIEMI PNPLLDRMEI
IAIAGYITDE KMHIARDYLE KNTREACGIK PEQAEVTDAA LLALIESYCR EAGVRNLQKQ
IEKIYRKIAL QLVRQGVSNE PTQEAAIVTA SEEPNGGDSA NKLKDETMED PATENAAMTN
ADTASKEASE LDLLKRTVDH DVHPAETPKE AVLTDSALST DKLCTPEGNK DMEGAKEESA
DKAVEKVVID SSNLGDYVGK PVFQAERIYE QTPVGVVMGL AWTAMGGSTL YIETTKVEEG
DGKGALVLTG QLGDVMKESA QIAHTVGRAI LLDKEPENLF FANSKVHLHV PAGSTPKDGP
SAGCTMITSM LSLAMGKPVK KDLAMTGEVT LTGRILPIGG VKEKTIAARR SAVKTIVFPA
ANKRDFDELA PNVKEGLEVH FVDTYNEIFD IAFQSETQTE TS
