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LONM_DROME
ID   LONM_DROME              Reviewed;        1024 AA.
AC   Q7KUT2; Q9VW20;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 102.
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};
DE   Flags: Precursor;
GN   Name=Lon; ORFNames=CG8798;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-898.
RX   PubMed=20930118; DOI=10.1073/pnas.1008924107;
RA   Matsushima Y., Goto Y., Kaguni L.S.;
RT   "Mitochondrial Lon protease regulates mitochondrial DNA copy number and
RT   transcription by selective degradation of mitochondrial transcription
RT   factor A (TFAM).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:18410-18415(2010).
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. Regulates mitochondrial DNA (mtDNA) copy
CC       number and transcription by stabilizing the mitochondrial TFAM:mtDNA
CC       ratio via selective degradation of TFAM. {ECO:0000255|HAMAP-
CC       Rule:MF_03120, ECO:0000269|PubMed:20930118}.
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, ECO:0000269|PubMed:20930118}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=C;
CC         IsoId=Q7KUT2-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=Q7KUT2-2; Sequence=VSP_039539;
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03120}.
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DR   EMBL; AE014296; AAF49134.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAN11654.2; -; Genomic_DNA.
DR   EMBL; BT099738; ACV53872.1; -; mRNA.
DR   RefSeq; NP_649133.1; NM_140876.3. [Q7KUT2-2]
DR   RefSeq; NP_730435.2; NM_168806.3. [Q7KUT2-1]
DR   AlphaFoldDB; Q7KUT2; -.
DR   SMR; Q7KUT2; -.
DR   BioGRID; 65408; 6.
DR   IntAct; Q7KUT2; 9.
DR   STRING; 7227.FBpp0271918; -.
DR   MEROPS; S16.002; -.
DR   PaxDb; Q7KUT2; -.
DR   PRIDE; Q7KUT2; -.
DR   DNASU; 40138; -.
DR   EnsemblMetazoa; FBtr0074967; FBpp0074735; FBgn0036892. [Q7KUT2-2]
DR   EnsemblMetazoa; FBtr0273410; FBpp0271918; FBgn0036892. [Q7KUT2-1]
DR   GeneID; 40138; -.
DR   KEGG; dme:Dmel_CG8798; -.
DR   UCSC; CG8798-RA; d. melanogaster.
DR   CTD; 40138; -.
DR   FlyBase; FBgn0036892; Lon.
DR   VEuPathDB; VectorBase:FBgn0036892; -.
DR   eggNOG; KOG2004; Eukaryota.
DR   GeneTree; ENSGT00530000063553; -.
DR   InParanoid; Q7KUT2; -.
DR   OMA; YVGPPIY; -.
DR   PhylomeDB; Q7KUT2; -.
DR   SignaLink; Q7KUT2; -.
DR   BioGRID-ORCS; 40138; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; Lon; fly.
DR   GenomeRNAi; 40138; -.
DR   PRO; PR:Q7KUT2; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0036892; Expressed in mouthpart and 37 other tissues.
DR   ExpressionAtlas; Q7KUT2; baseline and differential.
DR   Genevisible; Q7KUT2; DM.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR   GO; GO:0005777; C:peroxisome; ISS:FlyBase.
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; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017171; F:serine hydrolase activity; HDA:FlyBase.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:FlyBase.
DR   GO; GO:0070407; P:oxidation-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:FlyBase.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
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; 2.
DR   TIGRFAMs; TIGR00763; lon; 1.
DR   PROSITE; PS51787; LON_N; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR   PROSITE; PS01046; LON_SER; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; DNA-binding; Hydrolase; Mitochondrion;
KW   Nucleotide-binding; Protease; Reference proteome; Serine protease;
KW   Transit peptide.
FT   TRANSIT         1..56
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   CHAIN           57..1024
FT                   /note="Lon protease homolog, mitochondrial"
FT                   /id="PRO_0000395762"
FT   DOMAIN          94..409
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          800..992
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          219..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          999..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        898
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   ACT_SITE        941
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   BINDING         564..571
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   VAR_SEQ         199..216
FT                   /note="Missing (in isoform A)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_039539"
FT   MUTAGEN         898
FT                   /note="S->A: Severe retardation of TFAM degradation
FT                   following mtDNA depletion."
FT                   /evidence="ECO:0000269|PubMed:20930118"
SQ   SEQUENCE   1024 AA;  115033 MW;  2472ED9810956576 CRC64;
     MLARAIRVRP MMRGIASSSV WNRNRPIQSS LMQYCRDRSL RLQRLHGANL MVQRFYSRKR
     DDSNGDIIMG PDLMSDQDTH LPATVAVPDV WPHVPLLAMR KNPLFPRFMK IVEVSNPIIM
     DLLRRKVKLN QPYVGVFLKK TDGEEELITN LNDVYNLGTF AQIQELQDLG DKLRMVVVAH
     RRIRITGQVV EDVPPPKPVK MTTLHYPLFN IKLQIPAEDQ STDQADAAPI KSRSDPARKP
     RGRIPRSRTG KSRESAAAEE LIQNQTLEPP LKSGKVESSS LPKPPTEEKI VEPETGAKEN
     VNQSAPSAQP VLIVEVENVK QPIYKQTEEV KALTQEIIKT LRDIITMNPL YRESLQQMLH
     QNQRVVDNPI YLCDLGASLS AGEPAELQKI LEETDIPERL QLALTLLKKE LELSRLQQKI
     GREVEEKVKQ QHRKYILQEQ LKVIKKELGI EKDDKDAIGE KYREKLKDKV VPEAIMTVID
     EELTKLNFLE SHSSEFNVTR NYLDWLTSLP WGVISTENLC LEKATETLND DHYGMEDIKK
     RILEFIAVSS LKGSTQGKIL CFHGPPGVGK TSIAKSIARA LNREYFRFSV GGMTDVAEIK
     GHRRTYVGAM PGKLIQCLKK TKIENPLVLI DEVDKIGKGY QGDPSSALLE LLDPEQNANF
     LDHYLDVPVD LSRVLFICTA NVIDTIPEPL RDRMELIEMS GYVAEEKIAI ARQYLMPQAM
     KDCGLTDKHI NISEDALNML IRSYCRESGV RNLQKHIEKV IRKVAFRVVK KEGEHFPVNA
     DNLTTFLGKQ IFSSDRMYAT TPVGVVMGLA WTAMGGSSLY IETSRRHIRQ GAKTDPNTVA
     GSLHITGNLG DVMKESAQIA LTVARNFLYS LEPNNLFLEQ EHIHLHVPEG ATPKDGPSAG
     ITIITALVSL ATGKPVRQDI AMTGEVSLKG KVLPVGGIKE KTIAARRSGV NCLILPVDNK
     KDFEELPTYI TDGLEVHFAT TYEDVYKIAF TDVTETTTNN VEEQEPLQKL SSAAAAKSET
     WPYS
 
 
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