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RecName: Full=ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial; Flags: Precursor

UniProtKB/Swiss-Prot: Q5U2U0.1

Identical Proteins FASTA Graphics 

LOCUS       CLPX_RAT                 633 aa            linear   ROD 27-NOV-2024
DEFINITION  RecName: Full=ATP-dependent Clp protease ATP-binding subunit
            clpX-like, mitochondrial; Flags: Precursor.
ACCESSION   Q5U2U0
VERSION     Q5U2U0.1
DBSOURCE    UniProtKB: locus CLPX_RAT, accession Q5U2U0;
            class: standard.
            created: Mar 3, 2009.
            sequence updated: Dec 7, 2004.
            annotation updated: Nov 27, 2024.
            xrefs: BC085867.1, AAH85867.1, NP_001007804.1
            xrefs (non-sequence databases): AlphaFoldDB:Q5U2U0, SMR:Q5U2U0,
            BioGRID:256711, CORUM:Q5U2U0, STRING:10116.ENSRNOP00000050010,
            iPTMnet:Q5U2U0, PhosphoSitePlus:Q5U2U0, jPOST:Q5U2U0,
            PaxDb:10116-ENSRNOP00000050010, Ensembl:ENSRNOT00000048302.3,
            Ensembl:ENSRNOP00000050010.2, Ensembl:ENSRNOG00000030225.5,
            GeneID:300786, KEGG:rno:300786, UCSC:RGD:1304883, AGR:RGD:1304883,
            CTD:10845, RGD:1304883, eggNOG:KOG0745,
            GeneTree:ENSGT00390000017625, HOGENOM:CLU_014218_0_1_1,
            InParanoid:Q5U2U0, OrthoDB:452393at2759, PhylomeDB:Q5U2U0,
            TreeFam:TF312884, Reactome:R-RNO-9837999, PRO:PR:Q5U2U0,
            Proteomes:UP000002494, Bgee:ENSRNOG00000030225, GO:0009368,
            GO:0009841, GO:0005759, GO:0042645, GO:0005739, GO:0005524,
            GO:0016887, GO:0140662, GO:0016504, GO:0046983, GO:0051082,
            GO:0008270, GO:0046034, GO:0006508, GO:0051603, CDD:cd19497,
            FunFam:1.10.8.60:FF:000002, FunFam:3.40.50.300:FF:000378,
            FunFam:3.40.50.300:FF:003247, Gene3D:1.10.8.60, Gene3D:3.40.50.300,
            InterPro:IPR003593, InterPro:IPR050052, InterPro:IPR003959,
            InterPro:IPR019489, InterPro:IPR004487, InterPro:IPR027417,
            InterPro:IPR010603, NCBIfam:TIGR00382, PANTHER:PTHR48102:SF7,
            PANTHER:PTHR48102, Pfam:PF07724, Pfam:PF10431, SMART:SM00382,
            SMART:SM01086, SUPFAM:SSF52540, PROSITE:PS51902
KEYWORDS    Acetylation; ATP-binding; Chaperone; Metal-binding; Mitochondrion;
            Mitochondrion nucleoid; Nucleotide-binding; Phosphoprotein;
            Reference proteome; Transit peptide; Zinc.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            TISSUE=Heart
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
COMMENT     [FUNCTION] ATP-dependent specificity component of the Clp protease
            complex. Hydrolyzes ATP. Targets specific substrates for
            degradation by the Clp complex. Can perform chaperone functions in
            the absence of CLPP. Enhances the DNA-binding activity of TFAM and
            is required for maintaining a normal mitochondrial nucleoid
            structure. ATP-dependent unfoldase that stimulates the
            incorporation of the pyridoxal phosphate cofactor into
            5-aminolevulinate synthase, thereby activating 5-aminolevulinate
            (ALA) synthesis, the first step in heme biosynthesis. Important for
            efficient erythropoiesis through up-regulation of heme
            biosynthesis. {ECO:0000250|UniProtKB:O76031}.
            [SUBUNIT] Homohexamer that forms a ring structure; this
            hexamerization requires ATP binding. Component of the Clp complex
            formed by the assembly of two CLPP heptameric rings with two CLPX
            hexameric rings, giving rise to a symmetrical structure with two
            central CLPP rings flanked by a CLPX ring at either end of the
            complex. Interacts with TFAM. {ECO:0000250|UniProtKB:O76031}.
            [SUBCELLULAR LOCATION] Mitochondrion {ECO:0000250}. Mitochondrion
            matrix, mitochondrion nucleoid {ECO:0000250}.
            [SIMILARITY] Belongs to the ClpX chaperone family.
            {ECO:0000255|PROSITE-ProRule:PRU01250}.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
     gene            1..633
                     /gene="Clpx"
     Protein         1..633
                     /product="ATP-dependent Clp protease ATP-binding subunit
                     clpX-like, mitochondrial"
                     /UniProtKB_evidence="Evidence at transcript level"
     Region          1..56
                     /region_name="Transit peptide"
                     /note="Mitochondrion. /evidence=ECO:0000255."
     Region          57..633
                     /region_name="Mature chain"
                     /note="ATP-dependent Clp protease ATP-binding subunit
                     clpX-like, mitochondrial. /id=PRO_0000364189."
     Region          65..101
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          80..100
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          93..146
                     /region_name="Domain"
                     /note="ClpX-type ZB.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01250."
     Region          104..132
                     /region_name="Zn-ribbon"
                     /note="C-terminal zinc ribbon domain of RNA polymerase
                     intrinsic transcript cleavage subunit; cl02609"
                     /db_xref="CDD:445850"
     Site            order(105,108,127,130)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:259791"
     Region          172..605
                     /region_name="ClpX"
                     /note="ATP-dependent protease Clp, ATPase subunit ClpX
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1219"
                     /db_xref="CDD:440832"
     Site            437
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O76031."
     Region          598..633
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          598..613
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            617
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O76031."
ORIGIN      
        1 msscgactcg aaaarlltts ltsaqrgisc grihvpvlgr lgtldtqilr raplrtfset
       61 payfaskdgt nkdgsgdgnk ksvtegsskk sgsgnsgkgg nqlrcpkcgd lcthvetfvs
      121 strfvkcekc hhffvvlsea dskksiikep esaaeavkla fqqkpppppk kiynyldkyv
      181 vgqsfakkvl svavynhykr iynnipanlr qqaevekqts ltpreleirr redeyrftkl
      241 lqiagisphg nalgasmqqq gsqqmpqekr ggevldsphd dikleksnil llgptgsgkt
      301 llaqtlakcl dvpfaicdct tltqagyvge diesviakll qdanynveka qqgivfldev
      361 dkigsvpgih qlrdvggegv qqgllklleg tivnvpekns rklrgetvqv dttnilfvas
      421 gafngldrii srrknekylg fgtpsnlgkg rraaaaadla nrsgesnthq dieekdrllr
      481 hveardlief gmipefvgrl pvvvplhsld ektlvqilte prnavipqyq alfsmdkcel
      541 nvtedalkai arlalerktg arglrsimek lllepmfevp nsdivcvevd kevvegkkep
      601 gyirapskes seedydsgve edgwprqada ans
//
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