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
//