RNZ2_RAT
ID RNZ2_RAT Reviewed; 827 AA.
AC Q8CGS5;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Zinc phosphodiesterase ELAC protein 2;
DE EC=3.1.26.11;
DE AltName: Full=ElaC homolog protein 2;
DE AltName: Full=Ribonuclease Z 2;
DE Short=RNase Z 2;
DE AltName: Full=tRNA 3 endonuclease 2;
DE AltName: Full=tRNase Z 2;
DE Flags: Precursor;
GN Name=Elac2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=15358515; DOI=10.1016/j.bbaexp.2004.07.001;
RA Dumont M., Frank D., Moisan A.-M., Tranchant M., Soucy P., Breton R.,
RA Labrie F., Tavtigian S.V., Simard J.;
RT "Structure of primate and rodent orthologs of the prostate cancer
RT susceptibility gene ELAC2.";
RL Biochim. Biophys. Acta 1679:230-247(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-818, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Zinc phosphodiesterase, which displays mitochondrial tRNA 3'-
CC processing endonuclease activity. Involved in tRNA maturation, by
CC removing a 3'-trailer from precursor tRNA. Associates with
CC mitochondrial DNA complexes at the nucleoids to initiate RNA processing
CC and ribosome assembly. {ECO:0000250|UniProtKB:Q9BQ52}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing extra 3' nucleotides
CC from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy
CC group is left at the tRNA terminus and a 5'-phosphoryl group is left
CC at the trailer molecule.; EC=3.1.26.11;
CC Evidence={ECO:0000250|UniProtKB:Q9BQ52};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBUNIT: Homodimer. Interacts with PTCD1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BQ52}.
CC Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000250|UniProtKB:Q9BQ52}. Nucleus {ECO:0000250|UniProtKB:Q9BQ52}.
CC Note=Mainly mitochondrial. {ECO:0000250|UniProtKB:Q9BQ52}.
CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
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DR EMBL; AY149902; AAN75376.1; -; mRNA.
DR RefSeq; NP_758829.1; NM_172326.1.
DR AlphaFoldDB; Q8CGS5; -.
DR SMR; Q8CGS5; -.
DR STRING; 10116.ENSRNOP00000004722; -.
DR iPTMnet; Q8CGS5; -.
DR PhosphoSitePlus; Q8CGS5; -.
DR jPOST; Q8CGS5; -.
DR PaxDb; Q8CGS5; -.
DR PRIDE; Q8CGS5; -.
DR GeneID; 282826; -.
DR KEGG; rno:282826; -.
DR UCSC; RGD:628882; rat.
DR CTD; 60528; -.
DR RGD; 628882; Elac2.
DR eggNOG; KOG2121; Eukaryota.
DR InParanoid; Q8CGS5; -.
DR OrthoDB; 454909at2759; -.
DR PhylomeDB; Q8CGS5; -.
DR PRO; PR:Q8CGS5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004549; F:tRNA-specific ribonuclease activity; ISO:RGD.
DR GO; GO:0072684; P:mitochondrial tRNA 3'-trailer cleavage, endonucleolytic; ISS:UniProtKB.
DR Gene3D; 3.60.15.10; -; 2.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR027794; tRNase_Z_dom.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR Pfam; PF13691; Lactamase_B_4; 1.
DR SUPFAM; SSF56281; SSF56281; 2.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Metal-binding; Mitochondrion;
KW Mitochondrion nucleoid; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome; Transit peptide; tRNA processing; Zinc.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..827
FT /note="Zinc phosphodiesterase ELAC protein 2"
FT /id="PRO_0000155832"
FT REGION 15..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y81"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 795
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y81"
FT MOD_RES 800
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y81"
FT MOD_RES 818
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 827 AA; 92340 MW; 0D4D391BA0A581A8 CRC64;
MWALRSLLRP LGLRTMSQGS ARRPRPPKDP LRHLRTREKR GPGWGPGGPN TVYLQVVAAG
GRDAAAALYV FSEYNRYLFN CGEGVQRLMQ EHKLKVARLD NIFLTRMHWS NVGGLCGMIL
TLKETGLPKC VLSGPPQLEK YLEAIKIFSG PLKGIDLAVR PHSAPEYKDE TMTVYQVPIH
SERRCGEQEP SRSPKRSPNR LSPKQSSSDP GSAENGQCLP EGSSAGVNGK AWGRDPSLVV
AFVCKLHLRK GNFLVLKAKE LGLPVGTAAI APIIAAVKDG KSITYEGREI AAEELCTPPD
PGLVFIVVEC PDEGFIQPIC ENDTFQRYQG EADAPVAVVV HIAPESVLID SRYQQWMERF
GPDTQHLILN ENCPSVHNLR SHKIQTQLSL IHPDIFPQLT SFHSKEEGST FSLPTVRGEC
LLKYHVRPKR EWQRDTTLDC NTDEFIAEAL ELPNFQESVE EYRKNMQASP APAEKRSQYP
EIVFLGTGSA IPMKIRNVSS TLVNLSPDKS VLLDCGEGTF GQLCRHYGQQ IDRVLCNLTA
VFVSHLHADH HTGLLNILLQ REHALASLGK PFQPLLVVAP TQLRAWLQQY HNQCQEILHH
ISMIPAKCLQ KGAEVPSPPV ERLISLLLET CDLQEFQTCL VRHCKHAFGC ALVHSSGWKV
VYSGDTMPCE ALVQMGKDAT LLIHEATLED GLEEEAVEKT HSTTSQAIGV GMRMNAEFIM
LNHFSQRYAK IPLFSPDFNE KVGIAFDHMK VCFGDFPTVP KLIPPLKALF ADDIEEMVER
REKRELRLVR AALLTQQADS SEDREPHQKR AHSEEPHSPQ SKKVRAQ
