RNZ2_PANTR
ID RNZ2_PANTR Reviewed; 826 AA.
AC Q9GL72;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11175785; DOI=10.1038/84808;
RA Tavtigian S.V., Simard J., Teng D.H.F., Abtin V., Baumgard M., Beck A.,
RA Camp N.J., Carillo A.R., Chen Y., Dayananth P., Desrochers M., Dumont M.,
RA Farnham J.M., Frank D., Frye C., Ghaffari S., Gupte J.S., Hu R., Iliev D.,
RA Janecki T., Kort E.N., Laity K.E., Leavitt A., Leblanc G.,
RA McArthur-Morrison J., Pederson A., Penn B., Peterson K.T., Reid J.E.,
RA Richards S., Schroeder M., Smith R., Snyder S.C., Swedlund B., Swensen J.,
RA Thomas A., Tranchant M., Woodland A.-M., Labrie F., Skolnick M.H.,
RA Neuhausen S., Rommens J., Cannon-Albright L.A.;
RT "A candidate prostate cancer susceptibility gene at chromosome 17p.";
RL Nat. Genet. 27:172-180(2001).
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; AF308698; AAG24920.1; -; mRNA.
DR RefSeq; NP_001009034.1; NM_001009034.1.
DR AlphaFoldDB; Q9GL72; -.
DR SMR; Q9GL72; -.
DR STRING; 9598.ENSPTRP00000014982; -.
DR PaxDb; Q9GL72; -.
DR Ensembl; ENSPTRT00000090099; ENSPTRP00000081112; ENSPTRG00000008788.
DR GeneID; 450109; -.
DR KEGG; ptr:450109; -.
DR CTD; 60528; -.
DR VGNC; VGNC:9459; ELAC2.
DR eggNOG; KOG2121; Eukaryota.
DR GeneTree; ENSGT00730000111191; -.
DR HOGENOM; CLU_006220_2_0_1; -.
DR InParanoid; Q9GL72; -.
DR OMA; YICQLKP; -.
DR OrthoDB; 454909at2759; -.
DR TreeFam; TF105797; -.
DR Proteomes; UP000002277; Chromosome 17.
DR Bgee; ENSPTRG00000008788; Expressed in hindlimb stylopod muscle and 21 other tissues.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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: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 2: Evidence at transcript 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..826
FT /note="Zinc phosphodiesterase ELAC protein 2"
FT /id="PRO_0000155831"
FT REGION 16..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
SQ SEQUENCE 826 AA; 92324 MW; 51A62814155E7191 CRC64;
MWALCSLLRS AAGRTMSQGR TISQAPARRE RPRKDPLRHL RTREKRGPSG CSGGPNTVYL
QVVAAGSRDS GAALYVFSEF NRYLFNCGEG IQRLMQEHKL KVARLDNIFL TRMHWSNVGG
LSGMILTLKE TGLPKCVLSG PPQLEKYLEA IKIFSGPLKG IELAVRPHSA PEYEDETMTV
YQIPIHSEQR RGKHQPWQSP ERPLSRLSPE RSSDSESNEN EPHLPHGVSQ RRGVRDSSLV
VAFICKLHLK RGNFLVLKAK EMGLPVGTAA IAPIIAAVKD GKSITHEGRE ILAEELCTPP
DPGAAFVVVE CPDESFIQPI CENATFQRYQ GKADAPVALV VHMAPESVLV DSRYQQWMER
FGPDTQHLVL NENCASVHNL RSHKIQTQLN LIHPDIFPLL TSFPCKKEGP TLSVPMVQGE
CLLKYQLRPR REWQRDAIIT CNPEEFIIEA LQLPNFQQSV QEYRRSAQDG PAPAEKRSQY
PEIIFLGTGS AIPMKIRNVS ATLVNISPDT SLLLDCGEGT FGQLCRHYGD QVDRVLGTLA
AVFVSHLHAD HHTGLLNILL QRERALASLG KPFHPLLVVA PNQLKAWLQQ YHNQCQEVLH
HISMIPAKCL QEGAEISSPA VERLISSLLR TCDLEEFQTC LVRHCKHAFG CALVHTSGWK
VVYSGDTMPC EALVRMGKDA TLLIHEATLE DGLEEEAVEK THSTTSQAIS VGMRMNAEFI
MLNHFSQRYA KVPLFSPNFN EKVGVAFDHM KVCFGDFATM PKLIPPLKAL FAGDIEEMEE
RREKRELRQV RAALLSRELA GGLEDGEPQQ KRAHTEEPQA KKVRAQ