RNZ2_MOUSE
ID RNZ2_MOUSE Reviewed; 831 AA.
AC Q80Y81; B1ATP6; Q99MF0; Q99MF1; Q9CTA2; Q9D1A8; Q9EPZ2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 146.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 397-831 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 581-831 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-797, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-792, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; SER-195 AND SER-200, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-797, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80Y81-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80Y81-2; Sequence=VSP_009173;
CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF308696; AAG24918.2; -; mRNA.
DR EMBL; AF348157; AAK29420.1; -; Genomic_DNA.
DR EMBL; AF348157; AAK29421.1; -; Genomic_DNA.
DR EMBL; AL663045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048235; AAH48235.1; -; mRNA.
DR EMBL; AK003759; BAB22981.2; -; mRNA.
DR EMBL; AK004136; BAB23185.1; -; mRNA.
DR CCDS; CCDS24841.1; -. [Q80Y81-1]
DR CCDS; CCDS88171.1; -. [Q80Y81-2]
DR RefSeq; NP_075968.2; NM_023479.2. [Q80Y81-1]
DR AlphaFoldDB; Q80Y81; -.
DR SMR; Q80Y81; -.
DR BioGRID; 212960; 12.
DR STRING; 10090.ENSMUSP00000071788; -.
DR iPTMnet; Q80Y81; -.
DR PhosphoSitePlus; Q80Y81; -.
DR EPD; Q80Y81; -.
DR MaxQB; Q80Y81; -.
DR PaxDb; Q80Y81; -.
DR PRIDE; Q80Y81; -.
DR ProteomicsDB; 300462; -. [Q80Y81-1]
DR ProteomicsDB; 300463; -. [Q80Y81-2]
DR Antibodypedia; 13065; 209 antibodies from 30 providers.
DR DNASU; 68626; -.
DR Ensembl; ENSMUST00000071891; ENSMUSP00000071788; ENSMUSG00000020549. [Q80Y81-1]
DR Ensembl; ENSMUST00000101049; ENSMUSP00000098610; ENSMUSG00000020549. [Q80Y81-2]
DR GeneID; 68626; -.
DR KEGG; mmu:68626; -.
DR UCSC; uc007jks.2; mouse. [Q80Y81-1]
DR CTD; 60528; -.
DR MGI; MGI:1890496; Elac2.
DR VEuPathDB; HostDB:ENSMUSG00000020549; -.
DR eggNOG; KOG2121; Eukaryota.
DR GeneTree; ENSGT00730000111191; -.
DR InParanoid; Q80Y81; -.
DR OMA; YICQLKP; -.
DR OrthoDB; 454909at2759; -.
DR PhylomeDB; Q80Y81; -.
DR TreeFam; TF105797; -.
DR BRENDA; 3.1.26.11; 3474.
DR BioGRID-ORCS; 68626; 26 hits in 74 CRISPR screens.
DR PRO; PR:Q80Y81; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q80Y81; protein.
DR Bgee; ENSMUSG00000020549; Expressed in otic placode and 255 other tissues.
DR ExpressionAtlas; Q80Y81; baseline and differential.
DR Genevisible; Q80Y81; MM.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:MGI.
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 Alternative splicing; Endonuclease; Hydrolase; Metal-binding;
KW Mitochondrion; 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..831
FT /note="Zinc phosphodiesterase ELAC protein 2"
FT /id="PRO_0000155830"
FT REGION 15..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..831
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 183..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ52"
FT MOD_RES 792
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGS5"
FT VAR_SEQ 821..831
FT /note="ESVANTLGARV -> VRAQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009173"
FT CONFLICT 27
FT /note="S -> P (in Ref. 1; AAK29420/AAK29421)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="T -> S (in Ref. 4; BAB23185)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="L -> P (in Ref. 1; AAG24918)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="E -> G (in Ref. 1; AAG24918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 831 AA; 92719 MW; 77E3876AE2862224 CRC64;
MWALRSLLRP LGLRTMSQGS ARRPRPSKDP LRHLRTREKR GPGPGGPNTV YLQVVAAGGR
DAGAALYVFS EYNRYLFNCG EGVQRLMQEH KLKVARLDNI FLTRMHWSNV GGLCGMILTL
KETGLPKCVL SGPPQLEKYL EAIKIFSGPL KGIELAVRPH SAPEYKDETM TVYQVPIHSE
RRCGKQQPSQ SPRTSPNRLS PKQSSDSGSA ENGQCPPEDS SAGANRKAWG RDPSLVVAFV
CKLHLRKGNF LVLKAKELGL PVGTAAIAPI IAAVKDGKSI TYEGREIAAE ELCTPPDPGL
VFIVVECPDE GFILPICEND TFKRYQAEAD APVALVVHIA PESVLIDSRY QQWMERFGPD
TQHLILNENC PSVHNLRSHK IQTQLSLIHP DIFPQLTSFY SKEEGSTLSV PTVRGECLLK
YQLRPKREWQ RDTTLDCNTD EFIAEALELP SFQESVEEYR KNVQENPAPA EKRSQYPEIV
FLGTGSAIPM KIRNVSSTLV NLSPDKSVLL DCGEGTFGQL CRHYGQQIDR VLCSLTAVFV
SHLHADHHTG LLNILLQREH ALASLGKPFQ PLLVVAPTQL RAWLQQYHNH CQEILHHVSM
IPAKCLQKGA EVSNTTLERL ISLLLETCDL EEFQTCLVRH CKHAFGCALV HSSGWKVVYS
GDTMPCEALV QMGKDATLLI HEATLEDGLE EEAVEKTHST TSQAINVGMR MNAEFIMLNH
FSQRYAKIPL FSPDFNEKVG IAFDHMKVCF GDFPTVPKLI PPLKALFAGD IEEMVERREK
RELRLVRAAL LTQQADSPED REPQQKRAHT DEPHSPQSKK ESVANTLGAR V
