RNZ1_MOUSE
ID RNZ1_MOUSE Reviewed; 362 AA.
AC Q8VEB6; Q9CXB1; Q9ERF4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Zinc phosphodiesterase ELAC protein 1;
DE EC=3.1.26.11;
DE AltName: Full=ElaC homolog protein 1;
DE AltName: Full=Ribonuclease Z 1;
DE Short=RNase Z 1;
DE AltName: Full=tRNA 3 endonuclease 1;
DE AltName: Full=tRNase Z 1;
GN Name=Elac1;
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 MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'-
CC processing endonuclease activity. Probably involved in tRNA maturation,
CC by removing a 3'-trailer from precursor tRNA (By similarity).
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC {ECO:0000250}. Note=Mainly cytosolic. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VEB6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VEB6-2; Sequence=VSP_009167;
CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
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DR EMBL; AF308697; AAG24919.1; -; mRNA.
DR EMBL; AK018424; BAB31204.1; -; mRNA.
DR EMBL; BC019371; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS37855.1; -. [Q8VEB6-1]
DR RefSeq; NP_444485.2; NM_053255.3. [Q8VEB6-1]
DR AlphaFoldDB; Q8VEB6; -.
DR SMR; Q8VEB6; -.
DR STRING; 10090.ENSMUSP00000041793; -.
DR PhosphoSitePlus; Q8VEB6; -.
DR EPD; Q8VEB6; -.
DR MaxQB; Q8VEB6; -.
DR PaxDb; Q8VEB6; -.
DR PRIDE; Q8VEB6; -.
DR ProteomicsDB; 301629; -. [Q8VEB6-1]
DR ProteomicsDB; 301630; -. [Q8VEB6-2]
DR Antibodypedia; 22721; 243 antibodies from 21 providers.
DR Ensembl; ENSMUST00000041138; ENSMUSP00000041793; ENSMUSG00000036941. [Q8VEB6-1]
DR GeneID; 114615; -.
DR KEGG; mmu:114615; -.
DR UCSC; uc008fow.1; mouse. [Q8VEB6-1]
DR CTD; 55520; -.
DR MGI; MGI:1890495; Elac1.
DR VEuPathDB; HostDB:ENSMUSG00000036941; -.
DR eggNOG; KOG2121; Eukaryota.
DR GeneTree; ENSGT00730000111224; -.
DR HOGENOM; CLU_031317_2_2_1; -.
DR InParanoid; Q8VEB6; -.
DR OMA; GTQRQMM; -.
DR OrthoDB; 1387038at2759; -.
DR PhylomeDB; Q8VEB6; -.
DR TreeFam; TF324462; -.
DR BioGRID-ORCS; 114615; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Elac1; mouse.
DR PRO; PR:Q8VEB6; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8VEB6; protein.
DR Bgee; ENSMUSG00000036941; Expressed in pigmented layer of retina and 214 other tissues.
DR Genevisible; Q8VEB6; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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:0042779; P:tRNA 3'-trailer cleavage; IBA:GO_Central.
DR CDD; cd07717; RNaseZ_ZiPD-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR HAMAP; MF_01818; RNase_Z_BN; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR013471; RNase_Z/BN.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR02651; RNase_Z; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Endonuclease; Hydrolase; Metal-binding;
KW Nuclease; Nucleus; Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..362
FT /note="Zinc phosphodiesterase ELAC protein 1"
FT /id="PRO_0000155826"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..241
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009167"
FT CONFLICT 77
FT /note="T -> P (in Ref. 1; AAG24919)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="K -> N (in Ref. 2; BAB31204)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="T -> G (in Ref. 1; AAG24919)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="M -> I (in Ref. 1; AAG24919)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="E -> D (in Ref. 1; AAG24919)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="C -> S (in Ref. 1; AAG24919)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="S -> I (in Ref. 1; AAG24919)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="A -> P (in Ref. 1; AAG24919)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="A -> P (in Ref. 1; AAG24919)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 39740 MW; DC3D437211D6810C CRC64;
MSMDVTFLGT GAAYPSPTRG ASAVVLRCEG ECWLFDCGEG TQTQLMKSQL KAGRITKIFI
THLHGDHFFG LPGLLCTISL QSGSVVARQP IEIYGPVGLR DFIWRTMELS HTELVFPYVV
HELVPTADQC PVEELREFAH MDETDSSPKG QGRTILLDAE ENSYCLVDDE QFVVKAFRLF
HRIPSFGFSV VEKKRAGKLN AQKLRDLGVP PGPAYGKLKN GISVVLDNGV TISPQDVLKK
PMVGRKVCIL GDCSGVVGDG GVKLCFEADL LIHEATLDDS QMDKAREHGH STPQMAAAFA
KLCRAKRLVL THFSQRYKPT ALAREGEADG IAELRKQAEA VLELQEVTLA EDFMVIGIPI
KK
