RNZ1_HUMAN
ID RNZ1_HUMAN Reviewed; 363 AA.
AC Q9H777; Q9NS99;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Zinc phosphodiesterase ELAC protein 1;
DE EC=3.1.26.11;
DE AltName: Full=Deleted in Ma29;
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; Synonyms=D29;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT VAL-355.
RX PubMed=11401430; DOI=10.1006/geno.2000.6454;
RA Yanaihara N., Kohno T., Takakura S., Takei K., Otsuka A., Sunaga N.,
RA Takahashi M., Yamazaki M., Tashiro H., Fukuzumi Y., Fujimori Y.,
RA Hagiwara K., Tanaka T., Yokota J.;
RT "Physical and transcriptional map of a 311-kb segment of chromosome 18q21,
RT a candidate lung tumor suppressor locus.";
RL Genomics 72:169-179(2001).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Smooth muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [5]
RP ENZYME ACTIVITY.
RX PubMed=12711671; DOI=10.1093/nar/gkg337;
RA Takaku H., Minagawa A., Takagi M., Nashimoto M.;
RT "A candidate prostate cancer susceptibility gene encodes tRNA 3' processing
RT endoribonuclease.";
RL Nucleic Acids Res. 31:2272-2278(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=21593607; DOI=10.4161/rna.8.4.15393;
RA Brzezniak L.K., Bijata M., Szczesny R.J., Stepien P.P.;
RT "Involvement of human ELAC2 gene product in 3' end processing of
RT mitochondrial tRNAs.";
RL RNA Biol. 8:616-626(2011).
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.
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:0000269|PubMed:12711671};
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:0000269|PubMed:21593607}.
CC Nucleus {ECO:0000269|PubMed:21593607}. Note=Mainly cytosolic.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain,
CC placenta, lung, liver, skeletal muscle, kidney and pancreas.
CC {ECO:0000269|PubMed:11401430}.
CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
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DR EMBL; AB029151; BAA96799.1; -; mRNA.
DR EMBL; AF308695; AAG24917.1; -; mRNA.
DR EMBL; AK024822; BAB15021.1; -; mRNA.
DR EMBL; BC014624; AAH14624.1; -; mRNA.
DR CCDS; CCDS11949.1; -.
DR RefSeq; NP_061166.1; NM_018696.2.
DR PDB; 3ZWF; X-ray; 1.70 A; A/B=3-363.
DR PDBsum; 3ZWF; -.
DR AlphaFoldDB; Q9H777; -.
DR SMR; Q9H777; -.
DR BioGRID; 120694; 3.
DR STRING; 9606.ENSP00000269466; -.
DR iPTMnet; Q9H777; -.
DR PhosphoSitePlus; Q9H777; -.
DR BioMuta; ELAC1; -.
DR DMDM; 41017799; -.
DR EPD; Q9H777; -.
DR jPOST; Q9H777; -.
DR MassIVE; Q9H777; -.
DR MaxQB; Q9H777; -.
DR PaxDb; Q9H777; -.
DR PeptideAtlas; Q9H777; -.
DR PRIDE; Q9H777; -.
DR ProteomicsDB; 81086; -.
DR Antibodypedia; 22721; 243 antibodies from 21 providers.
DR DNASU; 55520; -.
DR Ensembl; ENST00000269466.8; ENSP00000269466.3; ENSG00000141642.9.
DR GeneID; 55520; -.
DR KEGG; hsa:55520; -.
DR MANE-Select; ENST00000269466.8; ENSP00000269466.3; NM_018696.3; NP_061166.1.
DR UCSC; uc002lez.4; human.
DR CTD; 55520; -.
DR DisGeNET; 55520; -.
DR GeneCards; ELAC1; -.
DR HGNC; HGNC:14197; ELAC1.
DR HPA; ENSG00000141642; Low tissue specificity.
DR MIM; 608079; gene.
DR neXtProt; NX_Q9H777; -.
DR OpenTargets; ENSG00000141642; -.
DR PharmGKB; PA27738; -.
DR VEuPathDB; HostDB:ENSG00000141642; -.
DR eggNOG; KOG2121; Eukaryota.
DR GeneTree; ENSGT00730000111224; -.
DR HOGENOM; CLU_031317_2_2_1; -.
DR InParanoid; Q9H777; -.
DR OMA; GTQRQMM; -.
DR OrthoDB; 1387038at2759; -.
DR PhylomeDB; Q9H777; -.
DR TreeFam; TF324462; -.
DR BRENDA; 3.1.26.11; 2681.
DR PathwayCommons; Q9H777; -.
DR BioGRID-ORCS; 55520; 6 hits in 1080 CRISPR screens.
DR ChiTaRS; ELAC1; human.
DR GeneWiki; ELAC1; -.
DR GenomeRNAi; 55520; -.
DR Pharos; Q9H777; Tbio.
DR PRO; PR:Q9H777; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9H777; protein.
DR Bgee; ENSG00000141642; Expressed in islet of Langerhans and 128 other tissues.
DR ExpressionAtlas; Q9H777; baseline and differential.
DR Genevisible; Q9H777; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA: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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW Nucleus; Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..363
FT /note="Zinc phosphodiesterase ELAC protein 1"
FT /id="PRO_0000155825"
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 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT VARIANT 355
FT /note="M -> V (in dbSNP:rs34524743)"
FT /evidence="ECO:0000269|PubMed:11401430"
FT /id="VAR_017424"
FT CONFLICT 314
FT /note="F -> S (in Ref. 3; BAB15021)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="S -> G (in Ref. 3; BAB15021)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:3ZWF"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3ZWF"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:3ZWF"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3ZWF"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:3ZWF"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:3ZWF"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:3ZWF"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:3ZWF"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 171..184
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:3ZWF"
FT HELIX 261..265
FT /evidence="ECO:0007829|PDB:3ZWF"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:3ZWF"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:3ZWF"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:3ZWF"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:3ZWF"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:3ZWF"
SQ SEQUENCE 363 AA; 40019 MW; 125A8416502D4C79 CRC64;
MSMDVTFLGT GAAYPSPTRG ASAVVLRCEG ECWLFDCGEG TQTQLMKSQL KAGRITKIFI
THLHGDHFFG LPGLLCTISL QSGSMVSKQP IEIYGPVGLR DFIWRTMELS HTELVFHYVV
HELVPTADQC PAEELKEFAH VNRADSPPKE EQGRTILLDS EENSYLLFDD EQFVVKAFRL
FHRIPSFGFS VVEKKRPGKL NAQKLKDLGV PPGPAYGKLK NGISVVLENG VTISPQDVLK
KPIVGRKICI LGDCSGVVGD GGVKLCFEAD LLIHEATLDD AQMDKAKEHG HSTPQMAATF
AKLCRAKRLV LTHFSQRYKP VALAREGETD GIAELKKQAE SVLDLQEVTL AEDFMVISIP
IKK
