MRPP3_HUMAN
ID MRPP3_HUMAN Reviewed; 583 AA.
AC O15091; B4DXD9; B4E0S8; B4E211; C4AM93; D3DS99; D3DSA1; Q86SZ4; Q86YB5;
AC Q8N5L5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Mitochondrial ribonuclease P catalytic subunit;
DE EC=3.1.26.5 {ECO:0000269|PubMed:25953853};
DE AltName: Full=Mitochondrial ribonuclease P protein 3 {ECO:0000303|PubMed:18984158};
DE Short=Mitochondrial RNase P protein 3 {ECO:0000303|PubMed:18984158};
DE AltName: Full=Protein only RNase P catalytic subunit {ECO:0000312|HGNC:HGNC:19958};
DE Flags: Precursor;
GN Name=PRORP {ECO:0000312|HGNC:HGNC:19958};
GN Synonyms=KIAA0391, MRPP3 {ECO:0000303|PubMed:18984158};
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Neuroblastoma, and T-cell;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), AND VARIANT
RP SER-437.
RC TISSUE=Testis, Thymus, and Trachea;
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 GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-437.
RC TISSUE=Lung, and Testis;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH HSD17B10 AND TRMT10C.
RX PubMed=18984158; DOI=10.1016/j.cell.2008.09.013;
RA Holzmann J., Frank P., Loeffler E., Bennett K.L., Gerner C., Rossmanith W.;
RT "RNase P without RNA: identification and functional reconstitution of the
RT human mitochondrial tRNA processing enzyme.";
RL Cell 135:462-474(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP PROTEOLYTIC PROCESSING, AND INDUCTION.
RX PubMed=27350246; DOI=10.1038/nature18302;
RA Muench C., Harper J.W.;
RT "Mitochondrial unfolded protein response controls matrix pre-RNA processing
RT and translation.";
RL Nature 534:710-713(2016).
RN [12] {ECO:0007744|PDB:4XGL, ECO:0007744|PDB:4XGM}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 207-583 IN COMPLEX WITH ZINC,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, AND MUTAGENESIS OF ASP-409;
RP ASP-478; ASP-479; PRO-480; ARG-498; ASP-499 AND SER-569.
RX PubMed=25953853; DOI=10.1093/nar/gkv481;
RA Reinhard L., Sridhara S., Hallberg B.M.;
RT "Structure of the nuclease subunit of human mitochondrial RNase P.";
RL Nucleic Acids Res. 43:5664-5672(2015).
CC -!- FUNCTION: Catalytic ribonuclease component of mitochondrial
CC ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and
CC PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends
CC (PubMed:18984158, PubMed:25953853). The presence of TRMT10C/MRPP1,
CC HSD17B10/MRPP2 is required to catalyze tRNA molecules in their 5'-ends
CC (PubMed:25953853). {ECO:0000269|PubMed:18984158,
CC ECO:0000269|PubMed:25953853}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC from tRNA precursor.; EC=3.1.26.5;
CC Evidence={ECO:0000269|PubMed:25953853};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:25953853};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:25953853};
CC Note=Binds 2 Mg(2+) or Mg(2+) ions per subunit.
CC {ECO:0000305|PubMed:25953853};
CC -!- SUBUNIT: Catalytic component of mitochondrial ribonuclease P, a complex
CC composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3
CC (PubMed:18984158). {ECO:0000269|PubMed:18984158}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18984158}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O15091-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15091-2; Sequence=VSP_036203;
CC Name=3;
CC IsoId=O15091-3; Sequence=VSP_036201;
CC Name=4;
CC IsoId=O15091-4; Sequence=VSP_036202;
CC -!- INDUCTION: Down-regulated following mitochondrial unfolded protein
CC response. {ECO:0000269|PubMed:27350246}.
CC -!- DOMAIN: Displays a distorted and non-productive active site that
CC probably switches to a fully productive state only upon association
CC with TRMT10C/MRPP1, HSD17B10/MRPP2 and pre-tRNA substrate.
CC {ECO:0000305|PubMed:25953853}.
CC -!- PTM: Degraded by LONP1 following mitochondrial unfolded protein
CC response, probably leading to inhibit translation in mitochondrion.
CC {ECO:0000269|PubMed:27350246}.
CC -!- SIMILARITY: Belongs to the PPR family. P subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20845.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB002389; BAA20845.2; ALT_INIT; mRNA.
DR EMBL; BX161394; CAD61881.1; -; mRNA.
DR EMBL; BX161487; CAD61937.1; -; mRNA.
DR EMBL; AK301931; BAG63351.1; -; mRNA.
DR EMBL; AK303508; BAG64540.1; -; mRNA.
DR EMBL; AK304066; BAG64973.1; -; mRNA.
DR EMBL; AL121594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65878.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65882.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65879.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65880.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65881.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65883.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65884.1; -; Genomic_DNA.
DR EMBL; BC032221; AAH32221.1; -; mRNA.
DR EMBL; BC044580; AAH44580.1; -; mRNA.
DR CCDS; CCDS32063.1; -. [O15091-1]
DR CCDS; CCDS58312.1; -. [O15091-2]
DR CCDS; CCDS58313.1; -. [O15091-4]
DR CCDS; CCDS58314.1; -. [O15091-3]
DR RefSeq; NP_001243607.1; NM_001256678.1. [O15091-2]
DR RefSeq; NP_001243608.1; NM_001256679.1. [O15091-4]
DR RefSeq; NP_001243609.1; NM_001256680.1. [O15091-3]
DR RefSeq; NP_001243610.1; NM_001256681.1. [O15091-3]
DR RefSeq; NP_055487.2; NM_014672.3. [O15091-1]
DR RefSeq; XP_005268294.1; XM_005268237.3. [O15091-1]
DR RefSeq; XP_011535711.1; XM_011537409.2.
DR RefSeq; XP_011535712.1; XM_011537410.2. [O15091-1]
DR RefSeq; XP_016877324.1; XM_017021835.1.
DR RefSeq; XP_016877325.1; XM_017021836.1. [O15091-2]
DR RefSeq; XP_016877326.1; XM_017021837.1.
DR PDB; 4ROU; X-ray; 2.71 A; A/B=274-583.
DR PDB; 4XGL; X-ray; 1.80 A; A=207-583.
DR PDB; 4XGM; X-ray; 1.98 A; A=207-583.
DR PDB; 7ONU; EM; 3.00 A; E=46-583.
DR PDBsum; 4ROU; -.
DR PDBsum; 4XGL; -.
DR PDBsum; 4XGM; -.
DR PDBsum; 7ONU; -.
DR AlphaFoldDB; O15091; -.
DR SMR; O15091; -.
DR BioGRID; 115044; 168.
DR ComplexPortal; CPX-6155; Mitochondrial ribonuclease P complex.
DR CORUM; O15091; -.
DR IntAct; O15091; 22.
DR MINT; O15091; -.
DR STRING; 9606.ENSP00000440915; -.
DR iPTMnet; O15091; -.
DR PhosphoSitePlus; O15091; -.
DR BioMuta; KIAA0391; -.
DR EPD; O15091; -.
DR jPOST; O15091; -.
DR MassIVE; O15091; -.
DR MaxQB; O15091; -.
DR PaxDb; O15091; -.
DR PeptideAtlas; O15091; -.
DR PRIDE; O15091; -.
DR ProteomicsDB; 48444; -. [O15091-1]
DR ProteomicsDB; 48445; -. [O15091-2]
DR ProteomicsDB; 48446; -. [O15091-3]
DR ProteomicsDB; 48447; -. [O15091-4]
DR Antibodypedia; 23191; 136 antibodies from 23 providers.
DR DNASU; 9692; -.
DR Ensembl; ENST00000250377.11; ENSP00000250377.8; ENSG00000100890.16. [O15091-2]
DR Ensembl; ENST00000321130.14; ENSP00000324697.9; ENSG00000100890.16. [O15091-3]
DR Ensembl; ENST00000534898.9; ENSP00000440915.2; ENSG00000100890.16. [O15091-1]
DR Ensembl; ENST00000603544.5; ENSP00000473856.1; ENSG00000100890.16. [O15091-2]
DR Ensembl; ENST00000604948.5; ENSP00000474620.1; ENSG00000100890.16. [O15091-4]
DR Ensembl; ENST00000605870.5; ENSP00000474299.1; ENSG00000100890.16. [O15091-3]
DR GeneID; 9692; -.
DR KEGG; hsa:9692; -.
DR MANE-Select; ENST00000534898.9; ENSP00000440915.2; NM_014672.4; NP_055487.2.
DR UCSC; uc001wsy.3; human. [O15091-1]
DR CTD; 9692; -.
DR DisGeNET; 9692; -.
DR GeneCards; PRORP; -.
DR HGNC; HGNC:19958; PRORP.
DR HPA; ENSG00000100890; Low tissue specificity.
DR MIM; 609947; gene.
DR neXtProt; NX_O15091; -.
DR OpenTargets; ENSG00000100890; -.
DR PharmGKB; PA134879499; -.
DR VEuPathDB; HostDB:ENSG00000100890; -.
DR eggNOG; ENOG502QRKG; Eukaryota.
DR GeneTree; ENSGT00390000002201; -.
DR HOGENOM; CLU_033070_1_0_1; -.
DR InParanoid; O15091; -.
DR OMA; TNNLSHD; -.
DR OrthoDB; 1247650at2759; -.
DR PhylomeDB; O15091; -.
DR TreeFam; TF324726; -.
DR BRENDA; 3.1.26.5; 2681.
DR PathwayCommons; O15091; -.
DR Reactome; R-HSA-6785470; tRNA processing in the mitochondrion.
DR Reactome; R-HSA-6787450; tRNA modification in the mitochondrion.
DR Reactome; R-HSA-8868766; rRNA processing in the mitochondrion.
DR SignaLink; O15091; -.
DR BioGRID-ORCS; 9692; 318 hits in 1081 CRISPR screens.
DR ChiTaRS; KIAA0391; human.
DR GenomeRNAi; 9692; -.
DR Pharos; O15091; Tbio.
DR PRO; PR:O15091; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O15091; protein.
DR Bgee; ENSG00000100890; Expressed in rectum and 103 other tissues.
DR ExpressionAtlas; O15091; baseline and differential.
DR Genevisible; O15091; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR GO; GO:0030678; C:mitochondrial ribonuclease P complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004526; F:ribonuclease P activity; IDA:UniProtKB.
DR GO; GO:0097745; P:mitochondrial tRNA 5'-end processing; IDA:UniProtKB.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR033495; MRPP3.
DR InterPro; IPR031595; PRORP_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13547:SF1; PTHR13547:SF1; 1.
DR Pfam; PF16953; PRORP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Mitochondrion; Nuclease; Phosphoprotein; Reference proteome;
KW Transit peptide; tRNA processing; Zinc.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 46..583
FT /note="Mitochondrial ribonuclease P catalytic subunit"
FT /id="PRO_0000050749"
FT DOMAIN 342..578
FT /note="PRORP"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25953853,
FT ECO:0007744|PDB:4XGL, ECO:0007744|PDB:4XGM"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25953853,
FT ECO:0007744|PDB:4XGL, ECO:0007744|PDB:4XGM"
FT BINDING 409
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:25953853"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:25953853"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:25953853"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:25953853"
FT BINDING 557
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25953853,
FT ECO:0007744|PDB:4XGL, ECO:0007744|PDB:4XGM"
FT BINDING 578
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25953853,
FT ECO:0007744|PDB:4XGL, ECO:0007744|PDB:4XGM"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..372
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_036201"
FT VAR_SEQ 1..95
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036202"
FT VAR_SEQ 329..344
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9205841"
FT /id="VSP_036203"
FT VARIANT 437
FT /note="N -> S (in dbSNP:rs11156878)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_054212"
FT MUTAGEN 409
FT /note="D->N: Abolishes ribonuclease activity."
FT /evidence="ECO:0000269|PubMed:25953853"
FT MUTAGEN 478
FT /note="D->N: Abolishes ribonuclease activity."
FT /evidence="ECO:0000269|PubMed:25953853"
FT MUTAGEN 479
FT /note="D->N: Abolishes ribonuclease activity."
FT /evidence="ECO:0000269|PubMed:25953853"
FT MUTAGEN 480
FT /note="P->G: Does not affect ribonuclease activity."
FT /evidence="ECO:0000269|PubMed:25953853"
FT MUTAGEN 498
FT /note="R->D,N: Does not affect ribonuclease activity."
FT /evidence="ECO:0000269|PubMed:25953853"
FT MUTAGEN 499
FT /note="D->N: Abolishes ribonuclease activity."
FT /evidence="ECO:0000269|PubMed:25953853"
FT MUTAGEN 569
FT /note="S->A: Does not affect ribonuclease activity."
FT /evidence="ECO:0000269|PubMed:25953853"
FT CONFLICT 315
FT /note="P -> L (in Ref. 3; BAG63351)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="S -> F (in Ref. 3; BAG64540)"
FT /evidence="ECO:0000305"
FT HELIX 121..135
FT /evidence="ECO:0007829|PDB:7ONU"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:7ONU"
FT HELIX 155..168
FT /evidence="ECO:0007829|PDB:7ONU"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:7ONU"
FT HELIX 175..187
FT /evidence="ECO:0007829|PDB:7ONU"
FT HELIX 191..204
FT /evidence="ECO:0007829|PDB:7ONU"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:4XGL"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:4XGL"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:4XGL"
FT HELIX 244..256
FT /evidence="ECO:0007829|PDB:4XGL"
FT HELIX 260..272
FT /evidence="ECO:0007829|PDB:4XGL"
FT HELIX 279..289
FT /evidence="ECO:0007829|PDB:4XGL"
FT HELIX 295..310
FT /evidence="ECO:0007829|PDB:4XGL"
FT HELIX 317..329
FT /evidence="ECO:0007829|PDB:4XGL"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:7ONU"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:4XGL"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:4XGL"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:4XGL"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:4XGL"
FT HELIX 362..376
FT /evidence="ECO:0007829|PDB:4XGL"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:7ONU"
FT HELIX 388..399
FT /evidence="ECO:0007829|PDB:4XGL"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:4XGL"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:4XGL"
FT HELIX 423..433
FT /evidence="ECO:0007829|PDB:4XGL"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:4XGL"
FT STRAND 440..445
FT /evidence="ECO:0007829|PDB:4XGL"
FT HELIX 446..449
FT /evidence="ECO:0007829|PDB:4XGL"
FT HELIX 460..466
FT /evidence="ECO:0007829|PDB:4XGL"
FT STRAND 467..472
FT /evidence="ECO:0007829|PDB:4XGL"
FT HELIX 481..489
FT /evidence="ECO:0007829|PDB:4XGL"
FT STRAND 494..498
FT /evidence="ECO:0007829|PDB:4XGL"
FT HELIX 502..506
FT /evidence="ECO:0007829|PDB:7ONU"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:7ONU"
FT HELIX 511..524
FT /evidence="ECO:0007829|PDB:4XGL"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:7ONU"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:7ONU"
FT STRAND 553..561
FT /evidence="ECO:0007829|PDB:4XGL"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:7ONU"
FT STRAND 575..581
FT /evidence="ECO:0007829|PDB:4XGL"
SQ SEQUENCE 583 AA; 67315 MW; 6AB17E7E8820D818 CRC64;
MTFYLFGIRS FPKLWKSPYL GLGPGHSYVS LFLADRCGIR NQQRLFSLKT MSPQNTKATN
LIAKARYLRK DEGSNKQVYS VPHFFLAGAA KERSQMNSQT EDHALAPVRN TIQLPTQPLN
SEEWDKLKED LKENTGKTSF ESWIISQMAG CHSSIDVAKS LLAWVAAKNN GIVSYDLLVK
YLYLCVFHMQ TSEVIDVFEI MKARYKTLEP RGYSLLIRGL IHSDRWREAL LLLEDIKKVI
TPSKKNYNDC IQGALLHQDV NTAWNLYQEL LGHDIVPMLE TLKAFFDFGK DIKDDNYSNK
LLDILSYLRN NQLYPGESFA HSIKTWFESV PGKQWKGQFT TVRKSGQCSG CGKTIESIQL
SPEEYECLKG KIMRDVIDGG DQYRKTTPQE LKRFENFIKS RPPFDVVIDG LNVAKMFPKV
RESQLLLNVV SQLAKRNLRL LVLGRKHMLR RSSQWSRDEM EEVQKQASCF FADDISEDDP
FLLYATLHSG NHCRFITRDL MRDHKACLPD AKTQRLFFKW QQGHQLAIVN RFPGSKLTFQ
RILSYDTVVQ TTGDSWHIPY DEDLVERCSC EVPTKWLCLH QKT
