POP7_HUMAN
ID POP7_HUMAN Reviewed; 140 AA.
AC O75817; A4D2E0; Q9BV74;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Ribonuclease P protein subunit p20;
DE Short=RNaseP protein p20;
DE AltName: Full=Ribonucleases P/MRP protein subunit POP7 homolog;
DE Short=hPOP7;
GN Name=POP7; Synonyms=RPP20 {ECO:0000303|PubMed:20215441};
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], PROTEIN SEQUENCE OF 10-20, FUNCTION, AND
RP IDENTIFICATION IN THE RNASE P COMPLEX.
RX PubMed=9630247;
RA Jarrous N., Eder P.S., Guerrier-Takada C., Hoog C., Altman S.;
RT "Autoantigenic properties of some protein subunits of catalytically active
RT complexes of human ribonuclease P.";
RL RNA 4:407-417(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 IDENTIFICATION IN THE RNASE P AND RNASE MRP COMPLEXES, AND SUBUNIT.
RX PubMed=15096576; DOI=10.1093/nar/gkh539;
RA Welting T.J., van Venrooij W.J., Pruijn G.J.;
RT "Mutual interactions between subunits of the human RNase MRP
RT ribonucleoprotein complex.";
RL Nucleic Acids Res. 32:2138-2146(2004).
RN [6]
RP INTERACTION WITH SMN1, AND SUBCELLULAR LOCATION.
RX PubMed=14715275; DOI=10.1016/j.bbrc.2003.12.084;
RA Hua Y., Zhou J.;
RT "Rpp20 interacts with SMN and is re-distributed into SMN granules in
RT response to stress.";
RL Biochem. Biophys. Res. Commun. 314:268-276(2004).
RN [7]
RP IDENTIFICATION IN RNASE P AND MRP COMPLEXES, AND SUBUNIT.
RX PubMed=16723659; DOI=10.1261/rna.2293906;
RA Welting T.J., Kikkert B.J., van Venrooij W.J., Pruijn G.J.;
RT "Differential association of protein subunits with the human RNase MRP and
RT RNase P complexes.";
RL RNA 12:1373-1382(2006).
RN [8]
RP SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH RPP25, AND MUTAGENESIS OF
RP ASN-40.
RX PubMed=20215441; DOI=10.1093/nar/gkq141;
RA Hands-Taylor K.L., Martino L., Tata R., Babon J.J., Bui T.T., Drake A.F.,
RA Beavil R.L., Pruijn G.J., Brown P.R., Conte M.R.;
RT "Heterodimerization of the human RNase P/MRP subunits Rpp20 and Rpp25 is a
RT prerequisite for interaction with the P3 arm of RNase MRP RNA.";
RL Nucleic Acids Res. 38:4052-4066(2010).
RN [9]
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 [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=28115465; DOI=10.1101/gad.286963.116;
RA Goldfarb K.C., Cech T.R.;
RT "Targeted CRISPR disruption reveals a role for RNase MRP RNA in human
RT preribosomal RNA processing.";
RL Genes Dev. 31:59-71(2017).
RN [11] {ECO:0007744|PDB:6AHR, ECO:0007744|PDB:6AHU}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.66 ANGSTROMS) OF RNASE P HOLOENZYME IN
RP COMPLEX WITH TRNA, FUNCTION, AND SUBUNIT.
RX PubMed=30454648; DOI=10.1016/j.cell.2018.10.003;
RA Wu J., Niu S., Tan M., Huang C., Li M., Song Y., Wang Q., Chen J., Shi S.,
RA Lan P., Lei M.;
RT "Cryo-EM Structure of the Human Ribonuclease P Holoenzyme.";
RL Cell 175:1393-1404.e11(2018).
RN [12] {ECO:0007744|PDB:6CWX}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH RPP25, SUBUNIT, AND
RP RNA-BINDING.
RX PubMed=29625199; DOI=10.1016/j.jmb.2018.03.029;
RA Chan C.W., Kiesel B.R., Mondragon A.;
RT "Crystal Structure of Human Rpp20/Rpp25 Reveals Quaternary Level Adaptation
RT of the Alba Scaffold as Structural Basis for Single-stranded RNA Binding.";
RL J. Mol. Biol. 430:1403-1416(2018).
CC -!- FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that
CC generates mature tRNA molecules by cleaving their 5'-ends
CC (PubMed:9630247, PubMed:30454648). Also a component of the MRP
CC ribonuclease complex, which cleaves pre-rRNA sequences
CC (PubMed:28115465). {ECO:0000269|PubMed:28115465,
CC ECO:0000269|PubMed:30454648, ECO:0000269|PubMed:9630247}.
CC -!- SUBUNIT: Component of nuclear RNase P and RNase MRP complexes
CC (PubMed:9630247, PubMed:15096576, PubMed:16723659, PubMed:20215441,
CC PubMed:30454648). RNase P consists of a catalytic RNA moiety and 10
CC different protein chains; POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25,
CC RPP30, RPP38 and RPP40 (PubMed:9630247, PubMed:16723659,
CC PubMed:30454648). Within the RNase P complex, POP1, POP7 and RPP25 form
CC the 'finger' subcomplex, POP5, RPP14, RPP40 and homodimeric RPP30 form
CC the 'palm' subcomplex, and RPP21, POP4 and RPP38 form the 'wrist'
CC subcomplex. All subunits of the RNase P complex interact with the
CC catalytic RNA (PubMed:30454648). Several subunits of RNase P are also
CC part of the RNase MRP complex. RNase MRP consists of a catalytic RNA
CC moiety and about 8 protein subunits; POP1, POP7, RPP25, RPP30, RPP38,
CC RPP40 and possibly also POP4 and POP5 (PubMed:15096576,
CC PubMed:16723659, PubMed:28115465). Interacts with SMN1
CC (PubMed:14715275). POP7 forms a heterodimer with RPP25 that binds to
CC the P3 stem loop of the catalytic RNA (PubMed:15096576,
CC PubMed:20215441, PubMed:29625199). {ECO:0000269|PubMed:14715275,
CC ECO:0000269|PubMed:15096576, ECO:0000269|PubMed:16723659,
CC ECO:0000269|PubMed:20215441, ECO:0000269|PubMed:28115465,
CC ECO:0000269|PubMed:29625199, ECO:0000269|PubMed:30454648,
CC ECO:0000269|PubMed:9630247}.
CC -!- INTERACTION:
CC O75817; Q96LT7: C9orf72; NbExp=3; IntAct=EBI-366574, EBI-2961725;
CC O75817; Q14657: LAGE3; NbExp=3; IntAct=EBI-366574, EBI-1052105;
CC O75817; Q9BUL9: RPP25; NbExp=8; IntAct=EBI-366574, EBI-366570;
CC O75817; Q8N5L8: RPP25L; NbExp=12; IntAct=EBI-366574, EBI-10189722;
CC O75817; Q16637: SMN2; NbExp=5; IntAct=EBI-366574, EBI-395421;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14715275,
CC ECO:0000269|PubMed:20215441}. Cytoplasm {ECO:0000269|PubMed:14715275}.
CC Cytoplasmic granule {ECO:0000269|PubMed:14715275}. Note=Under stress
CC conditions colocalizes with SMN1 in punctuated cytoplasmic granules.
CC {ECO:0000269|PubMed:14715275}.
CC -!- SIMILARITY: Belongs to the histone-like Alba family. {ECO:0000305}.
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DR EMBL; U94316; AAC24113.1; -; mRNA.
DR EMBL; CH236956; EAL23821.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76495.1; -; Genomic_DNA.
DR EMBL; BC001430; AAH01430.1; -; mRNA.
DR CCDS; CCDS5704.1; -.
DR RefSeq; NP_005828.2; NM_005837.2.
DR PDB; 6AHR; EM; 3.92 A; G=1-140.
DR PDB; 6AHU; EM; 3.66 A; G=1-140.
DR PDB; 6CWX; X-ray; 2.25 A; A=1-140.
DR PDB; 6LT7; X-ray; 2.70 A; A/D=1-140.
DR PDBsum; 6AHR; -.
DR PDBsum; 6AHU; -.
DR PDBsum; 6CWX; -.
DR PDBsum; 6LT7; -.
DR AlphaFoldDB; O75817; -.
DR SMR; O75817; -.
DR BioGRID; 115542; 59.
DR CORUM; O75817; -.
DR IntAct; O75817; 25.
DR MINT; O75817; -.
DR STRING; 9606.ENSP00000304353; -.
DR iPTMnet; O75817; -.
DR PhosphoSitePlus; O75817; -.
DR BioMuta; POP7; -.
DR EPD; O75817; -.
DR jPOST; O75817; -.
DR MassIVE; O75817; -.
DR MaxQB; O75817; -.
DR PaxDb; O75817; -.
DR PeptideAtlas; O75817; -.
DR PRIDE; O75817; -.
DR ProteomicsDB; 50207; -.
DR Antibodypedia; 30824; 84 antibodies from 23 providers.
DR DNASU; 10248; -.
DR Ensembl; ENST00000303151.5; ENSP00000304353.4; ENSG00000172336.5.
DR GeneID; 10248; -.
DR KEGG; hsa:10248; -.
DR MANE-Select; ENST00000303151.5; ENSP00000304353.4; NM_005837.3; NP_005828.2.
DR UCSC; uc003uwh.5; human.
DR CTD; 10248; -.
DR DisGeNET; 10248; -.
DR GeneCards; POP7; -.
DR HGNC; HGNC:19949; POP7.
DR HPA; ENSG00000172336; Low tissue specificity.
DR MIM; 606113; gene.
DR neXtProt; NX_O75817; -.
DR OpenTargets; ENSG00000172336; -.
DR PharmGKB; PA134887425; -.
DR VEuPathDB; HostDB:ENSG00000172336; -.
DR eggNOG; KOG3631; Eukaryota.
DR GeneTree; ENSGT00510000048483; -.
DR InParanoid; O75817; -.
DR OMA; NDIYITR; -.
DR OrthoDB; 1433955at2759; -.
DR PhylomeDB; O75817; -.
DR TreeFam; TF313948; -.
DR BRENDA; 3.1.26.5; 2681.
DR PathwayCommons; O75817; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR SignaLink; O75817; -.
DR BioGRID-ORCS; 10248; 591 hits in 1081 CRISPR screens.
DR GeneWiki; POP7; -.
DR GenomeRNAi; 10248; -.
DR Pharos; O75817; Tbio.
DR PRO; PR:O75817; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O75817; protein.
DR Bgee; ENSG00000172336; Expressed in prefrontal cortex and 185 other tissues.
DR ExpressionAtlas; O75817; baseline and differential.
DR Genevisible; O75817; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030681; C:multimeric ribonuclease P complex; IDA:UniProtKB.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IEA:InterPro.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000172; C:ribonuclease MRP complex; IDA:FlyBase.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR GO; GO:0033204; F:ribonuclease P RNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR DisProt; DP02615; -.
DR Gene3D; 3.30.110.20; -; 1.
DR InterPro; IPR036882; Alba-like_dom_sf.
DR InterPro; IPR014612; Pop7/Rpp20.
DR PANTHER; PTHR15314; PTHR15314; 1.
DR Pfam; PF12328; Rpp20; 1.
DR PIRSF; PIRSF036572; RPP20; 1.
DR SUPFAM; SSF82704; SSF82704; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Nucleus;
KW Reference proteome; RNA-binding; rRNA processing; tRNA processing.
FT CHAIN 1..140
FT /note="Ribonuclease P protein subunit p20"
FT /id="PRO_0000058518"
FT MUTAGEN 40
FT /note="N->Q: Strongly reduced interaction with RPP25."
FT /evidence="ECO:0000269|PubMed:20215441"
FT CONFLICT 80
FT /note="R -> H (in Ref. 1; AAC24113)"
FT /evidence="ECO:0000305"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6CWX"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6CWX"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:6CWX"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:6CWX"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6CWX"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:6CWX"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:6CWX"
FT STRAND 96..112
FT /evidence="ECO:0007829|PDB:6CWX"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6LT7"
FT STRAND 121..136
FT /evidence="ECO:0007829|PDB:6CWX"
SQ SEQUENCE 140 AA; 15651 MW; CA380F7D273A64B3 CRC64;
MAENREPRGA VEAELDPVEY TLRKRLPSRL PRRPNDIYVN MKTDFKAQLA RCQKLLDGGA
RGQNACSEIY IHGLGLAINR AINIALQLQA GSFGSLQVAA NTSTVELVDE LEPETDTREP
LTRIRNNSAI HIRVFRVTPK
