RPP40_HUMAN
ID RPP40_HUMAN Reviewed; 363 AA.
AC O75818; Q5VX97; Q8WVK8;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Ribonuclease P protein subunit p40;
DE Short=RNaseP protein p40;
DE AltName: Full=RNase P subunit 1;
GN Name=RPP40; Synonyms=RNASEP1;
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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-363, PROTEIN SEQUENCE OF 73-87;
RP 116-125 AND 202-208 (ISOFORM 1), FUNCTION, AND SUBUNIT.
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 [4]
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 [5]
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 [6] {ECO:0007744|PDB:6AHR, ECO:0007744|PDB:6AHU, ECO:0007744|PDB:6AHV}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF RNASE P HOLOENZYME IN COMPLEX
RP 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).
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 ribonucleoproteins
CC (PubMed:9630247, PubMed:16723659, PubMed:28115465, PubMed:30454648).
CC RNase P consists of a catalytic RNA moiety and about 10 protein
CC subunits; POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25, RPP30, RPP38 and
CC RPP40 (PubMed:9630247, PubMed:16723659, PubMed:30454648). Within the
CC RNase P complex, POP1, POP7 and RPP25 form the 'finger' subcomplex,
CC POP5, RPP14, RPP40 and homodimeric RPP30 form the 'palm' subcomplex,
CC and RPP21, POP4 and RPP38 form the 'wrist' subcomplex. All subunits of
CC the RNase P complex interact with the catalytic RNA (PubMed:30454648).
CC Several subunits of RNase P are also part of the RNase MRP complex.
CC RNase MRP consists of a catalytic RNA moiety and about 8 protein
CC subunits; POP1, POP7, RPP25, RPP30, RPP38, RPP40 and possibly also POP4
CC and POP5 (PubMed:16723659, PubMed:28115465).
CC {ECO:0000269|PubMed:16723659, ECO:0000269|PubMed:28115465,
CC ECO:0000269|PubMed:30454648, ECO:0000269|PubMed:9630247}.
CC -!- INTERACTION:
CC O75818; Q9H633: RPP21; NbExp=2; IntAct=EBI-366505, EBI-366586;
CC O75818-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12401132, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75818-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75818-2; Sequence=VSP_037346;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24114.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH17871.1; Type=Frameshift; Evidence={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; AL359643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017871; AAH17871.1; ALT_SEQ; mRNA.
DR EMBL; U94317; AAC24114.1; ALT_INIT; Genomic_DNA.
DR CCDS; CCDS34333.1; -. [O75818-1]
DR CCDS; CCDS69040.1; -. [O75818-2]
DR RefSeq; NP_001273061.1; NM_001286132.1. [O75818-2]
DR RefSeq; NP_001273062.1; NM_001286133.1.
DR RefSeq; NP_006629.2; NM_006638.3. [O75818-1]
DR PDB; 6AHR; EM; 3.92 A; L=1-363.
DR PDB; 6AHU; EM; 3.66 A; L=1-363.
DR PDB; 6AHV; X-ray; 2.60 A; A=1-363.
DR PDBsum; 6AHR; -.
DR PDBsum; 6AHU; -.
DR PDBsum; 6AHV; -.
DR AlphaFoldDB; O75818; -.
DR SMR; O75818; -.
DR BioGRID; 116013; 51.
DR CORUM; O75818; -.
DR IntAct; O75818; 16.
DR STRING; 9606.ENSP00000369391; -.
DR iPTMnet; O75818; -.
DR PhosphoSitePlus; O75818; -.
DR BioMuta; RPP40; -.
DR EPD; O75818; -.
DR jPOST; O75818; -.
DR MassIVE; O75818; -.
DR MaxQB; O75818; -.
DR PaxDb; O75818; -.
DR PeptideAtlas; O75818; -.
DR PRIDE; O75818; -.
DR ProteomicsDB; 50208; -. [O75818-1]
DR ProteomicsDB; 50209; -. [O75818-2]
DR Antibodypedia; 24532; 77 antibodies from 20 providers.
DR DNASU; 10799; -.
DR Ensembl; ENST00000319533.9; ENSP00000317998.5; ENSG00000124787.14. [O75818-2]
DR Ensembl; ENST00000380051.7; ENSP00000369391.2; ENSG00000124787.14. [O75818-1]
DR GeneID; 10799; -.
DR KEGG; hsa:10799; -.
DR MANE-Select; ENST00000380051.7; ENSP00000369391.2; NM_006638.4; NP_006629.2.
DR UCSC; uc003mwl.5; human. [O75818-1]
DR CTD; 10799; -.
DR GeneCards; RPP40; -.
DR HGNC; HGNC:20992; RPP40.
DR HPA; ENSG00000124787; Low tissue specificity.
DR MIM; 606117; gene.
DR neXtProt; NX_O75818; -.
DR OpenTargets; ENSG00000124787; -.
DR PharmGKB; PA134911809; -.
DR VEuPathDB; HostDB:ENSG00000124787; -.
DR eggNOG; ENOG502QSAV; Eukaryota.
DR GeneTree; ENSGT00390000014167; -.
DR InParanoid; O75818; -.
DR OMA; LQWETGF; -.
DR OrthoDB; 1273379at2759; -.
DR PhylomeDB; O75818; -.
DR TreeFam; TF330967; -.
DR BRENDA; 3.1.26.5; 2681.
DR PathwayCommons; O75818; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; O75818; -.
DR BioGRID-ORCS; 10799; 610 hits in 1086 CRISPR screens.
DR ChiTaRS; RPP40; human.
DR GeneWiki; RPP40; -.
DR GenomeRNAi; 10799; -.
DR Pharos; O75818; Tbio.
DR PRO; PR:O75818; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O75818; protein.
DR Bgee; ENSG00000124787; Expressed in adrenal tissue and 162 other tissues.
DR ExpressionAtlas; O75818; baseline and differential.
DR Genevisible; O75818; HS.
DR GO; GO:0030681; C:multimeric ribonuclease P complex; IDA:UniProtKB.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0000172; C:ribonuclease MRP complex; IBA:GO_Central.
DR GO; GO:0004526; F:ribonuclease P activity; TAS:ProtInc.
DR GO; GO:0033204; F:ribonuclease P RNA binding; IDA:UniProtKB.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:1905267; P:endonucleolytic cleavage involved in tRNA processing; IBA:GO_Central.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:UniProtKB.
DR InterPro; IPR013893; RNase_P_Rpp40.
DR PANTHER; PTHR15396; PTHR15396; 1.
DR Pfam; PF08584; Ribonuc_P_40; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing; Nucleus;
KW Reference proteome; RNA-binding; rRNA processing; tRNA processing.
FT CHAIN 1..363
FT /note="Ribonuclease P protein subunit p40"
FT /id="PRO_0000097434"
FT VAR_SEQ 90..112
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037346"
FT VARIANT 314
FT /note="V -> I (in dbSNP:rs12332997)"
FT /id="VAR_055405"
FT CONFLICT 255
FT /note="Missing (in Ref. 3; AAC24114)"
FT /evidence="ECO:0000305"
FT STRAND 13..21
FT /evidence="ECO:0007829|PDB:6AHV"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 39..48
FT /evidence="ECO:0007829|PDB:6AHV"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:6AHV"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:6AHV"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:6AHV"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:6AHV"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:6AHV"
FT HELIX 121..127
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 132..149
FT /evidence="ECO:0007829|PDB:6AHV"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:6AHV"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:6AHV"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 176..185
FT /evidence="ECO:0007829|PDB:6AHV"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:6AHV"
FT TURN 197..201
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 208..220
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6AHV"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:6AHV"
FT HELIX 237..253
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 268..285
FT /evidence="ECO:0007829|PDB:6AHV"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:6AHV"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 308..316
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:6AHV"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:6AHV"
SQ SEQUENCE 363 AA; 41834 MW; 9B4495BA6CD40E79 CRC64;
MATLRRLREA PRHLLVCEKS NFGNHKSRHR HLVQTHYYNY RVSFLIPECG ILSEELKNLV
MNTGPYYFVK NLPLHELITP EFISTFIKKG SCYALTYNTH IDEDNTVALL PNGKLILSLD
KDTYEETGLQ GHPSQFSGRK IMKFIVSIDL MELSLNLDSK KYERISWSFK EKKPLKFDFL
LAWHKTGSEE STMMSYFSKY QIQEHQPKVA LSTLRDLQCP VLQSSELEGT PEVSCRALEL
FDWLGAVFSN VDLNNEPNNF ISTYCCPEPS TVVAKAYLCT ITGFILPEKI CLLLEHLCHY
FDEPKLAPWV TLSVQGFADS PVSWEKNEHG FRKGGEHLYN FVIFNNQDYW LQMAVGANDH
CPP
