RPP40_RAT
ID RPP40_RAT Reviewed; 363 AA.
AC Q5BK64;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Ribonuclease P protein subunit p40;
DE Short=RNaseP protein p40;
GN Name=Rpp40;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
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: Component of ribonuclease P, a ribonucleoprotein complex that
CC generates mature tRNA molecules by cleaving their 5'-ends. Also a
CC component of the MRP ribonuclease complex, which cleaves pre-rRNA
CC sequences. {ECO:0000250|UniProtKB:O75818}.
CC -!- SUBUNIT: Component of nuclear RNase P and RNase MRP ribonucleoproteins.
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. Within the RNase P complex, POP1, POP7 and RPP25 form the
CC 'finger' subcomplex, POP5, RPP14, RPP40 and homodimeric RPP30 form the
CC '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. Several subunits of RNase P are also part of the RNase
CC MRP complex. RNase MRP consists of a catalytic RNA moiety and about 8
CC protein subunits; POP1, POP7, RPP25, RPP30, RPP38, RPP40 and possibly
CC also POP4 and POP5. {ECO:0000250|UniProtKB:O75818}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5BK64-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5BK64-2; Sequence=VSP_037347;
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DR EMBL; AABR03105027; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC091191; AAH91191.1; -; mRNA.
DR RefSeq; NP_001013073.1; NM_001013055.1. [Q5BK64-2]
DR RefSeq; XP_006253852.1; XM_006253790.2. [Q5BK64-1]
DR AlphaFoldDB; Q5BK64; -.
DR SMR; Q5BK64; -.
DR STRING; 10116.ENSRNOP00000062962; -.
DR jPOST; Q5BK64; -.
DR PaxDb; Q5BK64; -.
DR PRIDE; Q5BK64; -.
DR Ensembl; ENSRNOT00000021877; ENSRNOP00000021877; ENSRNOG00000016226. [Q5BK64-2]
DR GeneID; 291071; -.
DR KEGG; rno:291071; -.
DR UCSC; RGD:1310228; rat. [Q5BK64-1]
DR CTD; 10799; -.
DR RGD; 1310228; Rpp40.
DR VEuPathDB; HostDB:ENSRNOG00000016226; -.
DR eggNOG; ENOG502QSAV; Eukaryota.
DR GeneTree; ENSGT00390000014167; -.
DR HOGENOM; CLU_065211_0_0_1; -.
DR InParanoid; Q5BK64; -.
DR OMA; LQWETGF; -.
DR OrthoDB; 1273379at2759; -.
DR PhylomeDB; Q5BK64; -.
DR TreeFam; TF330967; -.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q5BK64; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000016226; Expressed in spleen and 19 other tissues.
DR Genevisible; Q5BK64; RN.
DR GO; GO:0030681; C:multimeric ribonuclease P complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0000172; C:ribonuclease MRP complex; IBA:GO_Central.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR GO; GO:0033204; F:ribonuclease P RNA binding; ISS: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; ISS:UniProtKB.
DR InterPro; IPR013893; RNase_P_Rpp40.
DR PANTHER; PTHR15396; PTHR15396; 1.
DR Pfam; PF08584; Ribonuc_P_40; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Nucleus; Reference proteome; rRNA processing;
KW tRNA processing.
FT CHAIN 1..363
FT /note="Ribonuclease P protein subunit p40"
FT /id="PRO_0000354077"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037347"
SQ SEQUENCE 363 AA; 41640 MW; 11A8BA4ECB7063DF CRC64;
MATLRRLQEA PRHLLVCEKS NFGHDKSRHK HLVETHYHNY RVSFLIPECG LLSKKLKDLV
MEMGPYYSVK KLPLHELITH EFINTFVKKG SLSALTYNTS IDEDNTVALL PNGKLILSLD
KDTYEETGLQ GHPSRYSGRK SMRFIISIDL MDLSLNLDSK KYRRISWSFK EKKPLKFDFL
LAWHHTGTEE STMMSYFSKY QIREHQPKVA LSTVRDLQCP VLQSSSLAGE PEEACNALEF
FDWLGAVFCN ADLNNEPHNF ISTYCCPQPN TVAAQACLCT ITGFVLPEKI LVLLEQLCHY
FDEPKLAPWV TLTVQGFADS PVAWREKEHG FHKGGEHLYN FVVFNNQDYW LQMAVGANDD
CPP