RPP38_MOUSE
ID RPP38_MOUSE Reviewed; 280 AA.
AC Q80UU2; Q3UTW5; Q8BU46;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Ribonuclease P protein subunit p38;
DE Short=RNaseP protein p38;
GN Name=Rpp38;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Ovary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/He; TISSUE=Mesenchymal stem cell;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:P78345}.
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:P78345}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P78345}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC {ECO:0000305}.
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DR EMBL; BC051448; AAH51448.1; -; mRNA.
DR EMBL; AK087782; BAC40000.1; -; mRNA.
DR EMBL; AK139023; BAE23865.1; -; mRNA.
DR CCDS; CCDS15645.1; -.
DR AlphaFoldDB; Q80UU2; -.
DR SMR; Q80UU2; -.
DR STRING; 10090.ENSMUSP00000050992; -.
DR iPTMnet; Q80UU2; -.
DR PhosphoSitePlus; Q80UU2; -.
DR EPD; Q80UU2; -.
DR MaxQB; Q80UU2; -.
DR PaxDb; Q80UU2; -.
DR PRIDE; Q80UU2; -.
DR ProteomicsDB; 300486; -.
DR MGI; MGI:2443607; Rpp38.
DR eggNOG; KOG3387; Eukaryota.
DR InParanoid; Q80UU2; -.
DR PhylomeDB; Q80UU2; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q80UU2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80UU2; protein.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0030681; C:multimeric ribonuclease P complex; ISS:UniProtKB.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IEA:InterPro.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0000172; C:ribonuclease MRP complex; IEA:InterPro.
DR GO; GO:0004526; F:ribonuclease P activity; ISO:MGI.
DR GO; GO:0033204; F:ribonuclease P RNA binding; ISS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0001682; P:tRNA 5'-leader removal; ISS:UniProtKB.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR042848; Rpp38.
DR PANTHER; PTHR46948; PTHR46948; 1.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
PE 1: Evidence at protein level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome; rRNA processing;
KW tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P78345"
FT CHAIN 2..280
FT /note="Ribonuclease P protein subunit p38"
FT /id="PRO_0000136784"
FT REGION 202..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..280
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P78345"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78345"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78345"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78345"
FT CONFLICT 26
FT /note="N -> D (in Ref. 1; BAE23865)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="Q -> K (in Ref. 1; BAE23865)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="S -> F (in Ref. 1; BAC40000/BAE23865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 31129 MW; E0AAF663AEEAB4F3 CRC64;
MAAAPQAPKR GSIRKTRPLV VKTSLNNPYV ISWSTLERED IHFILQTLEA KFKLIGLQKI
EDKKKRKKTA LMKKQSCRPD IEISEDPKEP DGDVLVSGWT PVHVRKQLVI GVNEVTRALE
RNELLLVLVC KSVKPAIITS HLIQLSLSRT VPACQVPQLS ERIAPVIGLK CVLALGSRKN
TRDFADEVEA IIPRVPSLNV PWLPDRTQGP TDSLETEPSE SQDNEILDTS FDDLTKLSKR
KLAEGGQASA ATLQPLKIKK LIPNPSKIRK PPKSKKSISK
