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POP7_MOUSE
ID   POP7_MOUSE              Reviewed;         140 AA.
AC   Q9DCH2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Ribonuclease P protein subunit p20;
DE            Short=RNaseP protein p20;
GN   Name=Pop7; Synonyms=Rpp20;
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 [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA   Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA   Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W.,
RA   Koop B.F.;
RT   "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT   chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL   Nucleic Acids Res. 29:1352-1365(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Egg, Kidney, and Visual cortex;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
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:O75817}.
CC   -!- SUBUNIT: Component of nuclear RNase P and RNase MRP complexes. RNase P
CC       consists of a catalytic RNA moiety and 10 different protein chains;
CC       POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25, RPP30, RPP38 and RPP40.
CC       Within the RNase P complex, POP1, POP7 and RPP25 form the 'finger'
CC       subcomplex, POP5, RPP14, RPP40 and homodimeric RPP30 form the 'palm'
CC       subcomplex, and RPP21, POP4 and RPP38 form the 'wrist' subcomplex. All
CC       subunits of the RNase P complex interact with the catalytic RNA.
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. Interacts with SMN1. POP7 forms a heterodimer with RPP25 that
CC       binds to the P3 stem loop of the catalytic RNA.
CC       {ECO:0000250|UniProtKB:O75817}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:O75817}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O75817}. Cytoplasmic granule
CC       {ECO:0000250|UniProtKB:O75817}. Note=Under stress conditions
CC       colocalizes with SMN1 in punctuated cytoplasmic granules.
CC       {ECO:0000250|UniProtKB:O75817}.
CC   -!- SIMILARITY: Belongs to the histone-like Alba family. {ECO:0000305}.
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DR   EMBL; AF312033; AAK28826.1; -; Genomic_DNA.
DR   EMBL; AK002782; BAB22355.1; -; mRNA.
DR   EMBL; AK158620; BAE34584.1; -; mRNA.
DR   EMBL; AK162268; BAE36826.1; -; mRNA.
DR   EMBL; BC010780; AAH10780.1; -; mRNA.
DR   CCDS; CCDS19768.1; -.
DR   RefSeq; NP_083029.1; NM_028753.2.
DR   AlphaFoldDB; Q9DCH2; -.
DR   SMR; Q9DCH2; -.
DR   STRING; 10090.ENSMUSP00000106664; -.
DR   PhosphoSitePlus; Q9DCH2; -.
DR   EPD; Q9DCH2; -.
DR   MaxQB; Q9DCH2; -.
DR   PaxDb; Q9DCH2; -.
DR   PeptideAtlas; Q9DCH2; -.
DR   PRIDE; Q9DCH2; -.
DR   ProteomicsDB; 289789; -.
DR   Antibodypedia; 30824; 84 antibodies from 23 providers.
DR   DNASU; 74097; -.
DR   Ensembl; ENSMUST00000031728; ENSMUSP00000031728; ENSMUSG00000029715.
DR   Ensembl; ENSMUST00000111035; ENSMUSP00000106664; ENSMUSG00000029715.
DR   GeneID; 74097; -.
DR   KEGG; mmu:74097; -.
DR   UCSC; uc009aco.1; mouse.
DR   CTD; 10248; -.
DR   MGI; MGI:1921347; Pop7.
DR   VEuPathDB; HostDB:ENSMUSG00000029715; -.
DR   eggNOG; KOG3631; Eukaryota.
DR   GeneTree; ENSGT00510000048483; -.
DR   HOGENOM; CLU_130587_1_0_1; -.
DR   InParanoid; Q9DCH2; -.
DR   OMA; NDIYITR; -.
DR   OrthoDB; 1433955at2759; -.
DR   PhylomeDB; Q9DCH2; -.
DR   TreeFam; TF313948; -.
DR   BioGRID-ORCS; 74097; 27 hits in 77 CRISPR screens.
DR   ChiTaRS; Pop7; mouse.
DR   PRO; PR:Q9DCH2; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9DCH2; protein.
DR   Bgee; ENSMUSG00000029715; Expressed in dorsal pancreas and 247 other tissues.
DR   Genevisible; Q9DCH2; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; 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:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000172; C:ribonuclease MRP complex; ISO:MGI.
DR   GO; GO:0004526; F:ribonuclease P activity; ISO:MGI.
DR   GO; GO:0033204; F:ribonuclease P RNA binding; ISS: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; ISS:UniProtKB.
DR   GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Reference proteome; rRNA processing; tRNA processing.
FT   CHAIN           1..140
FT                   /note="Ribonuclease P protein subunit p20"
FT                   /id="PRO_0000237701"
SQ   SEQUENCE   140 AA;  15777 MW;  0F30841C7F50DFA4 CRC64;
     MAENREPRCA IEAELDPVEY TLRKRLPHRL PRRPNDIYVN MKTDFKAQLA RCQKLLDGGT
     RGQNACTEIY IHGLGLAINR AINIALQLQA GSFGSLQVAA NTSTVELVDE LEPETDSREP
     LTRVRNNSAI HIRVFRVTPK
 
 
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