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RM44_MOUSE
ID   RM44_MOUSE              Reviewed;         333 AA.
AC   Q9CY73; Q3U0J0; Q8VE61;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=39S ribosomal protein L44, mitochondrial;
DE            Short=L44mt;
DE            Short=MRP-L44;
DE            EC=3.1.26.-;
DE   Flags: Precursor;
GN   Name=Mrpl44;
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] (ISOFORM 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
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 GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 219-333.
RC   STRAIN=Czech II; TISSUE=Mammary gland;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, and Testis;
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 the 39S subunit of mitochondrial ribosome. May
CC       have a function in the assembly/stability of nascent mitochondrial
CC       polypeptides exiting the ribosome. {ECO:0000250|UniProtKB:Q9H9J2}.
CC   -!- SUBUNIT: Component of the mitochondrial ribosome large subunit (39S)
CC       which comprises a 16S rRNA and about 50 distinct proteins.
CC       {ECO:0000250|UniProtKB:Q9H9J2}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9H9J2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CY73-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CY73-2; Sequence=VSP_014126, VSP_014127;
CC   -!- SIMILARITY: Belongs to the ribonuclease III family. Mitochondrion-
CC       specific ribosomal protein mL44 subfamily. {ECO:0000305}.
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DR   EMBL; AK019986; BAB31953.1; -; mRNA.
DR   EMBL; AK156814; BAE33863.1; -; mRNA.
DR   EMBL; CH466687; EDL16270.1; -; Genomic_DNA.
DR   EMBL; BC019727; AAH19727.1; -; mRNA.
DR   CCDS; CCDS35629.1; -. [Q9CY73-1]
DR   RefSeq; NP_001074679.1; NM_001081210.1. [Q9CY73-1]
DR   AlphaFoldDB; Q9CY73; -.
DR   SMR; Q9CY73; -.
DR   BioGRID; 213264; 3.
DR   ComplexPortal; CPX-5302; 39S mitochondrial large ribosomal subunit.
DR   STRING; 10090.ENSMUSP00000027464; -.
DR   iPTMnet; Q9CY73; -.
DR   PhosphoSitePlus; Q9CY73; -.
DR   EPD; Q9CY73; -.
DR   MaxQB; Q9CY73; -.
DR   PaxDb; Q9CY73; -.
DR   PeptideAtlas; Q9CY73; -.
DR   PRIDE; Q9CY73; -.
DR   ProteomicsDB; 299862; -. [Q9CY73-1]
DR   ProteomicsDB; 299863; -. [Q9CY73-2]
DR   Antibodypedia; 34365; 164 antibodies from 23 providers.
DR   Ensembl; ENSMUST00000027464; ENSMUSP00000027464; ENSMUSG00000026248. [Q9CY73-1]
DR   GeneID; 69163; -.
DR   KEGG; mmu:69163; -.
DR   UCSC; uc007bqx.1; mouse. [Q9CY73-2]
DR   UCSC; uc007bqy.1; mouse. [Q9CY73-1]
DR   CTD; 65080; -.
DR   MGI; MGI:1916413; Mrpl44.
DR   VEuPathDB; HostDB:ENSMUSG00000026248; -.
DR   eggNOG; KOG3769; Eukaryota.
DR   GeneTree; ENSGT00390000016956; -.
DR   HOGENOM; CLU_058895_0_0_1; -.
DR   InParanoid; Q9CY73; -.
DR   OMA; RHIKRWV; -.
DR   OrthoDB; 877695at2759; -.
DR   PhylomeDB; Q9CY73; -.
DR   TreeFam; TF324185; -.
DR   Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR   Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR   BioGRID-ORCS; 69163; 23 hits in 75 CRISPR screens.
DR   PRO; PR:Q9CY73; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q9CY73; protein.
DR   Bgee; ENSMUSG00000026248; Expressed in paneth cell and 264 other tissues.
DR   Genevisible; Q9CY73; MM.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR   GO; GO:0070125; P:mitochondrial translational elongation; ISS:UniProtKB.
DR   GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR   CDD; cd19874; DSRM_MRPL44; 1.
DR   Gene3D; 1.10.1520.10; -; 1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR044444; MRPL44_DSRM.
DR   InterPro; IPR011907; RNase_III.
DR   InterPro; IPR036389; RNase_III_sf.
DR   PANTHER; PTHR11207; PTHR11207; 1.
DR   SUPFAM; SSF69065; SSF69065; 1.
DR   PROSITE; PS50137; DS_RBD; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endonuclease; Hydrolase; Mitochondrion; Nuclease;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   Transit peptide.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           31..333
FT                   /note="39S ribosomal protein L44, mitochondrial"
FT                   /id="PRO_0000030822"
FT   DOMAIN          86..228
FT                   /note="RNase III"
FT   DOMAIN          236..306
FT                   /note="DRBM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT   REGION          311..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         217..220
FT                   /note="DFLI -> VGNG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014126"
FT   VAR_SEQ         221..333
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014127"
FT   CONFLICT        233
FT                   /note="T -> P (in Ref. 3; AAH19727)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        249
FT                   /note="N -> D (in Ref. 3; AAH19727)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   333 AA;  37527 MW;  D67C3BAC854DFD32 CRC64;
     MASAVFRLLQ QGPRRLLAPA VPTLAPPVRG VKKGFRAAFR FQKELERWRL LRCPPPPVRR
     SEKPNWDYHA EVQAFGSRLQ ETFSLDLLKT AFINSCYIKS EEAKRQSLGI EKEAALLNLK
     DNQELFEQGL SFSHRCLTQF LEDEFPDLPA EGTESLVSFL TGEAVVCHVA RNLAVEQLTL
     SAEFPVPLPV LRQTFFAVIG ALLQSSGPER AALFIRDFLI TQMTGKELFE MWTVVNPMGL
     LVEELKKRNI SAPESRLTRQ SGSTTALPLY FVGLYCDRKL IAEGPGETVL VAEEEAARVA
     LRKLYGFTEN RRPWDYSKPK ESPKRAEQTS VAS
 
 
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