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RM02_BOVIN
ID   RM02_BOVIN              Reviewed;         306 AA.
AC   Q2TA12;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=39S ribosomal protein L2, mitochondrial;
DE            Short=L2mt;
DE            Short=MRP-L2;
DE   Flags: Precursor;
GN   Name=MRPL2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=11279069; DOI=10.1074/jbc.m100432200;
RA   Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA   Watanabe K.;
RT   "Structural compensation for the deficit of rRNA with proteins in the
RT   mammalian mitochondrial ribosome. Systematic analysis of protein components
RT   of the large ribosomal subunit from mammalian mitochondria.";
RL   J. Biol. Chem. 276:21724-21736(2001).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=11551941; DOI=10.1074/jbc.m106510200;
RA   Koc E.C., Burkhart W., Blackburn K., Moyer M.B., Schlatzer D.M.,
RA   Moseley A., Spremulli L.L.;
RT   "The large subunit of the mammalian mitochondrial ribosome. Analysis of the
RT   complement of ribosomal proteins present.";
RL   J. Biol. Chem. 276:43958-43969(2001).
RN   [4]
RP   STRUCTURE BY ELECTRON MICROSCOPY (12 ANGSTROMS), AND SUBCELLULAR LOCATION.
RX   PubMed=16510155; DOI=10.1016/j.jmb.2006.01.094;
RA   Mears J.A., Sharma M.R., Gutell R.R., McCook A.S., Richardson P.E.,
RA   Caulfield T.R., Agrawal R.K., Harvey S.C.;
RT   "A structural model for the large subunit of the mammalian mitochondrial
RT   ribosome.";
RL   J. Mol. Biol. 358:193-212(2006).
CC   -!- SUBUNIT: Component of the mitochondrial ribosome large subunit (39S)
CC       which comprises a 16S rRNA and about 50 distinct proteins.
CC       {ECO:0000269|PubMed:11279069}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11279069,
CC       ECO:0000269|PubMed:11551941, ECO:0000269|PubMed:16510155}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BC111173; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC111173; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001035617.2; NM_001040527.3.
DR   PDB; 2FTC; EM; -; B=127-262.
DR   PDB; 3IY9; EM; 14.10 A; B=127-262.
DR   PDBsum; 2FTC; -.
DR   PDBsum; 3IY9; -.
DR   AlphaFoldDB; Q2TA12; -.
DR   SMR; Q2TA12; -.
DR   IntAct; Q2TA12; 1.
DR   STRING; 9913.ENSBTAP00000016951; -.
DR   iPTMnet; Q2TA12; -.
DR   PaxDb; Q2TA12; -.
DR   Ensembl; ENSBTAT00000016951; ENSBTAP00000016951; ENSBTAG00000012752.
DR   GeneID; 514403; -.
DR   KEGG; bta:514403; -.
DR   CTD; 51069; -.
DR   VEuPathDB; HostDB:ENSBTAG00000012752; -.
DR   VGNC; VGNC:31623; MRPL2.
DR   eggNOG; KOG0438; Eukaryota.
DR   GeneTree; ENSGT00940000153244; -.
DR   HOGENOM; CLU_036235_1_2_1; -.
DR   InParanoid; Q2TA12; -.
DR   OMA; CHLIHAA; -.
DR   OrthoDB; 1156335at2759; -.
DR   TreeFam; TF314647; -.
DR   EvolutionaryTrace; Q2TA12; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000012752; Expressed in tongue muscle and 106 other tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR002171; Ribosomal_L2.
DR   InterPro; IPR022669; Ribosomal_L2_C.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR13691; PTHR13691; 1.
DR   Pfam; PF00181; Ribosomal_L2; 1.
DR   Pfam; PF03947; Ribosomal_L2_C; 1.
DR   SMART; SM01383; Ribosomal_L2; 1.
DR   SMART; SM01382; Ribosomal_L2_C; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; Transit peptide.
FT   TRANSIT         1..60
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           61..306
FT                   /note="39S ribosomal protein L2, mitochondrial"
FT                   /id="PRO_0000261639"
SQ   SEQUENCE   306 AA;  33344 MW;  6E616AF1E0B405BF CRC64;
     MALRVVTRAL GSLSLTPRIA AVPGPSLLPA AQVTNNVLLQ LPSASMLLPS RPLLTSVALS
     AKFVSWKSRT KYTTMPVKMR KSGGRNHTGR IQVHGIGGGH KQRYRMIDFL RFRPEQESKP
     GPFEEKVIVV RYDPCRSADI ALVAGGNRKR WIIATENMKA GDTILNSDHI GRMAVAAREG
     DAHPLGALPV GTLINNVESE PGRGAQYIRA AGTCGVLLRK VNGTAIIQLP SKRQMQVLET
     CTATVGRVSN VDHNKRVIGK AGRNRWLGKR PNSGRWHRKG GWAGRKIRPL PPMKSYVKLP
     SAAAQN
 
 
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