RM12_BOVIN
ID RM12_BOVIN Reviewed; 198 AA.
AC Q7YR75; A5D9H8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=39S ribosomal protein L12, mitochondrial;
DE Short=L12mt;
DE Short=MRP-L12;
DE Flags: Precursor;
GN Name=MRPL12;
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 [MRNA].
RX PubMed=14757048; DOI=10.1016/j.jmb.2003.12.034;
RA Terasaki M., Suzuki T., Hanada T., Watanabe K.;
RT "Functional compatibility of elongation factors between mammalian
RT mitochondrial and bacterial ribosomes: characterization of GTPase activity
RT and translation elongation by hybrid ribosomes bearing heterologous L7/12
RT proteins.";
RL J. Mol. Biol. 336:331-342(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 45-69, AND SUBCELLULAR LOCATION.
RX PubMed=10600119; DOI=10.1021/bi991543s;
RA Graack H.R., Bryant M.L., O'Brien T.W.;
RT "Identification of mammalian mitochondrial ribosomal proteins (MRPs) by N-
RT terminal sequencing of purified bovine MRPs and comparison to data bank
RT sequences: the large subribosomal particle.";
RL Biochemistry 38:16569-16577(1999).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.1 ANGSTROMS) OF 62-198.
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 -!- FUNCTION: As a component of the mitochondrial large ribosomal subunit,
CC it plays a role in mitochondrial translation. Associates with
CC mitochondrial RNA polymerase to activate transcription.
CC {ECO:0000250|UniProtKB:P52815}.
CC -!- SUBUNIT: Component of the mitochondrial ribosome large subunit (39S)
CC which comprises a 16S rRNA and about 50 distinct proteins (By
CC similarity). Interacts with NOA1. {ECO:0000250|UniProtKB:P52815}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10600119}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC {ECO:0000305}.
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DR EMBL; AB116379; BAC81567.1; -; mRNA.
DR EMBL; BT020735; AAX08752.1; -; mRNA.
DR EMBL; BT020755; AAX08772.1; -; mRNA.
DR EMBL; BT020982; AAX08999.1; -; mRNA.
DR EMBL; BT030597; ABQ13037.1; -; mRNA.
DR EMBL; BC134767; AAI34768.1; -; mRNA.
DR RefSeq; NP_963900.1; NM_201606.2.
DR PDB; 2FTC; EM; 12.10 A; E/F=62-198.
DR PDBsum; 2FTC; -.
DR AlphaFoldDB; Q7YR75; -.
DR SMR; Q7YR75; -.
DR STRING; 9913.ENSBTAP00000000534; -.
DR PaxDb; Q7YR75; -.
DR PRIDE; Q7YR75; -.
DR Ensembl; ENSBTAT00000053193; ENSBTAP00000048266; ENSBTAG00000000417.
DR GeneID; 399560; -.
DR KEGG; bta:399560; -.
DR CTD; 6182; -.
DR VEuPathDB; HostDB:ENSBTAG00000000417; -.
DR VGNC; VGNC:106827; MRPL12.
DR eggNOG; KOG0759; Eukaryota.
DR eggNOG; KOG1715; Eukaryota.
DR GeneTree; ENSGT00390000000190; -.
DR InParanoid; Q7YR75; -.
DR OMA; LEDKWGV; -.
DR OrthoDB; 1626139at2759; -.
DR EvolutionaryTrace; Q7YR75; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000000417; Expressed in digestive system secreted substance and 105 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:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006390; P:mitochondrial transcription; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd00387; Ribosomal_L7_L12; 1.
DR Gene3D; 1.20.5.710; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR HAMAP; MF_00368; Ribosomal_L7_L12; 1.
DR InterPro; IPR000206; Ribosomal_L7/12.
DR InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR InterPro; IPR013823; Ribosomal_L7/L12_C.
DR InterPro; IPR008932; Ribosomal_L7/L12_oligo.
DR InterPro; IPR036235; Ribosomal_L7/L12_oligo_N_sf.
DR PANTHER; PTHR45987; PTHR45987; 1.
DR Pfam; PF00542; Ribosomal_L12; 1.
DR Pfam; PF16320; Ribosomal_L12_N; 1.
DR SUPFAM; SSF48300; SSF48300; 1.
DR SUPFAM; SSF54736; SSF54736; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Mitochondrion;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT CHAIN 46..198
FT /note="39S ribosomal protein L12, mitochondrial"
FT /id="PRO_0000239700"
FT REGION 106..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 138
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB15"
FT MOD_RES 150
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB15"
FT MOD_RES 162
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB15"
FT MOD_RES 178
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB15"
SQ SEQUENCE 198 AA; 21400 MW; 3A98308C159F3493 CRC64;
MLPSATSLLR GPCLGLRAAA LRLVRQQVPH VCAVRLMRCS SHRRGEALTG APLDNAPKEY
PPKIQQLVQD IASLTLLEIS DLNELLKKTL KIQDVGLMPM GGMVPGAAPA PTAPEAAEED
VPKQKERTHF TVRLTEAKPV DKVKLIKEIK NYVQGINLVQ AKKLVESLPQ EIKANVAKAE
AEKIKAALEA VGGTVVLE
