ID   RM12_CRICR              Reviewed;         203 AA.
AC   P52827;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=39S ribosomal protein L12, mitochondrial;
DE            Short=L12mt;
DE            Short=MRP-L12;
DE   AltName: Full=P2A1;
DE   Flags: Precursor;
GN   Name=MRPL12; Synonyms=RPML12;
OS   Cricetus cricetus (Black-bellied hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetus.
OX   NCBI_TaxID=10034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=8626705; DOI=10.1074/jbc.271.19.11468;
RA   Marty L., Fort P.;
RT   "A delayed-early response nuclear gene encoding MRPL12, the mitochondrial
RT   homologue to the bacterial translational regulator L7/L12 protein.";
RL   J. Biol. Chem. 271:11468-11476(1996).
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:0000250|UniProtKB:P52815}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC       {ECO:0000305}.
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DR   EMBL; X79864; CAA56248.1; -; mRNA.
DR   AlphaFoldDB; P52827; -.
DR   SMR; P52827; -.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISS:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Acetylation; Mitochondrion; Ribonucleoprotein; Ribosomal protein;
KW   Transit peptide.
FT   TRANSIT         1..47
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..203
FT                   /note="39S ribosomal protein L12, mitochondrial"
FT                   /id="PRO_0000030457"
FT   MOD_RES         143
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DB15"
FT   MOD_RES         155
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DB15"
FT   MOD_RES         167
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DB15"
FT   MOD_RES         183
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DB15"
SQ   SEQUENCE   203 AA;  21650 MW;  E36B28AAC4E1DA07 CRC64;
     MLPAAAAAAS LWAPRLGLRG ARLRLARQQV PGVCAARQLS SSSQRRSEAL AGAPLDNAPK
     EYPPKIQQLV QDIASLTLLE ISDLNELLKK TLKIQDVGLM PMGGMMPGAV PAAAAAAPEV
     AEGEDILKQK ERTHFTVRLT EAKPVDKVKL IKEIKNYVQG INLVQAKKLV ESLPQEIKAN
     VAKAEAEKIK AALEAVGGTV VLE