GenomeNet

Database: UniProt
Entry: D3ZXF9_RAT
LinkDB: D3ZXF9_RAT
Original site: D3ZXF9_RAT 
ID   D3ZXF9_RAT              Unreviewed;       276 AA.
AC   D3ZXF9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 83.
DE   SubName: Full=Mitochondrial ribosomal protein L12 {ECO:0000313|Ensembl:ENSRNOP00000051848.1};
GN   Name=Mrpl12 {ECO:0000313|Ensembl:ENSRNOP00000051848.1,
GN   ECO:0000313|RGD:1588559};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000051848.1, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000051848.1, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000051848.1,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000051848.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000051848.1};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC       {ECO:0000256|ARBA:ARBA00007197}.
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DR   RefSeq; NP_001025071.1; NM_001029900.1.
DR   AlphaFoldDB; D3ZXF9; -.
DR   SMR; D3ZXF9; -.
DR   STRING; 10116.ENSRNOP00000051848; -.
DR   PhosphoSitePlus; D3ZXF9; -.
DR   jPOST; D3ZXF9; -.
DR   PaxDb; 10116-ENSRNOP00000051848; -.
DR   PeptideAtlas; D3ZXF9; -.
DR   Ensembl; ENSRNOT00000054965.4; ENSRNOP00000051848.1; ENSRNOG00000036695.4.
DR   GeneID; 303746; -.
DR   KEGG; rno:303746; -.
DR   AGR; RGD:1588559; -.
DR   CTD; 6182; -.
DR   RGD; 1588559; Mrpl12.
DR   eggNOG; KOG1715; Eukaryota.
DR   GeneTree; ENSGT00390000000190; -.
DR   HOGENOM; CLU_086499_0_2_1; -.
DR   InParanoid; D3ZXF9; -.
DR   OMA; TMMMPGM; -.
DR   OrthoDB; 2878856at2759; -.
DR   PhylomeDB; D3ZXF9; -.
DR   TreeFam; TF105997; -.
DR   Reactome; R-RNO-5389840; Mitochondrial translation elongation.
DR   Reactome; R-RNO-5419276; Mitochondrial translation termination.
DR   PRO; PR:D3ZXF9; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000036695; Expressed in heart and 20 other cell types or tissues.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISO:RGD.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   Gene3D; 3.30.1390.10; -; 1.
DR   Gene3D; 1.20.5.710; Single helix bin; 1.
DR   HAMAP; MF_00368; Ribosomal_L7_L12; 1.
DR   InterPro; IPR000206; Ribosomal_bL12.
DR   InterPro; IPR013823; Ribosomal_bL12_C.
DR   InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR   InterPro; IPR008932; Ribosomal_bL12_oligo.
DR   InterPro; IPR036235; Ribosomal_bL12_oligo_N_sf.
DR   PANTHER; PTHR45987; 39S RIBOSOMAL PROTEIN L12; 1.
DR   PANTHER; PTHR45987:SF4; 39S RIBOSOMAL PROTEIN L12, MITOCHONDRIAL; 1.
DR   Pfam; PF00542; Ribosomal_L12; 1.
DR   Pfam; PF16320; Ribosomal_L12_N; 1.
DR   SUPFAM; SSF54736; ClpS-like; 1.
DR   SUPFAM; SSF48300; Ribosomal protein L7/12, oligomerisation (N-terminal) domain; 1.
PE   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|PeptideAtlas:D3ZXF9};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
FT   DOMAIN          139..190
FT                   /note="Large ribosomal subunit protein bL12
FT                   oligomerization"
FT                   /evidence="ECO:0000259|Pfam:PF16320"
FT   DOMAIN          208..275
FT                   /note="Large ribosomal subunit protein bL12 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00542"
FT   REGION          185..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   276 AA;  29441 MW;  739EE5653C677EDF CRC64;
     MPRRAAGESS DPVLFPGPDC VCASRRLVRN IRSQPSRPGR QGLVARAARP ARLLPDRASL
     PLRAACDLPA CGAMLPAAAA AASRLWGPRL GLGGSALRLV RQQMPGVCVA RQLRSSSHRR
     SEALAGAPLD NAPKEYPPKI QQLVQDIASL TLLEISDLNE LLKKTLKIQD VGLMPMGGMV
     PGAVPAAAPA PEAAEEEDLP KQKEQTHFTV RLTEAKPVDK VKLIKEIKNY VQGINLVQAK
     KLVESLPQEI KANVAKAEAE KIKAALEAVG GTVVLE
//
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