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RM38_MOUSE
ID   RM38_MOUSE              Reviewed;         380 AA.
AC   Q8K2M0; A2A869; Q3TXY6; Q8BTZ1; Q99LM1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=39S ribosomal protein L38, mitochondrial;
DE            Short=L38mt;
DE            Short=MRP-L38;
DE   Flags: Precursor;
GN   Name=Mrpl38;
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 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Thymus, and Visual cortex;
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].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=Czech II, and FVB/N; 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, Spleen, and
RC   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   -!- SUBUNIT: Component of the mitochondrial ribosome large subunit (39S)
CC       which comprises a 16S rRNA and about 50 distinct proteins.
CC       {ECO:0000250|UniProtKB:Q96DV4}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96DV4}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K2M0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K2M0-2; Sequence=VSP_021748;
CC   -!- SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein
CC       family. Mitochondrion-specific ribosomal protein mL38 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH30739.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE30538.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE34778.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK088343; BAC40295.1; ALT_SEQ; mRNA.
DR   EMBL; AK159033; BAE34778.1; ALT_INIT; mRNA.
DR   EMBL; AK151598; BAE30538.1; ALT_INIT; mRNA.
DR   EMBL; AL607108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002319; AAH02319.1; -; mRNA.
DR   EMBL; BC030739; AAH30739.1; ALT_INIT; mRNA.
DR   CCDS; CCDS25658.2; -. [Q8K2M0-1]
DR   RefSeq; NP_077139.2; NM_024177.3. [Q8K2M0-1]
DR   AlphaFoldDB; Q8K2M0; -.
DR   SMR; Q8K2M0; -.
DR   BioGRID; 208564; 15.
DR   ComplexPortal; CPX-5302; 39S mitochondrial large ribosomal subunit.
DR   STRING; 10090.ENSMUSP00000102047; -.
DR   iPTMnet; Q8K2M0; -.
DR   PhosphoSitePlus; Q8K2M0; -.
DR   SwissPalm; Q8K2M0; -.
DR   EPD; Q8K2M0; -.
DR   jPOST; Q8K2M0; -.
DR   MaxQB; Q8K2M0; -.
DR   PaxDb; Q8K2M0; -.
DR   PeptideAtlas; Q8K2M0; -.
DR   PRIDE; Q8K2M0; -.
DR   ProteomicsDB; 300402; -. [Q8K2M0-1]
DR   ProteomicsDB; 300403; -. [Q8K2M0-2]
DR   Antibodypedia; 19644; 110 antibodies from 24 providers.
DR   DNASU; 60441; -.
DR   Ensembl; ENSMUST00000106439; ENSMUSP00000102047; ENSMUSG00000020775. [Q8K2M0-1]
DR   GeneID; 60441; -.
DR   KEGG; mmu:60441; -.
DR   UCSC; uc007mkc.1; mouse. [Q8K2M0-1]
DR   CTD; 64978; -.
DR   MGI; MGI:1926269; Mrpl38.
DR   VEuPathDB; HostDB:ENSMUSG00000020775; -.
DR   eggNOG; KOG3346; Eukaryota.
DR   GeneTree; ENSGT00900000141125; -.
DR   HOGENOM; CLU_043994_0_0_1; -.
DR   InParanoid; Q8K2M0; -.
DR   OMA; EMCHYLP; -.
DR   OrthoDB; 1557122at2759; -.
DR   PhylomeDB; Q8K2M0; -.
DR   TreeFam; TF315074; -.
DR   Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR   Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR   BioGRID-ORCS; 60441; 23 hits in 110 CRISPR screens.
DR   ChiTaRS; Mrpl38; mouse.
DR   PRO; PR:Q8K2M0; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q8K2M0; protein.
DR   Bgee; ENSMUSG00000020775; Expressed in right kidney and 257 other tissues.
DR   Genevisible; Q8K2M0; MM.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISO:MGI.
DR   GO; GO:0005761; C:mitochondrial ribosome; ISS:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR   CDD; cd00866; PEBP_euk; 1.
DR   Gene3D; 3.90.280.10; -; 1.
DR   InterPro; IPR008914; PEBP.
DR   InterPro; IPR036610; PEBP-like_sf.
DR   InterPro; IPR035810; PEBP_euk.
DR   PANTHER; PTHR11362; PTHR11362; 1.
DR   Pfam; PF01161; PBP; 1.
DR   SUPFAM; SSF49777; SSF49777; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Mitochondrion; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT         1..26
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..380
FT                   /note="39S ribosomal protein L38, mitochondrial"
FT                   /id="PRO_0000261653"
FT   COILED          100..123
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         2..35
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021748"
FT   CONFLICT        16
FT                   /note="C -> S (in Ref. 1; BAE30538)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54
FT                   /note="F -> Y (in Ref. 1; BAE34778)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86
FT                   /note="D -> N (in Ref. 1; BAE34778)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="H -> N (in Ref. 3; AAH30739)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   380 AA;  45030 MW;  7CA22E40672E9BF3 CRC64;
     MAAPWWRAAF FGIGRCRGFS TSAFLSRRTP PLGPMPNEDI DVSNLERLEK YRSFERYRRR
     AEQEARAPHW WRTYREHFVK ETDPKDKIDI GLPPPRVSRT QKLLERKHFL RELRANVEEE
     RAARLRTASI PLEAVRAEWE RTCGPYHKQR LAEYYGLYRD LFHGATFVPW VPLHVAYAVG
     EEDLIPVYHG NEVTPTEASR APEVTYEADK DSLWTLLFIN LDGHLLEPDA EYVHWLLTNI
     PSNRVAEGQE TCPYLPPFPA RGSGFHRFAF LLFKQDKPIN FSEDTRPSPC YQLAQRTFRT
     FDFYKRHQEA MTPAGLAFFQ CRWDDSVTHT FHQLLDMREP VFEFVRPPPY HPKQKRFPHE
     QPLRYLDRYR DSHEPTYGIY
 
 
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