RT29_MOUSE
ID RT29_MOUSE Reviewed; 391 AA.
AC Q9ER88; Q8C2B2; Q8CCQ8; Q8VCK8; Q9CRT4; Q9CS11; Q9D5V9;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=28S ribosomal protein S29, mitochondrial;
DE Short=MRP-S29;
DE Short=S29mt;
DE AltName: Full=Death-associated protein 3;
DE Short=DAP-3;
DE Flags: Precursor;
GN Name=Dap3; Synonyms=Mrps29;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Embryonic kidney;
RX PubMed=11017876; DOI=10.1242/jcs.113.20.3603;
RA Berger T., Brigl M., Herrmann J.M., Vielhauer V., Luckow B.,
RA Schloendorff D., Kretzler M.;
RT "The apoptosis mediator mDAP-3 is a novel member of a conserved family of
RT mitochondrial proteins.";
RL J. Cell Sci. 113:3603-3612(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, FVB/N, and NOD;
RC TISSUE=Embryo, Embryonic head, Olfactory bulb, Testis, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
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, Lung, 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 -!- FUNCTION: Involved in mediating interferon-gamma-induced cell death.
CC {ECO:0000250|UniProtKB:P51398}.
CC -!- SUBUNIT: Component of the mitochondrial ribosome small subunit (28S)
CC which comprises a 12S rRNA and about 30 distinct proteins. Interacts
CC with DELE1. Interacts with NOA1. {ECO:0000250|UniProtKB:P51398}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P51398}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ER88-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ER88-2; Sequence=VSP_008916;
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mS29 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB29240.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB29605.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC27790.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC40673.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ250375; CAC05583.1; -; mRNA.
DR EMBL; AK014889; BAB29605.1; ALT_INIT; mRNA.
DR EMBL; AK014280; BAB29240.3; ALT_INIT; mRNA.
DR EMBL; AK021250; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK032275; BAC27790.1; ALT_INIT; mRNA.
DR EMBL; AK088960; BAC40673.1; ALT_INIT; mRNA.
DR EMBL; BC019566; AAH19566.2; -; mRNA.
DR CCDS; CCDS89651.1; -. [Q9ER88-1]
DR RefSeq; NP_001158005.1; NM_001164533.1.
DR RefSeq; NP_075370.2; NM_022994.3.
DR RefSeq; XP_006501925.1; XM_006501862.3.
DR RefSeq; XP_006501926.1; XM_006501863.3. [Q9ER88-1]
DR RefSeq; XP_006501927.1; XM_006501864.3. [Q9ER88-1]
DR RefSeq; XP_006501932.1; XM_006501869.3. [Q9ER88-1]
DR AlphaFoldDB; Q9ER88; -.
DR SMR; Q9ER88; -.
DR BioGRID; 211134; 6.
DR ComplexPortal; CPX-5301; 28S mitochondrial small ribosomal subunit.
DR IntAct; Q9ER88; 1.
DR STRING; 10090.ENSMUSP00000088456; -.
DR iPTMnet; Q9ER88; -.
DR PhosphoSitePlus; Q9ER88; -.
DR SwissPalm; Q9ER88; -.
DR EPD; Q9ER88; -.
DR jPOST; Q9ER88; -.
DR MaxQB; Q9ER88; -.
DR PaxDb; Q9ER88; -.
DR PeptideAtlas; Q9ER88; -.
DR PRIDE; Q9ER88; -.
DR ProteomicsDB; 262721; -. [Q9ER88-1]
DR ProteomicsDB; 262722; -. [Q9ER88-2]
DR Antibodypedia; 1656; 488 antibodies from 38 providers.
DR DNASU; 65111; -.
DR Ensembl; ENSMUST00000173135; ENSMUSP00000134422; ENSMUSG00000068921. [Q9ER88-1]
DR GeneID; 65111; -.
DR KEGG; mmu:65111; -.
DR UCSC; uc008pxh.2; mouse. [Q9ER88-2]
DR CTD; 7818; -.
DR MGI; MGI:1929538; Dap3.
DR VEuPathDB; HostDB:ENSMUSG00000068921; -.
DR eggNOG; KOG3928; Eukaryota.
DR GeneTree; ENSGT00390000015248; -.
DR InParanoid; Q9ER88; -.
DR OMA; DITNYDW; -.
DR OrthoDB; 1593937at2759; -.
DR PhylomeDB; Q9ER88; -.
DR Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR BioGRID-ORCS; 65111; 20 hits in 74 CRISPR screens.
DR ChiTaRS; Dap3; mouse.
DR PRO; PR:Q9ER88; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9ER88; protein.
DR Bgee; ENSMUSG00000068921; Expressed in spermatocyte and 270 other tissues.
DR ExpressionAtlas; Q9ER88; baseline and differential.
DR Genevisible; Q9ER88; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:MGI.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:MGI.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR InterPro; IPR019368; Ribosomal_S23/S29_mit.
DR InterPro; IPR008092; Ribosomal_S29_mit.
DR PANTHER; PTHR12810; PTHR12810; 1.
DR Pfam; PF10236; DAP3; 1.
DR PRINTS; PR01716; DEATHASSOCP3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Mitochondrion;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 18..391
FT /note="28S ribosomal protein S29, mitochondrial"
FT /id="PRO_0000087718"
FT REGION 30..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 168
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51398"
FT MOD_RES 200
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51398"
FT VAR_SEQ 295..324
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008916"
FT CONFLICT 90
FT /note="A -> R (in Ref. 2; BAB29605)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="H -> N (in Ref. 2; BAC27790)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="A -> G (in Ref. 2; BAB29605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 44699 MW; 038AC9DA7A61FFF4 CRC64;
MLTGITRLFS RVQKLDPRCF LHMSVQATQN SQVPAERPRT VSRTSDSDPA KHGEQHEGQH
YSIPLQDLKT VFPHGLPPRY MMQVKTFGEA CLMVRKPALE LLGYLKNTNF AHPAVRYLLY
GEKGTGKTLS LCHAVHFCAR HDWLILHIPD AHLWVKNCRE LLQSTHNKQR FDQPLEASTW
LKNFKTTNER FLSQIKVQEK YVWNKRESTE KGSPLGEVVE QGLTRVRNAT DAVGVVLKEL
KAQSALGLFH LLVAVDGVNA LWGRTTLKKE DRTLIAPEEL SLVHNLRKMV KNDWHGGAIV
LSLSQTGSLF KSRTAYLPHE LLGKEGFNAL EPFLPILIPN YNPKEFESSF QYYLENNWLQ
HEKASTEEGR KELRFLSNCN PEQLERLCAS L
