PTCD3_HUMAN
ID PTCD3_HUMAN Reviewed; 689 AA.
AC Q96EY7; A6NHD2; D6W5M1; Q597H0; Q658Y9; Q9BUZ8; Q9NWL0;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Pentatricopeptide repeat domain-containing protein 3, mitochondrial;
DE AltName: Full=28S ribosomal protein S39, mitochondrial;
DE Short=MRP-S39;
DE AltName: Full=Mitochondrial small ribosomal subunit protein mS39 {ECO:0000303|PubMed:25838379};
DE AltName: Full=Transformation-related gene 15 protein;
DE Short=TRG-15;
DE Flags: Precursor;
GN Name=PTCD3; Synonyms=MRPS39; ORFNames=TRG15;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Lung;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-689.
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 323-689.
RA Kim J.W.;
RT "Identification of a human transforming gene.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY, SUBUNIT, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19427859; DOI=10.1016/j.febslet.2009.04.048;
RA Davies S.M., Rackham O., Shearwood A.M., Hamilton K.L., Narsai R.,
RA Whelan J., Filipovska A.;
RT "Pentatricopeptide repeat domain protein 3 associates with the
RT mitochondrial small ribosomal subunit and regulates translation.";
RL FEBS Lett. 583:1853-1858(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-126, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23908630; DOI=10.3389/fphys.2013.00183;
RA Koc E.C., Cimen H., Kumcuoglu B., Abu N., Akpinar G., Haque M.E.,
RA Spremulli L.L., Koc H.;
RT "Identification and characterization of CHCHD1, AURKAIP1, and CRIF1 as new
RT members of the mammalian mitochondrial ribosome.";
RL Front. Physiol. 4:183-183(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP INVOLVEMENT IN COXPD51.
RX PubMed=30607703; DOI=10.1007/s10048-018-0561-9;
RA Borna N.N., Kishita Y., Kohda M., Lim S.C., Shimura M., Wu Y., Mogushi K.,
RA Yatsuka Y., Harashima H., Hisatomi Y., Fushimi T., Ichimoto K.,
RA Murayama K., Ohtake A., Okazaki Y.;
RT "Mitochondrial ribosomal protein PTCD3 mutations cause oxidative
RT phosphorylation defects with Leigh syndrome.";
RL Neurogenetics 20:9-25(2019).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
RX PubMed=25838379; DOI=10.1126/science.aaa1193;
RA Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.;
RT "Ribosome. The structure of the human mitochondrial ribosome.";
RL Science 348:95-98(2015).
CC -!- FUNCTION: Mitochondrial RNA-binding protein that has a role in
CC mitochondrial translation. {ECO:0000269|PubMed:19427859}.
CC -!- SUBUNIT: Component of the mitochondrial small ribosomal subunit (mt-
CC SSU). Mature mammalian 55S mitochondrial ribosomes consist of a small
CC (28S) and a large (39S) subunit. The 28S small subunit contains a 12S
CC ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large
CC subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial
CC valine transfer RNA (mt-tRNA(Val)), which plays an integral structural
CC role, and 52 different proteins. Associated with the 12S mitochondrial
CC rRNA (12S mt-rRNA). {ECO:0000269|PubMed:19427859,
CC ECO:0000269|PubMed:23908630, ECO:0000269|PubMed:25838379}.
CC -!- INTERACTION:
CC Q96EY7; Q8N448: LNX2; NbExp=3; IntAct=EBI-721110, EBI-2340947;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19427859,
CC ECO:0000269|PubMed:23908630}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96EY7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96EY7-2; Sequence=VSP_028191, VSP_028192;
CC -!- TISSUE SPECIFICITY: Abundant in testes, skeletal muscle and heart
CC tissue. {ECO:0000269|PubMed:19427859}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 51 (COXPD51)
CC [MIM:619057]: An autosomal recessive, mitochondrial disorder
CC characterized by intrauterine growth retardation, low birth weight,
CC poor overall growth, progressive limb rigidity, delayed psychomotor
CC development, hearing loss, and optic atrophy. Brain imaging shows
CC abnormal bilateral signs at the basal ganglia and brainstem. Patient
CC cells show decreased mitochondrial complex I and IV levels and
CC activities, and generalized mitochondrial translation defects.
CC {ECO:0000269|PubMed:30607703}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mS39 family. {ECO:0000305}.
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DR EMBL; AK000765; BAA91370.1; -; mRNA.
DR EMBL; AC009309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAW99464.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99465.1; -; Genomic_DNA.
DR EMBL; BC001758; AAH01758.3; -; mRNA.
DR EMBL; BC011832; AAH11832.3; -; mRNA.
DR EMBL; AL832520; CAH56345.1; -; mRNA.
DR EMBL; AY277598; AAQ18037.1; -; mRNA.
DR CCDS; CCDS33235.1; -. [Q96EY7-1]
DR RefSeq; NP_060422.4; NM_017952.5. [Q96EY7-1]
DR PDB; 3J9M; EM; 3.50 A; A4=1-689.
DR PDB; 6NU2; EM; 3.90 A; A4=56-639.
DR PDB; 6NU3; EM; 4.40 A; A4=56-639.
DR PDB; 6RW4; EM; 2.97 A; 4=1-689.
DR PDB; 6RW5; EM; 3.14 A; 4=1-689.
DR PDB; 6VLZ; EM; 2.97 A; A4=1-689.
DR PDB; 6VMI; EM; 2.96 A; A4=1-689.
DR PDB; 6ZM5; EM; 2.89 A; A4=1-689.
DR PDB; 6ZM6; EM; 2.59 A; A4=1-689.
DR PDB; 6ZS9; EM; 4.00 A; A4=56-689.
DR PDB; 6ZSA; EM; 4.00 A; A4=56-689.
DR PDB; 6ZSB; EM; 4.50 A; A4=56-689.
DR PDB; 6ZSC; EM; 3.50 A; A4=56-689.
DR PDB; 6ZSD; EM; 3.70 A; A4=56-689.
DR PDB; 6ZSE; EM; 5.00 A; A4=56-689.
DR PDB; 6ZSG; EM; 4.00 A; A4=56-689.
DR PDB; 7A5F; EM; 4.40 A; e6=1-689.
DR PDB; 7A5G; EM; 4.33 A; e6=1-689.
DR PDB; 7A5I; EM; 3.70 A; e6=1-689.
DR PDB; 7A5K; EM; 3.70 A; e6=1-689.
DR PDB; 7L08; EM; 3.49 A; A4=1-689.
DR PDB; 7OG4; EM; 3.80 A; A4=1-689.
DR PDBsum; 3J9M; -.
DR PDBsum; 6NU2; -.
DR PDBsum; 6NU3; -.
DR PDBsum; 6RW4; -.
DR PDBsum; 6RW5; -.
DR PDBsum; 6VLZ; -.
DR PDBsum; 6VMI; -.
DR PDBsum; 6ZM5; -.
DR PDBsum; 6ZM6; -.
DR PDBsum; 6ZS9; -.
DR PDBsum; 6ZSA; -.
DR PDBsum; 6ZSB; -.
DR PDBsum; 6ZSC; -.
DR PDBsum; 6ZSD; -.
DR PDBsum; 6ZSE; -.
DR PDBsum; 6ZSG; -.
DR PDBsum; 7A5F; -.
DR PDBsum; 7A5G; -.
DR PDBsum; 7A5I; -.
DR PDBsum; 7A5K; -.
DR PDBsum; 7L08; -.
DR PDBsum; 7OG4; -.
DR AlphaFoldDB; Q96EY7; -.
DR SMR; Q96EY7; -.
DR BioGRID; 120366; 315.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; Q96EY7; -.
DR IntAct; Q96EY7; 111.
DR MINT; Q96EY7; -.
DR STRING; 9606.ENSP00000254630; -.
DR GlyGen; Q96EY7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96EY7; -.
DR MetOSite; Q96EY7; -.
DR PhosphoSitePlus; Q96EY7; -.
DR SwissPalm; Q96EY7; -.
DR BioMuta; PTCD3; -.
DR DMDM; 74731633; -.
DR EPD; Q96EY7; -.
DR jPOST; Q96EY7; -.
DR MassIVE; Q96EY7; -.
DR MaxQB; Q96EY7; -.
DR PaxDb; Q96EY7; -.
DR PeptideAtlas; Q96EY7; -.
DR PRIDE; Q96EY7; -.
DR ProteomicsDB; 76472; -. [Q96EY7-1]
DR ProteomicsDB; 76473; -. [Q96EY7-2]
DR Antibodypedia; 32009; 69 antibodies from 21 providers.
DR DNASU; 55037; -.
DR Ensembl; ENST00000254630.12; ENSP00000254630.7; ENSG00000132300.19. [Q96EY7-1]
DR GeneID; 55037; -.
DR KEGG; hsa:55037; -.
DR MANE-Select; ENST00000254630.12; ENSP00000254630.7; NM_017952.6; NP_060422.4.
DR UCSC; uc002sqw.2; human. [Q96EY7-1]
DR CTD; 55037; -.
DR DisGeNET; 55037; -.
DR GeneCards; PTCD3; -.
DR HGNC; HGNC:24717; PTCD3.
DR HPA; ENSG00000132300; Low tissue specificity.
DR MalaCards; PTCD3; -.
DR MIM; 614918; gene.
DR MIM; 619057; phenotype.
DR neXtProt; NX_Q96EY7; -.
DR OpenTargets; ENSG00000132300; -.
DR PharmGKB; PA147357465; -.
DR VEuPathDB; HostDB:ENSG00000132300; -.
DR eggNOG; KOG4422; Eukaryota.
DR GeneTree; ENSGT00390000016876; -.
DR HOGENOM; CLU_026264_0_1_1; -.
DR InParanoid; Q96EY7; -.
DR OMA; FMHQEAQ; -.
DR OrthoDB; 405419at2759; -.
DR PhylomeDB; Q96EY7; -.
DR TreeFam; TF320158; -.
DR PathwayCommons; Q96EY7; -.
DR Reactome; R-HSA-5368286; Mitochondrial translation initiation.
DR Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR Reactome; R-HSA-5419276; Mitochondrial translation termination.
DR SignaLink; Q96EY7; -.
DR SIGNOR; Q96EY7; -.
DR BioGRID-ORCS; 55037; 421 hits in 1085 CRISPR screens.
DR ChiTaRS; PTCD3; human.
DR GenomeRNAi; 55037; -.
DR Pharos; Q96EY7; Tbio.
DR PRO; PR:Q96EY7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96EY7; protein.
DR Bgee; ENSG00000132300; Expressed in adrenal tissue and 201 other tissues.
DR ExpressionAtlas; Q96EY7; baseline and differential.
DR Genevisible; Q96EY7; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IDA:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IMP:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR037387; PTCD3.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR16276; PTHR16276; 1.
DR Pfam; PF13041; PPR_2; 1.
DR Pfam; PF13812; PPR_3; 1.
DR PROSITE; PS51375; PPR; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Mitochondrion;
KW Primary mitochondrial disease; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Transit peptide; Translation regulation.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 38..689
FT /note="Pentatricopeptide repeat domain-containing protein
FT 3, mitochondrial"
FT /id="PRO_0000305028"
FT REPEAT 149..183
FT /note="PPR 1"
FT REPEAT 184..219
FT /note="PPR 2"
FT REPEAT 255..289
FT /note="PPR 3"
FT REPEAT 290..330
FT /note="PPR 4"
FT REPEAT 331..367
FT /note="PPR 5"
FT REPEAT 368..409
FT /note="PPR 6"
FT REPEAT 412..446
FT /note="PPR 7"
FT REPEAT 454..488
FT /note="PPR 8"
FT REPEAT 489..523
FT /note="PPR 9"
FT REPEAT 572..606
FT /note="PPR 10"
FT REGION 665..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 126
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..409
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028191"
FT VAR_SEQ 410..413
FT /note="PDDD -> MMAY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028192"
FT VARIANT 2
FT /note="A -> V (in dbSNP:rs13393659)"
FT /id="VAR_035154"
FT VARIANT 681
FT /note="S -> G (in dbSNP:rs2241433)"
FT /id="VAR_035155"
FT CONFLICT 400
FT /note="L -> S (in Ref. 6; AAQ18037)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="P -> L (in Ref. 4; AAH01758)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 689 AA; 78550 MW; 901DBE1FF3A2E0B9 CRC64;
MAVVSAVRWL GLRSRLGQPL TGRRAGLCEQ ARSCRFYSGS ATLSKVEGTD VTGIEEVVIP
KKKTWDKVAV LQALASTVNR DTTAVPYVFQ DDPYLMPASS LESRSFLLAK KSGENVAKFI
INSYPKYFQK DIAEPHIPCL MPEYFEPQIK DISEAALKER IELRKVKASV DMFDQLLQAG
TTVSLETTNS LLDLLCYYGD QEPSTDYHFQ QTGQSEALEE ENDETSRRKA GHQFGVTWRA
KNNAERIFSL MPEKNEHSYC TMIRGMVKHR AYEQALNLYT ELLNNRLHAD VYTFNALIEA
TVCAINEKFE EKWSKILELL RHMVAQKVKP NLQTFNTILK CLRRFHVFAR SPALQVLREM
KAIGIEPSLA TYHHIIRLFD QPGDPLKRSS FIIYDIMNEL MGKRFSPKDP DDDKFFQSAM
SICSSLRDLE LAYQVHGLLK TGDNWKFIGP DQHRNFYYSK FFDLICLMEQ IDVTLKWYED
LIPSAYFPHS QTMIHLLQAL DVANRLEVIP KIWKDSKEYG HTFRSDLREE ILMLMARDKH
PPELQVAFAD CAADIKSAYE SQPIRQTAQD WPATSLNCIA ILFLRAGRTQ EAWKMLGLFR
KHNKIPRSEL LNELMDSAKV SNSPSQAIEV VELASAFSLP ICEGLTQRVM SDFAINQEQK
EALSNLTALT SDSDTDSSSD SDSDTSEGK
