PNPT1_MOUSE
ID PNPT1_MOUSE Reviewed; 783 AA.
AC Q8K1R3; Q3UEP9; Q810U7; Q812B3; Q8R2U3; Q9DC52;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Polyribonucleotide nucleotidyltransferase 1, mitochondrial;
DE EC=2.7.7.8;
DE AltName: Full=3'-5' RNA exonuclease OLD35;
DE AltName: Full=PNPase old-35;
DE AltName: Full=Polynucleotide phosphorylase 1;
DE Short=PNPase 1;
DE AltName: Full=Polynucleotide phosphorylase-like protein;
DE Flags: Precursor;
GN Name=Pnpt1; Synonyms=Pnpase;
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).
RX PubMed=12419256; DOI=10.1016/s0022-2836(02)00947-6;
RA Raijmakers R., Vree Egberts W., van Venrooij W.J., Pruijn G.J.M.;
RT "Protein-protein interactions between human exosome components support the
RT assembly of RNase PH-type subunits into a six-membered PNPase-like ring.";
RL J. Mol. Biol. 323:653-663(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Leszczyniecka M., Fisher P.B.;
RT "Cloning of mouse homolog of old-35.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Liver, and Lung;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland, and Mammary tumor;
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16966381; DOI=10.1128/mcb.01002-06;
RA Chen H.W., Rainey R.N., Balatoni C.E., Dawson D.W., Troke J.J., Wasiak S.,
RA Hong J.S., McBride H.M., Koehler C.M., Teitell M.A., French S.W.;
RT "Mammalian polynucleotide phosphorylase is an intermembrane space RNase
RT that maintains mitochondrial homeostasis.";
RL Mol. Cell. Biol. 26:8475-8487(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20691904; DOI=10.1016/j.cell.2010.06.035;
RA Wang G., Chen H.W., Oktay Y., Zhang J., Allen E.L., Smith G.M., Fan K.C.,
RA Hong J.S., French S.W., McCaffery J.M., Lightowlers R.N., Morse H.C. III,
RA Koehler C.M., Teitell M.A.;
RT "PNPASE regulates RNA import into mitochondria.";
RL Cell 142:456-467(2010).
RN [8]
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).
RN [9]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-552, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-250, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [11]
RP STRUCTURE BY NMR OF 273-363.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the alpha-helical domain from mouse hypothetical
RT PNPase.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: RNA-binding protein implicated in numerous RNA metabolic
CC processes. Catalyzes the phosphorolysis of single-stranded
CC polyribonucleotides processively in the 3'-to-5' direction.
CC Mitochondrial intermembrane factor with RNA-processing exoribonulease
CC activity. Component of the mitochondrial degradosome (mtEXO) complex,
CC that degrades 3' overhang double-stranded RNA with a 3'-to-5'
CC directionality in an ATP-dependent manner. Involved in the degradation
CC of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like
CC molecules (By similarity). Required for correct processing and
CC polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic
CC RNA import factor that mediates the translocation of small RNA
CC components, like the 5S RNA, the RNA subunit of ribonuclease P and the
CC mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix.
CC Plays a role in mitochondrial morphogenesis and respiration; regulates
CC the expression of the electron transport chain (ETC) components at the
CC mRNA and protein levels. In the cytoplasm, shows a 3'-to-5'
CC exoribonuclease mediating mRNA degradation activity; degrades c-myc
CC mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest
CC in melanoma cells. Regulates the stability of specific mature miRNAs in
CC melanoma cells; specifically and selectively degrades miR-221,
CC preferentially. Also plays a role in RNA cell surveillance by cleaning
CC up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA
CC and miR-221 microRNA. {ECO:0000250|UniProtKB:Q8TCS8,
CC ECO:0000269|PubMed:20691904}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate +
CC RNA(n); Xref=Rhea:RHEA:22096, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:140395;
CC EC=2.7.7.8;
CC -!- SUBUNIT: Homotrimer; in free form. Homooligomer. Component of the
CC mitochondrial degradosome (mtEXO) complex which is a heteropentamer
CC containing 2 copies of SUPV3L1 and 3 copies of PNPT1. As part of the
CC mitochondrial degradosome complex, interacts with GRSF1 in an RNA-
CC dependent manner; the interaction enhances the activity of the complex.
CC Interacts with TCL1A; the interaction has no effect on PNPT1
CC exonuclease activity. {ECO:0000250|UniProtKB:Q8TCS8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TCS8}.
CC Mitochondrion matrix {ECO:0000250|UniProtKB:Q8TCS8}. Mitochondrion
CC intermembrane space {ECO:0000269|PubMed:16966381}; Peripheral membrane
CC protein {ECO:0000269|PubMed:16966381}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K1R3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K1R3-2; Sequence=VSP_013639, VSP_013640;
CC -!- DISRUPTION PHENOTYPE: Mice show alteration in the mechanisms of
CC polycistronic mtRNAs processing in mitochondria, resulting in fewer
CC mature mtRNAs and a reduction in electron transport chain (ETC)
CC components formation. {ECO:0000269|PubMed:20691904}.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO33354.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ507387; CAD45436.1; -; mRNA.
DR EMBL; AF465249; AAO33354.1; ALT_FRAME; mRNA.
DR EMBL; AK004563; BAB23374.1; -; mRNA.
DR EMBL; AK149419; BAE28862.1; -; mRNA.
DR EMBL; BX000351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027228; AAH27228.2; -; mRNA.
DR EMBL; BC049283; AAH49283.1; -; mRNA.
DR EMBL; BC055826; AAH55826.1; -; mRNA.
DR CCDS; CCDS24490.1; -. [Q8K1R3-1]
DR RefSeq; NP_082145.1; NM_027869.1. [Q8K1R3-1]
DR RefSeq; XP_011242053.1; XM_011243751.2. [Q8K1R3-1]
DR PDB; 1WHU; NMR; -; A=273-363.
DR PDBsum; 1WHU; -.
DR AlphaFoldDB; Q8K1R3; -.
DR BMRB; Q8K1R3; -.
DR SMR; Q8K1R3; -.
DR BioGRID; 214865; 5.
DR IntAct; Q8K1R3; 1.
DR STRING; 10090.ENSMUSP00000020756; -.
DR iPTMnet; Q8K1R3; -.
DR PhosphoSitePlus; Q8K1R3; -.
DR SwissPalm; Q8K1R3; -.
DR EPD; Q8K1R3; -.
DR MaxQB; Q8K1R3; -.
DR PaxDb; Q8K1R3; -.
DR PeptideAtlas; Q8K1R3; -.
DR PRIDE; Q8K1R3; -.
DR ProteomicsDB; 289640; -. [Q8K1R3-1]
DR ProteomicsDB; 289641; -. [Q8K1R3-2]
DR Antibodypedia; 30432; 345 antibodies from 31 providers.
DR DNASU; 71701; -.
DR Ensembl; ENSMUST00000020756; ENSMUSP00000020756; ENSMUSG00000020464. [Q8K1R3-1]
DR GeneID; 71701; -.
DR KEGG; mmu:71701; -.
DR UCSC; uc007igp.1; mouse. [Q8K1R3-1]
DR CTD; 87178; -.
DR MGI; MGI:1918951; Pnpt1.
DR VEuPathDB; HostDB:ENSMUSG00000020464; -.
DR eggNOG; KOG1067; Eukaryota.
DR GeneTree; ENSGT00390000014001; -.
DR HOGENOM; CLU_004217_2_2_1; -.
DR InParanoid; Q8K1R3; -.
DR OMA; LHILDVM; -.
DR OrthoDB; 236073at2759; -.
DR PhylomeDB; Q8K1R3; -.
DR TreeFam; TF315264; -.
DR BRENDA; 2.7.7.8; 3474.
DR BioGRID-ORCS; 71701; 27 hits in 76 CRISPR screens.
DR ChiTaRS; Pnpt1; mouse.
DR EvolutionaryTrace; Q8K1R3; -.
DR PRO; PR:Q8K1R3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K1R3; protein.
DR Bgee; ENSMUSG00000020464; Expressed in spermatocyte and 259 other tissues.
DR Genevisible; Q8K1R3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0045025; C:mitochondrial degradosome; ISS:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0042788; C:polysomal ribosome; ISO:MGI.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0034046; F:poly(G) binding; ISS:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; ISS:UniProtKB.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035458; P:cellular response to interferon-beta; ISO:MGI.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0097222; P:mitochondrial mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0000964; P:mitochondrial RNA 5'-end processing; ISS:UniProtKB.
DR GO; GO:0000957; P:mitochondrial RNA catabolic process; ISS:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0045926; P:negative regulation of growth; ISS:UniProtKB.
DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:2000627; P:positive regulation of miRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0000962; P:positive regulation of mitochondrial RNA catabolic process; ISS:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0043457; P:regulation of cellular respiration; IMP:UniProtKB.
DR GO; GO:2000772; P:regulation of cellular senescence; ISS:UniProtKB.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
DR GO; GO:0006401; P:RNA catabolic process; ISS:UniProtKB.
DR GO; GO:0035927; P:RNA import into mitochondrion; ISS:UniProtKB.
DR GO; GO:0043631; P:RNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0035928; P:rRNA import into mitochondrion; ISS:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1370.10; -; 1.
DR Gene3D; 3.30.230.70; -; 2.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR015847; ExoRNase_PH_dom2.
DR InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012162; PNPase.
DR InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR InterPro; IPR036456; PNPase_PH_RNA-bd_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR11252; PTHR11252; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF03726; PNPase; 1.
DR Pfam; PF01138; RNase_PH; 2.
DR Pfam; PF03725; RNase_PH_C; 1.
DR Pfam; PF00575; S1; 1.
DR PIRSF; PIRSF005499; PNPase; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF46915; SSF46915; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54211; SSF54211; 2.
DR SUPFAM; SSF54791; SSF54791; 1.
DR SUPFAM; SSF55666; SSF55666; 2.
DR TIGRFAMs; TIGR03591; polynuc_phos; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Exonuclease;
KW Hydrolase; Membrane; Mitochondrion; mRNA processing; Nuclease;
KW Nucleotidyltransferase; Phosphoprotein; Reference proteome; RNA-binding;
KW Transferase; Transit peptide; Transport.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 46..783
FT /note="Polyribonucleotide nucleotidyltransferase 1,
FT mitochondrial"
FT /id="PRO_0000024752"
FT DOMAIN 605..664
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 679..750
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT MOD_RES 250
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 264
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCS8"
FT MOD_RES 285
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCS8"
FT MOD_RES 552
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCS8"
FT VAR_SEQ 535..540
FT /note="GIEDYN -> ASIFPV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013639"
FT VAR_SEQ 541..783
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013640"
FT CONFLICT 90
FT /note="A -> P (in Ref. 2; AAO33354)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="V -> G (in Ref. 2; AAO33354)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="K -> Q (in Ref. 2; AAO33354)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="I -> V (in Ref. 2; AAO33354)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="P -> L (in Ref. 3; BAB23374)"
FT /evidence="ECO:0000305"
FT HELIX 281..299
FT /evidence="ECO:0007829|PDB:1WHU"
FT HELIX 307..324
FT /evidence="ECO:0007829|PDB:1WHU"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:1WHU"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:1WHU"
FT HELIX 333..352
FT /evidence="ECO:0007829|PDB:1WHU"
SQ SEQUENCE 783 AA; 85683 MW; F35F6BE91AAB5626 CRC64;
MAACRLCCLC PCLRPLGCGP LGRPGRNRAL SYLQMRALWS STGSRAVTVD LGHRKLEISS
GKLARFADGC AVIQSGDTAV MVTAVSKTKA SPSQFMPLVV DYRQKAAAAG RIPTNYLRRE
IGSSDREVLT SRVIDRSIRP LFPAGYFYDT QVLCNLLAVD GINEPDILAV NGASVALSLS
DIPWNGPVGA VRIGMIDGEC VVNPTRREMS SSTLNLVVAG APKSQIVMLE ASAENILQQD
FCHAIKVGVK YTQQIIQGIQ QLVKEIGVAK RTPQKIFTPS AEIVKYTKII AMEKLYAVFT
DYEHDKVSRD EAVNKIRLDT EEHLKEKFPE VDQFEIIESF NIVAKEVFRS IILNEYKRCD
GRDLTSLRNI SCEVDMFKTL HGSALFQRGQ TQVLCTVTFD SLESSIKSDQ IITAINGVKD
KNFMLHYEFP PYATNETGKV TGVNRRELGH GALAEKALCP VIPKDFPFTI RVTSEVLESN
GSSSMASACG GSLALMDAGV PISSAVAGVA VGLVTKTNPE KGEIEDYRLL TDILGIEDYN
GDMDFKIAGT NKGITALQAD IKLPGVPIKI IMEAIQQASV AKKEILQIMN KTISKPRASR
KENGPVVETV KVPLSKRAKF VGPGGYHLKK LQAETGVTIS QVDEETFSIF APTPTAMHEA
RDFITEICRD DQEQQLEFGA VYTATITEIR DTGVMVKLYP NMTAVLLHNS QLDQRKIKHP
TALGLEVGQE IQVKYFGRDP ADGRMRLSRK VLQSPATTAL KTLNDRSSIV MGEPVSQSSN
SNP
