PGL3_CAEEL
ID PGL3_CAEEL Reviewed; 693 AA.
AC G5EBV6; Q965J2;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Guanyl-specific ribonuclease pgl-3 {ECO:0000305};
DE EC=4.6.1.24 {ECO:0000269|PubMed:26787882};
DE AltName: Full=P granule abnormality protein 3 {ECO:0000312|WormBase:C18G1.4a};
GN Name=pgl-3 {ECO:0000312|WormBase:C18G1.4a};
GN ORFNames=C18G1.4 {ECO:0000312|WormBase:C18G1.4a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PGL-1 AND PGL-2,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DOMAIN, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15238518; DOI=10.1534/genetics.103.023093;
RA Kawasaki I., Amiri A., Fan Y., Meyer N., Dunkelbarger S., Motohashi T.,
RA Karashima T., Bossinger O., Strome S.;
RT "The PGL family proteins associate with germ granules and function
RT redundantly in Caenorhabditis elegans germline development.";
RL Genetics 167:645-661(2004).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19372764; DOI=10.4161/auto.5.5.8552;
RA Zhao Y., Tian E., Zhang H.;
RT "Selective autophagic degradation of maternally-loaded germline P granule
RT components in somatic cells during C. elegans embryogenesis.";
RL Autophagy 5:717-719(2009).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SEPA-1, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=19167332; DOI=10.1016/j.cell.2008.12.022;
RA Zhang Y., Yan L., Zhou Z., Yang P., Tian E., Zhang K., Zhao Y., Li Z.,
RA Song B., Han J., Miao L., Zhang H.;
RT "SEPA-1 mediates the specific recognition and degradation of P granule
RT components by autophagy in C. elegans.";
RL Cell 136:308-321(2009).
RN [5] {ECO:0000305}
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 633-GLY--GLY-692.
RX PubMed=21402787; DOI=10.1083/jcb.201010106;
RA Hanazawa M., Yonetani M., Sugimoto A.;
RT "PGL proteins self associate and bind RNPs to mediate germ granule assembly
RT in C. elegans.";
RL J. Cell Biol. 192:929-937(2011).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PRMT-1 AND SEPA-1, SUBCELLULAR LOCATION,
RP METHYLATION, AND MUTAGENESIS OF ARG-641; ARG-650; ARG-658; ARG-661;
RP ARG-665; ARG-668; ARG-676; ARG-682 AND ARG-690.
RX PubMed=24140420; DOI=10.1016/j.molcel.2013.09.014;
RA Li S., Yang P., Tian E., Zhang H.;
RT "Arginine methylation modulates autophagic degradation of PGL granules in
RT C. elegans.";
RL Mol. Cell 52:421-433(2013).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24746798; DOI=10.1016/j.cub.2014.03.015;
RA Updike D.L., Knutson A.K., Egelhofer T.A., Campbell A.C., Strome S.;
RT "Germ-granule components prevent somatic development in the C. elegans
RT germline.";
RL Curr. Biol. 24:970-975(2014).
RN [8] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
RP DOMAIN, AND MUTAGENESIS OF ARG-634; ARG-638; ARG-650; ARG-661; ARG-665 AND
RP ARG-690.
RX PubMed=27594427; DOI=10.1016/j.cell.2016.08.006;
RA Saha S., Weber C.A., Nousch M., Adame-Arana O., Hoege C., Hein M.Y.,
RA Osborne-Nishimura E., Mahamid J., Jahnel M., Jawerth L., Pozniakovski A.,
RA Eckmann C.R., Juelicher F., Hyman A.A.;
RT "Polar positioning of phase-separated liquid compartments in cells
RT regulated by an mRNA competition mechanism.";
RL Cell 166:1572-1584(2016).
RN [9] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26598553; DOI=10.1242/jcs.174201;
RA Min H., Shim Y.H., Kawasaki I.;
RT "Loss of PGL-1 and PGL-3, members of a family of constitutive germ-granule
RT components, promotes germline apoptosis in C. elegans.";
RL J. Cell Sci. 129:341-353(2016).
RN [10] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND DOMAIN.
RX PubMed=26787882; DOI=10.1073/pnas.1524400113;
RA Aoki S.T., Kershner A.M., Bingman C.A., Wickens M., Kimble J.;
RT "PGL germ granule assembly protein is a base-specific, single-stranded
RT RNase.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:1279-1284(2016).
RN [11] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=27650246; DOI=10.1038/srep33884;
RA Al-Amin M., Min H., Shim Y.H., Kawasaki I.;
RT "Somatically expressed germ-granule components, PGL-1 and PGL-3, repress
RT programmed cell death in C. elegans.";
RL Sci. Rep. 6:33884-33884(2016).
RN [12] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=28806108; DOI=10.1080/15548627.2017.1339843;
RA Zhang G., Lin L., Qi D., Zhang H.;
RT "The composition of a protein aggregate modulates the specificity and
RT efficiency of its autophagic degradation.";
RL Autophagy 13:1487-1495(2017).
CC -!- FUNCTION: Guanyl-specific endoribonuclease which cleaves the
CC phosphodiester bond in single-stranded RNA between the 3'-guanylic
CC residue and the 5'-OH residue of adjacent nucleotide, resulting in the
CC formation of a corresponding 2',3'-cyclic phosphate intermediate
CC (PubMed:26787882). P-granule component involved in germline development
CC (PubMed:15238518, PubMed:19372764, PubMed:24746798). Together with the
CC P-granule component pgl-1, is involved in the formation of P-granules
CC (PubMed:21402787, PubMed:24746798, PubMed:27594427). Together with pgl-
CC 1, probably recruits other granule components such as pos-1, mex-3 and
CC glh-1, and RNA to P-granules (PubMed:21402787, PubMed:27594427). In
CC vitro, binds mRNA; this interaction is required for the formation of
CC liquid-like droplets that resemble P-granules (PubMed:27594427). Most
CC likely recruits pgl-1 into P-granules during autophagy
CC (PubMed:19167332). Associates with adapters such as sepa-1 and is
CC required for the accumulation and degradation of P-granules by
CC autophagy in somatic cells (PubMed:19167332, PubMed:24140420,
CC PubMed:28806108). This ensures exclusive localization of the P-granules
CC in germ cells (PubMed:19167332, PubMed:28806108). In addition, may act
CC redundantly with pgl-1 to protect germ cells from excessive germline
CC apoptosis during normal oogenesis and development of the two gonadal
CC arms (PubMed:26598553). This may in part be through regulating the
CC localization of sir-2.1 which is involved in germ cell apoptosis
CC (PubMed:26598553). May protect somatic cells from excessive apoptosis
CC during normal development (PubMed:27650246).
CC {ECO:0000269|PubMed:15238518, ECO:0000269|PubMed:19167332,
CC ECO:0000269|PubMed:19372764, ECO:0000269|PubMed:21402787,
CC ECO:0000269|PubMed:24140420, ECO:0000269|PubMed:24746798,
CC ECO:0000269|PubMed:26598553, ECO:0000269|PubMed:26787882,
CC ECO:0000269|PubMed:27594427, ECO:0000269|PubMed:27650246,
CC ECO:0000269|PubMed:28806108}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[RNA] containing guanosine + H2O = an [RNA fragment]-3'-
CC guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA
CC fragment].; EC=4.6.1.24; Evidence={ECO:0000269|PubMed:26787882};
CC -!- SUBUNIT: May form a homodimer (PubMed:21402787, PubMed:26787882).
CC Interacts with pgl-1 and pgl-2; this association is not required for P-
CC granule localization of either pgl-1 or pgl-2 (PubMed:15238518).
CC Interacts with sepa-1; the interaction is enhanced in the presence of
CC RNA (PubMed:19167332, PubMed:24140420). Interacts with prmt-1; the
CC interaction is direct (PubMed:24140420). {ECO:0000269|PubMed:15238518,
CC ECO:0000269|PubMed:19167332, ECO:0000269|PubMed:24140420,
CC ECO:0000269|PubMed:26787882, ECO:0000303|PubMed:21402787}.
CC -!- INTERACTION:
CC G5EBV6; G5EC37: sepa-1; NbExp=5; IntAct=EBI-328338, EBI-2256317;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:15238518,
CC ECO:0000269|PubMed:19372764, ECO:0000269|PubMed:21402787,
CC ECO:0000269|PubMed:24140420, ECO:0000269|PubMed:26598553,
CC ECO:0000269|PubMed:27594427, ECO:0000269|PubMed:27650246,
CC ECO:0000269|PubMed:28806108, ECO:0000305|PubMed:19167332}.
CC Note=Localizes to P granules in germ cells at all stages of development
CC except in spermatogenesis (PubMed:15238518). Localizes to the germ
CC precursor cells Z2 and Z3 in embryos (PubMed:19372764, PubMed:24140420,
CC PubMed:27650246). Co-localizes with pgl-1 in P-granules, but
CC localization in P-granules is not dependent on an association with pgl-
CC 1 (PubMed:15238518, PubMed:21402787). {ECO:0000269|PubMed:15238518,
CC ECO:0000269|PubMed:19372764, ECO:0000269|PubMed:21402787,
CC ECO:0000269|PubMed:24140420, ECO:0000269|PubMed:27650246}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:C18G1.4a};
CC IsoId=G5EBV6-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C18G1.4b};
CC IsoId=G5EBV6-2; Sequence=VSP_059308;
CC -!- TISSUE SPECIFICITY: Highly expressed in the germline (PubMed:15238518).
CC Expressed in most somatic cells (PubMed:27650246).
CC {ECO:0000269|PubMed:15238518, ECO:0000269|PubMed:27650246}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development from embryos to
CC adults (PubMed:15238518, PubMed:27650246). Not expressed in somatic
CC cells of embryos (PubMed:28806108). First expressed in 1-cell embryos,
CC and expression continues until the 24-cell stage (PubMed:15238518).
CC Highly expressed in early stage embryos (PubMed:19167332). Expression
CC decreases after the 24-cell stage and is negligible throughout the rest
CC of embryogenesis and early stages of larval development
CC (PubMed:15238518, PubMed:19167332). During larval development, first
CC expressed in the germline of L3 stage larvae (PubMed:15238518).
CC {ECO:0000269|PubMed:15238518, ECO:0000269|PubMed:19167332,
CC ECO:0000269|PubMed:27650246, ECO:0000269|PubMed:28806108}.
CC -!- DOMAIN: The dimerization domain also acts as a hinge; changes in its
CC structure probably impact oligomerization and RNA-binding.
CC {ECO:0000305|PubMed:26787882}.
CC -!- DOMAIN: The RNA-binding RGG-box is required for the recruitment of some
CC P-granule components such as pos-1 and probably mRNA, but is
CC dispensable for granule formation. {ECO:0000269|PubMed:21402787,
CC ECO:0000305|PubMed:15238518, ECO:0000305|PubMed:27594427}.
CC -!- PTM: Methylated at arginine residues in the RNA-binding RGG-box by
CC prmt-1. Methylation promotes P-granule degradation by autophagy.
CC {ECO:0000269|PubMed:24140420}.
CC -!- DISRUPTION PHENOTYPE: Viable, and not temperature sensitive
CC (PubMed:15238518). Failed degradation and diffuse cytoplasmic
CC localization of the P-granule component pgl-1 in the somatic cells of
CC embryos (PubMed:19167332). Increased germ cell apoptosis in gonadal
CC arms, and this is further increased following UV irradiation
CC (PubMed:26598553). Double knockout with pgl-1 results in 37% of progeny
CC arresting as late embryos and 9% as larvae at 26 degrees Celsius
CC (PubMed:15238518). Double knockout with pgl-1 enhances the temperature-
CC sensitive sterility phenotype and germline defects of the pgl-1 single
CC knockout (PubMed:15238518, PubMed:26598553). Germline defects include
CC increased apoptosis in the gonad, fewer germ nuclei, no sperm and no
CC oocytes in the gonad arms (PubMed:15238518, PubMed:26598553). The
CC gonads of the double knockout with pgl-1 degenerate as the adults age
CC (PubMed:15238518). Conversely, double knockout with ced-1 results in
CC reduced somatic cell apoptosis (PubMed:27650246). Triple knockout with
CC pgl-1 and pgl-2 results in 58% of progeny arresting as late embryos and
CC 5% as larvae at 26 degrees Celsius (PubMed:15238518). Triple knockout
CC with pgl-1 and him-3 further reduces the number of self-cross progeny
CC as compared to the pgl-1 and him-3 double mutant and him-3 single
CC mutant (PubMed:15238518). Double RNAi-mediated knockdown with pgl-1
CC results in a reduced number of pos-1, mex-1 and glh-1 positive granules
CC in embryos (PubMed:21402787). Quadruple RNAi-mediated knockdown with
CC glh-1, glh-4 and pgl-1 results in offspring that display 27-89%
CC sterility, abnormal oocytes and do not have embryos in the uterus
CC (PubMed:24746798). These sterile offspring still produce sperm
CC (PubMed:24746798). Furthermore, these offspring may have compromised P-
CC granule integrity as there is diffuse cytoplasmic localization of the
CC P-granule component deps-1, which may cause germ cells to initiate
CC somatic reprogramming (PubMed:24746798). RNAi-mediated knockdown in a
CC double ced-1 and hpl-2 mutant background rescues the reduced somatic
CC cell apoptotic cell defect in the ced-1 and hpl-2 double knockout at 25
CC degrees Celsius (PubMed:27650246). {ECO:0000269|PubMed:15238518,
CC ECO:0000269|PubMed:19167332, ECO:0000269|PubMed:21402787,
CC ECO:0000269|PubMed:24746798, ECO:0000269|PubMed:26598553,
CC ECO:0000269|PubMed:27650246}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB120729; BAC87886.1; -; mRNA.
DR EMBL; BX284605; CCD65226.1; -; Genomic_DNA.
DR EMBL; BX284605; CCD65227.1; -; Genomic_DNA.
DR PIR; T33251; T33251.
DR RefSeq; NP_504278.1; NM_071877.4. [G5EBV6-1]
DR RefSeq; NP_504279.1; NM_071878.3. [G5EBV6-2]
DR AlphaFoldDB; G5EBV6; -.
DR SMR; G5EBV6; -.
DR IntAct; G5EBV6; 1.
DR STRING; 6239.C18G1.4a; -.
DR EPD; G5EBV6; -.
DR PaxDb; G5EBV6; -.
DR PeptideAtlas; G5EBV6; -.
DR EnsemblMetazoa; C18G1.4a.1; C18G1.4a.1; WBGene00003994. [G5EBV6-1]
DR EnsemblMetazoa; C18G1.4b.1; C18G1.4b.1; WBGene00003994. [G5EBV6-2]
DR GeneID; 178867; -.
DR KEGG; cel:CELE_C18G1.4; -.
DR UCSC; C18G1.4a; c. elegans.
DR CTD; 178867; -.
DR WormBase; C18G1.4a; CE17420; WBGene00003994; pgl-3. [G5EBV6-1]
DR WormBase; C18G1.4b; CE27717; WBGene00003994; pgl-3. [G5EBV6-2]
DR eggNOG; ENOG502QVYU; Eukaryota.
DR GeneTree; ENSGT00970000196090; -.
DR HOGENOM; CLU_362575_0_0_1; -.
DR InParanoid; G5EBV6; -.
DR OMA; LEHYENE; -.
DR OrthoDB; 1081147at2759; -.
DR PhylomeDB; G5EBV6; -.
DR PRO; PR:G5EBV6; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003994; Expressed in adult organism and 3 other tissues.
DR GO; GO:0043229; C:intracellular organelle; IDA:WormBase.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:WormBase.
DR GO; GO:0042802; F:identical protein binding; IPI:WormBase.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046589; F:ribonuclease T1 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; ISS:WormBase.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:WormBase.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Endonuclease; Hydrolase;
KW Lyase; Methylation; Nuclease; Reference proteome; RNA-binding.
FT CHAIN 1..693
FT /note="Guanyl-specific ribonuclease pgl-3"
FT /evidence="ECO:0000305"
FT /id="PRO_0000443017"
FT REGION 205..447
FT /note="Involved in dimerization"
FT /evidence="ECO:0000269|PubMed:26787882"
FT REGION 445..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..614
FT /note="Required for interaction with sepa-1"
FT /evidence="ECO:0000269|PubMed:19167332"
FT REGION 620..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..693
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000269|PubMed:27594427,
FT ECO:0000305|PubMed:15238518"
FT COMPBIAS 524..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 437
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9TZQ3"
FT VAR_SEQ 1..88
FT /note="MEANKRQIVEVDGIKSYFFPHLAHYLASNDELLVNNIAQANKLAAFVLGATD
FT KRPSNEEIAEMILPNDSSAYVLAAGMDVCLILGDDF -> MTPVPTCLLLAWTFALFSG
FT MTSL (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059308"
FT MUTAGEN 627
FT /note="R->A: No effect on methylation of the RNA-binding
FT RGG-box."
FT /evidence="ECO:0000269|PubMed:24140420"
FT MUTAGEN 633..692
FT /note="Missing: Globular cytoplasmic granules form, but do
FT not contain the P-granule components such as pos-1."
FT /evidence="ECO:0000269|PubMed:21402787"
FT MUTAGEN 634
FT /note="R->A: No effect on methylation of the RNA-binding
FT RGG-box."
FT /evidence="ECO:0000269|PubMed:24140420"
FT MUTAGEN 634
FT /note="R->L: Abolishes RNA-binding; when associated with G-
FT 638; L-650; G-661; G-665 and G-690."
FT /evidence="ECO:0000269|PubMed:27594427"
FT MUTAGEN 638
FT /note="R->A: No effect on methylation of the RNA-binding
FT RGG-box."
FT /evidence="ECO:0000269|PubMed:24140420"
FT MUTAGEN 638
FT /note="R->G: Abolishes RNA-binding; when associated with L-
FT 634; L-650; G-661; G-665 and G-690."
FT /evidence="ECO:0000269|PubMed:27594427"
FT MUTAGEN 641
FT /note="R->A: Reduces methylation of the RNA-binding RGG-
FT box. Abolishes methylation of the RNA-binding RGG-box; when
FT associated with A-650; A-658; A-661; A-665; A-668; A-676;
FT A-682 and A-690."
FT /evidence="ECO:0000269|PubMed:24140420"
FT MUTAGEN 648
FT /note="R->A: No effect on methylation of the RNA-binding
FT RGG-box."
FT /evidence="ECO:0000269|PubMed:24140420"
FT MUTAGEN 650
FT /note="R->A: Reduces methylation of the RNA-binding RGG-
FT box. Abolishes methylation of the RNA-binding RGG-box; when
FT associated with A-641; A-658; A-661; A-665; A-668; A-676;
FT A-682 and A-690."
FT /evidence="ECO:0000269|PubMed:24140420"
FT MUTAGEN 650
FT /note="R->L: Abolishes RNA-binding; when associated with L-
FT 634; G-638; G-661; G-665 and G-690."
FT /evidence="ECO:0000269|PubMed:27594427"
FT MUTAGEN 658
FT /note="R->A: Reduces methylation of the RNA-binding RGG-
FT box. Abolishes methylation of the RNA-binding RGG-box; when
FT associated with A-641; A-650; A-661; A-665; A-668; A-676;
FT A-682 and A-690."
FT /evidence="ECO:0000269|PubMed:24140420"
FT MUTAGEN 661
FT /note="R->A: Reduces methylation of the RNA-binding RGG-
FT box. Abolishes methylation of the RNA-binding RGG-box; when
FT associated with A-641; A-650; A-658; A-665; A-668; A-676;
FT A-682 and A-690."
FT /evidence="ECO:0000269|PubMed:24140420"
FT MUTAGEN 661
FT /note="R->G: Abolishes RNA-binding; when associated with L-
FT 634; G-638; L-650; G-665 and G-690."
FT /evidence="ECO:0000269|PubMed:27594427"
FT MUTAGEN 665
FT /note="R->A: Reduces methylation of the RNA-binding RGG-
FT box. Abolishes methylation of the RNA-binding RGG-box; when
FT associated with A-641; A-650; A-658; A-661; A-668; A-676;
FT A-682 and A-690."
FT /evidence="ECO:0000269|PubMed:24140420"
FT MUTAGEN 665
FT /note="R->G: Abolishes RNA-binding; when associated with L-
FT 634; G-638; L-650; G-661 and G-690."
FT /evidence="ECO:0000269|PubMed:27594427"
FT MUTAGEN 668
FT /note="R->A: Reduces methylation of the RNA-binding RGG-
FT box. Abolishes methylation of the RNA-binding RGG-box; when
FT associated with A-641; A-650; A-658; A-661; A-665; A-676;
FT A-682 and A-690."
FT /evidence="ECO:0000269|PubMed:24140420"
FT MUTAGEN 676
FT /note="R->A: Reduces methylation of the RNA-binding RGG-
FT box. Abolishes methylation of the RNA-binding RGG-box; when
FT associated with A-641; A-650; A-658; A-661; A-665; A-668;
FT A-682 and A-690."
FT /evidence="ECO:0000269|PubMed:24140420"
FT MUTAGEN 682
FT /note="R->A: Reduces methylation of the RNA-binding RGG-
FT box. Abolishes methylation of the RNA-binding RGG-box; when
FT associated with A-641; A-650; A-658; A-661; A-665; A-668;
FT A-676 and A-690."
FT /evidence="ECO:0000269|PubMed:24140420"
FT MUTAGEN 690
FT /note="R->A: Reduces methylation of the RNA-binding RGG-
FT box. Abolishes methylation of the RNA-binding RGG-box; when
FT associated with A-641; A-650; A-658; A-661; A-665; A-668;
FT A-676 and A-682."
FT /evidence="ECO:0000269|PubMed:24140420"
FT MUTAGEN 690
FT /note="R->G: Abolishes RNA-binding; when associated with L-
FT 634; G-638; L-650; G-661 and G-665."
FT /evidence="ECO:0000269|PubMed:27594427"
SQ SEQUENCE 693 AA; 74845 MW; 16DA54282F3D8CB0 CRC64;
MEANKRQIVE VDGIKSYFFP HLAHYLASND ELLVNNIAQA NKLAAFVLGA TDKRPSNEEI
AEMILPNDSS AYVLAAGMDV CLILGDDFRP KFDSGAEKLS QLGQAHDLAP IIDDEKKISM
LARKTKLKKS NDAKILQVLL KVLGAEEAEE KFVELSELSS ALDLDFDVYV LAKLLGFASE
ELQEEIEIIR DNVTDAFEAC KPLLKKLMIE GPKIDSVDPF TQLLLTPQEE SIEKAVSHIV
ARFEEASAVE DDESLVLKSQ LGYQLIFLVV RSLADGKRDA SRTIQSLMPS SVRAEVFPGL
QRSVFKSAVF LASHIIQVFL GSMKSFEDWA FVGLAEDLES TWRRRAIAEL LKKFRISVLE
QCFSQPIPLL PQSELNNETV IENVNNALQF ALWITEFYGS ESEKKSLNQL QFLSPKSKNL
LVDSFKKFAQ GLDSKDHVNR IIESLEKSSS SEPSATAKQT TTSNGPTTVS TAAQVVTVEK
MPFSRQTIPC EGTDLANVLN SAKIIGESVT VAAHDVIPEK LNAEKNDNTP STASPVQFSS
DGWDSPTKSV ALPPKISTLE EEQEEDTTIT KVSPQPQERT GTAWGSGDAT PVPLATPVNE
YKVSGFGAAP VASGFGQFAS SNGTSGRGSY GGGRGGDRGG RGAYGGDRGR GGSGDGSRGY
RGGDRGGRGS YGEGSRGYQG GRAGFFGGSR GGS
