RBM20_RAT
ID RBM20_RAT Reviewed; 1207 AA.
AC E9PT37; C1IEE3;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=RNA-binding protein 20 {ECO:0000305};
DE AltName: Full=RNA-binding motif protein 20 {ECO:0000305};
GN Name=Rbm20 {ECO:0000303|PubMed:22466703, ECO:0000312|RGD:1307427};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Brown Norway;
RX PubMed=22466703; DOI=10.1038/nm.2693;
RA Guo W., Schafer S., Greaser M.L., Radke M.H., Liss M., Govindarajan T.,
RA Maatz H., Schulz H., Li S., Parrish A.M., Dauksaite V., Vakeel P.,
RA Klaassen S., Gerull B., Thierfelder L., Regitz-Zagrosek V., Hacker T.A.,
RA Saupe K.W., Dec G.W., Ellinor P.T., MacRae C.A., Spallek B., Fischer R.,
RA Perrot A., Ozcelik C., Saar K., Hubner N., Gotthardt M.;
RT "RBM20, a gene for hereditary cardiomyopathy, regulates titin splicing.";
RL Nat. Med. 18:766-773(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-963; SER-1057; SER-1096;
RP SER-1101 AND SER-1192, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23307558; DOI=10.1093/nar/gks1362;
RA Li S., Guo W., Dewey C.N., Greaser M.L.;
RT "Rbm20 regulates titin alternative splicing as a splicing repressor.";
RL Nucleic Acids Res. 41:2659-2672(2013).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24367651; DOI=10.1371/journal.pone.0084281;
RA Guo W., Pleitner J.M., Saupe K.W., Greaser M.L.;
RT "Pathophysiological defects and transcriptional profiling in the
RT RBM20-/- rat model.";
RL PLoS ONE 8:e84281-e84281(2013).
RN [6]
RP FUNCTION.
RX PubMed=24960161; DOI=10.1172/jci74523;
RA Maatz H., Jens M., Liss M., Schafer S., Heinig M., Kirchner M., Adami E.,
RA Rintisch C., Dauksaite V., Radke M.H., Selbach M., Barton P.J., Cook S.A.,
RA Rajewsky N., Gotthardt M., Landthaler M., Hubner N.;
RT "RNA-binding protein RBM20 represses splicing to orchestrate cardiac pre-
RT mRNA processing.";
RL J. Clin. Invest. 124:3419-3430(2014).
RN [7]
RP FUNCTION.
RX PubMed=25573899; DOI=10.1093/jmcb/mjv002;
RA Zhu C., Yin Z., Ren J., McCormick R.J., Ford S.P., Guo W.;
RT "RBM20 is an essential factor for thyroid hormone-regulated titin isoform
RT transition.";
RL J. Mol. Cell Biol. 7:88-90(2015).
RN [8]
RP FUNCTION.
RX PubMed=27289039; DOI=10.1002/1873-3468.12251;
RA Ito J., Iijima M., Yoshimoto N., Niimi T., Kuroda S., Maturana A.D.;
RT "RBM20 and RBM24 cooperatively promote the expression of short enh splice
RT variants.";
RL FEBS Lett. 590:2262-2274(2016).
RN [9]
RP FUNCTION.
RX PubMed=33805770; DOI=10.3390/ijms22062928;
RA Maimaiti R., Zhu C., Zhang Y., Ding Q., Guo W.;
RT "RBM20-mediated pre-mRNA splicing has muscle-specificity and differential
RT hormonal responses between muscles and in muscle cell cultures.";
RL Int. J. Mol. Sci. 22:0-0(2021).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-638; SER-640;
RP SER-643; SER-645; SER-652; SER-729; SER-789; SER-879; SER-881; SER-999;
RP SER-1034; SER-1046; SER-1057; SER-1096; SER-1190 AND SER-1192, AND
RP MUTAGENESIS OF SER-638; SER-640; SER-643; SER-645; SER-652; SER-729;
RP SER-789; SER-879; SER-881; SER-999; SER-1034; SER-1046; SER-1057; SER-1096;
RP SER-1190 AND SER-1192.
RX PubMed=35394688; DOI=10.1096/fj.202101811rr;
RA Zhang Y., Wang C., Sun M., Jin Y., Braz C.U., Khatib H., Hacker T.A.,
RA Liss M., Gotthardt M., Granzier H., Ge Y., Guo W.;
RT "RBM20 phosphorylation and its role in nucleocytoplasmic transport and
RT cardiac pathogenesis.";
RL FASEB J. 36:e22302-e22302(2022).
CC -!- FUNCTION: RNA-binding protein that acts as a regulator of mRNA splicing
CC of a subset of genes encoding key structural proteins involved in
CC cardiac development, such as TTN (Titin), CACNA1C, CAMK2D or PDLIM5/ENH
CC (PubMed:22466703, PubMed:23307558, PubMed:24367651, PubMed:24960161,
CC PubMed:25573899, PubMed:27289039, PubMed:33805770, PubMed:35394688).
CC Acts as a repressor of mRNA splicing: specifically binds the 5'UCUU-3'
CC motif that is predominantly found within intronic sequences of pre-
CC mRNAs, leading to the exclusion of specific exons in target transcripts
CC (PubMed:23307558, PubMed:24367651, PubMed:24960161, PubMed:25573899).
CC RBM20-mediated exon skipping is hormone-dependent and is essential for
CC TTN isoform transition in both cardiac and skeletal muscles
CC (PubMed:23307558, PubMed:24367651, PubMed:24960161, PubMed:25573899,
CC PubMed:33805770, PubMed:35394688). RBM20-mediated exon skipping of TTN
CC provides substrates for the formation of circular RNA (circRNAs) from
CC the TTN transcripts (By similarity). Together with RBM24, promotes the
CC expression of short isoforms of PDLIM5/ENH in cardiomyocytes
CC (PubMed:27289039). {ECO:0000250|UniProtKB:Q5T481,
CC ECO:0000269|PubMed:22466703, ECO:0000269|PubMed:23307558,
CC ECO:0000269|PubMed:24367651, ECO:0000269|PubMed:24960161,
CC ECO:0000269|PubMed:25573899, ECO:0000269|PubMed:27289039,
CC ECO:0000269|PubMed:33805770, ECO:0000269|PubMed:35394688}.
CC -!- SUBUNIT: Associates with components of the U1 and U2 U1 small nuclear
CC ribonucleoprotein complexes. {ECO:0000250|UniProtKB:Q5T481}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130,
CC ECO:0000269|PubMed:23307558, ECO:0000269|PubMed:35394688}. Cytoplasm,
CC Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:35394688}.
CC Note=The active form that regulates alternative splicing localizes to
CC the nucleus (PubMed:35394688). Also localizes to cytoplasmic
CC ribonucleoprotein granules; localization to cytoplasmic
CC ribonucleoprotein granules plays an important regulatory role (By
CC similarity). Subcellular localization is regulated by phosphorylation
CC of different parts of the protein: while phosphorylation of the RS
CC (arginine/serine-rich) region promotes nuclear localization,
CC phosphorylation of the C-terminal disordered region promotes
CC localization to cytoplasmic ribonucleoprotein granules
CC (PubMed:35394688). {ECO:0000250|UniProtKB:Q5T481,
CC ECO:0000269|PubMed:35394688}.
CC -!- PTM: Phosphorylation regulates the subcellular localization.
CC Phosphorylation of Ser-638 and Ser-640 in the RS (arginine/serine-rich)
CC region promotes nuclear localization of the protein (PubMed:35394688).
CC In contrast, phosphorylation of the C-terminal disordered region
CC promotes localization to cytoplasmic ribonucleoprotein granules (By
CC similarity). {ECO:0000250|UniProtKB:Q5T481,
CC ECO:0000269|PubMed:35394688}.
CC -!- DISRUPTION PHENOTYPE: Heterozygous or homozygous adults display left
CC ventricular dilatation (PubMed:22466703, PubMed:24367651). Left
CC ventricular diastolic diameters are significantly larger, although
CC there is no differences in the systolic ventricular dimensions or
CC contractility indices (PubMed:22466703). Subendocardial fibrosis
CC increases with age and was accompanied by electrical abnormalities,
CC such as widening of the QRS complex, atrioventricular conduction delay
CC and a predisposition to arrhythmia (PubMed:22466703). Rats are at risk
CC of sudden death caused by heart failure (PubMed:22466703,
CC PubMed:24367651). {ECO:0000269|PubMed:22466703,
CC ECO:0000269|PubMed:24367651}.
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DR EMBL; EU562301; ACD80091.1; -; mRNA.
DR RefSeq; NP_001101081.2; NM_001107611.2.
DR AlphaFoldDB; E9PT37; -.
DR SMR; E9PT37; -.
DR STRING; 10116.ENSRNOP00000051570; -.
DR iPTMnet; E9PT37; -.
DR PhosphoSitePlus; E9PT37; -.
DR PaxDb; E9PT37; -.
DR PRIDE; E9PT37; -.
DR Ensembl; ENSRNOT00000054685; ENSRNOP00000051570; ENSRNOG00000014705.
DR GeneID; 309544; -.
DR KEGG; rno:309544; -.
DR UCSC; RGD:1307427; rat.
DR CTD; 282996; -.
DR RGD; 1307427; Rbm20.
DR eggNOG; ENOG502QW62; Eukaryota.
DR GeneTree; ENSGT01030000234642; -.
DR HOGENOM; CLU_007364_0_0_1; -.
DR InParanoid; E9PT37; -.
DR OMA; HPFSGVM; -.
DR OrthoDB; 1545178at2759; -.
DR TreeFam; TF333921; -.
DR PRO; PR:E9PT37; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000014705; Expressed in heart and 16 other tissues.
DR Genevisible; E9PT37; RN.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:1990935; F:splicing factor binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0060914; P:heart formation; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISO:RGD.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12685; RRM_RBM20; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034791; RBM20.
DR InterPro; IPR034790; RBM20_RRM.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR15592:SF11; PTHR15592:SF11; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..1207
FT /note="RNA-binding protein 20"
FT /id="PRO_0000419984"
FT DOMAIN 521..596
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 412..446
FT /note="U1-type"
FT /evidence="ECO:0000255"
FT ZN_FING 1141..1172
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..650
FT /note="RS"
FT /evidence="ECO:0000250|UniProtKB:Q5T481"
FT REGION 722..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..57
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1067
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688"
FT MOD_RES 789
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T481"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T481"
FT MOD_RES 879
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688"
FT MOD_RES 963
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688"
FT MOD_RES 1046
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688"
FT MOD_RES 1057
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 1066
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UQS8"
FT MOD_RES 1078
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UQS8"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 1101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1190
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688"
FT MOD_RES 1192
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35394688,
FT ECO:0007744|PubMed:22673903"
FT MUTAGEN 638
FT /note="S->A: Impaired ability to regulate alternative
FT splicing of Ttn (Titin) mRNAs. Decreased localization to
FT the nucleus associated with an increased localization to
FT cytoplasmic ribonucleoprotein granules."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 638
FT /note="S->D: Mimics phosphorylation; does not restore
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 640
FT /note="S->D: Mimics phosphorylation; does not restore
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 640
FT /note="S->G: Impaired ability to regulate alternative
FT splicing of Ttn (Titin) mRNAs. Decreased localization to
FT the nucleus associated with an increased localization to
FT cytoplasmic ribonucleoprotein granules."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 643
FT /note="S->A: No effect; does not affect ability to regulate
FT alternative splicing."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 645
FT /note="S->A: No effect; does not affect ability to regulate
FT alternative splicing."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 652
FT /note="S->A: No effect; does not affect ability to regulate
FT alternative splicing."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 729
FT /note="S->A: No effect; does not affect ability to regulate
FT alternative splicing."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 789
FT /note="S->A: No effect; does not affect ability to regulate
FT alternative splicing."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 879
FT /note="S->A: No effect; does not affect ability to regulate
FT alternative splicing."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 881
FT /note="S->A: No effect; does not affect ability to regulate
FT alternative splicing."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 999
FT /note="S->A: No effect; does not affect ability to regulate
FT alternative splicing."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 1034
FT /note="S->A: No effect; does not affect ability to regulate
FT alternative splicing."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 1046
FT /note="S->A: No effect; does not affect ability to regulate
FT alternative splicing."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 1057
FT /note="S->A: No effect; does not affect ability to regulate
FT alternative splicing."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 1096
FT /note="S->A: No effect; does not affect ability to regulate
FT alternative splicing."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 1190
FT /note="S->A: No effect; does not affect ability to regulate
FT alternative splicing."
FT /evidence="ECO:0000269|PubMed:35394688"
FT MUTAGEN 1192
FT /note="S->A: No effect; does not affect ability to regulate
FT alternative splicing."
FT /evidence="ECO:0000269|PubMed:35394688"
FT CONFLICT 1043
FT /note="Q -> R (in Ref. 1; ACD80091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1207 AA; 130760 MW; 18BBB27389FAA953 CRC64;
MVLAAAMSQD ADPSGPEQPD RDACIVPGVQ GPPAPQGQQG MQPLPPPLPP PPQPQSSLPQ
IIQNAAKLLD KNPFSVSSQN PLLTSPASVQ LAQIQAQLTL HRLKMAQTAV TNNTAAATVL
NQVLSKVAMS QPLFNQLRHP SVLGTTHGPT GVSQHAATVP SAHFPSTAIA FSPPSQAGGP
GPSVSLPSQP PNAMVVHTFS GVVPQTPAQP AVILSIGKAG PTPATTGFYD YGKANPGQAY
GSETEGQPGF LPASASAAAS GGVTYEGHYS HTGQDGQATF SKDFYGPSAQ GSHAAGGFPA
DQAGSMKGDV GGLLQGTNSQ WERPSGFSGQ NKADITAGPG LWAPPASQPY ELYDPEEPTS
DRAPPAFGSR LNNSKQGFNC SCRRTKEGQA MLSVRPLQGH QLNDFRGLAP LHLPHICSIC
DKKVFDLKDW ELHVKGKLHA QKCLLFSESA GLRSICATGE GTLSASANST AVYNPTGNED
YTSTLGTSYA AIPTRAFAQS NPMFPSASSG TNFAQRKGAG RVVHICNLPE GSCTENDVIN
LGLPFGKVTN YILMKSTNQA FLEMAYTEAA QAMVQYYQEK PALINGEKLL IRMSTRYKEL
QLKKPGKNVA AIIQDIHSQR ERCMLREADR YGPERPRSRS PMSRSLSPRS HSPPGPSRAD
WGNGRDSYAW RDEDRETVPR RENGEDKRDR LDVWAHDRKH YPRQLDKAEL DERLEGGRGY
REKYLKSGSP GPLHSASGYK GREDGYHRKE TKAKLDKHPK QQQQDVPGRS RRKEEARLRE
PRHPHPEDSG KEEDLEPKVT RAPEGTKSKQ SEKSKTKRAD RDQEGADDKK EGRGAENEAG
TEEQEGMEES PASVGTQQEG TESSDPENTR TKKGQDCDSG SEPEGDNWYP TNMEELVTVD
EVGEEDFIME PDIPELEEIV PIDQKDKILP EICPCVTATL GLDLAKDFTK QGETLGNGDA
ELSPKLPGQV PSTSTSCPND TDMEMAGLNL DAERKPAESE TGLSPEVSNC YEKEARGAEG
SDVRLAPAAQ RMSSPQPADE RAQQSSPFLD DCKARGSPED GPHEVSPLEE KASPTTESDL
QSQACQENSR YTETRSLNSR SPEFTEAELK EPLSLPSWEP EVFSELSIPL GVEFVVPRTG
FYCKLCGLFY TSEEAAKVSH CRSTVHYRNL QKYLSQLAEE GLKETEGVDS PSPERSGIGP
HLERKKL
