U2AF4_MOUSE
ID U2AF4_MOUSE Reviewed; 220 AA.
AC Q8BGJ9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Splicing factor U2AF 26 kDa subunit;
DE AltName: Full=U2 auxiliary factor 26;
DE AltName: Full=U2 small nuclear RNA auxiliary factor 1-like protein 4;
DE Short=U2AF1-like 4 {ECO:0000303|PubMed:18460468};
GN Name=U2af1l4; Synonyms=U2af26;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION,
RP RNA-BINDING, INTERACTION WITH U2AF2, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/SvEvTacfBr, and C57BL/6J; TISSUE=Brain;
RX PubMed=11739736; DOI=10.1128/mcb.22.1.221-230.2002;
RA Shepard J., Reick M., Olson S., Graveley B.R.;
RT "Characterization of U2AF(6), a splicing factor related to U2AF(35).";
RL Mol. Cell. Biol. 22:221-230(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
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 TISSUE=Brain;
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 FUNCTION, INTERACTION WITH GFI1 AND U2AF2, INDUCTION, AND SUBCELLULAR
RP LOCATION (ISOFORM 1).
RX PubMed=16819553; DOI=10.1038/ni1361;
RA Heyd F., ten Dam G., Moeroey T.;
RT "Auxiliary splice factor U2AF26 and transcription factor Gfi1 cooperate
RT directly in regulating CD45 alternative splicing.";
RL Nat. Immunol. 7:859-867(2006).
RN [5]
RP SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), INTERACTION
RP WITH C1QBP, AND MUTAGENESIS OF PRO-190; PRO-195 AND PRO-196.
RX PubMed=18460468; DOI=10.1074/jbc.m801014200;
RA Heyd F., Carmo-Fonseca M., Moroy T.;
RT "Differential isoform expression and interaction with the P32 regulatory
RT protein controls the subcellular localization of the splicing factor
RT U2AF26.";
RL J. Biol. Chem. 283:19636-19645(2008).
RN [6]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 3 AND 4), INDUCTION BY CIRCADIAN RHYTHM
RP (ISOFORM 3), INTERACTION WITH PER1 (ISOFORM 3), DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 3).
RX PubMed=24837677; DOI=10.1016/j.molcel.2014.04.015;
RA Preussner M., Wilhelmi I., Schultz A.S., Finkernagel F., Michel M.,
RA Moeroey T., Heyd F.;
RT "Rhythmic U2af26 alternative splicing controls PERIOD1 stability and the
RT circadian clock in mice.";
RL Mol. Cell 54:651-662(2014).
CC -!- FUNCTION: RNA-binding protein that function as a pre-mRNA splicing
CC factor. Plays a critical role in both constitutive and enhancer-
CC dependent splicing by mediating protein-protein interactions and
CC protein-RNA interactions required for accurate 3'-splice site
CC selection. It can functionally substitute for U2AF1 in constitutive
CC splicing and enhancer-dependent splicing. Acts by enhancing the binding
CC of U2AF2 to weak pyrimidine tracts. Also participates in the regulation
CC of alternative pre-mRNA splicing. Activates exon 5 skipping of PTPRC
CC during T-cell activation; an event reversed by GFI1. Binds to RNA at
CC the AG dinucleotide at the 3'-splice site. Shows a preference for AGC
CC or AGA (PubMed:11739736, PubMed:16819553, PubMed:18460468). Alternative
CC splicing of U2AF1L4 may play a role in connecting the circadian rhythm
CC to changing external cues: may provide a circadian buffering system in
CC central and periphery clocks that allows synchronized adaption to
CC clock-resetting stimuli in order to prevent potentially pathogenic
CC desynchronization (PubMed:24837677). {ECO:0000269|PubMed:11739736,
CC ECO:0000269|PubMed:16819553, ECO:0000269|PubMed:24837677,
CC ECO:0000303|PubMed:18460468}.
CC -!- SUBUNIT: Interacts with GFI1, U2AF2 and C1QBP. Isoform 3 interacts with
CC PER1. {ECO:0000269|PubMed:11739736, ECO:0000269|PubMed:16819553,
CC ECO:0000269|PubMed:18460468, ECO:0000269|PubMed:24837677}.
CC -!- INTERACTION:
CC Q8BGJ9; O35658: C1qbp; NbExp=4; IntAct=EBI-4288480, EBI-642072;
CC Q8BGJ9; P70338: Gfi1; NbExp=5; IntAct=EBI-4288480, EBI-3954754;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:11739736, ECO:0000269|PubMed:18460468}. Nucleus
CC speckle {ECO:0000269|PubMed:11739736}. Cytoplasm
CC {ECO:0000269|PubMed:16819553, ECO:0000269|PubMed:18460468,
CC ECO:0000269|PubMed:24837677}. Note=Interaction with C1QBP is required
CC for the nuclear translocation. Displays active nucleo-cytoplasmic
CC shuttling. {ECO:0000269|PubMed:18460468}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC {ECO:0000269|PubMed:18460468, ECO:0000269|PubMed:24837677}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:18460468}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Circadian and light-inducible alternative splicing, which
CC occurs at least in brain and liver.;
CC Name=1; Synonyms=fl {ECO:0000303|PubMed:24837677};
CC IsoId=Q8BGJ9-1; Sequence=Displayed;
CC Name=2; Synonyms=U2AF26DeltaE7, DE7 {ECO:0000303|PubMed:18460468,
CC ECO:0000303|PubMed:24837677};
CC IsoId=Q8BGJ9-2; Sequence=VSP_056877;
CC Name=3; Synonyms=U2AF26DeltaE67, DE67 {ECO:0000303|PubMed:18460468,
CC ECO:0000303|PubMed:24837677};
CC IsoId=Q8BGJ9-3; Sequence=VSP_056875;
CC Name=4;
CC IsoId=Q8BGJ9-4; Sequence=VSP_056874, VSP_056876;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in the brain.
CC {ECO:0000269|PubMed:11739736}.
CC -!- INDUCTION: Up-regulated in response to T-cell activation (at protein
CC level) (PubMed:16819553). Circadian alternative splicing switch
CC accounts for rhythmic isoform expression. A circadian splicing switch
CC produces isoform 3 in the brain cerebellum and liver (at protein
CC level). Isoform 3 expression is regulated with the circadian rhythm but
CC is also quickly increased upon light exposure (4-8 hours after light
CC exposure). Expression of isoform 3 changes approximately 5-fold across
CC a period of 24 hours, with concomitant changes in isoform 1, resulting
CC in total U2af1l4 remaining constant (PubMed:24837677).
CC {ECO:0000269|PubMed:16819553, ECO:0000269|PubMed:24837677}.
CC -!- DOMAIN: The second zinc finger in necessary for interaction with GFI1
CC and for alternative pre-mRNA splicing events.
CC -!- DOMAIN: The region 162-220 is essential for the nuclear import of the
CC protein in spite of the absence of a nuclear localization signal (NLS).
CC This region is essential for the interaction with C1QBP, interaction
CC which is required for the nuclear translocation. This region may be
CC involved in the localization in nuclear dot-like structures and it also
CC confers the ability of nucleo-cytoplasmic shuttling.
CC {ECO:0000269|PubMed:18460468}.
CC -!- DOMAIN: Isoform 3 contains a C-terminus domain with homology to
CC Drosophila TIM (THD domain). Isoform 3 interacts with Per1 and
CC specifically down-regulates its expression, probably by facilitating
CC its recruitment to the proteasome. The interaction with PER1 depends on
CC the presence of the THD domain, but the THD domain is not directly
CC involved in the interaction. {ECO:0000269|PubMed:24837677}.
CC -!- PTM: Isoform 3 is rapidly degraded by a proteasome-mediated degradation
CC pathway. {ECO:0000269|PubMed:24837677}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice show defects in circadian gene
CC expression and jet lag phenotype, but the master clock is not strongly
CC affected. Per2 expression is rhythmic, but Per1 expression becomes
CC nearly arrhythmic as well as Per1 target genes, such as Dbp. No
CC splicing alteration was observed in the brain. Mutant mice show a
CC faster adaptation to experimental jet lag, which is consistent with the
CC circadian splicing switch providing a buffering system against sudden
CC light changes. {ECO:0000269|PubMed:24837677}.
CC -!- MISCELLANEOUS: [Isoform 1]: Cytoplasmic and nuclear. Displays active
CC nucleo-cytoplasmic shuttling. Shows a circadian expression at the mRNA
CC level. {ECO:0000269|PubMed:16819553, ECO:0000269|PubMed:18460468,
CC ECO:0000269|PubMed:24837677}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by exon 7 skipping. Cytoplasm
CC (PubMed:16819553). Shows a circadian expression at the mRNA level.
CC {ECO:0000269|PubMed:16819553, ECO:0000269|PubMed:18460468}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by exons 6 and 7 skipping.
CC Produced by a circadian splicing switch in brain and liver. Contains a
CC C-terminus domain with homology to Drosophila TIM (THD). Cytoplasmic.
CC Shows a circadian expression at the mRNA and protein levels. Expression
CC is quickly increased upon light exposure. Has a strongly reduced half-
CC life compared to other isoforms. {ECO:0000269|PubMed:24837677}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by usage of an alternative 3'
CC splice site in exon 8. {ECO:0000269|PubMed:24837677}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC -!- CAUTION: Orthologs of U2af1l4 do not appear to exist in lower
CC eukaryotes, Drosophila, C. elegans, plants, or vertebrates such as
CC Xenopus or zebrafish (PubMed:11739736). Existence of splicing isoforms
CC of U2af1l4 in human and rat is not yet proven.
CC {ECO:0000305|PubMed:24837677}.
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DR EMBL; AF419339; AAN63524.1; -; mRNA.
DR EMBL; AF419340; AAN63525.1; -; Genomic_DNA.
DR EMBL; AK160974; BAE36125.1; -; mRNA.
DR EMBL; BC060972; AAH60972.1; -; mRNA.
DR CCDS; CCDS21100.1; -. [Q8BGJ9-1]
DR RefSeq; NP_739566.1; NM_170760.3. [Q8BGJ9-1]
DR AlphaFoldDB; Q8BGJ9; -.
DR SMR; Q8BGJ9; -.
DR BioGRID; 231367; 6.
DR IntAct; Q8BGJ9; 2.
DR STRING; 10090.ENSMUSP00000039406; -.
DR iPTMnet; Q8BGJ9; -.
DR PhosphoSitePlus; Q8BGJ9; -.
DR SwissPalm; Q8BGJ9; -.
DR jPOST; Q8BGJ9; -.
DR MaxQB; Q8BGJ9; -.
DR PaxDb; Q8BGJ9; -.
DR PRIDE; Q8BGJ9; -.
DR ProteomicsDB; 298250; -. [Q8BGJ9-1]
DR ProteomicsDB; 298251; -. [Q8BGJ9-2]
DR ProteomicsDB; 298252; -. [Q8BGJ9-3]
DR ProteomicsDB; 298253; -. [Q8BGJ9-4]
DR DNASU; 233073; -.
DR Ensembl; ENSMUST00000043273; ENSMUSP00000039406; ENSMUSG00000078765. [Q8BGJ9-1]
DR Ensembl; ENSMUST00000163654; ENSMUSP00000131048; ENSMUSG00000078765. [Q8BGJ9-2]
DR Ensembl; ENSMUST00000167042; ENSMUSP00000128886; ENSMUSG00000109378. [Q8BGJ9-1]
DR Ensembl; ENSMUST00000171912; ENSMUSP00000130983; ENSMUSG00000109378. [Q8BGJ9-1]
DR GeneID; 233073; -.
DR KEGG; mmu:233073; -.
DR UCSC; uc009gfa.1; mouse. [Q8BGJ9-1]
DR CTD; 199746; -.
DR MGI; MGI:2678374; U2af1l4.
DR VEuPathDB; HostDB:ENSMUSG00000078765; -.
DR VEuPathDB; HostDB:ENSMUSG00000109378; -.
DR eggNOG; KOG2202; Eukaryota.
DR GeneTree; ENSGT00950000183152; -.
DR InParanoid; Q8BGJ9; -.
DR OMA; DSAGHYP; -.
DR OrthoDB; 1340384at2759; -.
DR PhylomeDB; Q8BGJ9; -.
DR TreeFam; TF300143; -.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR BioGRID-ORCS; 233073; 0 hits in 71 CRISPR screens.
DR ChiTaRS; U2af1l4; mouse.
DR PRO; PR:Q8BGJ9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BGJ9; protein.
DR Bgee; ENSMUSG00000078765; Expressed in primary oocyte and 61 other tissues.
DR ExpressionAtlas; Q8BGJ9; baseline and differential.
DR Genevisible; Q8BGJ9; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0089701; C:U2AF complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR009145; U2AF_small.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR12620; PTHR12620; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00642; zf-CCCH; 2.
DR PRINTS; PR01848; U2AUXFACTOR.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00361; RRM_1; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Biological rhythms; Cytoplasm;
KW Metal-binding; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Repeat; RNA-binding; Spliceosome; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WU68"
FT CHAIN 2..220
FT /note="Splicing factor U2AF 26 kDa subunit"
FT /id="PRO_0000309741"
FT DOMAIN 65..147
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 12..40
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 149..176
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 186..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8WU68"
FT VAR_SEQ 61..143
FT /note="TADGSHCHVSDVEVQEHYDNFFEEVFTELQEKYGEIEEMNVCDNLGDHLVGN
FT VYVKFRREEDAERAVAELNNRWFNGQAVHAE -> ASELHNIICSTQEPPPPVPPPIKV
FT KKFVNQGLWFPSTPTPKKGCKPTTVSAEELGASLGSGSALVSRGCFNTCNLRLSILGAF
FT (in isoform 4)"
FT /evidence="ECO:0000269|PubMed:16819553"
FT /id="VSP_056874"
FT VAR_SEQ 117..220
FT /note="FRREEDAERAVAELNNRWFNGQAVHAELSPVTDFRESCCRQYEMGECTRGGF
FT CNFMHLRPISRNLRRQLYGRGPRHRSPPRSHTGHRPRERNRRRSPDHRHGRF -> VTS
FT KVPHRSPSPRKEPTSFPRPPAWSLLRRVPLLSTQGHRCSCPASLFKVPFTLQSQHPQAS
FT ELHNIICSTQEPPPPVPPPIKVKKFVNQGLWFPSTPTPKKGCKPTTVSAEELGASLGSG
FT SALVSRGCFNTCNLRLSILGAF (in isoform 3)"
FT /evidence="ECO:0000269|PubMed:16819553"
FT /id="VSP_056875"
FT VAR_SEQ 144..220
FT /note="Missing (in isoform 4)"
FT /id="VSP_056876"
FT VAR_SEQ 162..193
FT /note="Missing (in isoform 2)"
FT /id="VSP_056877"
FT MUTAGEN 190
FT /note="P->A: Does not impair nuclear localization."
FT /evidence="ECO:0000269|PubMed:18460468"
FT MUTAGEN 195
FT /note="P->A: Does not impair nuclear localization."
FT /evidence="ECO:0000269|PubMed:18460468"
FT MUTAGEN 196
FT /note="P->A: Does not impair nuclear localization."
FT /evidence="ECO:0000269|PubMed:18460468"
SQ SEQUENCE 220 AA; 25836 MW; 90AC4B4126060169 CRC64;
MAEYLASIFG TEKDKVNCSF YFKIGACRHG DRCSRLHNKP TFSQTIVLLN LYRNPQNTAQ
TADGSHCHVS DVEVQEHYDN FFEEVFTELQ EKYGEIEEMN VCDNLGDHLV GNVYVKFRRE
EDAERAVAEL NNRWFNGQAV HAELSPVTDF RESCCRQYEM GECTRGGFCN FMHLRPISRN
LRRQLYGRGP RHRSPPRSHT GHRPRERNRR RSPDHRHGRF
