CELF4_HUMAN
ID CELF4_HUMAN Reviewed; 486 AA.
AC Q9BZC1; Q59EN7; Q86XB9; Q8N2M6; Q9BQ96; Q9NR84; Q9NR85;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=CUGBP Elav-like family member 4;
DE Short=CELF-4;
DE AltName: Full=Bruno-like protein 4;
DE AltName: Full=CUG-BP- and ETR-3-like factor 4;
DE AltName: Full=RNA-binding protein BRUNOL-4;
GN Name=CELF4; Synonyms=BRUNOL4;
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 [MRNA] (ISOFORM 1), FUNCTION, RNA-BINDING, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11158314; DOI=10.1128/mcb.21.4.1285-1296.2001;
RA Ladd A.N., Charlet-B N., Cooper T.A.;
RT "The CELF family of RNA binding proteins is implicated in cell-specific and
RT developmentally regulated alternative splicing.";
RL Mol. Cell. Biol. 21:1285-1296(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
RC TISSUE=Brain, 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 [MRNA] OF 1-304 (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 324-486 (ISOFORMS 1/3/4).
RX PubMed=10893231; DOI=10.1074/jbc.m003083200;
RA Good P.J., Chen Q., Warner S.J., Herring D.C.;
RT "A family of human RNA-binding proteins related to the Drosophila Bruno
RT translational regulator.";
RL J. Biol. Chem. 275:28583-28592(2000).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=12438720; DOI=10.1159/000066619;
RA Meins M., Schlickum S., Wilhelm C., Missbach J., Yadav S., Glaeser B.,
RA Grzmil M., Burfeind P., Laccone F.;
RT "Identification and characterization of murine Brunol4, a new member of the
RT elav/bruno family.";
RL Cytogenet. Genome Res. 97:254-260(2002).
RN [7]
RP FUNCTION.
RX PubMed=12649496; DOI=10.1261/rna.2191903;
RA Gromak N., Matlin A.J., Cooper T.A., Smith C.W.;
RT "Antagonistic regulation of alpha-actinin alternative splicing by CELF
RT proteins and polypyrimidine tract binding protein.";
RL RNA 9:443-456(2003).
RN [8]
RP FUNCTION.
RX PubMed=15009664; DOI=10.1046/j.1471-4159.2003.02232.x;
RA Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.;
RT "Tau exon 10, whose missplicing causes frontotemporal dementia, is
RT regulated by an intricate interplay of cis elements and trans factors.";
RL J. Neurochem. 88:1078-1090(2004).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND RNA-BINDING.
RX PubMed=14973222; DOI=10.1093/nar/gkh275;
RA Singh G., Charlet-B N., Han J., Cooper T.A.;
RT "ETR-3 and CELF4 protein domains required for RNA binding and splicing
RT activity in vivo.";
RL Nucleic Acids Res. 32:1232-1241(2004).
RN [10]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=15894795; DOI=10.1093/nar/gki561;
RA Han J., Cooper T.A.;
RT "Identification of CELF splicing activation and repression domains in
RT vivo.";
RL Nucleic Acids Res. 33:2769-2780(2005).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=16862542; DOI=10.1002/jnr.20980;
RA Leroy O., Dhaenens C.-M., Schraen-Maschke S., Belarbi K., Delacourte A.,
RA Andreadis A., Sablonniere B., Buee L., Sergeant N., Caillet-Boudin M.-L.;
RT "ETR-3 represses Tau exons 2/3 inclusion, a splicing event abnormally
RT enhanced in myotonic dystrophy type I.";
RL J. Neurosci. Res. 84:852-859(2006).
RN [12]
RP STRUCTURE BY NMR OF 143-235.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA-binding domain in Bruno-like 4 RNA-binding
RT protein.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: RNA-binding protein implicated in the regulation of pre-mRNA
CC alternative splicing. Mediates exon inclusion and/or exclusion in pre-
CC mRNA that are subject to tissue-specific and developmentally regulated
CC alternative splicing. Specifically activates exon 5 inclusion of
CC cardiac isoforms of TNNT2 during heart remodeling at the juvenile to
CC adult transition. Promotes exclusion of both the smooth muscle (SM) and
CC non-muscle (NM) exons in actinin pre-mRNAs. Activates the splicing of
CC MAPT/Tau exon 10. Binds to muscle-specific splicing enhancer (MSE)
CC intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA.
CC {ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:12649496,
CC ECO:0000269|PubMed:14973222, ECO:0000269|PubMed:15009664,
CC ECO:0000269|PubMed:15894795}.
CC -!- INTERACTION:
CC Q9BZC1-2; P57721-2: PCBP3; NbExp=3; IntAct=EBI-12818201, EBI-11983983;
CC Q9BZC1-2; P86480: PRR20D; NbExp=3; IntAct=EBI-12818201, EBI-12754095;
CC Q9BZC1-2; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-12818201, EBI-11987469;
CC Q9BZC1-2; Q01085-2: TIAL1; NbExp=3; IntAct=EBI-12818201, EBI-11064654;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14973222}. Cytoplasm
CC {ECO:0000269|PubMed:14973222}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9BZC1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZC1-2; Sequence=VSP_026829, VSP_026831;
CC Name=3;
CC IsoId=Q9BZC1-3; Sequence=VSP_026829, VSP_026830;
CC Name=4;
CC IsoId=Q9BZC1-4; Sequence=VSP_026830;
CC Name=5;
CC IsoId=Q9BZC1-5; Sequence=VSP_026828, VSP_026832;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in the cerebellum,
CC hippocampus, amygdala, temporal and frontal cortex and frontal lobes.
CC {ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:12438720,
CC ECO:0000269|PubMed:16862542}.
CC -!- SIMILARITY: Belongs to the CELF/BRUNOL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93011.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF329265; AAK07475.1; -; mRNA.
DR EMBL; AK074596; BAC11082.1; -; mRNA.
DR EMBL; AB209774; BAD93011.1; ALT_INIT; mRNA.
DR EMBL; BC001946; AAH01946.2; -; mRNA.
DR EMBL; BC004167; AAH04167.2; -; mRNA.
DR EMBL; BC045711; AAH45711.1; -; mRNA.
DR EMBL; AF248650; AAF86232.1; -; mRNA.
DR EMBL; AF248651; AAF86233.1; -; mRNA.
DR CCDS; CCDS32818.1; -. [Q9BZC1-1]
DR CCDS; CCDS45856.1; -. [Q9BZC1-4]
DR CCDS; CCDS45857.1; -. [Q9BZC1-3]
DR CCDS; CCDS45858.1; -. [Q9BZC1-5]
DR CCDS; CCDS82250.1; -. [Q9BZC1-2]
DR RefSeq; NP_001020258.1; NM_001025087.1. [Q9BZC1-4]
DR RefSeq; NP_001020259.1; NM_001025088.1. [Q9BZC1-3]
DR RefSeq; NP_001020260.1; NM_001025089.1. [Q9BZC1-5]
DR RefSeq; NP_001317532.1; NM_001330603.1. [Q9BZC1-2]
DR RefSeq; NP_064565.1; NM_020180.3. [Q9BZC1-1]
DR PDB; 2DGP; NMR; -; A=48-141.
DR PDB; 2DNK; NMR; -; A=143-235.
DR PDBsum; 2DGP; -.
DR PDBsum; 2DNK; -.
DR AlphaFoldDB; Q9BZC1; -.
DR SMR; Q9BZC1; -.
DR BioGRID; 121213; 10.
DR IntAct; Q9BZC1; 4.
DR STRING; 9606.ENSP00000410584; -.
DR iPTMnet; Q9BZC1; -.
DR PhosphoSitePlus; Q9BZC1; -.
DR BioMuta; CELF4; -.
DR DMDM; 74761348; -.
DR jPOST; Q9BZC1; -.
DR MassIVE; Q9BZC1; -.
DR PaxDb; Q9BZC1; -.
DR PeptideAtlas; Q9BZC1; -.
DR PRIDE; Q9BZC1; -.
DR ProteomicsDB; 79804; -. [Q9BZC1-1]
DR ProteomicsDB; 79805; -. [Q9BZC1-2]
DR ProteomicsDB; 79806; -. [Q9BZC1-3]
DR ProteomicsDB; 79807; -. [Q9BZC1-4]
DR ProteomicsDB; 79808; -. [Q9BZC1-5]
DR ABCD; Q9BZC1; 1 sequenced antibody.
DR Antibodypedia; 22364; 77 antibodies from 19 providers.
DR DNASU; 56853; -.
DR Ensembl; ENST00000334919.9; ENSP00000335631.4; ENSG00000101489.20. [Q9BZC1-5]
DR Ensembl; ENST00000361795.9; ENSP00000355089.4; ENSG00000101489.20. [Q9BZC1-3]
DR Ensembl; ENST00000420428.7; ENSP00000410584.2; ENSG00000101489.20. [Q9BZC1-1]
DR Ensembl; ENST00000591282.5; ENSP00000464794.1; ENSG00000101489.20. [Q9BZC1-1]
DR Ensembl; ENST00000591287.5; ENSP00000464917.1; ENSG00000101489.20. [Q9BZC1-2]
DR Ensembl; ENST00000603232.6; ENSP00000474788.2; ENSG00000101489.20. [Q9BZC1-4]
DR GeneID; 56853; -.
DR KEGG; hsa:56853; -.
DR MANE-Select; ENST00000420428.7; ENSP00000410584.2; NM_020180.4; NP_064565.1.
DR UCSC; uc002lae.3; human. [Q9BZC1-1]
DR CTD; 56853; -.
DR DisGeNET; 56853; -.
DR GeneCards; CELF4; -.
DR HGNC; HGNC:14015; CELF4.
DR HPA; ENSG00000101489; Tissue enriched (brain).
DR MIM; 612679; gene.
DR neXtProt; NX_Q9BZC1; -.
DR OpenTargets; ENSG00000101489; -.
DR PharmGKB; PA25428; -.
DR VEuPathDB; HostDB:ENSG00000101489; -.
DR eggNOG; KOG0146; Eukaryota.
DR GeneTree; ENSGT00940000158673; -.
DR HOGENOM; CLU_015367_0_1_1; -.
DR InParanoid; Q9BZC1; -.
DR OMA; LMQMFIP; -.
DR OrthoDB; 1209165at2759; -.
DR PhylomeDB; Q9BZC1; -.
DR TreeFam; TF314924; -.
DR PathwayCommons; Q9BZC1; -.
DR SignaLink; Q9BZC1; -.
DR SIGNOR; Q9BZC1; -.
DR BioGRID-ORCS; 56853; 9 hits in 1068 CRISPR screens.
DR ChiTaRS; CELF4; human.
DR EvolutionaryTrace; Q9BZC1; -.
DR GeneWiki; BRUNOL4; -.
DR GenomeRNAi; 56853; -.
DR Pharos; Q9BZC1; Tbio.
DR PRO; PR:Q9BZC1; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9BZC1; protein.
DR Bgee; ENSG00000101489; Expressed in cerebellar cortex and 124 other tissues.
DR ExpressionAtlas; Q9BZC1; baseline and differential.
DR Genevisible; Q9BZC1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0042835; F:BRE binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; NAS:UniProtKB.
DR GO; GO:0036002; F:pre-mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IDA:MGI.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; NAS:UniProtKB.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0007281; P:germ cell development; NAS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006376; P:mRNA splice site selection; IBA:GO_Central.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:1902866; P:regulation of retina development in camera-type eye; IEA:Ensembl.
DR CDD; cd12632; RRM1_CELF3_4_5_6; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR034648; CELF3/4/5/6_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cytoplasm; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..486
FT /note="CUGBP Elav-like family member 4"
FT /id="PRO_0000295221"
FT DOMAIN 54..135
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 152..232
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 404..479
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..298
FT /note="Sufficient for RNA-binding and MSE-dependent
FT splicing activity"
FT REGION 18..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..258
FT /note="Necessary for TNNT2 exon 5 inclusion"
FT VAR_SEQ 140..150
FT /note="GSSCLRQPPSQ -> E (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10893231,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_026828"
FT VAR_SEQ 150..151
FT /note="QD -> H (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_026829"
FT VAR_SEQ 268
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_026830"
FT VAR_SEQ 388..389
FT /note="GP -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026831"
FT VAR_SEQ 417..444
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10893231,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_026832"
FT VARIANT 388
FT /note="G -> S (in dbSNP:rs12458669)"
FT /id="VAR_052203"
FT CONFLICT 60
FT /note="Q -> R (in Ref. 2; BAC11082)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="D -> E (in Ref. 2; BAC11082)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="S -> G (in Ref. 2; BAC11082)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="T -> M (in Ref. 2; BAC11082)"
FT /evidence="ECO:0000305"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:2DGP"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:2DGP"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2DGP"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2DGP"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:2DGP"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:2DGP"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2DGP"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:2DGP"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:2DNK"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:2DNK"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:2DNK"
FT STRAND 189..201
FT /evidence="ECO:0007829|PDB:2DNK"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:2DNK"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:2DNK"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:2DNK"
SQ SEQUENCE 486 AA; 51966 MW; 17EA8A6A6752C565 CRC64;
MYIKMATLAN GQADNASLST NGLGSSPGSA GHMNGLSHSP GNPSTIPMKD HDAIKLFIGQ
IPRNLDEKDL KPLFEEFGKI YELTVLKDRF TGMHKGCAFL TYCERESALK AQSALHEQKT
LPGMNRPIQV KPADSESRGG SSCLRQPPSQ DRKLFVGMLN KQQSEDDVRR LFEAFGNIEE
CTILRGPDGN SKGCAFVKYS SHAEAQAAIN ALHGSQTMPG ASSSLVVKFA DTDKERTMRR
MQQMAGQMGM FNPMAIPFGA YGAYAQALMQ QQAALMASVA QGGYLNPMAA FAAAQMQQMA
ALNMNGLAAA PMTPTSGGST PPGITAPAVP SIPSPIGVNG FTGLPPQANG QPAAEAVFAN
GIHPYPAQSP TAADPLQQAY AGVQQYAGPA AYPAAYGQIS QAFPQPPPMI PQQQREGPEG
CNLFIYHLPQ EFGDAELMQM FLPFGFVSFD NPASAQTAIQ AMNGFQIGMK RLKVQLKRPK
DANRPY
