FNBP4_MOUSE
ID FNBP4_MOUSE Reviewed; 1031 AA.
AC Q6ZQ03; Q3TPA6; Q8BNC8; Q9JHC1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Formin-binding protein 4;
DE AltName: Full=Formin-binding protein 30;
GN Name=Fnbp4; Synonyms=Fbp30, Kiaa1014;
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), AND INTERACTION WITH FMN1.
RC STRAIN=FVB/NJ; TISSUE=Limb bud;
RX PubMed=8605874; DOI=10.1002/j.1460-2075.1996.tb00442.x;
RA Chan D.C., Bedford M.T., Leder P.;
RT "Formin binding proteins bear WWP/WW domains that bind proline-rich
RT peptides and functionally resemble SH3 domains.";
RL EMBO J. 15:1045-1054(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INTERACTION
RP WITH WW DOMAIN-BINDING PROTEINS.
RC STRAIN=FVB/NJ; TISSUE=Embryo, Fibroblast, and Limb bud;
RX PubMed=10744724; DOI=10.1074/jbc.275.14.10359;
RA Bedford M.T., Sarbassova D., Xu J., Leder P., Yaffe M.B.;
RT "A novel pro-Arg motif recognized by WW domains.";
RL J. Biol. Chem. 275:10359-10369(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 3-1031 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Heart, and Spinal ganglion;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 61-1031 (ISOFORM 2), TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=C57BL/6J; TISSUE=Embryo, Placenta, Thymic lymphoma, and Thymus;
RX PubMed=10510470; DOI=10.1038/sj.cdd.4400564;
RA Depraetere V., Golstein P.;
RT "WW domain-containing FBP-30 is regulated by p53.";
RL Cell Death Differ. 6:883-889(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-125; SER-128;
RP SER-435; SER-440; SER-443; SER-446; SER-450 AND SER-507, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-294, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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).
CC -!- SUBUNIT: Binds FMN1. Interacts with the Arg/Gly-rich-flanked Pro-rich
CC regions of KHDRBS1/SAM68. Arginine methylation in these regions has no
CC effect on this binding (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6ZQ03-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZQ03-2; Sequence=VSP_026025, VSP_026026;
CC Name=3;
CC IsoId=Q6ZQ03-3; Sequence=VSP_029267, VSP_029268;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels in spleen and thymus.
CC {ECO:0000269|PubMed:10510470, ECO:0000269|PubMed:10744724}.
CC -!- DEVELOPMENTAL STAGE: First detected at 9 dpc.
CC -!- INDUCTION: Up-regulated by p53. {ECO:0000269|PubMed:10510470}.
CC -!- DOMAIN: These WW domains interact with Arg/Gly-rich-flanked Pro-rich
CC domains found in several WW domain-binding proteins (WBPs). The N-
CC terminal WW domain has the greater ligand-binding ability (By
CC similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF59410.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC98073.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE37831.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAM20821.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U40750; AAF59410.1; ALT_INIT; mRNA.
DR EMBL; AK129263; BAC98073.2; ALT_INIT; mRNA.
DR EMBL; AK084018; BAC39098.1; -; mRNA.
DR EMBL; AK164543; BAE37831.1; ALT_FRAME; mRNA.
DR EMBL; AL714026; CAM20821.1; ALT_INIT; Genomic_DNA.
DR PIR; S64717; S64717.
DR RefSeq; NP_061298.1; NM_018828.2.
DR AlphaFoldDB; Q6ZQ03; -.
DR BioGRID; 207734; 3.
DR ELM; Q6ZQ03; -.
DR IntAct; Q6ZQ03; 1.
DR MINT; Q6ZQ03; -.
DR STRING; 10090.ENSMUSP00000013759; -.
DR iPTMnet; Q6ZQ03; -.
DR PhosphoSitePlus; Q6ZQ03; -.
DR EPD; Q6ZQ03; -.
DR jPOST; Q6ZQ03; -.
DR MaxQB; Q6ZQ03; -.
DR PaxDb; Q6ZQ03; -.
DR PeptideAtlas; Q6ZQ03; -.
DR PRIDE; Q6ZQ03; -.
DR ProteomicsDB; 271704; -. [Q6ZQ03-1]
DR ProteomicsDB; 271705; -. [Q6ZQ03-2]
DR ProteomicsDB; 271706; -. [Q6ZQ03-3]
DR DNASU; 55935; -.
DR GeneID; 55935; -.
DR KEGG; mmu:55935; -.
DR UCSC; uc008ktb.1; mouse. [Q6ZQ03-1]
DR CTD; 23360; -.
DR MGI; MGI:1860513; Fnbp4.
DR eggNOG; ENOG502QTDD; Eukaryota.
DR InParanoid; Q6ZQ03; -.
DR OrthoDB; 472232at2759; -.
DR PhylomeDB; Q6ZQ03; -.
DR TreeFam; TF331046; -.
DR BioGRID-ORCS; 55935; 9 hits in 71 CRISPR screens.
DR ChiTaRS; Fnbp4; mouse.
DR PRO; PR:Q6ZQ03; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6ZQ03; protein.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR CDD; cd00201; WW; 2.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF51045; SSF51045; 2.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..1031
FT /note="Formin-binding protein 4"
FT /id="PRO_0000289864"
FT DOMAIN 218..252
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 603..637
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..185
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..414
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..743
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..761
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..938
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3X1"
FT MOD_RES 294
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3X1"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3X1"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3X1"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3X1"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3X1"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3X1"
FT CROSSLNK 339
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3X1"
FT CROSSLNK 352
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8N3X1"
FT CROSSLNK 352
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8N3X1"
FT CROSSLNK 527
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8N3X1"
FT CROSSLNK 527
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8N3X1"
FT VAR_SEQ 616..630
FT /note="DHRRYFYVNEQSGES -> YALFSPSYLSPLTSQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029267"
FT VAR_SEQ 616..622
FT /note="DHRRYFY -> TSGSNYS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10510470"
FT /id="VSP_026025"
FT VAR_SEQ 623..1031
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10510470"
FT /id="VSP_026026"
FT VAR_SEQ 631..1031
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029268"
FT CONFLICT 68
FT /note="S -> T (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="T -> K (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="T -> P (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="A -> T (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="P -> S (in Ref. 3; BAC98073)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="S -> T (in Ref. 3; BAC98073)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="K -> Q (in Ref. 3; BAC98073)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1031 AA; 111245 MW; AC49681858666E69 CRC64;
MMGKKSRAVP GRRPILQLSP PGPRSSTPGR DPDPDPDPEA DSTAAATSQS APAAATAAAA
TSPAVPASAA PEDSPSEDEQ EVVVEVPNVV QNPPTPVMTT RPTAVKATGG LCLLGAYADS
DDDESDVSEK TAQSKEANGN QATDIDSTLA NFLAEIDAIT APQPAAPVVA SAPPPTPPRP
EPKEAATPAL SPTASNGSDT AQTPGWHYDT QCSLAGVEIE MGDWQEVWDE NTGCYYYWNT
QTNEVTWELP QYLATQVQGL QHYQPSSVTG TEAAFVVNTD MYTKERTTAA SSSKSGPVIT
KREVKKEVNE GIQALSNSEE ERKGVAAALL APLLPEGVKE EEERWRRKVI CKEADPVSET
KETSTASEET GPSIKPPEVM MDGTEDPSQE ELCSVVQSGE SEEEEEEEEQ DTLELELALE
RKKAELRALE EGDGSVSGSS PRSDISQPAS QDGVRRIMSK RGKWKMFVRA TSPESTSRSS
SKTGRDSPEN GETAIGAEDS EKIDEISDKE TEVEESSEKI KVQLAPKVEE EQDLKFQIGE
LANTLTSKFE FLGINRQSIS NFHMLLLQTE TRIADWREGA LNGNYLKRKL QDAAEQLKQY
EINATPKGWS CHWDRDHRRY FYVNEQSGES QWEFPDGEEE EESQTKEVRD ESLPKLTVKD
KTCTDPNSTE SSENPTGSLC KESFSGQVSS SLMPLTPFWT LLQSNVPVLQ PPLPLEMPPP
PPPPPESPPP PPPPPPPPPP LEDGEIQEVE MEDEGSEEPP APGTEEDTPL KPSTQTTAVT
SQSLVDSTAS SPPSNKAVKR KAPEMSTSVV QRSATIGSSP VLYSQSAIAA GHQAVGMAHQ
AVGMAHQAVS ASHAAAAGVG HQARGMSLQS NYLGLAAAPA LMSYAECSVP IGVTTPSLQP
AQARGTMAAP AVVEPPPPPP PPPTPTPPPP PPAPKVPPPE KTRKGKKDKA KKSKTKMPSL
VKKWQSIQRE LDEEDNSSSS EEDRESTAQK RIEEWKQQQL VSGLAERNAN FEALPEDWRA
RLKRRKMAPS T
