NFIL3_MOUSE
ID NFIL3_MOUSE Reviewed; 462 AA.
AC O08750; Q3ULK2; Q497U0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Nuclear factor interleukin-3-regulated protein;
DE AltName: Full=E4 promoter-binding protein 4;
DE AltName: Full=Embryo implantation-related NFIL3/E4BP4-like transcription factor;
GN Name=Nfil3; Synonyms=E4bp4;
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], FUNCTION, INDUCTION, AND DNA-BINDING.
RX PubMed=9122243; DOI=10.1073/pnas.94.6.2609;
RA Ikushima S., Inukai T., Inaba T., Nimer S.D., Cleveland J.L., Look A.T.;
RT "Pivotal role for the NFIL3/E4BP4 transcription factor in interleukin 3-
RT mediated survival of pro-B lymphocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:2609-2614(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Embryo, and Uterus;
RA Shen Q.-X., Wang J., Huang Z.-P.;
RT "Identification of novel endometrial factors involved in the mouse embryo
RT implantation.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Egg, and Mammary tumor;
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 FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11316793; DOI=10.1101/gad.873501;
RA Mitsui S., Yamaguchi S., Matsuo T., Ishida Y., Okamura H.;
RT "Antagonistic role of E4BP4 and PAR proteins in the circadian oscillatory
RT mechanism.";
RL Genes Dev. 15:995-1006(2001).
RN [6]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=12743120; DOI=10.1074/jbc.m212652200;
RA Ozkurt I.C., Tetradis S.;
RT "Parathyroid hormone-induced E4BP4/NFIL3 down-regulates transcription in
RT osteoblasts.";
RL J. Biol. Chem. 278:26803-26809(2003).
RN [7]
RP FUNCTION, INDUCTION, AND DNA-BINDING.
RX PubMed=15087429; DOI=10.1210/en.2003-1436;
RA Ozkurt I.C., Pirih F.Q., Tetradis S.;
RT "Parathyroid hormone induces E4bp4 messenger ribonucleic acid expression
RT primarily through cyclic adenosine 3',5'-monophosphate signaling in
RT osteoblasts.";
RL Endocrinology 145:3696-3703(2004).
RN [8]
RP INTERACTION WITH PER2 AND CRY2.
RX PubMed=17274955; DOI=10.1016/j.bbrc.2007.01.084;
RA Ohno T., Onishi Y., Ishida N.;
RT "The negative transcription factor E4BP4 is associated with circadian clock
RT protein PERIOD2.";
RL Biochem. Biophys. Res. Commun. 354:1010-1015(2007).
RN [9]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=17182630; DOI=10.1093/nar/gkl868;
RA Ohno T., Onishi Y., Ishida N.;
RT "A novel E4BP4 element drives circadian expression of mPeriod2.";
RL Nucleic Acids Res. 35:648-655(2007).
RN [10]
RP IDENTIFICATION BY 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 [11]
RP FUNCTION, AND INTERACTION WITH NR1D1.
RX PubMed=29653076; DOI=10.1016/j.bcp.2018.04.005;
RA Zhao M., Zhang T., Yu F., Guo L., Wu B.;
RT "E4bp4 regulates carboxylesterase 2 enzymes through repression of the
RT nuclear receptor Rev-erbalpha in mice.";
RL Biochem. Pharmacol. 152:293-301(2018).
RN [12]
RP FUNCTION, AND INTERACTION WITH NR0B2.
RX PubMed=30555544; DOI=10.7150/thno.28676;
RA Zhang T., Yu F., Guo L., Chen M., Yuan X., Wu B.;
RT "Small heterodimer partner regulates circadian cytochromes p450 and drug-
RT induced hepatotoxicity.";
RL Theranostics 8:5246-5258(2018).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=32190943; DOI=10.1096/fj.202000121r;
RA Xu X., Zhou Y., Fu B., Zhang J., Dong Z., Zhang X., Shen N., Sun R.,
RA Tian Z., Wei H.;
RT "PBX1 promotes development of natural killer cells by binding directly to
RT the Nfil3 promoter.";
RL FASEB J. 34:6479-6492(2020).
CC -!- FUNCTION: Acts as a transcriptional regulator that recognizes and binds
CC to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many
CC cellular and viral promoters. Represses transcription from promoters
CC with activating transcription factor (ATF) sites (By similarity).
CC Represses promoter activity in osteoblasts. Represses transcriptional
CC activity of PER1. Represses transcriptional activity of PER2 via the B-
CC site on the promoter. Activates transcription from the interleukin-3
CC promoter in T-cells (By similarity). Competes for the same consensus-
CC binding site with PAR DNA-binding factors (DBP, HLF and TEF). Component
CC of the circadian clock that acts as a negative regulator for the
CC circadian expression of PER2 oscillation in the cell-autonomous core
CC clock. Protects pro-B cells from programmed cell death. Represses the
CC transcription of CYP2A5 (PubMed:30555544). Positively regulates the
CC expression and activity of CES2 by antagonizing the repressive action
CC of NR1D1 on CES2 (PubMed:29653076). Required for the development of
CC natural killer cell precursors (PubMed:32190943).
CC {ECO:0000250|UniProtKB:Q16649, ECO:0000269|PubMed:11316793,
CC ECO:0000269|PubMed:15087429, ECO:0000269|PubMed:17182630,
CC ECO:0000269|PubMed:29653076, ECO:0000269|PubMed:30555544,
CC ECO:0000269|PubMed:32190943, ECO:0000269|PubMed:9122243}.
CC -!- SUBUNIT: Homodimer (By similarity). Binds DNA as a dimer (By
CC similarity). Interacts with DR1 (By similarity). Interacts with PER2
CC and CRY2 (PubMed:17274955). Interacts with NR0B2 (PubMed:30555544).
CC Interacts with NR1D1 (PubMed:29653076). Interacts with MYSM1 (By
CC similarity). {ECO:0000250|UniProtKB:Q16649,
CC ECO:0000269|PubMed:17274955, ECO:0000269|PubMed:29653076,
CC ECO:0000269|PubMed:30555544}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:11316793}.
CC -!- TISSUE SPECIFICITY: Expressed in suprachiasmatic nucleus and liver (at
CC protein level). Expressed in suprachiasmatic nucleus, hippocampus,
CC gyrus dentatus, piriform cortex, internal granular layer of olfactory
CC bulb, dorsomedial hypothalamic nucleus, pontine nuclei, granular layer
CC of cerebellum, liver and calvariae osteoblasts. Expressed in natural
CC killer cell precursors in bone marrow (PubMed:32190943).
CC {ECO:0000269|PubMed:11316793, ECO:0000269|PubMed:12743120,
CC ECO:0000269|PubMed:32190943}.
CC -!- INDUCTION: Expression is regulated by circadian rhythms. Up-regulated
CC by parathyroid hormone (PTH) (at protein level). Up-regulated by IL-3,
CC forskolin, 8-bromo-cAMP, phorbol myristate acetate and PTH in primary
CC osteoblasts and calvariae. {ECO:0000269|PubMed:12743120,
CC ECO:0000269|PubMed:15087429, ECO:0000269|PubMed:9122243}.
CC -!- DISRUPTION PHENOTYPE: Reduced number of natural killer cell-committed
CC progenitors in bone marrow. {ECO:0000269|PubMed:32190943}.
CC -!- SIMILARITY: Belongs to the bZIP family. NFIL3 subfamily. {ECO:0000305}.
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DR EMBL; U83148; AAB53973.1; -; Genomic_DNA.
DR EMBL; AY061760; AAL29942.1; -; mRNA.
DR EMBL; AK145451; BAE26446.1; -; mRNA.
DR EMBL; BC031377; AAH31377.1; -; mRNA.
DR EMBL; BC100384; AAI00385.1; -; mRNA.
DR CCDS; CCDS26519.1; -.
DR RefSeq; NP_059069.1; NM_017373.3.
DR RefSeq; XP_006516940.1; XM_006516877.2.
DR RefSeq; XP_011242681.1; XM_011244379.1.
DR RefSeq; XP_017170907.1; XM_017315418.1.
DR AlphaFoldDB; O08750; -.
DR SMR; O08750; -.
DR BioGRID; 201749; 1.
DR IntAct; O08750; 1.
DR MINT; O08750; -.
DR STRING; 10090.ENSMUSP00000065363; -.
DR iPTMnet; O08750; -.
DR PhosphoSitePlus; O08750; -.
DR EPD; O08750; -.
DR jPOST; O08750; -.
DR MaxQB; O08750; -.
DR PaxDb; O08750; -.
DR PeptideAtlas; O08750; -.
DR PRIDE; O08750; -.
DR ProteomicsDB; 293550; -.
DR Antibodypedia; 926; 383 antibodies from 39 providers.
DR DNASU; 18030; -.
DR Ensembl; ENSMUST00000071065; ENSMUSP00000065363; ENSMUSG00000056749.
DR GeneID; 18030; -.
DR KEGG; mmu:18030; -.
DR UCSC; uc007qnh.1; mouse.
DR CTD; 4783; -.
DR MGI; MGI:109495; Nfil3.
DR VEuPathDB; HostDB:ENSMUSG00000056749; -.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000160540; -.
DR HOGENOM; CLU_052045_0_0_1; -.
DR InParanoid; O08750; -.
DR OMA; KNVHATV; -.
DR OrthoDB; 1450431at2759; -.
DR PhylomeDB; O08750; -.
DR TreeFam; TF328374; -.
DR BioGRID-ORCS; 18030; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Nfil3; mouse.
DR PRO; PR:O08750; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; O08750; protein.
DR Bgee; ENSMUSG00000056749; Expressed in hindlimb stylopod muscle and 212 other tissues.
DR Genevisible; O08750; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
DR GO; GO:0007623; P:circadian rhythm; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0001779; P:natural killer cell differentiation; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR016743; NFIL3/E4BP4.
DR InterPro; IPR010533; Vert_IL3-reg_TF.
DR PANTHER; PTHR15284:SF1; PTHR15284:SF1; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR Pfam; PF06529; Vert_IL3-reg_TF; 1.
DR PIRSF; PIRSF019029; bZIP_E4BP4; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; Biological rhythms; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..462
FT /note="Nuclear factor interleukin-3-regulated protein"
FT /id="PRO_0000292668"
FT DOMAIN 73..136
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..95
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 99..106
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 188..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..420
FT /note="Necessary for transcriptional repression and
FT sufficient for interaction with PER2"
FT /evidence="ECO:0000269|PubMed:17274955"
FT COMPBIAS 188..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 314
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 326
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 332
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 360
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 394
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 401
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 412
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 434
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 448
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CONFLICT 101
FT /note="L -> F (in Ref. 3; BAE26446)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="L -> F (in Ref. 4; AAI00385)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="D -> G (in Ref. 4; AAI00385)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="F -> V (in Ref. 3; BAE26446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 50943 MW; DC711EB4CAC0112E CRC64;
MQLRKMQTIK KEPAPLDPTS SSDKMLLLNS ALAEVAEDLA SGEDLLLNEG SMGKNKSSAC
RRKREFIPDE KKDAMYWEKR RKNNEAAKRS REKRRLNDLV LENKLIALGE ENATLKAELL
SLKLKFGLIS STAYAQEIQK LSNSTAVYFQ DYQTSKAAVS SFVDEHEPAM VAGSCISVIK
HSPQSSLSDV SEVSSVEHTQ ESPAQGGCRS PENKFPVIKQ EPVELESFAR EAREERGTYS
TSIYQSYMGS SFSTYSHSPP LLQVHGSTSN SPRTSEADEG VVGKSSDGED EQQVPKGPIH
SPVELQRVHA TVVKVPEVNP SALPHKLRIK AKAMQVKVEA LDSEFEGMQK LSSPADAIAK
RHFDLEKHGT SGMAHSSLPP FSVQVTNIQD WSLKSEHWHH KELSSKTQSS FKTGVVEVKD
GGYKVSEAEN LYLKQGIANL SAEVVSLKRF IATQPISASD SR
