IKBZ_MOUSE
ID IKBZ_MOUSE Reviewed; 728 AA.
AC Q9EST8; Q3TVL7; Q3TWK9; Q3U8Y9; Q3UCI2; Q3URP0; Q3UW99; Q5NT97; Q99NA4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=NF-kappa-B inhibitor zeta;
DE AltName: Full=I-kappa-B-zeta;
DE Short=IkB-zeta;
DE Short=IkappaBzeta;
DE AltName: Full=IL-1 inducible nuclear ankyrin-repeat protein;
DE Short=INAP;
DE AltName: Full=Molecule possessing ankyrin repeats induced by lipopolysaccharide {ECO:0000303|PubMed:11086164};
DE Short=MAIL {ECO:0000303|PubMed:11086164};
GN Name=Nfkbiz; Synonyms=Inap, Mail {ECO:0000303|PubMed:11086164};
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=11086164; DOI=10.1016/s0014-5793(00)02185-2;
RA Kitamura H., Kanehira K., Okita K., Morimatsu M., Saito M.;
RT "MAIL, a novel nuclear I kappa B protein that potentiates LPS-induced IL-6
RT production.";
RL FEBS Lett. 485:53-56(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvEvTacfBr; TISSUE=Spleen;
RX PubMed=11797098; DOI=10.1007/s00251-001-0376-x;
RA Shiina T., Morimatsu M., Kitamura H., Ito T., Kidou S., Matsubara K.,
RA Matsuda Y., Saito M., Syuto B.;
RT "Genomic organization, chromosomal localization, and promoter analysis of
RT the mouse Mail gene.";
RL Immunogenetics 53:649-655(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=11278262; DOI=10.1074/jbc.c100075200;
RA Haruta H., Kato A., Todokoro K.;
RT "Isolation of a novel interleukin-1-inducible nuclear protein bearing
RT ankyrin-repeat motifs.";
RL J. Biol. Chem. 276:12485-12488(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN NF-KAPPA-B INHIBITION,
RP INTERACTION WITH NFKB1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=11356851; DOI=10.1074/jbc.m103426200;
RA Yamazaki S., Muta T., Takeshige K.;
RT "A novel IkappaB protein, IkappaB-zeta, induced by proinflammatory stimuli,
RT negatively regulates nuclear factor-kappaB in the nuclei.";
RL J. Biol. Chem. 276:27657-27662(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Cecum;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NMRI; TISSUE=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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 195-450 (ISOFORM 3), ALTERNATIVE SPLICING,
RP FUNCTION IN NF-KAPPA-B ACTIVATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-163; ARG-164 AND LYS-177.
RX PubMed=15618216; DOI=10.1074/jbc.m412738200;
RA Motoyama M., Yamazaki S., Eto-Kimura A., Takeshige K., Muta T.;
RT "Positive and negative regulation of nuclear factor-kappaB-mediated
RT transcription by IkappaB-zeta, an inducible nuclear protein.";
RL J. Biol. Chem. 280:7444-7451(2005).
RN [8]
RP FUNCTION IN NF-KAPPA-B ACTIVATION, DISRUPTION PHENOTYPE, INTERACTION WITH
RP NFKB1, AND INDUCTION.
RX PubMed=15241416; DOI=10.1038/nature02738;
RA Yamamoto M., Yamazaki S., Uematsu S., Sato S., Hemmi H., Hoshino K.,
RA Kaisho T., Kuwata H., Takeuchi O., Takeshige K., Saitoh T., Yamaoka S.,
RA Yamamoto N., Yamamoto S., Muta T., Takeda K., Akira S.;
RT "Regulation of Toll/IL-1-receptor-mediated gene expression by the inducible
RT nuclear protein IkappaBzeta.";
RL Nature 430:218-222(2004).
RN [9]
RP FUNCTION IN NF-KAPPA-B ACTIVATION.
RX PubMed=17447895; DOI=10.1042/bj20061797;
RA Matsuo S., Yamazaki S., Takeshige K., Muta T.;
RT "Crucial roles of binding sites for NF-kappaB and C/EBPs in IkappaB-zeta-
RT mediated transcriptional activation.";
RL Biochem. J. 405:605-615(2007).
RN [10]
RP FUNCTION.
RX PubMed=25282160; DOI=10.1038/ni.3008;
RA Jeltsch K.M., Hu D., Brenner S., Zoeller J., Heinz G.A., Nagel D.,
RA Vogel K.U., Rehage N., Warth S.C., Edelmann S.L., Gloury R., Martin N.,
RA Lohs C., Lech M., Stehklein J.E., Geerlof A., Kremmer E., Weber A.,
RA Anders H.J., Schmitz I., Schmidt-Supprian M., Fu M., Holtmann H.,
RA Krappmann D., Ruland J., Kallies A., Heikenwalder M., Heissmeyer V.;
RT "Cleavage of roquin and regnase-1 by the paracaspase MALT1 releases their
RT cooperatively repressed targets to promote T(H)17 differentiation.";
RL Nat. Immunol. 15:1079-1089(2014).
RN [11]
RP FUNCTION, AND INTERACTION WITH AKIRIN2.
RX PubMed=25107474; DOI=10.15252/embj.201488447;
RA Tartey S., Matsushita K., Vandenbon A., Ori D., Imamura T., Mino T.,
RA Standley D.M., Hoffmann J.A., Reichhart J.M., Akira S., Takeuchi O.;
RT "Akirin2 is critical for inducing inflammatory genes by bridging IkappaB-
RT zeta and the SWI/SNF complex.";
RL EMBO J. 33:2332-2348(2014).
CC -!- FUNCTION: Involved in regulation of NF-kappa-B transcription factor
CC complexes (PubMed:11356851, PubMed:15241416, PubMed:15618216,
CC PubMed:17447895). Inhibits NF-kappa-B activity without affecting its
CC nuclear translocation upon stimulation (PubMed:11356851,
CC PubMed:15241416, PubMed:15618216, PubMed:17447895). Inhibits DNA-
CC binding of RELA and NFKB1/p50, and of the NF-kappa-B p65-p50
CC heterodimer and the NF-kappa-B p50-p50 homodimer (PubMed:11356851,
CC PubMed:15241416, PubMed:15618216, PubMed:17447895). Seems also to
CC activate NF-kappa-B-mediated transcription (PubMed:11356851,
CC PubMed:15241416, PubMed:15618216, PubMed:17447895). In vitro, upon
CC association with NFKB1/p50 has transcriptional activation activity and,
CC together with NFKB1/p50 and RELA, is recruited to LCN2 promoters (By
CC similarity). Promotes transcription of LCN2 and DEFB4 (By similarity).
CC Is recruited to IL-6 promoters and activates IL-6 but decreases TNF-
CC alpha production in response to LPS (PubMed:11086164, PubMed:25107474).
CC Seems to be involved in the induction of inflammatory genes activated
CC through TLR/IL-1 receptor signaling (PubMed:11086164, PubMed:25107474).
CC Involved in the induction of T helper 17 cells (Th17) differentiation
CC upon recognition of antigen by T cell antigen receptor (TCR)
CC (PubMed:25282160). {ECO:0000250|UniProtKB:Q9BYH8,
CC ECO:0000269|PubMed:11086164, ECO:0000269|PubMed:11356851,
CC ECO:0000269|PubMed:15241416, ECO:0000269|PubMed:15618216,
CC ECO:0000269|PubMed:17447895, ECO:0000269|PubMed:25107474,
CC ECO:0000269|PubMed:25282160}.
CC -!- SUBUNIT: Interacts with NFKB1/p50 (PubMed:11356851). Interacts with
CC RELA (By similarity). Interacts with AKIRIN2 (PubMed:25107474).
CC {ECO:0000250|UniProtKB:Q9BYH8, ECO:0000269|PubMed:11356851,
CC ECO:0000269|PubMed:25107474}.
CC -!- INTERACTION:
CC Q9EST8; B1AXD8: Akirin2; NbExp=3; IntAct=EBI-10107924, EBI-10107866;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11086164,
CC ECO:0000269|PubMed:11278262, ECO:0000269|PubMed:11356851,
CC ECO:0000269|PubMed:15618216}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=MAIL-L;
CC IsoId=Q9EST8-1; Sequence=Displayed;
CC Name=2; Synonyms=MAIL-S;
CC IsoId=Q9EST8-2; Sequence=VSP_032024;
CC Name=3; Synonyms=D;
CC IsoId=Q9EST8-3; Sequence=VSP_032025;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, liver, lung and heart.
CC Expressed at very low levels in skeletal muscle, spleen and brain.
CC {ECO:0000269|PubMed:11356851}.
CC -!- INDUCTION: By IL-1, LPS, peptidoglycan, bacterial lipoprotein,
CC flagellin, MALP-2, R-848 and CpG DNA, but not by TNF-alpha.
CC {ECO:0000269|PubMed:11086164, ECO:0000269|PubMed:11278262,
CC ECO:0000269|PubMed:11356851, ECO:0000269|PubMed:15241416}.
CC -!- DISRUPTION PHENOTYPE: Mice have splenocytes with defective
CC proliferation in response to LPS but not to anti-CD40, IL-4 and anti-
CC IgM. Though mice grew normally after birth, some of them started to
CC develop atopic dermatitis-like skin lesions with acanthosis and
CC lichenoid changes at the age of 4-5 weeks. All mice developed the
CC disease by the age of 10 weeks. 5-week-old mice show pathological
CC changes in the conjunctiva, including a heavy lymphocyte infiltration
CC into the submucosa and loss of goblet cells in the conjunctival
CC epithelium. {ECO:0000269|PubMed:15241416}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE24648.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB020974; BAB18302.1; -; mRNA.
DR EMBL; AB040458; BAB85809.1; -; Genomic_DNA.
DR EMBL; AB026551; BAA95161.2; -; mRNA.
DR EMBL; AB047549; BAB32782.1; -; mRNA.
DR EMBL; AK082908; BAC38681.1; -; mRNA.
DR EMBL; AK136509; BAE23017.1; -; mRNA.
DR EMBL; AK141318; BAE24648.1; ALT_FRAME; mRNA.
DR EMBL; AK150519; BAE29631.1; -; mRNA.
DR EMBL; AK152016; BAE30878.1; -; mRNA.
DR EMBL; AK159093; BAE34809.1; -; mRNA.
DR EMBL; AK159171; BAE34871.1; -; mRNA.
DR EMBL; AK159459; BAE35101.1; -; mRNA.
DR EMBL; AK159645; BAE35257.1; -; mRNA.
DR EMBL; AK159917; BAE35480.1; -; mRNA.
DR EMBL; AK160065; BAE35601.1; -; mRNA.
DR EMBL; BC058188; AAH58188.1; -; mRNA.
DR EMBL; AB196497; BAD82955.1; -; mRNA.
DR CCDS; CCDS28216.1; -. [Q9EST8-1]
DR CCDS; CCDS49869.1; -. [Q9EST8-2]
DR RefSeq; NP_001152866.1; NM_001159394.1. [Q9EST8-1]
DR RefSeq; NP_001152867.1; NM_001159395.1. [Q9EST8-2]
DR RefSeq; NP_085115.1; NM_030612.3. [Q9EST8-1]
DR AlphaFoldDB; Q9EST8; -.
DR SMR; Q9EST8; -.
DR BioGRID; 219820; 7.
DR IntAct; Q9EST8; 6.
DR MINT; Q9EST8; -.
DR STRING; 10090.ENSMUSP00000110102; -.
DR iPTMnet; Q9EST8; -.
DR PhosphoSitePlus; Q9EST8; -.
DR EPD; Q9EST8; -.
DR MaxQB; Q9EST8; -.
DR PaxDb; Q9EST8; -.
DR PRIDE; Q9EST8; -.
DR ProteomicsDB; 267223; -. [Q9EST8-1]
DR ProteomicsDB; 267224; -. [Q9EST8-2]
DR ProteomicsDB; 267225; -. [Q9EST8-3]
DR Antibodypedia; 2134; 202 antibodies from 25 providers.
DR DNASU; 80859; -.
DR Ensembl; ENSMUST00000036273; ENSMUSP00000041173; ENSMUSG00000035356. [Q9EST8-1]
DR Ensembl; ENSMUST00000096026; ENSMUSP00000093726; ENSMUSG00000035356. [Q9EST8-2]
DR Ensembl; ENSMUST00000114457; ENSMUSP00000110101; ENSMUSG00000035356. [Q9EST8-2]
DR Ensembl; ENSMUST00000114458; ENSMUSP00000110102; ENSMUSG00000035356. [Q9EST8-1]
DR GeneID; 80859; -.
DR KEGG; mmu:80859; -.
DR UCSC; uc007zlm.2; mouse. [Q9EST8-1]
DR CTD; 64332; -.
DR MGI; MGI:1931595; Nfkbiz.
DR VEuPathDB; HostDB:ENSMUSG00000035356; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000153695; -.
DR HOGENOM; CLU_030240_0_0_1; -.
DR InParanoid; Q9EST8; -.
DR OMA; LQRNQQH; -.
DR OrthoDB; 867160at2759; -.
DR PhylomeDB; Q9EST8; -.
DR TreeFam; TF330224; -.
DR BioGRID-ORCS; 80859; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Nfkbiz; mouse.
DR PRO; PR:Q9EST8; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9EST8; protein.
DR Bgee; ENSMUSG00000035356; Expressed in granulocyte and 234 other tissues.
DR Genevisible; Q9EST8; MM.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0006954; P:inflammatory response; IDA:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
DR GO; GO:2000321; P:positive regulation of T-helper 17 cell differentiation; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; ANK repeat; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..728
FT /note="NF-kappa-B inhibitor zeta"
FT /id="PRO_0000323578"
FT REPEAT 453..482
FT /note="ANK 1"
FT REPEAT 489..518
FT /note="ANK 2"
FT REPEAT 522..551
FT /note="ANK 3"
FT REPEAT 561..589
FT /note="ANK 4"
FT REPEAT 591..617
FT /note="ANK 5"
FT REPEAT 622..651
FT /note="ANK 6"
FT REPEAT 658..691
FT /note="ANK 7"
FT REGION 45..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..403
FT /note="Required for transcriptional activity"
FT REGION 414..728
FT /note="Interaction with NFKB1/p50"
FT MOTIF 163..178
FT /note="Nuclear localization signal"
FT COMPBIAS 59..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..99
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11356851"
FT /id="VSP_032024"
FT VAR_SEQ 236..429
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15618216"
FT /id="VSP_032025"
FT MUTAGEN 163
FT /note="K->A: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:15618216"
FT MUTAGEN 164
FT /note="R->A: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:15618216"
FT MUTAGEN 177
FT /note="K->A: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:15618216"
FT CONFLICT 31
FT /note="N -> K (in Ref. 5; BAE30878)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="G -> D (in Ref. 5; BAE35257/BAE34809)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="K -> E (in Ref. 5; BAE35257/BAE34809)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="K -> E (in Ref. 5; BAE29631)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="K -> R (in Ref. 5; BAE35601)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="M -> I (in Ref. 3; BAE24648)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="S -> G (in Ref. 5; BAE29631)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="A -> V (in Ref. 5; BAE35257/BAE34809)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="R -> K (in Ref. 5; BAE35257/BAE34809)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="S -> G (in Ref. 3; BAE23017)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 728 AA; 79007 MW; E2CAB725295A08B7 CRC64;
MIVDKLLDDS RGGEGLLDAA GDCGLMTSPL NLAYFYGASP PSAPGAGDTG YLSAVPSAPG
SPGSDSSDFS STSSVSSCGA VESRPRGGAR AERPQVEPHM GVGRQQRGPF QGVRVKNSVK
ELLLHIRSNK QKASGQPVDE FKTQSVNIEQ LTDLKSAVSA VGKRKGPDPL SDGPVCKRPA
LLPSHFVTSP QTPTPGESME DVRHSESKLD SSAALLQNII NIKNECNPVS LNTVQVSWMS
PTVPQNSPRD QCQDFHGGQA FSPPQKYQPF QVSGSPQMMD QASMYQYSPQ TQNMQQPPPL
PPQQQHQQNY PHNSPLQFSP YSRMSQSPKY DSNLFDTHEP QFCTGQSFVS LLTGPGEPES
LAVPVPAPTS IPPQTETQLQ TFSLMPSNAC EAVVGVHDVG SHSLGTSLSL QNIMGSPMNT
TQLGKSFFQW QVEQEESKLA NIPQDQFLAR DGDGDTFLHI AVAQGRRALS YVLARKMNAL
HMLDIKEHNG QSAFQVAVAA NQHLIVQDLV NLGAQVNTTD CWGRTPLHVC AEKGHSQVLQ
AIQKGAVRSN QFVDLEATNY DGLTPLHCAV VAHNAVVHEL QRNRQSHSPE VQDLLLRNKS
LVDTIKCLIQ MGAAVEAKDR KSGRTALHLA AEEANLELIR LFLELPSCLS FVNAKAYNGN
TALHVAASLQ YRVTQLDAVR LLMRKGADPS TRNLENEQPV HLVPDGPVGE QIRRILKGKS
IQQRAPPY
