ID   ZEB1_MOUSE              Reviewed;        1117 AA.
AC   Q64318; A4QPD2; Q62519;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=Zinc finger E-box-binding homeobox 1 {ECO:0000312|MGI:MGI:1344313};
DE   AltName: Full=Delta EF1 {ECO:0000303|PubMed:8964504};
DE   AltName: Full=Transcription factor 8 {ECO:0000250|UniProtKB:P37275};
DE            Short=TCF-8 {ECO:0000250|UniProtKB:P37275};
DE   AltName: Full=Zinc finger homeobox protein 1a;
DE            Short=MEB1 {ECO:0000303|PubMed:8647466};
GN   Name=Zeb1 {ECO:0000312|MGI:MGI:1344313};
GN   Synonyms=Areb6 {ECO:0000312|MGI:MGI:1344313}, Tcf8
GN   {ECO:0000312|MGI:MGI:1344313}, Zfhx1a {ECO:0000312|MGI:MGI:1344313},
GN   Zfx1a {ECO:0000312|MGI:MGI:1344313}, Zfx1ha;
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].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=8964504; DOI=10.1016/0378-1119(96)00185-0;
RA   Sekido R., Takagi T., Okanami M., Moribe H., Yamamura M., Higashi Y.,
RA   Kondoh H.;
RT   "Organization of the gene encoding transcriptional repressor deltaEF1 and
RT   cross-species conservation of its domains.";
RL   Gene 173:227-232(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Spleen;
RA   Wu Y., Montoya G.D., Rubin S.E., Brodie S.G., Jenkins N., Williams T.M.;
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Brain;
RX   PubMed=8647466; DOI=10.1016/0378-1119(95)00824-1;
RA   Genetta T., Kadesch T.;
RT   "Cloning of a cDNA encoding a mouse transcriptional repressor displaying
RT   striking sequence conservation across vertebrates.";
RL   Gene 169:289-290(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
RX   PubMed=19935649; DOI=10.1038/ncb1998;
RA   Wellner U., Schubert J., Burk U.C., Schmalhofer O., Zhu F., Sonntag A.,
RA   Waldvogel B., Vannier C., Darling D., zur Hausen A., Brunton V.G.,
RA   Morton J., Sansom O., Schuler J., Stemmler M.P., Herzberger C., Hopt U.,
RA   Keck T., Brabletz S., Brabletz T.;
RT   "The EMT-activator ZEB1 promotes tumorigenicity by repressing stemness-
RT   inhibiting microRNAs.";
RL   Nat. Cell Biol. 11:1487-1495(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-302; SER-657;
RP   SER-664; SER-671; SER-678 AND SER-682, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   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   [7]
RP   FUNCTION.
RX   PubMed=20713358; DOI=10.1074/jbc.m110.165027;
RA   Kato M., Wang L., Putta S., Wang M., Yuan H., Sun G., Lanting L.,
RA   Todorov I., Rossi J.J., Natarajan R.;
RT   "Post-transcriptional up-regulation of Tsc-22 by Ybx1, a target of miR-
RT   216a, mediates TGF-{beta}-induced collagen expression in kidney cells.";
RL   J. Biol. Chem. 285:34004-34015(2010).
RN   [8]
RP   FUNCTION, DNA-BINDING, INDUCTION BY NEUROGENESIS, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=20346398; DOI=10.1016/j.mcn.2010.03.006;
RA   Ravanpay A.C., Hansen S.J., Olson J.M.;
RT   "Transcriptional inhibition of REST by NeuroD2 during neuronal
RT   differentiation.";
RL   Mol. Cell. Neurosci. 44:178-189(2010).
CC   -!- FUNCTION: Acts as a transcriptional repressor. Binds to E-box sequences
CC       in the immunoglobulin heavy chain enhancer as well as in the regulatory
CC       regions of many other tissue-specific genes. Represses E-cadherin
CC       promoter and induces an epithelial-mesenchymal transition (EMT) by
CC       recruiting SMARCA4/BRG1. Represses BCL6 transcription in the presence
CC       of the corepressor CTBP1 (By similarity). Positively regulates neuronal
CC       differentiation. Represses RCOR1 transcription activation during
CC       neurogenesis. Represses transcription by binding to the E box (5'-
CC       CANNTG-3'). In the absence of TGFB1, acts as a repressor of COL1A2
CC       transcription via binding to the E-box in the upstream enhancer region
CC       (PubMed:20713358). Promotes tumorigenicity by repressing stemness-
CC       inhibiting microRNAs (PubMed:19935649). {ECO:0000250,
CC       ECO:0000269|PubMed:19935649, ECO:0000269|PubMed:20346398,
CC       ECO:0000269|PubMed:20713358}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with SMARCA4/BRG1.
CC       {ECO:0000250|UniProtKB:P37275}.
CC   -!- INTERACTION:
CC       Q64318; O88712: Ctbp1; NbExp=5; IntAct=EBI-8560245, EBI-604547;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20346398}.
CC   -!- TISSUE SPECIFICITY: Expressed in the external germinal layer (EGL) and
CC       internal granular layer (IGL) of the cerebellum (at protein level).
CC       {ECO:0000269|PubMed:20346398}.
CC   -!- INDUCTION: Induced during Neurod2-induced neurogenesis.
CC       {ECO:0000269|PubMed:20346398}.
CC   -!- SIMILARITY: Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger
CC       family. {ECO:0000305}.
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DR   EMBL; U26259; AAA67564.1; -; mRNA.
DR   EMBL; D76432; BAA11177.1; -; mRNA.
DR   EMBL; L48363; AAB08442.1; -; Genomic_DNA.
DR   EMBL; BC139769; AAI39770.1; -; mRNA.
DR   CCDS; CCDS29039.1; -.
DR   PIR; JC4934; JC4934.
DR   RefSeq; NP_035676.1; NM_011546.3.
DR   AlphaFoldDB; Q64318; -.
DR   BioGRID; 204010; 21.
DR   DIP; DIP-60280N; -.
DR   IntAct; Q64318; 4.
DR   MINT; Q64318; -.
DR   STRING; 10090.ENSMUSP00000025081; -.
DR   iPTMnet; Q64318; -.
DR   PhosphoSitePlus; Q64318; -.
DR   EPD; Q64318; -.
DR   jPOST; Q64318; -.
DR   MaxQB; Q64318; -.
DR   PaxDb; 10090-ENSMUSP00000025081; -.
DR   ProteomicsDB; 302055; -.
DR   Pumba; Q64318; -.
DR   Antibodypedia; 12930; 887 antibodies from 45 providers.
DR   DNASU; 21417; -.
DR   Ensembl; ENSMUST00000025081.13; ENSMUSP00000025081.6; ENSMUSG00000024238.16.
DR   GeneID; 21417; -.
DR   KEGG; mmu:21417; -.
DR   UCSC; uc008dyy.2; mouse.
DR   AGR; MGI:1344313; -.
DR   CTD; 6935; -.
DR   MGI; MGI:1344313; Zeb1.
DR   VEuPathDB; HostDB:ENSMUSG00000024238; -.
DR   eggNOG; KOG3623; Eukaryota.
DR   GeneTree; ENSGT00950000183208; -.
DR   HOGENOM; CLU_005890_0_1_1; -.
DR   InParanoid; Q64318; -.
DR   OMA; ANYINFP; -.
DR   OrthoDB; 4266655at2759; -.
DR   PhylomeDB; Q64318; -.
DR   TreeFam; TF331759; -.
DR   BioGRID-ORCS; 21417; 4 hits in 77 CRISPR screens.
DR   ChiTaRS; Zeb1; mouse.
DR   PRO; PR:Q64318; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q64318; Protein.
DR   Bgee; ENSMUSG00000024238; Expressed in meninx of diencephalon and 273 other cell types or tissues.
DR   ExpressionAtlas; Q64318; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:MGI.
DR   GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0048513; P:animal organ development; IMP:MGI.
DR   GO; GO:0051216; P:cartilage development; IMP:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR   GO; GO:0007417; P:central nervous system development; IGI:MGI.
DR   GO; GO:0090103; P:cochlea morphogenesis; IMP:MGI.
DR   GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:MGI.
DR   GO; GO:0048598; P:embryonic morphogenesis; IGI:MGI.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR   GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR   GO; GO:0043616; P:keratinocyte proliferation; IMP:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0045602; P:negative regulation of endothelial cell differentiation; ISO:MGI.
DR   GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IMP:MGI.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0010464; P:regulation of mesenchymal cell proliferation; IMP:MGI.
DR   GO; GO:0051150; P:regulation of smooth muscle cell differentiation; IMP:MGI.
DR   GO; GO:0033081; P:regulation of T cell differentiation in thymus; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IGI:MGI.
DR   GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR   GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR   GO; GO:0048752; P:semicircular canal morphogenesis; IMP:MGI.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 6.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   InterPro; IPR008598; Di19_Zn-bd.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24391; HISTONE H4 TRANSCRIPTION FACTOR-RELATED; 1.
DR   PANTHER; PTHR24391:SF18; ZINC FINGER PROTEIN 1; 1.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   Pfam; PF05605; zf-Di19; 1.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
DR   Genevisible; Q64318; MM.
PE   1: Evidence at protein level;
KW   Activator; Differentiation; DNA-binding; Homeobox; Isopeptide bond;
KW   Metal-binding; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..1117
FT                   /note="Zinc finger E-box-binding homeobox 1"
FT                   /id="PRO_0000047233"
FT   ZN_FING         150..173
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         180..202
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         220..242
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         248..272
FT                   /note="C2H2-type 4; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   DNA_BIND        559..618
FT                   /note="Homeobox; atypical"
FT   ZN_FING         882..904
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         910..932
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         938..959
FT                   /note="C2H2-type 7; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          834..876
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          991..1117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..546
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..687
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1009..1032
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1067
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1096..1117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62947"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62947"
FT   MOD_RES         293
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         657
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         664
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         671
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         678
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         680
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P37275"
FT   MOD_RES         682
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        166
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P37275"
FT   CROSSLNK        175
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P37275"
FT   CROSSLNK        287
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P37275"
FT   CROSSLNK        311
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P37275"
FT   CROSSLNK        315
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P37275"
FT   CROSSLNK        327
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        327
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P37275"
FT   CROSSLNK        419
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P37275"
FT   CROSSLNK        473
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P37275"
FT   CROSSLNK        484
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P37275"
FT   CROSSLNK        495
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P37275"
FT   CROSSLNK        528
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P37275"
FT   CROSSLNK        752
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        752
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P37275"
FT   CONFLICT        33
FT                   /note="S -> A (in Ref. 3; AAB08442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="M -> K (in Ref. 3; AAB08442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125
FT                   /note="Missing (in Ref. 3; AAB08442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        146
FT                   /note="F -> L (in Ref. 3; AAB08442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        313
FT                   /note="E -> EV (in Ref. 3; AAB08442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        353
FT                   /note="G -> A (in Ref. 3; AAB08442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        400
FT                   /note="V -> L (in Ref. 3; AAB08442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        461
FT                   /note="Q -> E (in Ref. 3; AAB08442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        528
FT                   /note="K -> KK (in Ref. 3; AAB08442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        664
FT                   /note="S -> T (in Ref. 3; AAB08442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        744
FT                   /note="E -> L (in Ref. 3; AAB08442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        822
FT                   /note="T -> A (in Ref. 3; AAB08442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1062
FT                   /note="Missing (in Ref. 3; AAB08442)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1117 AA;  122465 MW;  D1FAC2D048D34237 CRC64;
     MADGPRCKRR KQANPRRNNV TNYNTVVEAN SDSDDEDKLH IVEEESITDA ADCEGGMPDD
     ELPADQTVLP GGSDRGGGAK NCWQDNVKDN ECDSDAENEQ NHDPNVEEFL QQQDTAVIYP
     EAPEEDQRQG TPEASSHDEN GTPDAFSQLL TCPYCDRGYK RFTSLKEHIK YRHEKNEDNF
     SCSLCSYTFA YRTQLERHMT SHKSGREQRH VTQSGGNRKF KCTECGKAFK YKHHLKEHLR
     IHSGEKPYEC PNCKKRFSHS GSYSSHISSK KCISLMPVNG RPRSGLKTSQ CSSPSLSTSP
     GSPTRPQIRQ KIENKPLQEP LSVNQIKTEP VDYEFKPIVV ASGINCSTPL QNGVFSSGGQ
     LQATSSPQGV VQAVVLPTVG LVSPISINLS DIQNVLKVAV DGNVIRQVLE TNQASLASKE
     QEAVSASPIQ QGGHSVISAI SLPLVDQDGT TKIIINYSLE QPSQLQVVPQ NLKKEIPAPT
     NSCKSEKLPE DLTVKSETDK SFEGARDDST CLLCEDCPGD LNALPELKHY DPECPAQPPP
     PAPATEKPES SASSAGNGDL SPSQPPLKNL LSLLKAYYAL NAQPSTEELS KIADSVNLPL
     DGVKKWFEKM QAGQIPGQSP DPPSPGTGSV NIPTKTDEQP QPADGNEPQE DSTRGQSPVK
     IRSSPVLPVG SAMNGSRSCT SSPSPLNLCS ARNPQGYSCV AEGAQEEPQV EPLDLSLPKQ
     QGELLERSTV SSVYQNSVYS VQEEPLNLSC AKKEPQKDSC VTDSEPVVNV VPPSANPINI
     AIPTVTAQLP TIVAIADQNS VPCLRALAAN KQTILIPQVA YTYSATVSPA VQEPPVKVIQ
     PNGNQDERQD TSSEGVSTVE DQNDSDSTPP KKKTRKTENG MYACDLCDKI FQKSSSLLRH
     KYEHTGKRPH ECGICRKAFK HKHHLIEHMR LHSGEKPYQC DKCGKRFSHS GSYSQHMNHR
     YSYCKRGAED RDAMEQEDAG PEVLPEVLAT EHVGARASPS QADSDERESL TREEDEDSEK
     EEEEEDKEME ELQEGKECEN PQGEEEEEEE EEEEEEEEEE EEVEADEAEH EAAAKTDGTV
     EVGAAQQAGS LEQKASESEM ESESESEQLS EEKTNEA
//