1433B_MOUSE
ID 1433B_MOUSE Reviewed; 246 AA.
AC Q9CQV8; O70455; Q3TY33; Q3UAN6;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=14-3-3 protein beta/alpha;
DE AltName: Full=Protein kinase C inhibitor protein 1;
DE Short=KCIP-1;
DE Contains:
DE RecName: Full=14-3-3 protein beta/alpha, N-terminally processed;
GN Name=Ywhab;
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;
RA Karpitskiy V.V., Shaw A.S.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Embryo, Kidney, Liver, Thymus, and Visual cortex;
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 [3]
RP PROTEIN SEQUENCE OF 1-12; 14-57; 61-70; 84-117; 128-169; 196-246 AND
RP 215-224, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP PHOSPHORYLATION AT SER-60.
RX PubMed=9705322; DOI=10.1074/jbc.273.34.21834;
RA Megidish T., Cooper J., Zhang L., Fu H., Hakomori S.;
RT "A novel sphingosine-dependent protein kinase (SDK1) specifically
RT phosphorylates certain isoforms of 14-3-3 protein.";
RL J. Biol. Chem. 273:21834-21845(1998).
RN [5]
RP INTERACTION WITH SYNPO2.
RX PubMed=15883195; DOI=10.1083/jcb.200411169;
RA Faul C., Huettelmaier S., Oh J., Hachet V., Singer R.H., Mundel P.;
RT "Promotion of importin alpha-mediated nuclear import by the
RT phosphorylation-dependent binding of cargo protein to 14-3-3.";
RL J. Cell Biol. 169:415-424(2005).
RN [6]
RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-84 AND TYR-106, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16800626; DOI=10.1021/bi060474w;
RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA Bigelow D.J.;
RT "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT disease.";
RL Biochemistry 45:8009-8022(2006).
RN [7]
RP INTERACTION WITH PRKCE.
RX PubMed=18604201; DOI=10.1038/ncb1749;
RA Saurin A.T., Durgan J., Cameron A.J., Faisal A., Marber M.S., Parker P.J.;
RT "The regulated assembly of a PKCepsilon complex controls the completion of
RT cytokinesis.";
RL Nat. Cell Biol. 10:891-901(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
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 [9]
RP INTERACTION WITH SAMSN1.
RX PubMed=20478393; DOI=10.1016/j.biocel.2010.05.004;
RA Brandt S., Ellwanger K., Beuter-Gunia C., Schuster M., Hausser A.,
RA Schmitz I., Beer-Hammer S.;
RT "SLy2 targets the nuclear SAP30/HDAC1 complex.";
RL Int. J. Biochem. Cell Biol. 42:1472-1481(2010).
RN [10]
RP INTERACTION WITH DAPK2.
RX PubMed=26047703; DOI=10.1016/j.bbrc.2015.05.105;
RA Yuasa K., Ota R., Matsuda S., Isshiki K., Inoue M., Tsuji A.;
RT "Suppression of death-associated protein kinase 2 by interaction with 14-3-
RT 3 proteins.";
RL Biochem. Biophys. Res. Commun. 464:70-75(2015).
CC -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC spectrum of both general and specialized signaling pathways. Binds to a
CC large number of partners, usually by recognition of a phosphoserine or
CC phosphothreonine motif. Binding generally results in the modulation of
CC the activity of the binding partner. Negative regulator of
CC osteogenesis. Blocks the nuclear translocation of the phosphorylated
CC form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on
CC cyclin D1 expression resulting in blockage of neuronal apoptosis
CC elicited by SRPK2. Negative regulator of signaling cascades that
CC mediate activation of MAP kinases via AKAP13.
CC {ECO:0000250|UniProtKB:P31946}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with SAMSN1 and PRKCE
CC (PubMed:18604201, PubMed:20478393). Interacts with AKAP13. Interacts
CC with SSH1 and TORC2/CRTC2. Interacts with ABL1; the interaction results
CC in cytoplasmic location of ABL1 and inhibition of cABL-mediated
CC apoptosis. Interacts with ROR2 (dimer); the interaction results in
CC phosphorylation of YWHAB on tyrosine residues. Interacts with GAB2.
CC Interacts with YAP1 (phosphorylated form). Interacts with the
CC phosphorylated (by AKT1) form of SRPK2. Interacts with PKA-
CC phosphorylated AANAT. Interacts with MYO1C. Interacts with SIRT2 (By
CC similarity). Interacts with the 'Thr-369' phosphorylated form of DAPK2
CC (PubMed:26047703). Interacts with PI4KB, TBC1D22A and TBC1D22B.
CC Interacts with the 'Ser-1134' and 'Ser-1161' phosphorylated form of
CC SOS1 (By similarity). Interacts (via phosphorylated form) with YWHAB;
CC this interaction occurs in a protein kinase AKT1-dependent manner (By
CC similarity). Interacts with SLITRK1 (By similarity). Interacts with
CC SYNPO2 (phosphorylated form); YWHAB competes with ACTN2 for interaction
CC with SYNPO2 (PubMed:15883195). Interacts with RIPOR2 (via
CC phosphorylated form); this interaction occurs in a chemokine-dependent
CC manner and does not compete for binding of RIPOR2 with RHOA nor blocks
CC inhibition of RIPOR2-mediated RHOA activity (By similarity). Interacts
CC with MARK2 and MARK3 (By similarity). Interacts with TESK1; the
CC interaction is dependent on the phosphorylation of TESK1 'Ser-439' and
CC inhibits TESK1 kinase activity (By similarity). Interacts with MEFV (By
CC similarity). {ECO:0000250|UniProtKB:P31946,
CC ECO:0000269|PubMed:15883195, ECO:0000269|PubMed:18604201,
CC ECO:0000269|PubMed:20478393, ECO:0000269|PubMed:26047703}.
CC -!- INTERACTION:
CC Q9CQV8; Q5S006: Lrrk2; NbExp=6; IntAct=EBI-771608, EBI-2693710;
CC Q9CQV8; P16054: Prkce; NbExp=5; IntAct=EBI-771608, EBI-298451;
CC Q9CQV8; Q91YE8: Synpo2; NbExp=3; IntAct=EBI-771608, EBI-7623057;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P31946}.
CC Melanosome {ECO:0000250|UniProtKB:P31946}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long;
CC IsoId=Q9CQV8-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q9CQV8-2; Sequence=VSP_018634;
CC -!- PTM: Isoform alpha differs from isoform beta in being phosphorylated
CC (By similarity). Phosphorylated on Ser-60 by protein kinase C delta
CC type catalytic subunit in a sphingosine-dependent fashion.
CC {ECO:0000250, ECO:0000269|PubMed:9705322}.
CC -!- PTM: Isoform Short contains a N-acetylmethionine at position 1.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; AF058797; AAC14343.1; -; mRNA.
DR EMBL; AK002632; BAB22246.1; -; mRNA.
DR EMBL; AK004872; BAB23631.1; -; mRNA.
DR EMBL; AK011389; BAB27587.1; -; mRNA.
DR EMBL; AK083367; BAC38886.1; -; mRNA.
DR EMBL; AK144061; BAE25678.1; -; mRNA.
DR EMBL; AK150414; BAE29538.1; -; mRNA.
DR EMBL; AK151294; BAE30278.1; -; mRNA.
DR EMBL; AK158932; BAE34730.1; -; mRNA.
DR CCDS; CCDS17019.1; -. [Q9CQV8-1]
DR RefSeq; NP_061223.2; NM_018753.6. [Q9CQV8-1]
DR RefSeq; XP_006499972.1; XM_006499909.1. [Q9CQV8-1]
DR PDB; 4GNT; X-ray; 2.41 A; A=1-239.
DR PDB; 5F74; X-ray; 2.35 A; A=1-246.
DR PDB; 5WFU; X-ray; 1.97 A; A/B/C/D=1-246.
DR PDB; 5WFX; X-ray; 1.65 A; A/B=1-246.
DR PDBsum; 4GNT; -.
DR PDBsum; 5F74; -.
DR PDBsum; 5WFU; -.
DR PDBsum; 5WFX; -.
DR AlphaFoldDB; Q9CQV8; -.
DR SMR; Q9CQV8; -.
DR BioGRID; 207648; 82.
DR IntAct; Q9CQV8; 35.
DR MINT; Q9CQV8; -.
DR STRING; 10090.ENSMUSP00000018470; -.
DR iPTMnet; Q9CQV8; -.
DR PhosphoSitePlus; Q9CQV8; -.
DR SwissPalm; Q9CQV8; -.
DR UCD-2DPAGE; Q9CQV8; -.
DR EPD; Q9CQV8; -.
DR jPOST; Q9CQV8; -.
DR MaxQB; Q9CQV8; -.
DR PaxDb; Q9CQV8; -.
DR PeptideAtlas; Q9CQV8; -.
DR PRIDE; Q9CQV8; -.
DR ProteomicsDB; 285886; -. [Q9CQV8-1]
DR ProteomicsDB; 285887; -. [Q9CQV8-2]
DR TopDownProteomics; Q9CQV8-1; -. [Q9CQV8-1]
DR Antibodypedia; 1906; 727 antibodies from 46 providers.
DR DNASU; 54401; -.
DR Ensembl; ENSMUST00000018470; ENSMUSP00000018470; ENSMUSG00000018326. [Q9CQV8-1]
DR GeneID; 54401; -.
DR KEGG; mmu:54401; -.
DR UCSC; uc008ntp.1; mouse. [Q9CQV8-1]
DR CTD; 7529; -.
DR MGI; MGI:1891917; Ywhab.
DR VEuPathDB; HostDB:ENSMUSG00000018326; -.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; Q9CQV8; -.
DR OMA; KGCQLAR; -.
DR PhylomeDB; Q9CQV8; -.
DR TreeFam; TF102003; -.
DR Reactome; R-MMU-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-MMU-165159; MTOR signalling.
DR Reactome; R-MMU-166208; mTORC1-mediated signalling.
DR Reactome; R-MMU-170968; Frs2-mediated activation.
DR Reactome; R-MMU-2028269; Signaling by Hippo.
DR Reactome; R-MMU-392517; Rap1 signalling.
DR Reactome; R-MMU-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-MMU-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-5673000; RAF activation.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-MMU-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-MMU-9614399; Regulation of localization of FOXO transcription factors.
DR BioGRID-ORCS; 54401; 2 hits in 109 CRISPR screens.
DR ChiTaRS; Ywhab; mouse.
DR PRO; PR:Q9CQV8; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CQV8; protein.
DR Bgee; ENSMUSG00000018326; Expressed in substantia nigra and 264 other tissues.
DR ExpressionAtlas; Q9CQV8; baseline and differential.
DR Genevisible; Q9CQV8; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0050815; F:phosphoserine residue binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IDA:MGI.
DR GO; GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; ISO:MGI.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Nitration; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..246
FT /note="14-3-3 protein beta/alpha"
FT /id="PRO_0000367902"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31946"
FT CHAIN 2..246
FT /note="14-3-3 protein beta/alpha, N-terminally processed"
FT /id="PRO_0000000005"
FT SITE 58
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT SITE 129
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P31946"
FT MOD_RES 2
FT /note="N-acetylthreonine; in 14-3-3 protein beta/alpha, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P31946"
FT MOD_RES 2
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31946"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27348"
FT MOD_RES 51
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P27348"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9705322"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31946"
FT MOD_RES 84
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0007744|PubMed:16800626"
FT MOD_RES 106
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0007744|PubMed:16800626"
FT MOD_RES 117
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31946"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68251"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31946"
FT CROSSLNK 51
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P27348"
FT VAR_SEQ 1..2
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018634"
FT CONFLICT 10
FT /note="Q -> H (in Ref. 1; AAC14343)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="N -> D (in Ref. 1; AAC14343)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="D -> Y (in Ref. 2; BAE29538/BAE30278)"
FT /evidence="ECO:0000305"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:5WFX"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:5WFX"
FT HELIX 40..68
FT /evidence="ECO:0007829|PDB:5WFX"
FT HELIX 75..105
FT /evidence="ECO:0007829|PDB:5WFX"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:5WFX"
FT HELIX 114..134
FT /evidence="ECO:0007829|PDB:5WFX"
FT HELIX 137..161
FT /evidence="ECO:0007829|PDB:5WFX"
FT HELIX 167..182
FT /evidence="ECO:0007829|PDB:5WFX"
FT HELIX 187..202
FT /evidence="ECO:0007829|PDB:5WFX"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:5WFX"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:5WFX"
FT HELIX 213..232
FT /evidence="ECO:0007829|PDB:5WFX"
FT MOD_RES Q9CQV8-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 28086 MW; 51C366ED85B38EED CRC64;
MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS
WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLILN ATQAESKVFY
LKMKGDYFRY LSEVASGENK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY
YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD
AGEGEN
