CINV1_ARATH
ID CINV1_ARATH Reviewed; 551 AA.
AC Q9LQF2;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Alkaline/neutral invertase CINV1 {ECO:0000305};
DE Short=AtCINV1 {ECO:0000303|PubMed:25256212};
DE EC=3.2.1.26 {ECO:0000269|PubMed:21441406};
DE AltName: Full=Alkaline/neutral invertase G {ECO:0000305};
DE Short=A/N-INVG {ECO:0000303|PubMed:21441406};
DE AltName: Full=Cytosolic invertase 1 {ECO:0000303|PubMed:17508130};
DE Short=AtCYT-INV1 {ECO:0000303|PubMed:17508130};
GN Name=CINV1 {ECO:0000303|PubMed:17508130};
GN Synonyms=INVG {ECO:0000303|PubMed:21441406}; OrderedLocusNames=At1g35580;
GN ORFNames=F15O4.33;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP INTERACTION WITH PIP5K9, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=17220200; DOI=10.1105/tpc.106.045658;
RA Lou Y., Gou J.Y., Xue H.W.;
RT "PIP5K9, an Arabidopsis phosphatidylinositol monophosphate kinase,
RT interacts with a cytosolic invertase to negatively regulate sugar-mediated
RT root growth.";
RL Plant Cell 19:163-181(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION BY
RP MANNITOL, AND DISRUPTION PHENOTYPE.
RX PubMed=17508130; DOI=10.1007/s11103-007-9177-4;
RA Qi X., Wu Z., Li J., Mo X., Wu S., Chu J., Wu P.;
RT "AtCYT-INV1, a neutral invertase, is involved in osmotic stress-induced
RT inhibition on lateral root growth in Arabidopsis.";
RL Plant Mol. Biol. 64:575-587(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-14; SER-61; THR-70
RP AND SER-547, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-61 AND THR-70, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP FUNCTION.
RX PubMed=19470642; DOI=10.1073/pnas.0900689106;
RA Barratt D.H., Derbyshire P., Findlay K., Pike M., Wellner N., Lunn J.,
RA Feil R., Simpson C., Maule A.J., Smith A.M.;
RT "Normal growth of Arabidopsis requires cytosolic invertase but not sucrose
RT synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:13124-13129(2009).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, INDUCTION BY HYDROGEN PEROXIDE, GENE FAMILY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21441406; DOI=10.1093/jxb/err069;
RA Xiang L., Le Roy K., Bolouri-Moghaddam M.R., Vanhaecke M., Lammens W.,
RA Rolland F., Van den Ende W.;
RT "Exploring the neutral invertase-oxidative stress defence connection in
RT Arabidopsis thaliana.";
RL J. Exp. Bot. 62:3849-3862(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH GRF1; GRF2; GRF3;
RP GRF4; GRF5; GRF6; GRF7; GRF8 AND GRF10, PHOSPHORYLATION AT SER-547,
RP INDUCTION BY LIGHT, AND MUTAGENESIS OF SER-547.
RX PubMed=25256212; DOI=10.1111/tpj.12677;
RA Gao J., van Kleeff P.J., Oecking C., Li K.W., Erban A., Kopka J.,
RA Hincha D.K., de Boer A.H.;
RT "Light modulated activity of root alkaline/neutral invertase involves the
RT interaction with 14-3-3 proteins.";
RL Plant J. 80:785-796(2014).
RN [13]
RP FUNCTION.
RX PubMed=29569779; DOI=10.1111/tpj.13909;
RA Barnes W.J., Anderson C.T.;
RT "Cytosolic invertases contribute to cellulose biosynthesis and influence
RT carbon partitioning in seedlings of Arabidopsis thaliana.";
RL Plant J. 94:956-974(2018).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.39 ANGSTROMS), AND SUBUNIT.
RX PubMed=32134001; DOI=10.1107/s2053230x2000179x;
RA Tarkowski L.P., Tsirkone V.G., Osipov E.M., Beelen S., Lammens W.,
RA Vergauwen R., Van den Ende W., Strelkov S.V.;
RT "Crystal structure of Arabidopsis thaliana neutral invertase 2.";
RL Acta Crystallogr. F Struct. Biol. Commun. 76:152-157(2020).
CC -!- FUNCTION: Cytosolic invertase that specifically cleaves sucrose into
CC glucose and fructose and is involved in the regulation of multiple
CC tissue development including primary root elongation, root hair growth,
CC leaf and silique development, and floral transition (PubMed:17220200,
CC PubMed:19470642, PubMed:21441406, PubMed:25256212). Is involved in
CC osmotic stress-induced inhibition on lateral root growth by controlling
CC the concentration of hexose in cells (PubMed:17508130). May regulate
CC sugar-mediated root development by controlling sucrose catabolism in
CC root cells (PubMed:17220200). Contributes to carbon partitioning and
CC cellulose biosynthesis in seedlings (PubMed:29569779).
CC {ECO:0000269|PubMed:17220200, ECO:0000269|PubMed:17508130,
CC ECO:0000269|PubMed:19470642, ECO:0000269|PubMed:21441406,
CC ECO:0000269|PubMed:25256212, ECO:0000269|PubMed:29569779}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC Evidence={ECO:0000269|PubMed:21441406};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.4 mM for sucrose {ECO:0000269|PubMed:17220200,
CC ECO:0000269|PubMed:17508130};
CC KM=8.4 mM for sucrose {ECO:0000269|PubMed:21441406};
CC pH dependence:
CC Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:17220200,
CC ECO:0000269|PubMed:17508130, ECO:0000269|PubMed:21441406};
CC Temperature dependence:
CC Optimum temperature is 9 degrees Celsius.
CC {ECO:0000269|PubMed:25256212};
CC -!- SUBUNIT: Forms homohexamers (PubMed:32134001). Interacts with PIP5K9
CC (PubMed:17220200). Interaction with PIP5K9 represses CINV1 activity
CC (PubMed:17220200). Interacts with GRF1, GRF2, GRF3, GRF4, GRF5, GRF6,
CC GRF7, GRF8 and GRF10; these interactions are dependent of the
CC phosphorylation at Ser-547 (PubMed:25256212).
CC {ECO:0000269|PubMed:17220200, ECO:0000269|PubMed:25256212,
CC ECO:0000269|PubMed:32134001}.
CC -!- INTERACTION:
CC Q9LQF2; Q8L850: PIP5K9; NbExp=6; IntAct=EBI-2008033, EBI-2008013;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21441406}.
CC Nucleus {ECO:0000269|PubMed:17220200}. Note=Detected in membrane and
CC nucleus when associated with PIP5K9. {ECO:0000269|PubMed:17220200}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LQF2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in radicle, hypocotyls, root tips and
CC vascular cylinder, leaf vasculature, shoot stipules, trichomes, stem,
CC stigma apex and base of siliques. {ECO:0000269|PubMed:17508130}.
CC -!- INDUCTION: Induced by mannitol in roots (PubMed:17508130). Induced by
CC hydrogen peroxide (PubMed:21441406). Induced by dark-to-light
CC transition in roots (PubMed:25256212). {ECO:0000269|PubMed:17508130,
CC ECO:0000269|PubMed:21441406, ECO:0000269|PubMed:25256212}.
CC -!- PTM: Phosphorylated at Ser-547 by CPK3 and CPK21.
CC {ECO:0000269|PubMed:25256212}.
CC -!- DISRUPTION PHENOTYPE: Reduced primary root length and increased length
CC and number of lateral roots. Reduced plant growth and early flowering.
CC Reduced seedling levels of glucose and fructose, but increased levels
CC of sucrose. {ECO:0000269|PubMed:17220200, ECO:0000269|PubMed:17508130,
CC ECO:0000269|PubMed:21441406}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 100 family.
CC {ECO:0000305}.
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DR EMBL; AM230708; CAJ76698.1; -; mRNA.
DR EMBL; AC007887; AAF79356.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31812.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31813.1; -; Genomic_DNA.
DR EMBL; AY065247; AAL38723.1; -; mRNA.
DR EMBL; AY142662; AAN13200.1; -; mRNA.
DR PIR; A86477; A86477.
DR RefSeq; NP_174791.2; NM_103255.2. [Q9LQF2-1]
DR RefSeq; NP_849750.1; NM_179419.4. [Q9LQF2-1]
DR PDB; 6TTJ; X-ray; 3.39 A; A/B/C/D/E/F/G/H/I/J/K/L=1-551.
DR PDBsum; 6TTJ; -.
DR AlphaFoldDB; Q9LQF2; -.
DR SMR; Q9LQF2; -.
DR BioGRID; 25686; 11.
DR IntAct; Q9LQF2; 3.
DR STRING; 3702.AT1G35580.2; -.
DR CAZy; GH100; Glycoside Hydrolase Family 100.
DR iPTMnet; Q9LQF2; -.
DR PaxDb; Q9LQF2; -.
DR PRIDE; Q9LQF2; -.
DR ProteomicsDB; 246497; -. [Q9LQF2-1]
DR EnsemblPlants; AT1G35580.1; AT1G35580.1; AT1G35580. [Q9LQF2-1]
DR EnsemblPlants; AT1G35580.2; AT1G35580.2; AT1G35580. [Q9LQF2-1]
DR GeneID; 840454; -.
DR Gramene; AT1G35580.1; AT1G35580.1; AT1G35580. [Q9LQF2-1]
DR Gramene; AT1G35580.2; AT1G35580.2; AT1G35580. [Q9LQF2-1]
DR KEGG; ath:AT1G35580; -.
DR Araport; AT1G35580; -.
DR TAIR; locus:2014676; AT1G35580.
DR eggNOG; ENOG502QPS0; Eukaryota.
DR HOGENOM; CLU_020846_1_1_1; -.
DR InParanoid; Q9LQF2; -.
DR OMA; GRECIEQ; -.
DR PhylomeDB; Q9LQF2; -.
DR BRENDA; 3.2.1.26; 399.
DR PRO; PR:Q9LQF2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQF2; baseline and differential.
DR Genevisible; Q9LQF2; AT.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IDA:TAIR.
DR GO; GO:0033926; F:glycopeptide alpha-N-acetylgalactosaminidase activity; IEA:InterPro.
DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; IDA:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IMP:TAIR.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IMP:TAIR.
DR GO; GO:0034214; P:protein hexamerization; IDA:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0005987; P:sucrose catabolic process; IDA:TAIR.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR024746; Glyco_hydro_100.
DR PANTHER; PTHR31916; PTHR31916; 1.
DR Pfam; PF12899; Glyco_hydro_100; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Carbohydrate metabolism;
KW Cytoplasm; Glycosidase; Hydrolase; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..551
FT /note="Alkaline/neutral invertase CINV1"
FT /id="PRO_0000422134"
FT REGION 50..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25256212,
FT ECO:0007744|PubMed:18433157"
FT MUTAGEN 547
FT /note="S->A: No effect on catalytic activity, but prevents
FT interaction with 14-3-3 proteins."
FT /evidence="ECO:0000269|PubMed:25256212"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:6TTJ"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:6TTJ"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:6TTJ"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:6TTJ"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:6TTJ"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 204..220
FT /evidence="ECO:0007829|PDB:6TTJ"
FT TURN 223..227
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 229..242
FT /evidence="ECO:0007829|PDB:6TTJ"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:6TTJ"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 273..287
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 294..316
FT /evidence="ECO:0007829|PDB:6TTJ"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 322..329
FT /evidence="ECO:0007829|PDB:6TTJ"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:6TTJ"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:6TTJ"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:6TTJ"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 381..389
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 395..407
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:6TTJ"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:6TTJ"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 428..433
FT /evidence="ECO:0007829|PDB:6TTJ"
FT TURN 445..447
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 454..464
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 468..478
FT /evidence="ECO:0007829|PDB:6TTJ"
FT TURN 479..486
FT /evidence="ECO:0007829|PDB:6TTJ"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:6TTJ"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 508..522
FT /evidence="ECO:0007829|PDB:6TTJ"
FT HELIX 524..529
FT /evidence="ECO:0007829|PDB:6TTJ"
SQ SEQUENCE 551 AA; 62834 MW; 8FE2EF4BC4DFC91F CRC64;
MEGVGLRAVG SHCSLSEMDD LDLTRALDKP RLKIERKRSF DERSMSELST GYSRHDGIHD
SPRGRSVLDT PLSSARNSFE PHPMMAEAWE ALRRSMVFFR GQPVGTLAAV DNTTDEVLNY
DQVFVRDFVP SALAFLMNGE PDIVKHFLLK TLQLQGWEKR VDRFKLGEGV MPASFKVLHD
PIRETDNIVA DFGESAIGRV APVDSGFWWI ILLRAYTKST GDLTLSETPE CQKGMKLILS
LCLAEGFDTF PTLLCADGCS MIDRRMGVYG YPIEIQALFF MALRSALSML KPDGDGREVI
ERIVKRLHAL SFHMRNYFWL DHQNLNDIYR FKTEEYSHTA VNKFNVMPDS IPEWVFDFMP
LRGGYFVGNV GPAHMDFRWF ALGNCVSILS SLATPDQSMA IMDLLEHRWA ELVGEMPLKI
CYPCLEGHEW RIVTGCDPKN TRWSYHNGGS WPVLLWQLTA ACIKTGRPQI ARRAVDLIES
RLHRDCWPEY YDGKLGRYVG KQARKYQTWS IAGYLVAKML LEDPSHIGMI SLEEDKLMKP
VIKRSASWPQ L
