SUS1_ARATH
ID SUS1_ARATH Reviewed; 808 AA.
AC P49040; B9DFM1; Q56WF2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Sucrose synthase 1;
DE Short=AtSUS1;
DE EC=2.4.1.13;
DE AltName: Full=Sucrose-UDP glucosyltransferase 1;
GN Name=SUS1; OrderedLocusNames=At5g20830; ORFNames=T1M15.230;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. C24;
RX PubMed=8220487; DOI=10.1046/j.1365-313x.1993.04020367.x;
RA Martin T., Frommer W.B., Salanoubat M., Willmitzer L.;
RT "Expression of an Arabidopsis sucrose synthase gene indicates a role in
RT metabolization of sucrose both during phloem loading and in sink organs.";
RL Plant J. 4:367-377(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 521-808.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION.
RX PubMed=10567234; DOI=10.1042/bj3440503;
RA Dejardin A., Sokolov L.N., Kleczkowski L.A.;
RT "Sugar/osmoticum levels modulate differential abscisic acid-independent
RT expression of two stress-responsive sucrose synthase genes in
RT Arabidopsis.";
RL Biochem. J. 344:503-509(1999).
RN [7]
RP GENE FAMILY, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14739263; DOI=10.1093/jxb/erh047;
RA Baud S., Vaultier M.N., Rochat C.;
RT "Structure and expression profile of the sucrose synthase multigene family
RT in Arabidopsis.";
RL J. Exp. Bot. 55:397-409(2004).
RN [8]
RP BIOTECHNOLOGY.
RX PubMed=17499718; DOI=10.1016/j.febslet.2007.04.074;
RA Masada S., Kawase Y., Nagatoshi M., Oguchi Y., Terasaka K., Mizukami H.;
RT "An efficient chemoenzymatic production of small molecule glucosides with
RT in situ UDP-glucose recycling.";
RL FEBS Lett. 581:2562-2566(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [10]
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17257168; DOI=10.1111/j.1365-313x.2006.03011.x;
RA Bieniawska Z., Paul Barratt D.H., Garlick A.P., Thole V., Kruger N.J.,
RA Martin C., Zrenner R., Smith A.M.;
RT "Analysis of the sucrose synthase gene family in Arabidopsis.";
RL Plant J. 49:810-828(2007).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=18635527; DOI=10.1093/jxb/ern180;
RA Fallahi H., Scofield G.N., Badger M.R., Chow W.S., Furbank R.T., Ruan Y.L.;
RT "Localization of sucrose synthase in developing seed and siliques of
RT Arabidopsis thaliana reveals diverse roles for SUS during development.";
RL J. Exp. Bot. 59:3283-3295(2008).
RN [12]
RP INDUCTION BY NUC.
RX PubMed=21265895; DOI=10.1111/j.1365-313x.2010.04432.x;
RA Seo P.J., Ryu J., Kang S.K., Park C.M.;
RT "Modulation of sugar metabolism by an INDETERMINATE DOMAIN transcription
RT factor contributes to photoperiodic flowering in Arabidopsis.";
RL Plant J. 65:418-429(2011).
RN [13]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22184213; DOI=10.1073/pnas.1117099109;
RA Baroja-Fernandez E., Munoz F.J., Li J., Bahaji A., Almagro G., Montero M.,
RA Etxeberria E., Hidalgo M., Sesma M.T., Pozueta-Romero J.;
RT "Sucrose synthase activity in the sus1/sus2/sus3/sus4 Arabidopsis mutant is
RT sufficient to support normal cellulose and starch production.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:321-326(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT,
RP AND FUNCTION.
RX PubMed=21865170; DOI=10.1074/jbc.m111.275974;
RA Zheng Y., Anderson S., Zhang Y., Garavito R.M.;
RT "The structure of sucrose synthase-1 from Arabidopsis thaliana and its
RT functional implications.";
RL J. Biol. Chem. 286:36108-36118(2011).
CC -!- FUNCTION: Sucrose-cleaving enzyme that provides UDP-glucose and
CC fructose for various metabolic pathways. {ECO:0000269|PubMed:21865170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an NDP-alpha-D-glucose + D-fructose = a ribonucleoside 5'-
CC diphosphate + H(+) + sucrose; Xref=Rhea:RHEA:16241,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17992, ChEBI:CHEBI:37721,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:76533; EC=2.4.1.13;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.37 mM for D-fructose (synthetic reaction) at pH 9.4
CC {ECO:0000269|PubMed:17257168};
CC KM=0.04 mM for UDP-glucose (synthetic reaction) at pH 9.4
CC {ECO:0000269|PubMed:17257168};
CC KM=31.58 mM for sucrose (degradative reaction) at pH 6
CC {ECO:0000269|PubMed:17257168};
CC KM=53 mM for sucrose (degradative reaction) at pH 7
CC {ECO:0000269|PubMed:22184213};
CC KM=0.08 mM for UDP (degradative reaction) at pH 6
CC {ECO:0000269|PubMed:17257168};
CC KM=0.39 mM for UDP (degradative reaction) at pH 7
CC {ECO:0000269|PubMed:22184213};
CC KM=0.17 mM for ADP (degradative reaction) at pH 7
CC {ECO:0000269|PubMed:22184213};
CC Vmax=11.14 umol/min/mg enzyme for synthetic reaction at pH 9.4
CC {ECO:0000269|PubMed:17257168};
CC Vmax=4.68 umol/min/mg enzyme for degradative reaction at pH 6
CC {ECO:0000269|PubMed:17257168};
CC Vmax=585 umol/min/mg enzyme for degradative reaction at pH 7
CC {ECO:0000269|PubMed:22184213};
CC pH dependence:
CC Optimum pH is 6.0-7.0 for degradative reaction (PubMed:22184213,
CC PubMed:17257168). Optimum pH is 7.0 for synthetic reaction
CC (PubMed:22184213). Optimum pH is 9.0-9.5 for synthetic reaction
CC (PubMed:17257168). {ECO:0000269|PubMed:17257168,
CC ECO:0000269|PubMed:22184213};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21865170}.
CC -!- TISSUE SPECIFICITY: Expressed in the phloem of leaves and in roots.
CC Detected in the whole plant but more precisely confined to the
CC vasculature in cotyledons, mature leaves and siliques.
CC {ECO:0000269|PubMed:14739263, ECO:0000269|PubMed:17257168,
CC ECO:0000269|PubMed:18635527, ECO:0000269|PubMed:8220487}.
CC -!- INDUCTION: By cold, drought and anaerobic stress. By sugar or
CC osmoticum. By anoxia in the roots (at protein level). Up-regulated by
CC NUC/IDD8. {ECO:0000269|PubMed:10567234, ECO:0000269|PubMed:14739263,
CC ECO:0000269|PubMed:17257168, ECO:0000269|PubMed:21265895,
CC ECO:0000269|PubMed:8220487}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17257168}.
CC -!- BIOTECHNOLOGY: A one-pot system for efficient enzymatic production of a
CC wide range of glucosides couples the activities of two recombinant
CC enzymes, UDP-glucose: curcumin glucosyltransferase from Catharanthus
CC roseus (CaUGT2) and sucrose synthase from Arabidopsis thaliana
CC (AtSUS1). UDP, a product inhibitor of UDP-glucosyltransferase, was
CC removed from the system and used for regeneration of UDP-glucose by the
CC second enzyme, AtSUS1. The productivity was increased several-fold and
CC UDP-glucose initially added to the reaction mixture could be reduced to
CC one-tenth of the normal level. {ECO:0000269|PubMed:17499718}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. Plant sucrose
CC synthase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94975.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; X70990; CAA50317.1; -; Genomic_DNA.
DR EMBL; AF296832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92894.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92895.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71045.1; -; Genomic_DNA.
DR EMBL; AK316826; BAH19538.1; -; mRNA.
DR EMBL; AK222090; BAD94975.1; ALT_INIT; mRNA.
DR RefSeq; NP_001031915.1; NM_001036838.2.
DR RefSeq; NP_001332603.1; NM_001343687.1.
DR RefSeq; NP_197583.1; NM_122090.4.
DR PDB; 3S27; X-ray; 2.91 A; A/B/C/D/E/F/G/H=1-808.
DR PDB; 3S28; X-ray; 2.80 A; A/B/C/D/E/F/G/H=1-808.
DR PDB; 3S29; X-ray; 2.85 A; A/B/C/D/E/F/G/H=1-808.
DR PDBsum; 3S27; -.
DR PDBsum; 3S28; -.
DR PDBsum; 3S29; -.
DR AlphaFoldDB; P49040; -.
DR SMR; P49040; -.
DR BioGRID; 17481; 4.
DR STRING; 3702.AT5G20830.1; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; P49040; -.
DR SwissPalm; P49040; -.
DR PaxDb; P49040; -.
DR PRIDE; P49040; -.
DR ProteomicsDB; 228313; -.
DR EnsemblPlants; AT5G20830.1; AT5G20830.1; AT5G20830.
DR EnsemblPlants; AT5G20830.2; AT5G20830.2; AT5G20830.
DR EnsemblPlants; AT5G20830.3; AT5G20830.3; AT5G20830.
DR GeneID; 832206; -.
DR Gramene; AT5G20830.1; AT5G20830.1; AT5G20830.
DR Gramene; AT5G20830.2; AT5G20830.2; AT5G20830.
DR Gramene; AT5G20830.3; AT5G20830.3; AT5G20830.
DR KEGG; ath:AT5G20830; -.
DR Araport; AT5G20830; -.
DR TAIR; locus:2180489; AT5G20830.
DR eggNOG; KOG0853; Eukaryota.
DR HOGENOM; CLU_019158_1_0_1; -.
DR InParanoid; P49040; -.
DR OMA; DMSVYFP; -.
DR OrthoDB; 153947at2759; -.
DR PhylomeDB; P49040; -.
DR BioCyc; ARA:AT5G20830-MON; -.
DR BioCyc; MetaCyc:AT5G20830-MON; -.
DR BRENDA; 2.4.1.13; 399.
DR EvolutionaryTrace; P49040; -.
DR PRO; PR:P49040; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P49040; baseline and differential.
DR Genevisible; P49040; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0016157; F:sucrose synthase activity; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009413; P:response to flooding; IEP:TAIR.
DR GO; GO:0009749; P:response to glucose; IEP:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEP:UniProtKB.
DR GO; GO:0010555; P:response to mannitol; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
DR GO; GO:0072708; P:response to sorbitol; IEP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:InterPro.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR000368; Sucrose_synth.
DR InterPro; IPR012820; Sucrose_synthase_pln/cyn.
DR PANTHER; PTHR45839; PTHR45839; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF00862; Sucrose_synth; 1.
DR TIGRFAMs; TIGR02470; sucr_synth; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Reference proteome; Stress response;
KW Transferase.
FT CHAIN 1..808
FT /note="Sucrose synthase 1"
FT /id="PRO_0000204644"
FT REGION 277..754
FT /note="GT-B glycosyltransferase"
FT CONFLICT 61
FT /note="R -> Q (in Ref. 1; CAA50317)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="V -> L (in Ref. 1; CAA50317)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="S -> P (in Ref. 1; CAA50317)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="N -> D (in Ref. 1; CAA50317)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="C -> QC (in Ref. 1; CAA50317)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="V -> I (in Ref. 1; CAA50317)"
FT /evidence="ECO:0000305"
FT CONFLICT 751..752
FT /note="EK -> DE (in Ref. 1; CAA50317)"
FT /evidence="ECO:0000305"
FT CONFLICT 799..800
FT /note="Missing (in Ref. 1; CAA50317)"
FT /evidence="ECO:0000305"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:3S29"
FT TURN 19..23
FT /evidence="ECO:0007829|PDB:3S29"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:3S28"
FT TURN 54..58
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3S28"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:3S29"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:3S28"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 203..219
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 246..261
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 265..274
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 303..325
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:3S27"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 360..367
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:3S28"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 389..403
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 415..429
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:3S28"
FT TURN 446..451
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 452..459
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 461..474
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 475..481
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 483..487
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 500..504
FT /evidence="ECO:0007829|PDB:3S28"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:3S28"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:3S28"
FT TURN 539..541
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 544..546
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 547..555
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:3S27"
FT STRAND 574..578
FT /evidence="ECO:0007829|PDB:3S28"
FT TURN 583..586
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 587..596
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 598..603
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 605..609
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 620..635
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 639..645
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 651..663
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 667..670
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 675..677
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 679..686
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 691..697
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 699..702
FT /evidence="ECO:0007829|PDB:3S28"
FT TURN 705..707
FT /evidence="ECO:0007829|PDB:3S28"
FT STRAND 710..712
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 717..733
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 736..751
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 755..776
FT /evidence="ECO:0007829|PDB:3S28"
FT TURN 777..779
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 780..793
FT /evidence="ECO:0007829|PDB:3S28"
FT HELIX 795..801
FT /evidence="ECO:0007829|PDB:3S28"
SQ SEQUENCE 808 AA; 92998 MW; CDB56C6A57BD852E CRC64;
MANAERMITR VHSQRERLNE TLVSERNEVL ALLSRVEAKG KGILQQNQII AEFEALPEQT
RKKLEGGPFF DLLKSTQEAI VLPPWVALAV RPRPGVWEYL RVNLHALVVE ELQPAEFLHF
KEELVDGVKN GNFTLELDFE PFNASIPRPT LHKYIGNGVD FLNRHLSAKL FHDKESLLPL
LKFLRLHSHQ GKNLMLSEKI QNLNTLQHTL RKAEEYLAEL KSETLYEEFE AKFEEIGLER
GWGDNAERVL DMIRLLLDLL EAPDPCTLET FLGRVPMVFN VVILSPHGYF AQDNVLGYPD
TGGQVVYILD QVRALEIEML QRIKQQGLNI KPRILILTRL LPDAVGTTCG ERLERVYDSE
YCDILRVPFR TEKGIVRKWI SRFEVWPYLE TYTEDAAVEL SKELNGKPDL IIGNYSDGNL
VASLLAHKLG VTQCTIAHAL EKTKYPDSDI YWKKLDDKYH FSCQFTADIF AMNHTDFIIT
STFQEIAGSK ETVGQYESHT AFTLPGLYRV VHGIDVFDPK FNIVSPGADM SIYFPYTEEK
RRLTKFHSEI EELLYSDVEN KEHLCVLKDK KKPILFTMAR LDRVKNLSGL VEWYGKNTRL
RELANLVVVG GDRRKESKDN EEKAEMKKMY DLIEEYKLNG QFRWISSQMD RVRNGELYRY
ICDTKGAFVQ PALYEAFGLT VVEAMTCGLP TFATCKGGPA EIIVHGKSGF HIDPYHGDQA
ADTLADFFTK CKEDPSHWDE ISKGGLQRIE EKYTWQIYSQ RLLTLTGVYG FWKHVSNLDR
LEARRYLEMF YALKYRPLAQ AVPLAQDD
