GenomeNet

Database: UniProt/SWISS-PROT
Entry: HXK1_ARATH
LinkDB: HXK1_ARATH
Original site: HXK1_ARATH 
ID   HXK1_ARATH              Reviewed;         496 AA.
AC   Q42525; Q42535;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   07-NOV-2018, entry version 149.
DE   RecName: Full=Hexokinase-1 {ECO:0000303|PubMed:9014361};
DE            EC=2.7.1.1 {ECO:0000255|PROSITE-ProRule:PRU01084, ECO:0000269|PubMed:7610198};
DE   AltName: Full=Protein GLUCOSE INSENSITIVE 2 {ECO:0000303|PubMed:16920781};
GN   Name=HXK1 {ECO:0000303|PubMed:9014361};
GN   Synonyms=GIN2 {ECO:0000303|PubMed:16920781};
GN   OrderedLocusNames=At4g29130 {ECO:0000312|Araport:AT4G29130};
GN   ORFNames=F19B15.160 {ECO:0000312|EMBL:CAB43927.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=7610198; DOI=10.1104/pp.108.2.879;
RA   Dai N., Schaffer A.A., Petreikov M., Granot D.;
RT   "Arabidopsis thaliana hexokinase cDNA isolated by complementation of
RT   yeast cells.";
RL   Plant Physiol. 108:879-880(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=9014361; DOI=10.1105/tpc.9.1.5;
RA   Jang J.-C., Leon P., Zhou L., Sheen J.;
RT   "Hexokinase as a sugar sensor in higher plants.";
RL   Plant Cell 9:5-19(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [4]
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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   FUNCTION, MUTAGENESIS OF GLY-104; SER-177 AND GLY-416, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=12690200; DOI=10.1126/science.1080585;
RA   Moore B., Zhou L., Rolland F., Hall Q., Cheng W.-H., Liu Y.-X.,
RA   Hwang I., Jones T., Sheen J.;
RT   "Role of the Arabidopsis glucose sensor HXK1 in nutrient, light, and
RT   hormonal signaling.";
RL   Science 300:332-336(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
RP   SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome
RT   highlights signaling and regulatory components, provides assessment of
RT   targeting prediction programs, and indicates plant-specific
RT   mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [8]
RP   INTERACTION WITH RPT5B, AND SUBCELLULAR LOCATION.
RX   PubMed=17081979; DOI=10.1016/j.cell.2006.09.028;
RA   Cho Y.H., Yoo S.D., Sheen J.;
RT   "Regulatory functions of nuclear hexokinase1 complex in glucose
RT   signaling.";
RL   Cell 127:579-589(2006).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16920781; DOI=10.1105/tpc.106.041509;
RA   Kim M., Lim J.-H., Ahn C.S., Park K., Kim G.T., Kim W.T., Pai H.-S.;
RT   "Mitochondria-associated hexokinases play a role in the control of
RT   programmed cell death in Nicotiana benthamiana.";
RL   Plant Cell 18:2341-2355(2006).
RN   [10]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH RHIP1.
RX   PubMed=26528314; DOI=10.3389/fpls.2015.00851;
RA   Huang J.-P., Tunc-Ozdemir M., Chang Y., Jones A.M.;
RT   "Cooperative control between AtRGS1 and AtHXK1 in a WD40-repeat
RT   protein pathway in Arabidopsis thaliana.";
RL   Front. Plant Sci. 6:851-851(2015).
RN   [11]
RP   XXX, AND X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 30-496 IN COMPLEX
RP   WITH GLUCOSE.
RX   PubMed=25664748; DOI=10.1107/S1399004714026091;
RA   Feng J., Zhao S., Chen X., Wang W., Dong W., Chen J., Shen J.R.,
RA   Liu L., Kuang T.;
RT   "Biochemical and structural study of Arabidopsis hexokinase 1.";
RL   Acta Crystallogr. D 71:367-375(2015).
CC   -!- FUNCTION: Fructose and glucose phosphorylating enzyme. May be
CC       involved in the phosphorylation of glucose during the export from
CC       mitochondrion to cytosol. Acts as sugar sensor which may regulate
CC       sugar-dependent gene repression or activation (PubMed:26528314).
CC       Mediates the effects of sugar on plant growth and development
CC       independently of its catalytic activity or the sugar metabolism.
CC       May regulate the execution of program cell death in plant cells.
CC       Promotes roots and leaves growth (PubMed:26528314).
CC       {ECO:0000269|PubMed:12690200, ECO:0000269|PubMed:16920781,
CC       ECO:0000269|PubMed:26528314, ECO:0000269|PubMed:9014361}.
CC   -!- CATALYTIC ACTIVITY: ATP + D-hexose = ADP + D-hexose 6-phosphate.
CC       {ECO:0000255|PROSITE-ProRule:PRU01084,
CC       ECO:0000269|PubMed:7610198}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=44 uM for glucose {ECO:0000269|PubMed:7610198};
CC         KM=17 mM for fructose {ECO:0000269|PubMed:7610198};
CC         Note=Measured in yeast lacking glucose and hexose kinase
CC         activity. {ECO:0000269|PubMed:7610198};
CC   -!- SUBUNIT: Interacts with RPT5B in nucleus. Interacts with RHIP1
CC       (PubMed:26528314). {ECO:0000269|PubMed:17081979,
CC       ECO:0000269|PubMed:26528314}.
CC   -!- INTERACTION:
CC       Q96292:ACT2; NbExp=2; IntAct=EBI-1644489, EBI-1644538;
CC       Q9SRH5:VDAC1; NbExp=2; IntAct=EBI-1644489, EBI-1644501;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC       membrane protein. Nucleus {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in flowers and siliques, at
CC       intermediate levels in roots and stems, and at lower levels in
CC       rosette and cauline leaves. {ECO:0000269|PubMed:9014361}.
CC   -!- DISRUPTION PHENOTYPE: Plants display a glucose-insensitive
CC       phenotype which allows them to grow on high glucose concentration
CC       medium (>6% glucose) (PubMed:12690200, PubMed:26528314). Dwarf
CC       plants with reduced roots and leaves growth (PubMed:26528314).
CC       {ECO:0000269|PubMed:12690200, ECO:0000269|PubMed:26528314}.
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01084, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA60333.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; U18754; AAA60333.1; ALT_INIT; mRNA.
DR   EMBL; U28214; AAB49908.1; -; mRNA.
DR   EMBL; AL078470; CAB43927.1; -; Genomic_DNA.
DR   EMBL; AL161574; CAB79671.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85590.1; -; Genomic_DNA.
DR   EMBL; AY075658; AAL77665.1; -; mRNA.
DR   EMBL; AY124809; AAM70518.1; -; mRNA.
DR   PIR; S71205; S71205.
DR   RefSeq; NP_194642.1; NM_119057.4.
DR   UniGene; At.24726; -.
DR   UniGene; At.70249; -.
DR   PDB; 4QS7; X-ray; 2.00 A; A=30-496.
DR   PDB; 4QS8; X-ray; 1.80 A; A=30-496.
DR   PDB; 4QS9; X-ray; 2.10 A; A=30-496.
DR   PDBsum; 4QS7; -.
DR   PDBsum; 4QS8; -.
DR   PDBsum; 4QS9; -.
DR   ProteinModelPortal; Q42525; -.
DR   SMR; Q42525; -.
DR   BioGrid; 14321; 12.
DR   IntAct; Q42525; 3.
DR   STRING; 3702.AT4G29130.1; -.
DR   MoonProt; Q42525; -.
DR   iPTMnet; Q42525; -.
DR   SwissPalm; Q42525; -.
DR   PaxDb; Q42525; -.
DR   PRIDE; Q42525; -.
DR   EnsemblPlants; AT4G29130.1; AT4G29130.1; AT4G29130.
DR   GeneID; 829034; -.
DR   Gramene; AT4G29130.1; AT4G29130.1; AT4G29130.
DR   KEGG; ath:AT4G29130; -.
DR   Araport; AT4G29130; -.
DR   TAIR; locus:2119931; AT4G29130.
DR   eggNOG; KOG1369; Eukaryota.
DR   eggNOG; COG5026; LUCA.
DR   HOGENOM; HOG000162670; -.
DR   InParanoid; Q42525; -.
DR   KO; K00844; -.
DR   OMA; EEMPIGY; -.
DR   OrthoDB; EOG093608SG; -.
DR   PhylomeDB; Q42525; -.
DR   BioCyc; ARA:AT4G29130-MONOMER; -.
DR   BioCyc; MetaCyc:AT4G29130-MONOMER; -.
DR   BRENDA; 2.7.1.1; 399.
DR   Reactome; R-ATH-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR   Reactome; R-ATH-6798695; Neutrophil degranulation.
DR   Reactome; R-ATH-70171; Glycolysis.
DR   PRO; PR:Q42525; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q42525; baseline and differential.
DR   Genevisible; Q42525; AT.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0009536; C:plastid; IDA:TAIR.
DR   GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR   GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
DR   GO; GO:0005773; C:vacuole; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0001047; F:core promoter binding; IMP:CAFA.
DR   GO; GO:0008865; F:fructokinase activity; IDA:TAIR.
DR   GO; GO:0004340; F:glucokinase activity; IDA:TAIR.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; IDA:TAIR.
DR   GO; GO:0019158; F:mannokinase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IDA:TAIR.
DR   GO; GO:0001678; P:cellular glucose homeostasis; IBA:GO_Central.
DR   GO; GO:0010255; P:glucose mediated signaling pathway; IMP:CAFA.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   GO; GO:0019320; P:hexose catabolic process; IDA:TAIR.
DR   GO; GO:0012501; P:programmed cell death; IMP:TAIR.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:CAFA.
DR   GO; GO:0090332; P:stomatal closure; IMP:TAIR.
DR   GO; GO:0010182; P:sugar mediated signaling pathway; TAS:TAIR.
DR   GO; GO:0010148; P:transpiration; IMP:TAIR.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR019807; Hexokinase_BS.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; PTHR19443; 1.
DR   Pfam; PF00349; Hexokinase_1; 1.
DR   Pfam; PF03727; Hexokinase_2; 1.
DR   PROSITE; PS00378; HEXOKINASE_1; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Glycolysis; Kinase;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Nucleotide-binding; Nucleus; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    496       Hexokinase-1.
FT                                /FTId=PRO_0000197612.
FT   TRANSMEM      4     24       Helical. {ECO:0000255}.
FT   DOMAIN       35    487       Hexokinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01084}.
FT   NP_BIND     101    106       ATP. {ECO:0000250|UniProtKB:P19367}.
FT   NP_BIND     320    321       ATP. {ECO:0000250|UniProtKB:P19367}.
FT   NP_BIND     357    361       ATP. {ECO:0000250|UniProtKB:P19367}.
FT   NP_BIND     441    445       ATP. {ECO:0000250|UniProtKB:P19367}.
FT   REGION       25     26       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P19367}.
FT   REGION       90    228       Hexokinase small subdomain.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   REGION      101    105       Glucose-6-phosphate binding.
FT                                {ECO:0000250|UniProtKB:P19367}.
FT   REGION      177    178       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P19367}.
FT   REGION      194    195       Substrate binding. {ECO:0000244|PDB:4QS7,
FT                                ECO:0000244|PDB:4QS9,
FT                                ECO:0000269|PubMed:25664748}.
FT   REGION      229    476       Hexokinase large subdomain.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   REGION      229    230       Substrate binding. {ECO:0000244|PDB:4QS7,
FT                                ECO:0000244|PDB:4QS9,
FT                                ECO:0000269|PubMed:25664748}.
FT   REGION      255    256       Substrate binding. {ECO:0000244|PDB:4QS7,
FT                                ECO:0000244|PDB:4QS9,
FT                                ECO:0000269|PubMed:25664748}.
FT   REGION      439    441       Glucose-6-phosphate binding.
FT                                {ECO:0000250|UniProtKB:P19367}.
FT   BINDING     230    230       Glucose-6-phosphate.
FT                                {ECO:0000250|UniProtKB:P19367}.
FT   BINDING     253    253       ATP. {ECO:0000250|UniProtKB:P19367}.
FT   BINDING     253    253       Glucose-6-phosphate.
FT                                {ECO:0000250|UniProtKB:P19367}.
FT   BINDING     284    284       Substrate. {ECO:0000244|PDB:4QS7,
FT                                ECO:0000244|PDB:4QS9,
FT                                ECO:0000269|PubMed:25664748}.
FT   BINDING     315    315       Substrate. {ECO:0000244|PDB:4QS7,
FT                                ECO:0000244|PDB:4QS9,
FT                                ECO:0000269|PubMed:25664748}.
FT   BINDING     478    478       Glucose-6-phosphate.
FT                                {ECO:0000250|UniProtKB:P19367}.
FT   MUTAGEN     104    104       G->A: Abolishes glucose phosphorylation
FT                                activity. {ECO:0000269|PubMed:12690200}.
FT   MUTAGEN     177    177       S->D: Abolishes glucose phosphorylation
FT                                activity. {ECO:0000269|PubMed:12690200}.
FT   MUTAGEN     416    416       G->A: In gin2-2; insensitive to glucose.
FT                                {ECO:0000269|PubMed:12690200}.
FT   HELIX        34     48       {ECO:0000244|PDB:4QS8}.
FT   HELIX        52     71       {ECO:0000244|PDB:4QS8}.
FT   STRAND       75     78       {ECO:0000244|PDB:4QS8}.
FT   STRAND       94    115       {ECO:0000244|PDB:4QS8}.
FT   TURN        117    119       {ECO:0000244|PDB:4QS8}.
FT   STRAND      121    130       {ECO:0000244|PDB:4QS8}.
FT   TURN        133    136       {ECO:0000244|PDB:4QS8}.
FT   HELIX       140    155       {ECO:0000244|PDB:4QS8}.
FT   HELIX       160    162       {ECO:0000244|PDB:4QS7}.
FT   STRAND      170    176       {ECO:0000244|PDB:4QS8}.
FT   STRAND      178    184       {ECO:0000244|PDB:4QS8}.
FT   STRAND      187    190       {ECO:0000244|PDB:4QS8}.
FT   HELIX       200    202       {ECO:0000244|PDB:4QS8}.
FT   HELIX       207    216       {ECO:0000244|PDB:4QS8}.
FT   TURN        217    219       {ECO:0000244|PDB:4QS8}.
FT   STRAND      222    228       {ECO:0000244|PDB:4QS8}.
FT   HELIX       230    241       {ECO:0000244|PDB:4QS8}.
FT   STRAND      245    262       {ECO:0000244|PDB:4QS8}.
FT   HELIX       263    265       {ECO:0000244|PDB:4QS8}.
FT   STRAND      277    282       {ECO:0000244|PDB:4QS8}.
FT   HELIX       285    287       {ECO:0000244|PDB:4QS8}.
FT   HELIX       297    304       {ECO:0000244|PDB:4QS8}.
FT   STRAND      306    308       {ECO:0000244|PDB:4QS8}.
FT   HELIX       315    318       {ECO:0000244|PDB:4QS8}.
FT   HELIX       320    338       {ECO:0000244|PDB:4QS8}.
FT   STRAND      342    344       {ECO:0000244|PDB:4QS8}.
FT   HELIX       347    350       {ECO:0000244|PDB:4QS8}.
FT   HELIX       357    364       {ECO:0000244|PDB:4QS8}.
FT   HELIX       369    371       {ECO:0000244|PDB:4QS9}.
FT   HELIX       372    382       {ECO:0000244|PDB:4QS8}.
FT   HELIX       389    420       {ECO:0000244|PDB:4QS8}.
FT   STRAND      434    440       {ECO:0000244|PDB:4QS8}.
FT   HELIX       441    444       {ECO:0000244|PDB:4QS8}.
FT   HELIX       447    466       {ECO:0000244|PDB:4QS8}.
FT   STRAND      469    473       {ECO:0000244|PDB:4QS8}.
FT   TURN        477    479       {ECO:0000244|PDB:4QS8}.
FT   HELIX       480    488       {ECO:0000244|PDB:4QS8}.
SQ   SEQUENCE   496 AA;  53707 MW;  6DC81CE114E0B52B CRC64;
     MGKVAVGATV VCTAAVCAVA VLVVRRRMQS SGKWGRVLAI LKAFEEDCAT PISKLRQVAD
     AMTVEMHAGL ASDGGSKLKM LISYVDNLPS GDEKGLFYAL DLGGTNFRVM RVLLGGKQER
     VVKQEFEEVS IPPHLMTGGS DELFNFIAEA LAKFVATECE DFHLPEGRQR ELGFTFSFPV
     KQTSLSSGSL IKWTKGFSIE EAVGQDVVGA LNKALERVGL DMRIAALVND TVGTLAGGRY
     YNPDVVAAVI LGTGTNAAYV ERATAIPKWH GLLPKSGEMV INMEWGNFRS SHLPLTEFDH
     TLDFESLNPG EQILEKIISG MYLGEILRRV LLKMAEDAAF FGDTVPSKLR IPFIIRTPHM
     SAMHNDTSPD LKIVGSKIKD ILEVPTTSLK MRKVVISLCN IIATRGARLS AAGIYGILKK
     LGRDTTKDEE VQKSVIAMDG GLFEHYTQFS ECMESSLKEL LGDEASGSVE VTHSNDGSGI
     GAALLAASHS LYLEDS
//
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