ID   HXK6_ORYSJ              Reviewed;         506 AA.
AC   Q8LQ68; Q0JJF0;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=Hexokinase-6;
DE            EC=2.7.1.1 {ECO:0000305|PubMed:16552590};
DE   AltName: Full=Hexokinase-2;
GN   Name=HXK6; Synonyms=HXK2;
GN   OrderedLocusNames=Os01g0742500, LOC_Os01g53930; ORFNames=P0439E07.19;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, INDUCTION, AND NOMENCLATURE.
RC   STRAIN=cv. Jinmi;
RX   PubMed=16552590; DOI=10.1007/s00425-006-0251-y;
RA   Cho J.-I., Ryoo N., Ko S., Lee S.-K., Lee J., Jung K.-H., Lee Y.-H.,
RA   Bhoo S.H., Winderickx J., An G., Hahn T.-R., Jeon J.-S.;
RT   "Structure, expression, and functional analysis of the hexokinase gene
RT   family in rice (Oryza sativa L.).";
RL   Planta 224:598-611(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Zhonghua 15; TISSUE=Flower;
RA   Wang Y.D., Cheng W., Wang X.S., Zhou X.J.;
RT   "The hexokinase gene family in rice.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [6]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [8]
RP   FUNCTION, AND MUTAGENESIS OF GLY-112 AND SER-185.
RX   PubMed=19010999; DOI=10.1104/pp.108.131227;
RA   Cho J.I., Ryoo N., Eom J.S., Lee D.W., Kim H.B., Jeong S.W., Lee Y.H.,
RA   Kwon Y.K., Cho M.H., Bhoo S.H., Hahn T.R., Park Y.I., Hwang I., Sheen J.,
RA   Jeon J.S.;
RT   "Role of the rice hexokinases OsHXK5 and OsHXK6 as glucose sensors.";
RL   Plant Physiol. 149:745-759(2009).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 45-506 IN COMPLEX WITH D-GLUCOSE.
RA   Matsudaira K., Mochizuki S., Yoshida H., Kamitori S., Akimitsu K.;
RT   "Crystal structure of Oryza sativa hexokinase 6.";
RL   Submitted (APR-2018) to the PDB data bank.
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 39-506 IN COMPLEX WITH D-GLUCOSE
RP   AND ADP.
RX   PubMed=31176485; DOI=10.1016/j.bbrc.2019.05.139;
RA   He C., Chen J., Wang H., Wan Y., Zhou J., Dan Z., Zeng Y., Xu W., Zhu Y.,
RA   Huang W., Yin L.;
RT   "Crystal structures of rice hexokinase 6 with a series of substrates shed
RT   light on its enzymatic mechanism.";
RL   Biochem. Biophys. Res. Commun. 515:614-620(2019).
CC   -!- FUNCTION: Fructose and glucose phosphorylating enzyme
CC       (PubMed:16552590). Functions as a glucose sensor for plant growth and
CC       photosynthesis (PubMed:19010999). {ECO:0000269|PubMed:16552590,
CC       ECO:0000269|PubMed:19010999}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61567, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000305|PubMed:16552590};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC         Evidence={ECO:0000305|PubMed:16552590};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000305|PubMed:16552590};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC         Evidence={ECO:0000305|PubMed:16552590};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000305|PubMed:16552590};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC         Evidence={ECO:0000305|PubMed:16552590};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000305|PubMed:16552590}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000305|PubMed:16552590}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC       {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers, immature seeds
CC       and endosperm. {ECO:0000269|PubMed:16552590}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during flower development until 15 days
CC       after flowering. {ECO:0000269|PubMed:16552590}.
CC   -!- INDUCTION: By glucose or fructose treatment in leaves.
CC       {ECO:0000269|PubMed:16552590}.
CC   -!- MISCELLANEOUS: Plants over-expressing HXK6 exhibit hypersensitive plant
CC       growth retardation and enhanced repression of the photosynthetic gene
CC       RbcS in response to glucose treatment. {ECO:0000269|PubMed:19010999}.
CC   -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01084, 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; DQ116388; AAZ93623.1; -; mRNA.
DR   EMBL; AY884165; AAX68418.1; -; mRNA.
DR   EMBL; AP003768; BAB91930.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF06128.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS74288.1; -; Genomic_DNA.
DR   EMBL; AK065656; BAG89607.1; -; mRNA.
DR   RefSeq; XP_015618116.1; XM_015762630.1.
DR   PDB; 5ZQT; X-ray; 2.84 A; A/B/C=45-506.
DR   PDB; 6JJ4; X-ray; 2.60 A; A=40-506.
DR   PDB; 6JJ7; X-ray; 2.90 A; A/C/E=39-503.
DR   PDB; 6JJ8; X-ray; 2.80 A; A/B/C=39-503.
DR   PDB; 6JJ9; X-ray; 3.00 A; A/C/E=39-503.
DR   PDBsum; 5ZQT; -.
DR   PDBsum; 6JJ4; -.
DR   PDBsum; 6JJ7; -.
DR   PDBsum; 6JJ8; -.
DR   PDBsum; 6JJ9; -.
DR   AlphaFoldDB; Q8LQ68; -.
DR   SMR; Q8LQ68; -.
DR   STRING; 39947.Q8LQ68; -.
DR   PaxDb; 39947-Q8LQ68; -.
DR   EnsemblPlants; Os01t0742500-01; Os01t0742500-01; Os01g0742500.
DR   GeneID; 4326547; -.
DR   Gramene; Os01t0742500-01; Os01t0742500-01; Os01g0742500.
DR   KEGG; osa:4326547; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   HOGENOM; CLU_014393_5_1_1; -.
DR   InParanoid; Q8LQ68; -.
DR   OMA; EILHDDC; -.
DR   OrthoDB; 5481886at2759; -.
DR   BRENDA; 2.7.1.1; 4460.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:CACAO.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008865; F:fructokinase activity; IBA:GO_Central.
DR   GO; GO:0004340; F:glucokinase activity; IMP:CACAO.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IBA:GO_Central.
DR   GO; GO:0009749; P:response to glucose; IMP:CACAO.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR019807; Hexokinase_BS.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; HEXOKINASE; 1.
DR   PANTHER; PTHR19443:SF15; HEXOKINASE-6; 1.
DR   Pfam; PF00349; Hexokinase_1; 1.
DR   Pfam; PF03727; Hexokinase_2; 1.
DR   PRINTS; PR00475; HEXOKINASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00378; HEXOKINASE_1; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
DR   Genevisible; Q8LQ68; OS.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Chloroplast; Glycolysis; Kinase; Membrane;
KW   Nucleotide-binding; Plastid; Plastid outer membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..506
FT                   /note="Hexokinase-6"
FT                   /id="PRO_0000247569"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          43..497
FT                   /note="Hexokinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          98..236
FT                   /note="Hexokinase small subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          237..486
FT                   /note="Hexokinase large subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   BINDING         112
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000269|PubMed:31176485,
FT                   ECO:0007744|PDB:6JJ8, ECO:0007744|PDB:6JJ9"
FT   BINDING         113
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000269|PubMed:31176485,
FT                   ECO:0007744|PDB:6JJ8, ECO:0007744|PDB:6JJ9"
FT   BINDING         114
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000269|PubMed:31176485,
FT                   ECO:0007744|PDB:6JJ8"
FT   BINDING         202
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000269|PubMed:31176485, ECO:0000269|Ref.9,
FT                   ECO:0007744|PDB:5ZQT, ECO:0007744|PDB:6JJ7"
FT   BINDING         203
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000269|PubMed:31176485, ECO:0000269|Ref.9,
FT                   ECO:0007744|PDB:5ZQT, ECO:0007744|PDB:6JJ7"
FT   BINDING         237
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000269|PubMed:31176485, ECO:0000269|Ref.9,
FT                   ECO:0007744|PDB:5ZQT, ECO:0007744|PDB:6JJ7"
FT   BINDING         238
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000269|PubMed:31176485, ECO:0000269|Ref.9,
FT                   ECO:0007744|PDB:5ZQT, ECO:0007744|PDB:6JJ7"
FT   BINDING         261
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000269|PubMed:31176485,
FT                   ECO:0007744|PDB:6JJ8, ECO:0007744|PDB:6JJ9"
FT   BINDING         264
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000269|PubMed:31176485, ECO:0000269|Ref.9,
FT                   ECO:0007744|PDB:5ZQT, ECO:0007744|PDB:6JJ7"
FT   BINDING         292
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000269|PubMed:31176485, ECO:0000269|Ref.9,
FT                   ECO:0007744|PDB:5ZQT, ECO:0007744|PDB:6JJ7"
FT   BINDING         323
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000269|PubMed:31176485, ECO:0000269|Ref.9,
FT                   ECO:0007744|PDB:5ZQT, ECO:0007744|PDB:6JJ7"
FT   BINDING         451
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000269|PubMed:31176485,
FT                   ECO:0007744|PDB:6JJ8, ECO:0007744|PDB:6JJ9"
FT   MUTAGEN         112
FT                   /note="G->D: Abolishes glucose phosphorylation activity."
FT                   /evidence="ECO:0000269|PubMed:19010999"
FT   MUTAGEN         185
FT                   /note="S->A: Abolishes glucose phosphorylation activity."
FT                   /evidence="ECO:0000269|PubMed:19010999"
FT   HELIX           49..55
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           60..77
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          102..110
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          112..123
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           124..127
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          129..138
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   TURN            141..144
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           148..163
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          172..175
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          178..184
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          188..192
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          195..198
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           208..210
FT                   /evidence="ECO:0007829|PDB:5ZQT"
FT   STRAND          211..214
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           215..224
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   TURN            225..227
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          230..236
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           238..249
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          253..271
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   TURN            275..277
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          279..281
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          285..290
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           293..295
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           305..312
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          314..320
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           323..326
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           328..344
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          350..352
FT                   /evidence="ECO:0007829|PDB:5ZQT"
FT   HELIX           356..358
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           365..372
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          376..378
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           380..389
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           397..428
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          436..439
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          444..450
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           451..455
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           457..470
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           473..476
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          479..483
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   STRAND          487..489
FT                   /evidence="ECO:0007829|PDB:6JJ4"
FT   HELIX           493..496
FT                   /evidence="ECO:0007829|PDB:6JJ4"
SQ   SEQUENCE   506 AA;  55121 MW;  242F8DCCB5FF8947 CRC64;
     MGKGTVVGTA VVVCAAAAAA VGVAVVVSRR RRSKREAEEE RRRRAAAVIE EVEQRFSTPT
     ALLRGIADAM VEEMERGLRA DPHAPLKMLI SYVDNLPTGD EHGLFYALDL GGTNFRVIRV
     QLGGREKRVV SQQYEEVAIP PHLMVGTSME LFDFIAAELE SFVKTEGEDF HLPEGRQREL
     GFTFSFPVHQ TSISSGTLIK WTKGFSINGT VGEDVVAELS RAMERQGLDM KVTALVNDTV
     GTLAGGRYVD NDVAAAVILG TGTNAAYVEH ANAIPKWTGL LPRSGNMVIN MEWGNFKSER
     LPRSDYDNAL DFESLNPGEQ IYEKMISGMY LGEIVRRILL KLAHDASLFG DVVPTKLEQR
     FILRTPDMSA MHHDTSHDLK HLGAKLKDIL GVADTSLEAR YITLHVCDLV AERGARLAAA
     GIYGILKKLG RDRVPSDGSQ KQRTVIALDG GLYEHYKKFR TCLEATLADL LGEEAASSVV
     VKLANDGSGI GAALLAASHS QYASVE
//