RBSK_HUMAN
ID RBSK_HUMAN Reviewed; 322 AA.
AC Q9H477; A9UK04; B4DV96;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Ribokinase {ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000303|PubMed:17585908};
DE Short=RK {ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000303|PubMed:17585908};
DE EC=2.7.1.15 {ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000269|PubMed:17585908};
GN Name=RBKS {ECO:0000255|HAMAP-Rule:MF_03215}; Synonyms=RBSK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wightman P.J.;
RL Thesis (2000), University of Edinburgh, United Kingdom.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Li X., Mao Y., Xie Y.;
RT "Cloning and characterization of RBS protein.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=17585908; DOI=10.1016/j.febslet.2007.06.009;
RA Park J., van Koeverden P., Singh B., Gupta R.S.;
RT "Identification and characterization of human ribokinase and comparison of
RT its properties with E. coli ribokinase and human adenosine kinase.";
RL FEBS Lett. 581:3211-3216(2007).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 11-322 IN COMPLEX WITH ADP; SODIUM
RP AND MAGNESIUM.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human ribokinase.";
RL Submitted (JAN-2006) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a reaction
CC requiring ATP and magnesium. The resulting D-ribose-5-phosphate can
CC then be used either for sythesis of nucleotides, histidine, and
CC tryptophan, or as a component of the pentose phosphate pathway.
CC {ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000269|PubMed:17585908}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:13697, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:47013, ChEBI:CHEBI:78346, ChEBI:CHEBI:456216;
CC EC=2.7.1.15; Evidence={ECO:0000255|HAMAP-Rule:MF_03215,
CC ECO:0000269|PubMed:17585908};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03215};
CC Note=Requires a divalent cation, most likely magnesium in vivo, as an
CC electrophilic catalyst to aid phosphoryl group transfer. It is the
CC chelate of the metal and the nucleotide that is the actual substrate.
CC {ECO:0000255|HAMAP-Rule:MF_03215};
CC -!- ACTIVITY REGULATION: Activated by a monovalent cation that binds near,
CC but not in, the active site. The most likely occupant of the site in
CC vivo is potassium. Ion binding induces a conformational change that may
CC alter substrate affinity (By similarity). Competitively inhibited by
CC phosphonoacetic acid, etidronate, 2-carboxethylphosphonic acid, N-
CC (phosphonomethyl)glycine, N-(phosphonomethyl)iminodiacetic acid and
CC clodronate (PubMed:17585908). {ECO:0000255|HAMAP-Rule:MF_03215,
CC ECO:0000269|PubMed:17585908}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.17 mM for ribose (in the presence of 10 mM inorganic phosphate)
CC {ECO:0000269|PubMed:17585908};
CC KM=3.39 mM for ribose (in the presence of 5 mM inorganic phosphate)
CC {ECO:0000269|PubMed:17585908};
CC KM=6.62 mM for ribose (in the presence of 2 mM inorganic phosphate)
CC {ECO:0000269|PubMed:17585908};
CC KM=30.43 mM for ribose (in the presence of 1 mM inorganic phosphate)
CC {ECO:0000269|PubMed:17585908};
CC KM=0.07 mM for ATP (in the presence of 5 mM inorganic phosphate)
CC {ECO:0000269|PubMed:17585908};
CC KM=0.08 mM for ATP (in the presence of 2 mM inorganic phosphate)
CC {ECO:0000269|PubMed:17585908};
CC KM=0.10 mM for ATP (in the presence of 1 mM inorganic phosphate)
CC {ECO:0000269|PubMed:17585908};
CC -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-
CC phosphate from beta-D-ribopyranose: step 2/2. {ECO:0000255|HAMAP-
CC Rule:MF_03215}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A9J6, ECO:0000255|HAMAP-
CC Rule:MF_03215}.
CC -!- INTERACTION:
CC Q9H477; Q96AP0: ACD; NbExp=2; IntAct=EBI-10982959, EBI-717666;
CC Q9H477; Q9H477: RBKS; NbExp=4; IntAct=EBI-10982959, EBI-10982959;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25332,
CC ECO:0000255|HAMAP-Rule:MF_03215}. Nucleus
CC {ECO:0000250|UniProtKB:P25332, ECO:0000255|HAMAP-Rule:MF_03215}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H477-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H477-2; Sequence=VSP_054380;
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. Ribokinase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03215}.
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DR EMBL; AJ404857; CAC12877.1; -; mRNA.
DR EMBL; AY643715; AAT64917.1; -; mRNA.
DR EMBL; AK300989; BAG62608.1; -; mRNA.
DR EMBL; AC021171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017425; AAH17425.1; -; mRNA.
DR CCDS; CCDS1762.1; -. [Q9H477-1]
DR RefSeq; NP_001274509.1; NM_001287580.1.
DR RefSeq; NP_071411.1; NM_022128.2. [Q9H477-1]
DR PDB; 2FV7; X-ray; 2.10 A; A/B=11-322.
DR PDB; 5BYC; X-ray; 1.95 A; A/B=1-322.
DR PDB; 5BYD; X-ray; 2.10 A; A/B=1-322.
DR PDB; 5BYE; X-ray; 1.75 A; A/B=1-322.
DR PDB; 5BYF; X-ray; 2.00 A; A/B=1-322.
DR PDB; 5C3Y; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=1-322.
DR PDB; 5C3Z; X-ray; 1.90 A; A/B=1-322.
DR PDB; 5C40; X-ray; 1.50 A; A/B=1-322.
DR PDB; 5C41; X-ray; 1.95 A; A/B/C/D=1-322.
DR PDB; 6WJZ; X-ray; 1.80 A; A/B=14-322.
DR PDB; 6WK0; X-ray; 2.00 A; A/B/C/D=14-322.
DR PDBsum; 2FV7; -.
DR PDBsum; 5BYC; -.
DR PDBsum; 5BYD; -.
DR PDBsum; 5BYE; -.
DR PDBsum; 5BYF; -.
DR PDBsum; 5C3Y; -.
DR PDBsum; 5C3Z; -.
DR PDBsum; 5C40; -.
DR PDBsum; 5C41; -.
DR PDBsum; 6WJZ; -.
DR PDBsum; 6WK0; -.
DR AlphaFoldDB; Q9H477; -.
DR SMR; Q9H477; -.
DR BioGRID; 122046; 16.
DR IntAct; Q9H477; 8.
DR MINT; Q9H477; -.
DR STRING; 9606.ENSP00000306817; -.
DR iPTMnet; Q9H477; -.
DR PhosphoSitePlus; Q9H477; -.
DR BioMuta; RBKS; -.
DR DMDM; 20139730; -.
DR EPD; Q9H477; -.
DR jPOST; Q9H477; -.
DR MassIVE; Q9H477; -.
DR MaxQB; Q9H477; -.
DR PaxDb; Q9H477; -.
DR PeptideAtlas; Q9H477; -.
DR PRIDE; Q9H477; -.
DR ProteomicsDB; 5255; -.
DR ProteomicsDB; 80790; -. [Q9H477-1]
DR Antibodypedia; 13898; 141 antibodies from 21 providers.
DR DNASU; 64080; -.
DR Ensembl; ENST00000302188.8; ENSP00000306817.3; ENSG00000171174.15. [Q9H477-1]
DR GeneID; 64080; -.
DR KEGG; hsa:64080; -.
DR MANE-Select; ENST00000302188.8; ENSP00000306817.3; NM_022128.3; NP_071411.1.
DR UCSC; uc002rlo.3; human. [Q9H477-1]
DR CTD; 64080; -.
DR DisGeNET; 64080; -.
DR GeneCards; RBKS; -.
DR HGNC; HGNC:30325; RBKS.
DR HPA; ENSG00000171174; Tissue enhanced (liver).
DR MIM; 611132; gene.
DR neXtProt; NX_Q9H477; -.
DR OpenTargets; ENSG00000171174; -.
DR PharmGKB; PA134951602; -.
DR VEuPathDB; HostDB:ENSG00000171174; -.
DR eggNOG; KOG2855; Eukaryota.
DR GeneTree; ENSGT00390000005743; -.
DR HOGENOM; CLU_027634_2_3_1; -.
DR InParanoid; Q9H477; -.
DR OMA; IPWRDEL; -.
DR OrthoDB; 918144at2759; -.
DR PhylomeDB; Q9H477; -.
DR TreeFam; TF105770; -.
DR BRENDA; 2.7.1.15; 2681.
DR PathwayCommons; Q9H477; -.
DR Reactome; R-HSA-71336; Pentose phosphate pathway.
DR SABIO-RK; Q9H477; -.
DR SignaLink; Q9H477; -.
DR SIGNOR; Q9H477; -.
DR UniPathway; UPA00916; UER00889.
DR BioGRID-ORCS; 64080; 12 hits in 1070 CRISPR screens.
DR ChiTaRS; RBKS; human.
DR EvolutionaryTrace; Q9H477; -.
DR GenomeRNAi; 64080; -.
DR Pharos; Q9H477; Tbio.
DR PRO; PR:Q9H477; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H477; protein.
DR Bgee; ENSG00000171174; Expressed in jejunal mucosa and 164 other tissues.
DR ExpressionAtlas; Q9H477; baseline and differential.
DR Genevisible; Q9H477; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004747; F:ribokinase activity; TAS:Reactome.
DR GO; GO:0019303; P:D-ribose catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006098; P:pentose-phosphate shunt; TAS:Reactome.
DR CDD; cd01174; ribokinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_01987; Ribokinase; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011877; D_ribokin.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR002139; Ribo/fructo_kinase.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR PRINTS; PR00990; RIBOKINASE.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR02152; D_ribokin_bact; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Carbohydrate metabolism;
KW Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW Potassium; Reference proteome; Transferase.
FT CHAIN 1..322
FT /note="Ribokinase"
FT /id="PRO_0000080092"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6, ECO:0000255|HAMAP-
FT Rule:MF_03215"
FT BINDING 25..27
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6, ECO:0000255|HAMAP-
FT Rule:MF_03215"
FT BINDING 53..57
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6, ECO:0000255|HAMAP-
FT Rule:MF_03215"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6, ECO:0000255|HAMAP-
FT Rule:MF_03215"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215,
FT ECO:0000269|Ref.7"
FT BINDING 235..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215,
FT ECO:0000269|Ref.7"
FT BINDING 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215,
FT ECO:0000269|Ref.7"
FT BINDING 263
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215,
FT ECO:0000305|Ref.7"
FT BINDING 265
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6, ECO:0000255|HAMAP-
FT Rule:MF_03215"
FT BINDING 268..269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215,
FT ECO:0000269|Ref.7"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6, ECO:0000255|HAMAP-
FT Rule:MF_03215"
FT BINDING 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215,
FT ECO:0000269|Ref.7"
FT BINDING 301
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215,
FT ECO:0000305|Ref.7"
FT BINDING 304
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215,
FT ECO:0000305|Ref.7"
FT BINDING 306
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6, ECO:0000255|HAMAP-
FT Rule:MF_03215"
FT BINDING 310
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215,
FT ECO:0000305|Ref.7"
FT VAR_SEQ 266..322
FT /note="GAGDSFVGALAFYLAYYPNLSLEDMLNRSNFIAAVSVQAAGTQSSYPYKKDL
FT PLTLF -> CRPGSRPKSEAASVKKQKHYK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054380"
FT CONFLICT 101
FT /note="T -> A (in Ref. 2; AAT64917)"
FT /evidence="ECO:0000305"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:5C40"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:5C40"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5C40"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:5C40"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:5C40"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:5C40"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:5C40"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:5C40"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:5C40"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:5C40"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:5C40"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:5C40"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:5C40"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:5C40"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:5C40"
FT HELIX 157..169
FT /evidence="ECO:0007829|PDB:5C40"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:5C40"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:5C40"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:5C40"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:5C40"
FT HELIX 214..225
FT /evidence="ECO:0007829|PDB:5C40"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:5C40"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:5C40"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:5C40"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:5C40"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:5C40"
FT HELIX 267..281
FT /evidence="ECO:0007829|PDB:5C40"
FT HELIX 287..301
FT /evidence="ECO:0007829|PDB:5C40"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:5C40"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:5C40"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:5C40"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:5C40"
SQ SEQUENCE 322 AA; 34143 MW; 50D0E7161F33E94B CRC64;
MAASGEPQRQ WQEEVAAVVV VGSCMTDLVS LTSRLPKTGE TIHGHKFFIG FGGKGANQCV
QAARLGAMTS MVCKVGKDSF GNDYIENLKQ NDISTEFTYQ TKDAATGTAS IIVNNEGQNI
IVIVAGANLL LNTEDLRAAA NVISRAKVMV CQLEITPATS LEALTMARRS GVKTLFNPAP
AIADLDPQFY TLSDVFCCNE SEAEILTGLT VGSAADAGEA ALVLLKRGCQ VVIITLGAEG
CVVLSQTEPE PKHIPTEKVK AVDTTGAGDS FVGALAFYLA YYPNLSLEDM LNRSNFIAAV
SVQAAGTQSS YPYKKDLPLT LF
