ST1B1_HUMAN
ID ST1B1_HUMAN Reviewed; 296 AA.
AC O43704; O15497; Q96FI1; Q9UK34;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Sulfotransferase 1B1 {ECO:0000303|PubMed:9443824};
DE Short=ST1B1;
DE EC=2.8.2.1 {ECO:0000269|PubMed:28084139, ECO:0000269|PubMed:9443824, ECO:0000269|PubMed:9463486};
DE AltName: Full=Sulfotransferase 1B2 {ECO:0000303|PubMed:9443824};
DE AltName: Full=Sulfotransferase family cytosolic 1B member 1;
DE AltName: Full=Thyroid hormone sulfotransferase;
GN Name=SULT1B1; Synonyms=ST1B2 {ECO:0000303|PubMed:9443824}, SULT1B2;
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=9443824; DOI=10.1093/oxfordjournals.jbchem.a021846;
RA Fujita K., Nagata K., Ozawa S., Sasano H., Yamazoe Y.;
RT "Molecular cloning and characterization of rat ST1B1 and human ST1B2 cDNAs,
RT encoding thyroid hormone sulfotransferases.";
RL J. Biochem. 122:1052-1061(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=9463486; DOI=10.1124/mol.53.2.274;
RA Wang J., Falany J.L., Falany C.N.;
RT "Expression and characterization of a novel thyroid hormone-sulfating form
RT of cytosolic sulfotransferase from human liver.";
RL Mol. Pharmacol. 53:274-282(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
RA Falany C.N., Wang J.;
RT "Mapping of the SULT1B2 gene to human chromosome 4q11-13.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=35165440; DOI=10.1038/s41586-022-04396-8;
RA Needham B.D., Funabashi M., Adame M.D., Wang Z., Boktor J.C., Haney J.,
RA Wu W.L., Rabut C., Ladinsky M.S., Hwang S.J., Guo Y., Zhu Q.,
RA Griffiths J.A., Knight R., Bjorkman P.J., Shapiro M.G., Geschwind D.H.,
RA Holschneider D.P., Fischbach M.A., Mazmanian S.K.;
RT "A gut-derived metabolite alters brain activity and anxiety behaviour in
RT mice.";
RL Nature 602:647-653(2022).
RN [6]
RP VARIANT VAL-145, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND CHARACTERIZATION OF VARIANT VAL-145.
RX PubMed=28084139; DOI=10.1080/00498254.2017.1282646;
RA Tibbs Z.E., Guidry A.L., Falany J.L., Kadlubar S.A., Falany C.N.;
RT "A high frequency missense SULT1B1 allelic variant (L145V) selectively
RT expressed in African descendants exhibits altered kinetic properties.";
RL Xenobiotica 48:79-88(2018).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH
RP ADENOSINE-3'-5'-DIPHOSPHATE.
RX PubMed=16804942; DOI=10.1002/prot.21048;
RA Dombrovski L., Dong A., Bochkarev A., Plotnikov A.N.;
RT "Crystal structures of human sulfotransferases SULT1B1 and SULT1C1
RT complexed with the cofactor product adenosine-3'- 5'-diphosphate (PAP).";
RL Proteins 64:1091-1094(2006).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH
RP ADENOSINE-3'-5'-DIPHOSPHATE AND RESVERATROL.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human cytosolic sulfotransferase SULT1B1 in complex
RT with PAP and resveratrol.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of
CC dopamine, small phenols such as 1-naphthol and p-nitrophenol and
CC thyroid hormones, including 3,3'-diiodothyronine, triidothyronine (T3)
CC and reverse triiodothyronine (rT3) (PubMed:28084139, PubMed:9443824,
CC PubMed:9463486). May play a role in gut microbiota-host metabolic
CC interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary tyrosine-
CC derived metabolite produced by gut bacteria. The product 4-EPS crosses
CC the blood-brain barrier and may negatively regulate oligodendrocyte
CC maturation and myelination, affecting the functional connectivity of
CC different brain regions associated with the limbic system
CC (PubMed:35165440). {ECO:0000269|PubMed:28084139,
CC ECO:0000269|PubMed:35165440, ECO:0000269|PubMed:9443824,
CC ECO:0000269|PubMed:9463486}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-
CC bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1;
CC Evidence={ECO:0000269|PubMed:28084139, ECO:0000269|PubMed:9443824,
CC ECO:0000269|PubMed:9463486};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165;
CC Evidence={ECO:0000305|PubMed:9443824};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3,3',5-triiodo-L-thyronine =
CC 3,3',5-triiodo-L-thyronine sulfate + adenosine 3',5'-bisphosphate +
CC H(+); Xref=Rhea:RHEA:67876, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:176511, ChEBI:CHEBI:533015;
CC Evidence={ECO:0000269|PubMed:9443824, ECO:0000269|PubMed:9463486};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67877;
CC Evidence={ECO:0000305|PubMed:9463486};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3,3',5'-triiodo-L-thyronine =
CC 3,3',5'-triiodo-L-thyronine sulfate + adenosine 3',5'-bisphosphate +
CC H(+); Xref=Rhea:RHEA:67888, ChEBI:CHEBI:15378, ChEBI:CHEBI:57261,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:176513;
CC Evidence={ECO:0000269|PubMed:9463486};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67889;
CC Evidence={ECO:0000305|PubMed:9463486};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3,3'-diiodo-L-thyronine = 3,3'-
CC diiodo-L-thyronine sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:67892, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:176514, ChEBI:CHEBI:176515;
CC Evidence={ECO:0000269|PubMed:9463486};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67893;
CC Evidence={ECO:0000305|PubMed:9463486};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-
CC bisphosphate + dopamine 3-O-sulfate + H(+); Xref=Rhea:RHEA:67880,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:59905, ChEBI:CHEBI:133524;
CC Evidence={ECO:0000269|PubMed:9443824};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67881;
CC Evidence={ECO:0000305|PubMed:9443824};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-
CC bisphosphate + dopamine 4-O-sulfate + H(+); Xref=Rhea:RHEA:67884,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:59905, ChEBI:CHEBI:133529;
CC Evidence={ECO:0000269|PubMed:9443824};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67885;
CC Evidence={ECO:0000305|PubMed:9443824};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 4-ethylphenol = 4-ethylphenyl
CC sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:70607,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:49584, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:133681;
CC Evidence={ECO:0000269|PubMed:35165440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70608;
CC Evidence={ECO:0000305|PubMed:35165440};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=63.5 uM for 3,3',5-triiodo-L-thyronine (T3)
CC {ECO:0000269|PubMed:9443824};
CC KM=7.2 uM for p-nitrophenol {ECO:0000269|PubMed:28084139};
CC KM=24.1 uM for p-nitrophenol {ECO:0000269|PubMed:9443824};
CC KM=1.4 uM for 1-naphtol {ECO:0000269|PubMed:28084139};
CC KM=141 uM for 3,3',5'-triiodo-L-thyronine (rT3)
CC {ECO:0000269|PubMed:9463486};
CC KM=1.4 uM for 3,3'-diiodo-L-thyronine (T2)
CC {ECO:0000269|PubMed:9463486};
CC KM=1.2 uM for PAPS {ECO:0000269|PubMed:9463486};
CC KM=1.3 uM for PAPS {ECO:0000269|PubMed:28084139};
CC KM=23 uM for thyroxine (T4) {ECO:0000269|PubMed:9463486};
CC Vmax=5.1 nmol/min/mg enzyme with p-nitrophenol as substrate
CC {ECO:0000269|PubMed:28084139};
CC -!- INTERACTION:
CC O43704; Q9NUX5: POT1; NbExp=2; IntAct=EBI-10179062, EBI-752420;
CC O43704; O00560: SDCBP; NbExp=3; IntAct=EBI-10179062, EBI-727004;
CC O43704; Q06520: SULT2A1; NbExp=6; IntAct=EBI-10179062, EBI-3921363;
CC O43704; O00204: SULT2B1; NbExp=9; IntAct=EBI-10179062, EBI-749441;
CC O43704; P26639: TARS1; NbExp=3; IntAct=EBI-10179062, EBI-1042683;
CC O43704; P31930: UQCRC1; NbExp=3; IntAct=EBI-10179062, EBI-1052596;
CC O43704; P61758: VBP1; NbExp=3; IntAct=EBI-10179062, EBI-357430;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9443824,
CC ECO:0000269|PubMed:9463486}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver, peripheral blood
CC leukocytes, colon (mucosal lining), small intestine (jejunum) and
CC spleen. A lesser expression was observed in the lung, placenta and
CC thymus. {ECO:0000269|PubMed:9463486}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; D89479; BAA24547.1; -; mRNA.
DR EMBL; U95726; AAB65154.1; -; mRNA.
DR EMBL; BC010895; AAH10895.1; -; mRNA.
DR EMBL; AF184894; AAF05917.1; -; Genomic_DNA.
DR CCDS; CCDS3530.1; -.
DR PIR; JC5885; JC5885.
DR RefSeq; NP_055280.2; NM_014465.3.
DR RefSeq; XP_005265734.1; XM_005265677.3.
DR PDB; 2Z5F; X-ray; 2.10 A; A/B=1-296.
DR PDB; 3CKL; X-ray; 2.00 A; A/B=1-296.
DR PDBsum; 2Z5F; -.
DR PDBsum; 3CKL; -.
DR AlphaFoldDB; O43704; -.
DR SMR; O43704; -.
DR BioGRID; 118108; 5.
DR IntAct; O43704; 7.
DR STRING; 9606.ENSP00000308770; -.
DR ChEMBL; CHEMBL1743294; -.
DR DrugBank; DB01812; Adenosine 3',5'-diphosphate.
DR DrugBank; DB00714; Apomorphine.
DR DrugBank; DB14635; Curcumin sulfate.
DR DrugBank; DB12471; Ibrexafungerp.
DR DrugBank; DB00968; Methyldopa.
DR DrugBank; DB00960; Pindolol.
DR DrugBank; DB00871; Terbutaline.
DR DrugBank; DB09100; Thyroid, porcine.
DR GlyGen; O43704; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43704; -.
DR PhosphoSitePlus; O43704; -.
DR BioMuta; SULT1B1; -.
DR EPD; O43704; -.
DR jPOST; O43704; -.
DR MassIVE; O43704; -.
DR MaxQB; O43704; -.
DR PaxDb; O43704; -.
DR PeptideAtlas; O43704; -.
DR PRIDE; O43704; -.
DR ProteomicsDB; 49124; -.
DR Antibodypedia; 951; 218 antibodies from 25 providers.
DR DNASU; 27284; -.
DR Ensembl; ENST00000310613.8; ENSP00000308770.2; ENSG00000173597.9.
DR GeneID; 27284; -.
DR KEGG; hsa:27284; -.
DR MANE-Select; ENST00000310613.8; ENSP00000308770.2; NM_014465.4; NP_055280.2.
DR UCSC; uc003hen.4; human.
DR CTD; 27284; -.
DR DisGeNET; 27284; -.
DR GeneCards; SULT1B1; -.
DR HGNC; HGNC:17845; SULT1B1.
DR HPA; ENSG00000173597; Tissue enhanced (intestine, stomach).
DR MIM; 608436; gene.
DR neXtProt; NX_O43704; -.
DR OpenTargets; ENSG00000173597; -.
DR PharmGKB; PA415; -.
DR VEuPathDB; HostDB:ENSG00000173597; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000161848; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; O43704; -.
DR OMA; CAFVSNW; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; O43704; -.
DR TreeFam; TF321745; -.
DR BRENDA; 2.8.2.1; 2681.
DR BRENDA; 2.8.2.2; 2681.
DR PathwayCommons; O43704; -.
DR Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
DR SignaLink; O43704; -.
DR BioGRID-ORCS; 27284; 7 hits in 1074 CRISPR screens.
DR EvolutionaryTrace; O43704; -.
DR GeneWiki; SULT1B1; -.
DR GenomeRNAi; 27284; -.
DR Pharos; O43704; Tbio.
DR PRO; PR:O43704; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O43704; protein.
DR Bgee; ENSG00000173597; Expressed in rectum and 111 other tissues.
DR ExpressionAtlas; O43704; baseline and differential.
DR Genevisible; O43704; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IDA:CAFA.
DR GO; GO:0006576; P:cellular biogenic amine metabolic process; TAS:ProtInc.
DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR GO; GO:0006068; P:ethanol catabolic process; IDA:CAFA.
DR GO; GO:0009812; P:flavonoid metabolic process; IDA:BHF-UCL.
DR GO; GO:0018958; P:phenol-containing compound metabolic process; IDA:UniProtKB.
DR GO; GO:0051923; P:sulfation; IDA:UniProtKB.
DR GO; GO:0042403; P:thyroid hormone metabolic process; IDA:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:BHF-UCL.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR InterPro; IPR033289; SULT1B1.
DR PANTHER; PTHR11783:SF14; PTHR11783:SF14; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..296
FT /note="Sulfotransferase 1B1"
FT /id="PRO_0000085161"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 48..53
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16804942, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:2Z5F, ECO:0007744|PDB:3CKL"
FT BINDING 107..109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16804942, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:2Z5F, ECO:0007744|PDB:3CKL"
FT BINDING 139
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16804942, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:2Z5F, ECO:0007744|PDB:3CKL"
FT BINDING 194
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16804942, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:2Z5F, ECO:0007744|PDB:3CKL"
FT BINDING 228..233
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16804942, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:2Z5F, ECO:0007744|PDB:3CKL"
FT BINDING 258..260
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16804942, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:2Z5F, ECO:0007744|PDB:3CKL"
FT VARIANT 145
FT /note="L -> V (reduces Vmax with p-nitrophenol as
FT substrate; binds to adenosine 3',5'-bisphosphate with a
FT dissociation constant (Kd) value increases 4-fold compared
FT with wild-type; binds to PAPS with a dissociation constant
FT (Kd) value similar to wild-type; dbSNP:rs11569736)"
FT /evidence="ECO:0000269|PubMed:28084139"
FT /id="VAR_085176"
FT CONFLICT 183
FT /note="K -> R (in Ref. 3; AAH10895)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="E -> G (in Ref. 1; BAA24547)"
FT /evidence="ECO:0000305"
FT TURN 5..9
FT /evidence="ECO:0007829|PDB:2Z5F"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:3CKL"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:3CKL"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:3CKL"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:3CKL"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3CKL"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:3CKL"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:3CKL"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:3CKL"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:3CKL"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:2Z5F"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:3CKL"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:3CKL"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3CKL"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:3CKL"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:3CKL"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:3CKL"
FT HELIX 156..165
FT /evidence="ECO:0007829|PDB:3CKL"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:3CKL"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:3CKL"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:3CKL"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:3CKL"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:3CKL"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:3CKL"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:3CKL"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:3CKL"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:3CKL"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:3CKL"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:3CKL"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:3CKL"
SQ SEQUENCE 296 AA; 34899 MW; AFEB61B21DBD782C CRC64;
MLSPKDILRK DLKLVHGYPM TCAFASNWEK IEQFHSRPDD IVIATYPKSG TTWVSEIIDM
ILNDGDIEKC KRGFITEKVP MLEMTLPGLR TSGIEQLEKN PSPRIVKTHL PTDLLPKSFW
ENNCKMIYLA RNAKDVSVSY YHFDLMNNLQ PFPGTWEEYL EKFLTGKVAY GSWFTHVKNW
WKKKEEHPIL FLYYEDMKEN PKEEIKKIIR FLEKNLNDEI LDRIIHHTSF EVMKDNPLVN
YTHLPTTVMD HSKSPFMRKG TAGDWKNYFT VAQNEKFDAI YETEMSKTAL QFRTEI
