ST1C4_HUMAN
ID ST1C4_HUMAN Reviewed; 302 AA.
AC O75897; Q069I8; Q08AS5; Q53S63;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Sulfotransferase 1C4;
DE Short=ST1C4;
DE EC=2.8.2.1 {ECO:0000269|PubMed:17425406, ECO:0000269|PubMed:26948952, ECO:0000269|PubMed:28222028, ECO:0000269|PubMed:9852044};
DE AltName: Full=Sulfotransferase 1C2 {ECO:0000303|PubMed:17425406};
DE Short=SULT1C#2;
GN Name=SULT1C4 {ECO:0000312|HGNC:HGNC:11457};
GN Synonyms=SULT1C2 {ECO:0000303|PubMed:17425406};
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), VARIANT GLU-5, TISSUE SPECIFICITY,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Fetal lung;
RX PubMed=9852044; DOI=10.1074/jbc.273.51.33929;
RA Sakakibara Y., Yanagisawa K., Katafuchi J., Ringer D.P., Takami Y.,
RA Nakayama T., Suiko M., Liu M.-C.;
RT "Molecular cloning, expression, and characterization of novel human SULT1C
RT sulfotransferases that catalyze the sulfonation of N-hydroxy-2-
RT acetylaminofluorene.";
RL J. Biol. Chem. 273:33929-33935(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10783263; DOI=10.1006/geno.2000.6150;
RA Freimuth R.R., Raftogianis R.B., Wood T.C., Moon E., Kim U.-J., Xu J.,
RA Siciliano M.J., Weinshilboum R.M.;
RT "Human sulfotransferases SULT1C1 and SULT1C2: cDNA characterization, gene
RT cloning, and chromosomal localization.";
RL Genomics 65:157-165(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Heart;
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 [GENOMIC DNA], AND VARIANTS GLU-5 AND MET-68.
RG NIEHS SNPs program;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 7-302 IN COMPLEX WITH
RP ADENOSINE-3'-5'-DIPHOSPHATE (PAPS) AND PENTACHLOROPHENOL (PCP), FUNCTION,
RP AND CATALYTIC ACTIVITY.
RX PubMed=17425406; DOI=10.1371/journal.pbio.0050097;
RA Allali-Hassani A., Pan P.W., Dombrovski L., Najmanovich R., Tempel W.,
RA Dong A., Loppnau P., Martin F., Thornton J., Edwards A.M., Bochkarev A.,
RA Plotnikov A.N., Vedadi M., Arrowsmith C.H.;
RT "Structural and chemical profiling of the human cytosolic
RT sulfotransferases.";
RL PLoS Biol. 5:E97-E97(2007).
RN [9]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26948952; DOI=10.1016/j.dmpk.2016.01.003;
RA Luo L., Zhou C., Hui Y., Kurogi K., Sakakibara Y., Suiko M., Liu M.C.;
RT "Human cytosolic sulfotransferase SULT1C4 mediates the sulfation of
RT doxorubicin and epirubicin.";
RL Drug Metab. Pharmacokinet. 31:163-166(2016).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=28222028; DOI=10.1515/hmbci-2016-0053;
RA Guidry A.L., Tibbs Z.E., Runge-Morris M., Falany C.N.;
RT "Expression, purification and characterization of human cytosolic
RT sulfotransferase (SULT) 1C4.";
RL Horm. Mol. Bio. Clin. Investig. 29:27-36(2017).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of
CC phenolic compounds. Can also sulfonate estrogenic compounds, however,
CC the dietary flavonoids (phytoestrogen) and environmental estrogens,
CC like bisphenol A are better substrates than 17beta-estradiol (E2)
CC (PubMed:17425406, PubMed:28222028, PubMed:9852044, PubMed:26948952).
CC Mediates the sulfation of doxorubicin and its analog epirubicin, two
CC antitumor anthracyclines (PubMed:26948952).
CC {ECO:0000269|PubMed:17425406, ECO:0000269|PubMed:26948952,
CC ECO:0000269|PubMed:28222028, ECO:0000269|PubMed:9852044}.
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:17425406, ECO:0000269|PubMed:26948952,
CC ECO:0000269|PubMed:28222028, ECO:0000269|PubMed:9852044};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165;
CC Evidence={ECO:0000305|PubMed:28222028};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + 3'-phosphoadenylyl sulfate = 17beta-
CC estradiol 3-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52372, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136582;
CC Evidence={ECO:0000269|PubMed:28222028};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373;
CC Evidence={ECO:0000305|PubMed:28222028};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + bisphenol A = adenosine 3',5'-
CC bisphosphate + bisphenyl A sulfate + H(+); Xref=Rhea:RHEA:66580,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33216, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:167171;
CC Evidence={ECO:0000269|PubMed:28222028};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66581;
CC Evidence={ECO:0000305|PubMed:28222028};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.0 uM for PAPS {ECO:0000269|PubMed:28222028};
CC KM=36.2 uM for 17beta-estradiol (E2) {ECO:0000269|PubMed:28222028};
CC KM=3.3 uM for genistein {ECO:0000269|PubMed:28222028};
CC KM=10.5 uM for daidzein {ECO:0000269|PubMed:28222028};
CC KM=0.9 uM for apigenin {ECO:0000269|PubMed:28222028};
CC KM=0.97 uM for chrysin {ECO:0000269|PubMed:28222028};
CC KM=32.8 uM for bisphenol A {ECO:0000269|PubMed:28222028};
CC KM=1.1 uM for 1-naphthol {ECO:0000269|PubMed:28222028};
CC Vmax=5.04 nmol/min/ng enzyme with doxorubicin as substrate
CC {ECO:0000269|PubMed:26948952};
CC Vmax=1.85 nmol/min/ng enzyme with epirubicin as substrate
CC {ECO:0000269|PubMed:26948952};
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:28222028};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28222028}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75897-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75897-2; Sequence=VSP_056255;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in fetal lung and kidney
CC and at low levels in fetal heart, adult kidney, ovary and spinal chord.
CC {ECO:0000269|PubMed:9852044}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/sult1c2/";
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DR EMBL; AF055584; AAC95519.1; -; mRNA.
DR EMBL; AF186263; AAF72810.1; -; Genomic_DNA.
DR EMBL; AK297851; BAG60183.1; -; mRNA.
DR EMBL; DQ987914; ABI75348.1; -; Genomic_DNA.
DR EMBL; AC068941; AAY14742.1; -; Genomic_DNA.
DR EMBL; CH471182; EAW53886.1; -; Genomic_DNA.
DR EMBL; BC125043; AAI25044.1; -; mRNA.
DR CCDS; CCDS2077.1; -. [O75897-1]
DR CCDS; CCDS82492.1; -. [O75897-2]
DR RefSeq; NP_001308699.1; NM_001321770.1. [O75897-2]
DR RefSeq; NP_006579.2; NM_006588.3. [O75897-1]
DR PDB; 2AD1; X-ray; 2.00 A; A=7-302.
DR PDB; 2GWH; X-ray; 1.80 A; A/B=7-302.
DR PDBsum; 2AD1; -.
DR PDBsum; 2GWH; -.
DR AlphaFoldDB; O75897; -.
DR SMR; O75897; -.
DR BioGRID; 118082; 133.
DR IntAct; O75897; 2.
DR STRING; 9606.ENSP00000272452; -.
DR ChEMBL; CHEMBL1743296; -.
DR DrugBank; DB14635; Curcumin sulfate.
DR DrugBank; DB12471; Ibrexafungerp.
DR DrugBank; DB00968; Methyldopa.
DR DrugBank; DB00960; Pindolol.
DR DrugBank; DB00871; Terbutaline.
DR iPTMnet; O75897; -.
DR PhosphoSitePlus; O75897; -.
DR BioMuta; SULT1C4; -.
DR MassIVE; O75897; -.
DR MaxQB; O75897; -.
DR PaxDb; O75897; -.
DR PeptideAtlas; O75897; -.
DR PRIDE; O75897; -.
DR ProteomicsDB; 50251; -. [O75897-1]
DR ProteomicsDB; 58685; -.
DR Antibodypedia; 33063; 96 antibodies from 22 providers.
DR DNASU; 27233; -.
DR Ensembl; ENST00000272452.7; ENSP00000272452.2; ENSG00000198075.10. [O75897-1]
DR Ensembl; ENST00000409309.3; ENSP00000387225.3; ENSG00000198075.10. [O75897-2]
DR GeneID; 27233; -.
DR KEGG; hsa:27233; -.
DR MANE-Select; ENST00000272452.7; ENSP00000272452.2; NM_006588.4; NP_006579.2.
DR UCSC; uc002tea.2; human. [O75897-1]
DR CTD; 27233; -.
DR GeneCards; SULT1C4; -.
DR HGNC; HGNC:11457; SULT1C4.
DR HPA; ENSG00000198075; Low tissue specificity.
DR MIM; 608357; gene.
DR neXtProt; NX_O75897; -.
DR OpenTargets; ENSG00000198075; -.
DR PharmGKB; PA162405070; -.
DR VEuPathDB; HostDB:ENSG00000198075; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000157101; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; O75897; -.
DR OMA; DLYESFC; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; O75897; -.
DR TreeFam; TF321745; -.
DR BRENDA; 2.8.2.1; 2681.
DR PathwayCommons; O75897; -.
DR Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
DR Reactome; R-HSA-9753281; Paracetamol ADME.
DR SignaLink; O75897; -.
DR BioGRID-ORCS; 27233; 6 hits in 1059 CRISPR screens.
DR EvolutionaryTrace; O75897; -.
DR GeneWiki; SULT1C4; -.
DR GenomeRNAi; 27233; -.
DR Pharos; O75897; Tbio.
DR PRO; PR:O75897; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O75897; protein.
DR Bgee; ENSG00000198075; Expressed in ventricular zone and 96 other tissues.
DR Genevisible; O75897; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
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:UniProtKB.
DR GO; GO:0044598; P:doxorubicin metabolic process; IDA:UniProtKB.
DR GO; GO:0006068; P:ethanol catabolic process; IDA:CAFA.
DR GO; GO:0009812; P:flavonoid metabolic process; IDA:UniProtKB.
DR GO; GO:0051923; P:sulfation; IDA:BHF-UCL.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Reference proteome;
KW Transferase.
FT CHAIN 1..302
FT /note="Sulfotransferase 1C4"
FT /id="PRO_0000085137"
FT ACT_SITE 115
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 55..60
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:17425406"
FT BINDING 113..115
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:17425406"
FT BINDING 145
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:17425406"
FT BINDING 200
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:17425406"
FT BINDING 234..239
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:17425406"
FT BINDING 262..266
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:17425406"
FT VAR_SEQ 99..173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_056255"
FT VARIANT 5
FT /note="D -> E (in dbSNP:rs1402467)"
FT /evidence="ECO:0000269|PubMed:9852044, ECO:0000269|Ref.4"
FT /id="VAR_025404"
FT VARIANT 68
FT /note="I -> M (in dbSNP:rs41322445)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_061889"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:2GWH"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:2GWH"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:2GWH"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:2GWH"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:2GWH"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:2GWH"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 207..218
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:2GWH"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:2GWH"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:2GWH"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 277..290
FT /evidence="ECO:0007829|PDB:2GWH"
FT HELIX 295..299
FT /evidence="ECO:0007829|PDB:2GWH"
SQ SEQUENCE 302 AA; 35520 MW; 905E1820A6E222F3 CRC64;
MALHDMEDFT FDGTKRLSVN YVKGILQPTD TCDIWDKIWN FQAKPDDLLI STYPKAGTTW
TQEIVELIQN EGDVEKSKRA PTHQRFPFLE MKIPSLGSGL EQAHAMPSPR ILKTHLPFHL
LPPSLLEKNC KIIYVARNPK DNMVSYYHFQ RMNKALPAPG TWEEYFETFL AGKVCWGSWH
EHVKGWWEAK DKHRILYLFY EDMKKNPKHE IQKLAEFIGK KLDDKVLDKI VHYTSFDVMK
QNPMANYSSI PAEIMDHSIS PFMRKGAVGD WKKHFTVAQN ERFDEDYKKK MTDTRLTFHF
QF
