ST1C2_HUMAN
ID ST1C2_HUMAN Reviewed; 296 AA.
AC O00338; B2R813; Q53SG4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Sulfotransferase 1C2;
DE Short=ST1C2;
DE EC=2.8.2.1 {ECO:0000269|PubMed:10481272, ECO:0000269|PubMed:10783263, ECO:0000269|PubMed:9852044};
DE AltName: Full=Sulfotransferase 1C1;
DE Short=SULT1C#1 {ECO:0000303|PubMed:9852044};
DE AltName: Full=humSULTC2;
GN Name=SULT1C2; Synonyms=SULT1C1;
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].
RC TISSUE=Fetal liver, and Fetal spleen;
RX PubMed=9169148; DOI=10.1006/geno.1997.4683;
RA Her C., Kaur G.P., Athwal R.S., Weinshilboum R.M.;
RT "Human sulfotransferase SULT1C1: cDNA cloning, tissue-specific expression,
RT and chromosomal localization.";
RL Genomics 41:467-470(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal liver;
RX PubMed=9635888; DOI=10.1093/carcin/19.5.951;
RA Yoshinari K., Nagata K., Shimada M., Yamazoe Y.;
RT "Molecular characterization of ST1C1-related human sulfotransferase.";
RL Carcinogenesis 19:951-953(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], 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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Stomach;
RX PubMed=10481272; DOI=10.1016/s1357-2725(99)00038-2;
RA Hehonah N., Zhu X., Brix L., Bolton-Grob R., Barnett A., Windmill K.,
RA McManus M.;
RT "Molecular cloning, expression, localisation and functional
RT characterisation of a rabbit SULT1C2 sulfotransferase.";
RL Int. J. Biochem. Cell Biol. 31:869-882(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, CATALYTIC ACTIVITY, AND
RP FUNCTION.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC TISSUE=Kidney;
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 [8]
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 [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 3-296 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).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation.
CC Sulfonates p-nitrophenol, a small phenolic compond. Does not sulfonate
CC steroids, dopamine, acetaminophen, or alpha-naphthol (PubMed:9852044,
CC PubMed:10783263, PubMed:10481272). Catalyzes the sulfonation of the
CC carcinogenic N-Hydroxy-2-acetylaminofluorene leading to highly reactive
CC intermediates capable of forming DNA adducts, potentially resulting in
CC mutagenesis (PubMed:9852044). {ECO:0000269|PubMed:10481272,
CC ECO:0000269|PubMed:10783263, 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:10481272, ECO:0000269|PubMed:10783263,
CC ECO:0000269|PubMed:9852044};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.3 mM for p-nitrophenol {ECO:0000269|PubMed:10481272};
CC Vmax=0.005 nmol/min/mg enzyme with p-nitrophenol as substrate
CC {ECO:0000269|PubMed:10481272};
CC -!- INTERACTION:
CC O00338; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-3913419, EBI-717399;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O46503}.
CC Lysosome {ECO:0000250|UniProtKB:Q9WUW8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Short;
CC IsoId=O00338-1; Sequence=Displayed;
CC Name=Long;
CC IsoId=O00338-2; Sequence=VSP_006303;
CC -!- TISSUE SPECIFICITY: Found in adult stomach, kidney and thyroid gland,
CC and in fetal kidney and liver.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; U66036; AAC51285.1; -; mRNA.
DR EMBL; AB008164; BAA28346.1; -; mRNA.
DR EMBL; AF026303; AAC00409.1; -; mRNA.
DR EMBL; AF186251; AAF72799.1; -; mRNA.
DR EMBL; AF186252; AAF72800.1; -; mRNA.
DR EMBL; AF186253; AAF72801.1; -; mRNA.
DR EMBL; AF186254; AAF72802.1; -; mRNA.
DR EMBL; AF186255; AAF72803.1; -; mRNA.
DR EMBL; AF186256; AAF72804.1; -; mRNA.
DR EMBL; AF186262; AAF72805.1; -; Genomic_DNA.
DR EMBL; AF186258; AAF72805.1; JOINED; Genomic_DNA.
DR EMBL; AF186260; AAF72805.1; JOINED; Genomic_DNA.
DR EMBL; AF186261; AAF72805.1; JOINED; Genomic_DNA.
DR EMBL; AF186262; AAF72806.1; -; Genomic_DNA.
DR EMBL; AF186258; AAF72806.1; JOINED; Genomic_DNA.
DR EMBL; AF186259; AAF72806.1; JOINED; Genomic_DNA.
DR EMBL; AF186260; AAF72806.1; JOINED; Genomic_DNA.
DR EMBL; AF186261; AAF72806.1; JOINED; Genomic_DNA.
DR EMBL; BT006951; AAP35597.1; -; mRNA.
DR EMBL; AK313193; BAG36010.1; -; mRNA.
DR EMBL; AC019100; AAY14790.1; -; Genomic_DNA.
DR EMBL; CH471182; EAW53889.1; -; Genomic_DNA.
DR EMBL; CH471182; EAW53890.1; -; Genomic_DNA.
DR EMBL; BC005353; AAH05353.1; -; mRNA.
DR CCDS; CCDS2075.1; -. [O00338-1]
DR CCDS; CCDS2076.1; -. [O00338-2]
DR RefSeq; NP_001047.1; NM_001056.3. [O00338-1]
DR RefSeq; NP_789795.1; NM_176825.2. [O00338-2]
DR PDB; 3BFX; X-ray; 1.80 A; A/B=3-296.
DR PDBsum; 3BFX; -.
DR AlphaFoldDB; O00338; -.
DR SMR; O00338; -.
DR BioGRID; 112688; 16.
DR IntAct; O00338; 9.
DR STRING; 9606.ENSP00000319622; -.
DR ChEMBL; CHEMBL1743295; -.
DR DrugBank; DB12471; Ibrexafungerp.
DR DrugBank; DB00968; Methyldopa.
DR DrugBank; DB00960; Pindolol.
DR DrugBank; DB00871; Terbutaline.
DR DrugBank; DB09100; Thyroid, porcine.
DR iPTMnet; O00338; -.
DR PhosphoSitePlus; O00338; -.
DR BioMuta; SULT1C2; -.
DR EPD; O00338; -.
DR jPOST; O00338; -.
DR MassIVE; O00338; -.
DR MaxQB; O00338; -.
DR PeptideAtlas; O00338; -.
DR PRIDE; O00338; -.
DR ProteomicsDB; 47854; -. [O00338-1]
DR ProteomicsDB; 47855; -. [O00338-2]
DR Antibodypedia; 1928; 312 antibodies from 27 providers.
DR DNASU; 6819; -.
DR Ensembl; ENST00000251481.11; ENSP00000251481.6; ENSG00000198203.10. [O00338-1]
DR Ensembl; ENST00000326853.9; ENSP00000319622.5; ENSG00000198203.10. [O00338-2]
DR GeneID; 6819; -.
DR KEGG; hsa:6819; -.
DR MANE-Select; ENST00000251481.11; ENSP00000251481.6; NM_001056.4; NP_001047.1.
DR UCSC; uc002tdx.3; human. [O00338-1]
DR CTD; 6819; -.
DR DisGeNET; 6819; -.
DR GeneCards; SULT1C2; -.
DR HGNC; HGNC:11456; SULT1C2.
DR HPA; ENSG00000198203; Tissue enhanced (kidney, stomach).
DR MIM; 602385; gene.
DR neXtProt; NX_O00338; -.
DR OpenTargets; ENSG00000198203; -.
DR PharmGKB; PA164742557; -.
DR VEuPathDB; HostDB:ENSG00000198203; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000160912; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; O00338; -.
DR OMA; FQRMNQM; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; O00338; -.
DR TreeFam; TF321745; -.
DR PathwayCommons; O00338; -.
DR Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
DR SignaLink; O00338; -.
DR BioGRID-ORCS; 6819; 10 hits in 1070 CRISPR screens.
DR EvolutionaryTrace; O00338; -.
DR GeneWiki; SULT1C2; -.
DR GenomeRNAi; 6819; -.
DR Pharos; O00338; Tbio.
DR PRO; PR:O00338; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O00338; protein.
DR Bgee; ENSG00000198203; Expressed in pylorus and 146 other tissues.
DR ExpressionAtlas; O00338; baseline and differential.
DR Genevisible; O00338; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:BHF-UCL.
DR GO; GO:0009308; P:amine metabolic process; TAS:ProtInc.
DR GO; GO:0051923; P:sulfation; 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; Lysosome; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..296
FT /note="Sulfotransferase 1C2"
FT /id="PRO_0000085132"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 49..54
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16804942"
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"
FT BINDING 139
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16804942"
FT BINDING 194
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16804942"
FT BINDING 228..233
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16804942"
FT BINDING 256..260
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16804942"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D939"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D939"
FT VAR_SEQ 93..113
FT /note="GVEKAKAMPSPRILKTHLSTQ -> ETGFHHVAQAGLKLLSSSNPPASTSQS
FT AKITD (in isoform Long)"
FT /evidence="ECO:0000305"
FT /id="VSP_006303"
FT VARIANT 128
FT /note="Y -> H (in dbSNP:rs17036091)"
FT /id="VAR_021986"
FT VARIANT 255
FT /note="S -> A (in dbSNP:rs17036104)"
FT /id="VAR_021987"
FT VARIANT 282
FT /note="R -> T (in dbSNP:rs45515691)"
FT /id="VAR_061888"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3BFX"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:3BFX"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:3BFX"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:3BFX"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:3BFX"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:3BFX"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:3BFX"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:3BFX"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3BFX"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:3BFX"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:3BFX"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:3BFX"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:3BFX"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:3BFX"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:3BFX"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:3BFX"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:3BFX"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:3BFX"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:3BFX"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:3BFX"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:3BFX"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:3BFX"
SQ SEQUENCE 296 AA; 34880 MW; 3DC01C8A8ED61EFD CRC64;
MALTSDLGKQ IKLKEVEGTL LQPATVDNWS QIQSFEAKPD DLLICTYPKA GTTWIQEIVD
MIEQNGDVEK CQRAIIQHRH PFIEWARPPQ PSGVEKAKAM PSPRILKTHL STQLLPPSFW
ENNCKFLYVA RNAKDCMVSY YHFQRMNHML PDPGTWEEYF ETFINGKVVW GSWFDHVKGW
WEMKDRHQIL FLFYEDIKRD PKHEIRKVMQ FMGKKVDETV LDKIVQETSF EKMKENPMTN
RSTVSKSILD QSISSFMRKG TVGDWKNHFT VAQNERFDEI YRRKMEGTSI NFCMEL
