TPK1_HUMAN
ID TPK1_HUMAN Reviewed; 243 AA.
AC Q9H3S4; A8K0T7; D3DWG0; I6L9B8; Q6NUR5; Q9H602;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Thiamin pyrophosphokinase 1 {ECO:0000303|PubMed:11342117};
DE Short=hTPK1 {ECO:0000303|PubMed:11342111};
DE EC=2.7.6.2 {ECO:0000269|PubMed:11342111};
DE AltName: Full=Placental protein 20 {ECO:0000303|PubMed:15664409};
DE Short=PP20 {ECO:0000303|PubMed:15664409};
DE AltName: Full=Thiamine pyrophosphokinase 1 {ECO:0000303|PubMed:11342111};
GN Name=TPK1 {ECO:0000303|PubMed:11342111, ECO:0000312|HGNC:HGNC:17358};
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), FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=11342111; DOI=10.1016/s0167-4781(00)00247-5;
RA Nosaka K., Onozuka M., Kakazu N., Hibi S., Nishimura H., Nishino H.,
RA Abe T.;
RT "Isolation and characterization of a human thiamine pyrophosphokinase
RT cDNA.";
RL Biochim. Biophys. Acta 1517:293-297(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=11342117; DOI=10.1016/s0167-4781(00)00264-5;
RA Zhao R., Gao F., Goldman I.D.;
RT "Molecular cloning of human thiamin pyrophosphokinase.";
RL Biochim. Biophys. Acta 1517:320-322(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=15664409; DOI=10.1016/j.placenta.2004.03.008;
RA Bellyei S., Szigeti A., Boronkai A., Szabo Z., Bene J., Janaky T.,
RA Barna L., Sipos K., Minik O., Kravjak A., Ohmacht R., Melegh B.,
RA Zavodszky P., Than G.N., Sumegi B., Bohn H., Than N.G.;
RT "Cloning, sequencing, structural and molecular biological characterization
RT of placental protein 20 (PP20)/human thiamin pyrophosphokinase (hTPK).";
RL Placenta 26:34-46(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala, and 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
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] (ISOFORMS 1 AND 2).
RC TISSUE=Hypothalamus, and Testis;
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 VARIANTS THMD5 PRO-40; HIS-50 AND SER-219.
RX PubMed=22152682; DOI=10.1016/j.ajhg.2011.11.007;
RA Mayr J.A., Freisinger P., Schlachter K., Rolinski B., Zimmermann F.A.,
RA Scheffner T., Haack T.B., Koch J., Ahting U., Prokisch H., Sperl W.;
RT "Thiamine pyrophosphokinase deficiency in encephalopathic children with
RT defects in the pyruvate oxidation pathway.";
RL Am. J. Hum. Genet. 89:806-812(2011).
CC -!- FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine
CC pyrophosphate. Can also catalyze the phosphorylation of pyrithiamine to
CC pyrithiamine pyrophosphate. {ECO:0000269|PubMed:11342111}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thiamine = AMP + H(+) + thiamine diphosphate;
CC Xref=Rhea:RHEA:11576, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58937, ChEBI:CHEBI:456215; EC=2.7.6.2;
CC Evidence={ECO:0000269|PubMed:11342111};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine diphosphate from thiamine: step 1/1.
CC {ECO:0000269|PubMed:11342111}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:11342111}.
CC -!- INTERACTION:
CC Q9H3S4; O14841: OPLAH; NbExp=3; IntAct=EBI-7054500, EBI-3938544;
CC Q9H3S4; Q9H3S4: TPK1; NbExp=8; IntAct=EBI-7054500, EBI-7054500;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H3S4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H3S4-2; Sequence=VSP_056302, VSP_056303;
CC -!- TISSUE SPECIFICITY: Detected in heart, kidney, testis, small intestine
CC and peripheral blood leukocytes, and at very low levels in a variety of
CC tissues. {ECO:0000269|PubMed:11342111, ECO:0000269|PubMed:11342117}.
CC -!- DISEASE: Thiamine metabolism dysfunction syndrome 5, episodic
CC encephalopathy type (THMD5) [MIM:614458]: An autosomal recessive
CC metabolic disorder due to an inborn error of thiamine metabolism. The
CC phenotype is highly variable, but in general, affected individuals have
CC onset in early childhood of acute encephalopathic episodes associated
CC with increased serum and CSF lactate. These episodes result in
CC progressive neurologic dysfunction manifest as gait disturbances,
CC ataxia, dystonia, and spasticity, which in some cases may result in
CC loss of ability to walk. Cognitive function is usually preserved,
CC although mildly delayed development has been reported. These episodes
CC are usually associated with infection and metabolic decompensation.
CC Some patients may have recovery of some neurologic deficits.
CC {ECO:0000269|PubMed:22152682}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the thiamine pyrophosphokinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15465.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB028138; BAB20326.1; -; mRNA.
DR EMBL; AF297710; AAK01351.1; -; mRNA.
DR EMBL; AY206415; AAO38775.1; -; mRNA.
DR EMBL; AK026374; BAB15465.1; ALT_INIT; mRNA.
DR EMBL; AK289652; BAF82341.1; -; mRNA.
DR EMBL; AC004534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC074384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471146; EAW80091.1; -; Genomic_DNA.
DR EMBL; CH471146; EAW80092.1; -; Genomic_DNA.
DR EMBL; BC040555; AAH40555.1; -; mRNA.
DR EMBL; BC068460; AAH68460.1; -; mRNA.
DR CCDS; CCDS5888.1; -. [Q9H3S4-1]
DR RefSeq; NP_001035947.1; NM_001042482.1.
DR RefSeq; NP_071890.2; NM_022445.3. [Q9H3S4-1]
DR RefSeq; XP_005250027.1; XM_005249970.1. [Q9H3S4-1]
DR RefSeq; XP_011514349.1; XM_011516047.2.
DR RefSeq; XP_011514350.1; XM_011516048.1.
DR RefSeq; XP_011514352.1; XM_011516050.1.
DR RefSeq; XP_016867462.1; XM_017011973.1.
DR RefSeq; XP_016867471.1; XM_017011982.1.
DR RefSeq; XP_016867472.1; XM_017011983.1.
DR RefSeq; XP_016867473.1; XM_017011984.1.
DR RefSeq; XP_016867474.1; XM_017011985.1.
DR RefSeq; XP_016867475.1; XM_017011986.1.
DR PDB; 3S4Y; X-ray; 1.80 A; A/B=15-243.
DR PDBsum; 3S4Y; -.
DR AlphaFoldDB; Q9H3S4; -.
DR SMR; Q9H3S4; -.
DR BioGRID; 117952; 28.
DR IntAct; Q9H3S4; 2.
DR MINT; Q9H3S4; -.
DR STRING; 9606.ENSP00000353165; -.
DR ChEMBL; CHEMBL6155; -.
DR DrugBank; DB04768; Pyrithiamine Pyrophosphate.
DR DrugBank; DB00152; Thiamine.
DR DrugCentral; Q9H3S4; -.
DR iPTMnet; Q9H3S4; -.
DR PhosphoSitePlus; Q9H3S4; -.
DR BioMuta; TPK1; -.
DR DMDM; 44888537; -.
DR EPD; Q9H3S4; -.
DR jPOST; Q9H3S4; -.
DR MassIVE; Q9H3S4; -.
DR MaxQB; Q9H3S4; -.
DR PaxDb; Q9H3S4; -.
DR PeptideAtlas; Q9H3S4; -.
DR PRIDE; Q9H3S4; -.
DR ProteomicsDB; 80748; -. [Q9H3S4-1]
DR Antibodypedia; 18523; 182 antibodies from 24 providers.
DR DNASU; 27010; -.
DR Ensembl; ENST00000360057.7; ENSP00000353165.3; ENSG00000196511.15. [Q9H3S4-1]
DR GeneID; 27010; -.
DR KEGG; hsa:27010; -.
DR MANE-Select; ENST00000360057.7; ENSP00000353165.3; NM_022445.4; NP_071890.2.
DR UCSC; uc003weq.3; human. [Q9H3S4-1]
DR CTD; 27010; -.
DR DisGeNET; 27010; -.
DR GeneCards; TPK1; -.
DR HGNC; HGNC:17358; TPK1.
DR HPA; ENSG00000196511; Tissue enhanced (intestine).
DR MalaCards; TPK1; -.
DR MIM; 606370; gene.
DR MIM; 614458; phenotype.
DR neXtProt; NX_Q9H3S4; -.
DR OpenTargets; ENSG00000196511; -.
DR Orphanet; 293955; Childhood encephalopathy due to thiamine pyrophosphokinase deficiency.
DR PharmGKB; PA38235; -.
DR VEuPathDB; HostDB:ENSG00000196511; -.
DR eggNOG; KOG3153; Eukaryota.
DR GeneTree; ENSGT00390000016016; -.
DR InParanoid; Q9H3S4; -.
DR OMA; HHLYMMT; -.
DR OrthoDB; 1428589at2759; -.
DR PhylomeDB; Q9H3S4; -.
DR TreeFam; TF313224; -.
DR BRENDA; 2.7.6.2; 2681.
DR PathwayCommons; Q9H3S4; -.
DR Reactome; R-HSA-196819; Vitamin B1 (thiamin) metabolism.
DR SignaLink; Q9H3S4; -.
DR UniPathway; UPA00060; UER00597.
DR BioGRID-ORCS; 27010; 34 hits in 1087 CRISPR screens.
DR ChiTaRS; TPK1; human.
DR GeneWiki; TPK1; -.
DR GenomeRNAi; 27010; -.
DR Pharos; Q9H3S4; Tbio.
DR PRO; PR:Q9H3S4; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9H3S4; protein.
DR Bgee; ENSG00000196511; Expressed in secondary oocyte and 151 other tissues.
DR ExpressionAtlas; Q9H3S4; baseline and differential.
DR Genevisible; Q9H3S4; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030975; F:thiamine binding; IEA:InterPro.
DR GO; GO:0004788; F:thiamine diphosphokinase activity; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006772; P:thiamine metabolic process; IEA:Ensembl.
DR CDD; cd07995; TPK; 1.
DR Gene3D; 3.40.50.10240; -; 1.
DR InterPro; IPR006282; Thi_PPkinase.
DR InterPro; IPR016966; Thiamin_pyrophosphokinase_euk.
DR InterPro; IPR007373; Thiamin_PyroPKinase_B1-bd.
DR InterPro; IPR036371; TPK_B1-bd_sf.
DR InterPro; IPR007371; TPK_catalytic.
DR InterPro; IPR036759; TPK_catalytic_sf.
DR Pfam; PF04265; TPK_B1_binding; 1.
DR Pfam; PF04263; TPK_catalytic; 1.
DR PIRSF; PIRSF031057; Thiamin_pyrophosphokinase; 1.
DR SMART; SM00983; TPK_B1_binding; 1.
DR SUPFAM; SSF63862; SSF63862; 1.
DR SUPFAM; SSF63999; SSF63999; 1.
DR TIGRFAMs; TIGR01378; thi_PPkinase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Disease variant; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..243
FT /note="Thiamin pyrophosphokinase 1"
FT /id="PRO_0000072647"
FT VAR_SEQ 1..118
FT /note="MEHAFTPLEPLLSTGNLKYCLVILNQPLDNYFRHLWNKALLRACADGGANRL
FT YDITEGERESFLPEFINGDFDSIRPEVREYYATKGCELISTPDQDHTDFTKCLKMLQKK
FT IEEKDLK -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056302"
FT VAR_SEQ 205..243
FT /note="TNDVLAFGTLVSTSNTYDGSGVVTVETDHPLLWTMAIKS -> RTCDYTRTT
FT WIAKDNPVPRLIRLIRLNHICKVPLAIK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056303"
FT VARIANT 40
FT /note="L -> P (in THMD5; dbSNP:rs387906936)"
FT /evidence="ECO:0000269|PubMed:22152682"
FT /id="VAR_067391"
FT VARIANT 50
FT /note="N -> H (in THMD5; dbSNP:rs387906935)"
FT /evidence="ECO:0000269|PubMed:22152682"
FT /id="VAR_067392"
FT VARIANT 219
FT /note="N -> S (in THMD5; dbSNP:rs371271054)"
FT /evidence="ECO:0000269|PubMed:22152682"
FT /id="VAR_067393"
FT CONFLICT 193
FT /note="M -> S (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="S -> P (in Ref. 4)"
FT /evidence="ECO:0000305"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:3S4Y"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:3S4Y"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:3S4Y"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:3S4Y"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3S4Y"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3S4Y"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:3S4Y"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3S4Y"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:3S4Y"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:3S4Y"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:3S4Y"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:3S4Y"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:3S4Y"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:3S4Y"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:3S4Y"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:3S4Y"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:3S4Y"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:3S4Y"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:3S4Y"
FT STRAND 192..202
FT /evidence="ECO:0007829|PDB:3S4Y"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:3S4Y"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:3S4Y"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:3S4Y"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:3S4Y"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:3S4Y"
SQ SEQUENCE 243 AA; 27265 MW; F7E96F8127CB4FA5 CRC64;
MEHAFTPLEP LLSTGNLKYC LVILNQPLDN YFRHLWNKAL LRACADGGAN RLYDITEGER
ESFLPEFING DFDSIRPEVR EYYATKGCEL ISTPDQDHTD FTKCLKMLQK KIEEKDLKVD
VIVTLGGLAG RFDQIMASVN TLFQATHITP FPIIIIQEES LIYLLQPGKH RLHVDTGMEG
DWCGLIPVGQ PCMQVTTTGL KWNLTNDVLA FGTLVSTSNT YDGSGVVTVE TDHPLLWTMA
IKS
