PANK3_HUMAN
ID PANK3_HUMAN Reviewed; 370 AA.
AC Q9H999; D3DQL1; Q53FJ9; Q7RTX4;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Pantothenate kinase 3;
DE Short=hPanK3;
DE EC=2.7.1.33 {ECO:0000269|PubMed:17631502, ECO:0000269|PubMed:20797618, ECO:0000269|PubMed:27555321, ECO:0000269|PubMed:30927326};
DE AltName: Full=Pantothenic acid kinase 3;
GN Name=PANK3;
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 [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Synovium;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=11479594; DOI=10.1038/ng572;
RA Zhou B., Westaway S.K., Levinson B., Johnson M.A., Gitschier J.,
RA Hayflick S.J.;
RT "A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-
RT Spatz syndrome.";
RL Nat. Genet. 28:345-349(2001).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=23152917; DOI=10.1371/journal.pone.0049509;
RA Alfonso-Pecchio A., Garcia M., Leonardi R., Jackowski S.;
RT "Compartmentalization of mammalian pantothenate kinases.";
RL PLoS ONE 7:e49509-e49509(2012).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND MUTAGENESIS OF GLU-138 AND ARG-207.
RX PubMed=30927326; DOI=10.1002/pro.3611;
RA Yao J., Subramanian C., Rock C.O., Jackowski S.;
RT "Human pantothenate kinase 4 is a pseudo-pantothenate kinase.";
RL Protein Sci. 28:1031-1047(2019).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 12-368 IN COMPLEX WITH
RP ACETYL-COA, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=17631502; DOI=10.1074/jbc.m701915200;
RA Hong B.S., Senisterra G., Rabeh W.M., Vedadi M., Leonardi R., Zhang Y.M.,
RA Rock C.O., Jackowski S., Park H.W.;
RT "Crystal structures of human pantothenate kinases. Insights into allosteric
RT regulation and mutations linked to a neurodegeneration disorder.";
RL J. Biol. Chem. 282:27984-27993(2007).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 12-368 IN COMPLEX WITH
RP ACETYL-COA, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, SUBUNIT, AND MUTAGENESIS OF SER-195; ARG-207; ALA-267
RP AND ALA-269.
RX PubMed=20797618; DOI=10.1016/j.chembiol.2010.06.006;
RA Leonardi R., Zhang Y.M., Yun M.K., Zhou R., Zeng F.Y., Lin W., Cui J.,
RA Chen T., Rock C.O., White S.W., Jackowski S.;
RT "Modulation of pantothenate kinase 3 activity by small molecules that
RT interact with the substrate/allosteric regulatory domain.";
RL Chem. Biol. 17:892-902(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 12-370 IN COMPLEX WITH MAGNESIUM
RP IONS; AMPPNP AND PANTOTHENATE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF GLY-19 AND GLU-138.
RX PubMed=27555321; DOI=10.1074/jbc.m116.748061;
RA Subramanian C., Yun M.K., Yao J., Sharma L.K., Lee R.E., White S.W.,
RA Jackowski S., Rock C.O.;
RT "Allosteric Regulation of Mammalian Pantothenate Kinase.";
RL J. Biol. Chem. 291:22302-22314(2016).
CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate to generate 4'-
CC phosphopantothenate in the first and rate-determining step of coenzyme
CC A (CoA) synthesis. {ECO:0000269|PubMed:17631502,
CC ECO:0000269|PubMed:20797618, ECO:0000269|PubMed:27555321,
CC ECO:0000269|PubMed:30927326}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP +
CC H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC EC=2.7.1.33; Evidence={ECO:0000269|PubMed:17631502,
CC ECO:0000269|PubMed:20797618, ECO:0000269|PubMed:27555321,
CC ECO:0000269|PubMed:30927326};
CC -!- ACTIVITY REGULATION: Subject to allosteric regulation, exists in two
CC distinct conformational states, a catalytically incompetent (or open)
CC conformation stabilized by the binding of acetyl(acyl)-CoA, and a
CC catalytically competent (or closed) conformation stabilized by ATP-
CC binding (PubMed:27555321). Inhibited by acetyl-CoA and its thioesters
CC which act as allosteric inhibitors and compete with the ATP-binding
CC site (PubMed:30927326, PubMed:17631502, PubMed:20797618,
CC PubMed:27555321). Inhibited by sulfonylureas and thiazolidinediones
CC (PubMed:20797618). Activated by oleoylethanolamide, palmitoyl-carnitine
CC and oleoyl-carnitine (PubMed:20797618). {ECO:0000269|PubMed:17631502,
CC ECO:0000269|PubMed:20797618, ECO:0000269|PubMed:27555321,
CC ECO:0000269|PubMed:30927326}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=175 uM for ATP {ECO:0000269|PubMed:30927326};
CC KM=311 uM for ATP {ECO:0000269|PubMed:20797618};
CC KM=17 uM for pantothenate {ECO:0000269|PubMed:30927326};
CC KM=14 uM for pantothenate {ECO:0000269|PubMed:20797618};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5. {ECO:0000269|PubMed:17631502,
CC ECO:0000269|PubMed:20797618, ECO:0000269|PubMed:27555321,
CC ECO:0000305|PubMed:30927326}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17631502,
CC ECO:0000269|PubMed:20797618, ECO:0000269|PubMed:27555321}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23152917,
CC ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver.
CC {ECO:0000269|PubMed:11479594}.
CC -!- SIMILARITY: Belongs to the type II pantothenate kinase family.
CC {ECO:0000305}.
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DR EMBL; AK022961; BAB14333.1; -; mRNA.
DR EMBL; AK223285; BAD97005.1; -; mRNA.
DR EMBL; CH471062; EAW61503.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61505.1; -; Genomic_DNA.
DR EMBL; BC013705; AAH13705.1; -; mRNA.
DR EMBL; BK000011; DAA00005.1; -; mRNA.
DR CCDS; CCDS4368.1; -.
DR RefSeq; NP_078870.1; NM_024594.3.
DR PDB; 2I7P; X-ray; 2.05 A; A/B/C/D=12-368.
DR PDB; 3MK6; X-ray; 1.98 A; A/B/C/D=12-368.
DR PDB; 3SMS; X-ray; 2.20 A; A=10-370.
DR PDB; 5KPR; X-ray; 1.83 A; A=12-370.
DR PDB; 5KPT; X-ray; 2.30 A; A=12-370.
DR PDB; 5KPZ; X-ray; 2.40 A; A=12-370.
DR PDB; 5KQ8; X-ray; 2.00 A; A=12-370.
DR PDB; 5KQD; X-ray; 2.60 A; A=12-370.
DR PDB; 6B3V; X-ray; 1.60 A; A=12-370.
DR PDB; 6PE6; X-ray; 1.60 A; A=12-370.
DR PDB; 6X4J; X-ray; 2.30 A; A=12-370.
DR PDB; 6X4K; X-ray; 2.10 A; A=12-370.
DR PDB; 6X4L; X-ray; 2.00 A; A=12-370.
DR PDBsum; 2I7P; -.
DR PDBsum; 3MK6; -.
DR PDBsum; 3SMS; -.
DR PDBsum; 5KPR; -.
DR PDBsum; 5KPT; -.
DR PDBsum; 5KPZ; -.
DR PDBsum; 5KQ8; -.
DR PDBsum; 5KQD; -.
DR PDBsum; 6B3V; -.
DR PDBsum; 6PE6; -.
DR PDBsum; 6X4J; -.
DR PDBsum; 6X4K; -.
DR PDBsum; 6X4L; -.
DR AlphaFoldDB; Q9H999; -.
DR SMR; Q9H999; -.
DR BioGRID; 122774; 9.
DR STRING; 9606.ENSP00000239231; -.
DR BindingDB; Q9H999; -.
DR ChEMBL; CHEMBL3407328; -.
DR iPTMnet; Q9H999; -.
DR PhosphoSitePlus; Q9H999; -.
DR SwissPalm; Q9H999; -.
DR BioMuta; PANK3; -.
DR DMDM; 27805668; -.
DR EPD; Q9H999; -.
DR jPOST; Q9H999; -.
DR MassIVE; Q9H999; -.
DR MaxQB; Q9H999; -.
DR PaxDb; Q9H999; -.
DR PeptideAtlas; Q9H999; -.
DR PRIDE; Q9H999; -.
DR ProteomicsDB; 81299; -.
DR Antibodypedia; 16804; 229 antibodies from 24 providers.
DR DNASU; 79646; -.
DR Ensembl; ENST00000239231.7; ENSP00000239231.6; ENSG00000120137.7.
DR GeneID; 79646; -.
DR KEGG; hsa:79646; -.
DR MANE-Select; ENST00000239231.7; ENSP00000239231.6; NM_024594.4; NP_078870.1.
DR UCSC; uc003lzy.4; human.
DR CTD; 79646; -.
DR DisGeNET; 79646; -.
DR GeneCards; PANK3; -.
DR HGNC; HGNC:19365; PANK3.
DR HPA; ENSG00000120137; Low tissue specificity.
DR MIM; 606161; gene.
DR neXtProt; NX_Q9H999; -.
DR OpenTargets; ENSG00000120137; -.
DR PharmGKB; PA134903180; -.
DR VEuPathDB; HostDB:ENSG00000120137; -.
DR eggNOG; KOG2201; Eukaryota.
DR GeneTree; ENSGT00940000156396; -.
DR HOGENOM; CLU_011154_0_1_1; -.
DR InParanoid; Q9H999; -.
DR OMA; WAQEGDN; -.
DR OrthoDB; 865329at2759; -.
DR PhylomeDB; Q9H999; -.
DR TreeFam; TF314866; -.
DR BioCyc; MetaCyc:HS04372-MON; -.
DR BRENDA; 2.7.1.33; 2681.
DR PathwayCommons; Q9H999; -.
DR Reactome; R-HSA-196783; Coenzyme A biosynthesis.
DR UniPathway; UPA00241; UER00352.
DR BioGRID-ORCS; 79646; 14 hits in 1079 CRISPR screens.
DR ChiTaRS; PANK3; human.
DR EvolutionaryTrace; Q9H999; -.
DR GenomeRNAi; 79646; -.
DR Pharos; Q9H999; Tchem.
DR PRO; PR:Q9H999; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9H999; protein.
DR Bgee; ENSG00000120137; Expressed in jejunal mucosa and 207 other tissues.
DR ExpressionAtlas; Q9H999; baseline and differential.
DR Genevisible; Q9H999; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1905502; F:acetyl-CoA binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004594; F:pantothenate kinase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019842; F:vitamin binding; IDA:UniProtKB.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004567; Type_II_PanK.
DR PANTHER; PTHR12280; PTHR12280; 1.
DR Pfam; PF03630; Fumble; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00555; panK_eukar; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..370
FT /note="Pantothenate kinase 3"
FT /id="PRO_0000161804"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:27555321"
FT BINDING 192
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:17631502"
FT BINDING 195
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:17631502,
FT ECO:0000269|PubMed:20797618"
FT BINDING 207
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:17631502,
FT ECO:0000269|PubMed:20797618"
FT MUTAGEN 19
FT /note="G->V: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:27555321"
FT MUTAGEN 138
FT /note="E->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:27555321"
FT MUTAGEN 138
FT /note="E->V: Prevents acetyl-CoA production."
FT /evidence="ECO:0000269|PubMed:30927326"
FT MUTAGEN 195
FT /note="S->V: Retains 30% of wild-type activity. Refractory
FT to inhibition by acetyl-CoA. Exhibits a 10-fold increase in
FT the Km for pantothenate."
FT /evidence="ECO:0000269|PubMed:20797618"
FT MUTAGEN 207
FT /note="R->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:20797618"
FT MUTAGEN 207
FT /note="R->W: Increases affinity for ATP and decreases
FT affinity for acetyl-CoA. Increases acetyl-CoA production."
FT /evidence="ECO:0000269|PubMed:30927326"
FT MUTAGEN 267
FT /note="A->F: Loss of catalytic activity but can bind ATP
FT normally."
FT /evidence="ECO:0000269|PubMed:20797618"
FT MUTAGEN 269
FT /note="A->F: Loss of catalytic activity but can bind ATP
FT normally."
FT /evidence="ECO:0000269|PubMed:20797618"
FT CONFLICT 335
FT /note="A -> V (in Ref. 2; BAD97005)"
FT /evidence="ECO:0000305"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:6PE6"
FT STRAND 20..31
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:6PE6"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6PE6"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:6PE6"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6PE6"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:6PE6"
FT STRAND 78..88
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:5KPR"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:3MK6"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 116..120
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:6PE6"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 138..152
FT /evidence="ECO:0007829|PDB:6PE6"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:6PE6"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:6PE6"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:6PE6"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:6PE6"
FT STRAND 184..201
FT /evidence="ECO:0007829|PDB:6PE6"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:6PE6"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:6PE6"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 286..312
FT /evidence="ECO:0007829|PDB:6PE6"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 328..341
FT /evidence="ECO:0007829|PDB:6PE6"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:6PE6"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:6PE6"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 357..364
FT /evidence="ECO:0007829|PDB:6PE6"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:6PE6"
SQ SEQUENCE 370 AA; 41094 MW; 71EEFA56079F352D CRC64;
MKIKDAKKPS FPWFGMDIGG TLVKLSYFEP IDITAEEEQE EVESLKSIRK YLTSNVAYGS
TGIRDVHLEL KDLTLFGRRG NLHFIRFPTQ DLPTFIQMGR DKNFSTLQTV LCATGGGAYK
FEKDFRTIGN LHLHKLDELD CLVKGLLYID SVSFNGQAEC YYFANASEPE RCQKMPFNLD
DPYPLLVVNI GSGVSILAVH SKDNYKRVTG TSLGGGTFLG LCSLLTGCES FEEALEMASK
GDSTQADKLV RDIYGGDYER FGLPGWAVAS SFGNMIYKEK RESVSKEDLA RATLVTITNN
IGSVARMCAV NEKINRVVFV GNFLRVNTLS MKLLAYALDY WSKGQLKALF LEHEGYFGAV
GALLGLPNFS
