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   24-JAN-2024, entry version 167.
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   PDB; 7UE3; X-ray; 1.56 A; A=12-370.
DR   PDB; 7UE4; X-ray; 1.94 A; A=12-370.
DR   PDB; 7UE5; X-ray; 1.63 A; A=12-370.
DR   PDB; 7UE6; X-ray; 1.74 A; A=12-370.
DR   PDB; 7UE7; X-ray; 1.55 A; A=12-370.
DR   PDB; 7UE8; X-ray; 2.01 A; A=12-370.
DR   PDB; 7UEO; X-ray; 1.80 A; A=12-370.
DR   PDB; 7UEP; X-ray; 2.00 A; A=12-370.
DR   PDB; 7UEQ; X-ray; 1.70 A; A=12-370.
DR   PDB; 7UER; X-ray; 1.70 A; A=12-370.
DR   PDB; 7UES; X-ray; 1.80 A; A=12-370.
DR   PDB; 7UET; X-ray; 1.90 A; A=12-370.
DR   PDB; 7UEU; X-ray; 2.00 A; A=12-370.
DR   PDB; 7UEV; X-ray; 1.80 A; A=12-370.
DR   PDB; 7UEX; X-ray; 1.90 A; A=12-370.
DR   PDB; 7UEY; X-ray; 1.70 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   PDBsum; 7UE3; -.
DR   PDBsum; 7UE4; -.
DR   PDBsum; 7UE5; -.
DR   PDBsum; 7UE6; -.
DR   PDBsum; 7UE7; -.
DR   PDBsum; 7UE8; -.
DR   PDBsum; 7UEO; -.
DR   PDBsum; 7UEP; -.
DR   PDBsum; 7UEQ; -.
DR   PDBsum; 7UER; -.
DR   PDBsum; 7UES; -.
DR   PDBsum; 7UET; -.
DR   PDBsum; 7UEU; -.
DR   PDBsum; 7UEV; -.
DR   PDBsum; 7UEX; -.
DR   PDBsum; 7UEY; -.
DR   AlphaFoldDB; Q9H999; -.
DR   SMR; Q9H999; -.
DR   BioGRID; 122774; 15.
DR   IntAct; Q9H999; 4.
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; 9606-ENSP00000239231; -.
DR   PeptideAtlas; Q9H999; -.
DR   ProteomicsDB; 81299; -.
DR   Pumba; Q9H999; -.
DR   Antibodypedia; 16804; 243 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   AGR; HGNC:19365; -.
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; 167164at2759; -.
DR   PhylomeDB; Q9H999; -.
DR   TreeFam; TF314866; -.
DR   BioCyc; MetaCyc:HS04372-MONOMER; -.
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; 15 hits in 1160 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 209 other cell types or tissues.
DR   ExpressionAtlas; Q9H999; baseline and differential.
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   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.510; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR004567; Type_II_PanK.
DR   NCBIfam; TIGR00555; panK_eukar; 1.
DR   PANTHER; PTHR12280; PANTOTHENATE KINASE; 1.
DR   PANTHER; PTHR12280:SF21; PANTOTHENATE KINASE 3; 1.
DR   Pfam; PF03630; Fumble; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   Genevisible; Q9H999; HS.
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:7UE7"
FT   STRAND          20..31
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           35..40
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           43..54
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   TURN            59..61
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   STRAND          70..75
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   STRAND          78..88
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           92..100
FT                   /evidence="ECO:0007829|PDB:7UE7"
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:7UE7"
FT   HELIX           116..120
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           122..125
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   STRAND          132..135
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           138..152
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   STRAND          159..164
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   TURN            165..167
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   TURN            169..171
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   STRAND          173..176
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   STRAND          184..201
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   STRAND          204..212
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           215..226
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           231..240
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           243..245
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   STRAND          247..249
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           250..254
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           259..261
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   STRAND          267..270
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           273..276
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           278..283
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           286..312
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   STRAND          316..321
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           322..324
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           328..341
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   TURN            342..344
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   STRAND          347..351
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   TURN            352..355
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           357..364
FT                   /evidence="ECO:0007829|PDB:7UE7"
FT   HELIX           365..368
FT                   /evidence="ECO:0007829|PDB:7UE7"
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
//