PANK1_HUMAN
ID PANK1_HUMAN Reviewed; 598 AA.
AC Q8TE04; A6NIP0; Q7RTX6; Q7Z495; Q8TBQ8;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Pantothenate kinase 1;
DE Short=hPanK;
DE Short=hPanK1;
DE EC=2.7.1.33 {ECO:0000269|PubMed:11809413, ECO:0000269|PubMed:17631502};
DE AltName: Full=Pantothenic acid kinase 1;
GN Name=PANK1; Synonyms=PANK;
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 3), AND TISSUE SPECIFICITY (ISOFORM 3).
RC TISSUE=Fetal brain;
RX PubMed=11809413; DOI=10.1016/s1357-2725(01)00114-5;
RA Ni X., Ma Y., Cheng H., Jiang M., Ying K., Xie Y., Mao Y.;
RT "Cloning and characterization of a novel human pantothenate kinase gene.";
RL Int. J. Biochem. Cell Biol. 34:109-115(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INDUCTION, FUNCTION (ISOFORM 1), AND CATALYTIC ACTIVITY
RP (ISOFORM 1).
RX PubMed=14523052; DOI=10.1194/jlr.m300279-jlr200;
RA Ramaswamy G., Karim M.A., Murti K.G., Jackowski S.;
RT "PPARalpha controls the intracellular coenzyme A concentration via
RT regulation of PANK1alpha gene expression.";
RL J. Lipid Res. 45:17-31(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 460-598 (ISOFORM 2).
RC TISSUE=Skeletal muscle;
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 [6]
RP IDENTIFICATION (ISOFORM 2).
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 [7]
RP IDENTIFICATION (ISOFORM 1).
RA Zhou B., Westaway S.K., Levinson B., Johnson M.A., Gitschier J.,
RA Hayflick S.J.;
RL Unpublished observations (JUL-2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), NUCLEAR LOCALIZATION SIGNAL, AND
RP MUTAGENESIS OF 218-LYS--ARG-233.
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 234-593 IN COMPLEX WITH
RP ACETYL-COA, SUBUNIT, ACTIVITY REGULATION, FUNCTION (ISOFORM 1), AND
RP CATALYTIC ACTIVITY (ISOFORM 1).
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).
CC -!- FUNCTION: [Isoform 1]: Catalyzes the phosphorylation of pantothenate to
CC generate 4'-phosphopantothenate in the first and rate-determining step
CC of coenzyme A (CoA) synthesis. {ECO:0000269|PubMed:14523052,
CC ECO:0000269|PubMed:17631502}.
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:14523052,
CC ECO:0000269|PubMed:17631502};
CC -!- ACTIVITY REGULATION: Regulated by feedback inhibition by CoA and its
CC thioesters. {ECO:0000269|PubMed:17631502}.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5. {ECO:0000269|PubMed:14523052,
CC ECO:0000269|PubMed:17631502}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17631502}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14523052}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:23152917}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:23152917}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:23152917}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:23152917}. Recycling endosome
CC {ECO:0000269|PubMed:23152917}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=PanK1-alpha, PANK1a;
CC IsoId=Q8TE04-1; Sequence=Displayed;
CC Name=2; Synonyms=PANK1a, PanK1-beta;
CC IsoId=Q8TE04-2; Sequence=VSP_004520;
CC Name=3; Synonyms=PANK1b;
CC IsoId=Q8TE04-3; Sequence=VSP_004520, VSP_004521;
CC Name=4; Synonyms=PanK1-gamma;
CC IsoId=Q8TE04-4; Sequence=VSP_012823, VSP_012824;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed at high levels in brain,
CC heart, kidney, liver, skeletal muscle and testis.
CC {ECO:0000269|PubMed:11809413, ECO:0000269|PubMed:14523052}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Detected at much lower levels in
CC kidney, liver, brain and testis and not detected in heart or skeletal
CC muscle. {ECO:0000269|PubMed:14523052}.
CC -!- INDUCTION: [Isoform 1]: Induced by bezafibrate, a hypolipidemic drug
CC which acts as an agonist of peroxisome proliferator activator receptor
CC alpha (PPARA), while isoform 2 levels decrease slightly.
CC {ECO:0000269|PubMed:14523052}.
CC -!- DOMAIN: [Isoform 1]: The N-terminal extension, may be the regulatory
CC domain. {ECO:0000250|UniProtKB:Q8K4K6}.
CC -!- SIMILARITY: Belongs to the type II pantothenate kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26296.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF355198; AAL86371.1; -; mRNA.
DR EMBL; AL157400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY027661; AAK20916.1; -; mRNA.
DR EMBL; AY027662; AAK20917.1; -; mRNA.
DR EMBL; AY027663; AAK20918.1; -; mRNA.
DR EMBL; CH471066; EAW50131.1; -; Genomic_DNA.
DR EMBL; BC026296; AAH26296.1; ALT_INIT; mRNA.
DR EMBL; BK000008; DAA00002.1; -; mRNA.
DR EMBL; BK000009; DAA00003.1; -; mRNA.
DR CCDS; CCDS7405.1; -. [Q8TE04-3]
DR CCDS; CCDS7406.1; -. [Q8TE04-2]
DR RefSeq; NP_612189.2; NM_138316.3. [Q8TE04-3]
DR RefSeq; NP_683878.1; NM_148977.2. [Q8TE04-1]
DR RefSeq; NP_683879.1; NM_148978.2. [Q8TE04-2]
DR RefSeq; XP_016871822.1; XM_017016333.1. [Q8TE04-4]
DR RefSeq; XP_016871827.1; XM_017016338.1.
DR PDB; 2I7N; X-ray; 1.90 A; A/B=234-593.
DR PDB; 3SMP; X-ray; 1.90 A; A/B=231-597.
DR PDBsum; 2I7N; -.
DR PDBsum; 3SMP; -.
DR AlphaFoldDB; Q8TE04; -.
DR SMR; Q8TE04; -.
DR BioGRID; 119751; 5.
DR IntAct; Q8TE04; 1.
DR MINT; Q8TE04; -.
DR STRING; 9606.ENSP00000302108; -.
DR BindingDB; Q8TE04; -.
DR ChEMBL; CHEMBL3407326; -.
DR iPTMnet; Q8TE04; -.
DR PhosphoSitePlus; Q8TE04; -.
DR BioMuta; PANK1; -.
DR DMDM; 27805665; -.
DR EPD; Q8TE04; -.
DR jPOST; Q8TE04; -.
DR MassIVE; Q8TE04; -.
DR MaxQB; Q8TE04; -.
DR PaxDb; Q8TE04; -.
DR PeptideAtlas; Q8TE04; -.
DR PRIDE; Q8TE04; -.
DR ProteomicsDB; 74385; -. [Q8TE04-1]
DR ProteomicsDB; 74386; -. [Q8TE04-2]
DR ProteomicsDB; 74387; -. [Q8TE04-3]
DR ProteomicsDB; 74388; -. [Q8TE04-4]
DR Antibodypedia; 35332; 248 antibodies from 28 providers.
DR DNASU; 53354; -.
DR Ensembl; ENST00000322191.10; ENSP00000318526.6; ENSG00000152782.18. [Q8TE04-3]
DR Ensembl; ENST00000342512.3; ENSP00000345118.3; ENSG00000152782.18. [Q8TE04-2]
DR GeneID; 53354; -.
DR KEGG; hsa:53354; -.
DR UCSC; uc001kgn.3; human. [Q8TE04-1]
DR CTD; 53354; -.
DR DisGeNET; 53354; -.
DR GeneCards; PANK1; -.
DR HGNC; HGNC:8598; PANK1.
DR HPA; ENSG00000152782; Tissue enhanced (kidney, liver).
DR MIM; 606160; gene.
DR neXtProt; NX_Q8TE04; -.
DR OpenTargets; ENSG00000152782; -.
DR PharmGKB; PA32928; -.
DR VEuPathDB; HostDB:ENSG00000152782; -.
DR eggNOG; KOG2201; Eukaryota.
DR GeneTree; ENSGT00940000157373; -.
DR HOGENOM; CLU_011154_4_1_1; -.
DR InParanoid; Q8TE04; -.
DR OMA; KQRSFPW; -.
DR OrthoDB; 865329at2759; -.
DR PhylomeDB; Q8TE04; -.
DR TreeFam; TF314866; -.
DR BioCyc; MetaCyc:HS07852-MON; -.
DR BRENDA; 2.7.1.33; 2681.
DR PathwayCommons; Q8TE04; -.
DR Reactome; R-HSA-196783; Coenzyme A biosynthesis.
DR SignaLink; Q8TE04; -.
DR UniPathway; UPA00241; UER00352.
DR BioGRID-ORCS; 53354; 20 hits in 1078 CRISPR screens.
DR ChiTaRS; PANK1; human.
DR EvolutionaryTrace; Q8TE04; -.
DR GeneWiki; PANK1; -.
DR GenomeRNAi; 53354; -.
DR Pharos; Q8TE04; Tbio.
DR PRO; PR:Q8TE04; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8TE04; protein.
DR Bgee; ENSG00000152782; Expressed in kidney epithelium and 168 other tissues.
DR Genevisible; Q8TE04; HS.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:1905502; F:acetyl-CoA binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004594; F:pantothenate kinase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; Alternative splicing; ATP-binding; Coenzyme A biosynthesis;
KW Cytoplasm; Cytoplasmic vesicle; Endosome; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..598
FT /note="Pantothenate kinase 1"
FT /id="PRO_0000161802"
FT REGION 32..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 218..235
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000269|PubMed:23152917"
FT ACT_SITE 363
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H999"
FT BINDING 417
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:17631502"
FT BINDING 420
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:17631502"
FT BINDING 432
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:17631502"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..235
FT /note="MLKLVGGGGGQDWACSVAGTSLGGEEAAFEVARPGDQGKAGGGSPGWGCAGI
FT PDSAPGAGVLQAGAVGPARGGQGAEEVGESAGGGEERRVRHPQAPALRLLNRKPQGGSG
FT EIKTPENDLQRGRLSRGPRTAPPAPGMGDRSGQQERSVPHSPGAPVGTSAAAVNGLLHN
FT GFHPPPVQPPHVCSRGPVGGSDAAPQRLPLLPELQPQPLLPQHDSPAKKCRLRRRMDSG
FT RKNRPP -> MKLINGKKQT (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11809413,
FT ECO:0000303|PubMed:14523052, ECO:0000303|PubMed:15489334"
FT /id="VSP_004520"
FT VAR_SEQ 1..198
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14523052"
FT /id="VSP_012823"
FT VAR_SEQ 199..235
FT /note="PLLPELQPQPLLPQHDSPAKKCRLRRRMDSGRKNRPP -> MAKSKHALLPF
FT CHGMMQQEGLHQMQSLDLGLLSLQNS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14523052"
FT /id="VSP_012824"
FT VAR_SEQ 438..496
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11809413"
FT /id="VSP_004521"
FT MUTAGEN 218..233
FT /note="KKCRLRRRMDSGRKNR->AACALAAAMDSGAANA: Loss of nuclear
FT localization."
FT /evidence="ECO:0000269|PubMed:23152917"
FT CONFLICT 306
FT /note="N -> D (in Ref. 1; AAL86371)"
FT /evidence="ECO:0000305"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:2I7N"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:2I7N"
FT HELIX 260..265
FT /evidence="ECO:0007829|PDB:3SMP"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:2I7N"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:3SMP"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2I7N"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3SMP"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:2I7N"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:2I7N"
FT STRAND 304..313
FT /evidence="ECO:0007829|PDB:2I7N"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:2I7N"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:2I7N"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:3SMP"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:2I7N"
FT TURN 341..344
FT /evidence="ECO:0007829|PDB:2I7N"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:2I7N"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:3SMP"
FT HELIX 363..377
FT /evidence="ECO:0007829|PDB:2I7N"
FT STRAND 384..390
FT /evidence="ECO:0007829|PDB:2I7N"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:2I7N"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:2I7N"
FT STRAND 409..426
FT /evidence="ECO:0007829|PDB:2I7N"
FT STRAND 429..437
FT /evidence="ECO:0007829|PDB:2I7N"
FT HELIX 440..451
FT /evidence="ECO:0007829|PDB:2I7N"
FT HELIX 456..465
FT /evidence="ECO:0007829|PDB:2I7N"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:2I7N"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:2I7N"
FT HELIX 475..479
FT /evidence="ECO:0007829|PDB:2I7N"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:2I7N"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:2I7N"
FT TURN 496..501
FT /evidence="ECO:0007829|PDB:2I7N"
FT HELIX 503..506
FT /evidence="ECO:0007829|PDB:2I7N"
FT HELIX 511..537
FT /evidence="ECO:0007829|PDB:2I7N"
FT STRAND 542..546
FT /evidence="ECO:0007829|PDB:2I7N"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:2I7N"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:2I7N"
FT HELIX 554..566
FT /evidence="ECO:0007829|PDB:2I7N"
FT TURN 567..569
FT /evidence="ECO:0007829|PDB:2I7N"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:2I7N"
FT TURN 577..580
FT /evidence="ECO:0007829|PDB:2I7N"
FT HELIX 582..591
FT /evidence="ECO:0007829|PDB:2I7N"
SQ SEQUENCE 598 AA; 64339 MW; 0A92115D5BEDFC4C CRC64;
MLKLVGGGGG QDWACSVAGT SLGGEEAAFE VARPGDQGKA GGGSPGWGCA GIPDSAPGAG
VLQAGAVGPA RGGQGAEEVG ESAGGGEERR VRHPQAPALR LLNRKPQGGS GEIKTPENDL
QRGRLSRGPR TAPPAPGMGD RSGQQERSVP HSPGAPVGTS AAAVNGLLHN GFHPPPVQPP
HVCSRGPVGG SDAAPQRLPL LPELQPQPLL PQHDSPAKKC RLRRRMDSGR KNRPPFPWFG
MDIGGTLVKL VYFEPKDITA EEEQEEVENL KSIRKYLTSN TAYGKTGIRD VHLELKNLTM
CGRKGNLHFI RFPSCAMHRF IQMGSEKNFS SLHTTLCATG GGAFKFEEDF RMIADLQLHK
LDELDCLIQG LLYVDSVGFN GKPECYYFEN PTNPELCQKK PYCLDNPYPM LLVNMGSGVS
ILAVYSKDNY KRVTGTSLGG GTFLGLCCLL TGCETFEEAL EMAAKGDSTN VDKLVKDIYG
GDYERFGLQG SAVASSFGNM MSKEKRDSIS KEDLARATLV TITNNIGSIA RMCALNENID
RVVFVGNFLR INMVSMKLLA YAMDFWSKGQ LKALFLEHEG YFGAVGALLE LFKMTDDK
