ID   P4K2B_HUMAN             Reviewed;         481 AA.
AC   Q8TCG2; Q9NUW2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   02-SEP-2026, entry version 155.
DE   RecName: Full=Phosphatidylinositol 4-kinase type 2-beta;
DE            EC=2.7.1.67 {ECO:0000269|PubMed:11923287, ECO:0000269|PubMed:12324459};
DE   AltName: Full=Phosphatidylinositol 4-kinase type II-beta;
DE            Short=PI4KII-BETA;
GN   Name=PI4K2B;
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], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT PRO-78, AND
RP   MUTAGENESIS OF ASP-304.
RX   PubMed=11923287; DOI=10.1074/jbc.m111807200;
RA   Balla A., Tuymetova G., Barshishat M., Geiszt M., Balla T.;
RT   "Characterization of type II phosphatidylinositol 4-kinase isoforms reveals
RT   association of the enzymes with endosomal vesicular compartments.";
RL   J. Biol. Chem. 277:20041-20050(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, SUBCELLULAR LOCATION, TOPOLOGY, AND VARIANT PRO-78.
RC   TISSUE=Brain;
RX   PubMed=12324459; DOI=10.1074/jbc.m206860200;
RA   Wei Y.J., Sun H.Q., Yamamoto M., Wlodarski P., Kunii K., Martinez M.,
RA   Barylko B., Albanesi J.P., Yin H.L.;
RT   "Type II phosphatidylinositol 4-kinase beta is a cytosolic and peripheral
RT   membrane protein that is recruited to the plasma membrane and activated by
RT   Rac-GTP.";
RL   J. Biol. Chem. 277:46586-46593(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hong W.;
RT   "Beta isoform of human type II phosphatidylinositol 4-kinase
RT   (PI4KIIbeta).";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-78.
RC   TISSUE=Placenta;
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 MRNA], AND VARIANT PRO-78.
RC   TISSUE=Skin;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-17, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8] {ECO:0007744|PDB:4WTV}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 90-165 AND 176-450 IN COMPLEX
RP   WITH ATP.
RX   PubMed=26143926; DOI=10.1107/s1399004715009505;
RA   Klima M., Baumlova A., Chalupska D., Hrebabecky H., Dejmek M., Nencka R.,
RA   Boura E.;
RT   "The high-resolution crystal structure of phosphatidylinositol 4-kinase
RT   IIbeta and the crystal structure of phosphatidylinositol 4-kinase IIalpha
RT   containing a nucleoside analogue provide a structural basis for isoform-
RT   specific inhibitor design.";
RL   Acta Crystallogr. 71:1555-1563(2015).
RN   [9]
RP   VARIANT [LARGE SCALE ANALYSIS] PRO-78, AND IDENTIFICATION BY MASS
RP   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).
CC   -!- FUNCTION: Together with PI4K2A and the type III PI4Ks (PIK4CA and
CC       PIK4CB) it contributes to the overall PI4-kinase activity of the cell
CC       (PubMed:11923287, PubMed:12324459). This contribution may be especially
CC       significant in plasma membrane, endosomal and Golgi compartments
CC       (PubMed:11923287, PubMed:12324459). The phosphorylation of
CC       phosphatidylinositol (PI) to PI4P is the first committed step in the
CC       generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor
CC       of the second messenger inositol 1,4,5-trisphosphate (InsP3)
CC       (PubMed:11923287, PubMed:12324459). Contributes to the production of
CC       InsP3 in stimulated cells and is likely to be involved in the
CC       regulation of vesicular trafficking. {ECO:0000269|PubMed:11923287,
CC       ECO:0000269|PubMed:12324459}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC         1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC         H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC         EC=2.7.1.67; Evidence={ECO:0000269|PubMed:11923287,
CC         ECO:0000269|PubMed:12324459};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC         Evidence={ECO:0000305|PubMed:11923287};
CC   -!- ACTIVITY REGULATION: Inhibited by phenylarsine oxide and adenosine
CC       (PubMed:11923287). Activation through membrane association is
CC       stimulated by active RAC1 (PubMed:12324459).
CC       {ECO:0000269|PubMed:11923287, ECO:0000269|PubMed:12324459}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12324459}.
CC       Golgi apparatus membrane {ECO:0000269|PubMed:11923287,
CC       ECO:0000269|PubMed:12324459}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:12324459}. Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:12324459}. Cell membrane
CC       {ECO:0000269|PubMed:11923287, ECO:0000269|PubMed:12324459}. Early
CC       endosome membrane {ECO:0000269|PubMed:11923287}. Note=Mainly cytosolic,
CC       association with membranes of the Golgi, endoplasmic and plasma
CC       membrane is stimulated by active RAC1 (PubMed:12324459). Association
CC       with early endosomes has not been confirmed (PubMed:11923287,
CC       PubMed:12324459). {ECO:0000269|PubMed:11923287,
CC       ECO:0000269|PubMed:12324459}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11923287}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY065990; AAL47580.1; -; mRNA.
DR   EMBL; AF411320; AAL04154.1; -; mRNA.
DR   EMBL; AY091514; AAM12049.1; -; mRNA.
DR   EMBL; AK001967; BAA92006.1; -; mRNA.
DR   EMBL; BC051749; AAH51749.1; -; mRNA.
DR   CCDS; CCDS3433.1; -.
DR   RefSeq; NP_060793.2; NM_018323.4.
DR   PDB; 4WTV; X-ray; 1.90 A; A/B=90-165, A/B=176-450.
DR   PDB; 8A5X; X-ray; 2.40 A; A=90-165, A=176-450.
DR   PDB; 9HHM; X-ray; 2.25 A; A/B=90-165, A/B=176-450.
DR   AlphaFoldDB; Q8TCG2; -.
DR   SMR; Q8TCG2; -.
DR   BioGRID; 120587; 78.
DR   FunCoup; Q8TCG2; 2069.
DR   IntAct; Q8TCG2; 57.
DR   MINT; Q8TCG2; -.
DR   NDEx; IQUERY-CP-PI4K2B; 1 NDEx IQuery Curated Pathway.
DR   STRING; 9606.ENSP00000264864; -.
DR   BindingDB; Q8TCG2; -.
DR   ChEMBL; CHEMBL3220; -.
DR   DrugBank; DB02709; Resveratrol.
DR   DrugCentral; Q8TCG2; -.
DR   GuidetoPHARMACOLOGY; 2499; -.
DR   iPTMnet; Q8TCG2; -.
DR   PhosphoSitePlus; Q8TCG2; -.
DR   SwissPalm; Q8TCG2; -.
DR   BioMuta; PI4K2B; -.
DR   DMDM; 74715788; -.
DR   jPOST; Q8TCG2; -.
DR   MassIVE; Q8TCG2; -.
DR   PaxDb; 9606-ENSP00000264864; -.
DR   PeptideAtlas; Q8TCG2; -.
DR   ProteomicsDB; 74134; -.
DR   Pumba; Q8TCG2; -.
DR   Antibodypedia; 1318; 185 antibodies from 27 providers.
DR   DNASU; 55300; -.
DR   Ensembl; ENST00000264864.8; ENSP00000264864.6; ENSG00000038210.15.
DR   Ensembl; ENST00000871538.1; ENSP00000541597.1; ENSG00000038210.15.
DR   GeneID; 55300; -.
DR   KEGG; hsa:55300; -.
DR   MANE-Select; ENST00000264864.8; ENSP00000264864.6; NM_018323.4; NP_060793.2.
DR   UCSC; uc003grk.3; human.
DR   AGR; HGNC:18215; -.
DR   ClinPGx; PA142671173; -.
DR   CTD; 55300; -.
DR   DisGeNET; 55300; -.
DR   GeneCards; PI4K2B; -.
DR   HGNC; HGNC:18215; PI4K2B.
DR   HPA; ENSG00000038210; Tissue enhanced (liver).
DR   MIM; 612101; gene.
DR   OpenTargets; ENSG00000038210; -.
DR   VEuPathDB; HostDB:ENSG00000038210; -.
DR   eggNOG; KOG2381; Eukaryota.
DR   GeneTree; ENSGT00390000010434; -.
DR   HOGENOM; CLU_032516_1_0_1; -.
DR   InParanoid; Q8TCG2; -.
DR   OMA; PYAKVPF; -.
DR   OrthoDB; 3349449at2759; -.
DR   PAN-GO; Q8TCG2; 7 GO annotations based on evolutionary models.
DR   PhylomeDB; Q8TCG2; -.
DR   BioCyc; MetaCyc:HS00529-MONOMER; -.
DR   BRENDA; 2.7.1.67; 2681.
DR   PathwayCommons; Q8TCG2; -.
DR   Reactome; R-HSA-1483248; Synthesis of PIPs at the ER membrane.
DR   Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR   Reactome; R-HSA-1660514; Synthesis of PIPs at the Golgi membrane.
DR   Reactome; R-HSA-1660516; Synthesis of PIPs at the early endosome membrane.
DR   SignaLink; Q8TCG2; -.
DR   SIGNOR; Q8TCG2; -.
DR   Agora; ENSG00000038210; -.
DR   BioGRID-ORCS; 55300; 13 hits in 1161 CRISPR screens.
DR   ChiTaRS; PI4K2B; human.
DR   EvolutionaryTrace; Q8TCG2; -.
DR   GeneWiki; PI4K2B; -.
DR   GenomeRNAi; 55300; -.
DR   Pharos; Q8TCG2; Tbio.
DR   PRO; PR:Q8TCG2; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q8TCG2; protein.
DR   Bgee; ENSG00000038210; Expressed in secondary oocyte and 176 other cell types or tissues.
DR   ExpressionAtlas; Q8TCG2; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR   GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IDA:UniProtKB.
DR   GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR   GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR   GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 1.10.1070.20; -; 1.
DR   InterPro; IPR039756; Lsb6/PI4K2.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   PANTHER; PTHR12865:SF6; PHOSPHATIDYLINOSITOL 4-KINASE TYPE 2-BETA; 1.
DR   PANTHER; PTHR12865; PHOSPHATIDYLINOSITOL 4-KINASE TYPE-II; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PDBsum; 4WTV; -.
DR   PDBsum; 8A5X; -.
DR   PDBsum; 9HHM; -.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell membrane; Cytoplasm; Endoplasmic reticulum;
KW   Endosome; Golgi apparatus; Kinase; Lipid metabolism; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Transferase.
FT   CHAIN           1..481
FT                   /note="Phosphatidylinositol 4-kinase type 2-beta"
FT                   /id="PRO_0000285164"
FT   DOMAIN          120..451
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..132
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          153..155
FT                   /note="Important for substrate binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT   REGION          161..174
FT                   /note="Important for interaction with membranes"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT   REGION          264..272
FT                   /note="Important for interaction with membranes"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT   REGION          301..309
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          342..362
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          357..366
FT                   /note="Important for interaction with membranes"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT   COMPBIAS        1..11
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..64
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:26143926,
FT                   ECO:0007744|PDB:4WTV"
FT   BINDING         148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:26143926,
FT                   ECO:0007744|PDB:4WTV"
FT   BINDING         257..260
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:26143926,
FT                   ECO:0007744|PDB:4WTV"
FT   BINDING         271..272
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:26143926,
FT                   ECO:0007744|PDB:4WTV"
FT   BINDING         344
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:26143926,
FT                   ECO:0007744|PDB:4WTV"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VARIANT         78
FT                   /note="S -> P (in dbSNP:rs313549)"
FT                   /evidence="ECO:0000269|PubMed:11923287,
FT                   ECO:0000269|PubMed:12324459, ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:19690332"
FT                   /id="VAR_031974"
FT   MUTAGEN         304
FT                   /note="D->A: Increased localization to plasma membrane."
FT                   /evidence="ECO:0000269|PubMed:11923287"
FT   TURN            97..100
FT                   /evidence="ECO:0007829|PDB:8A5X"
FT   HELIX           104..118
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   STRAND          124..130
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   STRAND          134..137
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   STRAND          143..149
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:8A5X"
FT   HELIX           163..165
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   HELIX           176..178
FT                   /evidence="ECO:0007829|PDB:8A5X"
FT   HELIX           185..199
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   STRAND          207..212
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   HELIX           221..225
FT                   /evidence="ECO:0007829|PDB:8A5X"
FT   HELIX           249..251
FT                   /evidence="ECO:0007829|PDB:8A5X"
FT   STRAND          252..258
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   HELIX           266..272
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   TURN            273..275
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   HELIX           277..279
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   HELIX           280..299
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   STRAND          307..314
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   STRAND          337..342
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   STRAND          356..358
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   HELIX           363..366
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   HELIX           368..371
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   HELIX           373..375
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   HELIX           376..386
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   HELIX           389..403
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   HELIX           411..433
FT                   /evidence="ECO:0007829|PDB:4WTV"
FT   HELIX           438..441
FT                   /evidence="ECO:0007829|PDB:4WTV"
SQ   SEQUENCE   481 AA;  54744 MW;  B4E16257E0AEC026 CRC64;
     MEDPSEPDRL ASADGGSPEE EEDGEREPLL PRIAWAHPRR GAPGSAVRLL DAAGEEGEAG
     DEELPLPPGD VGVSRSSSAE LDRSRPAVSV TIGTSEMNAF LDDPEFADIM LRAEQAIEVG
     IFPERISQGS SGSYFVKDPK RKIIGVFKPK SEEPYGQLNP KWTKYVHKVC CPCCFGRGCL
     IPNQGYLSEA GAYLVDNKLH LSIVPKTKVV WLVSETFNYN AIDRAKSRGK KYALEKVPKV
     GRKFHRIGLP PKIGSFQLFV EGYKEAEYWL RKFEADPLPE NIRKQFQSQF ERLVILDYII
     RNTDRGNDNW LVRYEKQKCE KEIDHKESKW IDDEEFLIKI AAIDNGLAFP FKHPDEWRAY
     PFHWAWLPQA KVPFSEEIRN LILPYISDMN FVQDLCEDLY ELFKTDKGFD KATFESQMSV
     MRGQILNLTQ ALRDGKSPFQ LVQIPCVIVE RSQGGSQGRI VHLSNSFTQT VNCRKPFFSS
     W
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