P4K2B_HUMAN
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 03-AUG-2022, entry version 137.
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_018323.3.
DR PDB; 4WTV; X-ray; 1.90 A; A/B=90-165, A/B=176-450.
DR PDBsum; 4WTV; -.
DR AlphaFoldDB; Q8TCG2; -.
DR SMR; Q8TCG2; -.
DR BioGRID; 120587; 65.
DR IntAct; Q8TCG2; 24.
DR MINT; Q8TCG2; -.
DR STRING; 9606.ENSP00000264864; -.
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 EPD; Q8TCG2; -.
DR jPOST; Q8TCG2; -.
DR MassIVE; Q8TCG2; -.
DR MaxQB; Q8TCG2; -.
DR PaxDb; Q8TCG2; -.
DR PeptideAtlas; Q8TCG2; -.
DR PRIDE; Q8TCG2; -.
DR ProteomicsDB; 74134; -.
DR Antibodypedia; 1318; 188 antibodies from 26 providers.
DR DNASU; 55300; -.
DR Ensembl; ENST00000264864.8; ENSP00000264864.6; ENSG00000038210.14.
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 CTD; 55300; -.
DR DisGeNET; 55300; -.
DR GeneCards; PI4K2B; -.
DR HGNC; HGNC:18215; PI4K2B.
DR HPA; ENSG00000038210; Tissue enhanced (liver).
DR MIM; 612101; gene.
DR neXtProt; NX_Q8TCG2; -.
DR OpenTargets; ENSG00000038210; -.
DR PharmGKB; PA142671173; -.
DR VEuPathDB; HostDB:ENSG00000038210; -.
DR eggNOG; KOG2381; Eukaryota.
DR GeneTree; ENSGT00390000010434; -.
DR HOGENOM; CLU_032516_1_0_1; -.
DR InParanoid; Q8TCG2; -.
DR OMA; FHWAWLS; -.
DR OrthoDB; 1273723at2759; -.
DR PhylomeDB; Q8TCG2; -.
DR TreeFam; TF314740; -.
DR BioCyc; MetaCyc:HS00529-MON; -.
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 BioGRID-ORCS; 55300; 12 hits in 1082 CRISPR screens.
DR ChiTaRS; PI4K2B; human.
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 174 other tissues.
DR ExpressionAtlas; Q8TCG2; baseline and differential.
DR Genevisible; Q8TCG2; HS.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR039756; Lsb6/PI4K2.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR PANTHER; PTHR12865; PTHR12865; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
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; 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..16
FT /note="Basic and 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 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 185..199
FT /evidence="ECO:0007829|PDB:4WTV"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:4WTV"
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 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 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
