PLEK_HUMAN
ID PLEK_HUMAN Reviewed; 350 AA.
AC P08567; B2R9E8; Q53SU8; Q6FGM8; Q6FGQ1; Q8WV81;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Pleckstrin;
DE AltName: Full=Platelet 47 kDa protein;
DE Short=p47;
GN Name=PLEK; Synonyms=P47;
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], AND VARIANTS ASN-97 AND LYS-340.
RX PubMed=2897630; DOI=10.1038/333470a0;
RA Tyers M., Rachubinski R.A., McCaw M.L., Varrichio A.M., Shorr R.G.L.,
RA Haslam R.J., Harley C.B.;
RT "Molecular cloning and expression of the major protein kinase C substrate
RT of platelets.";
RL Nature 333:470-473(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASN-97 AND LYS-340.
RX PubMed=2768345; DOI=10.1002/jcb.240400202;
RA Tyers M., Haslam R.J., Rachubinski R.A., Harley C.B.;
RT "Molecular analysis of pleckstrin: the major protein kinase C substrate of
RT platelets.";
RL J. Cell. Biochem. 40:133-145(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-340.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-340.
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 [8]
RP PHOSPHORYLATION AT SER-113 AND SER-117.
RX PubMed=8615792; DOI=10.1042/bj3140937;
RA Craig K.L., Harley C.B.;
RT "Phosphorylation of human pleckstrin on Ser-113 and Ser-117 by protein
RT kinase C.";
RL Biochem. J. 314:937-942(1996).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP STRUCTURE BY NMR OF 1-105.
RX PubMed=8208296; DOI=10.1038/369672a0;
RA Yoon H.S., Hajduk P.J., Petros A.M., Olejniczak E.T., Meadows R.P.,
RA Fesik S.W.;
RT "Solution structure of a pleckstrin-homology domain.";
RL Nature 369:672-675(1994).
RN [14]
RP STRUCTURE BY NMR OF 121-223.
RX PubMed=15573383; DOI=10.1002/prot.20320;
RA Civera C., Simon B., Stier G., Sattler M., Macias M.J.;
RT "Structure and dynamics of the human pleckstrin DEP domain: distinct
RT molecular features of a novel DEP domain subfamily.";
RL Proteins 58:354-366(2005).
RN [15]
RP STRUCTURE BY NMR OF 116-350.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the DEP domain and of the C-terminal PH domain of
RT human pleckstrin.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Major protein kinase C substrate of platelets.
CC -!- INTERACTION:
CC P08567; O95810: CAVIN2; NbExp=4; IntAct=EBI-2565501, EBI-742141;
CC P08567; Q14642: INPP5A; NbExp=4; IntAct=EBI-2565501, EBI-8670520;
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DR EMBL; X07743; CAA30564.1; -; mRNA.
DR EMBL; CR542056; CAG46853.1; -; mRNA.
DR EMBL; CR542079; CAG46876.1; -; mRNA.
DR EMBL; AK313756; BAG36495.1; -; mRNA.
DR EMBL; AC015969; AAX93121.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99876.1; -; Genomic_DNA.
DR EMBL; BC018549; AAH18549.1; -; mRNA.
DR CCDS; CCDS1887.1; -.
DR PIR; S00755; S00755.
DR RefSeq; NP_002655.2; NM_002664.2.
DR PDB; 1PLS; NMR; -; A=1-105.
DR PDB; 1W4M; NMR; -; A=121-223.
DR PDB; 1X05; NMR; -; A=235-350.
DR PDB; 1XX0; NMR; -; A=234-350.
DR PDB; 1ZM0; X-ray; 2.10 A; A/B=240-350.
DR PDB; 2CSO; NMR; -; A=116-229.
DR PDB; 2I5C; X-ray; 1.75 A; A/B/C=244-347.
DR PDB; 2I5F; X-ray; 1.35 A; A=244-347.
DR PDBsum; 1PLS; -.
DR PDBsum; 1W4M; -.
DR PDBsum; 1X05; -.
DR PDBsum; 1XX0; -.
DR PDBsum; 1ZM0; -.
DR PDBsum; 2CSO; -.
DR PDBsum; 2I5C; -.
DR PDBsum; 2I5F; -.
DR AlphaFoldDB; P08567; -.
DR BMRB; P08567; -.
DR SMR; P08567; -.
DR BioGRID; 111357; 7.
DR IntAct; P08567; 11.
DR MINT; P08567; -.
DR STRING; 9606.ENSP00000234313; -.
DR ChEMBL; CHEMBL4523171; -.
DR iPTMnet; P08567; -.
DR PhosphoSitePlus; P08567; -.
DR BioMuta; PLEK; -.
DR DMDM; 317373523; -.
DR OGP; P08567; -.
DR EPD; P08567; -.
DR jPOST; P08567; -.
DR MassIVE; P08567; -.
DR MaxQB; P08567; -.
DR PaxDb; P08567; -.
DR PeptideAtlas; P08567; -.
DR PRIDE; P08567; -.
DR ProteomicsDB; 52121; -.
DR Antibodypedia; 30933; 476 antibodies from 37 providers.
DR DNASU; 5341; -.
DR Ensembl; ENST00000234313.8; ENSP00000234313.7; ENSG00000115956.10.
DR GeneID; 5341; -.
DR KEGG; hsa:5341; -.
DR MANE-Select; ENST00000234313.8; ENSP00000234313.7; NM_002664.3; NP_002655.2.
DR UCSC; uc002sen.5; human.
DR CTD; 5341; -.
DR DisGeNET; 5341; -.
DR GeneCards; PLEK; -.
DR HGNC; HGNC:9070; PLEK.
DR HPA; ENSG00000115956; Tissue enriched (bone).
DR MIM; 173570; gene.
DR neXtProt; NX_P08567; -.
DR OpenTargets; ENSG00000115956; -.
DR PharmGKB; PA33400; -.
DR VEuPathDB; HostDB:ENSG00000115956; -.
DR eggNOG; ENOG502QQIA; Eukaryota.
DR GeneTree; ENSGT00940000157885; -.
DR HOGENOM; CLU_067828_0_0_1; -.
DR InParanoid; P08567; -.
DR OMA; MEPKQIR; -.
DR OrthoDB; 717547at2759; -.
DR PhylomeDB; P08567; -.
DR TreeFam; TF332246; -.
DR PathwayCommons; P08567; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; P08567; -.
DR SIGNOR; P08567; -.
DR BioGRID-ORCS; 5341; 19 hits in 1071 CRISPR screens.
DR ChiTaRS; PLEK; human.
DR EvolutionaryTrace; P08567; -.
DR GenomeRNAi; 5341; -.
DR Pharos; P08567; Tbio.
DR PRO; PR:P08567; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P08567; protein.
DR Bgee; ENSG00000115956; Expressed in monocyte and 171 other tissues.
DR Genevisible; P08567; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032587; C:ruffle membrane; IDA:BHF-UCL.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR GO; GO:0005080; F:protein kinase C binding; IDA:BHF-UCL.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:BHF-UCL.
DR GO; GO:0030030; P:cell projection organization; IDA:BHF-UCL.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IDA:BHF-UCL.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEP:BHF-UCL.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0050849; P:negative regulation of calcium-mediated signaling; NAS:BHF-UCL.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0010920; P:negative regulation of inositol phosphate biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:BHF-UCL.
DR GO; GO:0030845; P:phospholipase C-inhibiting G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
DR GO; GO:0002576; P:platelet degranulation; IEP:BHF-UCL.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IDA:BHF-UCL.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IDA:BHF-UCL.
DR GO; GO:0010925; P:positive regulation of inositol-polyphosphate 5-phosphatase activity; IDA:BHF-UCL.
DR GO; GO:0033625; P:positive regulation of integrin activation; ISS:BHF-UCL.
DR GO; GO:0010572; P:positive regulation of platelet activation; ISS:BHF-UCL.
DR GO; GO:0070528; P:protein kinase C signaling; ISS:BHF-UCL.
DR GO; GO:0070560; P:protein secretion by platelet; ISS:BHF-UCL.
DR GO; GO:0060305; P:regulation of cell diameter; IDA:BHF-UCL.
DR GO; GO:0031529; P:ruffle organization; IDA:BHF-UCL.
DR GO; GO:0070493; P:thrombin-activated receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; ISS:BHF-UCL.
DR CDD; cd04445; DEP_PLEK1; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037371; PLEK_DEP.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00169; PH; 2.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00233; PH; 2.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..350
FT /note="Pleckstrin"
FT /id="PRO_0000053859"
FT DOMAIN 4..101
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 136..221
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 244..347
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT MOD_RES 64
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 113
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:8615792"
FT MOD_RES 117
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:8615792,
FT ECO:0007744|PubMed:19367720"
FT VARIANT 5
FT /note="R -> W (in dbSNP:rs17035364)"
FT /id="VAR_027797"
FT VARIANT 92
FT /note="W -> R"
FT /id="VAR_005524"
FT VARIANT 97
FT /note="K -> N (in dbSNP:rs3816281)"
FT /evidence="ECO:0000269|PubMed:2768345,
FT ECO:0000269|PubMed:2897630"
FT /id="VAR_027798"
FT VARIANT 108
FT /note="K -> Q (in dbSNP:rs34515106)"
FT /id="VAR_056666"
FT VARIANT 340
FT /note="R -> K (in dbSNP:rs1063479)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2768345, ECO:0000269|PubMed:2897630,
FT ECO:0000269|Ref.3"
FT /id="VAR_027799"
FT CONFLICT 284
FT /note="E -> G (in Ref. 3; CAG46876)"
FT /evidence="ECO:0000305"
FT STRAND 6..19
FT /evidence="ECO:0007829|PDB:1PLS"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:1PLS"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:1PLS"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:1PLS"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1PLS"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:1PLS"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1PLS"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1PLS"
FT HELIX 86..103
FT /evidence="ECO:0007829|PDB:1PLS"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:1W4M"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:1W4M"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:2CSO"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1W4M"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:1W4M"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1W4M"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:1W4M"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:1W4M"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:1W4M"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:1W4M"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2CSO"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2CSO"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:1XX0"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:2I5F"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:2I5F"
FT STRAND 261..269
FT /evidence="ECO:0007829|PDB:2I5F"
FT TURN 270..273
FT /evidence="ECO:0007829|PDB:2I5F"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:2I5F"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:1ZM0"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:2I5F"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:2I5F"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1X05"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:2I5F"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:2I5F"
FT HELIX 332..346
FT /evidence="ECO:0007829|PDB:2I5F"
SQ SEQUENCE 350 AA; 40125 MW; 2E292CB18B533261 CRC64;
MEPKRIREGY LVKKGSVFNT WKPMWVVLLE DGIEFYKKKS DNSPKGMIPL KGSTLTSPCQ
DFGKRMFVFK ITTTKQQDHF FQAAFLEERD AWVRDIKKAI KCIEGGQKFA RKSTRRSIRL
PETIDLGALY LSMKDTEKGI KELNLEKDKK IFNHCFTGNC VIDWLVSNQS VRNRQEGLMI
ASSLLNEGYL QPAGDMSKSA VDGTAENPFL DNPDAFYYFP DSGFFCEENS SDDDVILKEE
FRGVIIKQGC LLKQGHRRKN WKVRKFILRE DPAYLHYYDP AGAEDPLGAI HLRGCVVTSV
ESNSNGRKSE EENLFEIITA DEVHYFLQAA TPKERTEWIR AIQMASRTGK
