ID WBP4_HUMAN Reviewed; 376 AA. AC O75554; B7Z4M2; Q32P29; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 27-MAR-2024, entry version 181. DE RecName: Full=WW domain-binding protein 4; DE Short=WBP-4; DE AltName: Full=Formin-binding protein 21 {ECO:0000303|PubMed:19592703}; DE AltName: Full=WW domain-containing-binding protein 4; GN Name=WBP4; Synonyms=FBP21 {ECO:0000303|PubMed:19592703}, FNBP21; 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 1), FUNCTION, SUBCELLULAR LOCATION, AND RP INTERACTION WITH SNRPB; SNRPC; SF1 AND U2. RX PubMed=9724750; DOI=10.1073/pnas.95.18.10602; RA Bedford M.T., Reed R., Leder P.; RT "WW domain-mediated interactions reveal a spliceosome-associated protein RT that binds a third class of proline-rich motif: the proline glycine and RT methionine-rich motif."; RL Proc. Natl. Acad. Sci. U.S.A. 95:10602-10607(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Testis; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220 AND SER-262, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227 AND SER-229, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, 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 [9] RP STRUCTURE BY NMR OF 124-164. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of WW domain in WW domain binding protein 4 (WBP-4)."; RL Submitted (OCT-2006) to the PDB data bank. RN [10] RP STRUCTURE BY NMR OF 122-196, FUNCTION, MUTAGENESIS OF TRP-150 AND TRP-191, RP SUBCELLULAR LOCATION, AND INTERACTION WITH WBP11. RX PubMed=19592703; DOI=10.1074/jbc.m109.024828; RA Huang X., Beullens M., Zhang J., Zhou Y., Nicolaescu E., Lesage B., Hu Q., RA Wu J., Bollen M., Shi Y.; RT "Structure and function of the two tandem WW domains of the pre-mRNA RT splicing factor FBP21 (formin-binding protein 21)."; RL J. Biol. Chem. 284:25375-25387(2009). RN [11] {ECO:0007744|PDB:5O9Z} RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBUNIT, RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011; RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N., RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.; RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for RT Activation."; RL Cell 170:701-713(2017). RN [12] {ECO:0007744|PDB:7OS1} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 199-376 IN COMPLEX RP WITH SNRNP200. RX PubMed=35241646; DOI=10.1038/s41467-022-28754-2; RA Bergfort A., Preussner M., Kuropka B., Ilik I.A., Hilal T., Weber G., RA Freund C., Aktas T., Heyd F., Wahl M.C.; RT "A multi-factor trafficking site on the spliceosome remodeling enzyme BRR2 RT recruits C9ORF78 to regulate alternative splicing."; RL Nat. Commun. 13:1132-1132(2022). RN [13] RP VARIANT [LARGE SCALE ANALYSIS] ARG-113. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the CC spliceosome (PubMed:9724750, PubMed:19592703, PubMed:28781166). May CC play a role in cross-intron bridging of U1 and U2 snRNPs in the CC mammalian A complex (PubMed:9724750). {ECO:0000269|PubMed:19592703, CC ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:9724750}. CC -!- SUBUNIT: Component of the spliceosome B complex (PubMed:9724750, CC PubMed:28781166). Associated with U2 snRNPs (PubMed:9724750, CC PubMed:28781166). Binds splicing factors SNRPB, SNRPC and SF1 CC (PubMed:9724750). Interacts via the WW domains with the Pro-rich CC domains of KHDRBS1/SAM68 (By similarity). Interacts via the WW domains CC with the Pro-rich domains of WBP11 (PubMed:19592703). Interacts with CC SNRNP200 (PubMed:35241646). {ECO:0000250|UniProtKB:Q61048, CC ECO:0000269|PubMed:19592703, ECO:0000269|PubMed:28781166, CC ECO:0000269|PubMed:9724750}. CC -!- INTERACTION: CC O75554; P42858: HTT; NbExp=3; IntAct=EBI-7251981, EBI-466029; CC O75554; O75643: SNRNP200; NbExp=11; IntAct=EBI-7251981, EBI-1045395; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28781166}. Nucleus CC speckle {ECO:0000255|PROSITE-ProRule:PRU00130, CC ECO:0000269|PubMed:19592703, ECO:0000269|PubMed:9724750}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O75554-1; Sequence=Displayed; CC Name=2; CC IsoId=O75554-2; Sequence=VSP_056413; CC -!- DOMAIN: The WW domain recognizes the proline, glycine and methionine- CC rich (PGM) motif present in the splicing factors, as well as the CC Arg/Gly-rich-flanked Pro-rich domains found in several WW domain- CC binding proteins. {ECO:0000250}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF071185; AAC34811.1; -; mRNA. DR EMBL; AK297536; BAH12608.1; -; mRNA. DR EMBL; AL157877; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC104879; AAI04880.1; -; mRNA. DR EMBL; BC108310; AAI08311.1; -; mRNA. DR CCDS; CCDS9375.1; -. [O75554-1] DR RefSeq; NP_009118.1; NM_007187.4. [O75554-1] DR PDB; 2DK1; NMR; -; A=127-163. DR PDB; 2JXW; NMR; -; A=122-196. DR PDB; 5O9Z; EM; 4.50 A; Q=1-376. DR PDB; 6AHD; EM; 3.80 A; X=1-376. DR PDB; 7OS1; EM; 3.30 A; F=199-376. DR PDBsum; 2DK1; -. DR PDBsum; 2JXW; -. DR PDBsum; 5O9Z; -. DR PDBsum; 6AHD; -. DR PDBsum; 7OS1; -. DR AlphaFoldDB; O75554; -. DR EMDB; EMD-13045; -. DR EMDB; EMD-3766; -. DR EMDB; EMD-9624; -. DR SMR; O75554; -. DR BioGRID; 116363; 122. DR IntAct; O75554; 30. DR MINT; O75554; -. DR STRING; 9606.ENSP00000368801; -. DR GlyGen; O75554; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; O75554; -. DR MetOSite; O75554; -. DR PhosphoSitePlus; O75554; -. DR BioMuta; WBP4; -. DR EPD; O75554; -. DR jPOST; O75554; -. DR MassIVE; O75554; -. DR MaxQB; O75554; -. DR PaxDb; 9606-ENSP00000368801; -. DR PeptideAtlas; O75554; -. DR ProteomicsDB; 50083; -. [O75554-1] DR ProteomicsDB; 6615; -. DR Pumba; O75554; -. DR TopDownProteomics; O75554-1; -. [O75554-1] DR Antibodypedia; 42181; 59 antibodies from 13 providers. DR DNASU; 11193; -. DR Ensembl; ENST00000379487.5; ENSP00000368801.3; ENSG00000120688.9. [O75554-1] DR GeneID; 11193; -. DR KEGG; hsa:11193; -. DR MANE-Select; ENST00000379487.5; ENSP00000368801.3; NM_007187.5; NP_009118.1. DR UCSC; uc001uxt.4; human. [O75554-1] DR AGR; HGNC:12739; -. DR CTD; 11193; -. DR DisGeNET; 11193; -. DR GeneCards; WBP4; -. DR HGNC; HGNC:12739; WBP4. DR HPA; ENSG00000120688; Low tissue specificity. DR MIM; 604981; gene. DR neXtProt; NX_O75554; -. DR OpenTargets; ENSG00000120688; -. DR PharmGKB; PA37350; -. DR VEuPathDB; HostDB:ENSG00000120688; -. DR eggNOG; KOG0150; Eukaryota. DR GeneTree; ENSGT00390000013956; -. DR HOGENOM; CLU_050927_1_0_1; -. DR InParanoid; O75554; -. DR OMA; IDPMRLE; -. DR OrthoDB; 38440at2759; -. DR PhylomeDB; O75554; -. DR TreeFam; TF316671; -. DR PathwayCommons; O75554; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; O75554; -. DR BioGRID-ORCS; 11193; 91 hits in 1158 CRISPR screens. DR ChiTaRS; WBP4; human. DR EvolutionaryTrace; O75554; -. DR GeneWiki; WBP4; -. DR GenomeRNAi; 11193; -. DR Pharos; O75554; Tbio. DR PRO; PR:O75554; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; O75554; Protein. DR Bgee; ENSG00000120688; Expressed in oocyte and 216 other cell types or tissues. DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central. DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB. DR GO; GO:0070064; F:proline-rich region binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central. DR CDD; cd00201; WW; 2. DR DisProt; DP01531; -. DR Gene3D; 2.20.70.10; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2. DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2. DR InterPro; IPR013085; U1-CZ_Znf_C2H2. DR InterPro; IPR040023; WBP4. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR PANTHER; PTHR13173; WW DOMAIN BINDING PROTEIN 4; 1. DR PANTHER; PTHR13173:SF10; WW DOMAIN-BINDING PROTEIN 4; 1. DR Pfam; PF00397; WW; 2. DR Pfam; PF06220; zf-U1; 1. DR SMART; SM00456; WW; 2. DR SMART; SM00451; ZnF_U1; 1. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR SUPFAM; SSF51045; WW domain; 2. DR PROSITE; PS01159; WW_DOMAIN_1; 2. DR PROSITE; PS50020; WW_DOMAIN_2; 2. DR PROSITE; PS50171; ZF_MATRIN; 1. DR Genevisible; O75554; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Metal-binding; mRNA processing; KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Spliceosome; Zinc; Zinc-finger. FT CHAIN 1..376 FT /note="WW domain-binding protein 4" FT /id="PRO_0000076065" FT DOMAIN 122..155 FT /note="WW 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 163..196 FT /note="WW 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT ZN_FING 11..42 FT /note="Matrin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130" FT REGION 94..128 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 189..335 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 356..376 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 357..375 FT /note="Interaction with SNRNP200" FT /evidence="ECO:0000269|PubMed:35241646" FT COMPBIAS 94..108 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 203..220 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 221..270 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 300..314 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 220 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 227 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 229 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 262 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 26..46 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056413" FT VARIANT 113 FT /note="K -> R (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036352" FT MUTAGEN 150 FT /note="W->A: Nearly abolishes activation of pre-mRNA FT splicing. Abolishes interaction with WBP11." FT /evidence="ECO:0000269|PubMed:19592703" FT MUTAGEN 191 FT /note="W->A: Nearly abolishes activation of pre-mRNA FT splicing. Abolishes interaction with WBP11." FT /evidence="ECO:0000269|PubMed:19592703" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:2DK1" FT TURN 134..136 FT /evidence="ECO:0007829|PDB:2JXW" FT STRAND 140..145 FT /evidence="ECO:0007829|PDB:2DK1" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:2DK1" FT STRAND 161..164 FT /evidence="ECO:0007829|PDB:2JXW" FT STRAND 168..174 FT /evidence="ECO:0007829|PDB:2JXW" FT TURN 175..177 FT /evidence="ECO:0007829|PDB:2JXW" FT STRAND 178..183 FT /evidence="ECO:0007829|PDB:2JXW" FT TURN 184..187 FT /evidence="ECO:0007829|PDB:2JXW" FT STRAND 188..192 FT /evidence="ECO:0007829|PDB:2JXW" SQ SEQUENCE 376 AA; 42507 MW; 7A122A29D4325D11 CRC64; MADYWKSQPK KFCDYCKCWI ADNRPSVEFH ERGKNHKENV AKRISEIKQK SLDKAKEEEK ASKEFAAMEA AALKAYQEDL KRLGLESEIL EPSITPVTST IPPTSTSNQQ KEKKEKKKRK KDPSKGRWVE GITSEGYHYY YDLISGASQW EKPEGFQGDL KKTAVKTVWV EGLSEDGFTY YYNTETGESR WEKPDDFIPH TSDLPSSKVN ENSLGTLDES KSSDSHSDSD GEQEAEEGGV STETEKPKIK FKEKNKNSDG GSDPETQKEK SIQKQNSLGS NEEKSKTLKK SNPYGEWQEI KQEVESHEEV DLELPSTENE YVSTSEADGG GEPKVVFKEK TVTSLGVMAD GVAPVFKKRR TENGKSRNLR QRGDDQ //