WBP4_HUMAN
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 03-AUG-2022, entry version 172.
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]
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).
CC {ECO:0000250|UniProtKB:Q61048, ECO:0000269|PubMed:19592703,
CC ECO:0000269|PubMed:28781166, 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 SMR; O75554; -.
DR BioGRID; 116363; 114.
DR IntAct; O75554; 30.
DR MINT; O75554; -.
DR STRING; 9606.ENSP00000368801; -.
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; O75554; -.
DR PeptideAtlas; O75554; -.
DR PRIDE; O75554; -.
DR ProteomicsDB; 50083; -. [O75554-1]
DR ProteomicsDB; 6615; -.
DR TopDownProteomics; O75554-1; -. [O75554-1]
DR Antibodypedia; 42181; 53 antibodies from 12 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 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; 1585242at2759; -.
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; 81 hits in 1079 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 214 other tissues.
DR Genevisible; O75554; HS.
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 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; PTHR13173; 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; SSF51045; SSF51045; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
DR PROSITE; PS50171; ZF_MATRIN; 1.
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 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
