NXF2_DROME
ID NXF2_DROME Reviewed; 841 AA.
AC Q9VV73; Q0E8E0;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Nuclear RNA export factor 2;
GN Name=nxf2; ORFNames=CG4118;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=11780633;
RA Herold A., Klymenko T., Izaurralde E.;
RT "NXF1/p15 heterodimers are essential for mRNA nuclear export in
RT Drosophila.";
RL RNA 7:1768-1780(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX
RP WITH PANX AND NXT1, INTERACTION WITH PANX, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 751-ILE--GLU-754; 754-GLU--LEU-756; 755-ARG--ILE-758; ARG-755;
RP 811-ILE--GLU-814 AND 835-ILE-PRO-836.
RX PubMed=31219034; DOI=10.7554/elife.47999;
RA Fabry M.H., Ciabrelli F., Munafo M., Eastwood E.L., Kneuss E.,
RA Falciatori I., Falconio F.A., Hannon G.J., Czech B.;
RT "piRNA-guided co-transcriptional silencing coopts nuclear export factors.";
RL Elife 8:0-0(2019).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX
RP WITH PANX; NXT1 AND PIWI, INTERACTION WITH NXT1 AND PANX, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=31368590; DOI=10.15252/embj.2019102870;
RA Murano K., Iwasaki Y.W., Ishizu H., Mashiko A., Shibuya A., Kondo S.,
RA Adachi S., Suzuki S., Saito K., Natsume T., Siomi M.C., Siomi H.;
RT "Nuclear RNA export factor variant initiates piRNA-guided co-
RT transcriptional silencing.";
RL EMBO J. 38:E102870-E102870(2019).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX
RP WITH PANX AND NXT1, INTERACTION WITH PANX AND NXF1, TISSUE SPECIFICITY,
RP DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-823; ASP-837 AND
RP 826-PHE-LEU-827.
RX PubMed=31570835; DOI=10.1038/s41556-019-0396-0;
RA Zhao K., Cheng S., Miao N., Xu P., Lu X., Zhang Y., Wang M., Ouyang X.,
RA Yuan X., Liu W., Lu X., Zhou P., Gu J., Zhang Y., Qiu D., Jin Z., Su C.,
RA Peng C., Wang J.H., Dong M.Q., Wan Y., Ma J., Cheng H., Huang Y., Yu Y.;
RT "A Pandas complex adapted for piRNA-guided transcriptional silencing and
RT heterochromatin formation.";
RL Nat. Cell Biol. 21:1261-1272(2019).
RN [8] {ECO:0007744|PDB:6MRK, ECO:0007744|PDB:6OPF}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 781-841 IN COMPLEX WITH PANX AND
RP NXT1, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A
RP COMPLEX WITH PANX; NXT1 AND PIWI, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-210 AND
RP 236-LYS--ARG-240.
RX PubMed=31384064; DOI=10.1038/s41594-019-0270-6;
RA Batki J., Schnabl J., Wang J., Handler D., Andreev V.I., Stieger C.E.,
RA Novatchkova M., Lampersberger L., Kauneckaite K., Xie W., Mechtler K.,
RA Patel D.J., Brennecke J.;
RT "The nascent RNA binding complex SFiNX licenses piRNA-guided
RT heterochromatin formation.";
RL Nat. Struct. Mol. Biol. 26:720-731(2019).
CC -!- FUNCTION: May be involved in the export of mRNA from the nucleus to the
CC cytoplasm (PubMed:11780633). In the ovaries, forms a complex with nxf2,
CC piwi and Nxt1 which acts as effectors of cotranscriptional transposon
CC silencing (PubMed:31219034, PubMed:31368590, PubMed:31570835,
CC PubMed:31384064). On recruitment to a target transcript, interacts with
CC single stranded RNA, thereby anchoring the complex via the nascent
CC target transcript to chromatin and allowing Panx to recruit silencing
CC effectors to establishing repressive heterochromatin at transposon loci
CC (PubMed:31368590, PubMed:31570835, PubMed:31384064). Does not affect
CC piRNA biogenesis (PubMed:31384064). The interaction with Panx
CC stabilizes the nuclear protein complex (PubMed:31384064). Does not bind
CC nucleoporins, but regulates sbr/Nxf1 binding to nucleoporins and,
CC indirectly, transposon exports (PubMed:31570835, PubMed:31384064).
CC {ECO:0000269|PubMed:11780633, ECO:0000269|PubMed:31219034,
CC ECO:0000269|PubMed:31368590, ECO:0000269|PubMed:31384064,
CC ECO:0000269|PubMed:31570835}.
CC -!- SUBUNIT: In the ovaries, part of a complex composed of at least Panx,
CC nxf2, piwi and Nxt1 (PubMed:31570835, PubMed:31219034, PubMed:31368590,
CC PubMed:31384064). The complex is knowns as Panx-induced
CC cotranscriptional silencing (PICTS) complex, Panx-nxf2-dependent
CC TAP/p15 silencing (Pandas complex), SFiNX (silencing factor interacting
CC nuclear export variant) or piwi-Panx-nxf2-p15 (PPNP) complex
CC (PubMed:31570835, PubMed:31219034, PubMed:31368590, PubMed:31384064).
CC Interacts (via TAP-C domain) with Panx (via NIR region); the
CC interaction is direct (PubMed:31570835, PubMed:31219034,
CC PubMed:31368590). Interacts (via NTF2 domain) with Nxt1; the
CC interaction is direct and prevents Nxt1 binding to nucleoporins
CC (PubMed:31368590). Interacts with sbr/Nxf1 (PubMed:31570835).
CC {ECO:0000269|PubMed:31219034, ECO:0000269|PubMed:31368590,
CC ECO:0000269|PubMed:31384064, ECO:0000269|PubMed:31570835}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00611,
CC ECO:0000269|PubMed:11780633, ECO:0000269|PubMed:31219034}. Nucleus
CC {ECO:0000269|PubMed:31219034, ECO:0000269|PubMed:31368590,
CC ECO:0000269|PubMed:31384064}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:11780633}. Note=Localized in both the nucleoplasm
CC and the cytoplasm (PubMed:11780633). Not detected at the nuclear rim
CC (PubMed:11780633). Nuclear localization depends on interaction with
CC Panx (PubMed:31219034, PubMed:31384064). {ECO:0000269|PubMed:11780633,
CC ECO:0000269|PubMed:31219034, ECO:0000269|PubMed:31384064}.
CC -!- TISSUE SPECIFICITY: Expressed in female gonads (at protein level)
CC (PubMed:31219034, PubMed:31570835, PubMed:31368590, PubMed:31384064).
CC Expressed ubiquitously (PubMed:11780633). {ECO:0000269|PubMed:11780633,
CC ECO:0000269|PubMed:31219034, ECO:0000269|PubMed:31368590,
CC ECO:0000269|PubMed:31384064, ECO:0000269|PubMed:31570835}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development.
CC {ECO:0000269|PubMed:11780633}.
CC -!- DOMAIN: The RNA-binding domain is a non-canonical RNP-type domain.
CC -!- DOMAIN: The TAP-C domain (also known as UBA domain) mediates the
CC interaction with Panx. {ECO:0000269|PubMed:31219034,
CC ECO:0000269|PubMed:31368590, ECO:0000269|PubMed:31384064,
CC ECO:0000269|PubMed:31570835}.
CC -!- DISRUPTION PHENOTYPE: Results in sterility where fewer eggs are laid
CC and none reach larval stage (PubMed:31219034, PubMed:31384064).
CC Increases transposon expression (PubMed:31219034, PubMed:31384064).
CC RNAi-mediated knockdown in the germline does not affect ovary
CC morphology but results in severe fertility defects where eggs are laied
CC but do not hatch (PubMed:31368590). RNAi-mediated knockdown in the
CC germline increases transposon expression and impairs Panx localization
CC in nurse cells by reducing its stability (PubMed:31219034,
CC PubMed:31570835, PubMed:31368590, PubMed:31384064).
CC {ECO:0000269|PubMed:31219034, ECO:0000269|PubMed:31368590,
CC ECO:0000269|PubMed:31384064, ECO:0000269|PubMed:31570835}.
CC -!- SIMILARITY: Belongs to the NXF family. {ECO:0000305}.
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; AJ312282; CAC41644.1; -; mRNA.
DR EMBL; AE014296; AAF49448.3; -; Genomic_DNA.
DR EMBL; AY075582; AAL68387.1; -; mRNA.
DR RefSeq; NP_524111.3; NM_079387.6.
DR RefSeq; NP_730179.2; NM_168674.4.
DR PDB; 6IEW; X-ray; 1.50 A; A=789-841.
DR PDB; 6MRK; X-ray; 2.80 A; A/B=573-777.
DR PDB; 6OPF; X-ray; 2.00 A; A/B/D/F=781-841.
DR PDBsum; 6IEW; -.
DR PDBsum; 6MRK; -.
DR PDBsum; 6OPF; -.
DR AlphaFoldDB; Q9VV73; -.
DR SMR; Q9VV73; -.
DR BioGRID; 65146; 17.
DR IntAct; Q9VV73; 1.
DR STRING; 7227.FBpp0088483; -.
DR PaxDb; Q9VV73; -.
DR PRIDE; Q9VV73; -.
DR EnsemblMetazoa; FBtr0089478; FBpp0088483; FBgn0036640.
DR EnsemblMetazoa; FBtr0089479; FBpp0088484; FBgn0036640.
DR GeneID; 39843; -.
DR KEGG; dme:Dmel_CG4118; -.
DR CTD; 56001; -.
DR FlyBase; FBgn0036640; nxf2.
DR VEuPathDB; VectorBase:FBgn0036640; -.
DR eggNOG; KOG3763; Eukaryota.
DR GeneTree; ENSGT00390000007539; -.
DR HOGENOM; CLU_016827_0_0_1; -.
DR InParanoid; Q9VV73; -.
DR OMA; YPCYYKY; -.
DR OrthoDB; 231208at2759; -.
DR PhylomeDB; Q9VV73; -.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR SignaLink; Q9VV73; -.
DR BioGRID-ORCS; 39843; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39843; -.
DR PRO; PR:Q9VV73; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036640; Expressed in egg chamber and 32 other tissues.
DR ExpressionAtlas; Q9VV73; baseline and differential.
DR Genevisible; Q9VV73; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0010529; P:negative regulation of transposition; IMP:UniProtKB.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR InterPro; IPR030217; NXF_fam.
DR InterPro; IPR005637; TAP_C_dom.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR10662; PTHR10662; 3.
DR Pfam; PF03943; TAP_C; 1.
DR SMART; SM00804; TAP_C; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR PROSITE; PS51450; LRR; 5.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS51281; TAP_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Leucine-rich repeat; mRNA transport; Nucleus;
KW Reference proteome; Repeat; RNA-binding; Transport.
FT CHAIN 1..841
FT /note="Nuclear RNA export factor 2"
FT /id="PRO_0000220539"
FT REPEAT 200..221
FT /note="LRR 1"
FT REPEAT 224..245
FT /note="LRR 2"
FT REPEAT 249..270
FT /note="LRR 3"
FT DOMAIN 325..408
FT /note="RRM"
FT REPEAT 475..496
FT /note="LRR 4"
FT REPEAT 500..521
FT /note="LRR 5"
FT REPEAT 524..545
FT /note="LRR 6"
FT DOMAIN 585..758
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT DOMAIN 788..841
FT /note="TAP-C"
FT /evidence="ECO:0000269|PubMed:31219034,
FT ECO:0000269|PubMed:31368590, ECO:0000269|PubMed:31384064,
FT ECO:0000269|PubMed:31570835"
FT REGION 1..285
FT /note="RNA-binding unit probably involved in Piwi-dependent
FT recruitment and single-stranded RNA-PPNP complex formation"
FT /evidence="ECO:0000269|PubMed:31368590,
FT ECO:0000269|PubMed:31384064, ECO:0000269|PubMed:31570835"
FT REGION 286..553
FT /note="Necessary for silencing function"
FT /evidence="ECO:0000269|PubMed:31570835"
FT MUTAGEN 210
FT /note="R->A: Abolishes RNA-binding; when associated with
FT 236-A--A-240."
FT /evidence="ECO:0000269|PubMed:31384064"
FT MUTAGEN 236..240
FT /note="KSAER->ASAEA: Abolishes RNA-binding; when associated
FT with A-210."
FT /evidence="ECO:0000269|PubMed:31384064"
FT MUTAGEN 751..754
FT /note="IANE->GGAA: Retains localization to the nucleus and
FT interaction with Panx but reduces interaction with Nxt1.
FT Increases transposon expression after loss of gene."
FT /evidence="ECO:0000269|PubMed:31219034"
FT MUTAGEN 754..756
FT /note="ERL->AGA: Retains localization to the nucleus and
FT interaction with Panx but reduces interaction with Nxt1.
FT Increases transposon expression after loss of gene."
FT /evidence="ECO:0000269|PubMed:31219034"
FT MUTAGEN 755..758
FT /note="RLHI->AGVK: Retains localization to the nucleus and
FT interaction with Panx. Increases transposon expression
FT after loss of gene."
FT /evidence="ECO:0000269|PubMed:31219034"
FT MUTAGEN 755
FT /note="R->G: Retains localization to the nucleus and
FT interaction with Panx. Reduces transposon expression after
FT loss of gene."
FT /evidence="ECO:0000269|PubMed:31219034"
FT MUTAGEN 811..814
FT /note="IVEE->KRGG: Reduces binding to Panx, increases
FT cytoplasmic localization and increases transposon
FT expression after loss of gene."
FT /evidence="ECO:0000269|PubMed:31219034"
FT MUTAGEN 823
FT /note="L->A: Reduces binding to Panx."
FT /evidence="ECO:0000269|PubMed:31570835"
FT MUTAGEN 826..827
FT /note="FI->AA: Reduces binding to Panx."
FT /evidence="ECO:0000269|PubMed:31570835"
FT MUTAGEN 835..836
FT /note="IP->NA: Reduces binding to Panx, increases
FT cytoplasmic localization and increases transposon
FT expression after loss of gene."
FT /evidence="ECO:0000269|PubMed:31219034"
FT MUTAGEN 837
FT /note="D->A: Reduces binding to Panx."
FT /evidence="ECO:0000269|PubMed:31570835"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:6MRK"
FT HELIX 583..598
FT /evidence="ECO:0007829|PDB:6MRK"
FT HELIX 600..609
FT /evidence="ECO:0007829|PDB:6MRK"
FT STRAND 615..620
FT /evidence="ECO:0007829|PDB:6MRK"
FT HELIX 630..641
FT /evidence="ECO:0007829|PDB:6MRK"
FT HELIX 652..656
FT /evidence="ECO:0007829|PDB:6MRK"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:6MRK"
FT HELIX 663..670
FT /evidence="ECO:0007829|PDB:6MRK"
FT STRAND 675..678
FT /evidence="ECO:0007829|PDB:6MRK"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:6MRK"
FT STRAND 684..706
FT /evidence="ECO:0007829|PDB:6MRK"
FT STRAND 723..737
FT /evidence="ECO:0007829|PDB:6MRK"
FT STRAND 747..759
FT /evidence="ECO:0007829|PDB:6MRK"
FT HELIX 763..768
FT /evidence="ECO:0007829|PDB:6MRK"
FT HELIX 788..801
FT /evidence="ECO:0007829|PDB:6IEW"
FT HELIX 805..814
FT /evidence="ECO:0007829|PDB:6IEW"
FT TURN 815..817
FT /evidence="ECO:0007829|PDB:6IEW"
FT HELIX 819..831
FT /evidence="ECO:0007829|PDB:6IEW"
FT HELIX 837..839
FT /evidence="ECO:0007829|PDB:6IEW"
SQ SEQUENCE 841 AA; 96635 MW; 581CE6B0C57FF098 CRC64;
MPNQMRVLDF GDGSVPIQLD YPDSKIFSKC SSYGDRVPGT HWNEITVHHK GRLEYSPNPE
QIILDALYQA IDGADFFPVF YQRGKNMDTM LVRNCKAAID KLFKQRLSIN LKGGASIPIS
IQLGVAQYQR HQITPTFHIA RVVTRLMKQL IQRDGVDGLL NLDNFGSHPE FKNLVVSLGN
PSILMNVCQV IHNDDNERFR LNGFILSNNR IRDIRPLTLL ANVDYALLDL RGNKIKSAER
LCRALEQFRA RELLLENNPI VKISNFPANI KSLESNFELV DGKPFNMLHK IFSPLDVEID
LEVDGARIDT NNMWKLPEFE NSQHWHAFMI PDPSHEFNQE VFFDFFFIRL DPTLSNFYPC
YYKYINTEHV FLVRNCFDQI AHLVNNCNLE MTIPTGDRIF RYYLRMNVST VKQHHVDPEE
CIQKAVSQCY VAQNRMLNLE RFHSRECLKD VMVSLSSPKI LTYVLSVASR KFMTTCSEIR
LCHNKVLVLD GAHVLGMMGC LRAVDLSHNW VQDLSSIHSL GNLPLKSLVL HGNKLCRNYR
LPSEYVRAVK EVFPQLTTLD GVDLQTNPGQ SLQKNFLCDT GAYELVGAFL ENYLREFEND
EFRHNLYKYY SENSIFTLTC NYNVVQNHQT PKILQRLSKY NRHARNLRNK DYSKASDGVF
FGCTYIVEIL LQLPRVTHDF HSLQTDVMHY NGKGAVIYVA GLLRDEPPST RNGHGSKTDI
GGVLLGFSRQ FVVTFDEANL GLGKRARRLK IANERLHITN PSKTAIRNAF SVNFPDPSER
QAEEDSLDVK DHKLLLFQEV TGLISTWVTS IVEEADWDFE RALKLFIQKN ADHEIPDLAF
A
