SMG_DROME
ID SMG_DROME Reviewed; 999 AA.
AC Q23972; A4V1P7; B7Z0F4; B7Z0F5; Q9V3T0; Q9VSS8;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Protein Smaug;
GN Name=smg; ORFNames=CG5263;
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] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP RNA-BINDING, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP OSK.
RC STRAIN=Iso-1;
RX PubMed=10488336; DOI=10.1016/s1097-2765(00)80368-8;
RA Dahanukar A., Walker J.A., Wharton R.P.;
RT "Smaug, a novel RNA-binding protein that operates a translational switch in
RT Drosophila.";
RL Mol. Cell 4:209-218(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 95-102;
RP 272-287; 461-469; 570-580; 740-754; 776-788; 935-953; 966-977 AND 980-991,
RP FUNCTION, RNA-BINDING, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=10606265; DOI=10.1017/s1355838299991392;
RA Smibert C.A., Lie Y.S., Shillinglaw W., Henzel W.J., Macdonald P.M.;
RT "Smaug, a novel and conserved protein, contributes to repression of nanos
RT mRNA translation in vitro.";
RL RNA 5:1535-1547(1999).
RN [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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 [6]
RP NUCLEOTIDE SEQUENCE OF 573-792 (ISOFORMS A/D).
RC STRAIN=Sevelin; TISSUE=Embryo;
RA Edgar B.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=8895661; DOI=10.1101/gad.10.20.2600;
RA Smibert C.A., Wilson J.E., Kerr K., Macdonald P.M.;
RT "smaug protein represses translation of unlocalized nanos mRNA in the
RT Drosophila embryo.";
RL Genes Dev. 10:2600-2609(1996).
RN [8]
RP RNA-BINDING.
RX PubMed=10882131; DOI=10.1016/s1097-2765(00)80440-2;
RA Crucs S., Chatterjee S., Gavis E.R.;
RT "Overlapping but distinct RNA elements control repression and activation of
RT nanos translation.";
RL Mol. Cell 5:457-467(2000).
RN [9]
RP MUTAGENESIS OF LYS-606; ARG-609; HIS-611; LYS-612; TYR-613 AND ALA-642.
RX PubMed=12858164; DOI=10.1038/nsb956;
RA Aviv T., Lin Z., Lau S., Rendl L.M., Sicheri F., Smibert C.A.;
RT "The RNA-binding SAM domain of Smaug defines a new family of post-
RT transcriptional regulators.";
RL Nat. Struct. Biol. 10:614-621(2003).
RN [10]
RP FUNCTION, AND INTERACTION WITH CUP.
RX PubMed=14685270; DOI=10.1038/sj.emboj.7600026;
RA Nelson M.R., Leidal A.M., Smibert C.A.;
RT "Drosophila Cup is an eIF4E-binding protein that functions in Smaug-
RT mediated translational repression.";
RL EMBO J. 23:150-159(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564; SER-575 AND SER-972, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [12]
RP INTERACTION WITH AUB, TWIN AND AGO3, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=20953170; DOI=10.1038/nature09465;
RA Rouget C., Papin C., Boureux A., Meunier A.C., Franco B., Robine N.,
RA Lai E.C., Pelisson A., Simonelig M.;
RT "Maternal mRNA deadenylation and decay by the piRNA pathway in the early
RT Drosophila embryo.";
RL Nature 467:1128-1132(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 596-764, AND MUTAGENESIS OF
RP PHE-632; GLN-634; LYS-640; ASN-658; GLN-665; VAL-724 AND HIS-749.
RX PubMed=12820967; DOI=10.1016/s1097-2765(03)00178-3;
RA Green J.B., Gardner C.D., Wharton R.P., Aggarwal A.K.;
RT "RNA recognition via the SAM domain of Smaug.";
RL Mol. Cell 11:1537-1548(2003).
CC -!- FUNCTION: Translation regulator that binds to the 3'-UTR of specific
CC mRNAs such as nanos (nos) and prevents their translation. Prevents
CC translation of unlocalized nos in the bulk cytoplasm via the
CC recruitment of cup. {ECO:0000269|PubMed:10488336,
CC ECO:0000269|PubMed:10606265, ECO:0000269|PubMed:14685270,
CC ECO:0000269|PubMed:8895661}.
CC -!- SUBUNIT: Interacts with oskar (osk). Binds to the 3'-UTR of nos.
CC Interacts with cup, which in turn recruits eIF4-E, leading to an
CC indirect interaction between smg and eIF4-E that prevents mRNA
CC translation. Forms a complex with aub, twin, AGO3, nos mRNA and piRNAs
CC that targets the nos 3'-untranslated region, in early embryos.
CC {ECO:0000269|PubMed:10488336, ECO:0000269|PubMed:14685270,
CC ECO:0000269|PubMed:20953170}.
CC -!- INTERACTION:
CC Q23972; Q9VMA3: cup; NbExp=4; IntAct=EBI-108638, EBI-95398;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10488336,
CC ECO:0000269|PubMed:20953170}. Note=In the cytoplasm of syncytial
CC embryos, accumulates in discrete foci.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=B, C, E;
CC IsoId=Q23972-1; Sequence=Displayed;
CC Name=D;
CC IsoId=Q23972-2; Sequence=VSP_039395;
CC -!- TISSUE SPECIFICITY: At syncytial blastoderm, it is located throughout
CC the bulk cytoplasm and pole plasm. By the time of cellularization, it
CC concentrates at the posterior pole. {ECO:0000269|PubMed:10488336,
CC ECO:0000269|PubMed:10606265, ECO:0000269|PubMed:20953170}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally. The protein accumulates
CC during the first 3 hours after fertilization, and then decreases
CC rapidly. {ECO:0000269|PubMed:10488336}.
CC -!- DOMAIN: The SAM domain mediates the association with the 3'-UTR of
CC specific mRNAs.
CC -!- SIMILARITY: Belongs to the SMAUG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA03462.1; Type=Miscellaneous discrepancy; Note=Absence of a large region from Gly-793 to the end of the coding region that changes the frame.; Evidence={ECO:0000305};
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DR EMBL; AF159852; AAD54965.1; -; mRNA.
DR EMBL; AF132213; AAF61321.1; -; mRNA.
DR EMBL; AE014296; AAF50333.3; -; Genomic_DNA.
DR EMBL; AE014296; AAF50334.3; -; Genomic_DNA.
DR EMBL; AE014296; ACL83279.1; -; Genomic_DNA.
DR EMBL; AE014296; ACL83280.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11981.1; -; Genomic_DNA.
DR EMBL; AY058607; AAL13836.1; -; mRNA.
DR EMBL; U03277; AAA03462.1; ALT_SEQ; Unassigned_DNA.
DR RefSeq; NP_001137924.1; NM_001144452.2. [Q23972-2]
DR RefSeq; NP_001137925.1; NM_001144453.2. [Q23972-1]
DR RefSeq; NP_523987.1; NM_079263.3. [Q23972-1]
DR RefSeq; NP_729441.1; NM_168309.3. [Q23972-1]
DR RefSeq; NP_729442.1; NM_168310.3. [Q23972-1]
DR PDB; 1OXJ; X-ray; 1.80 A; A=593-764.
DR PDBsum; 1OXJ; -.
DR AlphaFoldDB; Q23972; -.
DR SMR; Q23972; -.
DR BioGRID; 64438; 50.
DR IntAct; Q23972; 8.
DR MINT; Q23972; -.
DR STRING; 7227.FBpp0288542; -.
DR iPTMnet; Q23972; -.
DR PaxDb; Q23972; -.
DR ABCD; Q23972; 10 sequenced antibodies.
DR DNASU; 39034; -.
DR EnsemblMetazoa; FBtr0076549; FBpp0076276; FBgn0016070. [Q23972-1]
DR EnsemblMetazoa; FBtr0076550; FBpp0076277; FBgn0016070. [Q23972-1]
DR EnsemblMetazoa; FBtr0076551; FBpp0076278; FBgn0016070. [Q23972-1]
DR EnsemblMetazoa; FBtr0290103; FBpp0288542; FBgn0016070. [Q23972-2]
DR EnsemblMetazoa; FBtr0290104; FBpp0288543; FBgn0016070. [Q23972-1]
DR GeneID; 39034; -.
DR KEGG; dme:Dmel_CG5263; -.
DR UCSC; CG5263-RA; d. melanogaster. [Q23972-1]
DR CTD; 39034; -.
DR FlyBase; FBgn0016070; smg.
DR VEuPathDB; VectorBase:FBgn0016070; -.
DR eggNOG; KOG3791; Eukaryota.
DR GeneTree; ENSGT00940000169155; -.
DR HOGENOM; CLU_003304_0_0_1; -.
DR InParanoid; Q23972; -.
DR OMA; HHSQHAQ; -.
DR PhylomeDB; Q23972; -.
DR SignaLink; Q23972; -.
DR BioGRID-ORCS; 39034; 0 hits in 3 CRISPR screens.
DR ChiTaRS; smg; fly.
DR EvolutionaryTrace; Q23972; -.
DR GenomeRNAi; 39034; -.
DR PRO; PR:Q23972; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0016070; Expressed in cleaving embryo and 41 other tissues.
DR Genevisible; Q23972; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:FlyBase.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; TAS:FlyBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; TAS:FlyBase.
DR GO; GO:0017022; F:myosin binding; IPI:FlyBase.
DR GO; GO:0030371; F:translation repressor activity; IDA:UniProtKB.
DR GO; GO:0051236; P:establishment of RNA localization; IMP:FlyBase.
DR GO; GO:0017148; P:negative regulation of translation; IDA:FlyBase.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IMP:FlyBase.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:FlyBase.
DR GO; GO:0043488; P:regulation of mRNA stability; IMP:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd09557; SAM_Smaug; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.170; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015327; PHAT_dom.
DR InterPro; IPR037093; PHAT_dom_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR037634; Smaug_SAM.
DR Pfam; PF09246; PHAT; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repressor;
KW RNA-binding; Translation regulation.
FT CHAIN 1..999
FT /note="Protein Smaug"
FT /id="PRO_0000071972"
FT DOMAIN 600..654
FT /note="SAM"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..763
FT /note="Interaction with cup"
FT REGION 773..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 972
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 987..999
FT /note="ENLAKFDQHFTLF -> VSNPNQNQDQHDQPQILINNNNNNSMLNNNLINQQ
FT QLQLLAAAAAAVGSGSCLCSNGGGGACVHNICHQSSKNNNHGVDHCLSQSPLGSLGMSP
FT HVTEYKMNDFKSLEQLETLCRQMTEQAMN (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_039395"
FT MUTAGEN 606
FT /note="K->A: Reduced RNA-binding. Complete loss; when
FT associated with R-609."
FT /evidence="ECO:0000269|PubMed:12858164"
FT MUTAGEN 609
FT /note="R->A: Reduced RNA-binding. Complete loss; when
FT associated with A-606."
FT /evidence="ECO:0000269|PubMed:12858164"
FT MUTAGEN 611
FT /note="H->S,Q: Reduced RNA-binding."
FT /evidence="ECO:0000269|PubMed:12858164"
FT MUTAGEN 612
FT /note="K->Q: Loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:12858164"
FT MUTAGEN 613
FT /note="Y->F: Reduced RNA-binding."
FT /evidence="ECO:0000269|PubMed:12858164"
FT MUTAGEN 632
FT /note="F->L: No effect on RNA-binding; when associated with
FT L-634."
FT /evidence="ECO:0000269|PubMed:12820967"
FT MUTAGEN 634
FT /note="Q->L: No effect on RNA-binding; when associated with
FT L-632."
FT /evidence="ECO:0000269|PubMed:12820967"
FT MUTAGEN 640
FT /note="K->S: Reduced RNA-binding."
FT /evidence="ECO:0000269|PubMed:12820967"
FT MUTAGEN 642
FT /note="A->H,Q: Loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:12858164"
FT MUTAGEN 658
FT /note="N->D: No effect on RNA-binding; when associated with
FT R-665; I-724 and R-749."
FT /evidence="ECO:0000269|PubMed:12820967"
FT MUTAGEN 665
FT /note="Q->R: No effect on RNA-binding; when associated with
FT D-658; I-724 and R-749."
FT /evidence="ECO:0000269|PubMed:12820967"
FT MUTAGEN 724
FT /note="V->I: No effect on RNA-binding; when associated with
FT D-658; R-665 and R-749."
FT /evidence="ECO:0000269|PubMed:12820967"
FT MUTAGEN 739
FT /note="R->S: No effect on RNA-binding."
FT MUTAGEN 749
FT /note="H->R: No effect on RNA-binding; when associated with
FT D-658; I-724 and R-665."
FT /evidence="ECO:0000269|PubMed:12820967"
FT HELIX 601..607
FT /evidence="ECO:0007829|PDB:1OXJ"
FT HELIX 611..617
FT /evidence="ECO:0007829|PDB:1OXJ"
FT HELIX 622..625
FT /evidence="ECO:0007829|PDB:1OXJ"
FT HELIX 630..635
FT /evidence="ECO:0007829|PDB:1OXJ"
FT HELIX 640..668
FT /evidence="ECO:0007829|PDB:1OXJ"
FT HELIX 674..682
FT /evidence="ECO:0007829|PDB:1OXJ"
FT TURN 683..686
FT /evidence="ECO:0007829|PDB:1OXJ"
FT HELIX 698..700
FT /evidence="ECO:0007829|PDB:1OXJ"
FT HELIX 702..718
FT /evidence="ECO:0007829|PDB:1OXJ"
FT HELIX 723..725
FT /evidence="ECO:0007829|PDB:1OXJ"
FT HELIX 727..741
FT /evidence="ECO:0007829|PDB:1OXJ"
FT HELIX 744..749
FT /evidence="ECO:0007829|PDB:1OXJ"
FT HELIX 750..761
FT /evidence="ECO:0007829|PDB:1OXJ"
SQ SEQUENCE 999 AA; 109065 MW; 6EBB615435F07190 CRC64;
MKYATGTDNA MTSGISGQTN NSNSASNEMQ PTTSTPTAAH KEATSTATTT ATYANGNPNS
NANPSQSQPS NALFCEQVTT VTNLFEKWND CERTVVMYAL LKRLRYPSLK FLQYSIDSNL
TQNLGTSQTN LSSVVIDINA NNPVYLQNLL NAYKTFQPCD LLDAMSSSSS DKDSMPCYGS
DFQITTSAQC DERKLYARKE DILHEVLNML PLLKPGNEEA KLIYLTLIPV AVKDTMQQIV
PTELVQQIFS YLLIHPAITS EDRRSLNIWL RHLEDHIQAA AAGLTNRSYF LQPSPQLVAG
GSSTGSGSCS SSATSSSTAS CSSVASSSLC PASGSRSSRT NDWQTIAPPS KQLQNKLAGD
WRGNGGGSSS GSINPLCDNL NGITLNELAS SQNSLGLSLE GSSSLVNGVV AGAGSMLGIA
GGDDHDTSFS KNGTEILDFD PVTADMGEAC SLASSSLCGR NGGNPVEDRS QPPPNLQQQL
LQPPPYASIL MGNVGDQFGE INRWSLDSKI AALKTRRSNS LTTQTISSCS SSSNSSVITV
NDNCSNSTEN LAQFANKPRS FSLSIEHQRG ALMNSGSDTR LDEFKPNYIK FHTRNVGMSG
IGLWLKSLRL HKYIELFKNM TYEEMLLITE DFLQSVGVTK GASHKLALCI DKLKERANIL
NRVEQELLSG QMELSTAVEE LTNIVLTPMK PLESPGPPEE NIGLRFLKVI DIVTNTLQQD
PYAVQDDETL GVLMWILDRS IHNEAFMNHA SQLKDLKFKL SKMKISMVPK MHHVKPAGVG
PNNGNINKPR WNGKTRKCDT KNGSNDRINN RKNSNDMLNF SLNCLPHPLP HHSQQAPPPL
PQFDYNGYGG GPSHQPQYKS SSYPSFMGNP QQQPPPPPSS KSHHHPQQMQ QMLQQHNHFP
ALPQQTPPQS HRRSLNNLIL VAGGPQQPQQ LIFKPGQGVL TNNGSNDNLV LERNQQSQQQ
QQQRKLSGGV SSAEQQPKKT MAAVVMENLA KFDQHFTLF
