GGYF1_DROME
ID GGYF1_DROME Reviewed; 1574 AA.
AC Q7KQM6; B8A422; D1YSG2; E8NH20; Q961G4; Q9V482;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=GIGYF family protein Gyf {ECO:0000303|PubMed:26086452};
DE Short=Gigyf {ECO:0000312|FlyBase:FBgn0039936};
GN Name=Gyf {ECO:0000303|PubMed:26086452, ECO:0000312|FlyBase:FBgn0039936};
GN ORFNames=CG11148 {ECO:0000312|FlyBase:FBgn0039936};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1142-1574 (ISOFORMS D/G).
RC STRAIN=Berkeley; TISSUE=Head;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-391 (ISOFORM D), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-1543 (ISOFORM G).
RC STRAIN=Berkeley;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272; SER-399; SER-403;
RP SER-407; THR-412; SER-1007 AND SER-1370, AND IDENTIFICATION BY MASS
RP 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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26086452; DOI=10.1080/15548627.2015.1063766;
RA Kim M., Semple I., Kim B., Kiers A., Nam S., Park H.W., Park H., Ro S.H.,
RA Kim J.S., Juhasz G., Lee J.H.;
RT "Drosophila Gyf/GRB10 interacting GYF protein is an autophagy regulator
RT that controls neuron and muscle homeostasis.";
RL Autophagy 11:1358-1372(2015).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE 4EHP-GYF2 COMPLEX, INTERACTION WITH
RP DDX6/ME31B; PATR-1; EDC3; GE-1; NOT1; NOT3; POP2; TWIN; RGA; PAN2 AND PAN3,
RP AND MUTAGENESIS OF TYR-58; TYR-60; MET-65; 331-LEU--LYS-374; TYR-571;
RP PHE-582; TRP-590 AND PHE-596.
RX PubMed=31114929; DOI=10.1093/nar/gkz429;
RA Ruscica V., Bawankar P., Peter D., Helms S., Igreja C., Izaurralde E.;
RT "Direct role for the Drosophila GIGYF protein in 4EHP-mediated mRNA
RT repression.";
RL Nucleic Acids Res. 47:7035-7048(2019).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 343-369, INTERACTION WITH
RP DDX6/ME31B, AND MUTAGENESIS OF TRP-349; PHE-361 AND PHE-367.
RX PubMed=31439631; DOI=10.1101/gad.329219.119;
RA Peter D., Ruscica V., Bawankar P., Weber R., Helms S., Valkov E.,
RA Igreja C., Izaurralde E.;
RT "Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated
RT translational repression.";
RL Genes Dev. 33:1355-1360(2019).
CC -!- FUNCTION: Key component of the 4EHP-GYF2 complex, a multiprotein
CC complex that acts as a repressor of translation initiation
CC (PubMed:31114929). In the 4EHP-GYF2 complex, promotes translational
CC repression and decay of mRNA targets by recruiting and bridging the
CC association of the 4EHP complex with decapping effector proteins, such
CC as me31B and Patr-1, and the deadenylation CCR4-NOT complex
CC (PubMed:31114929). Involved in regulating starvation-induced,
CC developmental and physiological autophagy, which is critical for
CC eliminating ubiquitinated proteins and dysfunctional organelles in
CC order to maintain tissue homeostasis (PubMed:26086452).
CC {ECO:0000269|PubMed:26086452, ECO:0000269|PubMed:31114929}.
CC -!- SUBUNIT: Component of the 4EHP-GYF2 complex, composed of at least
CC eIF4EHP and Gyf (PubMed:31114929). Interacts (via N-terminus) with
CC eIF4EHP; interaction is required for eIF4EHP-mediated translational
CC repression and mRNA decay (PubMed:31114929). Interacts (via me31B
CC binding motif) with the decapping activator DDX6/ME31B (via RecA-like
CC domain 2), and also interacts (via GYF domain) with the decapping
CC effector protein Patr-1 (PubMed:31114929, PubMed:31439631). Also
CC interacts with other decapping effector proteins, such as Edc3 and Ge-1
CC (PubMed:31114929). Interacts with CCR4-NOT deadenylase complex members
CC Not1, Not3, Pop2 and twin, and other components of the deadenylation
CC complexes such as Rga, PAN2 and PAN3 (PubMed:31114929).
CC {ECO:0000269|PubMed:31114929, ECO:0000269|PubMed:31439631}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=G; Synonyms=H;
CC IsoId=Q7KQM6-1; Sequence=Displayed;
CC Name=D; Synonyms=E, F;
CC IsoId=Q7KQM6-2; Sequence=VSP_037201;
CC -!- DISRUPTION PHENOTYPE: Larvae and adults display defects in starvation-
CC induced, developmental and physiological autophagy, which result in the
CC accumulation of autophagosomes, autolysosomes, and increased Atg8a
CC expression (PubMed:26086452). Adults display reduced locomotion and
CC decreased life span, likely due to the dysregulation of autophagy which
CC results in the accumulation of ubiquitinated proteins and dysfunctional
CC mitochondria in neuronal and muscle tissues (PubMed:26086452). TORC1
CC signaling is also inhibited, possibly to compensate for the loss of
CC autophagy (PubMed:26086452). {ECO:0000269|PubMed:26086452}.
CC -!- SIMILARITY: Belongs to the GIGYF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK93031.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ACL68761.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ADV15453.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014135; AAF59406.3; -; Genomic_DNA.
DR EMBL; AE014135; AAS64612.2; -; Genomic_DNA.
DR EMBL; AE014135; ACZ95096.1; -; Genomic_DNA.
DR EMBL; AE014135; ACZ95097.1; -; Genomic_DNA.
DR EMBL; AY051607; AAK93031.1; ALT_INIT; mRNA.
DR EMBL; BT056314; ACL68761.1; ALT_INIT; mRNA.
DR EMBL; BT125874; ADV15453.1; ALT_INIT; mRNA.
DR RefSeq; NP_001162827.1; NM_001169356.2. [Q7KQM6-1]
DR RefSeq; NP_001162828.1; NM_001169357.4. [Q7KQM6-1]
DR RefSeq; NP_651950.3; NM_143693.4. [Q7KQM6-2]
DR RefSeq; NP_995600.2; NM_205878.3. [Q7KQM6-2]
DR PDB; 6S8R; X-ray; 2.41 A; B=343-369.
DR PDBsum; 6S8R; -.
DR AlphaFoldDB; Q7KQM6; -.
DR SMR; Q7KQM6; -.
DR BioGRID; 68666; 25.
DR IntAct; Q7KQM6; 7.
DR MINT; Q7KQM6; -.
DR STRING; 7227.FBpp0290107; -.
DR iPTMnet; Q7KQM6; -.
DR PaxDb; Q7KQM6; -.
DR PRIDE; Q7KQM6; -.
DR EnsemblMetazoa; FBtr0300882; FBpp0290104; FBgn0039936. [Q7KQM6-2]
DR EnsemblMetazoa; FBtr0300884; FBpp0290106; FBgn0039936. [Q7KQM6-2]
DR EnsemblMetazoa; FBtr0300885; FBpp0290107; FBgn0039936. [Q7KQM6-1]
DR EnsemblMetazoa; FBtr0300886; FBpp0290108; FBgn0039936. [Q7KQM6-1]
DR GeneID; 43842; -.
DR KEGG; dme:Dmel_CG11148; -.
DR UCSC; CG11148-RA; d. melanogaster.
DR UCSC; CG11148-RB; d. melanogaster. [Q7KQM6-1]
DR CTD; 43842; -.
DR FlyBase; FBgn0039936; Gyf.
DR VEuPathDB; VectorBase:FBgn0039936; -.
DR eggNOG; KOG1862; Eukaryota.
DR GeneTree; ENSGT00940000168947; -.
DR HOGENOM; CLU_002878_0_0_1; -.
DR InParanoid; Q7KQM6; -.
DR OMA; AIEMTEW; -.
DR PhylomeDB; Q7KQM6; -.
DR SignaLink; Q7KQM6; -.
DR BioGRID-ORCS; 43842; 0 hits in 3 CRISPR screens.
DR ChiTaRS; CG11148; fly.
DR GenomeRNAi; 43842; -.
DR PRO; PR:Q7KQM6; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0039936; Expressed in eye disc (Drosophila) and 26 other tissues.
DR Genevisible; Q7KQM6; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IDA:UniProtKB.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IMP:UniProtKB.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IGI:FlyBase.
DR GO; GO:0070050; P:neuron cellular homeostasis; IGI:FlyBase.
DR GO; GO:0010506; P:regulation of autophagy; IGI:FlyBase.
DR CDD; cd00072; GYF; 1.
DR Gene3D; 3.30.1490.40; -; 1.
DR InterPro; IPR003169; GYF.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR Pfam; PF02213; GYF; 1.
DR SMART; SM00444; GYF; 1.
DR SUPFAM; SSF55277; SSF55277; 1.
DR PROSITE; PS50829; GYF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Phosphoprotein; Reference proteome.
FT CHAIN 1..1574
FT /note="GIGYF family protein Gyf"
FT /id="PRO_0000372840"
FT DOMAIN 566..614
FT /note="GYF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00101"
FT REGION 1..640
FT /note="Important for promoting translational repression"
FT /evidence="ECO:0000269|PubMed:31114929"
FT REGION 100..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1142..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1507..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 341..369
FT /note="me31B binding motif"
FT /evidence="ECO:0000269|PubMed:31114929"
FT COMPBIAS 100..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 412
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1007
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1370
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 113..119
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_037201"
FT MUTAGEN 58
FT /note="Y->A: In C; impairs interaction with eIF4EHP but has
FT no effect on translational repression or induction of mRNA
FT decay; when associated with A-60 and a-65."
FT /evidence="ECO:0000269|PubMed:31114929"
FT MUTAGEN 60
FT /note="Y->A: In C; impairs interaction with eIF4EHP but has
FT no effect on translational repression or induction of mRNA
FT decay; when associated with A-58 and a-65."
FT /evidence="ECO:0000269|PubMed:31114929"
FT MUTAGEN 65
FT /note="M->A: In C; impairs interaction with eIF4EHP but has
FT no effect on translational repression or induction of mRNA
FT decay; when associated with A-58 and A-60."
FT /evidence="ECO:0000269|PubMed:31114929"
FT MUTAGEN 331..374
FT /note="Missing: Abolishes interaction with me31B and
FT impairs translational repression and induction of mRNA
FT decay."
FT /evidence="ECO:0000269|PubMed:31114929"
FT MUTAGEN 349
FT /note="W->A: Abolishes interaction with me31B."
FT /evidence="ECO:0000269|PubMed:31439631"
FT MUTAGEN 361
FT /note="F->A: In FF; abolishes interaction with me31B; when
FT associated with A-367."
FT /evidence="ECO:0000269|PubMed:31439631"
FT MUTAGEN 367
FT /note="F->A: In FF; abolishes interaction with me31B; when
FT associated with A-361."
FT /evidence="ECO:0000269|PubMed:31439631"
FT MUTAGEN 571
FT /note="Y->A: In GYF; impairs interaction with Patr-1 but
FT has no effect on translational repression or induction of
FT mRNA decay, and does not affect interaction with me31B or
FT Not1; when associated with A-582, A-590 and A-596."
FT /evidence="ECO:0000269|PubMed:31114929"
FT MUTAGEN 582
FT /note="F->A: In GYF; impairs interaction with Patr-1 but
FT has no effect on translational repression or induction of
FT mRNA decay, and does not affect interaction with me31B or
FT Not1; when associated with A-571, A-590 and A-596."
FT /evidence="ECO:0000269|PubMed:31114929"
FT MUTAGEN 590
FT /note="W->A: In GYF; impairs interaction with Patr-1 but
FT has no effect on translational repression or induction of
FT mRNA decay, and does not affect interaction with me31B or
FT Not1; when associated with A-571, A-582,and A-596."
FT /evidence="ECO:0000269|PubMed:31114929"
FT MUTAGEN 596
FT /note="F->A: In GYF; impairs interaction with Patr-1 but
FT has no effect on translational repression or induction of
FT mRNA decay, and does not affect interaction with me31B or
FT Not1; when associated with A-571, A-582 and A-590."
FT /evidence="ECO:0000269|PubMed:31114929"
FT CONFLICT 391
FT /note="Y -> K (in Ref. 4; ADV15453)"
FT /evidence="ECO:0000305"
FT CONFLICT 1331
FT /note="S -> T (in Ref. 4; ACL68761)"
FT /evidence="ECO:0000305"
FT CONFLICT 1536..1543
FT /note="QKKIKKNK -> KKRLKRIR (in Ref. 4; ACL68761)"
FT /evidence="ECO:0000305"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:6S8R"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:6S8R"
SQ SEQUENCE 1574 AA; 173730 MW; DE378F20E6DA4474 CRC64;
MTDSMKFGPE WLRNMSAEPS GSPSTYNVGN AAQNNSIGGH NLGNNTAASA SRNLFPEYRY
GREEMLSLFD RNCLLPQILP SFKKLFVEKV QCPLALTPSS EEDINQNSLG NNSRPAWLQR
SPSGFGSASR GSGRGGTVDR GRMRGKSAYH PIYQRPSGLY DESLSVISKA ERTWSDRNGT
GDSAATTTST SGSGALDWNG TPSSSPRKDY SNNHRNLENW RRTRNEDGSG DGPSSSGSMS
GPDIAGWRSG VVGGSTNAGF GTNSHRWGRS TSWRDEDPSV DNAASLQRSI STVATLSTDR
TGNNKGSGIG AAEGVGSISH PRLSSSKISQ LWTVNNAAGV DADENLPEWA IENPSKLGGS
FDASGAFHGD TDLKPIKSSH NTLKTKSLDS YDDVKRPKSK DLSDPDSGND ITPETSLTKD
TNTTAVQEEV ESSLSPISST TTKEVIHGDI SDRIKEVADE VEKLIMDDDH KISSNQSQHQ
NHDGFTAALP RMADIEINVK PSVTAVHRQA PSTMPIQITP TITDVAPPSH AVVSFSDHET
MQHHNMHHLP QFPMIPTPHI ITPNLNELWF YRDPQANVQG PFSAVEMTEW YRAGYFNENL
FVRRYSDNRF RPLGELIKFC HGNMPFTHSH LLPSPIELEN IPVGQIPAPL TASLSITPHK
PSPIPIALSV VEQQLQQQRD EQLKANVTAT AEALRAAIKG SFGGNSIGNT SHLLTMRFQM
LQDQYIQHQE YQILAELSKN ECFQRLSAVE QETVVRRKVQ LLGLPEYLIS LNGLSNSLSV
LNPVAGRQLY RAVVEHAKKD QQHIFANTEQ QRSVGNLLDA NNFILNAQIM IQQSQQEVGP
LVSSVDCIMQ GGTAADLNKP NEIPRNELDL INEYNLRMLL RGQPTSTQQQ PPALTNSATE
NLPGVDFLTE TQLLERQNLM IPIWLPPNNN KQQETDQQWA EMSNADASLW ETANLNEERN
EDQQLLIQKS SEACFADTEK DVKIAQLFQV QSGNVVNHTA LEELDQSPQN LKGSHNQKIV
KSLVSDIQQN HNEELNSHQH QVKQANKQNL NTKQNAAQSA LKPINNENDR KREQTEEKKR
QREERKRQQL EDDKRRALNE SEEQTRQIQE EKERQQQIQA QRRKALLGNV HSLSVQNGMS
GTLASAQSKK NDDAKTAEPQ VSSRLPSTSV APWSFQLQNS MRSAPGLAEI QKAERRERRA
DQQRHQELLD KQLRANAAAA AEANDALLKW QSTPASAPVM SLAEIQAEEA RRLANDLVDR
QRRRELEHHQ QAPLSSAVLV TSATSNIWGN ANKAWSSSAA QSLSLKTSSG TGLWDEPNPL
GSNGSGTSGT SSVTAAAVLA GGLNSANKST LQAQNKSSAL FASPRNLRKS QTLPALSNPE
KSNKNGPGQR PEKQKLAQTR SKGAAVSIEE KDRERKLNAK SQQSSTDQAI SKVNEYENEF
TSWCIKSLDN MSAKVDVPTF VAFLQDLEAP YEVKDYVRIY LGDGKDSLDF AKQFLERRSK
YKSLQRAQKA HNDDMCKPAP AITPSANDYA DSKNKQKKIK KNKMTKMDAR ILGFSVTAAE
GRINVGIRDY VEGP
