SUHW_DROME
ID SUHW_DROME Reviewed; 941 AA.
AC P08970; Q0KI74; Q9VFK9;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Protein suppressor of hairy wing;
GN Name=su(Hw); ORFNames=CG8573;
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 [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=2462523; DOI=10.1101/gad.2.10.1205;
RA Parkhurst S.M., Harrison D.A., Remington M.P., Spana C., Kelley R.L.,
RA Coyne R.S., Corces V.G.;
RT "The Drosophila su(Hw) gene, which controls the phenotypic effect of the
RT gypsy transposable element, encodes a putative DNA-binding protein.";
RL Genes Dev. 2:1205-1215(1988).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8382607; DOI=10.1002/j.1460-2075.1993.tb05675.x;
RA Roseman R.R., Pirrotta V., Gelyer P.K.;
RT "The su(Hw) protein insulates expression of the Drosophila melanogaster
RT white gene from chromosomal position-effects.";
RL EMBO J. 12:435-442(1993).
RN [6]
RP FUNCTION.
RX PubMed=7916729; DOI=10.1101/gad.7.10.1966;
RA Harrison D.A., Gdula D.A., Coyne R.S., Corces V.G.;
RT "A leucine zipper domain of the suppressor of Hairy-wing protein mediates
RT its repressive effect on enhancer function.";
RL Genes Dev. 7:1966-1978(1993).
RN [7]
RP FUNCTION, AND INTERACTION WITH MOD(MDG4).
RX PubMed=7664338; DOI=10.1016/0092-8674(95)90031-4;
RA Gerasimova T.I., Gdula D.A., Gerasimov D.V., Simonova O., Corces V.G.;
RT "A Drosophila protein that imparts directionality on a chromatin insulator
RT is an enhancer of position-effect variegation.";
RL Cell 82:587-597(1995).
RN [8]
RP FUNCTION.
RX PubMed=7761470; DOI=10.1073/pnas.92.11.5184;
RA Georgiev P.G., Corces V.G.;
RT "The su(Hw) protein bound to gypsy sequences in one chromosome can repress
RT enhancer-promoter interactions in the paired gene located in the other
RT homolog.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5184-5188(1995).
RN [9]
RP FUNCTION.
RX PubMed=8852842; DOI=10.1093/genetics/142.2.425;
RA Georgiev P.G., Kozycina M.;
RT "Interaction between mutations in the suppressor of Hairy wing and modifier
RT of mdg4 genes of Drosophila melanogaster affecting the phenotype of gypsy-
RT induced mutations.";
RL Genetics 142:425-436(1996).
RN [10]
RP FUNCTION.
RX PubMed=9017397; DOI=10.1093/genetics/145.1.153;
RA Gdula D.A., Corces V.G.;
RT "Characterization of functional domains of the su(Hw) protein that mediate
RT the silencing effect of mod(mdg4) mutations.";
RL Genetics 145:153-161(1997).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=9491892; DOI=10.1016/s0092-8674(00)80944-7;
RA Gerasimova T.I., Corces V.G.;
RT "Polycomb and trithorax group proteins mediate the function of a chromatin
RT insulator.";
RL Cell 92:511-521(1998).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=11106742; DOI=10.1016/s1097-2765(00)00101-5;
RA Gerasimova T.I., Byrd K., Corces V.G.;
RT "A chromatin insulator determines the nuclear localization of DNA.";
RL Mol. Cell 6:1025-1035(2000).
RN [13]
RP INTERACTION WITH MOD(MDG4), AND SUBCELLULAR LOCATION.
RX PubMed=11350941; DOI=10.1093/emboj/20.10.2518;
RA Ghosh D., Gerasimova T.I., Corces V.G.;
RT "Interactions between the Su(Hw) and Mod(mdg4) proteins required for gypsy
RT insulator function.";
RL EMBO J. 20:2518-2527(2001).
RN [14]
RP FUNCTION.
RX PubMed=11779804; DOI=10.1093/genetics/159.4.1649;
RA Chen S., Corces V.G.;
RT "The gypsy insulator of Drosophila affects chromatin structure in a
RT directional manner.";
RL Genetics 159:1649-1658(2001).
RN [15]
RP INTERACTION WITH MOD(MDG4).
RX PubMed=11416154; DOI=10.1128/mcb.21.14.4807-4817.2001;
RA Gause M., Morcillo P., Dorsett D.;
RT "Insulation of enhancer-promoter communication by a gypsy transposon insert
RT in the Drosophila cut gene: cooperation between suppressor of hairy-wing
RT and modifier of mdg4 proteins.";
RL Mol. Cell. Biol. 21:4807-4817(2001).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=14996934; DOI=10.1242/jcs.00964;
RA Xu Q., Li M., Adams J., Cai H.N.;
RT "Nuclear location of a chromatin insulator in Drosophila melanogaster.";
RL J. Cell Sci. 117:1025-1032(2004).
RN [17]
RP INTERACTION WITH CP190 AND MOD(MDG4), AND SUBCELLULAR LOCATION.
RX PubMed=15574329; DOI=10.1016/j.molcel.2004.11.004;
RA Pai C.-Y., Lei E.P., Ghosh D., Corces V.G.;
RT "The centrosomal protein CP190 is a component of the gypsy chromatin
RT insulator.";
RL Mol. Cell 16:737-748(2004).
RN [18]
RP INTERACTION WITH TOPORS, AND SUBCELLULAR LOCATION.
RX PubMed=16209949; DOI=10.1016/j.molcel.2005.08.031;
RA Capelson M., Corces V.G.;
RT "The ubiquitin ligase dTopors directs the nuclear organization of a
RT chromatin insulator.";
RL Mol. Cell 20:105-116(2005).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186, AND IDENTIFICATION BY
RP 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 [20]
RP INTERACTION WITH NUP98.
RX PubMed=28366641; DOI=10.1016/j.molcel.2017.02.020;
RA Pascual-Garcia P., Debo B., Aleman J.R., Talamas J.A., Lan Y., Nguyen N.H.,
RA Won K.J., Capelson M.;
RT "Metazoan nuclear pores provide a scaffold for poised genes and mediate
RT induced enhancer-promoter contacts.";
RL Mol. Cell 66:63-76(2017).
CC -!- FUNCTION: Component of the gypsy chromatin insulator complex which is
CC required for the function of the gypsy chromatin insulator and other
CC endogenous chromatin insulators. Chromatin insulators are regulatory
CC elements which establish independent domains of transcriptional
CC activity within eukaryotic genomes. Insulators have two defining
CC properties; they can block the communication between an enhancer and a
CC promoter when placed between them and can also buffer transgenes from
CC position effect variegation (PEV). Insulators are proposed to structure
CC the chromatin fiber into independent domains of differing
CC transcriptional potential by promoting the formation of distinct
CC chromatin loops. This chromatin looping may involve the formation of
CC insulator bodies, where homotypic interactions between individual
CC subunits of the insulator complex could promote the clustering of
CC widely spaced insulators at the nuclear periphery. Within the gypsy
CC insulator complex, this protein binds specifically to a region of the
CC gypsy element located 3' of the 5' long terminal repeat (LTR), and may
CC also mediate interaction with other endogenous insulators at sites
CC distinct from those recognized by Cp190. {ECO:0000269|PubMed:11779804,
CC ECO:0000269|PubMed:2462523, ECO:0000269|PubMed:7664338,
CC ECO:0000269|PubMed:7761470, ECO:0000269|PubMed:7916729,
CC ECO:0000269|PubMed:8382607, ECO:0000269|PubMed:8852842,
CC ECO:0000269|PubMed:9017397}.
CC -!- SUBUNIT: Component of the gypsy chromatin insulator complex, composed
CC of Cp190, mod(mdg4) and su(Hw) (PubMed:7664338, PubMed:11350941,
CC PubMed:11416154, PubMed:15574329). The gypsy chromatin insulator
CC complex interacts with Topors via mod(mdg4) and su(Hw)
CC (PubMed:16209949). Upon ecdysone stimulation, interacts with Nup98
CC (PubMed:28366641). {ECO:0000269|PubMed:11350941,
CC ECO:0000269|PubMed:11416154, ECO:0000269|PubMed:15574329,
CC ECO:0000269|PubMed:16209949, ECO:0000269|PubMed:28366641,
CC ECO:0000269|PubMed:7664338}.
CC -!- INTERACTION:
CC P08970; Q24478: Cp190; NbExp=4; IntAct=EBI-101373, EBI-868840;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Colocalizes with other
CC elements of the gypsy chromatin insulator complex at multiple sites on
CC polytene chromosomes and at nuclear insulator bodies.
CC -!- DEVELOPMENTAL STAGE: Expressed in all stages of development.
CC {ECO:0000269|PubMed:2462523}.
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DR EMBL; Y00228; CAA68371.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55044.1; -; Genomic_DNA.
DR EMBL; BT003273; AAO25030.1; -; mRNA.
DR PIR; S01909; S01909.
DR RefSeq; NP_001247098.1; NM_001260169.2.
DR RefSeq; NP_524349.1; NM_079625.3.
DR RefSeq; NP_731897.1; NM_169574.2.
DR AlphaFoldDB; P08970; -.
DR SMR; P08970; -.
DR BioGRID; 66816; 55.
DR DIP; DIP-17895N; -.
DR IntAct; P08970; 21.
DR MINT; P08970; -.
DR STRING; 7227.FBpp0082404; -.
DR iPTMnet; P08970; -.
DR PaxDb; P08970; -.
DR PRIDE; P08970; -.
DR DNASU; 41740; -.
DR EnsemblMetazoa; FBtr0082945; FBpp0082404; FBgn0003567.
DR EnsemblMetazoa; FBtr0082946; FBpp0082405; FBgn0003567.
DR EnsemblMetazoa; FBtr0310002; FBpp0301708; FBgn0003567.
DR GeneID; 41740; -.
DR KEGG; dme:Dmel_CG8573; -.
DR CTD; 41740; -.
DR FlyBase; FBgn0003567; su(Hw).
DR VEuPathDB; VectorBase:FBgn0003567; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000166978; -.
DR HOGENOM; CLU_013489_0_0_1; -.
DR InParanoid; P08970; -.
DR OMA; HLGHINC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P08970; -.
DR SignaLink; P08970; -.
DR BioGRID-ORCS; 41740; 0 hits in 1 CRISPR screen.
DR ChiTaRS; su(Hw); fly.
DR GenomeRNAi; 41740; -.
DR PRO; PR:P08970; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003567; Expressed in cleaving embryo and 77 other tissues.
DR ExpressionAtlas; P08970; baseline and differential.
DR Genevisible; P08970; DM.
DR GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0043035; F:chromatin insulator sequence binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:1990188; F:euchromatin binding; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0033696; P:heterochromatin boundary formation; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:1905632; P:protein localization to euchromatin; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035075; P:response to ecdysone; IDA:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..941
FT /note="Protein suppressor of hairy wing"
FT /id="PRO_0000047053"
FT ZN_FING 220..242
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 290..313
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 319..341
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 348..366
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 380..402
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 413..435
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 441..463
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 469..491
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 497..519
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 523..545
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 553..577
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 596..619
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..860
FT /note="Interaction with mod(mdg4)"
FT REGION 864..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..201
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 186
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 31
FT /note="R -> K (in Ref. 1; CAA68371)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="E -> G (in Ref. 1; CAA68371)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="G -> D (in Ref. 1; CAA68371)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="G -> E (in Ref. 1; CAA68371)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="H -> R (in Ref. 1; CAA68371)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="P -> S (in Ref. 1; CAA68371)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="Q -> R (in Ref. 1; CAA68371)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="G -> D (in Ref. 1; CAA68371)"
FT /evidence="ECO:0000305"
FT CONFLICT 874
FT /note="N -> NEDN (in Ref. 1; CAA68371)"
FT /evidence="ECO:0000305"
FT CONFLICT 892
FT /note="T -> K (in Ref. 1; CAA68371)"
FT /evidence="ECO:0000305"
FT CONFLICT 896
FT /note="R -> K (in Ref. 1; CAA68371)"
FT /evidence="ECO:0000305"
FT CONFLICT 923
FT /note="S -> T (in Ref. 1; CAA68371)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 941 AA; 105780 MW; 60C6243AD088F961 CRC64;
MSASKEGKEK KGKLLGVENI SPPKDKRPAT RMKLLNDVGA GEDSEASTTT TTSRTPSNKQ
EKRGSVAGSR IKILNEEILG TPKTEKRGAT KSTAPAASTV KILNEKKTPS ATVTAVETTK
IKTSPSKRKK MEHYVLQAVK SENTKADTTV TVVTEEDDTI DFILADDEEV VPGRIENNNG
QEIVVTEDDE DLGEDGDEDG EDSSGKGNSS QTKIKEIVEH VCGKCYKTFR RVQSLKKHLE
FCRYDSGYHL RKADMLKNLE KIEKDAVVME KKDICFCCSE SYDTFHLGHI NCPDCPKSFK
TQTSYERHIF ITHSEFSDFP CSICNANLRS EALLALHEEQ HKSRGKPYAC KICGKDFTRS
YHLKRHQKYS SCSSNETDTM SCKVCDRVFY RLDNLRSHLK QHLGTQVVKK PEYMCHTCKN
CFYSLSTLNI HIRTHTGEKP FDCDLCDKKF SALVALKKHR RYHTGEKPYS CTVCNQAFAV
KEVLNRHMKR HTGERPHKCD ECGKSFIQAT QLRTHSKTHI RPFPCEQCDE KFKTEKQLER
HVKTHSRTKR PVFSCAECKR NFRTPALLKE HMDEGKHSPK QQRSSMRSAV KIMERTDCAI
CDKNFDSSDT LRRHIRTVHE CDPDDIFGVE PHPSKRAKKD IESEEVVPVA LNTSAGSLIS
SQTDGNGVVV REFLVDEGDG AAQTITLENE TYTILPLDGA IEGEQLTDEA GVKPEAKKEE
AQVSPVVKKE QRKSLAASLA AAIADNLEES CSEDDFSGEI LTEEDIKLKE NVGKLIDMLV
DPPILKKYGW PNAPEETVLC KVIENCGHDL TKGGENYAEL DYGSRMREYC KLLFTVVIHN
DSIKSLLNNF PIDDVIEYVL GDEDQDEGGL DKDNESHSGD EEAVSVTGET KTNEIREKPE
KKEVSAKSEK KEIVGKAVDK DNSEEVVREN KKKPVGEQEK A
