MYSN_DROME
ID MYSN_DROME Reviewed; 2057 AA.
AC Q99323; Q24138; Q7JPC1; Q7JPC2; Q8MMC2; Q94987; Q94992; Q9W0W8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Myosin heavy chain, non-muscle;
DE AltName: Full=Myosin II;
DE AltName: Full=Non-muscle MHC;
DE AltName: Full=Zipper protein;
GN Name=zip; ORFNames=CG15792;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo;
RX PubMed=2117279; DOI=10.1073/pnas.87.16.6316;
RA Ketchum A.S., Stewart C.T., Stewart M., Kiehart D.P.;
RT "Complete sequence of the Drosophila nonmuscle myosin heavy-chain
RT transcript: conserved sequences in the myosin tail and differential
RT splicing in the 5' untranslated sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6316-6320(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3 AND 4), AND
RP DEVELOPMENTAL STAGE.
RX PubMed=8568878; DOI=10.1006/jmbi.1996.0009;
RA Mansfield S.G., Al-Shirawi D.Y., Ketchum A.S., Newbern E.C., Kiehart D.P.;
RT "Molecular organization and alternative splicing in zipper, the gene that
RT encodes the Drosophila non-muscle myosin II heavy chain.";
RL J. Mol. Biol. 255:98-109(1996).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2021 AND SER-2022, 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 [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=18816840; DOI=10.1002/dvdy.21722;
RA Zahedi B., Shen W., Xu X., Chen X., Mahey M., Harden N.;
RT "Leading edge-secreted Dpp cooperates with ACK-dependent signaling from the
RT amnioserosa to regulate myosin levels during dorsal closure.";
RL Dev. Dyn. 237:2936-2946(2008).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=23579691; DOI=10.1371/journal.pone.0060180;
RA Shen W., Chen X., Cormier O., Cheng D.C., Reed B., Harden N.;
RT "Modulation of morphogenesis by Egfr during dorsal closure in Drosophila.";
RL PLoS ONE 8:E60180-E60180(2013).
RN [8]
RP FUNCTION, AND INTERACTION WITH SAU.
RX PubMed=24786584; DOI=10.1371/journal.pgen.1004305;
RA Sechi S., Colotti G., Belloni G., Mattei V., Frappaolo A., Raffa G.D.,
RA Fuller M.T., Giansanti M.G.;
RT "GOLPH3 is essential for contractile ring formation and Rab11 localization
RT to the cleavage site during cytokinesis in Drosophila melanogaster.";
RL PLoS Genet. 10:E1004305-E1004305(2014).
RN [9]
RP FUNCTION, INTERACTION WITH CK AND UBR3, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, UBIQUITINATION, AND MUTAGENESIS OF ASP-1932.
RX PubMed=27331610; DOI=10.7554/elife.15258;
RA Li T., Giagtzoglou N., Eberl D.F., Jaiswal S.N., Cai T., Godt D.,
RA Groves A.K., Bellen H.J.;
RT "The E3 ligase Ubr3 regulates Usher syndrome and MYH9 disorder proteins in
RT the auditory organs of Drosophila and mammals.";
RL Elife 5:E15258-E15258(2016).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=33835025; DOI=10.7554/elife.63535;
RA Sharma S., Rikhy R.;
RT "Spatiotemporal recruitment of RhoGTPase protein GRAF inhibits actomyosin
RT ring constriction in Drosophila cellularization.";
RL Elife 10:0-0(2021).
CC -!- FUNCTION: Nonmuscle myosin appears to be responsible for
CC cellularization. Required for morphogenesis and cytokinesis
CC (PubMed:24786584). Necessary for auditory transduction: plays a role in
CC Johnston's organ organization by acting in scolopidial apical
CC attachment (PubMed:27331610). Interaction with the myosin ck may be
CC important for this function (PubMed:27331610).
CC {ECO:0000269|PubMed:24786584, ECO:0000269|PubMed:27331610}.
CC -!- SUBUNIT: Interacts with sau (PubMed:24786584). Interacts with ck and
CC Ubr3 (PubMed:27331610). {ECO:0000269|PubMed:24786584,
CC ECO:0000269|PubMed:27331610}.
CC -!- INTERACTION:
CC Q99323; Q99323: zip; NbExp=2; IntAct=EBI-118064, EBI-118064;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:27331610}. Cytoplasm {ECO:0000269|PubMed:33835025}.
CC Note=Expression in neurons and scolopale cells is increased at the
CC apical tips of cilia (PubMed:27331610). During embryo cellularization,
CC located in foci at the edges of the furrow canal tips
CC (PubMed:33835025). {ECO:0000269|PubMed:27331610,
CC ECO:0000269|PubMed:33835025}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=3; Synonyms=a;
CC IsoId=Q99323-3; Sequence=Displayed;
CC Name=1; Synonyms=Long;
CC IsoId=Q99323-1; Sequence=VSP_011159;
CC Name=2; Synonyms=Short;
CC IsoId=Q99323-2; Sequence=VSP_003342, VSP_011159;
CC Name=4; Synonyms=b;
CC IsoId=Q99323-4; Sequence=VSP_003342;
CC -!- TISSUE SPECIFICITY: In Johnston's organ, expressed in neurons and
CC scolopale cells. {ECO:0000269|PubMed:27331610}.
CC -!- DEVELOPMENTAL STAGE: At germband retraction (stage 12), expression is
CC high in the embryo amnioserosa and relatively low at the apical edge of
CC the leading edge/ dorsalmost epidermal (DME) cells (PubMed:18816840,
CC PubMed:23579691). Whereas at dorsal closure (stage 13), expression is
CC relatively low in the amnioserosa and high in the DME cells
CC (PubMed:18816840, PubMed:23579691). Isoforms containing exon 7 are
CC detected in all stages of development and are expressed in embryos,
CC early and late larvae, and adults (PubMed:8568878).
CC {ECO:0000269|PubMed:18816840, ECO:0000269|PubMed:23579691,
CC ECO:0000269|PubMed:8568878}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:27331610}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; M35012; AAA28713.1; -; mRNA.
DR EMBL; U35816; AAB09048.1; -; Genomic_DNA.
DR EMBL; U35816; AAB09049.1; -; Genomic_DNA.
DR EMBL; U35816; AAB09050.1; -; Genomic_DNA.
DR EMBL; U35816; AAB09051.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF47311.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM70805.1; -; Genomic_DNA.
DR PIR; A36014; A36014.
DR PIR; S61477; S61477.
DR RefSeq; NP_523860.2; NM_079136.4.
DR RefSeq; NP_726506.1; NM_166704.4.
DR AlphaFoldDB; Q99323; -.
DR SMR; Q99323; -.
DR BioGRID; 63569; 88.
DR IntAct; Q99323; 13.
DR STRING; 7227.FBpp0072306; -.
DR BindingDB; Q99323; -.
DR ChEMBL; CHEMBL4295929; -.
DR iPTMnet; Q99323; -.
DR PaxDb; Q99323; -.
DR PeptideAtlas; Q99323; -.
DR PRIDE; Q99323; -.
DR GeneID; 38001; -.
DR KEGG; dme:Dmel_CG15792; -.
DR CTD; 38001; -.
DR FlyBase; FBgn0287873; zip.
DR VEuPathDB; VectorBase:FBgn0265434; -.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; Q99323; -.
DR PhylomeDB; Q99323; -.
DR Reactome; R-DME-350480; Activation of non-muscle Myosin II.
DR Reactome; R-DME-5627123; RHO GTPases activate PAKs.
DR SignaLink; Q99323; -.
DR BioGRID-ORCS; 38001; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38001; -.
DR PRO; PR:Q99323; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR ExpressionAtlas; Q99323; baseline and differential.
DR Genevisible; Q99323; DM.
DR GO; GO:0005826; C:actomyosin contractile ring; IDA:FlyBase.
DR GO; GO:0106037; C:apicomedial cortex; IDA:FlyBase.
DR GO; GO:0045180; C:basal cortex; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0044291; C:cell-cell contact zone; IDA:FlyBase.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0032154; C:cleavage furrow; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0016460; C:myosin II complex; IDA:FlyBase.
DR GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000146; F:microfilament motor activity; ISS:FlyBase.
DR GO; GO:0032027; F:myosin light chain binding; IPI:FlyBase.
DR GO; GO:0007496; P:anterior midgut development; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:FlyBase.
DR GO; GO:0060289; P:compartment boundary maintenance; IMP:FlyBase.
DR GO; GO:0035017; P:cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0046664; P:dorsal closure, amnioserosa morphology change; IMP:FlyBase.
DR GO; GO:0046663; P:dorsal closure, leading edge cell differentiation; IMP:FlyBase.
DR GO; GO:0007395; P:dorsal closure, spreading of leading edge cells; IMP:FlyBase.
DR GO; GO:0007455; P:eye-antennal disc morphogenesis; IMP:FlyBase.
DR GO; GO:0008258; P:head involution; IMP:FlyBase.
DR GO; GO:0035317; P:imaginal disc-derived wing hair organization; IGI:FlyBase.
DR GO; GO:0070986; P:left/right axis specification; IMP:FlyBase.
DR GO; GO:0032507; P:maintenance of protein location in cell; IMP:FlyBase.
DR GO; GO:0007443; P:Malpighian tubule morphogenesis; IMP:FlyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
DR GO; GO:0060571; P:morphogenesis of an epithelial fold; IMP:FlyBase.
DR GO; GO:0006936; P:muscle contraction; IMP:FlyBase.
DR GO; GO:0030239; P:myofibril assembly; IMP:FlyBase.
DR GO; GO:0031036; P:myosin II filament assembly; IDA:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:FlyBase.
DR GO; GO:0090175; P:regulation of establishment of planar polarity; IMP:FlyBase.
DR GO; GO:1901739; P:regulation of myoblast fusion; IGI:FlyBase.
DR GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IDA:FlyBase.
DR GO; GO:0042060; P:wound healing; IMP:FlyBase.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Cell projection; Coiled coil; Cytoplasm; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..2057
FT /note="Myosin heavy chain, non-muscle"
FT /id="PRO_0000123388"
FT DOMAIN 78..128
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 132..867
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 870..899
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 250..260
FT /note="25 kDa/50 kDa junction"
FT REGION 722..734
FT /note="50 kDa/20 kDa junction"
FT REGION 745..767
FT /note="Actin-binding"
FT REGION 782..798
FT /note="Reactive sulfhydryl/actin-binding"
FT REGION 1124..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..2057
FT /note="Light meromyosin (LMM)"
FT REGION 1343..2010
FT /note="Alpha-helical tailpiece (LMM)"
FT REGION 1782..1802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2008..2057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2011..2057
FT /note="Globular tailpiece"
FT COILED 926..2016
FT /evidence="ECO:0000255"
FT COMPBIAS 1782..1801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2016..2030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225..232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2021
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2022
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..45
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:2117279"
FT /id="VSP_003342"
FT VAR_SEQ 264..303
FT /note="Missing (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:2117279"
FT /id="VSP_011159"
FT MUTAGEN 1256
FT /note="R->C: Large percentage of detached scolopidia in
FT Johnston's organs but no effect on interaction with ck."
FT /evidence="ECO:0000269|PubMed:27331610"
FT MUTAGEN 1515
FT /note="D->N: Small percentage of detached scolopidia in
FT Johnston's organs but no effect on interaction with ck."
FT /evidence="ECO:0000269|PubMed:27331610"
FT MUTAGEN 1932
FT /note="D->K: Increased interaction with ck and large
FT percentage of detached scolopidia in Johnston's organs."
FT /evidence="ECO:0000269|PubMed:27331610"
FT MUTAGEN 2024
FT /note="R->X: Small percentage of detached scolopidia in
FT Johnston's organs but no effect on interaction with ck."
FT /evidence="ECO:0000269|PubMed:27331610"
FT CONFLICT 69..81
FT /note="PIRPRRPSGHRSV -> DPATQAEWTQKR (in Ref. 3; AAF47311/
FT AAM70805)"
FT /evidence="ECO:0000305"
FT CONFLICT 1121
FT /note="T -> S (in Ref. 3; AAF47311/AAM70805)"
FT /evidence="ECO:0000305"
FT CONFLICT 1763..1764
FT /note="DG -> ER (in Ref. 3; AAF47311/AAM70805)"
FT /evidence="ECO:0000305"
FT CONFLICT 1843..1846
FT /note="SRKA -> AAAR (in Ref. 1; AAA28713)"
FT /evidence="ECO:0000305"
FT CONFLICT 1909..1910
FT /note="NL -> KV (in Ref. 1; AAA28713)"
FT /evidence="ECO:0000305"
FT CONFLICT 2040
FT /note="S -> G (in Ref. 3; AAF47311/AAM70805)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2057 AA; 236644 MW; 0D59519C1E83A411 CRC64;
MKSAWLALKS KSALHPKSEY PVSNIHYPKA ANYRQTRNYL EIAAKMSEEV DRNDPELKYL
SVERNQFNPI RPRRPSGHRS VLVWVPHENQ GFVAASIKRE HGDEVEVELA ETGKRVMILR
DDIQKMNPPK FDKVEDMAEL TCLNEASVLH NIKDRYYSGL IYTYSGLFCV VVNPYKKLPI
YTEKIMERYK GIKRHEVPPH VFAITDSAYR NMLGDREDQS ILCTGESGAG KTENTKKVIQ
FLAYVAASKP KGSGAVPHPA VLINFSVNTN KYIKVKIMAQ NQNQTIEVVN GLKMVEVNSN
CQEGELEQQL LQANPILEAF GNAKTVKNDN SSRFGKFIRI NFDASGFISG ANIETYLLEK
SRAIRQAKDE RTFHIFYQLL AGATPEQREK FILDDVKSYA FLSNGSLPVP GVDDYAEFQA
TVKSMNIMGM TSEDFNSIFR IVSAVLLFGS MKFRQERNND QATLPDNTVA QKIAHLLGLS
VTDMTRAFLT PRIKVGRDFV TKAQTKEQVE FAVEAIAKAC YERMFKWLVN RINRSLDRTK
RQGASFIGIL DMAGFEIFEL NSFEQLCINY TNEKLQQLFN HTMFILEQEE YQREGIEWKF
IDFGLDLQPT IDLIDKPGGI MALLDEECWF PKATDKTFVD KLVSAHSMHP KFMKTDFRGV
ADFAIVHYAG RVDYSAAKWL MKNMDPLNEN IVSLLQGSQD PFVVNIWKDA EIVGMAQQAL
TDTQFGARTR KGMFRTVSHL YKEQLAKLMD TLRNTNPNFV RCIIPNHEKR AGKIDAPLVL
DQLRCNGVLE GIRICRQGFP NRIPFQEFRQ RYELLTPNVI PKGFMDGKKA CEKMIQALEL
DSNLYRVGQS KIFFRAGVLA HLEEERDFKI SDLIVNFQAF CRGFLARRNY QKRLQQLNAI
RIIQRNCAAY LKLRNWQWWR LYTKVKPLLE VTKQEEKLVQ KEDELKQVRE KLDTLAKNTQ
EYERKYQQAL VEKTTLAEQL QAEIELCAEA EESRSRLMAR KQELEDMMQE LETRIEEEEE
RVLALGGEKK KLELNIQDLE EQLEEEEAAR QKLQLEKVQL DAKIKKYEED LALTDDQNQK
LLKEKKLLEE RANDLSQTLA EEEEKAKHLA KLKAKHEATI TELEERLHKD QQQRQESDRS
KRKIETEVAD LKEQLNERRV QVDEMQAQLA KREEELTQTL LRIDEESATK ATAQKAQREL
ESQLAEIQED LEAEKAARAK AEKVRRDLSE ELEALKNELL DSLDTTAAQQ ELRSKREQEL
ATLKKSLEEE TVNHEGVLAD MRHKHSQELN SINDQLENLR KAKTVLEKAK GTLEAENADL
ATELRSVNSS RQENDRRRKQ AESQIAELQV KLAEIERARS ELQEKCTKLQ QEAENITNQL
EEAELKASAA VKSASNMESQ LTEAQQLLEE ETRQKLGLSS KLRQIESEKE ALQEQLEEDD
EAKRNYERKL AEVTTQMQEI KKKAEEDADL AKELEEGKKR LNKDIEALER QVKELIAQND
RLDKSKKKIQ SELEDATIEL EAQRTKVLEL EKKQKNFDKI LAEEKAISEQ IAQERDTAER
EAREKETKVL SVSRELDEAF DKIEDLENKR KTLQNELDDL ANTQGTADKN VHELEKAKRA
LESQLAELKA QNEELEDDLQ LTEDAKLRLE VNMQALRSQF ERDLLAKEEG AEEKRRGLVK
QLRDLETELD EERKQRTAAV ASKKKLEGDL KEIETTMEMH NKVKEDALKH AKKLQAQVKD
ALRDAEEAKA AKEELQALSK EADGKVKALE AEVLQLTEDL ASSERARRAA ETERDELAEE
IANNANKGSL MIDEKRRLEA RIATLEEELE EEQSNSEVLL DRSRKAQLQI EQLTTELANE
KSNSQKNENG RALLERQNKE LKAKLAEIET AQRTKVKATI ATLEAKIANL EEQLENEGKE
RLLQQKANRK MDKKIKELTM NIEDERRHVD QHKEQMDKLN SRIKLLKRNL DETEEELQKE
KTQKRKYQRE CEDMIESQEA MNREINSLKT KLRRTGGIGL SSSRLTGTPS SKRAGGGGGS
DDSSVQDESL DGEDSAN
