DS_DROME
ID DS_DROME Reviewed; 3503 AA.
AC Q24292; Q9VPS4;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protein dachsous {ECO:0000303|PubMed:26073018, ECO:0000303|PubMed:7601355};
DE AltName: Full=Adherin;
DE Flags: Precursor;
GN Name=ds; ORFNames=CG17941;
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 {ECO:0000312|EMBL:AAF51468.3};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Embryo;
RX PubMed=7601355; DOI=10.1101/gad.9.12.1530;
RA Clark H.F., Brentrup D., Schneitz K., Bieber A., Goodman C., Noll M.;
RT "Dachsous encodes a member of the cadherin superfamily that controls
RT imaginal disc morphogenesis in Drosophila.";
RL Genes Dev. 9:1530-1542(1995).
RN [2] {ECO:0000305}
RP SEQUENCE REVISION.
RA Noll M.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
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.
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-3465 AND SER-3469, 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 PHOSPHORYLATION AT SER-236, AND MUTAGENESIS OF SER-236.
RX PubMed=18635802; DOI=10.1126/science.1158159;
RA Ishikawa H.O., Takeuchi H., Haltiwanger R.S., Irvine K.D.;
RT "Four-jointed is a Golgi kinase that phosphorylates a subset of cadherin
RT domains.";
RL Science 321:401-404(2008).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH MYO31DF.
RX PubMed=26073018; DOI=10.1016/j.devcel.2015.04.026;
RA Gonzalez-Morales N., Geminard C., Lebreton G., Cerezo D., Coutelis J.B.,
RA Noselli S.;
RT "The Atypical Cadherin Dachsous Controls Left-Right Asymmetry in
RT Drosophila.";
RL Dev. Cell 33:675-689(2015).
CC -!- FUNCTION: Required for normal morphogenesis of adult structures derived
CC from imaginal disks (PubMed:7601355, PubMed:26073018). Plays a role in
CC planar cell polarity and in determining body left-right asymmetry.
CC Expression in segment H1 of the imaginal ring and interaction with
CC Myo31DF are required to induce changes of cell shape and orientation in
CC segment H2, which then gives rise to normal, dextral looping of the
CC adult hindgut (PubMed:26073018). {ECO:0000269|PubMed:26073018,
CC ECO:0000269|PubMed:7601355}.
CC -!- SUBUNIT: Interacts (via cytoplasmic region) with Myo31DF.
CC {ECO:0000269|PubMed:26073018}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26073018};
CC Single-pass type I membrane protein {ECO:0000305}. Cell junction
CC {ECO:0000269|PubMed:26073018}. Note=Colocalizes with Myo32DF at cell
CC contact sites. {ECO:0000269|PubMed:26073018}.
CC -!- TISSUE SPECIFICITY: Expressed in embryonic ectoderm. In larvae,
CC expression is restricted to imaginal disks and brain.
CC {ECO:0000269|PubMed:7601355}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis where it is
CC first detected during gastrulation. Also expressed in larvae and
CC adults. {ECO:0000269|PubMed:7601355}.
CC -!- PTM: Phosphorylated by fj on Ser/Thr of cadherin domains.
CC {ECO:0000269|PubMed:18635802}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in subdomain H1 of the
CC imaginal ring causes loss of H2 cell orientation bias, resulting in
CC aberrant looping of the adult hindgut. {ECO:0000269|PubMed:26073018}.
CC -!- MISCELLANEOUS: Overexpression in segment H1 of the imaginal ring causes
CC aberrant gut looping in about 40% of the cases, but no phenotype is
CC observed when both Myo31DF and ds are overexpressed.
CC {ECO:0000269|PubMed:26073018}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF51468.3; Type=Erroneous initiation; Evidence={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; L08811; AAA79329.2; -; mRNA.
DR EMBL; AE014134; AAF51468.3; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_001285551.1; NM_001298622.1.
DR RefSeq; NP_523446.2; NM_078722.3.
DR SMR; Q24292; -.
DR BioGRID; 59500; 35.
DR DIP; DIP-49190N; -.
DR IntAct; Q24292; 5.
DR STRING; 7227.FBpp0077708; -.
DR GlyGen; Q24292; 32 sites.
DR iPTMnet; Q24292; -.
DR PaxDb; Q24292; -.
DR PRIDE; Q24292; -.
DR EnsemblMetazoa; FBtr0078045; FBpp0077708; FBgn0284247.
DR GeneID; 33245; -.
DR KEGG; dme:Dmel_CG17941; -.
DR UCSC; CG17941-RA; d. melanogaster.
DR CTD; 109661; -.
DR FlyBase; FBgn0284247; ds.
DR VEuPathDB; VectorBase:FBgn0284247; -.
DR eggNOG; KOG3594; Eukaryota.
DR HOGENOM; CLU_000265_0_0_1; -.
DR InParanoid; Q24292; -.
DR PhylomeDB; Q24292; -.
DR Reactome; R-DME-350379; Homo-/heterophilic binding of transmembrane components.
DR Reactome; R-DME-390023; Subcellular localisation of D.
DR Reactome; R-DME-390150; DS ligand bound to FT receptor.
DR SignaLink; Q24292; -.
DR GenomeRNAi; 33245; -.
DR PRO; PR:Q24292; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0284247; Expressed in wing disc and 20 other tissues.
DR ExpressionAtlas; Q24292; baseline and differential.
DR Genevisible; Q24292; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0042067; P:establishment of ommatidial planar polarity; IMP:UniProtKB.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0007560; P:imaginal disc morphogenesis; IMP:UniProtKB.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IGI:FlyBase.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:0090251; P:protein localization involved in establishment of planar polarity; IMP:FlyBase.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR027397; Catenin-bd_sf.
DR Pfam; PF00028; Cadherin; 23.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 27.
DR SUPFAM; SSF49313; SSF49313; 27.
DR PROSITE; PS00232; CADHERIN_1; 20.
DR PROSITE; PS50268; CADHERIN_2; 27.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Developmental protein; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..3503
FT /note="Protein dachsous"
FT /id="PRO_0000004009"
FT TOPO_DOM 21..3045
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 3046..3066
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3067..3503
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..121
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 122..233
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 234..340
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 345..451
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 452..558
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 559..662
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 663..774
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 775..878
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 879..983
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 984..1100
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1101..1203
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1205..1312
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1313..1432
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1433..1549
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1556..1666
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1667..1794
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1796..1899
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1900..2004
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2005..2111
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2114..2269
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2270..2375
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2375..2479
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2489..2595
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2596..2699
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2701..2809
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2810..2916
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2919..3028
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 2193..2225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3114..3195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3360..3404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3431..3503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3138..3159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3160..3176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3362..3385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3439..3466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18635802"
FT MOD_RES 3465
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 3469
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 991
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1006
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1029
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1700
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1884
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2845
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2967
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 236
FT /note="S->A: Decreased phosphorylation by fj."
FT /evidence="ECO:0000269|PubMed:18635802"
FT CONFLICT 1070
FT /note="V -> I (in Ref. 1; AAA79329)"
FT /evidence="ECO:0000305"
FT CONFLICT 1490
FT /note="R -> S (in Ref. 1; AAA79329)"
FT /evidence="ECO:0000305"
FT CONFLICT 1636
FT /note="G -> S (in Ref. 1; AAA79329)"
FT /evidence="ECO:0000305"
FT CONFLICT 1692
FT /note="S -> P (in Ref. 1; AAA79329)"
FT /evidence="ECO:0000305"
FT CONFLICT 1804
FT /note="V -> I (in Ref. 1; AAA79329)"
FT /evidence="ECO:0000305"
FT CONFLICT 2029
FT /note="L -> I (in Ref. 1; AAA79329)"
FT /evidence="ECO:0000305"
FT CONFLICT 2210
FT /note="P -> A (in Ref. 1; AAA79329)"
FT /evidence="ECO:0000305"
FT CONFLICT 2289
FT /note="A -> S (in Ref. 1; AAA79329)"
FT /evidence="ECO:0000305"
FT CONFLICT 2536
FT /note="S -> T (in Ref. 1; AAA79329)"
FT /evidence="ECO:0000305"
FT CONFLICT 2862
FT /note="R -> Q (in Ref. 1; AAA79329)"
FT /evidence="ECO:0000305"
FT CONFLICT 3038
FT /note="S -> G (in Ref. 1; AAA79329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3503 AA; 379780 MW; 975B09F059F7EEF5 CRC64;
MLRSSLLILL AIVLLGSSQA ASHDQERERK LEVFEGVAVD YQIGYIGDFG GIDSGPPYII
VAEAGVETDL AIDRATGEIR TKVKLDRETR ASYSLVAIPL SGRNIRVLVT VKDENDNAPT
FPQTSMHIEF PENTPREVKR TLLPARDLDL EPYNTQRYNI VSGNVNDAFR LSSHRERDGV
LYLDLQISGF LDRETTPGYS LLIEALDGGT PPLRGFMTVN ITIQDVNDNQ PIFNQSRYFA
TVPENATVGT SVLQVYASDT DADENGLVEY AINRRQSDKE QMFRIDPRTG AIYINKALDF
ETKELHELVV VAKDHGEQPL ETTAFVSIRV TDVNDNQPTI NVIFLSDDAS PKISESAQPG
EFVARISVHD PDSKTEYANV NVTLNGGDGH FALTTRDNSI YLVIVHLPLD REIVSNYTLS
VVATDKGTPP LHASKSIFLR ITDVNDNPPE FEQDLYHANV MEVADPGTSV LQVLAHDRDE
GLNSALTYSL AETPETHAQW FQIDPQTGLI TTRSHIDCET EPVPQLTVVA RDGGVPPLSS
TATVLVTIHD VNDNEPIFDQ SFYNVSVAEN EPVGRCILKV SASDPDCGVN AMVNYTIGEG
FKHLTEFEVR SASGEICIAG ELDFERRSSY EFPVLATDRG GLSTTAMIKM QLTDVNDNRP
VFYPREYKVS LRESPKASSQ ASSTPIVAVV ATDPDYGNFG QVSYRIVAGN EAGIFRIDRS
TGEIFVVRPD MLSVRTQPMH MLNISATDGG NLRSNADAVV FLSIIDAMQR PPIFEKARYN
YYVKEDIPRG TVVGSVIAAS GDVAHRSPVR YSIYSGDPDG YFSIETNSGN IRIAKPLDHE
AKSQVLLNIQ ATLGEPPVYG HTQVNIEVED VNDNAPEFEA SMVRISVPES AELGAPLYAA
HAHDKDSGSS GQVTYSLVKE SGKGLFAIDA RSGHLILSQH LDYESSQRHT LIVTATDGGV
PSLSTNLTIL VDVQDVNDNP PVFEKDEYSV NVSESRSINA QIIQVNASDL DTGNNARITY
RIVDAGVDNV TNSISSSDVS QHFGIFPNSG WIYLRAPLDR ETRDRYQLTV LATDNGTPAA
HAKTRVIVRV LDANDNDPKF QKSKYEFRIE ENLRRGSVVG VVTASDLDLG ENAAIRYSLL
PINSSFQVHP VTGEISTREP LDRELRELYD LVVEARDQGT PVRSARVPVR IHVSDVNDNA
PEIADPQEDV VSVREEQPPG TEVVRVRAVD RDHGQNASIT YSIVKGRDSD GHGLFSIDPT
SGVIRTRVVL DHEERSIYRL GVAASDGGNP PRETVRMLRV EVLDLNDNRP TFTSSSLVFR
VREDAALGHV VGSISPIERP ADVVRNSVEE SFEDLRVTYT LNPLTKDLIE AAFDIDRHSG
NLVVARLLDR EVQSEFRLEI RALDTTASNN PQSSAITVKI EVADVNDNAP EWPQDPIDLQ
VSEATPVGTI IHNFTATDAD TGTNGDLQYR LIRYFPQLNE SQEQAMSLFR MDSLTGALSL
QAPLDFEAVQ EYLLIVQALD QSSNVTERLQ TSVTVRLRIL DANDHAPHFV SPNSSGGKTA
SLFISDATRI GEVVAHIVAV DEDSGDNGQL TYEITGGNGE GRFRINSQTG IIELVKSLPP
ATEDVEKGGR FNLIIGAKDH GQPEPKKSSL NLHLIVQGSH NNPPRFLQAV YRATILENVP
SGSFVLQVTA KSLHGAENAN LSYEIPAGVA NDLFHVDWQR GIITTRGQFD RESQASYVLP
VYVRDANRQS TLSSSAVRKQ RSSDSIGDTS NGQHFDVATI YITVGDVNDN SPEFRPGSCY
GLSVPENSEP GVIHTVVASD LDEGPNADLI YSITGGNLGN KFSIDSSSGE LSARPLDREQ
HSRYTLQIQA SDRGQPKSRQ GHCNITIFVE DQNDNAPRFK LSKYTGSVQE DAPLGTSVVQ
ISAVDADLGV NARLVYSLAN ETQWQFAIDG QSGLITTVGK LDRELQASYN FMVLATDGGR
YEVRSATVPV QINVLDINDN RPIFERYPYI GQVPALIQPG QTLLKVQALD ADLGANAEIV
YSLNAENSAV SAKFRINPST GALSASQSLA SESGKLLHLE VVARDKGNPP QSSLGLIELL
IGEAPQGTPV LRFQNETYRV MLKENSPSGT RLLQVVALRS DGRRQKVQFS FGAGNEDGIL
SLDSLSGEIR VNKPHLLDYD RFSTPSMSAL SRGRALHYEE EIDESSEEDP NNSTRSQRAL
TSSSFALTNS QPNEIRVVLV ARTADAPFLA SYAELVIELE DENDNSPKFS QKQFVATVSE
GNNKGTFVAQ VHAFDSDAGS NARLRYHIVD GNHDNAFVIE PAFSGIVRTN IVLDREIRDI
YKLKIIATDE GVPQMTGTAT IRVQIVDVND NQPTFPPNNL VTVSEATELG AVITSISAND
VDTYPALTYR LGAESTVDIE NMSIFALDRY SGKLVLKRRL DYELQQEYEL DVIASDAAHE
ARTVLTVRVN DENDNAPVFL AQQPPAYFAI LPAISEISES LSVDFDLLTV NATDADSEGN
NSKVIYIIEP AQEGFSVHPS NGVVSVNMSR LQPAVSSSGD YFVRIIAKDA GKPALKSSTL
LRVQANDNGS GRSQFLQNQY RAQISEAAPL GSVVLQLGQD ALDQSLAIIA GNEESAFELL
QSKAIVLVKP LDRERNDLYK LRLVLSHPHG PPLISSLNSS SGISVIITIL DANDNFPIFD
RSAKYEAEIS ELAPLRYSIA QLQAIDADQE NTPNSEVVYD ITSGNDEHMF TIDLVTGVLF
VNNRLDYDSG AKSYELIIRA CDSHHQRPLC SLQPFRLELH DENDNEPKFP LTEYVHFLAE
NEPVGSSVFR AHASDLDKGP FGQLNYSIGP APSDESSWKM FRVDSESGLV TSAFVFDYEQ
RQRYDMELLA SDMGGKKASV AVRVEIESRD EFTPQFTERT YRFVLPAAVA LPQGYVVGQV
TATDSDSGPD GRVVYQLSAP HSHFKVNRSS GAVLIKRKLK LDGDGDGNLY MDGRDISLVI
SASSGRHNSL SSMAVVEIAL DPLAHPGTNL ASAGGSSSGS IGDWAIGLLV AFLLVLCAAA
GIFLFIHMRS RKPRNAVKPH LATDNAGVGN TNSYVDPSAF DTIPIRGSIS GGAAGAASGQ
FAPPKYDEIP PFGAHAGSSG AATTSELSGS EQSGSSGRGS AEDDGEDEEI RMINEGPLHH
RNGGAGAGSD DGRISDISVQ NTQEYLARLG IVDHDPSGAG GGASSMAGSS HPMHLYHDDD
ATARSDITNL IYAKLNDVTG AGSEIGSSAD DAGTTAGSIG TIGTAITHGH GVMSSYGEVP
VPVPVVVGGS NVGGSLSSIV HSEEELTGSY NWDYLLDWGP QYQPLAHVFS EIARLKDDTL
SEHSGSGASS SAKSKHSSSH SSAGAGSVVL KPPPSAPPTH IPPPLLTNVA PRAINLPMRL
PPHLSLAPAH LPRSPIGHEA SGSFSTSSAM SPSFSPSLSP LATRSPSISP LGAGPPTHLP
HVSLPRHGHA PQPSQRGNVG TRM
