WLS_DROME
ID WLS_DROME Reviewed; 594 AA.
AC Q95ST2; Q9VTG4;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein wntless {ECO:0000303|PubMed:16678095, ECO:0000303|PubMed:18160348, ECO:0000303|PubMed:18193032, ECO:0000303|PubMed:18193037};
DE AltName: Full=Evenness interrupted {ECO:0000303|PubMed:16678096, ECO:0000303|PubMed:19837038};
DE AltName: Full=Sprinter {ECO:0000303|PubMed:17108000};
GN Name=wls {ECO:0000303|PubMed:16678095, ECO:0000303|PubMed:18160348,
GN ECO:0000303|PubMed:18193032, ECO:0000303|PubMed:18193037};
GN Synonyms=evi {ECO:0000303|PubMed:16678096, ECO:0000303|PubMed:19837038},
GN srt {ECO:0000303|PubMed:17108000}; ORFNames=CG6210;
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] {ECO:0000305, ECO:0000312|EMBL:ABD58936.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-250.
RX PubMed=16678095; DOI=10.1016/j.cell.2006.02.049;
RA Baenziger C., Soldini D., Schuett C., Zipperlen P., Hausmann G., Basler K.;
RT "Wntless, a conserved membrane protein dedicated to the secretion of Wnt
RT proteins from signaling cells.";
RL Cell 125:509-522(2006).
RN [2] {ECO:0000312|EMBL:AAF50085.2}
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] {ECO:0000305, ECO:0000312|EMBL:AAF50085.2}
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAL28148.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28148.1};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16678096; DOI=10.1016/j.cell.2006.04.009;
RA Bartscherer K., Pelte N., Ingelfinger D., Boutros M.;
RT "Secretion of Wnt ligands requires Evi, a conserved transmembrane
RT protein.";
RL Cell 125:523-533(2006).
RN [6] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17108000; DOI=10.1242/dev.02674;
RA Goodman R.M., Thombre S., Firtina Z., Gray D., Betts D., Roebuck J.,
RA Spana E.P., Selva E.M.;
RT "Sprinter: a novel transmembrane protein required for Wg secretion and
RT signaling.";
RL Development 133:4901-4911(2006).
RN [7] {ECO:0000305}
RP INTERACTION WITH VPS35, AND SUBCELLULAR LOCATION.
RX PubMed=18160348; DOI=10.1016/j.devcel.2007.12.003;
RA Belenkaya T.Y., Wu Y., Tang X., Zhou B., Cheng L., Sharma Y.V., Yan D.,
RA Selva E.M., Lin X.;
RT "The retromer complex influences Wnt secretion by recycling wntless from
RT endosomes to the trans-Golgi network.";
RL Dev. Cell 14:120-131(2008).
RN [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH WG, AND SUBCELLULAR LOCATION.
RX PubMed=18193037; DOI=10.1038/ncb1678;
RA Franch-Marro X., Wendler F., Guidato S., Griffith J., Baena-Lopez A.,
RA Itasaki N., Maurice M.M., Vincent J.P.;
RT "Wingless secretion requires endosome-to-Golgi retrieval of
RT Wntless/Evi/Sprinter by the retromer complex.";
RL Nat. Cell Biol. 10:170-177(2008).
RN [9] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18193032; DOI=10.1038/ncb1687;
RA Port F., Kuster M., Herr P., Furger E., Banziger C., Hausmann G.,
RA Basler K.;
RT "Wingless secretion promotes and requires retromer-dependent cycling of
RT Wntless.";
RL Nat. Cell Biol. 10:178-185(2008).
RN [10] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19837038; DOI=10.1016/j.cell.2009.07.051;
RA Korkut C., Ataman B., Ramachandran P., Ashley J., Barria R., Gherbesi N.,
RA Budnik V.;
RT "Trans-synaptic transmission of vesicular Wnt signals through
RT Evi/Wntless.";
RL Cell 139:393-404(2009).
CC -!- FUNCTION: A segment polarity gene required for wingless (wg)-dependent
CC patterning processes, acting in both wg-sending cells and wg-target
CC cells. In non-neuronal cells wls directs wg secretion. The wls traffic
CC loop encompasses the Golgi, the cell surface, an endocytic compartment
CC and a retrograde route leading back to the Golgi, and involves
CC clathrin-mediated endocytosis and the retromer complex (a conserved
CC protein complex consisting of Vps35 and Vps26). In neuronal cells (the
CC larval motorneuron NMJ), the wg signal moves across the synapse via the
CC release of wls-containing exosome-like vesicles. Postsynaptic wls is
CC required for the trafficking of fz2 through the fz2-interacting protein
CC Grip. {ECO:0000269|PubMed:16678095, ECO:0000269|PubMed:16678096,
CC ECO:0000269|PubMed:17108000, ECO:0000269|PubMed:18193032,
CC ECO:0000269|PubMed:18193037, ECO:0000269|PubMed:19837038}.
CC -!- SUBUNIT: Interacts with wg; in the Golgi. Interacts with Vps35, a
CC component of the retromer complex; wls stability is regulated by Vps35.
CC {ECO:0000269|PubMed:18160348, ECO:0000269|PubMed:18193037}.
CC -!- SUBCELLULAR LOCATION: Presynaptic cell membrane
CC {ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
CC ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
CC ECO:0000269|PubMed:19837038}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
CC ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
CC ECO:0000269|PubMed:19837038}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
CC ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
CC ECO:0000269|PubMed:19837038}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
CC ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
CC ECO:0000269|PubMed:19837038}. Cell membrane
CC {ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
CC ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
CC ECO:0000269|PubMed:19837038}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
CC ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
CC ECO:0000269|PubMed:19837038}. Endosome membrane
CC {ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
CC ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
CC ECO:0000269|PubMed:19837038}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
CC ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
CC ECO:0000269|PubMed:19837038}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
CC ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
CC ECO:0000269|PubMed:19837038}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
CC ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
CC ECO:0000269|PubMed:19837038}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
CC ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
CC ECO:0000269|PubMed:19837038}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
CC ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
CC ECO:0000269|PubMed:19837038}. Note=In non-neuronal cells, wls binds to
CC wg in the Golgi and accompanies it to the plasma membrane where the two
CC proteins dissociate. Wg is secreted and wls is then internalized and
CC returns to the Golgi apparatus in a retromer-dependent manner. Wls and
CC wg colocalize in the Golgi apparatus in wg-producing cells, and reduced
CC expression is seen in non-producing cells. Endoplasmic reticulum
CC expression is unchanged in wg-producing versus non-producing cells. In
CC neuronal cells, wls is localized both pre- and postsynaptically and is
CC transferred trans-synaptically from the pre- to the postsynaptic
CC compartment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000269|PubMed:18193032};
CC IsoId=Q95ST2-1; Sequence=Displayed;
CC Name=B {ECO:0000269|PubMed:10731132};
CC IsoId=Q95ST2-2; Sequence=VSP_053188;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in the wing imaginal disk,
CC increased expression is observed in a stripe at the dorso-ventral
CC boundary and other regions of the wing disk that express wg. Also
CC expresses in the leg imaginal disk. During larval development,
CC expression is seen in both motorneurons and muscle.
CC {ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18193032,
CC ECO:0000269|PubMed:19837038}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout development. {ECO:0000269|PubMed:16678095,
CC ECO:0000269|PubMed:17108000}.
CC -!- DISRUPTION PHENOTYPE: Segment polarity phenotype (cuticles are smaller
CC and lack the alternate naked regions) and wing margin defects (a
CC reduced number of posterior wing-margin bristles and the even bristles
CC distribution is interrupted). Heterozygotes die as pharate adults with
CC appendage malformations, such as lack of arista and antennal segments,
CC rudimentary legs and wing-to-notum transformations.
CC {ECO:0000269|PubMed:16678095, ECO:0000269|PubMed:16678096,
CC ECO:0000269|PubMed:17108000}.
CC -!- SIMILARITY: Belongs to the wntless family. {ECO:0000255}.
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DR EMBL; DQ305404; ABD58936.1; -; mRNA.
DR EMBL; AE014296; AAF50085.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN11905.1; -; Genomic_DNA.
DR EMBL; AY060600; AAL28148.1; -; mRNA.
DR RefSeq; NP_648445.1; NM_140188.4. [Q95ST2-1]
DR RefSeq; NP_729681.1; NM_168450.3. [Q95ST2-2]
DR AlphaFoldDB; Q95ST2; -.
DR SMR; Q95ST2; -.
DR BioGRID; 64631; 11.
DR IntAct; Q95ST2; 5.
DR STRING; 7227.FBpp0075947; -.
DR TCDB; 8.A.56.1.1; the wntless protein (wls) family.
DR GlyGen; Q95ST2; 1 site.
DR PaxDb; Q95ST2; -.
DR PRIDE; Q95ST2; -.
DR DNASU; 39259; -.
DR EnsemblMetazoa; FBtr0076218; FBpp0075947; FBgn0036141. [Q95ST2-1]
DR EnsemblMetazoa; FBtr0076219; FBpp0075948; FBgn0036141. [Q95ST2-2]
DR GeneID; 39259; -.
DR KEGG; dme:Dmel_CG6210; -.
DR UCSC; CG6210-RA; d. melanogaster. [Q95ST2-1]
DR UCSC; CG6210-RB; d. melanogaster.
DR CTD; 79971; -.
DR FlyBase; FBgn0036141; wls.
DR VEuPathDB; VectorBase:FBgn0036141; -.
DR eggNOG; ENOG502QSE2; Eukaryota.
DR GeneTree; ENSGT00390000005897; -.
DR InParanoid; Q95ST2; -.
DR OMA; YWRHLSA; -.
DR PhylomeDB; Q95ST2; -.
DR Reactome; R-DME-3238698; WNT ligand biogenesis and trafficking.
DR SignaLink; Q95ST2; -.
DR BioGRID-ORCS; 39259; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39259; -.
DR PRO; PR:Q95ST2; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036141; Expressed in wing disc and 43 other tissues.
DR Genevisible; Q95ST2; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005769; C:early endosome; IDA:FlyBase.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0070062; C:extracellular exosome; IDA:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0031301; C:integral component of organelle membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0031302; C:intrinsic component of endosome membrane; IDA:UniProtKB.
DR GO; GO:0031228; C:intrinsic component of Golgi membrane; IDA:UniProtKB.
DR GO; GO:0005771; C:multivesicular body; IDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0035017; P:cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:FlyBase.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:UniProtKB.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
DR GO; GO:0061357; P:positive regulation of Wnt protein secretion; IMP:ParkinsonsUK-UCL.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0033157; P:regulation of intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0007367; P:segment polarity determination; IMP:UniProtKB.
DR GO; GO:0099157; P:trans-synaptic signalling via exosome; IDA:SynGO.
DR GO; GO:0061355; P:Wnt protein secretion; IMP:FlyBase.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR009551; Wntless.
DR PANTHER; PTHR13449; PTHR13449; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection;
KW Developmental protein; Endoplasmic reticulum; Endosome; Glycoprotein;
KW Golgi apparatus; Membrane; Postsynaptic cell membrane; Reference proteome;
KW Segmentation polarity protein; Synapse; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT CHAIN 1..594
FT /note="Protein wntless"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390664"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT TRANSMEM 14..34
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..239
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT TRANSMEM 240..260
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT TRANSMEM 271..291
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..311
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT TRANSMEM 312..332
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT TRANSMEM 345..365
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..390
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT TRANSMEM 391..411
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT TRANSMEM 474..494
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..514
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT TRANSMEM 515..535
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 536..594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT REGION 571..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 437..468
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_053188"
FT MUTAGEN 250
FT /note="P->S: In wls-2; Homozygous lethal."
FT /evidence="ECO:0000269|PubMed:16678095"
SQ SEQUENCE 594 AA; 67890 MW; D8401B3C5D41E069 CRC64;
MSGTILENLS GRKLSILVAT LLLCQVLCFL LGGLYAPLPA GHVTVLGSLC REDHARQNDT
SFLLYSRGAG ACIPVTREEV EQDSTKMANE LVHVFQMPLP RDLRDLDYSR WQQNLIGVLQ
VEFGYDSSSE LREPPRELQL TIDMRLAYRN KGDPDNGWKL YAHGVEHRYL DCVTSHVGPT
ETLYSCDMIP LFELGALHHS FYLLNLRFPL DTPSQMNLQF GHMHDLTLTA IHQNGGFTQI
WLLLKTMLFP FVVGIMIWFW RRVHLLQRSP ALLEYMLIYL GAALTFLNLP LEYLSLVYEM
PYMLLLSDIR QGIFYAMLLT FWLVFAGEHM LIQDAPNKST IRSRYWKHLS AVVVGCISLF
VFDICERGVQ LRNPFYSIWT TPLGAKVAMT FIVLAGVSAA IYFLFLCYMI WKVFRNIGDK
RTSLPSMSQA RRLHYEVPLD QKVEDWAGIV YFYTKAFFFQ LHKANESKGL IYRFKFLMLA
TLVCAALTVA GFIMGQMAEG QWDWNDNVAI QPTSAFLTGV YGMWNIYIFA LLILYAPSHK
QWPTMHHSDE TTQSNENIVA SAASEEIEFS HLPSDSNPSE ISSLTSFTRK VAFD
