WLS_DROSI
ID WLS_DROSI Reviewed; 562 AA.
AC B4QPR1;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Protein wntless {ECO:0000250|UniProtKB:Q95ST2};
GN Name=wls {ECO:0000250|UniProtKB:Q95ST2}; ORFNames=GD12816;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1] {ECO:0000312|EMBL:EDX10052.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q95ST2}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q95ST2}. Cell membrane
CC {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q95ST2}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q95ST2}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q95ST2}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q95ST2}. Note=In non-neuronal cells, wls binds
CC to wg in the Golgi and accompanies it to the plasma membrane where the
CC two proteins dissociate. Wg is secreted and wls is then internalized
CC and returns to the Golgi apparatus in a retromer-dependent manner. Wls
CC and wg colocalize in the Golgi apparatus in wg-producing cells, and
CC reduced expression is seen in non-producing cells. Endoplasmic
CC reticulum expression is unchanged in wg-producing versus non-producing
CC cells. In neuronal cells, wls is localized both pre- and
CC postsynaptically and is transferred trans-synaptically from the pre- to
CC the postsynaptic compartment (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the wntless family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDX10052.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CM000363; EDX10052.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002084467.1; XM_002084431.2.
DR RefSeq; XP_016031406.1; XM_016169776.1.
DR AlphaFoldDB; B4QPR1; -.
DR SMR; B4QPR1; -.
DR STRING; 7240.B4QPR1; -.
DR EnsemblMetazoa; FBtr0353365; FBpp0317858; FBgn0184542.
DR GeneID; 6737635; -.
DR Proteomes; UP000000304; Chromosome 3l.
DR Bgee; FBgn0184542; Expressed in embryo and 3 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0031302; C:intrinsic component of endosome membrane; ISS:UniProtKB.
DR GO; GO:0031228; C:intrinsic component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0017147; F:Wnt-protein binding; ISS:UniProtKB.
DR GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; ISS:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISS:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0033157; P:regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0007367; P:segment polarity determination; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR009551; Wntless.
DR PANTHER; PTHR13449; PTHR13449; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell projection; Developmental protein;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; Membrane;
KW Postsynaptic cell membrane; Reference proteome;
KW Segmentation polarity protein; Synapse; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT CHAIN 1..562
FT /note="Protein wntless"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390669"
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..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT TRANSMEM 442..462
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..482
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT TRANSMEM 483..503
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..562
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT REGION 539..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 562 AA; 64088 MW; 2009D25D1A1F2A0F 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 RRLHYEGLIY RFKFLMLATL VCAALTVAGF IMGQMAEGQW DWNDNVAIQP
TSAFLTGVYG MWNIYIFALL ILYAPSHKQW PTMHHSDETT QSNENIVASA ASEEIEFSHL
PSDSNPSEIS SLTSFTRKVA FD
