WLS_CAEEL
ID WLS_CAEEL Reviewed; 549 AA.
AC Q7YWX7;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein wntless homolog {ECO:0000250|UniProtKB:Q5T9L3};
DE AltName: Full=Abnormal cell migration protein 14 {ECO:0000312|WormBase:R06B9.6};
DE Flags: Precursor;
GN Name=mig-14 {ECO:0000312|WormBase:R06B9.6};
GN Synonyms=let-553 {ECO:0000312|WormBase:R06B9.6},
GN mom-3 {ECO:0000312|WormBase:R06B9.6}, pvl-2 {ECO:0000312|WormBase:R06B9.6};
GN ORFNames=R06B9.6 {ECO:0000312|WormBase:R06B9.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=8898225; DOI=10.1242/dev.122.10.3117;
RA Harris J., Honigberg L., Robinson N., Kenyon C.;
RT "Neuronal cell migration in C. elegans: regulation of Hox gene expression
RT and cell position.";
RL Development 122:3117-3131(1996).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9288749; DOI=10.1016/s0092-8674(00)80530-9;
RA Thorpe C.J., Schlesinger A., Carter J.C., Bowerman B.;
RT "Wnt signaling polarizes an early C. elegans blastomere to distinguish
RT endoderm from mesoderm.";
RL Cell 90:695-705(1997).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=10388818; DOI=10.1093/genetics/152.3.985;
RA Nishiwaki K.;
RT "Mutations affecting symmetrical migration of distal tip cells in
RT Caenorhabditis elegans.";
RL Genetics 152:985-997(1999).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=11063687; DOI=10.1093/genetics/156.3.1097;
RA Eisenmann D.M., Kim S.K.;
RT "Protruding vulva mutants identify novel loci and Wnt signaling factors
RT that function during Caenorhabditis elegans vulva development.";
RL Genetics 156:1097-1116(2000).
RN [6] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-329.
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 [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=18077322; DOI=10.1073/pnas.0709989104;
RA Myers T.R., Greenwald I.;
RT "Wnt signal from multiple tissues and lin-3/EGF signal from the gonad
RT maintain vulval precursor cell competence in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:20368-20373(2007).
RN [8] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18160346; DOI=10.1016/j.devcel.2007.12.001;
RA Pan C.L., Baum P.D., Gu M., Jorgensen E.M., Clark S.G., Garriga G.;
RT "C. elegans AP-2 and retromer control Wnt signaling by regulating mig-
RT 14/Wntless.";
RL Dev. Cell 14:132-139(2008).
RN [9] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=18160347; DOI=10.1016/j.devcel.2007.12.004;
RA Yang P.T., Lorenowicz M.J., Silhankova M., Coudreuse D.Y., Betist M.C.,
RA Korswagen H.C.;
RT "Wnt signaling requires retromer-dependent recycling of MIG-14/Wntless in
RT Wnt-producing cells.";
RL Dev. Cell 14:140-147(2008).
RN [10] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=19763082; DOI=10.1038/emboj.2009.272;
RA Shi A., Sun L., Banerjee R., Tobin M., Zhang Y., Grant B.D.;
RT "Regulation of endosomal clathrin and retromer-mediated endosome to Golgi
RT retrograde transport by the J-domain protein RME-8.";
RL EMBO J. 28:3290-3302(2009).
RN [11] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21076391; DOI=10.1038/emboj.2010.278;
RA Silhankova M., Port F., Harterink M., Basler K., Korswagen H.C.;
RT "Wnt signalling requires MTM-6 and MTM-9 myotubularin lipid-phosphatase
RT function in Wnt-producing cells.";
RL EMBO J. 29:4094-4105(2010).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=26115433; DOI=10.1371/journal.pone.0130778;
RA Zhu M., Wu G., Li Y.X., Stevens J.K., Fan C.X., Spang A., Dong M.Q.;
RT "Serum- and Glucocorticoid-Inducible Kinase-1 (SGK-1) Plays a Role in
RT Membrane Trafficking in Caenorhabditis elegans.";
RL PLoS ONE 10:e0130778-e0130778(2015).
RN [13]
RP ERRATUM.
RX PubMed=27631731; DOI=10.1371/journal.pone.0163398;
RA Zhu M., Wu G., Li Y.X., Stevens J.K., Fan C.X., Spang A., Dong M.Q.;
RT "Correction: Serum- and Glucocorticoid-Inducible Kinase-1 (SGK-1) Plays a
RT Role in Membrane Trafficking in Caenorhabditis elegans.";
RL PLoS ONE 11:e0163398-e0163398(2016).
CC -!- FUNCTION: Probable sorting receptor which regulates endocytosis and
CC secretion of the wnt ligand egl-20 (PubMed:18160346, PubMed:18160347,
CC PubMed:21076391). Recycling of mig-14 from the plasma membrane to the
CC Golgi apparatus by the retromer complex is essential for its function
CC (PubMed:18160346, PubMed:18160347, PubMed:21076391). Its endosomal
CC trafficking is regulated by its association with sorting nexin snx-3 on
CC early endosomes and the mtm-6/mtm-9 myotubularin complex
CC (PubMed:21076391). Required in embryonic development for endoderm
CC specification and the correct positioning and orientation of the
CC mitotic spindles and division planes in blastomere cells
CC (PubMed:9288749, PubMed:16678095). Functions during vulval development,
CC playing a role in vulval precursor cell fate specification
CC (PubMed:11063687, PubMed:18077322). During development, specifically
CC regulates the migration of HSN neurons, the left Q neuroblast (QL) and
CC its descendants and the distal tip cells of the gonads (PubMed:8898225,
CC PubMed:10388818, PubMed:11063687, PubMed:18160346, PubMed:18160347).
CC Positioning of Q neuroblasts may be both dependent and independent of
CC hox gene mab-5 (PubMed:8898225). Involved in establishing ALM and PLM
CC neuronal cell polarity (PubMed:18160346). {ECO:0000269|PubMed:10388818,
CC ECO:0000269|PubMed:11063687, ECO:0000269|PubMed:16678095,
CC ECO:0000269|PubMed:18077322, ECO:0000269|PubMed:18160346,
CC ECO:0000269|PubMed:18160347, ECO:0000269|PubMed:21076391,
CC ECO:0000269|PubMed:8898225, ECO:0000269|PubMed:9288749}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18160346,
CC ECO:0000269|PubMed:18160347}; Multi-pass membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:19763082,
CC ECO:0000269|PubMed:21076391}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:18160347,
CC ECO:0000269|PubMed:19763082}; Multi-pass membrane protein
CC {ECO:0000255}. Basal cell membrane {ECO:0000269|PubMed:26115433};
CC Multi-pass membrane protein {ECO:0000255}. Late endosome membrane
CC {ECO:0000269|PubMed:26115433}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Traffics between endosomal cell membrane and the
CC Golgi apparatus membrane and the cell membrane to mediate wnt/egl-20
CC secretion (PubMed:18160347, PubMed:21076391). Co-localizes with snx-3
CC on intracellular punctae and early endosomes to facilitate recycling
CC and wnt/egl-20 secretion (PubMed:21076391). Localizes to the
CC basolateral cell membrane of intestine cells, but not the apical cell
CC membrane (PubMed:26115433). {ECO:0000269|PubMed:18160347,
CC ECO:0000269|PubMed:21076391, ECO:0000269|PubMed:26115433}.
CC -!- TISSUE SPECIFICITY: Expressed in the tail hypodermis, stomatointestinal
CC muscle, the mesoblast cell M and its descendants, CAN neurons, the
CC developing vulva, the pharynx and the pharyngeal intestinal valve.
CC {ECO:0000269|PubMed:18160347}.
CC -!- DEVELOPMENTAL STAGE: Expressed in posterior regions at the comma stage
CC of embryogenesis, during larval development and in adults.
CC {ECO:0000269|PubMed:18160347}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal with severely defective
CC embryonic morphogenesis with no endoderm and excess mesoderm
CC (PubMed:9288749, PubMed:18160347). In addition, embryos have defective
CC mitotic spindle orientation in the 8-cell stage ABar blastomere
CC (PubMed:9288749, PubMed:16678095). {ECO:0000269|PubMed:16678095,
CC ECO:0000269|PubMed:18160347, ECO:0000269|PubMed:9288749}.
CC -!- SIMILARITY: Belongs to the wntless family. {ECO:0000305}.
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DR EMBL; BX284602; CAE17879.1; -; Genomic_DNA.
DR RefSeq; NP_001022275.1; NM_001027104.1.
DR AlphaFoldDB; Q7YWX7; -.
DR SMR; Q7YWX7; -.
DR IntAct; Q7YWX7; 5.
DR MINT; Q7YWX7; -.
DR STRING; 6239.R06B9.6; -.
DR EPD; Q7YWX7; -.
DR PaxDb; Q7YWX7; -.
DR PeptideAtlas; Q7YWX7; -.
DR PRIDE; Q7YWX7; -.
DR EnsemblMetazoa; R06B9.6.1; R06B9.6.1; WBGene00003246.
DR GeneID; 175020; -.
DR KEGG; cel:CELE_R06B9.6; -.
DR UCSC; R06B9.6; c. elegans.
DR CTD; 175020; -.
DR WormBase; R06B9.6; CE34955; WBGene00003246; mig-14.
DR eggNOG; ENOG502QSE2; Eukaryota.
DR GeneTree; ENSGT00390000005897; -.
DR HOGENOM; CLU_022911_0_0_1; -.
DR InParanoid; Q7YWX7; -.
DR OMA; YWRHLSA; -.
DR OrthoDB; 418201at2759; -.
DR PhylomeDB; Q7YWX7; -.
DR Reactome; R-CEL-3238698; WNT ligand biogenesis and trafficking.
DR PRO; PR:Q7YWX7; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003246; Expressed in embryo and 4 other tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:WormBase.
DR GO; GO:0071944; C:cell periphery; IDA:WormBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:WormBase.
DR GO; GO:0005794; C:Golgi apparatus; ISS:WormBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031301; C:integral component of organelle membrane; IBA:GO_Central.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0017147; F:Wnt-protein binding; ISS:WormBase.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:UniProtKB.
DR GO; GO:0001714; P:endodermal cell fate specification; IMP:WormBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:WormBase.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0070986; P:left/right axis specification; IGI:UniProtKB.
DR GO; GO:0061357; P:positive regulation of Wnt protein secretion; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010623; P:programmed cell death involved in cell development; IMP:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR GO; GO:0061359; P:regulation of Wnt signaling pathway by Wnt protein secretion; ISS:WormBase.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR GO; GO:0061355; P:Wnt protein secretion; IBA:GO_Central.
DR GO; GO:0060069; P:Wnt signaling pathway, regulating spindle positioning; IMP:WormBase.
DR InterPro; IPR009551; Wntless.
DR PANTHER; PTHR13449; PTHR13449; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Endosome; Golgi apparatus; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..549
FT /note="Protein wntless homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436194"
FT TOPO_DOM 36..236
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 237..257
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 276..296
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..310
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 311..331
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 346..366
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..383
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 384..404
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 440..460
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..483
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 484..504
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 524..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 329
FT /note="H->Y: In ga62."
FT /evidence="ECO:0000269|PubMed:16678095"
SQ SEQUENCE 549 AA; 63306 MW; 2F8DC5853F45529B CRC64;
MAGGAVIENL SNRKLFVIFA GLLVIQIMFF LIGAWYAPSP SSYMEFEMIT CRDETKGLSG
EWIHRDNCQQ ISELSEYTPS SFDLREIVFI AKMPHTRDGI ELEYSPWFQF LLGVLHVDVE
YSEHFKYVAH APLELEVRMG YRDKESKKNE WKELVTSNVT RILECTIAED EKKAGGTYDC
DMLDLFELGS SSYPFYLINI RIPINQQACQ FDNKSANCQI GKLTGLRLIE IHQNGGFTLV
WLWTKTFMTP VVAICLWWYY NRINQLARNP LLLERAILLL GLSLVILDFP IEWISLTYRI
PFLLLISDLR QGLFYTVLFS FWLIFAGEHL IDDNTRNNLK SYRFNLSFII TASLGLLIYD
LIERGIQLYD PFYSVWSSPT GSQIAYFAIF ISAISTVAYF IFLFFKIARV WSTIKSKRSA
QIYQTSENRR LKVEGVIYRF KFLMLFTLLC SAFTIAAYFM KQYGEAQLHG DEARDGFLTG
STSAFFTGAF GMCNIYVLLL LAMYAPSHKH YRGASQLIDE NDDDEIMEDP SNQHTESNAM
TTFLKPSTD
