ID   MIG5_CAEEL              Reviewed;         672 AA.
AC   Q22227; G5EC49; O76471; Q95ZQ0;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=Segment polarity protein dishevelled homolog mig-5 {ECO:0000305};
DE   AltName: Full=Abnormal cell migration protein 5 {ECO:0000312|WormBase:T05C12.6a};
GN   Name=mig-5 {ECO:0000312|WormBase:T05C12.6a};
GN   ORFNames=T05C12.6 {ECO:0000312|WormBase:T05C12.6a};
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:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), NUCLEOTIDE SEQUENCE [MRNA] OF
RP   72-625 (ISOFORM C), FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=16899238; DOI=10.1016/j.ydbio.2006.06.053;
RA   Walston T., Guo C., Proenca R., Wu M., Herman M., Hardin J., Hedgecock E.;
RT   "mig-5/Dsh controls cell fate determination and cell migration in C.
RT   elegans.";
RL   Dev. Biol. 298:485-497(2006).
RN   [2] {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   [3] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=16631156; DOI=10.1016/j.ydbio.2005.12.024;
RA   Wu M., Herman M.A.;
RT   "A novel noncanonical Wnt pathway is involved in the regulation of the
RT   asymmetric B cell division in C. elegans.";
RL   Dev. Biol. 293:316-329(2006).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX   PubMed=17196955; DOI=10.1016/j.ydbio.2006.12.002;
RA   Wu M., Herman M.A.;
RT   "Asymmetric localizations of LIN-17/Fz and MIG-5/Dsh are involved in the
RT   asymmetric B cell division in C. elegans.";
RL   Dev. Biol. 303:650-662(2007).
RN   [5] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=19298786; DOI=10.1016/j.ydbio.2009.01.017;
RA   King R.S., Maiden S.L., Hawkins N.C., Kidd A.R. III, Kimble J., Hardin J.,
RA   Walston T.D.;
RT   "The N- or C-terminal domains of DSH-2 can activate the C. elegans
RT   Wnt/beta-catenin asymmetry pathway.";
RL   Dev. Biol. 328:234-244(2009).
RN   [6] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=19259273; DOI=10.1371/journal.pone.0004690;
RA   Maro G.S., Klassen M.P., Shen K.;
RT   "A beta-catenin-dependent Wnt pathway mediates anteroposterior axon
RT   guidance in C. elegans motor neurons.";
RL   PLoS ONE 4:E4690-E4690(2009).
RN   [7] {ECO:0000305}
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=25344071; DOI=10.1242/dev.113266;
RA   Dejima K., Kang S., Mitani S., Cosman P.C., Chisholm A.D.;
RT   "Syndecan defines precise spindle orientation by modulating Wnt signaling
RT   in C. elegans.";
RL   Development 141:4354-4365(2014).
RN   [8] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=26460008; DOI=10.1073/pnas.1518686112;
RA   Zheng C., Diaz-Cuadros M., Chalfie M.;
RT   "Dishevelled attenuates the repelling activity of Wnt signaling during
RT   neurite outgrowth in Caenorhabditis elegans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13243-13248(2015).
RN   [9] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26795562; DOI=10.1242/jcs.175802;
RA   Baldwin A.T., Clemons A.M., Phillips B.T.;
RT   "Unique and redundant beta-catenin regulatory roles of two Dishevelled
RT   paralogs during C. elegans asymmetric cell division.";
RL   J. Cell Sci. 129:983-993(2016).
CC   -!- FUNCTION: Plays a role in the signal transduction pathways mediated by
CC       multiple Wnt genes (PubMed:26795562). Functions redundantly with other
CC       dishevelled family members throughout development (PubMed:19298786,
CC       PubMed:25344071, PubMed:26460008, PubMed:26795562). During embryonic
CC       and larval development, controls cell migration and/or cell fate
CC       specification of hypodermal cells, hypodermal seam cells, vulval
CC       precursor cells and, through distal tip cell migration, somatic gonad
CC       precursor cells (PubMed:16899238, PubMed:26795562). In early embryos,
CC       regulates the orientation of the mitotic spindle of blastomeres and
CC       specifically, along with dsh-2, is required for the correct mitotic
CC       spindle orientation of the ABar blastomere division plane
CC       (PubMed:16899238, PubMed:25344071). Controls the polarity and the
CC       asymmetric localization of downstream components of the wnt/beta-
CC       catenin asymmetry pathway, and in particular, controls the asymmetric
CC       localization of the wnt receptor lin-17/Frizzled in ectodermal blast B
CC       cells (PubMed:16631156, PubMed:17196955, PubMed:19298786,
CC       PubMed:26795562). May act redundantly with dsh-2 to regulate the
CC       expression and nuclear localization of the beta-catenin homolog wrm-2,
CC       but alone seems to be required for the polarity of wrm-2 during the
CC       asymmetric cell division of hypodermal seam cells (PubMed:26795562).
CC       Also, maintains the polarity and migration of QL neuroblasts in larvae
CC       (PubMed:16899238). During the embryonic development of touch receptor
CC       neurons, may act redundantly with dsh-1, downstream of wnt signaling
CC       ligands and the wnt receptor lin-17/Frizzled, to direct the growth of
CC       neurites of touch receptor neurons towards the anterior of the body of
CC       the worm and towards the PLM touch receptor neuron and other tail
CC       neurons (PubMed:26460008). May play a role in the guidance of posterior
CC       D-type motor neuron axons along the anteroposterior axis
CC       (PubMed:19259273). {ECO:0000269|PubMed:16631156,
CC       ECO:0000269|PubMed:16899238, ECO:0000269|PubMed:17196955,
CC       ECO:0000269|PubMed:19259273, ECO:0000269|PubMed:19298786,
CC       ECO:0000269|PubMed:25344071, ECO:0000269|PubMed:26460008,
CC       ECO:0000269|PubMed:26795562}.
CC   -!- INTERACTION:
CC       Q22227; P03949: abl-1; NbExp=3; IntAct=EBI-316403, EBI-2315883;
CC       Q22227; O16393: CELE_C17E7.4; NbExp=3; IntAct=EBI-316403, EBI-327108;
CC       Q22227; O01580: CELE_F53F10.1; NbExp=4; IntAct=EBI-316403, EBI-327154;
CC       Q22227; G5EEN7: CELE_Y39A1A.3; NbExp=2; IntAct=EBI-316403, EBI-2412943;
CC       Q22227; Q94392: nsf-1; NbExp=3; IntAct=EBI-316403, EBI-316816;
CC       Q22227; O62090: pry-1; NbExp=4; IntAct=EBI-316403, EBI-2917690;
CC       Q22227; G5ECG0: tac-1; NbExp=3; IntAct=EBI-316403, EBI-320612;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000269|PubMed:16899238, ECO:0000269|PubMed:17196955,
CC       ECO:0000269|PubMed:25344071}. Cell membrane
CC       {ECO:0000269|PubMed:17196955}. Cell junction
CC       {ECO:0000269|PubMed:25344071}. Cytoplasm {ECO:0000269|PubMed:16899238,
CC       ECO:0000269|PubMed:17196955, ECO:0000269|PubMed:26795562}. Note=Mainly
CC       localized to the cell cortex, but localizes to the cytoplasm following
CC       dorsal intercalation during hypodermal morphogenesis (PubMed:16899238).
CC       Localizes in puncta in the cytoplasm during interphase prior to seam
CC       cell division (PubMed:26795562). Localizes in puncta in the cell cortex
CC       or cell membrane prior to and after asymmetric blast B cell division
CC       (PubMed:17196955). {ECO:0000269|PubMed:16899238,
CC       ECO:0000269|PubMed:17196955, ECO:0000269|PubMed:26795562}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=a {ECO:0000312|WormBase:T05C12.6a};
CC         IsoId=Q22227-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:T05C12.6b};
CC         IsoId=Q22227-2; Sequence=VSP_058544;
CC       Name=c {ECO:0000312|WormBase:T05C12.6c};
CC         IsoId=Q22227-3; Sequence=VSP_058543, VSP_058544;
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic and larval
CC       development (PubMed:16899238). Expressed in most embryonic cells during
CC       hypodermal morphogenesis, and in Z1 and Z4 distal tip precursor cells,
CC       in distal tips cells during gonadal migration and in the gonandal
CC       primordium, which become vulval precursor cells, during larval
CC       development (PubMed:16899238). Also expressed in hypodermal precursor
CC       cells P11 and P12 and their daughter cells P11.a, P11.p, P12.a and
CC       P12.p, and in the SDQL and PVM neurons which are derived from the QL
CC       neuroblast (PubMed:16899238). During larval development, expressed in
CC       blast B cells and its descendants, the QL cell and in cells in the
CC       nerve ring (PubMed:16631156). {ECO:0000269|PubMed:16631156,
CC       ECO:0000269|PubMed:16899238}.
CC   -!- DOMAIN: The DEP domain is required for cell membrane localization.
CC       {ECO:0000269|PubMed:17196955}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic and larval cell fate, polarity,
CC       division and migration defects (PubMed:16899238, PubMed:17196955,
CC       PubMed:26795562). In several lineages of the developing gonad 42.6% of
CC       hermaphrodites do not have either one or both distal tip cells, which
CC       results in the absence of the corresponding gonad arm, and germline
CC       proliferation defects in the male germ line (PubMed:16899238). Defects
CC       in hypodermal morphogenesis including disorganized dorsal cell
CC       intercalation, eventually resulting in 2-fold stage arrest, and failed
CC       ventral enclosure in some worms (PubMed:16899238). Cell polarity and
CC       migration defects including mitotic spindle misalignment, particularly
CC       in the ABar blastomere which results in the posterior cells of the
CC       blastomere adopting an alternate more anterior position
CC       (PubMed:16899238). Defective QL neuroblast migration with 100% of
CC       descendants migrating towards the anterior rather than the posterior of
CC       larvae (PubMed:16899238). Disrupted asymmetric cell divisions of
CC       hypodermal seam cells with the mislocalization and reduced expression
CC       of a wnt/beta catenin pathway component sys-1 and its negative
CC       regulator apr-1, and wrm-1 in daughter seam cells (PubMed:26795562).
CC       Irregular symmetric localization of lin-17/Frizzled in ectodermal blast
CC       B cells (PubMed:17196955). {ECO:0000269|PubMed:16899238,
CC       ECO:0000269|PubMed:17196955, ECO:0000269|PubMed:26795562}.
CC   -!- SIMILARITY: Belongs to the DSH family. {ECO:0000305}.
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DR   EMBL; AF063244; AAC16434.1; -; mRNA.
DR   EMBL; AF070920; AAC24231.1; -; mRNA.
DR   EMBL; BX284602; CAA91307.1; -; Genomic_DNA.
DR   EMBL; BX284602; CAB61022.1; -; Genomic_DNA.
DR   EMBL; BX284602; CAC42334.1; -; Genomic_DNA.
DR   PIR; T24507; T24507.
DR   PIR; T43171; T43171.
DR   PIR; T43211; T43211.
DR   RefSeq; NP_001022316.1; NM_001027145.2. [Q22227-1]
DR   RefSeq; NP_001022317.1; NM_001027146.2. [Q22227-2]
DR   RefSeq; NP_001022318.1; NM_001027147.2. [Q22227-3]
DR   AlphaFoldDB; Q22227; -.
DR   SMR; Q22227; -.
DR   DIP; DIP-27038N; -.
DR   IntAct; Q22227; 98.
DR   MINT; Q22227; -.
DR   STRING; 6239.T05C12.6a.1; -.
DR   PaxDb; 6239-T05C12-6a; -.
DR   EnsemblMetazoa; T05C12.6a.1; T05C12.6a.1; WBGene00003241. [Q22227-1]
DR   EnsemblMetazoa; T05C12.6b.1; T05C12.6b.1; WBGene00003241. [Q22227-2]
DR   EnsemblMetazoa; T05C12.6c.1; T05C12.6c.1; WBGene00003241. [Q22227-3]
DR   GeneID; 174317; -.
DR   KEGG; cel:CELE_T05C12.6; -.
DR   UCSC; T05C12.6b; c. elegans.
DR   AGR; WB:WBGene00003241; -.
DR   WormBase; T05C12.6a; CE02318; WBGene00003241; mig-5. [Q22227-1]
DR   WormBase; T05C12.6b; CE25100; WBGene00003241; mig-5. [Q22227-2]
DR   WormBase; T05C12.6c; CE28076; WBGene00003241; mig-5. [Q22227-3]
DR   eggNOG; KOG3571; Eukaryota.
DR   GeneTree; ENSGT00950000182903; -.
DR   HOGENOM; CLU_012601_2_0_1; -.
DR   InParanoid; Q22227; -.
DR   OMA; TFTEKCY; -.
DR   OrthoDB; 4268327at2759; -.
DR   PhylomeDB; Q22227; -.
DR   Reactome; R-CEL-201688; WNT mediated activation of DVL.
DR   Reactome; R-CEL-2028269; Signaling by Hippo.
DR   Reactome; R-CEL-4086400; PCP/CE pathway.
DR   Reactome; R-CEL-4641258; Degradation of DVL.
DR   Reactome; R-CEL-5099900; WNT5A-dependent internalization of FZD4.
DR   Reactome; R-CEL-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR   SignaLink; Q22227; -.
DR   PRO; PR:Q22227; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00003241; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR   GO; GO:0035591; F:signaling adaptor activity; IC:WormBase.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0001709; P:cell fate determination; IMP:WormBase.
DR   GO; GO:0060573; P:cell fate specification involved in pattern specification; IGI:WormBase.
DR   GO; GO:0016477; P:cell migration; IMP:WormBase.
DR   GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:UniProtKB.
DR   GO; GO:0048598; P:embryonic morphogenesis; IMP:WormBase.
DR   GO; GO:0001714; P:endodermal cell fate specification; IGI:WormBase.
DR   GO; GO:0048730; P:epidermis morphogenesis; IMP:WormBase.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:WormBase.
DR   GO; GO:0040039; P:inductive cell migration; IMP:WormBase.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0070986; P:left/right axis specification; IGI:UniProtKB.
DR   GO; GO:0001764; P:neuron migration; IMP:WormBase.
DR   GO; GO:0010623; P:programmed cell death involved in cell development; IMP:UniProtKB.
DR   GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; IMP:WormBase.
DR   GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IGI:WormBase.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IGI:WormBase.
DR   GO; GO:0060069; P:Wnt signaling pathway, regulating spindle positioning; IMP:WormBase.
DR   CDD; cd04438; DEP_dishevelled; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.240.130; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR001158; DIX.
DR   InterPro; IPR038207; DIX_dom_sf.
DR   InterPro; IPR015506; Dsh/Dvl-rel.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10878; SEGMENT POLARITY PROTEIN DISHEVELLED; 1.
DR   PANTHER; PTHR10878:SF24; SEGMENT POLARITY PROTEIN DISHEVELLED HOMOLOG MIG-5; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00778; DIX; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00021; DAX; 1.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS50841; DIX; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Cytoplasm;
KW   Developmental protein; Membrane; Reference proteome; Wnt signaling pathway.
FT   CHAIN           1..672
FT                   /note="Segment polarity protein dishevelled homolog mig-5"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000437491"
FT   DOMAIN          9..91
FT                   /note="DIX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT   DOMAIN          226..294
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          427..501
FT                   /note="DEP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT   REGION          97..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          604..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..672
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         300..340
FT                   /note="Missing (in isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058543"
FT   VAR_SEQ         624..672
FT                   /note="GSGGLGGPPPTPLSSTMVLAASPIQSQNAVNHDFDGENSSNSRTRILRT ->
FT                   VTNSRKWWLRRPSADSSIQYYGSSSFSDSVAERSQPRFRRGEQ (in isoform b
FT                   and isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058544"
SQ   SEQUENCE   672 AA;  75018 MW;  198FA92312997CF6 CRC64;
     MEPPCTSDCS QIKVFYYLDD ETTPYVSVIE AREGVATLGN FKNSFTKRGY KYYAKELDPD
     IQREVKVELT TDSDRLRKSQ NGFYEIFLVS TPGYGTLPRN SGTMTRPQRT ALDKRRRRSA
     DFDATPYSDA SLAPSTIVSR RAGEHLAELY TSNSEDPYQY DEHTRRTGDD SSLYEPLAAR
     DMNKIYDDDR RRKKQKKERF RRPYVPSTIS SATESSVNSG LPRILEIYLP MKNVPYLGLS
     VCTIDGHIFV SEIAPEGAVE KDGRVNVGDQ ILQVNRVSFE ELSGPQAVRS LREAASSKRP
     ITLYISKFAR GAPSEYDDPL ASMASETMPL DVGVWVETAV QNTEKMKALG LDPQEQTATT
     IDDGTLPFTS TASDDEERML YDQRRNGIPR ALIEEAERKR ENEQNEKIEQ LTEMIDPIIV
     VRSMARPDSG LAVKNRKWLK ILVPMSFIGR DLVDWLVDHM ADIHNRKKAR IYAARLLAAG
     LIRHVVSKLT FTEKCYYVFG DGILGNDRNS TDTTGTSGTT MRVEATTEVT YVGSPAPHAL
     AARVGRNIPH RLETTTLSPV AHDQTWLRRR RDCESPMTND YASMVGESQI GMNPVGNYHV
     FGTKNNHRQV PAPSQVTSSS LTNGSGGLGG PPPTPLSSTM VLAASPIQSQ NAVNHDFDGE
     NSSNSRTRIL RT
//