MIG5_CAEEL
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 03-AUG-2022, entry version 175.
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; -.
DR PaxDb; Q22227; -.
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 CTD; 174317; -.
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; 474724at2759; -.
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-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
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 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 Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.240.130; -; 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; PTHR10878; 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF54236; SSF54236; 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
