VNG2B_XENLA
ID VNG2B_XENLA Reviewed; 521 AA.
AC Q90Z05;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Vang-like protein 2-B;
DE AltName: Full=Protein strabismus-B;
DE AltName: Full=Van Gogh-like protein 2-B;
DE AltName: Full=Xstrabismus-B;
DE Short=Xstbm-B;
GN Name=vangl2-b; Synonyms=stbm-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK70879.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF 500-SER--VAL-521.
RC TISSUE=Gastrula {ECO:0000269|PubMed:12074560};
RX PubMed=12074560; DOI=10.1006/dbio.2002.0673;
RA Goto T., Keller R.;
RT "The planar cell polarity gene strabismus regulates convergence and
RT extension and neural fold closure in Xenopus.";
RL Dev. Biol. 247:165-181(2002).
RN [2] {ECO:0000312|EMBL:AAH99002.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg {ECO:0000312|EMBL:AAH99002.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=15854914; DOI=10.1016/j.cub.2005.03.040;
RA Goto T., Davidson L., Asashima M., Keller R.;
RT "Planar cell polarity genes regulate polarized extracellular matrix
RT deposition during frog gastrulation.";
RL Curr. Biol. 15:787-793(2005).
RN [4]
RP INTERACTION WITH PRICKLE3.
RX PubMed=26079437; DOI=10.1016/j.ydbio.2015.06.013;
RA Ossipova O., Chu C.W., Fillatre J., Brott B.K., Itoh K., Sokol S.Y.;
RT "The involvement of PCP proteins in radial cell intercalations during
RT Xenopus embryonic development.";
RL Dev. Biol. 408:316-327(2015).
RN [5]
RP INTERACTION WITH PRICKLE3.
RX PubMed=27658614; DOI=10.7554/elife.16463;
RA Chu C.W., Sokol S.Y.;
RT "Wnt proteins can direct planar cell polarity in vertebrate ectoderm.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Has a role in non-canonical Wnt/planar cell polarity (PCP)
CC signaling; can recruit dvl/dsh and prickle from the cytoplasm to the
CC plasma membrane. Acts in a PCP complex to regulate the polarized
CC assembly of fibronectrin on the surface of the mesoderm during
CC gastrulation. Regulates convergent extension in both dorsal mesoderm
CC and neural tissue without affecting cell fate. Regulates neural fold
CC closure during neurulation (PubMed:12074560, PubMed:15854914). May be
CC required for cell surface localization of fzd3 and fzd6 in the inner
CC ear (By similarity). {ECO:0000250|UniProtKB:Q90X64,
CC ECO:0000250|UniProtKB:Q91ZD4, ECO:0000269|PubMed:12074560,
CC ECO:0000269|PubMed:15854914}.
CC -!- SUBUNIT: Interacts with dvl/dsh (By similarity). Interacts with
CC prickle3 (PubMed:27658614, PubMed:26079437).
CC {ECO:0000250|UniProtKB:Q90X64, ECO:0000269|PubMed:26079437,
CC ECO:0000269|PubMed:27658614}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q90X64};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q90X64}. Note=Cell
CC membrane localization is regulated by prickle.
CC {ECO:0000250|UniProtKB:Q90X64}.
CC -!- TISSUE SPECIFICITY: During gastrulation, broadly expressed in the
CC dorsal region in both mesodermal and neural tissues. From the neurula
CC stages, expressed throughout the neural tube. In tailbud stages,
CC expression declines in the anterior notochord but remains strong in the
CC posterior notochord and in the neural tube. Also weakly expressed in
CC the prenephritic region of late tailbud embryos.
CC {ECO:0000269|PubMed:12074560}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout early development. Maternal expression declines gradually by
CC the early gastrula stage (stage 10). Zygotic expression increases by
CC late gastrula stage (stage 12) with strong expression from the
CC midneurula stage (stage 15) onward. {ECO:0000269|PubMed:12074560}.
CC -!- SIMILARITY: Belongs to the Vang family. {ECO:0000255}.
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DR EMBL; AF387816; AAK70879.1; -; mRNA.
DR EMBL; BC099002; AAH99002.1; -; mRNA.
DR RefSeq; NP_001083892.1; NM_001090423.1.
DR RefSeq; XP_018087414.1; XM_018231925.1.
DR AlphaFoldDB; Q90Z05; -.
DR SMR; Q90Z05; -.
DR DNASU; 399177; -.
DR GeneID; 399177; -.
DR KEGG; xla:399177; -.
DR CTD; 399177; -.
DR Xenbase; XB-GENE-973465; vangl2.S.
DR OMA; DKSVMIQ; -.
DR OrthoDB; 1325060at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 399177; Expressed in egg cell and 19 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IMP:UniProtKB.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR009539; VANGL.
DR PANTHER; PTHR20886; PTHR20886; 1.
DR Pfam; PF06638; Strabismus; 1.
DR PIRSF; PIRSF007991; Strabismus; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Gastrulation; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT CHAIN 1..521
FT /note="Vang-like protein 2-B"
FT /id="PRO_0000282965"
FT TOPO_DOM 1..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..147
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 518..521
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 500..521
FT /note="Missing: Dominant negative that inhibits vangl2-B
FT function."
FT /evidence="ECO:0000269|PubMed:12074560"
SQ SEQUENCE 521 AA; 60105 MW; 220006483DFB1F60 CRC64;
MDNDSQYSGY SYKSGQSRSS RKHRDRRERH RSKSREGSRG DKSVTIQAPG EPLLDNESTR
GEDRDDNWGE TTTVVTGTSE HSISHDDITR ITKDMEDSAK LDCSRHLGVV IAGALALLSF
LTPIAFMLLP QILWREDLEQ CGTACEGLFI SVAFKLLILL LGSWALFFRR PKAFFPRVFV
FRALLMVLVF LLVVSYWLFY GVRILESRDK NYQGIVQYAV SLVDALLFVH YLAVVLLELR
QLQPQFTIKV VRSTDGASRF YNIGHLSIQR VAVWILENYY HDFPVYNPAL LNLPKSILSK
KMSGFKVYSL GEENNTNNST GQSRAVIAAA ARRRDNSHNE YYYEEAEHER RVRKRKARLV
VAVEEAFTHI KRLQDEDPKN PREIMDPREA AQAIFASMAR AMQKYLRTTK QQPYHTMESI
LQHLEFCITH DMTPKAFLER YLGPGPTIQY HKDRWLAKQW TLVSEEPVTN GLKDGVVFEL
KRQDFSLVVS TKKIPFFKLS EEFVDPKSHK FVMRLQSETS V
