VNG2A_XENLA
ID VNG2A_XENLA Reviewed; 521 AA.
AC Q90X64;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Vang-like protein 2-A;
DE AltName: Full=Protein strabismus-A;
DE AltName: Full=Van Gogh-like protein 2-A;
DE AltName: Full=Xstrabismus-A;
DE Short=Xstbm-A;
GN Name=vangl2-a; 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:AAL58480.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Gastrula {ECO:0000269|PubMed:11867525};
RX PubMed=11867525; DOI=10.1093/emboj/21.5.976;
RA Darken R.S., Scola A.M., Rakeman A.S., Das G., Mlodzik M., Wilson P.A.;
RT "The planar polarity gene strabismus regulates convergent extension
RT movements in Xenopus.";
RL EMBO J. 21:976-985(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAL28089.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH DVL, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Tail bud {ECO:0000269|PubMed:11780127};
RX PubMed=11780127; DOI=10.1038/ncb716;
RA Park M., Moon R.T.;
RT "The planar cell-polarity gene stbm regulates cell behaviour and cell fate
RT in vertebrate embryos.";
RL Nat. Cell Biol. 4:20-25(2002).
RN [3]
RP ERRATUM OF PUBMED:11780127.
RA Park M., Moon R.T.;
RL Nat. Cell Biol. 4:467-467(2002).
RN [4] {ECO:0000312|EMBL:AAH72119.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary {ECO:0000312|EMBL:AAH72119.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=12421719; DOI=10.1242/dev.00123;
RA Wallingford J.B., Harland R.M.;
RT "Neural tube closure requires Dishevelled-dependent convergent extension of
RT the midline.";
RL Development 129:5815-5825(2002).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=12941693; DOI=10.1093/emboj/cdg424;
RA Jenny A., Darken R.S., Wilson P.A., Mlodzik M.;
RT "Prickle and Strabismus form a functional complex to generate a correct
RT axis during planar cell polarity signaling.";
RL EMBO J. 22:4409-4420(2003).
RN [7]
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 [8]
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 cell movements in both
CC dorsal mesoderm and neural tissue during gastrulation, without
CC affecting cell fate. Regulates neural fold closure during neurulation
CC (PubMed:11867525, PubMed:11780127, PubMed:12421719). May be required
CC for cell surface localization of fzd3 and fzd6 in the inner ear (By
CC similarity). {ECO:0000250|UniProtKB:Q90Z05,
CC ECO:0000250|UniProtKB:Q91ZD4, ECO:0000269|PubMed:11780127,
CC ECO:0000269|PubMed:11867525, ECO:0000269|PubMed:12421719}.
CC -!- SUBUNIT: Interacts with dvl/dsh (PubMed:11780127). Interacts with
CC prickle3 (PubMed:27658614, PubMed:26079437).
CC {ECO:0000269|PubMed:11780127, ECO:0000269|PubMed:26079437,
CC ECO:0000269|PubMed:27658614}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11780127,
CC ECO:0000269|PubMed:12941693}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11780127, ECO:0000269|PubMed:12941693}. Note=Cell
CC membrane localization is regulated by prickle.
CC {ECO:0000269|PubMed:11780127, ECO:0000269|PubMed:12941693}.
CC -!- TISSUE SPECIFICITY: During gastrulation, broadly expressed throughout
CC the marginal zone and animal cap region. From the neurula stages,
CC expression becomes concentrated in neural tissues, in the neural plate
CC and neural tube. {ECO:0000269|PubMed:11780127,
CC ECO:0000269|PubMed:11867525}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout early development, with expression peaking at the neurula
CC stage. {ECO:0000269|PubMed:11780127, ECO:0000269|PubMed:11867525}.
CC -!- SIMILARITY: Belongs to the Vang family. {ECO:0000255}.
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DR EMBL; AY069979; AAL58480.1; -; mRNA.
DR EMBL; AF427792; AAL28089.1; -; mRNA.
DR EMBL; BC072119; AAH72119.1; -; mRNA.
DR RefSeq; NP_001082179.1; NM_001088710.1.
DR RefSeq; XP_018084209.1; XM_018228720.1.
DR AlphaFoldDB; Q90X64; -.
DR SMR; Q90X64; -.
DR DNASU; 398271; -.
DR GeneID; 398271; -.
DR KEGG; xla:398271; -.
DR CTD; 398271; -.
DR Xenbase; XB-GENE-6251797; vangl2.L.
DR OMA; TRDMDNE; -.
DR OrthoDB; 1325060at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 398271; Expressed in egg cell and 19 other tissues.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IMP:UniProtKB.
DR GO; GO:0001736; P:establishment of planar polarity; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
DR GO; GO:0045813; P:positive regulation of Wnt signaling pathway, calcium modulating pathway; ISS:UniProtKB.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; ISS:UniProtKB.
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-A"
FT /id="PRO_0000282964"
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..81
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..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 60097 MW; 49D0BC3EDADB77DA CRC64;
MDNDSQYSGY SYKSGHSRSS RKHRDRRERH RSKSREGSRG DKSVTIQAPG EPLLDNESTR
GEDRDDNWGE TTTVVTGTSE HSISHDDITR ITKDMEDSAK LDCSRHLGVV IGGALALLSF
LTPIAFMLLP QILWREDLEQ CGTACEGLFI SVAFKLLILL LGSWALFFRR PKAFFPRVFV
FRALLMVLVF LLVVSYWLFY GVRILESRDK NYQGIVQYAV SLVDALLFVH YLAVVLLELR
QLQPQFTIKV VRSTDGASRF YNIGHLSIQR VAVWILENYY HDFPVYNPAL LNLPKSILSK
KMSGFKVYSL GEENTTNNST GQSRAVIAAA ARRRDNSHNE YYYEEAEHER RVRKRKARLV
VAVEEAFTHI KRLQDEDQKN PREIMDPREA AQAIFASMAR AMQKYLRTTK QQPYHTMESI
LHHLEFCITH DMTPKAFLER YLGPGPTIQY HKDRWLAKQW TLVSEEPVTN GLKDGVVFVL
KRQDFSLVVS TKKIPFFKLS EEFVDPKSHK FVMRLQSETS V
