VANG2_XENTR
ID VANG2_XENTR Reviewed; 521 AA.
AC Q4VBG5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Vang-like protein 2;
DE AltName: Full=Protein strabismus;
DE AltName: Full=Van Gogh-like protein 2;
GN Name=vangl2 {ECO:0000250|UniProtKB:Q9ULK5};
GN Synonyms=stbm {ECO:0000250|UniProtKB:Q90X64};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH95909.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud {ECO:0000312|EMBL:AAH95909.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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. May be required for cell surface
CC localization of fzd3 and fzd6 in the inner ear (By similarity).
CC {ECO:0000250|UniProtKB:Q90X64, ECO:0000250|UniProtKB:Q90Z05,
CC ECO:0000250|UniProtKB:Q91ZD4}.
CC -!- SUBUNIT: Interacts with dvl/dsh (By similarity). Interacts with
CC prickle3 (By similarity). {ECO:0000250|UniProtKB:Q90X64}.
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 -!- SIMILARITY: Belongs to the Vang family. {ECO:0000255}.
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DR EMBL; BC095909; AAH95909.1; -; mRNA.
DR RefSeq; NP_001027481.1; NM_001032310.1.
DR RefSeq; XP_012825299.1; XM_012969845.1.
DR AlphaFoldDB; Q4VBG5; -.
DR PaxDb; Q4VBG5; -.
DR Ensembl; ENSXETT00000012852; ENSXETP00000012852; ENSXETG00000005842.
DR GeneID; 613073; -.
DR KEGG; xtr:613073; -.
DR CTD; 57216; -.
DR Xenbase; XB-GENE-973460; vangl2.
DR eggNOG; KOG3814; Eukaryota.
DR HOGENOM; CLU_015742_1_0_1; -.
DR InParanoid; Q4VBG5; -.
DR OrthoDB; 1325060at2759; -.
DR PhylomeDB; Q4VBG5; -.
DR Reactome; R-XTR-9696273; RND1 GTPase cycle.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000005842; Expressed in 4-cell stage embryo and 29 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; ISS: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:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IBA:GO_Central.
DR InterPro; IPR009539; VANGL.
DR PANTHER; PTHR20886; PTHR20886; 1.
DR Pfam; PF06638; Strabismus; 1.
DR PIRSF; PIRSF007991; Strabismus; 1.
PE 2: Evidence at transcript 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"
FT /id="PRO_0000282966"
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; 60083 MW; 49D568D54AD3EAE5 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
QLQPQFTVKV 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
