VANG2_DANRE
ID VANG2_DANRE Reviewed; 526 AA.
AC Q8UVJ6; Q6NZS8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Vang-like protein 2;
DE AltName: Full=Protein strabismus;
DE AltName: Full=Protein trilobite;
DE AltName: Full=Van Gogh-like protein 2;
GN Name=vangl2 {ECO:0000312|ZFIN:ZDB-GENE-020507-3};
GN Synonyms=stbm {ECO:0000303|PubMed:12105418},
GN tri {ECO:0000303|PubMed:9007230};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL30891.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DVL2, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 517-VAL--VAL-526.
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 [2]
RP ERRATUM OF PUBMED:11780127, AND FUNCTION.
RA Park M., Moon R.T.;
RL Nat. Cell Biol. 4:467-467(2002).
RN [3] {ECO:0000312|EMBL:AAH65983.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH65983.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=9007230; DOI=10.1242/dev.123.1.67;
RA Solnica-Krezel L., Stemple D.L., Mountcastle-Shah E., Rangini Z.,
RA Neuhauss S.C.F., Malicki J., Schier A.F., Stainier D.Y.R., Zwartkruis F.,
RA Abdelilah S., Driever W.;
RT "Mutations affecting cell fates and cellular rearrangements during
RT gastrulation in zebrafish.";
RL Development 123:67-80(1996).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=9007234; DOI=10.1242/dev.123.1.117;
RA Stemple D.L., Solnica-Krezel L., Zwartkruis F., Neuhauss S.C.F.,
RA Schier A.F., Malicki J., Stainier D.Y.R., Abdelilah S., Rangini Z.,
RA Mountcastle-Shah E., Driever W.;
RT "Mutations affecting development of the notochord in zebrafish.";
RL Development 123:117-128(1996).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=9007236; DOI=10.1242/dev.123.1.143;
RA Hammerschmidt M., Pelegri F., Mullins M.C., Kane D.A., Brand M.,
RA van Eeden F.J.M., Furutani-Seiki M., Granato M., Haffter P.,
RA Heisenberg C.-P., Jiang Y.-J., Kelsh R.N., Odenthal J., Warga R.M.,
RA Nuesslein-Volhard C.;
RT "Mutations affecting morphogenesis during gastrulation and tail formation
RT in the zebrafish, Danio rerio.";
RL Development 123:143-151(1996).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=9808788; DOI=10.1006/dbio.1998.9032;
RA Marlow F., Zwartkruis F., Malicki J., Neuhauss S.C.F., Abbas L., Weaver M.,
RA Driever W., Solnica-Krezel L.;
RT "Functional interactions of genes mediating convergent extension, knypek
RT and trilobite, during the partitioning of the eye primordium in
RT zebrafish.";
RL Dev. Biol. 203:382-399(1998).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=10996075; DOI=10.1016/s0960-9822(00)00677-1;
RA Henry C.A., Hall L.A., Burr Hille M., Solnica-Krezel L., Cooper M.S.;
RT "Somites in zebrafish doubly mutant for knypek and trilobite form without
RT internal mesenchymal cells or compaction.";
RL Curr. Biol. 10:1063-1066(2000).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=10992326;
RX DOI=10.1002/1526-968x(200008)27:4<159::aid-gene50>3.0.co;2-t;
RA Sepich D.S., Myers D.C., Short R., Topczewski J., Marlow F.,
RA Solnica-Krezel L.;
RT "Role of the zebrafish trilobite locus in gastrulation movements of
RT convergence and extension.";
RL Genesis 27:159-173(2000).
RN [10] {ECO:0000305}
RP FUNCTION.
RX PubMed=11820812; DOI=10.1006/dbio.2001.0532;
RA Bingham S., Higashijima S., Okamoto H., Chandrasekhar A.;
RT "The Zebrafish trilobite gene is essential for tangential migration of
RT branchiomotor neurons.";
RL Dev. Biol. 242:149-160(2002).
RN [11] {ECO:0000305}
RP FUNCTION, AND IDENTIFICATION OF TRILOBITE AS VANGL2.
RX PubMed=12105418; DOI=10.1038/ncb828;
RA Jessen J.R., Topczewski J., Bingham S., Sepich D.S., Marlow F.,
RA Chandrasekhar A., Solnica-Krezel L.;
RT "Zebrafish trilobite identifies new roles for Strabismus in gastrulation
RT and neuronal movements.";
RL Nat. Cell Biol. 4:610-615(2002).
RN [12] {ECO:0000305}
RP FUNCTION.
RX PubMed=12874125; DOI=10.1242/dev.00567;
RA Carreira-Barbosa F., Concha M.L., Takeuchi M., Ueno N., Wilson S.W.,
RA Tada M.;
RT "Prickle 1 regulates cell movements during gastrulation and neuronal
RT migration in zebrafish.";
RL Development 130:4037-4046(2003).
RN [13] {ECO:0000305}
RP FUNCTION.
RX PubMed=15829519; DOI=10.1242/dev.01810;
RA Wada H., Iwasaki M., Sato T., Masai I., Nishiwaki Y., Tanaka H., Sato A.,
RA Nojima Y., Okamoto H.;
RT "Dual roles of zygotic and maternal Scribble1 in neural migration and
RT convergent extension movements in zebrafish embryos.";
RL Development 132:2273-2285(2005).
RN [14] {ECO:0000305}
RP FUNCTION.
RX PubMed=16407953; DOI=10.1038/nature04375;
RA Ciruna B., Jenny A., Lee D., Mlodzik M., Schier A.F.;
RT "Planar cell polarity signalling couples cell division and morphogenesis
RT during neurulation.";
RL Nature 439:220-224(2006).
RN [15] {ECO:0000305}
RP FUNCTION.
RX PubMed=17239849; DOI=10.1016/j.ydbio.2006.12.030;
RA Yin C., Solnica-Krezel L.;
RT "Convergence and extension movements mediate the specification and fate
RT maintenance of zebrafish slow muscle precursors.";
RL Dev. Biol. 304:141-155(2007).
CC -!- FUNCTION: Plays a role in non-canonical Wnt/planar cell polarity (PCP)
CC signaling to regulate convergent extension cell movements during
CC gastrulation. Acts together with scrib and prickle1 and localizes
CC prickle1 and dvl2/dsh to the plasma membrane. Has an overlapping role
CC with kny during both convergent extension and eye development. In the
CC eye, involved in establishing proper alignment of the anterior neural
CC plate and midline cells expressing shha and shhb/twhh. Has indirect
CC effects on a number of other developmental processes including
CC notochord shape formation, neural progenitor cell morphogenesis,
CC segregation of somites and adaxial cell development. Together with
CC prickle1, required for the posterior (caudal) movement of branchiomotor
CC neurons in the hindbrain independently of, and a few hours after,
CC convergent extension (PubMed:11780127, Ref.2, PubMed:9007230,
CC PubMed:9007234, PubMed:9007236, PubMed:9808788, PubMed:10996075,
CC PubMed:10992326, PubMed:11820812, PubMed:12105418, PubMed:12874125,
CC PubMed:15829519, PubMed:16407953, PubMed:17239849). May be required for
CC cell surface localization of fzd3 and fzd6 in the inner ear (By
CC similarity). {ECO:0000250|UniProtKB:Q91ZD4,
CC ECO:0000269|PubMed:10992326, ECO:0000269|PubMed:10996075,
CC ECO:0000269|PubMed:11780127, ECO:0000269|PubMed:11820812,
CC ECO:0000269|PubMed:12105418, ECO:0000269|PubMed:12874125,
CC ECO:0000269|PubMed:15829519, ECO:0000269|PubMed:16407953,
CC ECO:0000269|PubMed:17239849, ECO:0000269|PubMed:9007230,
CC ECO:0000269|PubMed:9007234, ECO:0000269|PubMed:9007236,
CC ECO:0000269|PubMed:9808788, ECO:0000269|Ref.2}.
CC -!- SUBUNIT: Interacts with the PDZ domain of dvl2/dsh.
CC {ECO:0000269|PubMed:11780127}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at the 4-cell stage. In
CC early somitogenesis, becomes more abundant in anterior neural tissue
CC where expression is seen in the neural tube but not in the notochord.
CC {ECO:0000269|PubMed:11780127}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically, with
CC expression peaking at the neurula stage. {ECO:0000269|PubMed:11780127}.
CC -!- SIMILARITY: Belongs to the Vang family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH65983.1; Type=Miscellaneous discrepancy; Note=Sequence differs from that shown at the C-terminus, most likely because of a sequence artifact.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF428249; AAL30891.1; -; mRNA.
DR EMBL; BC065983; AAH65983.1; ALT_SEQ; mRNA.
DR RefSeq; NP_705960.1; NM_153674.1.
DR AlphaFoldDB; Q8UVJ6; -.
DR SMR; Q8UVJ6; -.
DR BioGRID; 79765; 1.
DR STRING; 7955.ENSDARP00000031546; -.
DR PaxDb; Q8UVJ6; -.
DR PRIDE; Q8UVJ6; -.
DR Ensembl; ENSDART00000033316; ENSDARP00000031546; ENSDARG00000027397.
DR GeneID; 245949; -.
DR KEGG; dre:245949; -.
DR CTD; 57216; -.
DR ZFIN; ZDB-GENE-020507-3; vangl2.
DR eggNOG; KOG3814; Eukaryota.
DR GeneTree; ENSGT00390000012496; -.
DR InParanoid; Q8UVJ6; -.
DR OMA; TRDMDNE; -.
DR OrthoDB; 1325060at2759; -.
DR PhylomeDB; Q8UVJ6; -.
DR TreeFam; TF313467; -.
DR Reactome; R-DRE-9696264; RND3 GTPase cycle.
DR Reactome; R-DRE-9696270; RND2 GTPase cycle.
DR Reactome; R-DRE-9696273; RND1 GTPase cycle.
DR PRO; PR:Q8UVJ6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000027397; Expressed in gastrula and 33 other tissues.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:ZFIN.
DR GO; GO:0007015; P:actin filament organization; IMP:ZFIN.
DR GO; GO:0033564; P:anterior/posterior axon guidance; IMP:ZFIN.
DR GO; GO:0003401; P:axis elongation; IGI:ZFIN.
DR GO; GO:0021535; P:cell migration in hindbrain; IMP:ZFIN.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IMP:ZFIN.
DR GO; GO:0000902; P:cell morphogenesis; IMP:ZFIN.
DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR GO; GO:0044782; P:cilium organization; IMP:ZFIN.
DR GO; GO:0035844; P:cloaca development; IMP:ZFIN.
DR GO; GO:0071679; P:commissural neuron axon guidance; IMP:ZFIN.
DR GO; GO:0060026; P:convergent extension; IDA:ZFIN.
DR GO; GO:0060028; P:convergent extension involved in axis elongation; IMP:ZFIN.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IMP:UniProtKB.
DR GO; GO:0060030; P:dorsal convergence; IMP:ZFIN.
DR GO; GO:0048048; P:embryonic eye morphogenesis; IMP:ZFIN.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:ZFIN.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:ZFIN.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:ZFIN.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:ZFIN.
DR GO; GO:0001654; P:eye development; IGI:UniProtKB.
DR GO; GO:0060972; P:left/right pattern formation; IMP:ZFIN.
DR GO; GO:0097475; P:motor neuron migration; IMP:ZFIN.
DR GO; GO:0014812; P:muscle cell migration; IMP:ZFIN.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0001839; P:neural plate morphogenesis; IMP:ZFIN.
DR GO; GO:0021915; P:neural tube development; IMP:UniProtKB.
DR GO; GO:0001841; P:neural tube formation; IMP:ZFIN.
DR GO; GO:0048884; P:neuromast development; IMP:ZFIN.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:0030903; P:notochord development; IMP:UniProtKB.
DR GO; GO:0048570; P:notochord morphogenesis; IMP:ZFIN.
DR GO; GO:0048840; P:otolith development; IMP:ZFIN.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IGI:ZFIN.
DR GO; GO:0045813; P:positive regulation of Wnt signaling pathway, calcium modulating pathway; IMP:UniProtKB.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:ZFIN.
DR GO; GO:0001756; P:somitogenesis; IGI:UniProtKB.
DR GO; GO:0055002; P:striated muscle cell development; IMP:ZFIN.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IMP: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; Differentiation; Gastrulation;
KW Membrane; Neurogenesis; Reference proteome; Transmembrane;
KW Transmembrane helix; Wnt signaling pathway.
FT CHAIN 1..526
FT /note="Vang-like protein 2"
FT /id="PRO_0000283730"
FT TOPO_DOM 1..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..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..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 523..526
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"
FT COMPBIAS 71..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 517..526
FT /note="Missing: No effect on dvl2/dsh-binding."
FT /evidence="ECO:0000269|PubMed:11780127"
SQ SEQUENCE 526 AA; 60082 MW; 3B2FA8D5E2939431 CRC64;
MDNESQYSGY SYKSSHSRSS RKHRDRRDRH RSKSRDSSSR GDKSVTIQAP GEPLLDAEST
RGDDRDDNWG ETTTVVTGTS EHSVSNEDLT RASKELEDSS PLECRRFAGP IVSGVLGLFA
LLTPLAFLLL PQLLWRDSLE PCGTPCEGLY VSLAFKLLVL LISSWALFLR PSRSTLPRFF
VFRCLLMALV FLFVASYWLF YGVRVLEPRE RDYRGIVGYA VSLVDALLFI QYLALVLLEV
RHLRPAFCLK VVRTTDGASR FYNVGHLSIQ RAAVWVLDHY YTDFPVYNPA LLNLPKSILS
KKMSGFKVYS LGEENSTNNS TGQSRAMIAA AARRRDNSHN EYYYEEAEMD RRVRKRKARL
VVAVEEAFTH IKRLQDDEAA ASPKHPREVM DPREAAQAIF APMARAMQKY LRTTRQQPYH
SMESIISHLQ FCITHNMTPK AFLERYLTPG PTMQYQRENG RGRQWTLVSE EPVTAALRQG
LVFSLRRLDF ALVVTVTPLP FLNLGEEFID PKSHKFVMRL QSETSV