位置:首页 > 蛋白库 > VANG2_DANRE
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024