VANG1_MOUSE
ID VANG1_MOUSE Reviewed; 526 AA.
AC Q80Z96; B2RRP5; Q8QZT3;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Vang-like protein 1;
DE AltName: Full=Loop-tail protein 2;
DE AltName: Full=Van Gogh-like protein 1;
GN Name=Vangl1; Synonyms=Lpp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Doudney K., Paternotte C., Murdoch J.N., Copp A.J., Stanier P.;
RT "Identification of LPP2, a second Vang-like protein.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary cancer;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH DVL1; DVL2 AND DVL3.
RX PubMed=15456783; DOI=10.1074/jbc.m408675200;
RA Torban E., Wang H.-J., Groulx N., Gros P.;
RT "Independent mutations in mouse Vangl2 that cause neural tube defects in
RT looptail mice impair interaction with members of the Dishevelled family.";
RL J. Biol. Chem. 279:52703-52713(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-90, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=23029439; DOI=10.1371/journal.pone.0046213;
RA Belotti E., Puvirajesinghe T.M., Audebert S., Baudelet E., Camoin L.,
RA Pierres M., Lasvaux L., Ferracci G., Montcouquiol M., Borg J.P.;
RT "Molecular characterisation of endogenous Vangl2/Vangl1 heteromeric protein
RT complexes.";
RL PLoS ONE 7:E46213-E46213(2012).
CC -!- SUBUNIT: Heterodimer with Vangl2. Interacts through its C-terminal
CC region with the N-terminal half of DVL1, DVL2 and DVL3. The PDZ domain
CC of DVL1, DVL2 and DVL3 is required for the interaction.
CC {ECO:0000269|PubMed:15456783, ECO:0000269|PubMed:23029439}.
CC -!- INTERACTION:
CC Q80Z96; P51141: Dvl1; NbExp=2; IntAct=EBI-1750708, EBI-1538407;
CC Q80Z96; Q60838: Dvl2; NbExp=4; IntAct=EBI-1750708, EBI-641940;
CC Q80Z96; Q61062: Dvl3; NbExp=2; IntAct=EBI-1750708, EBI-1538450;
CC Q80Z96; P31016: Dlg4; Xeno; NbExp=4; IntAct=EBI-1750708, EBI-375655;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23029439};
CC Multi-pass membrane protein {ECO:0000269|PubMed:23029439}.
CC -!- SIMILARITY: Belongs to the Vang family. {ECO:0000305}.
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DR EMBL; AF481860; AAO61752.1; -; mRNA.
DR EMBL; CH466608; EDL07618.1; -; Genomic_DNA.
DR EMBL; BC138519; AAI38520.1; -; mRNA.
DR EMBL; BC138520; AAI38521.1; -; mRNA.
DR EMBL; BC024687; AAH24687.1; -; mRNA.
DR CCDS; CCDS17686.1; -.
DR RefSeq; NP_808213.2; NM_177545.5.
DR AlphaFoldDB; Q80Z96; -.
DR BioGRID; 230877; 13.
DR CORUM; Q80Z96; -.
DR IntAct; Q80Z96; 15.
DR MINT; Q80Z96; -.
DR STRING; 10090.ENSMUSP00000125043; -.
DR iPTMnet; Q80Z96; -.
DR PhosphoSitePlus; Q80Z96; -.
DR jPOST; Q80Z96; -.
DR MaxQB; Q80Z96; -.
DR PaxDb; Q80Z96; -.
DR PRIDE; Q80Z96; -.
DR ProteomicsDB; 297956; -.
DR Antibodypedia; 20174; 193 antibodies from 31 providers.
DR DNASU; 229658; -.
DR Ensembl; ENSMUST00000029453; ENSMUSP00000029453; ENSMUSG00000027860.
DR GeneID; 229658; -.
DR KEGG; mmu:229658; -.
DR UCSC; uc008qrs.3; mouse.
DR CTD; 81839; -.
DR MGI; MGI:2159344; Vangl1.
DR VEuPathDB; HostDB:ENSMUSG00000027860; -.
DR eggNOG; KOG3814; Eukaryota.
DR GeneTree; ENSGT00390000012496; -.
DR HOGENOM; CLU_059010_0_0_1; -.
DR InParanoid; Q80Z96; -.
DR OMA; MWHREND; -.
DR OrthoDB; 1325060at2759; -.
DR PhylomeDB; Q80Z96; -.
DR TreeFam; TF313467; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 229658; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Vangl1; mouse.
DR PRO; PR:Q80Z96; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q80Z96; protein.
DR Bgee; ENSMUSG00000027860; Expressed in yolk sac and 266 other tissues.
DR ExpressionAtlas; Q80Z96; baseline and differential.
DR Genevisible; Q80Z96; MM.
DR GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
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; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..526
FT /note="Vang-like protein 1"
FT /id="PRO_0000186194"
FT TOPO_DOM 1..114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 279
FT /note="L -> V (in Ref. 1; AAO61752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 60064 MW; DCA3CD50A4C0E69A CRC64;
MDTESTYSGY SYYSSHSKKS HRQGERTRER HKSPRNKDGR GSEKSVTIQA PAGEPLLAND
SARTGAEEVQ DDNWGETTTA ITGTSEHSIS QEDIARISKD MEDSVGLDCK RYLGLTVASF
LGLLVFLTPI AFILLPQILW REELKPCGAI CEGLLISVSF KLLILLIGTW ALFFRKQRAD
VPRVFVFRAL LLVLIFLFVV SYWLFYGVRI LDSRDQNYKD IVQYAVSLVD ALLFIHYLAI
VLLELRQLQP MFTLQVVRST DGESRFYSLG HLSIQRAALV VLENYYKDFT IYNPNLLTAS
KFRAAKHMAG LKVYNVDGPS NNATGQSRAM IAAAARRRDS SHNELYYEEA EHERRVKKRR
ARLVVAVEEA FIHIQRLQAE EQQKSPGEVM DPREAAQAIF PSMARALQKY LRTTRQQHYH
SMESILQHLA FCITNSMTPK AFLERYLSAG PTLQYDKDRW LSTQWRLISE EAVTNGLRDG
IVFVLKCLDF SLVVNVKKIP FIVLSEEFID PKSHKFVLRL QSETSV
