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VANG2_RAT
ID   VANG2_RAT               Reviewed;         521 AA.
AC   P84889;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Vang-like protein 2;
DE   AltName: Full=Van Gogh-like protein 2;
GN   Name=Vangl2 {ECO:0000312|RGD:1309442};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000305}
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16687519; DOI=10.1523/jneurosci.4680-05.2006;
RA   Montcouquiol M., Sans N., Huss D., Kach J., Dickman J.D., Forge A.,
RA   Rachel R.A., Copeland N.G., Jenkins N.A., Bogani D., Murdoch J.,
RA   Warchol M.E., Wenthold R.J., Kelley M.W.;
RT   "Asymmetric localization of Vangl2 and Fz3 indicate novel mechanisms for
RT   planar cell polarity in mammals.";
RL   J. Neurosci. 26:5265-5275(2006).
CC   -!- FUNCTION: Involved in the control of early morphogenesis and patterning
CC       of both axial midline structures and the development of neural plate.
CC       Plays a role in the regulation of planar cell polarity, particularly in
CC       the orientation of stereociliary bundles in the cochlea. Required for
CC       polarization and movement of myocardializing cells in the outflow tract
CC       and seems to act via RHOA signaling to regulate this process. Required
CC       for cell surface localization of FZD3 and FZD6 in the inner ear (By
CC       similarity). {ECO:0000250|UniProtKB:Q91ZD4}.
CC   -!- SUBUNIT: Homodimer and heterodimer with VANGL1. Interacts through its
CC       C-terminal region with the N-terminal half of DVL1, DVL2 and DVL3. The
CC       PDZ domain of DVL1, DVL2 and DVL3 is required for the interaction. Also
CC       interacts with the PDZ domains of MAGI3, SCRIB/SCRB1 and FZD3 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Asymmetrically localized to specific cell-cell
CC       boundaries in the developing inner ear. {ECO:0000269|PubMed:16687519}.
CC   -!- DEVELOPMENTAL STAGE: Expression does not persist beyond the early
CC       postnatal period in the sensory region of the inner ear.
CC       {ECO:0000269|PubMed:16687519}.
CC   -!- SIMILARITY: Belongs to the Vang family. {ECO:0000255}.
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DR   EMBL; AABR03084676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001099439.1; NM_001105969.1.
DR   RefSeq; XP_006250338.1; XM_006250276.3.
DR   RefSeq; XP_006250339.1; XM_006250277.3.
DR   RefSeq; XP_017454201.1; XM_017598712.1.
DR   RefSeq; XP_017454202.1; XM_017598713.1.
DR   AlphaFoldDB; P84889; -.
DR   SMR; P84889; -.
DR   BioGRID; 252835; 4.
DR   CORUM; P84889; -.
DR   IntAct; P84889; 4.
DR   MINT; P84889; -.
DR   STRING; 10116.ENSRNOP00000006849; -.
DR   iPTMnet; P84889; -.
DR   PhosphoSitePlus; P84889; -.
DR   SwissPalm; P84889; -.
DR   PaxDb; P84889; -.
DR   PRIDE; P84889; -.
DR   Ensembl; ENSRNOT00000006849; ENSRNOP00000006849; ENSRNOG00000004889.
DR   GeneID; 289229; -.
DR   KEGG; rno:289229; -.
DR   UCSC; RGD:1309442; rat.
DR   CTD; 57216; -.
DR   RGD; 1309442; Vangl2.
DR   eggNOG; KOG3814; Eukaryota.
DR   GeneTree; ENSGT00390000012496; -.
DR   InParanoid; P84889; -.
DR   OMA; TRDMDNE; -.
DR   OrthoDB; 1325060at2759; -.
DR   PhylomeDB; P84889; -.
DR   TreeFam; TF313467; -.
DR   Reactome; R-RNO-9696264; RND3 GTPase cycle.
DR   Reactome; R-RNO-9696270; RND2 GTPase cycle.
DR   Reactome; R-RNO-9696273; RND1 GTPase cycle.
DR   PRO; PR:P84889; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000004889; Expressed in thymus and 17 other tissues.
DR   Genevisible; P84889; RN.
DR   GO; GO:0090651; C:apical cytoplasm; ISO:RGD.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR   GO; GO:0071944; C:cell periphery; ISO:RGD.
DR   GO; GO:0060187; C:cell pole; ISO:RGD.
DR   GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR   GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0001725; C:stress fiber; ISO:RGD.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD.
DR   GO; GO:0045176; P:apical protein localization; ISO:RGD.
DR   GO; GO:0035787; P:cell migration involved in kidney development; ISO:RGD.
DR   GO; GO:0090102; P:cochlea development; ISO:RGD.
DR   GO; GO:0090103; P:cochlea morphogenesis; ISO:RGD.
DR   GO; GO:0060028; P:convergent extension involved in axis elongation; ISO:RGD.
DR   GO; GO:0022007; P:convergent extension involved in neural plate elongation; ISO:RGD.
DR   GO; GO:0060029; P:convergent extension involved in organogenesis; ISO:RGD.
DR   GO; GO:0048546; P:digestive tract morphogenesis; ISO:RGD.
DR   GO; GO:0036514; P:dopaminergic neuron axon guidance; ISO:RGD.
DR   GO; GO:0048105; P:establishment of body hair planar orientation; ISO:RGD.
DR   GO; GO:0001736; P:establishment of planar polarity; ISO:RGD.
DR   GO; GO:0090177; P:establishment of planar polarity involved in neural tube closure; ISO:RGD.
DR   GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; ISO:RGD.
DR   GO; GO:0032835; P:glomerulus development; ISO:RGD.
DR   GO; GO:0001942; P:hair follicle development; ISO:RGD.
DR   GO; GO:0001947; P:heart looping; ISO:RGD.
DR   GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISO:RGD.
DR   GO; GO:0060119; P:inner ear receptor cell development; ISO:RGD.
DR   GO; GO:0060122; P:inner ear receptor cell stereocilium organization; ISO:RGD.
DR   GO; GO:0060993; P:kidney morphogenesis; ISO:RGD.
DR   GO; GO:0060490; P:lateral sprouting involved in lung morphogenesis; ISO:RGD.
DR   GO; GO:0003149; P:membranous septum morphogenesis; ISO:RGD.
DR   GO; GO:0003150; P:muscular septum morphogenesis; ISO:RGD.
DR   GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR   GO; GO:0035567; P:non-canonical Wnt signaling pathway; ISO:RGD.
DR   GO; GO:1905515; P:non-motile cilium assembly; ISO:RGD.
DR   GO; GO:0060488; P:orthogonal dichotomous subdivision of terminal units involved in lung branching morphogenesis; ISO:RGD.
DR   GO; GO:0003402; P:planar cell polarity pathway involved in axis elongation; ISO:RGD.
DR   GO; GO:1904938; P:planar cell polarity pathway involved in axon guidance; ISO:RGD.
DR   GO; GO:0061346; P:planar cell polarity pathway involved in heart morphogenesis; ISO:RGD.
DR   GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; ISO:RGD.
DR   GO; GO:0060489; P:planar dichotomous subdivision of terminal units involved in lung branching morphogenesis; ISO:RGD.
DR   GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:RGD.
DR   GO; GO:0036342; P:post-anal tail morphogenesis; ISO:RGD.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
DR   GO; GO:0090175; P:regulation of establishment of planar polarity; ISO:RGD.
DR   GO; GO:0030111; P:regulation of Wnt signaling pathway; ISO:RGD.
DR   GO; GO:0007266; P:Rho protein signal transduction; ISO:RGD.
DR   GO; GO:0036515; P:serotonergic neuron axon guidance; ISO:RGD.
DR   GO; GO:0048103; P:somatic stem cell division; ISO:RGD.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; ISO:RGD.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; ISO:RGD.
DR   GO; GO:0042060; P:wound healing; ISO:RGD.
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; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..521
FT                   /note="Vang-like protein 2"
FT                   /id="PRO_0000247591"
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..217
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..238
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        239..521
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  59771 MW;  94ECEF3EE63DF5BC CRC64;
     MDTESQYSGY SYKSGHSRSS RKHRDRRDRH RSKSRDGSRG DKSVTIQAPG EPLLDNESTR
     GDERDDNWGE TTTVVTGTSE HSISHDDLTR IAKDMEDSVP LDCSRHLGVA AGAILALLSF
     LTPLAFLLLP PLLWREELEP CGTACEGLFI SVAFKLLILL LGSWALFFRR PKASLPRVFV
     LRALLMVLVF LLVISYWLFY GVRILDARER SYQGVVQFAV SLVDALLFVH YLAVVLLELR
     QLQPQFTLKV VRSTDGASRF YNVGHLSIQR VAVWILEKYY HDFPVYNPAL LNLPKSVLAK
     KVSGFKVYSL GEENSTNNST GQSRAVIAAA ARRRDNSHNE YYYEEAEHER RVRKRRARLV
     VAVEEAFTHI KRLQEEEQKN PREVMDPREA AQAIFASMAR AMQKYLRTTK QQPYHTMESI
     LQHLEFCITH DMTPKAFLER YLAAGPTIQY HKERWLAKQW TLVSEEPVTN GLKDGIVFLL
     KRQDFSLVVS TKKVPFFKLS EEFVDPKSHK FVMRLQSETS V
 
 
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