PAR6B_MOUSE
ID PAR6B_MOUSE Reviewed; 371 AA.
AC Q9JK83; A2ANX8; Q8R3J8;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Partitioning defective 6 homolog beta;
DE Short=PAR-6 beta;
DE Short=PAR-6B;
GN Name=Pard6b; Synonyms=Par6b;
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] (ISOFORM 1), FUNCTION, INTERACTION WITH PARD3;
RP PRKCI; PRKCZ; RHOQ AND CDC42, SUBUNIT OF A COMPLEX CONTAINING CDC42; PARD3
RP AND PRKCI, AND MUTAGENESIS OF 133-ILE-SER-134; PRO-136; PHE-139 AND
RP 167-LYS--GLY-170.
RC TISSUE=Embryo;
RX PubMed=10934474; DOI=10.1038/35019573;
RA Joberty G., Petersen C., Gao L., Macara I.G.;
RT "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to
RT Cdc42.";
RL Nat. Cell Biol. 2:531-539(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
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 [5]
RP FUNCTION.
RX PubMed=11839275; DOI=10.1016/s0960-9822(01)00663-7;
RA Gao L., Joberty G., Macara I.G.;
RT "Assembly of epithelial tight junctions is negatively regulated by Par6.";
RL Curr. Biol. 12:221-225(2002).
RN [6]
RP INTERACTION WITH PALS1, AND DOMAIN.
RX PubMed=12545177; DOI=10.1038/ncb923;
RA Hurd T.W., Gao L., Roh M.H., Macara I.G., Margolis B.;
RT "Direct interaction of two polarity complexes implicated in epithelial
RT tight junction assembly.";
RL Nat. Cell Biol. 5:137-142(2003).
RN [7]
RP INTERACTION WITH PALS1, AND MUTAGENESIS OF MET-235.
RX PubMed=15140881; DOI=10.1074/jbc.m401930200;
RA Wang Q., Hurd T.W., Margolis B.;
RT "Tight junction protein Par6 interacts with an evolutionarily conserved
RT region in the amino terminus of PALS1/stardust.";
RL J. Biol. Chem. 279:30715-30721(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-11, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Testis;
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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 112-252 IN COMPLEX WITH CDC42.
RX PubMed=12606577; DOI=10.1093/emboj/cdg110;
RA Garrard S.M., Capaldo C.T., Gao L., Rosen M.K., Macara I.G., Tomchick D.R.;
RT "Structure of Cdc42 in a complex with the GTPase-binding domain of the cell
RT polarity protein, Par6.";
RL EMBO J. 22:1125-1133(2003).
CC -!- FUNCTION: Adapter protein involved in asymmetrical cell division and
CC cell polarization processes. Probably involved in formation of
CC epithelial tight junctions. Association with PARD3 may prevent the
CC interaction of PARD3 with F11R/JAM1, thereby preventing tight junction
CC assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to
CC atypical protein kinase C proteins. {ECO:0000269|PubMed:10934474,
CC ECO:0000269|PubMed:11839275}.
CC -!- SUBUNIT: Interacts with PARD3. Interacts with GTP-bound forms of CDC42,
CC RHOQ/TC10 and RAC1. Interacts with the N-terminal part of PRKCI and
CC PRKCZ. Part of a complex with PARD3, CDC42 or RAC1 and PRKCI or PRKCZ.
CC Part of a complex with LLGL1 and PRKCI. Interacts with ALS2CR19.
CC Interacts with ECT2 (By similarity). Interacts with PALS1.
CC {ECO:0000250, ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:12545177,
CC ECO:0000269|PubMed:12606577, ECO:0000269|PubMed:15140881}.
CC -!- INTERACTION:
CC Q9JK83; P60953: CDC42; Xeno; NbExp=6; IntAct=EBI-81861, EBI-81752;
CC Q9JK83; Q8TEW0: PARD3; Xeno; NbExp=3; IntAct=EBI-81861, EBI-81968;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Cell junction, tight
CC junction. Note=Colocalizes with active form of CDC42 or RAC1 at
CC membrane ruffles. Also localizes to tight junctions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JK83-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JK83-2; Sequence=VSP_007460, VSP_007461;
CC -!- TISSUE SPECIFICITY: Expressed in pancreas and in both adult and fetal
CC kidney. Weakly expressed in placenta and lung. Not expressed in other
CC tissues.
CC -!- DOMAIN: The pseudo-CRIB domain together with the PDZ domain is required
CC for the interaction with Rho small GTPases.
CC {ECO:0000269|PubMed:12545177}.
CC -!- DOMAIN: The PDZ domain mediates the interaction with PALS1.
CC {ECO:0000269|PubMed:12545177}.
CC -!- SIMILARITY: Belongs to the PAR6 family. {ECO:0000305}.
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DR EMBL; AF252291; AAF71528.1; -; mRNA.
DR EMBL; AL831766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466551; EDL06536.1; -; Genomic_DNA.
DR EMBL; BC025147; AAH25147.1; -; mRNA.
DR CCDS; CCDS17108.1; -. [Q9JK83-1]
DR RefSeq; NP_067384.2; NM_021409.2. [Q9JK83-1]
DR PDB; 1NF3; X-ray; 2.10 A; C/D=126-253.
DR PDB; 6JUE; X-ray; 1.55 A; A=362-371.
DR PDBsum; 1NF3; -.
DR PDBsum; 6JUE; -.
DR AlphaFoldDB; Q9JK83; -.
DR SMR; Q9JK83; -.
DR BioGRID; 208398; 12.
DR CORUM; Q9JK83; -.
DR IntAct; Q9JK83; 15.
DR STRING; 10090.ENSMUSP00000052619; -.
DR iPTMnet; Q9JK83; -.
DR PhosphoSitePlus; Q9JK83; -.
DR EPD; Q9JK83; -.
DR MaxQB; Q9JK83; -.
DR PaxDb; Q9JK83; -.
DR PeptideAtlas; Q9JK83; -.
DR PRIDE; Q9JK83; -.
DR ProteomicsDB; 288061; -. [Q9JK83-1]
DR ProteomicsDB; 288062; -. [Q9JK83-2]
DR Antibodypedia; 2853; 154 antibodies from 29 providers.
DR DNASU; 58220; -.
DR Ensembl; ENSMUST00000052125; ENSMUSP00000052619; ENSMUSG00000044641. [Q9JK83-1]
DR GeneID; 58220; -.
DR KEGG; mmu:58220; -.
DR UCSC; uc008oao.2; mouse. [Q9JK83-1]
DR CTD; 84612; -.
DR MGI; MGI:2135605; Pard6b.
DR VEuPathDB; HostDB:ENSMUSG00000044641; -.
DR eggNOG; KOG3606; Eukaryota.
DR GeneTree; ENSGT00950000183211; -.
DR HOGENOM; CLU_040653_2_0_1; -.
DR InParanoid; Q9JK83; -.
DR OMA; HGASSGC; -.
DR OrthoDB; 825211at2759; -.
DR PhylomeDB; Q9JK83; -.
DR TreeFam; TF312899; -.
DR Reactome; R-MMU-420029; Tight junction interactions.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR BioGRID-ORCS; 58220; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Pard6b; mouse.
DR EvolutionaryTrace; Q9JK83; -.
DR PRO; PR:Q9JK83; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9JK83; protein.
DR Bgee; ENSMUSG00000044641; Expressed in secondary oocyte and 158 other tissues.
DR Genevisible; Q9JK83; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007043; P:cell-cell junction assembly; IEA:InterPro.
DR GO; GO:0007098; P:centrosome cycle; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0060341; P:regulation of cellular localization; IBA:GO_Central.
DR CDD; cd06403; PB1_Par6; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR IDEAL; IID50101; -.
DR InterPro; IPR034873; PAR-6B.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR034868; PB1_Par6.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR14102:SF4; PTHR14102:SF4; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division;
KW Cell junction; Cell membrane; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome; Tight junction.
FT CHAIN 1..371
FT /note="Partitioning defective 6 homolog beta"
FT /id="PRO_0000112517"
FT DOMAIN 16..96
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 133..150
FT /note="Pseudo-CRIB"
FT DOMAIN 157..250
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 126..253
FT /note="Interaction with PARD3 and CDC42"
FT /evidence="ECO:0000269|PubMed:10934474"
FT REGION 253..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 298
FT /note="I -> C (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007460"
FT VAR_SEQ 299..371
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007461"
FT MUTAGEN 133..134
FT /note="IS->AA: Does not abolish interaction with CDC42 and
FT RHOQ."
FT /evidence="ECO:0000269|PubMed:10934474"
FT MUTAGEN 136
FT /note="P->A: Abolishes interaction with RHOQ, but not the
FT interaction with CDC42; when associated with A-139."
FT /evidence="ECO:0000269|PubMed:10934474"
FT MUTAGEN 139
FT /note="F->A: Abolishes interaction with RHOQ, but not the
FT interaction with CDC42; when associated with A-136."
FT /evidence="ECO:0000269|PubMed:10934474"
FT MUTAGEN 167..170
FT /note="KPLG->AAAA: Strongly reduces interaction with PARD3.
FT Does not abolish interaction with CDC42 and RHOQ."
FT /evidence="ECO:0000269|PubMed:10934474"
FT MUTAGEN 235
FT /note="M->W: Prevents interaction with PALS1."
FT /evidence="ECO:0000269|PubMed:15140881"
FT CONFLICT 13
FT /note="C -> W (in Ref. 4; AAH25147)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="L -> P (in Ref. 1; AAF71528)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="Y -> C (in Ref. 1; AAF71528)"
FT /evidence="ECO:0000305"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:1NF3"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:1NF3"
FT STRAND 171..182
FT /evidence="ECO:0007829|PDB:1NF3"
FT STRAND 185..197
FT /evidence="ECO:0007829|PDB:1NF3"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:1NF3"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:1NF3"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1NF3"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:1NF3"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:1NF3"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:1NF3"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:6JUE"
SQ SEQUENCE 371 AA; 41067 MW; 664C7D25262494A9 CRC64;
MNRGHRHGAS SGCLGTMEVK SKFGAEFRRF SLERSKPGKF EEFYGLLQHV HKIPNVDVLV
GYADIHGDLL PINNDDNYHK AVSTANPLLR IFIQKKEEAD YSAFGTDTLI RKKNMLSNVL
RPDNHRKKPH IVISMPQDFR PVSSIIDVDI LPETHRRVRL YKYGTEKPLG FYIRDGSSVR
VTPHGLEKVP GIFISRLVPG GLAQSTGLLA VNDEVLEVNG IEVSGKSLDQ VTDMMIANSR
NLIITVRPAN QRNNVVRNSR TSGSSSQSTD NSLLGFPQQV EASFEPEDQD SDEDDIIIED
SGEPQQIPKA TPAQSLESLT QIELSFESGQ NGFSPPQDTS LVPVPGSLDT ELESRAPDQK
LLEEDGTIIT L
