PAR6G_MOUSE
ID PAR6G_MOUSE Reviewed; 382 AA.
AC Q9JK84;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Partitioning defective 6 homolog gamma;
DE Short=PAR-6 gamma;
DE Short=PAR6A;
GN Name=Pard6g; Synonyms=Par6g;
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].
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).
CC -!- FUNCTION: Adapter protein involved in asymmetrical cell division and
CC cell polarization processes. May play a role in the formation of
CC epithelial tight junctions. The PARD6-PARD3 complex links GTP-bound Rho
CC small GTPases to atypical protein kinase C proteins (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PARD3 (Probable). Interacts with GTP-bound
CC forms of CDC42, RHOQ/TC10 and RAC1 (By similarity). Interacts with the
CC N-terminal part of PRKCI and PRKCZ (By similarity). {ECO:0000250,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}. Cell
CC junction, tight junction {ECO:0000250}.
CC -!- DOMAIN: The pseudo-CRIB domain together with the PDZ domain is required
CC for the interaction with Rho small GTPases. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PAR6 family. {ECO:0000305}.
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DR EMBL; AF252290; AAF71527.1; -; mRNA.
DR CCDS; CCDS29363.1; -.
DR RefSeq; NP_444347.3; NM_053117.3.
DR AlphaFoldDB; Q9JK84; -.
DR SMR; Q9JK84; -.
DR BioGRID; 220281; 4.
DR STRING; 10090.ENSMUSP00000069182; -.
DR iPTMnet; Q9JK84; -.
DR PhosphoSitePlus; Q9JK84; -.
DR MaxQB; Q9JK84; -.
DR PaxDb; Q9JK84; -.
DR PRIDE; Q9JK84; -.
DR ProteomicsDB; 294013; -.
DR Antibodypedia; 23537; 108 antibodies from 19 providers.
DR DNASU; 93737; -.
DR Ensembl; ENSMUST00000070219; ENSMUSP00000069182; ENSMUSG00000056214.
DR GeneID; 93737; -.
DR KEGG; mmu:93737; -.
DR UCSC; uc008fsj.2; mouse.
DR CTD; 84552; -.
DR MGI; MGI:2135606; Pard6g.
DR VEuPathDB; HostDB:ENSMUSG00000056214; -.
DR eggNOG; KOG3606; Eukaryota.
DR GeneTree; ENSGT00950000183211; -.
DR HOGENOM; CLU_040653_2_0_1; -.
DR InParanoid; Q9JK84; -.
DR OMA; HTNTSDE; -.
DR OrthoDB; 825211at2759; -.
DR PhylomeDB; Q9JK84; -.
DR TreeFam; TF312899; -.
DR Reactome; R-MMU-420029; Tight junction interactions.
DR BioGRID-ORCS; 93737; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q9JK84; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9JK84; protein.
DR Bgee; ENSMUSG00000056214; Expressed in skin epidermis and 247 other tissues.
DR Genevisible; Q9JK84; MM.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
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:0007098; P:centrosome cycle; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
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 InterPro; IPR034874; PAR-6_G.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR034868; PB1_Par6.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR14102:SF3; PTHR14102:SF3; 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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cell junction; Cell membrane; Cytoplasm;
KW Membrane; Reference proteome; Tight junction.
FT CHAIN 1..382
FT /note="Partitioning defective 6 homolog gamma"
FT /id="PRO_0000112519"
FT DOMAIN 18..98
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 134..151
FT /note="Pseudo-CRIB"
FT DOMAIN 158..251
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..115
FT /note="Interaction with PRKCI and PRKCZ"
FT /evidence="ECO:0000250"
FT REGION 254..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 42341 MW; 9ED30843B8925533 CRC64;
MNRSFHKSQT LRFYDCSAVE VKSKFGAEFR RFSLDRHKPG KFEDFYQLVV HTHHISNTEV
TIGYADVHGD LLPINNDDNF CKAVSSANPL LRVFIQKREE ADHYSFGAGT LSRKKKVLVT
LRDDGLRRRP HLNISMPHDF RPVSSIIDVD ILPETHRRVR LYRHGYEKPL GFYIRDGTSV
RVTPHGLEKV PGIFISRMVP GGLAESTGLL AVNDEVLEVN GIEVAGKTLD QVTDMMIANS
HNLIVTVKPA NQRNNVVRSS RTSGSSVHST DSTTSHHSLP GAHVLQNSED VESDEEADIV
IEGALEPQHI PKTQAVPPGS LSRANGTSLA HGLHRRDMSL HSSGRESNGS IHRFLSSLKP
DPRHSLVLPQ GGVEEHGPAI TL
