PAR6A_RAT
ID PAR6A_RAT Reviewed; 346 AA.
AC Q6B4M5; Q4U4X0; Q6B4M6;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Partitioning defective 6 homolog alpha;
DE Short=PAR-6;
DE Short=PAR-6 alpha;
DE Short=PAR-6A;
GN Name=Pard6a; Synonyms=Par-6a, Par6a;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=CD Charles River; TISSUE=Hepatocyte;
RA Braiterman L.T., Olin J.C., Sharma A., McNickle A., Chen Y.-H.,
RA Yamanaka T., Hubbard A.L.;
RT "Identification of the PAR-aPKC complex in hepatic cells: Identification of
RT a PAR6 splice variant with a dominant negative phenotype.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RA Liu X.J., He A.B., Zuo J., Fang F.D., Meng Y.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Adapter protein involved in asymmetrical cell division and
CC cell polarization processes. Probably involved in the 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. Regulates centrosome organization
CC and function. Essential for the centrosomal recruitment of key proteins
CC that control centrosomal microtubule organization.
CC {ECO:0000250|UniProtKB:Q9NPB6, ECO:0000250|UniProtKB:Q9Z101}.
CC -!- SUBUNIT: Interacts with PALS1 and CRB3. Interacts with PARD3. Interacts
CC with GTP-bound forms of CDC42, RHOQ/TC10 and RAC1. Interacts with the
CC N-terminal part of PRKCI and PRKCZ. Part of a complex with PARD3, CDC42
CC or RAC1 and PRKCI or PRKCZ. Part of a complex with LLGL1 and PRKCI.
CC Interacts with MAP2K5. Interacts with TGFBR1; involved in TGF-beta
CC induced epithelial to mesenchymal transition. Interacts with ECT2
CC ('Thr-359' phosphorylated form) and PRKCI. Interacts with DCTN1 and
CC PCM1. {ECO:0000250|UniProtKB:Q9NPB6, ECO:0000250|UniProtKB:Q9Z101}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriolar
CC satellite {ECO:0000250|UniProtKB:Q9NPB6}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9NPB6}. Note=Colocalizes with GTP-bound CDC42
CC or RAC1 at membrane ruffles and with PARD3 at epithelial tight
CC junctions. Recruited to the centrosome by a microtubule and dynein-
CC dynactin-dependent mechanism. {ECO:0000250|UniProtKB:Q9NPB6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6B4M5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6B4M5-2; Sequence=VSP_015769;
CC Name=3; Synonyms=Short;
CC IsoId=Q6B4M5-3; Sequence=VSP_015768;
CC -!- DOMAIN: The PB1 domain mediates interactions with MAP2K5.
CC {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 -!- DOMAIN: The PDZ domain mediates interaction with CRB3. {ECO:0000250}.
CC -!- PTM: Phosphorylated by the TGF-beta receptor. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PAR6 family. {ECO:0000305}.
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DR EMBL; AY682586; AAT80897.1; -; mRNA.
DR EMBL; AY682587; AAT80898.1; -; mRNA.
DR EMBL; DQ011518; AAY32917.1; -; mRNA.
DR AlphaFoldDB; Q6B4M5; -.
DR SMR; Q6B4M5; -.
DR BioGRID; 258812; 2.
DR CORUM; Q6B4M5; -.
DR DIP; DIP-46160N; -.
DR IntAct; Q6B4M5; 2.
DR STRING; 10116.ENSRNOP00000043456; -.
DR iPTMnet; Q6B4M5; -.
DR PhosphoSitePlus; Q6B4M5; -.
DR PaxDb; Q6B4M5; -.
DR RGD; 1303273; Pard6a.
DR eggNOG; KOG3606; Eukaryota.
DR InParanoid; Q6B4M5; -.
DR PhylomeDB; Q6B4M5; -.
DR Reactome; R-RNO-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-RNO-420029; Tight junction interactions.
DR Reactome; R-RNO-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013420; RHOU GTPase cycle.
DR Reactome; R-RNO-9013424; RHOV GTPase cycle.
DR PRO; PR:Q6B4M5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0044295; C:axonal growth cone; IDA:RGD.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0120157; C:PAR polarity complex; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISO:RGD.
DR GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045217; P:cell-cell junction maintenance; ISO:RGD.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:1904781; P:positive regulation of protein localization to centrosome; ISS:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:RGD.
DR GO; GO:0060341; P:regulation of cellular localization; IMP:RGD.
DR CDD; cd06403; PB1_Par6; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR034872; PAR-6_a.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR034868; PB1_Par6.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR14102:SF9; PTHR14102:SF9; 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 Alternative splicing; Cell cycle; Cell division; Cell junction;
KW Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW Reference proteome; Tight junction.
FT CHAIN 1..346
FT /note="Partitioning defective 6 homolog alpha"
FT /id="PRO_0000112515"
FT DOMAIN 15..95
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 1..116
FT /note="Interaction with PRKCI and PRKCZ"
FT /evidence="ECO:0000250"
FT REGION 126..253
FT /note="Interaction with PARD3 and CDC42"
FT /evidence="ECO:0000250"
FT REGION 257..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPB6"
FT VAR_SEQ 1..176
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_015768"
FT VAR_SEQ 96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_015769"
SQ SEQUENCE 346 AA; 37398 MW; E363D7F8960DEF7F CRC64;
MARPQRTPAR SPDSIVEVKS KFDAEFRRFA LPRTSVRGFQ EFSRLLCVVH QIPGLDVLLG
YTDAHGDLLP LTNDDSLHRA LASGPPPLRL LVQKRAEGDS SGLAFASNSL QRRKKGLLLR
PVAPLRTRPP LLISLPQDFR QVSSVIDVDL LPETHRRVRL HKHGSDRPLG FYIRDGMSVR
VAPQGLERVP GIFISRLVRG GLAESTGLLA VSDEILEVNG IEVAGKTLDQ VTDMMVANSH
NLIVTVKPAN QRNNVVRGAS GRLTGPSSVG PGPTDPDSDD DNSDPVIENR HPPCSNGLSQ
GPLCWDLQPG CLHPSAGSSL PSLDSREQAN SGWGNGMRGD VSGFSL
