ID PARD3_MOUSE Reviewed; 1333 AA.
AC Q99NH2; Q58T10; Q58T11; Q8CB21;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 24-JAN-2024, entry version 187.
DE RecName: Full=Partitioning defective 3 homolog;
DE Short=PAR-3;
DE Short=PARD-3;
DE AltName: Full=Atypical PKC isotype-specific-interacting protein;
DE Short=ASIP;
DE AltName: Full=Ephrin-interacting protein;
DE Short=PHIP;
GN Name=Pard3; Synonyms=Par3;
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 3).
RC STRAIN=NIH Swiss; TISSUE=Embryo;
RX PubMed=9920925; DOI=10.1074/jbc.274.6.3726;
RA Lin D., Gish G.D., Songyang Z., Pawson T.;
RT "The carboxyl terminus of B class ephrins constitutes a PDZ domain binding
RT motif.";
RL J. Biol. Chem. 274:3726-3733(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION,
RP PHOSPHORYLATION BY PRKCZ, INTERACTION WITH PRKCI AND PARD6A, SUBUNIT OF A
RP COMPLEX CONTAINING PARD6A AND CDC42, AND MUTAGENESIS OF 824-SER--SER-826.
RC STRAIN=NIH Swiss;
RX PubMed=10934475; DOI=10.1038/35019582;
RA Lin D., Edwards A.S., Fawcett J.P., Mbamalu G., Scott J.D., Pawson T.;
RT "A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC
RT signalling and cell polarity.";
RL Nat. Cell Biol. 2:540-547(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND PTM.
RC STRAIN=C57BL/6J x SJL/J;
RX PubMed=15766746; DOI=10.1016/j.ydbio.2004.12.034;
RA Duncan F.E., Moss S.B., Schultz R.M., Williams C.J.;
RT "PAR-3 defines a central subdomain of the cortical actin cap in mouse
RT eggs.";
RL Dev. Biol. 280:38-47(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 458-1333 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP INTERACTION WITH PARD6B, AND SUBUNIT OF A COMPLEX CONTAINING PARD6B; PRKCI
RP AND CDC42.
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 [6]
RP INTERACTION WITH F11R.
RX PubMed=11447115; DOI=10.1093/emboj/20.14.3738;
RA Ebnet K., Suzuki A., Horikoshi Y., Hirose T., Meyer zu Brickwedde M.-K.,
RA Ohno S., Vestweber D.;
RT "The cell polarity protein ASIP/PAR-3 directly associates with junctional
RT adhesion molecule (JAM).";
RL EMBO J. 20:3738-3748(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH F11R AND PARD6B.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-156 AND SER-728, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
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 [10]
RP INTERACTION WITH TIAM1 AND TIAM2.
RX PubMed=19893486; DOI=10.1038/emboj.2009.323;
RA Terawaki S., Kitano K., Mori T., Zhai Y., Higuchi Y., Itoh N., Watanabe T.,
RA Kaibuchi K., Hakoshima T.;
RT "The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding
RT module.";
RL EMBO J. 29:236-250(2010).
RN [11]
RP SUBCELLULAR LOCATION, INTERACTION WITH FRMD4A, AND SUBUNIT.
RX PubMed=20080746; DOI=10.1073/pnas.0908423107;
RA Ikenouchi J., Umeda M.;
RT "FRMD4A regulates epithelial polarity by connecting Arf6 activation with
RT the PAR complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:748-753(2010).
RN [12]
RP FUNCTION IN REGULATION OF PERIPHERAL MYELINATION, ACETYLATION AT LYS-831;
RP LYS-848; LYS-881 AND LYS-1327, DEACETYLATION BY SIRT2, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF LYS-831; LYS-848; LYS-881 AND LYS-1327, AND MASS
RP SPECTROMETRY.
RX PubMed=21949390; DOI=10.1073/pnas.1104969108;
RA Beirowski B., Gustin J., Armour S.M., Yamamoto H., Viader A., North B.J.,
RA Michan S., Baloh R.H., Golden J.P., Schmidt R.E., Sinclair D.A., Auwerx J.,
RA Milbrandt J.;
RT "Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through
RT polarity protein Par-3/atypical protein kinase C (aPKC) signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:E952-961(2011).
RN [13]
RP DEVELOPMENTAL STAGE.
RX PubMed=23001562; DOI=10.1093/hmg/dds398;
RA Alves C.H., Sanz A.S., Park B., Pellissier L.P., Tanimoto N., Beck S.C.,
RA Huber G., Murtaza M., Richard F., Sridevi Gurubaran I., Garcia Garrido M.,
RA Levelt C.N., Rashbass P., Le Bivic A., Seeliger M.W., Wijnholds J.;
RT "Loss of CRB2 in the mouse retina mimics human retinitis pigmentosa due to
RT mutations in the CRB1 gene.";
RL Hum. Mol. Genet. 22:35-50(2013).
RN [14]
RP STRUCTURE BY NMR OF 448-558.
RG Center for eukaryotic structural genomics (CESG);
RT "Macromolecular structure determination by NMR spectroscopy.";
RL Submitted (NOV-2009) to the PDB data bank.
RN [15]
RP STRUCTURE BY NMR OF 581-689 IN COMPLEX WITH CDH5 PEPTIDE, AND SUBUNIT.
RX PubMed=20047332; DOI=10.1021/bi9017335;
RA Tyler R.C., Peterson F.C., Volkman B.F.;
RT "Distal interactions within the par3-VE-cadherin complex.";
RL Biochemistry 49:951-957(2010).
CC -!- FUNCTION: Adapter protein involved in asymmetrical cell division and
CC cell polarization processes (By similarity). Seems to play a central
CC role in the formation of epithelial tight junctions (By similarity).
CC Targets the phosphatase PTEN to cell junctions (By similarity).
CC Association with PARD6B may prevent the interaction of PARD3 with
CC F11R/JAM1, thereby preventing tight junction assembly
CC (PubMed:11839275). The PARD6-PARD3 complex links GTP-bound Rho small
CC GTPases to atypical protein kinase C proteins (By similarity). Required
CC for establishment of neuronal polarity and normal axon formation in
CC cultured hippocampal neurons (By similarity). Involved in Schwann cell
CC peripheral myelination (PubMed:21949390).
CC {ECO:0000250|UniProtKB:Q8TEW0, ECO:0000250|UniProtKB:Q9Z340,
CC ECO:0000269|PubMed:11839275, ECO:0000269|PubMed:21949390}.
CC -!- SUBUNIT: Interacts with PRCKI and CDH5. Interacts (via PDZ 3 domain)
CC with PTEN (via C-terminus). Component of a complex whose core is
CC composed of ARHGAP17, AMOT, PALS1, PATJ and PARD3/PAR3. Interacts with
CC LIMK2, AURKA and AURKB. Component of the Par polarity complex, composed
CC of at least phosphorylated PRKCZ, PARD3 and TIAM1. Interacts with ECT2
CC and FBF1 (By similarity). Interacts (via PDZ 1 domain) with F11R/JAM1,
CC PARD6A and PARD6B. Part of a complex with PARD6A or PARD6B, PRKCI or
CC PRKCZ and CDC42 or RAC1. Directly interacts with TIAM1 and TIAM2.
CC Interacts with SIRT2. Interacts (via coiled-coil domain) with FRMD4A
CC (PubMed:20080746). Found in a complex with PARD3, CYTH1 and FRMD4A
CC (PubMed:20080746). Interacts with SAPCD2 (By similarity). Interacts
CC with PRKCA (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8TEW0,
CC ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:10934475,
CC ECO:0000269|PubMed:11447115, ECO:0000269|PubMed:11839275,
CC ECO:0000269|PubMed:19893486, ECO:0000269|PubMed:20047332,
CC ECO:0000269|PubMed:20080746}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with PRKCZ.
CC {ECO:0000269|PubMed:10934475}.
CC -!- INTERACTION:
CC Q99NH2-1; P98078: Dab2; NbExp=2; IntAct=EBI-15946047, EBI-1391846;
CC Q99NH2-1; P35917: Flt4; NbExp=3; IntAct=EBI-15946047, EBI-7845747;
CC Q99NH2-1; Q8R1S4: Mtss1; NbExp=2; IntAct=EBI-15946047, EBI-15622277;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endomembrane system. Cell junction.
CC Cell junction, tight junction {ECO:0000269|PubMed:10934475,
CC ECO:0000269|PubMed:20080746}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:20080746}. Cytoplasm, cell cortex. Cytoplasm,
CC cytoskeleton. Cell membrane {ECO:0000250}. Note=Localized along the
CC cell-cell contact region. Colocalizes with PARD6A and PRKCI at
CC epithelial tight junctions. Colocalizes with the cortical actin that
CC overlays the meiotic spindle during metaphase I and metaphase II.
CC Presence of KRIT1, CDH5 and RAP1B is required for its localization to
CC the cell junction (By similarity). Colocalized with SIRT2 in internode
CC region of myelin sheath. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=180 kDa;
CC IsoId=Q99NH2-1; Sequence=Displayed;
CC Name=2; Synonyms=150 kDa;
CC IsoId=Q99NH2-2; Sequence=VSP_007474;
CC Name=3; Synonyms=100 kDa;
CC IsoId=Q99NH2-3; Sequence=VSP_007472, VSP_007473;
CC Name=4; Synonyms=PAR-3o1, Partitioning defective 3 oocyte form 1;
CC IsoId=Q99NH2-4; Sequence=VSP_035895, VSP_035898, VSP_035899;
CC Name=5; Synonyms=PAR-3o2, Partitioning defective 3 oocyte form 2;
CC IsoId=Q99NH2-5; Sequence=VSP_035895, VSP_035896, VSP_035897;
CC -!- TISSUE SPECIFICITY: All isoforms are expressed in heart, while
CC expression in brain is mainly limited to isoform 1, and to isoform 3 to
CC a weaker level.
CC -!- DEVELOPMENTAL STAGE: Expressed at the outer limiting membrane of the
CC retina at 3 months of age. {ECO:0000269|PubMed:23001562}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 2]: Not expressed in the oocyte.
CC {ECO:0000269|PubMed:15766746}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 1]: Expressed in the oocyte from 9.5 dpc
CC to 14.5 dpc. {ECO:0000269|PubMed:15766746}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 3]: Expressed in the oocyte from 9.5 dpc
CC to 14.5 dpc. {ECO:0000269|PubMed:15766746}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 4]: Expression increases steadily
CC throughout oocyte maturation. {ECO:0000269|PubMed:15766746}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 5]: Expression decreases in the egg as
CC compared to the oocyte. {ECO:0000269|PubMed:15766746}.
CC -!- DOMAIN: Contains a conserved N-terminal oligomerization domain (NTD)
CC that is involved in oligomerization and is essential for proper
CC subapical membrane localization. {ECO:0000250}.
CC -!- DOMAIN: The second PDZ domain mediates interaction with membranes
CC containing phosphoinositol lipids. {ECO:0000250}.
CC -!- PTM: Acetylated. Deacetylated by SIRT2, thereby inhibiting Schwann cell
CC peripheral myelination. {ECO:0000269|PubMed:21949390}.
CC -!- PTM: Phosphorylation at Ser-824 by PRKCZ and PRKCI occurs at the most
CC apical tip of epithelial cell-cell contacts during the initial phase of
CC tight junction formation and may promote dissociation of the complex
CC with PARD6. EGF-induced Tyr-1123 phosphorylation mediates dissociation
CC from LIMK2 (By similarity). Phosphorylation by AURKA at Ser-958 is
CC required for the normal establishment of neuronal polarity (By
CC similarity). Isoform 4 and isoform 5 are phosphorylated during oocyte
CC maturation (Probable). {ECO:0000250, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PAR3 family. {ECO:0000305}.
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DR EMBL; AY026057; AAK07669.1; -; mRNA.
DR EMBL; AY856081; AAX48908.1; -; mRNA.
DR EMBL; AY856082; AAX48909.1; -; mRNA.
DR EMBL; AK037015; BAC29670.1; -; mRNA.
DR CCDS; CCDS22788.1; -. [Q99NH2-1]
DR CCDS; CCDS40523.1; -. [Q99NH2-5]
DR RefSeq; NP_001013598.1; NM_001013580.3. [Q99NH2-5]
DR RefSeq; NP_001013599.1; NM_001013581.2.
DR PDB; 2KOH; NMR; -; A=581-689.
DR PDB; 2KOJ; NMR; -; A=450-558.
DR PDBsum; 2KOH; -.
DR PDBsum; 2KOJ; -.
DR AlphaFoldDB; Q99NH2; -.
DR SMR; Q99NH2; -.
DR BioGRID; 220283; 18.
DR CORUM; Q99NH2; -.
DR DIP; DIP-41727N; -.
DR ELM; Q99NH2; -.
DR IntAct; Q99NH2; 14.
DR MINT; Q99NH2; -.
DR STRING; 10090.ENSMUSP00000125453; -.
DR GlyGen; Q99NH2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99NH2; -.
DR PhosphoSitePlus; Q99NH2; -.
DR jPOST; Q99NH2; -.
DR MaxQB; Q99NH2; -.
DR PaxDb; 10090-ENSMUSP00000125453; -.
DR PeptideAtlas; Q99NH2; -.
DR ProteomicsDB; 287774; -. [Q99NH2-1]
DR ProteomicsDB; 287775; -. [Q99NH2-2]
DR ProteomicsDB; 287776; -. [Q99NH2-3]
DR ProteomicsDB; 287777; -. [Q99NH2-4]
DR ProteomicsDB; 287778; -. [Q99NH2-5]
DR Pumba; Q99NH2; -.
DR Antibodypedia; 26597; 285 antibodies from 35 providers.
DR DNASU; 93742; -.
DR Ensembl; ENSMUST00000108752.10; ENSMUSP00000104383.4; ENSMUSG00000025812.19. [Q99NH2-5]
DR Ensembl; ENSMUST00000160717.8; ENSMUSP00000125612.2; ENSMUSG00000025812.19. [Q99NH2-5]
DR GeneID; 93742; -.
DR KEGG; mmu:93742; -.
DR UCSC; uc009nzk.2; mouse. [Q99NH2-5]
DR AGR; MGI:2135608; -.
DR CTD; 56288; -.
DR MGI; MGI:2135608; Pard3.
DR VEuPathDB; HostDB:ENSMUSG00000025812; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00950000183214; -.
DR InParanoid; Q99NH2; -.
DR OrthoDB; 5405986at2759; -.
DR Reactome; R-MMU-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-MMU-420029; Tight junction interactions.
DR BioGRID-ORCS; 93742; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Pard3; mouse.
DR EvolutionaryTrace; Q99NH2; -.
DR PRO; PR:Q99NH2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q99NH2; Protein.
DR Bgee; ENSMUSG00000025812; Expressed in esophagus and 254 other cell types or tissues.
DR ExpressionAtlas; Q99NH2; baseline and differential.
DR Genevisible; Q99NH2; MM.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0044295; C:axonal growth cone; ISO:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0033269; C:internode region of axon; IDA:UniProtKB.
DR GO; GO:0043219; C:lateral loop; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0120157; C:PAR polarity complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:BHF-UCL.
DR GO; GO:0005819; C:spindle; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0003383; P:apical constriction; IGI:MGI.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IC:MGI.
DR GO; GO:0051642; P:centrosome localization; IMP:MGI.
DR GO; GO:0030010; P:establishment of cell polarity; IBA:GO_Central.
DR GO; GO:0051660; P:establishment of centrosome localization; IBA:GO_Central.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; ISS:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:UniProtKB.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; ISO:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0022011; P:myelination in peripheral nervous system; IMP:UniProtKB.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IMP:UniProtKB.
DR GO; GO:0031643; P:positive regulation of myelination; IMP:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IMP:CACAO.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0032970; P:regulation of actin filament-based process; IGI:MGI.
DR GO; GO:0060341; P:regulation of cellular localization; ISO:MGI.
DR GO; GO:0044319; P:wound healing, spreading of cells; IMP:MGI.
DR CDD; cd00992; PDZ_signaling; 3.
DR Gene3D; 2.30.42.10; -; 3.
DR InterPro; IPR021922; Par3/HAL_N.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR16484:SF10; PARTITIONING DEFECTIVE 3 HOMOLOG; 1.
DR PANTHER; PTHR16484; PARTITIONING DEFECTIVE 3 RELATED; 1.
DR Pfam; PF12053; Par3_HAL_N_term; 1.
DR Pfam; PF00595; PDZ; 3.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF50156; PDZ domain-like; 3.
DR PROSITE; PS50106; PDZ; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Cell junction; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Differentiation; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Tight junction.
FT CHAIN 1..1333
FT /note="Partitioning defective 3 homolog"
FT /id="PRO_0000185070"
FT DOMAIN 271..359
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 461..546
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 590..677
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 143..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..936
FT /note="Interaction with PRKCI and PRKCZ"
FT /evidence="ECO:0000250"
FT REGION 712..932
FT /note="Interaction with PRKCI and PRKCZ"
FT /evidence="ECO:0000250|UniProtKB:Q9Z340"
FT REGION 861..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..1333
FT /note="Interaction with FRMD4A"
FT /evidence="ECO:0000269|PubMed:20080746"
FT REGION 1024..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1046..1078
FT /evidence="ECO:0000255"
FT COILED 1145..1168
FT /evidence="ECO:0000255"
FT COILED 1195..1218
FT /evidence="ECO:0000255"
FT COILED 1274..1295
FT /evidence="ECO:0000255"
FT COMPBIAS 146..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 489
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 831
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:21949390"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 848
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:21949390"
FT MOD_RES 849
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 881
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:21949390"
FT MOD_RES 958
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 967
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 969
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 1327
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:21949390"
FT VAR_SEQ 1..135
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15766746"
FT /id="VSP_035895"
FT VAR_SEQ 741..744
FT /note="KCQL -> ESGT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10934475,
FT ECO:0000303|PubMed:9920925"
FT /id="VSP_007472"
FT VAR_SEQ 741
FT /note="K -> T (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15766746"
FT /id="VSP_035896"
FT VAR_SEQ 742..1333
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15766746"
FT /id="VSP_035897"
FT VAR_SEQ 745..1333
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10934475,
FT ECO:0000303|PubMed:9920925"
FT /id="VSP_007473"
FT VAR_SEQ 1021..1030
FT /note="RFGKHRKDDK -> SLAKLKPEKR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15766746"
FT /id="VSP_035898"
FT VAR_SEQ 1030..1333
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10934475"
FT /id="VSP_007474"
FT VAR_SEQ 1031..1333
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15766746"
FT /id="VSP_035899"
FT MUTAGEN 824..826
FT /note="SMS->AMA,EME: Strongly reduces phosphorylation by
FT PRKCZ and abolishes interaction with PKRCI."
FT /evidence="ECO:0000269|PubMed:10934475"
FT MUTAGEN 831
FT /note="K->A: Inhibits Schwann cell peripheral myelination;
FT when associated with A-848; A-881 and A-1327."
FT /evidence="ECO:0000269|PubMed:21949390"
FT MUTAGEN 848
FT /note="K->A: Inhibits Schwann cell peripheral myelination;
FT when associated with A-831; A-881 and A-1327."
FT /evidence="ECO:0000269|PubMed:21949390"
FT MUTAGEN 881
FT /note="K->A: Inhibits Schwann cell peripheral myelination;
FT when associated with A-831; A-848 and A-1327."
FT /evidence="ECO:0000269|PubMed:21949390"
FT MUTAGEN 1327
FT /note="K->A: Inhibits Schwann cell peripheral myelination;
FT when associated with A-831; A-848 and A-881."
FT /evidence="ECO:0000269|PubMed:21949390"
FT CONFLICT 477
FT /note="S -> C (in Ref. 4; BAC29670)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="V -> GI (in Ref. 3; AAX48909)"
FT /evidence="ECO:0000305"
FT CONFLICT 1009
FT /note="K -> N (in Ref. 2; AAK07669)"
FT /evidence="ECO:0000305"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:2KOJ"
FT STRAND 458..465
FT /evidence="ECO:0007829|PDB:2KOJ"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:2KOJ"
FT STRAND 481..486
FT /evidence="ECO:0007829|PDB:2KOJ"
FT STRAND 488..493
FT /evidence="ECO:0007829|PDB:2KOJ"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:2KOJ"
FT HELIX 498..502
FT /evidence="ECO:0007829|PDB:2KOJ"
FT STRAND 510..514
FT /evidence="ECO:0007829|PDB:2KOJ"
FT HELIX 524..533
FT /evidence="ECO:0007829|PDB:2KOJ"
FT STRAND 537..546
FT /evidence="ECO:0007829|PDB:2KOJ"
FT STRAND 584..595
FT /evidence="ECO:0007829|PDB:2KOH"
FT STRAND 597..610
FT /evidence="ECO:0007829|PDB:2KOH"
FT TURN 611..614
FT /evidence="ECO:0007829|PDB:2KOH"
FT STRAND 615..624
FT /evidence="ECO:0007829|PDB:2KOH"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:2KOH"
FT HELIX 629..632
FT /evidence="ECO:0007829|PDB:2KOH"
FT STRAND 641..645
FT /evidence="ECO:0007829|PDB:2KOH"
FT HELIX 655..668
FT /evidence="ECO:0007829|PDB:2KOH"
FT HELIX 670..673
FT /evidence="ECO:0007829|PDB:2KOH"
FT STRAND 674..683
FT /evidence="ECO:0007829|PDB:2KOH"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:2KOH"
SQ SEQUENCE 1333 AA; 149075 MW; 1DD680EE824C3837 CRC64;
MKVTVCFGRT RVVVPCGDGR MKVFSLIQQA VTRYRKAVAK DPNYWIQVHR LEHGDGGILD
LDDILCDVAD DKDRLVAVFD EQDPHHGGDG TSASFTGTQS PEIFGSELGT NNVSAFQPYQ
ATSEIEVTPS VLRANMPLHV RRSSDPALTG LSTSVSDNNF SSEEPSRKNP TRWSTTAGFL
KQNTAGSPKT CDRKKDENYR SLPRDPSSWS NQFQRDNARS SLSASHPMVD RWLEKQEQDE
EGTEEDSSRV EPVGHADTGL ENMPNFSLDD MVKLVQVPND GGPLGIHVVP FSARGGRTLG
LLVKRLEKGG KAEQENLFHE NDCIVRINDG DLRNRRFEQA QHMFRQAMRA RVIWFHVVPA
ANKEQYEQLS QREKNNYSPG RFSPDSHCVA NRSVANNAPQ ALPRAPRLSQ PPEQLDAHPR
LPHSAHASTK PPAAPALAPP SVLSTNVGSV YNTKKVGKRL NIQLKKGTEG LGFSITSRDV
TIGGSAPIYV KNILPRGAAI QDGRLKAGDR LIEVNGVDLA GKSQEEVVSL LRSTKMEGTV
SLLVFRQEEA FHPREMNAEP SQMQTPKETK AEDEDVVLTP DGTREFLTFE VPLNDSGSAG
LGVSVKGNRS KENHADLGIF VKSIINGGAA SKDGRLRVND QLIAVNGESL LGKANQEAME
TLRRSMSTEG NKRGMIQLIV ARRISRCNEL RSPGSPAAPE LPIETELDDR ERRISHSLYS
GIEGLDESPT RNAALSRIMG KCQLSPTVNM PHDDTVMIED DRLPVLPPHL SDQSSSSSHD
DVGFIMTEAG TWAKATISDS ADCSLSPDVD PVLAFQREGF GRQSMSEKRT KQFSDASQLD
FVKTRKSKSM DLVADETKLN TVDDQRAGSP SRDVGPSLGL KKSSSLESLQ TAVAEVTLNG
NIPFHRPRPR IIRGRGCNES FRAAIDKSYD KPMVDDDDEG METLEEDTEE SSRSGRESVS
TSSDQPSYSL ERQMNGDPEK RDKTERKKDK AGKDKKKDRE KEKDKLKAKK GMLKGLGDMF
RFGKHRKDDK MEKMGRIKIQ DSFTSEEDRV RMKEEQERIQ AKTREFRERQ ARERDYAEIQ
DFHRTFGCDD ELLYGGMSSY EGCLALNARP QSPREGHLMD TLYAQVKKPR SSKPGDSNRS
TPSNHDRIQR LRQEFQQAKQ DEDVEDRRRT YSFEQSWSSS RPASQSGRHS VSVEVQVQRQ
RQEERESFQQ AQRQYSSLPR QSRKNASSIS QDSWEQNYAP GEGFQSAKEN PRYSSYQGSR
NGYLGGHGFN ARVMLETQEL LRQEQRRKEQ QLKKQPPADG VRGPFRQDVP PSPSQVARLN
RLQTPEKGRP FYS
//
