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Protein

Partitioning defective 3 homolog

Gene

Pard3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adapter protein involved in asymmetrical cell division and cell polarization processes. Seems to play a central role in the formation of epithelial tight junctions. Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons (By similarity). Involved in Schwann cell peripheral myelination. Targets the phosphatase PTEN to cell junctions.By similarity3 Publications

GO - Molecular functioni

  • phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
  • phosphatidylinositol-3-phosphate binding Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB

GO - Biological processi

  • bicellular tight junction assembly Source: UniProtKB
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • establishment of epithelial cell polarity Source: UniProtKB
  • establishment or maintenance of epithelial cell apical/basal polarity Source: RGD
  • myelination in peripheral nervous system Source: UniProtKB
  • negative regulation of peptidyl-threonine phosphorylation Source: UniProtKB
  • positive regulation of myelination Source: UniProtKB
  • protein targeting to membrane Source: UniProtKB
  • regulation of cellular localization Source: RGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Differentiation

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-RNO-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-RNO-420029. Tight junction interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Partitioning defective 3 homolog
Short name:
PAR-3
Short name:
PARD-3
Alternative name(s):
Atypical PKC isotype-specific-interacting protein
Short name:
ASIP
Atypical PKC-specific-binding protein
Short name:
ASBP
Gene namesi
Name:Pard3
Synonyms:Par3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi620374. Pard3.

Subcellular locationi

GO - Cellular componenti

  • axonal growth cone Source: RGD
  • bicellular tight junction Source: UniProtKB
  • cell-cell junction Source: UniProtKB
  • cell cortex Source: UniProtKB-SubCell
  • cytoskeleton Source: UniProtKB-SubCell
  • endomembrane system Source: UniProtKB-SubCell
  • internode region of axon Source: UniProtKB
  • neuronal cell body Source: RGD
  • plasma membrane Source: UniProtKB-SubCell
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Tight junction

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi458K → E: Reduces binding to membranes containing phosphoinositol lipids by half. Abolishes binding to membranes containing phosphoinositol lipids; when associated with E-546. 1 Publication1
Mutagenesisi491K → A: Slightly reduced binding to membranes containing phosphoinositol lipids. 1 Publication1
Mutagenesisi491K → E: Strongly reduced binding to membranes containing phosphoinositol lipids. 1 Publication1
Mutagenesisi504R → A: Slightly reduced binding to membranes containing phosphoinositol lipids; when associated with A-506. 1 Publication1
Mutagenesisi504R → E: Abolishes binding to membranes containing phosphoinositol lipids; when associated with E-506. 1 Publication1
Mutagenesisi506K → A: Slightly reduced binding to membranes containing phosphoinositol lipids; when associated with A-504. 1 Publication1
Mutagenesisi506K → E: Abolishes binding to membranes containing phosphoinositol lipids; when associated with E-504. 1 Publication1
Mutagenesisi532R → A: Reduces binding to membranes containing phosphoinositol lipids by half; when associated with A-535. 1 Publication1
Mutagenesisi532R → E: Almost abolished binding to membranes containing phosphoinositol lipids; when associated with E-535. 1 Publication1
Mutagenesisi535K → A: Reduces binding to membranes containing phosphoinositol lipids by half; when associated with A-532. 1 Publication1
Mutagenesisi535K → E: Almost abolished binding to membranes containing phosphoinositol lipids; when associated with E-532. 1 Publication1
Mutagenesisi546R → E: Abolishes binding to membranes containing phosphoinositol lipids; when associated with E-458. 1 Publication1
Mutagenesisi827S → E: Abolishes binding to PKCI. 1 Publication1
Mutagenesisi829S → A: No detectable impact on binding to PKCI. 1 Publication1
Mutagenesisi829S → E: Abolishes binding to PKCI. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001850711 – 1337Partitioning defective 3 homologAdd BLAST1337

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25PhosphoserineBy similarity1
Modified residuei91PhosphothreonineBy similarity1
Modified residuei156PhosphoserineBy similarity1
Modified residuei174PhosphoserineCombined sources1
Modified residuei383PhosphoserineBy similarity1
Modified residuei489PhosphotyrosineBy similarity1
Modified residuei692PhosphoserineBy similarity1
Modified residuei695PhosphoserineBy similarity1
Modified residuei715PhosphoserineBy similarity1
Modified residuei728PhosphoserineBy similarity1
Modified residuei809PhosphoserineBy similarity1
Modified residuei827Phosphoserine2 Publications1
Modified residuei834N6-acetyllysineBy similarity1
Modified residuei837PhosphoserineBy similarity1
Modified residuei851N6-acetyllysineBy similarity1
Modified residuei852PhosphoserineCombined sources1
Modified residuei873PhosphoserineBy similarity1
Modified residuei885N6-acetyllysineBy similarity1
Modified residuei962Phosphoserine; by AURKABy similarity1
Modified residuei971PhosphoserineBy similarity1
Modified residuei973PhosphoserineBy similarity1
Modified residuei1046PhosphoserineBy similarity1
Modified residuei1331N6-acetyllysineBy similarity1

Post-translational modificationi

Acetylated. Deacetylated by SIRT2, thereby inhibiting Schwann cell peripheral myelination.1 Publication
Phosphorylation at Ser-827 by PRKCZ and PRKCI occurs at the most apical tip of epithelial cell-cell contacts during the initial phase of tight junction formation and may promote dissociation of the complex with PARD6. EGF-induced Tyr-1127 phosphorylation mediates dissociation from LIMK2 (By similarity). Phosphorylation by AURKA at Ser-962 is required for the normal establishment of neuronal polarity (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9Z340.
PRIDEiQ9Z340.

PTM databases

iPTMnetiQ9Z340.
PhosphoSitePlusiQ9Z340.

Expressioni

Tissue specificityi

Isoform 1 is predominantly expressed in lung, glandular stomach, prostate, ovary and uterus. Isoform 1 is also expressed in brain, with a high expression in the cortex, hippocampus and in the striatum. Isoform 2 is predominantly expressed in intestinal epithelial cells, kidney and prostate.

Gene expression databases

BgeeiENSRNOG00000032437.
ExpressionAtlasiQ9Z340. baseline and differential.
GenevisibleiQ9Z340. RN.

Interactioni

Subunit structurei

Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, PATJ and PARD3/PAR3. Interacts (via PDZ 1 domain) with PARD6A, PARD6B and F11R/JAM1. Interacts with AURKA, AURKB and SIRT2 (By similarity). Interacts with PRKCI. Interacts with PRKCZ (Probable). Part of a complex with PARD6A or PARD6B, PRKCI or PRKCZ and CDC42 or RAC1. Interacts with LIMK2 and CDH5. Component of the Par polarity complex, composed of at least phosphorylated PRKCZ, PARD3 and TIAM1. Directly interacts with TIAM1 and TIAM2. Interacts with ECT2 and FBF1 (By similarity). Interacts (via PDZ 3 domain) with PTEN (via C-terminus).By similarityCurated4 Publications

GO - Molecular functioni

  • protein phosphatase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi249693. 2 interactors.
DIPiDIP-33271N.
IntActiQ9Z340. 2 interactors.
MINTiMINT-204258.
STRINGi10116.ENSRNOP00000048964.

Structurei

Secondary structure

11337
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Beta strandi10 – 17Combined sources8
Helixi23 – 38Combined sources16
Beta strandi46 – 52Combined sources7
Beta strandi54 – 56Combined sources3
Helixi65 – 68Combined sources4
Beta strandi74 – 81Combined sources8
Beta strandi458 – 465Combined sources8
Beta strandi472 – 477Combined sources6
Beta strandi481 – 484Combined sources4
Beta strandi488 – 493Combined sources6
Beta strandi495 – 497Combined sources3
Helixi498 – 502Combined sources5
Beta strandi507 – 514Combined sources8
Beta strandi520 – 522Combined sources3
Helixi524 – 533Combined sources10
Beta strandi539 – 546Combined sources8
Beta strandi583 – 591Combined sources9
Turni594 – 599Combined sources6
Beta strandi600 – 609Combined sources10
Beta strandi611 – 614Combined sources4
Beta strandi616 – 624Combined sources9
Helixi629 – 633Combined sources5
Beta strandi641 – 645Combined sources5
Beta strandi648 – 653Combined sources6
Helixi655 – 668Combined sources14
Beta strandi672 – 674Combined sources3
Beta strandi676 – 684Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K1ZNMR-A582-685[»]
2K20NMR-A582-685[»]
2NS5NMR-A2-83[»]
2OGPNMR-A454-550[»]
3ZEEelectron microscopy6.10A2-82[»]
4DC2X-ray2.40Z813-840[»]
4I6PX-ray2.90A/B2-83[»]
ProteinModelPortaliQ9Z340.
SMRiQ9Z340.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Z340.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini271 – 359PDZ 1PROSITE-ProRule annotationAdd BLAST89
Domaini461 – 546PDZ 2PROSITE-ProRule annotationAdd BLAST86
Domaini590 – 677PDZ 3PROSITE-ProRule annotationAdd BLAST88

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni712 – 936Interaction with PRKCI and PRKCZ1 PublicationAdd BLAST225

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1050 – 1082Sequence analysisAdd BLAST33
Coiled coili1149 – 1172Sequence analysisAdd BLAST24
Coiled coili1199 – 1222Sequence analysisAdd BLAST24
Coiled coili1278 – 1299Sequence analysisAdd BLAST22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi984 – 1042Lys-richAdd BLAST59

Domaini

Contains a conserved N-terminal oligomerization domain (NTD) that is involved in oligomerization and is essential for proper subapical membrane localization.
The second PDZ domain mediates interaction with membranes containing phosphoinositol lipids.

Sequence similaritiesi

Belongs to the PAR3 family.Curated
Contains 3 PDZ (DHR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG3528. Eukaryota.
ENOG4110362. LUCA.
GeneTreeiENSGT00760000119017.
HOGENOMiHOG000232109.
HOVERGENiHBG053508.
InParanoidiQ9Z340.
KOiK04237.
OMAiFQRDNAR.
OrthoDBiEOG091G04AU.
PhylomeDBiQ9Z340.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
InterProiIPR021922. DUF3534.
IPR001478. PDZ.
[Graphical view]
PfamiPF12053. DUF3534. 1 hit.
PF00595. PDZ. 2 hits.
[Graphical view]
SMARTiSM00228. PDZ. 3 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 3 hits.
PROSITEiPS50106. PDZ. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Z340-1) [UniParc]FASTAAdd to basket
Also known as: 180 kDa

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKVTVCFGRT RVVVPCGDGR MKVFSLIQQA VTRYRKAVAK DPNYWIQVHR
60 70 80 90 100
LEHGDGGILD LDDILCDVAD DKDRLVAVFD EQDPHHGGDG TSASSTGTQS
110 120 130 140 150
PEIFGSELGT NNVSAFRPYQ TTSEIEVTPS VLRANMPLHV RRSSDPALTG
160 170 180 190 200
LSTSVSDNNF SSEEPSRKNP TRWSTTAGFL KQNTTGSPKT CDRKKDENYR
210 220 230 240 250
SLPRDPSSWS NQFQRDNARS SLSASHPMVD RWLEKQEQDE EGTEEDSSRV
260 270 280 290 300
EPVGHADTGL ENMPNFSLDD MVKLVQVPND GGPLGIHVVP FSARGGRTLG
310 320 330 340 350
LLVKRLEKGG KAEQENLFHE NDCIVRINDG DLRNRRFEQA QHMFRQAMRA
360 370 380 390 400
RVIWFHVVPA ANKEQYEQLS QREMNNYSPG RFSPDSHCVA NRSVANNAPQ
410 420 430 440 450
ALPRAPRLSQ PPEQLDAHPR LPHSAHASTK PPTAPALAPP NVLSTSVGSV
460 470 480 490 500
YNTKRVGKRL NIQLKKGTEG LGFSITSRDV TIGGSAPIYV KNILPRGAAI
510 520 530 540 550
QDGRLKAGDR LIEVNGVDLA GKSQEEVVSL LRSTKMEGTV SLLVFRQEEA
560 570 580 590 600
FHPREMNAEP SQMQSPKETK AEDEDIVLTP DGTREFLTFE VPLNDSGSAG
610 620 630 640 650
LGVSVKGNRS KENHADLGIF VKSIINGGAA SKDGRLRVND QLIAVNGESL
660 670 680 690 700
LGKANQEAME TLRRSMSTEG NKRGMIQLIV ARRISRCNEL RSPGSPAAPE
710 720 730 740 750
LPIETELDDR ERRISHSLYS GIEGLDESPT RNAALSRIMG ESGKCQLSPT
760 770 780 790 800
VNMPHDDTVM IEDDRLPVLP PHLSDQSSSS SHDDVGFIMT EAGTWAKATI
810 820 830 840 850
SDSADCSLSP DVDPVLAFQR EGFGRQSMSE KRTKQFSNAS QLDFVKTRKS
860 870 880 890 900
KSMDLGIADE TKLNTVDDQR AGSPNRDVGP SLGLKKSSSL ESLQTAVAEV
910 920 930 940 950
TLNGNIPFHR PRPRIIRGRG CNESFRAAID KSYDKPMVDD DDEGMETLEE
960 970 980 990 1000
DTEESSRSGR ESVSTSSDQP SYSLERQMNG DPEKRDKAEK KKDKAGKDKK
1010 1020 1030 1040 1050
KDREKEKDKL KAKKGMLKGL GDMFRFGKHR KDDKMEKMGR IKIQDSFTSE
1060 1070 1080 1090 1100
EDRVRMKEEQ ERIQAKTREF RERQARERDY AEIQDFHRTF GCDDELLYGG
1110 1120 1130 1140 1150
MSSYDGCLAL NARPQSPREG HLMDTLYAQV KKPRSSKPGD SNRSTPSNHD
1160 1170 1180 1190 1200
RIQRLRQEFQ QAKQDEDVED RRRTYSFEQS WSSSRPASQS GRHSVSVEVQ
1210 1220 1230 1240 1250
VQRQRQEERE SFQQAQRQYS SLPRQSRKNA SSVSQDSWEQ NYAPGEGFQS
1260 1270 1280 1290 1300
AKENPRYSSY QGSRNGYLGG HGFNARVMLE TQELLRQEQR RKEQQLKKQP
1310 1320 1330
PADGVRGPFR QDVPPSPSQV ARLNRLQTPE KGRPFYS
Length:1,337
Mass (Da):149,448
Last modified:May 1, 1999 - v1
Checksum:iEC980C5106B52F9C
GO
Isoform 2 (identifier: Q9Z340-2) [UniParc]FASTAAdd to basket
Also known as: 150 kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1034-1337: Missing.

Show »
Length:1,033
Mass (Da):113,906
Checksum:i0E010FC4F6E2B2C8
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0074751034 – 1337Missing in isoform 2. 1 PublicationAdd BLAST304

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005549 mRNA. Translation: BAA34216.1.
PIRiT13948.
RefSeqiNP_112514.1. NM_031235.1. [Q9Z340-1]
UniGeneiRn.31803.

Genome annotation databases

EnsembliENSRNOT00000042623; ENSRNOP00000048964; ENSRNOG00000032437. [Q9Z340-1]
GeneIDi81918.
KEGGirno:81918.
UCSCiRGD:620374. rat. [Q9Z340-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005549 mRNA. Translation: BAA34216.1.
PIRiT13948.
RefSeqiNP_112514.1. NM_031235.1. [Q9Z340-1]
UniGeneiRn.31803.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K1ZNMR-A582-685[»]
2K20NMR-A582-685[»]
2NS5NMR-A2-83[»]
2OGPNMR-A454-550[»]
3ZEEelectron microscopy6.10A2-82[»]
4DC2X-ray2.40Z813-840[»]
4I6PX-ray2.90A/B2-83[»]
ProteinModelPortaliQ9Z340.
SMRiQ9Z340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249693. 2 interactors.
DIPiDIP-33271N.
IntActiQ9Z340. 2 interactors.
MINTiMINT-204258.
STRINGi10116.ENSRNOP00000048964.

PTM databases

iPTMnetiQ9Z340.
PhosphoSitePlusiQ9Z340.

Proteomic databases

PaxDbiQ9Z340.
PRIDEiQ9Z340.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000042623; ENSRNOP00000048964; ENSRNOG00000032437. [Q9Z340-1]
GeneIDi81918.
KEGGirno:81918.
UCSCiRGD:620374. rat. [Q9Z340-1]

Organism-specific databases

CTDi56288.
RGDi620374. Pard3.

Phylogenomic databases

eggNOGiKOG3528. Eukaryota.
ENOG4110362. LUCA.
GeneTreeiENSGT00760000119017.
HOGENOMiHOG000232109.
HOVERGENiHBG053508.
InParanoidiQ9Z340.
KOiK04237.
OMAiFQRDNAR.
OrthoDBiEOG091G04AU.
PhylomeDBiQ9Z340.

Enzyme and pathway databases

ReactomeiR-RNO-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-RNO-420029. Tight junction interactions.

Miscellaneous databases

EvolutionaryTraceiQ9Z340.
PROiQ9Z340.

Gene expression databases

BgeeiENSRNOG00000032437.
ExpressionAtlasiQ9Z340. baseline and differential.
GenevisibleiQ9Z340. RN.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
InterProiIPR021922. DUF3534.
IPR001478. PDZ.
[Graphical view]
PfamiPF12053. DUF3534. 1 hit.
PF00595. PDZ. 2 hits.
[Graphical view]
SMARTiSM00228. PDZ. 3 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 3 hits.
PROSITEiPS50106. PDZ. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPARD3_RAT
AccessioniPrimary (citable) accession number: Q9Z340
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 1, 1999
Last modified: November 2, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.