PAR3_CAEEL
ID PAR3_CAEEL Reviewed; 1379 AA.
AC Q17353; Q27GV0; Q95QE9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Partitioning defective protein 3;
DE AltName: Full=Abnormal embryonic partitioning of cytoplasm protein 3;
GN Name=par-3 {ECO:0000312|EMBL:AAB18670.1}; ORFNames=F54E7.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB18670.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:8521491};
RC TISSUE=Embryo {ECO:0000269|PubMed:8521491};
RX PubMed=8521491; DOI=10.1016/0092-8674(95)90187-6;
RA Etemad-Moghadam B., Guo S., Kemphues K.J.;
RT "Asymmetrically distributed PAR-3 protein contributes to cell polarity and
RT spindle alignment in early C. elegans embryos.";
RL Cell 83:743-752(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH PAR-6.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:8898226};
RX PubMed=8898226; DOI=10.1242/dev.122.10.3133;
RA Watts J.L., Etemad-Moghadam B., Guo S., Boyd L., Draper B.W., Mello C.C.,
RA Priess J.R., Kemphues K.J.;
RT "par-6, a gene involved in the establishment of asymmetry in early C.
RT elegans embryos, mediates the asymmetric localization of PAR-3.";
RL Development 122:3133-3140(1996).
RN [4] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH PKC-3.
RX PubMed=9716526; DOI=10.1242/dev.125.18.3607;
RA Tabuse Y., Izumi Y., Piano F., Kemphues K.J., Miwa J., Ohno S.;
RT "Atypical protein kinase C cooperates with PAR-3 to establish embryonic
RT polarity in Caenorhabditis elegans.";
RL Development 125:3607-3614(1998).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PAR-6 AND PKC-3, AND TISSUE SPECIFICITY.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:9834192};
RX PubMed=9834192; DOI=10.1242/dev.126.1.127;
RA Hung T.-J., Kemphues K.J.;
RT "PAR-6 is a conserved PDZ domain-containing protein that colocalizes with
RT PAR-3 in Caenorhabditis elegans embryos.";
RL Development 126:127-135(1999).
RN [6] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=13129846; DOI=10.1242/dev.00735;
RA Nance J., Munro E.M., Priess J.R.;
RT "C. elegans PAR-3 and PAR-6 are required for apicobasal asymmetries
RT associated with cell adhesion and gastrulation.";
RL Development 130:5339-5350(2003).
RN [7]
RP FUNCTION.
RX PubMed=14534135; DOI=10.1242/dev.00790;
RA Tsou M.-F.B., Hayashi A., Rose L.S.;
RT "LET-99 opposes Galpha/GPR signaling to generate asymmetry for spindle
RT positioning in response to PAR and MES-1/SRC-1 signaling.";
RL Development 130:5717-5730(2003).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15151982; DOI=10.1242/dev.01146;
RA Aono S., Legouis R., Hoose W.A., Kemphues K.J.;
RT "PAR-3 is required for epithelial cell polarity in the distal spermatheca
RT of C. elegans.";
RL Development 131:2865-2874(2004).
RN [9]
RP FUNCTION.
RX PubMed=18694560; DOI=10.1016/j.devcel.2008.06.002;
RA Panbianco C., Weinkove D., Zanin E., Jones D., Divecha N., Gotta M.,
RA Ahringer J.;
RT "A casein kinase 1 and PAR proteins regulate asymmetry of a PIP(2)
RT synthesis enzyme for asymmetric spindle positioning.";
RL Dev. Cell 15:198-208(2008).
CC -!- FUNCTION: In cooperation with pkc-3, required for establishing cell
CC polarity and regulating spindle orientation in the early embryo
CC (PubMed:8521491, PubMed:9716526). Localization is crucial for
CC recruiting par-6 and pkc-3 to the peripheral apical cortex and
CC restricting par-2 to basolateral surfaces (PubMed:8898226,
CC PubMed:9834192). Necessary for apicobasal and anterior-posterior
CC asymmetries associated with cell adhesion and gastrulation during the
CC first few cycles of embryogenesis, and also for epithelial cell
CC polarity in the distal spermatheca (PubMed:13129846, PubMed:15151982).
CC Regulates the asymmetric localization of csnk-1, ppk-1 and gpr-1/2
CC during the first embryonic division (PubMed:14534135, PubMed:18694560).
CC {ECO:0000269|PubMed:13129846, ECO:0000269|PubMed:14534135,
CC ECO:0000269|PubMed:15151982, ECO:0000269|PubMed:18694560,
CC ECO:0000269|PubMed:8521491, ECO:0000269|PubMed:8898226,
CC ECO:0000269|PubMed:9716526, ECO:0000269|PubMed:9834192}.
CC -!- SUBUNIT: Required, together with pkc-3, for the localization of par-6;
CC par-6 is involved in localizing/maintaining par-3 at the cell
CC periphery. Interacts with par-6 and pkc-3 for localization at the
CC periphery of anterior cortex of the embryo.
CC {ECO:0000269|PubMed:8898226, ECO:0000269|PubMed:9716526,
CC ECO:0000269|PubMed:9834192}.
CC -!- INTERACTION:
CC Q17353; Q19266: pkc-3; NbExp=3; IntAct=EBI-321762, EBI-319158;
CC Q17353-2; Q09248: dnc-2; NbExp=3; IntAct=EBI-11467668, EBI-316282;
CC Q17353-3; O16502: abu-7; NbExp=2; IntAct=EBI-1812329, EBI-328492;
CC Q17353-3; H2L055: CELE_F53A10.2; NbExp=2; IntAct=EBI-1812329, EBI-2413872;
CC Q17353-3; Q22387: CELE_T11B7.1; NbExp=3; IntAct=EBI-1812329, EBI-320525;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8521491}.
CC Note=Cytoplasmic and cell periphery.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000269|PubMed:8521491};
CC IsoId=Q17353-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q17353-2; Sequence=VSP_051597;
CC Name=c;
CC IsoId=Q17353-3; Sequence=VSP_034689, VSP_051597;
CC -!- TISSUE SPECIFICITY: Asymmetrically distributed at the periphery of the
CC zygote and in dividing blastomeres of the germline lineage. Coexpressed
CC with par-6; patchy expression observed at the periphery after
CC completion of meiosis I and in meiosis II. On completion of metaphase
CC II, expression is restricted to the anterior 85% of embryo length; this
CC decreases to 55% in embryos between prophase and telophase of the first
CC mitosis. During the first cleavage, expression is detected in the
CC advancing furrow. Transiently coexpressed and colocalized
CC asymmetrically with par-6 and pkc-3, in the developing somatic gonad,
CC including the spermathecal precursor cells of L4 larvae.
CC {ECO:0000269|PubMed:13129846, ECO:0000269|PubMed:15151982,
CC ECO:0000269|PubMed:8521491, ECO:0000269|PubMed:9834192}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:8521491}.
CC -!- SIMILARITY: Belongs to the PAR3 family. {ECO:0000269|PubMed:8521491}.
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DR EMBL; U25032; AAB18670.1; -; mRNA.
DR EMBL; FO080172; CCD61764.1; -; Genomic_DNA.
DR EMBL; FO080172; CCD61765.1; -; Genomic_DNA.
DR EMBL; FO080172; CCD61766.1; -; Genomic_DNA.
DR RefSeq; NP_001022607.1; NM_001027436.2. [Q17353-1]
DR RefSeq; NP_001040857.1; NM_001047392.1.
DR RefSeq; NP_498217.2; NM_065816.6.
DR AlphaFoldDB; Q17353; -.
DR SMR; Q17353; -.
DR BioGRID; 41010; 28.
DR DIP; DIP-25317N; -.
DR IntAct; Q17353; 55.
DR STRING; 6239.F54E7.3i; -.
DR iPTMnet; Q17353; -.
DR EPD; Q17353; -.
DR PaxDb; Q17353; -.
DR PeptideAtlas; Q17353; -.
DR EnsemblMetazoa; F54E7.3a.1; F54E7.3a.1; WBGene00003918. [Q17353-2]
DR EnsemblMetazoa; F54E7.3b.1; F54E7.3b.1; WBGene00003918. [Q17353-1]
DR EnsemblMetazoa; F54E7.3b.2; F54E7.3b.2; WBGene00003918. [Q17353-1]
DR EnsemblMetazoa; F54E7.3b.3; F54E7.3b.3; WBGene00003918. [Q17353-1]
DR EnsemblMetazoa; F54E7.3c.1; F54E7.3c.1; WBGene00003918. [Q17353-3]
DR EnsemblMetazoa; F54E7.3c.2; F54E7.3c.2; WBGene00003918. [Q17353-3]
DR GeneID; 175783; -.
DR UCSC; F54E7.3b; c. elegans.
DR CTD; 175783; -.
DR WormBase; F54E7.3a; CE28449; WBGene00003918; par-3. [Q17353-2]
DR WormBase; F54E7.3b; CE28450; WBGene00003918; par-3. [Q17353-1]
DR WormBase; F54E7.3c; CE39941; WBGene00003918; par-3. [Q17353-3]
DR eggNOG; KOG3528; Eukaryota.
DR InParanoid; Q17353; -.
DR PhylomeDB; Q17353; -.
DR SignaLink; Q17353; -.
DR PRO; PR:Q17353; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003918; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q17353; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0061802; C:anterior cell cortex; IDA:UniProtKB.
DR GO; GO:0045179; C:apical cortex; IDA:WormBase.
DR GO; GO:0043296; C:apical junction complex; IBA:GO_Central.
DR GO; GO:0045177; C:apical part of cell; IDA:WormBase.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0045178; C:basal part of cell; IDA:WormBase.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0043186; C:P granule; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0008356; P:asymmetric cell division; IMP:WormBase.
DR GO; GO:0007155; P:cell adhesion; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:WormBase.
DR GO; GO:0051660; P:establishment of centrosome localization; IBA:GO_Central.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IGI:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:WormBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IGI:UniProtKB.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0007369; P:gastrulation; IMP:UniProtKB.
DR GO; GO:0008406; P:gonad development; IMP:UniProtKB.
DR GO; GO:0007506; P:gonadal mesoderm development; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0009949; P:polarity specification of anterior/posterior axis; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 3.
DR InterPro; IPR021922; Par3/HAL_N.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF12053; Par3_HAL_N_term; 1.
DR Pfam; PF00595; PDZ; 3.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF50156; SSF50156; 3.
DR PROSITE; PS50106; PDZ; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Developmental protein; Differentiation;
KW Fertilization; Gastrulation; Gonadal differentiation; Reference proteome;
KW Repeat.
FT CHAIN 1..1379
FT /note="Partitioning defective protein 3"
FT /id="PRO_0000185074"
FT DOMAIN 381..483
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 515..599
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 659..750
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 606..626
FT /evidence="ECO:0000255"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..107
FT /note="MSASSTSSSSTSCPEGGEPSGSCKSSDEGESTLKKRMQQYGIASGYANSSIS
FT TLDRSQYQSLPLNGTRRVTVQFGRMKIVVPWKESDQTVGQLADAALLRYKKARGM ->
FT MHNGRGGRYDVCPPPPPPPYHFNHVHTPPSKVIVQQQKQQQKAHREPPPSYPASKMTTT
FT NDNVTVSKRNFQ (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_034689"
FT VAR_SEQ 1017..1019
FT /note="Missing (in isoform a and isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_051597"
SQ SEQUENCE 1379 AA; 149326 MW; 3B498E7652CFF17D CRC64;
MSASSTSSSS TSCPEGGEPS GSCKSSDEGE STLKKRMQQY GIASGYANSS ISTLDRSQYQ
SLPLNGTRRV TVQFGRMKIV VPWKESDQTV GQLADAALLR YKKARGMANE DRIHVHRLEC
ASDGGILDMD DVLEEVFDLN YDQILAITDE ANGGSTTPTY SQIQKQQHHY AQPLPYARKF
DGGPSTPIAS AFGSVTVNHQ AHRAASPYNV GFARSNSRDF APQPTHSKER RDSVVEVSSF
DQIPQSGLRV STPKPSRQSE DVIDGKPMNQ PILRSSLRTE ASGSRTEEAT PVKQSRVTLS
PEVEKKLAEQ DERKSERRKH YDKNPGRFAR GSDRKSRITD ALLDARDRIA DQLESQNPAE
ETKSQMIRVK IDQGPMPGTS LVTFPPIPEK SENEKQLGIE VNAVFDESSE LPGTSEPTKL
SSVQIMKIED GGRIAKDGRI RVGDCIVAID GKPVDQMSII RVRASISDLA AVTSRPVTLI
INRSLESFLE QESSAKPIQS ALQQANTQYI GHTTVVELIK SSNGFGFTVT GRETAKGERL
FYIGTVKPYG VALGHLKSGD RLLEINGTPT GQWTQSEIVE KLKETMVGEK IKFLVSRVSQ
SAIMSTSASS ENKENEETLK VVEEEKIPQK LPLPALMTPP VPKDTPALSP SGASRFEIVI
PFINGSSSAG LGVSLKARVS KKSNGSKVDC GIFIKNVMHG GAAFKEGGLR VDDRIVGVED
IDLEPLDNRE AQAALAKKLK EVGMISSNVR LTISRYNECN PGQISRDLSR ITVDASSPSP
SSRMSSHTAP DSLLPSPATR GTSSSGADSS HSRQSSASSA VPAVPARLTE RDSIVSDGTS
RNDESELPDS ADPFNREGLG RKSLSEKRGM GAAADPQHIK LFQDIKHQRQ NSAPTSSTQK
RSKSQPRSSS QRNYRSPMKL VDLPTTAAAS ASTNSQNLDD SDMLNRRSQS MESINRPVES
ILRGTGQIPT GSSSKVQFMQ AASPDQHPFP PGAALLRLKN EESRSRDKSR RKSMGNPFSA
MRNFFGFGSK SRDASPEKTP TESVQLRSVE RPKSIIDERN NGSSERAPPP LPPHQSQRRG
SGGNVFVDYG EPYGLIPQYP HNTTSGYESY ADSELYDRYA AHRYHPRGGP IIDEDEYIYR
QQSTSGNSPI NTSSYVNYGL PASNAYHVGS RIPPQTSSGS ISKTSGAMRR VYPAEYDEDV
AYHQQIPQQS TRYQQGSGSG RGNADYHHMF NSWFAYTGGG AVGAAPVIKS SYGSSPVRIA
AASAIERGES FVVEPVSGSS ASATDRRGRS TSSGAVASGS SSTGFQYAAK EKYADARSGK
FNGGSTRLFI PRHGGGLSAA AFATNFGGEA YETRGGGAGG SPSQYRRRDQ GPPHRFPQY
