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Database: UniProt
Entry: PAR3_CAEEL
LinkDB: PAR3_CAEEL
Original site: 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   24-JAN-2024, entry version 172.
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; 30.
DR   DIP; DIP-25317N; -.
DR   IntAct; Q17353; 55.
DR   STRING; 6239.F54E7.3i.1; -.
DR   iPTMnet; Q17353; -.
DR   EPD; Q17353; -.
DR   PaxDb; 6239-F54E7-3i; -.
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   AGR; WB:WBGene00003918; -.
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 cell types or 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:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:GO_Central.
DR   GO; GO:0016020; C: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   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:SF17; BAZOOKA, ISOFORM B; 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   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
//
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