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PAR6_CAEEL
ID   PAR6_CAEEL              Reviewed;         309 AA.
AC   Q9NAN2; Q1ZXS2; Q9XY93;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Partitioning defective protein 6;
GN   Name=par-6 {ECO:0000312|EMBL:CAB61018.2}; ORFNames=T26E3.3;
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:AAD15926.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:AAD15926.1};
RC   TISSUE=Embryo {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   [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, INTERACTION WITH PAR-3, AND DEVELOPMENTAL STAGE.
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]
RP   FUNCTION.
RX   PubMed=11003841; DOI=10.1242/dev.127.20.4419;
RA   Berkowitz L.A., Strome S.;
RT   "MES-1, a protein required for unequal divisions of the germline in early
RT   C. elegans embryos, resembles receptor tyrosine kinases and is localized to
RT   the boundary between the germline and gut cells.";
RL   Development 127:4419-4431(2000).
RN   [5]
RP   INTERACTION WITH CDC-42.
RC   STRAIN=Bristol N2 {ECO:0000269|PubMed:11412997};
RX   PubMed=11412997; DOI=10.1016/s0960-9822(01)00142-7;
RA   Gotta M., Abraham M.C., Ahringer J.;
RT   "CDC-42 controls early cell polarity and spindle orientation in C.
RT   elegans.";
RL   Curr. Biol. 11:482-488(2001).
RN   [6]
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, 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   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17115027; DOI=10.1038/ncb1511;
RA   Cowan C.R., Hyman A.A.;
RT   "Cyclin E-Cdk2 temporally regulates centrosome assembly and establishment
RT   of polarity in Caenorhabditis elegans embryos.";
RL   Nat. Cell Biol. 8:1441-1447(2006).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22634595; DOI=10.1038/ncb2508;
RA   Winter J.F., Hoepfner S., Korn K., Farnung B.O., Bradshaw C.R., Marsico G.,
RA   Volkmer M., Habermann B., Zerial M.;
RT   "Caenorhabditis elegans screen reveals role of PAR-5 in RAB-11-recycling
RT   endosome positioning and apicobasal cell polarity.";
RL   Nat. Cell Biol. 14:666-676(2012).
CC   -!- FUNCTION: Necessary for apicobasal and anterior-posterior asymmetries
CC       associated with cell adhesion and gastrulation during the first few
CC       cell cycles of embryogenesis (PubMed:8898226). Required for localizing/
CC       maintaining par-3 at the cell periphery (PubMed:9834192,
CC       PubMed:8898226). Regulates mes-1 expression and/or localization pattern
CC       during early embryogenesis (PubMed:11003841). Acts together with par-3
CC       and pkc-3 in maintaining epithelial cell polarity in the distal
CC       spermatheca (PubMed:13129846, PubMed:15151982). Plays a role in
CC       endosome and Golgi body positioning (PubMed:22634595).
CC       {ECO:0000269|PubMed:11003841, ECO:0000269|PubMed:13129846,
CC       ECO:0000269|PubMed:15151982, ECO:0000269|PubMed:22634595,
CC       ECO:0000269|PubMed:8898226, ECO:0000269|PubMed:9834192}.
CC   -!- SUBUNIT: Interacts with par-3, required for its peripheral
CC       localization, and with cdc-42, required for the activation of a par-
CC       3/par-6/pkc-3 complex. {ECO:0000269|PubMed:11412997,
CC       ECO:0000269|PubMed:8898226}.
CC   -!- INTERACTION:
CC       Q9NAN2; Q8MXV3: CELE_H06I04.1; NbExp=2; IntAct=EBI-318782, EBI-2422468;
CC       Q9NAN2; P34288-2: pac-1; NbExp=3; IntAct=EBI-318782, EBI-11465290;
CC       Q9NAN2; Q19266: pkc-3; NbExp=4; IntAct=EBI-318782, EBI-319158;
CC       Q9NAN2; Q20709: tra-4; NbExp=5; IntAct=EBI-318782, EBI-315012;
CC       Q9NAN2; Q9NEZ5: unc-95; NbExp=3; IntAct=EBI-318782, EBI-2913259;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9834192}. Cell
CC       membrane {ECO:0000269|PubMed:9834192}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:9834192}. Cell junction, tight junction
CC       {ECO:0000250}. Note=Membrane-associated at the periphery of blastomeres
CC       up to about the 50 cell stage. Peripheral expression is asymmetric in
CC       the cells of the germline lineage P0, P1, P2 and P3 (PubMed:9834192).
CC       Asymmetric distribution in the 1-cell embryo is regulated by the cye-
CC       1/cdk-2 complex (PubMed:17115027). {ECO:0000269|PubMed:17115027,
CC       ECO:0000269|PubMed:9834192}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a;
CC         IsoId=Q9NAN2-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=Q9NAN2-2; Sequence=VSP_034690;
CC   -!- TISSUE SPECIFICITY: Colocalized with par-3 at all stages in early
CC       embryos, at the anterior cortex of the embryo. Patchy expression
CC       observed at the periphery after completion of meiosis I and in meiosis
CC       II, which on completion of metaphase II, is restricted to the anterior
CC       85% of embryo length; this decreases to 55% in embryos between prophase
CC       and telophase of the first mitosis. During the first cleavage,
CC       expression is detected in the advancing furrow. Along with pkc-3, is
CC       unable to associate with the apical cortex of cells that lack par-3.
CC       Transiently coexpressed and colocalized with par-3 and pkc-3,
CC       asymmetrically in the developing somatic gonad, including the
CC       spermathecal precursor cells of L4 larvae.
CC       {ECO:0000269|PubMed:13129846, ECO:0000269|PubMed:15151982,
CC       ECO:0000269|PubMed:9834192}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       {ECO:0000269|PubMed:8898226}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in a diffuse
CC       distribution of early, recycling and late endosomes and Golgi bodies
CC       and reduced intensities of markers for these organelles.
CC       {ECO:0000269|PubMed:22634595}.
CC   -!- SIMILARITY: Belongs to the PAR6 family. {ECO:0000269|PubMed:9834192}.
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DR   EMBL; AF070968; AAD15926.1; -; mRNA.
DR   EMBL; Z82053; CAB61018.2; -; Genomic_DNA.
DR   EMBL; Z82053; CAJ85768.1; -; Genomic_DNA.
DR   PIR; T43216; T43216.
DR   RefSeq; NP_001040687.1; NM_001047222.4. [Q9NAN2-1]
DR   RefSeq; NP_001040688.1; NM_001047223.3. [Q9NAN2-2]
DR   AlphaFoldDB; Q9NAN2; -.
DR   SMR; Q9NAN2; -.
DR   BioGRID; 38534; 36.
DR   DIP; DIP-26707N; -.
DR   IntAct; Q9NAN2; 24.
DR   STRING; 6239.T26E3.3a.1; -.
DR   iPTMnet; Q9NAN2; -.
DR   EPD; Q9NAN2; -.
DR   PaxDb; Q9NAN2; -.
DR   PeptideAtlas; Q9NAN2; -.
DR   EnsemblMetazoa; T26E3.3a.1; T26E3.3a.1; WBGene00003921. [Q9NAN2-1]
DR   EnsemblMetazoa; T26E3.3a.2; T26E3.3a.2; WBGene00003921. [Q9NAN2-1]
DR   EnsemblMetazoa; T26E3.3b.1; T26E3.3b.1; WBGene00003921. [Q9NAN2-2]
DR   GeneID; 173137; -.
DR   KEGG; cel:CELE_T26E3.3; -.
DR   UCSC; T26E3.3b; c. elegans.
DR   CTD; 32752; -.
DR   WormBase; T26E3.3a; CE28089; WBGene00003921; par-6. [Q9NAN2-1]
DR   WormBase; T26E3.3b; CE40130; WBGene00003921; par-6. [Q9NAN2-2]
DR   eggNOG; KOG3606; Eukaryota.
DR   GeneTree; ENSGT00950000183211; -.
DR   HOGENOM; CLU_040653_0_1_1; -.
DR   InParanoid; Q9NAN2; -.
DR   OMA; SQGSPCW; -.
DR   OrthoDB; 825211at2759; -.
DR   PhylomeDB; Q9NAN2; -.
DR   Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR   Reactome; R-CEL-9013420; RHOU GTPase cycle.
DR   Reactome; R-CEL-9013424; RHOV GTPase cycle.
DR   PRO; PR:Q9NAN2; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00003921; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
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:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0043186; C:P granule; IDA:UniProtKB.
DR   GO; GO:0005080; F:protein kinase C binding; IPI:WormBase.
DR   GO; GO:0031267; F:small GTPase binding; IPI:WormBase.
DR   GO; GO:0007155; P:cell adhesion; IMP:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007098; P:centrosome cycle; IBA:GO_Central.
DR   GO; GO:0040001; P:establishment of mitotic spindle localization; IGI:UniProtKB.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IGI:UniProtKB.
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:0009949; P:polarity specification of anterior/posterior axis; IMP:WormBase.
DR   GO; GO:0060341; P:regulation of cellular localization; IBA:GO_Central.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   CDD; cd06403; PB1_Par6; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR034876; Par6.
DR   InterPro; IPR000270; PB1_dom.
DR   InterPro; IPR034868; PB1_Par6.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   PANTHER; PTHR14102:SF11; PTHR14102:SF11; 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 adhesion; Cell cycle; Cell division;
KW   Cell junction; Cell membrane; Cytoplasm; Developmental protein;
KW   Differentiation; Fertilization; Gastrulation; Gonadal differentiation;
KW   Membrane; Reference proteome; Tight junction.
FT   CHAIN           1..309
FT                   /note="Partitioning defective protein 6"
FT                   /id="PRO_0000112520"
FT   DOMAIN          14..96
FT                   /note="PB1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT   DOMAIN          132..149
FT                   /note="Pseudo-CRIB"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          156..249
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          249..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..120
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_034690"
SQ   SEQUENCE   309 AA;  34219 MW;  4247E7875124953B CRC64;
     MSYNGSYHQN HHSTLQVKSK FDSEWRRFSI PMHSASGVSY DGFRSLVEKL HHLESVQFTL
     CYNSTGGDLL PITNDDNLRK SFESARPLLR LLIQRRGESW EEKYGYGTDS DKRWKGISSL
     MAQKPPKRSY SISNPEDFRQ VSAIIDVDIV PEAHRRVRLC KHGQERPLGF YIRDGTSVRV
     TERGVVKVSG IFISRLVDGG LAESTGLLGV NDEVLEVNGI EVLGKTLDQV TDMMVANAHN
     LIITVKPANQ RNTLSRGPSQ QGTPNASEMS AATAAATGGI QRPMKMNGSS DGSYHPKQHD
     ANDSDSGED
 
 
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