POP1_CAEBR
ID POP1_CAEBR Reviewed; 439 AA.
AC A8WWH5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Protein pop-1;
DE AltName: Full=Posterior pharynx defect protein 1;
GN Name=pop-1 {ECO:0000312|WormBase:CBG04236};
GN ORFNames=CBG04236 {ECO:0000312|WormBase:CBG04236};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Part of the Wnt signaling pathway essential for the
CC specification of the mesodermal cell fate in early embryos (By
CC similarity). Required for asymmetrical division of somatic gonadal
CC precursor descendants which initiate axis formation required to control
CC organ shape (By similarity). Similarly, involved in asymmetrical
CC division of seam cells, a stem cell-like lineage (By similarity).
CC Represses expression of target genes via its interaction with hda-1
CC histone deacetylase (By similarity). Required for specification of the
CC M lineage-derived coelomocyte and sex myoblast fate (By similarity).
CC Regulates coelomocyte fate by positively regulating proliferation and
CC ceh-34 and possibly eya-1 expression in M.dlpa and M.drpa precursors
CC (By similarity). {ECO:0000250|UniProtKB:Q10666}.
CC -!- SUBUNIT: Interacts with hda-1 (By similarity). Interacts with bar-1 (By
CC similarity). Interacts with par-5; the interaction is direct and is
CC enhanced by lit-1-mediated pop-1 phosphorylation (By similarity). The
CC interaction also leads to the subsequent nuclear export of pop-1 (By
CC similarity). Interacts (when phosphorylated on Ser-125) with lit-1; the
CC interaction is dependent on the beta-catenin-lit-1 complex (By
CC similarity). Interacts with wrm-1 (By similarity).
CC {ECO:0000250|UniProtKB:Q10666}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q10666,
CC ECO:0000255|PROSITE-ProRule:PRU00267}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q10666}. Note=Predominantly nuclear, but is
CC exported out of the nucleus and into the cytoplasm upon lit-1-mediated
CC phosphorylation (By similarity). Soon after the nuclei reform in
CC telophase, pop-1 levels decrease in the posterior nucleus, in contrast
CC to the anterior nucleus (By similarity). There is a ~2-fold nuclear
CC enrichment of pop-1 in the anterior compared with posterior daughter
CC cells at the time of cytokinesis (By similarity).
CC {ECO:0000250|UniProtKB:Q10666}.
CC -!- PTM: Phosphorylated on Ser-125 by lit-1 in the beta-catenin-lit-1
CC complex (By similarity). Phosphorylation promotes the interaction of
CC pop-1 and par-5 and the subsequent translocation of pop-1 from the
CC nucleus to the cytoplasm (By similarity).
CC {ECO:0000250|UniProtKB:Q10666}.
CC -!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}.
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DR EMBL; HE600926; CAP24984.2; -; Genomic_DNA.
DR AlphaFoldDB; A8WWH5; -.
DR SMR; A8WWH5; -.
DR STRING; 6238.CBG04236; -.
DR EnsemblMetazoa; CBG04236.1; CBG04236.1; WBGene00026953.
DR WormBase; CBG04236; CBP25143; WBGene00026953; Cbr-pop-1.
DR eggNOG; KOG3248; Eukaryota.
DR HOGENOM; CLU_625901_0_0_1; -.
DR InParanoid; A8WWH5; -.
DR OrthoDB; 1542800at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IEA:EnsemblMetazoa.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0035035; F:histone acetyltransferase binding; IEA:EnsemblMetazoa.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:EnsemblMetazoa.
DR GO; GO:0019901; F:protein kinase binding; IEA:EnsemblMetazoa.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:EnsemblMetazoa.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:EnsemblMetazoa.
DR GO; GO:0001222; F:transcription corepressor binding; IEA:EnsemblMetazoa.
DR GO; GO:0008356; P:asymmetric cell division; ISS:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0009880; P:embryonic pattern specification; IEA:EnsemblMetazoa.
DR GO; GO:0035262; P:gonad morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0007500; P:mesodermal cell fate determination; IEA:EnsemblMetazoa.
DR GO; GO:0007501; P:mesodermal cell fate specification; IEA:EnsemblMetazoa.
DR GO; GO:0051782; P:negative regulation of cell division; IEA:EnsemblMetazoa.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IEA:EnsemblMetazoa.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0043282; P:pharyngeal muscle development; IEA:EnsemblMetazoa.
DR GO; GO:0010085; P:polarity specification of proximal/distal axis; IEA:EnsemblMetazoa.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblMetazoa.
DR GO; GO:0040026; P:positive regulation of vulval development; IEA:EnsemblMetazoa.
DR GO; GO:0009786; P:regulation of asymmetric cell division; IEA:EnsemblMetazoa.
DR GO; GO:0042659; P:regulation of cell fate specification; IEA:EnsemblMetazoa.
DR GO; GO:2000746; P:regulation of defecation rhythm; IEA:EnsemblMetazoa.
DR GO; GO:0061853; P:regulation of neuroblast migration; IEA:EnsemblMetazoa.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR028782; Pangolin-like.
DR InterPro; IPR024940; TCF/LEF.
DR PANTHER; PTHR10373; PTHR10373; 1.
DR PANTHER; PTHR10373:SF38; PTHR10373:SF38; 1.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 3: Inferred from homology;
KW Activator; Cytoplasm; Developmental protein; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Wnt signaling pathway.
FT CHAIN 1..439
FT /note="Protein pop-1"
FT /id="PRO_0000348936"
FT DNA_BIND 199..269
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..138
FT /note="Involved in nuclear asymmetry"
FT /evidence="ECO:0000250"
FT REGION 254..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 125
FT /note="Phosphoserine; by LIT1"
FT /evidence="ECO:0000250|UniProtKB:Q10666"
SQ SEQUENCE 439 AA; 48851 MW; D4845C1A357B5801 CRC64;
MMADEELGDE VKVFRRDEDA DDDPMISGET SEQQLADDKK DAVMEAELDG AGRVPLIGGL
KAEIKAEPSP SFPMPSMLPC GPYSPFSGLP IMFPMVVPQY LSPNPNINMM NMMTMRAAMA
GAPLSPAFPA MFSPNPLFPF PGVVAKQHLE NTMPMHMRAG PLSSLNHMKM PPYMPHQMMP
QHNERRGHGG GKVKKEDHIK KPLNAFMWYM KENRPKLLEE VGNDQKQSAE LNKELGKRWH
DLPKEEQQKY FEMAKKDRES HKEKYPQWSA RENYAVNKKK PKRKRDKSVV SGSENNDQKK
CRARFGVTNT SMWCKPCQRK KKCIYATDRS GSELNDGHDG RGTSGGCSSS SESSSPNNNQ
PMPMNAPQTV AAMHAMLMGM QIGQSAHLAS SHSTGSSGTS PPVANPSDSE SDVDEDEDID
PTITQQTQEY IMQESVCTL
