PRY1_CAEEL
ID PRY1_CAEEL Reviewed; 586 AA.
AC O62090;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Axin-like protein pry-1;
DE AltName: Full=Protein polyray {ECO:0000303|PubMed:12023307};
GN Name=pry-1 {ECO:0000312|EMBL:AAL77082.1, ECO:0000312|WormBase:C37A5.9};
GN ORFNames=C37A5.9;
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:AAL77082.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH APR-1; BAR-1; GSK-3
RP AND MIG-5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=12023307; DOI=10.1101/gad.981802;
RA Korswagen H.C., Coudreuse D.Y.M., Betist M.C., van de Water S.,
RA Zivkovic D., Clevers H.C.;
RT "The axin-like protein PRY-1 is a negative regulator of a canonical Wnt
RT pathway in C. elegans.";
RL Genes Dev. 16:1291-1302(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 DISRUPTION PHENOTYPE.
RX PubMed=9834184; DOI=10.1242/dev.126.1.37;
RA Maloof J.N., Whangbo J., Harris J.M., Jongeward G.D., Kenyon C.;
RT "A Wnt signaling pathway controls hox gene expression and neuroblast
RT migration in C. elegans.";
RL Development 126:37-49(1999).
RN [4] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16077004; DOI=10.1101/gad.1323705;
RA Nakamura K., Kim S., Ishidate T., Bei Y., Pang K., Shirayama M.,
RA Trzepacz C., Brownell D.R., Mello C.C.;
RT "Wnt signaling drives WRM-1/beta-catenin asymmetries in early C. elegans
RT embryos.";
RL Genes Dev. 19:1749-1754(2005).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=16631156; DOI=10.1016/j.ydbio.2005.12.024;
RA Wu M., Herman M.A.;
RT "A novel noncanonical Wnt pathway is involved in the regulation of the
RT asymmetric B cell division in C. elegans.";
RL Dev. Biol. 293:316-329(2006).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=17276345; DOI=10.1016/j.devcel.2007.01.004;
RA Mizumoto K., Sawa H.;
RT "Cortical beta-catenin and APC regulate asymmetric nuclear beta-catenin
RT localization during asymmetric cell division in C. elegans.";
RL Dev. Cell 12:287-299(2007).
RN [7] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH GSK-3.
RX PubMed=17601533; DOI=10.1016/j.ydbio.2007.05.043;
RA Oosterveen T., Coudreuse D.Y.M., Yang P.-T., Fraser E., Bergsma J.,
RA Dale T.C., Korswagen H.C.;
RT "Two functionally distinct axin-like proteins regulate canonical Wnt
RT signaling in C. elegans.";
RL Dev. Biol. 308:438-448(2007).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=17213328; DOI=10.1073/pnas.0510527104;
RA Schmitz C., Kinge P., Hutter H.;
RT "Axon guidance genes identified in a large-scale RNAi screen using the
RT RNAi-hypersensitive Caenorhabditis elegans strain nre-1(hd20) lin-
RT 15b(hd126).";
RL Proc. Natl. Acad. Sci. U.S.A. 104:834-839(2007).
CC -!- FUNCTION: Works in parallel with axl-1 in negatively regulating bar-1
CC signaling in vulval precursor cells and Q neuroblasts. Inhibits Wnt
CC signaling, which affects tissue specific expression of Hox genes, egl-
CC 5, lin-39 and mab-5. This in turn affects QR (postembryonic neuroblast)
CC cell migration, vulval cell fate specification, and the development of
CC sensory structures by the seam cell lineage. Has a role in alae V cell
CC patterning, ray formation in the male tail and axon guidance. Does not
CC affect B cell polarity. {ECO:0000269|PubMed:12023307,
CC ECO:0000269|PubMed:16077004, ECO:0000269|PubMed:16631156,
CC ECO:0000269|PubMed:17213328, ECO:0000269|PubMed:17276345,
CC ECO:0000269|PubMed:17601533, ECO:0000269|PubMed:9834184}.
CC -!- SUBUNIT: Interacts (via N-terminus) with apr-1 (via C-terminus).
CC Interacts with bar-1 (via ARM repeats), gsk-3, and mig-5.
CC {ECO:0000269|PubMed:12023307, ECO:0000269|PubMed:17601533}.
CC -!- INTERACTION:
CC O62090; Q18825: bar-1; NbExp=3; IntAct=EBI-2917690, EBI-2528850;
CC O62090; Q9U2Q9: gsk-3; NbExp=6; IntAct=EBI-2917690, EBI-330089;
CC O62090; Q22227: mig-5; NbExp=4; IntAct=EBI-2917690, EBI-316403;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12023307,
CC ECO:0000269|PubMed:16077004}. Nucleus {ECO:0000269|PubMed:12023307,
CC ECO:0000269|PubMed:16077004}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:12023307, ECO:0000269|PubMed:16077004}.
CC Note=Subcellular location was measured using a GFP reporter gene.
CC Location of the pry-1:GFP fusion protein ranges from plasma membrane
CC and cytoplasmic dots to diffuse cytoplasmic and nuclear staining. This
CC difference may be due to variations in expression levels of the fusion
CC protein in different transgenic lines. {ECO:0000269|PubMed:12023307,
CC ECO:0000269|PubMed:16077004}.
CC -!- TISSUE SPECIFICITY: Expressed in hypodermal cells (seam cells) V5 and
CC V6, Q neuroblasts, ventral hypodermal cells P7/8 to P11/12, body wall
CC muscle cells and neurons in the head, the tail and the ventral nerve
CC cord. {ECO:0000269|PubMed:12023307}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:12023307}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit ectopic rays and lack alae in V
CC cells of the male tail. Mutants appear scrawny, often herniated,
CC uncoordinated, show defects in dorsal and ventral cord fasciculation,
CC commissure guidance defects, and over activated Wnt signaling pathway.
CC Phenotypes are more penetrant in the pry-1 and axl-1 double mutant,
CC suggesting some functional overlaps. {ECO:0000269|PubMed:9834184}.
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DR EMBL; AF468834; AAL77082.1; -; mRNA.
DR EMBL; Z92828; CAB07332.2; -; Genomic_DNA.
DR PIR; T19802; T19802.
DR RefSeq; NP_493474.2; NM_061073.5.
DR AlphaFoldDB; O62090; -.
DR SMR; O62090; -.
DR BioGRID; 38675; 39.
DR IntAct; O62090; 14.
DR STRING; 6239.C37A5.9; -.
DR EPD; O62090; -.
DR PaxDb; O62090; -.
DR EnsemblMetazoa; C37A5.9.1; C37A5.9.1; WBGene00004202.
DR GeneID; 173287; -.
DR KEGG; cel:CELE_C37A5.9; -.
DR UCSC; C37A5.9.1; c. elegans.
DR CTD; 173287; -.
DR WormBase; C37A5.9; CE30125; WBGene00004202; pry-1.
DR eggNOG; ENOG502S33C; Eukaryota.
DR HOGENOM; CLU_471192_0_0_1; -.
DR InParanoid; O62090; -.
DR OMA; ITAECKS; -.
DR OrthoDB; 732602at2759; -.
DR PhylomeDB; O62090; -.
DR Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-CEL-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-CEL-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR SignaLink; O62090; -.
DR PRO; PR:O62090; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004202; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0030877; C:beta-catenin destruction complex; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0070016; F:armadillo repeat domain binding; IPI:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:WormBase.
DR GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0048468; P:cell development; IBA:GO_Central.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0040027; P:negative regulation of vulval development; IMP:WormBase.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IGI:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0042659; P:regulation of cell fate specification; IMP:WormBase.
DR GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 2.40.240.130; -; 1.
DR InterPro; IPR043581; Axin-like.
DR InterPro; IPR001158; DIX.
DR InterPro; IPR038207; DIX_dom_sf.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46102; PTHR46102; 1.
DR Pfam; PF00778; DIX; 1.
DR Pfam; PF00615; RGS; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50841; DIX; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Developmental protein; Membrane; Nucleus;
KW Reference proteome; Wnt signaling pathway.
FT CHAIN 1..586
FT /note="Axin-like protein pry-1"
FT /id="PRO_0000347254"
FT DOMAIN 10..131
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 505..586
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT REGION 1..135
FT /note="Required for interaction with apr-1"
FT /evidence="ECO:0000269|PubMed:12023307"
FT REGION 137..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 66002 MW; 366D09FFC1568AE1 CRC64;
METHLGWARS LEAVLSDRSA LDAFQEWLIE YSSPQYLDLF FAIRAYERMA LEGKPEKSQL
SKSIYSKFLS SRTGNCEAIP KHFRAPIGEK LRHGTELEDR VFSHCSNFVQ EFLRRQHEEF
VGSEEFIEAF NKMSSTTADQ LPGGSAHHSS HQNTMRRSSG TTSRKSAAQI ATQLTAEALL
KSKHDRHSKL GETKLEKMYP PTRQPYVCNA TTSHNDSAVS STFSGDTPEA HRMHSNRLRH
IRDEQARENH GTMTLPRVEK ASVDGQQWDH SSESGRRNFA MEITRKLLRH IDKVKLNDEM
EKRIDDIEEC RYTTIDMVNG TEPNDDLGKI DEDEELDDYL KMKMTDDSQK GSTNRSPKGP
AGEPNKSGEG SKNTTLSPTN RAPAQLHNTI RVPRRKDYPR DTSASLKSHR HHQIDTNRMM
SQSMCAPSYS SASSSYSRDS FAPAPTTRVN FAPGSSKSSQ FYDSSGIGSM APSAFSATSS
LDYKDRRQHR KAPTPKKHSK IGKNLSNLIT ISYLGTDKIP VVTHVPNDGP MTLAEFKRHF
ALPNGAHQLF FKTECEDGSA PFQLLLIKDE HHLLPVFEGR IAAELR
