PRY1_CAEBR
ID PRY1_CAEBR Reviewed; 625 AA.
AC A8XU52;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Axin-like protein pry-1 {ECO:0000250|UniProtKB:O62090};
DE AltName: Full=Protein polyray {ECO:0000250|UniProtKB:O62090};
GN Name=pry-1; ORFNames=CBG18802;
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: 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 (By similarity). {ECO:0000250|UniProtKB:O62090}.
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 (By
CC similarity). {ECO:0000250|UniProtKB:O62090}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O62090}.
CC Nucleus {ECO:0000250|UniProtKB:O62090}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:O62090}.
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DR EMBL; HE601380; CAP36177.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XU52; -.
DR SMR; A8XU52; -.
DR STRING; 6238.CBG18802; -.
DR WormBase; CBG18802; CBP41347; WBGene00038147; Cbr-pry-1.
DR eggNOG; ENOG502S33C; Eukaryota.
DR HOGENOM; CLU_471192_0_0_1; -.
DR InParanoid; A8XU52; -.
DR OMA; ITAECKS; -.
DR OrthoDB; 732602at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0030877; C:beta-catenin destruction complex; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
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: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:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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 SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50841; DIX; 1.
DR PROSITE; PS50132; RGS; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cytoplasm; Developmental protein; Membrane; Nucleus;
KW Reference proteome; Wnt signaling pathway.
FT CHAIN 1..625
FT /note="Axin-like protein pry-1"
FT /id="PRO_0000347253"
FT DOMAIN 14..135
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 544..625
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT REGION 153..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 70334 MW; BB795F6C15CB4600 CRC64;
MESGPSSHLD WARSLEAVLS DRTALDLFQK WLMEYSLPQY LDLYFAIRAF ERMTLEGKPE
KNQLSKSIYC KFLSSRTGNC EAIPKHFKAP IGEKIRHGID LEDRAFSHCS SFVVDFLRRQ
HEEFVRSDEF IEALNKVRLR PLFPKPTVIL QMSSSTDSSS SHQNTIRKSG SSKRTATQLT
AEALLKTKHD RHTKFGELKL EKMYPSARQP YVCNATTSHN DSAVSSSFSG DAPGAHRSNR
LRHLREEQAH QNRDTATVPR VEKQQASSAA DQPFDHATEN GRRGFSMEIT KKLLRHLDKV
KMNEEMERRI DDIEECRYTT IDMVNGTEAD VDMGGIDEDE ELDDYLKMKM TDDSQKGSQN
RSPKGPNSGE KEKDGVSKNA TFSPAPPPPR DSPRGLISSH LHHHSIHHNT IRPPRRTSKE
YPLDISLSRN QYPRHHQIDT NRSLMSQSMC VPGPSYSSAS STFSRDSFAP SPMLKGFAGA
PGSSKSSQMY DSSGIGSMAP SAFSATSSLD YKEKRHRKSL PNHHSMMSNS LTTPRKHHKI
GKSLSNLITL SYVGSDKIPV VTHVPYDGPM TLAEFKRHFA LPTGGQQLFF KTDCEDGSAP
FQLLLVRDEH TLLPVFEGRI AAEIR
