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Axin-like protein pry-1 (Protein polyray)

 PRY1_CAEEL              Reviewed;         586 AA.
O62090;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 2.
30-AUG-2017, entry version 116.
RecName: Full=Axin-like protein pry-1;
AltName: Full=Protein polyray {ECO:0000303|PubMed:12023307};
Name=pry-1 {ECO:0000312|EMBL:AAL77082.1,
ECO:0000312|WormBase:C37A5.9}; ORFNames=C37A5.9;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1] {ECO:0000305, ECO:0000312|EMBL:AAL77082.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH APR-1; BAR-1;
GSK-3 AND MIG-5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=12023307; DOI=10.1101/gad.981802;
Korswagen H.C., Coudreuse D.Y.M., Betist M.C., van de Water S.,
Zivkovic D., Clevers H.C.;
"The axin-like protein PRY-1 is a negative regulator of a canonical
Wnt pathway in C. elegans.";
Genes Dev. 16:1291-1302(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9834184;
Maloof J.N., Whangbo J., Harris J.M., Jongeward G.D., Kenyon C.;
"A Wnt signaling pathway controls hox gene expression and neuroblast
migration in C. elegans.";
Development 126:37-49(1999).
[4] {ECO:0000305}
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16077004; DOI=10.1101/gad.1323705;
Nakamura K., Kim S., Ishidate T., Bei Y., Pang K., Shirayama M.,
Trzepacz C., Brownell D.R., Mello C.C.;
"Wnt signaling drives WRM-1/beta-catenin asymmetries in early C.
elegans embryos.";
Genes Dev. 19:1749-1754(2005).
[5] {ECO:0000305}
FUNCTION.
PubMed=16631156; DOI=10.1016/j.ydbio.2005.12.024;
Wu M., Herman M.A.;
"A novel noncanonical Wnt pathway is involved in the regulation of the
asymmetric B cell division in C. elegans.";
Dev. Biol. 293:316-329(2006).
[6] {ECO:0000305}
FUNCTION.
PubMed=17276345; DOI=10.1016/j.devcel.2007.01.004;
Mizumoto K., Sawa H.;
"Cortical beta-catenin and APC regulate asymmetric nuclear beta-
catenin localization during asymmetric cell division in C. elegans.";
Dev. Cell 12:287-299(2007).
[7] {ECO:0000305}
FUNCTION, AND INTERACTION WITH GSK-3.
PubMed=17601533; DOI=10.1016/j.ydbio.2007.05.043;
Oosterveen T., Coudreuse D.Y.M., Yang P.-T., Fraser E., Bergsma J.,
Dale T.C., Korswagen H.C.;
"Two functionally distinct axin-like proteins regulate canonical Wnt
signaling in C. elegans.";
Dev. Biol. 308:438-448(2007).
[8] {ECO:0000305}
FUNCTION.
PubMed=17213328; DOI=10.1073/pnas.0510527104;
Schmitz C., Kinge P., Hutter H.;
"Axon guidance genes identified in a large-scale RNAi screen using the
RNAi-hypersensitive Caenorhabditis elegans strain nre-1(hd20) lin-
15b(hd126).";
Proc. Natl. Acad. Sci. U.S.A. 104:834-839(2007).
-!- FUNCTION: Works in parallel with axl-1 in negatively regulating
bar-1 signaling in vulval precursor cells and Q neuroblasts.
Inhibits Wnt signaling, which affects tissue specific expression
of Hox genes, egl-5, lin-39 and mab-5. This in turn affects QR
(postembryonic neuroblast) cell migration, vulval cell fate
specification, and the development of sensory structures by the
seam cell lineage. Has a role in alae V cell patterning, ray
formation in the male tail and axon guidance. Does not affect B
cell polarity. {ECO:0000269|PubMed:12023307,
ECO:0000269|PubMed:16077004, ECO:0000269|PubMed:16631156,
ECO:0000269|PubMed:17213328, ECO:0000269|PubMed:17276345,
ECO:0000269|PubMed:17601533, ECO:0000269|PubMed:9834184}.
-!- SUBUNIT: Interacts (via N-terminus) with apr-1 (via C-terminus).
Interacts with bar-1 (via ARM repeats), gsk-3, and mig-5.
{ECO:0000269|PubMed:12023307, ECO:0000269|PubMed:17601533}.
-!- INTERACTION:
Q18825:bar-1; NbExp=3; IntAct=EBI-2917690, EBI-2528850;
Q9U2Q9:gsk-3; NbExp=6; IntAct=EBI-2917690, EBI-330089;
Q22227:mig-5; NbExp=4; IntAct=EBI-2917690, EBI-316403;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12023307,
ECO:0000269|PubMed:16077004}. Nucleus
{ECO:0000269|PubMed:12023307, ECO:0000269|PubMed:16077004}.
Cytoplasm, cell cortex {ECO:0000269|PubMed:12023307,
ECO:0000269|PubMed:16077004}. Note=Subcellular location was
measured using a GFP reporter gene. Location of the pry-1:GFP
fusion protein ranges from plasma membrane and cytoplasmic dots to
diffuse cytoplasmic and nuclear staining. This difference may be
due to variations in expression levels of the fusion protein in
different transgenic lines. {ECO:0000269|PubMed:12023307,
ECO:0000269|PubMed:16077004}.
-!- TISSUE SPECIFICITY: Expressed in hypodermal cells (seam cells) V5
and V6, Q neuroblasts, ventral hypodermal cells P7/8 to P11/12,
body wall muscle cells and neurons in the head, the tail and the
ventral nerve cord. {ECO:0000269|PubMed:12023307}.
-!- DEVELOPMENTAL STAGE: Expressed throughout development.
{ECO:0000269|PubMed:12023307}.
-!- DISRUPTION PHENOTYPE: Worms exhibit ectopic rays and lack alae in
V cells of the male tail. Mutants appear scrawny, often herniated,
uncoordinated, show defects in dorsal and ventral cord
fasciculation, commissure guidance defects, and over activated Wnt
signaling pathway. Phenotypes are more penetrant in the pry-1 and
axl-1 double mutant, suggesting some functional overlaps.
{ECO:0000269|PubMed:9834184}.
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EMBL; AF468834; AAL77082.1; -; mRNA.
EMBL; Z92828; CAB07332.2; -; Genomic_DNA.
PIR; T19802; T19802.
RefSeq; NP_493474.2; NM_061073.5.
UniGene; Cel.8800; -.
ProteinModelPortal; O62090; -.
SMR; O62090; -.
BioGrid; 38675; 30.
IntAct; O62090; 14.
STRING; 6239.C37A5.9; -.
EPD; O62090; -.
PaxDb; O62090; -.
EnsemblMetazoa; C37A5.9; C37A5.9; WBGene00004202.
GeneID; 173287; -.
KEGG; cel:CELE_C37A5.9; -.
UCSC; C37A5.9.1; c. elegans.
CTD; 173287; -.
WormBase; C37A5.9; CE30125; WBGene00004202; pry-1.
eggNOG; ENOG410K7XD; Eukaryota.
eggNOG; ENOG4110KZ2; LUCA.
InParanoid; O62090; -.
KO; K02157; -.
OMA; CNATTSH; -.
OrthoDB; EOG091G067M; -.
PhylomeDB; O62090; -.
SignaLink; O62090; -.
PRO; PR:O62090; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00004202; -.
GO; GO:0005938; C:cell cortex; IDA:WormBase.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0070016; F:armadillo repeat domain binding; IPI:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:WormBase.
GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0040027; P:negative regulation of vulval development; IMP:WormBase.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IGI:UniProtKB.
GO; GO:0042659; P:regulation of cell fate specification; IMP:WormBase.
GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
InterPro; IPR001158; DIX.
InterPro; IPR016137; RGS.
InterPro; IPR029071; Ubiquitin-rel_dom.
Pfam; PF00778; DIX; 1.
Pfam; PF00615; RGS; 1.
SMART; SM00315; RGS; 1.
SUPFAM; SSF48097; SSF48097; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50841; DIX; 1.
PROSITE; PS50132; RGS; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasm; Developmental protein;
Membrane; Nucleus; Reference proteome; Wnt signaling pathway.
CHAIN 1 586 Axin-like protein pry-1.
/FTId=PRO_0000347254.
DOMAIN 10 131 RGS. {ECO:0000255|PROSITE-
ProRule:PRU00171}.
DOMAIN 505 586 DIX. {ECO:0000255|PROSITE-
ProRule:PRU00069}.
REGION 1 135 Required for interaction with apr-1.
{ECO:0000269|PubMed:12023307}.
COMPBIAS 421 480 Ser-rich. {ECO:0000255}.
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


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