AXLP1_CAEEL
ID AXLP1_CAEEL Reviewed; 400 AA.
AC Q3LRZ3; Q14V27;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Axin-like protein 1 {ECO:0000303|PubMed:17601533};
GN Name=axl-1 {ECO:0000312|EMBL:ABA28304.1}; ORFNames=K02B12.4;
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:ABA28304.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, INTERACTION WITH BAR-1;
RP DSH-2; GSK-3 AND MIG-5, AND DISRUPTION PHENOTYPE.
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 [2] {ECO:0000312|EMBL:CAK55175.1}
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).
CC -!- FUNCTION: Works in parallel with pry-1 in negatively regulating bar-1
CC signaling in vulval precursor cells and Q neuroblasts. Shown to have a
CC role in excretory cell development. {ECO:0000269|PubMed:17601533}.
CC -!- SUBUNIT: Interacts with bar-1, dsh-2, gsk-3, and mig-5.
CC {ECO:0000269|PubMed:17601533}.
CC -!- INTERACTION:
CC Q3LRZ3; Q9U2Q9: gsk-3; NbExp=4; IntAct=EBI-327368, EBI-330089;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000269|PubMed:17601533};
CC IsoId=Q3LRZ3-1; Sequence=Displayed;
CC Name=a {ECO:0000269|PubMed:9851916};
CC IsoId=Q3LRZ3-2; Sequence=VSP_052860, VSP_052861;
CC -!- DISRUPTION PHENOTYPE: Worms exhibit defects in excretory cell
CC development and axonal migration. {ECO:0000269|PubMed:17601533}.
CC -!- MISCELLANEOUS: Reporter transgenes fail to show detectable expression
CC indicating that axl-1 may be expressed at low levels.
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DR EMBL; DQ185512; ABA28304.1; -; mRNA.
DR EMBL; Z75711; CAK55175.1; -; Genomic_DNA.
DR EMBL; Z75711; CAK55176.1; -; Genomic_DNA.
DR RefSeq; NP_001040671.1; NM_001047206.3. [Q3LRZ3-2]
DR RefSeq; NP_001040672.1; NM_001047207.3. [Q3LRZ3-1]
DR AlphaFoldDB; Q3LRZ3; -.
DR BioGRID; 51582; 8.
DR IntAct; Q3LRZ3; 10.
DR STRING; 6239.K02B12.4b; -.
DR PaxDb; Q3LRZ3; -.
DR EnsemblMetazoa; K02B12.4a.1; K02B12.4a.1; WBGene00010497. [Q3LRZ3-2]
DR EnsemblMetazoa; K02B12.4b.1; K02B12.4b.1; WBGene00010497. [Q3LRZ3-1]
DR GeneID; 186869; -.
DR KEGG; cel:CELE_K02B12.4; -.
DR UCSC; K02B12.4b; c. elegans.
DR CTD; 186869; -.
DR WormBase; K02B12.4a; CE40260; WBGene00010497; axl-1. [Q3LRZ3-2]
DR WormBase; K02B12.4b; CE40261; WBGene00010497; axl-1. [Q3LRZ3-1]
DR eggNOG; ENOG502TG1M; Eukaryota.
DR HOGENOM; CLU_058688_0_0_1; -.
DR InParanoid; Q3LRZ3; -.
DR OMA; HMAMSTQ; -.
DR OrthoDB; 1629042at2759; -.
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; Q3LRZ3; -.
DR PRO; PR:Q3LRZ3; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00010497; Expressed in larva and 4 other tissues.
DR GO; GO:0030877; C:beta-catenin destruction complex; IBA:GO_Central.
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; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
DR GO; GO:0048468; P:cell development; IMP:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IMP: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:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46102; PTHR46102; 3.
DR Pfam; PF00778; DIX; 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 Alternative splicing; Developmental protein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..400
FT /note="Axin-like protein 1"
FT /id="PRO_0000347252"
FT DOMAIN 4..132
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 305..392
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT REGION 190..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..69
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_052860"
FT VAR_SEQ 70..91
FT /note="NTGTCHVIGDSIRTKISTRVHE -> MATMSRRWNYFTPHYNDEGSID (in
FT isoform a)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_052861"
SQ SEQUENCE 400 AA; 45588 MW; 7C1E5CADC18D3B26 CRC64;
MTMRSKFSID RVLHDTAFAK WCQKEESRNA DSITLYTSIL DFESKLKTGS PSLSLLKLAR
HIHRKYVSLN TGTCHVIGDS IRTKISTRVH EVLDGKPPYI DLFDPLKQPL FQHLRSMHTE
FSTTTADVNT TWEDASSTSS SNKGATIWFN EDAIDKSSRH EIGQSTVTHE SEDDRFSFFN
AVCTRLNSLQ ETKNSSETEE HAESPRKEKS STPYGTDGFA PPPRSTQTNT LKVSNLPKRF
ESLYKKKRQQ VATSDSSGFG SNASDFWSFE RYGKSNQGTL ERPNRLFTGT NNGFSTLQPK
RRGSEAPKMT VELRYENDVP MVAKISANHA QSVTLRYFRH LFGLHYTDNC RFFFKSTCED
GSAQYQWTLL FHDDDILPVF QNRITAICRM CPPPEDHDLI
