AXLP1_CAEBR
ID AXLP1_CAEBR Reviewed; 395 AA.
AC A8XFZ3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Axin-like protein 1 {ECO:0000250|UniProtKB:Q3LRZ3};
GN Name=axl-1; ORFNames=CBG12528;
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 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q3LRZ3}.
CC -!- SUBUNIT: Interacts with bar-1, dsh-2, gsk-3, and mig-5.
CC {ECO:0000250|UniProtKB:Q3LRZ3}.
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DR EMBL; HE600940; CAP31498.3; -; Genomic_DNA.
DR AlphaFoldDB; A8XFZ3; -.
DR STRING; 6238.CBG12528; -.
DR PRIDE; A8XFZ3; -.
DR EnsemblMetazoa; CBG12528a.1; CBG12528a.1; WBGene00033468.
DR WormBase; CBG12528a; CBP37566; WBGene00033468; Cbr-axl-1.
DR eggNOG; ENOG502TG1M; Eukaryota.
DR HOGENOM; CLU_058688_0_0_1; -.
DR InParanoid; A8XFZ3; -.
DR OMA; HMAMSTQ; -.
DR OrthoDB; 1629042at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0048468; P:cell development; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:InterPro.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
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; 2.
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 3: Inferred from homology;
KW Developmental protein; Reference proteome; Wnt signaling pathway.
FT CHAIN 1..395
FT /note="Axin-like protein 1"
FT /id="PRO_0000347251"
FT DOMAIN 4..132
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 301..386
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT REGION 190..230
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"
SQ SEQUENCE 395 AA; 45583 MW; 85ED500F6AEEF843 CRC64;
MTMRSKTFSD RILNDSEFFK WCQKEESRNA DSITLYKSIL EFESKFKSGS PSLSLLKLAR
HIHRKYVSLN TGTCNVIEDS TRTEMSKRVH EVLDGKSPYI ELFDPLKQPL FQHLRSMHTE
YSTTTADVSN TWEDTSSTDS SDKGATIWFN DDAIDRSSRH EISQNTVTHE SEDDRFAFFN
AVCTRLNSLQ ETKNSSETEE EKKKERSADP YGSDGFAPPP QSTQTHTLRN LPKRFESLYK
KKRQQNTTTT DSSGFGSNAS DFWSFERYGK SNHGTLERPN RLFPGSNNGF STLQPKKRSG
EIQKLTVELR YENDVPMVAK ISANQSVTLR YFRHLFGLHY SDNCRFFFKS TCEDGSAHYQ
WTLLFQDDDI LPVFQNRITA ICRMCPPPPE DHHLI