ID A0A0V1CE78_TRIBR Unreviewed; 1031 AA.
AC A0A0V1CE78;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Axin-1 {ECO:0000313|EMBL:KRY47647.1};
DE Flags: Fragment;
GN Name=axin1 {ECO:0000313|EMBL:KRY47647.1};
GN ORFNames=T03_7015 {ECO:0000313|EMBL:KRY47647.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY47647.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY47647.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY47647.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY47647.1}.
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DR EMBL; JYDI01000234; KRY47647.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CE78; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:InterPro.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.196.10; -; 1.
DR Gene3D; 2.40.240.130; -; 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 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; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46102; AXIN; 1.
DR PANTHER; PTHR46102:SF2; AXIN; 1.
DR Pfam; PF00778; DIX; 1.
DR Pfam; PF00615; RGS; 1.
DR SMART; SM00021; DAX; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50841; DIX; 1.
DR PROSITE; PS50132; RGS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Signal {ECO:0000256|SAM:SignalP};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|PROSITE-
KW ProRule:PRU00069}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..1031
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012475353"
FT DOMAIN 131..235
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 948..1031
FT /note="DIX"
FT /evidence="ECO:0000259|PROSITE:PS50841"
FT REGION 29..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 559..586
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 40..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY47647.1"
SQ SEQUENCE 1031 AA; 112193 MW; D7B1831694E8AE05 CRC64;
LHFLTLLMST AGKLAEEAAS EEFISCATRP PAIGASSDPA DYANESSTSG VVEMKHSHQG
GGSPKSSKLN SRNHSPLLFT SKKSSRSASL SDFPKEGSEE APLGYVPCEE SDDVSPYSER
ATPPYMRWAV DLQNVLEDFE GLQLFKKFLT NEGCENELDF WYACKGLKQY SDKEWSLVER
VAHMIHQNYV RPQGEYSLTC IRGETRVEIQ KRFVAKDICQ SMFDTAQMEV EAFLRIKHAA
FVESDLYISY LQAIQTGGWD SPRCYSNDSR SNSSSSNSAD GQRPSSTLLP TVQEEVEIEV
AETDGRTEQE QQQKSKQQQQ QQQKQSPKQQ QQQQLKSQSL QKHPAASGDE ATTSSSCSNK
PTKSAVGGGT AGPASTPVVA SSIPVVPTVT RTTFKSDERL RISGRDAAHP TTTSFTTTSV
APSSDSQPTP VVMIKKKSSG SSGQSYGGRL TAGALVATFE QRMAYSACSR GTRGGVPPNP
YHTKYVPYLP TSAQDSELQS MSSDAATDSS FGNSRSRHKE KRIIRQHIEQ NRDNVSSQIF
IPRTQREVVA RDMMDEEFKF QVVEKLENLR RERETYEKLN ESLQRLSEPE NNSNSHRAAV
EKFCKVEKSF RAAPEDAEAI LDDYYNRVGW KDSPKQSPMR SPGFAFGSRK KSPGIKLKFL
QIVWSKSPDR RVISRMMTTS YPLPYAMSQT LPLQHQGGST AVMRGSLGQD QNQTMIQVPP
NVPVHLSSKH RATHASATSG SGGGGGGSHR SSSRTESTTA ASSGGGGGGT ATAATAAAAA
AAAVAAAGSG SSAAQRTSGS GKSSRQYSRY PVLTSDTSGI SSGTSSDPSL VSAKIPPMTA
AYNRSSTNEQ WILEERPSYE TESGRHRSRS SNQSGSGLSS GKSHKTSSHK SGASDSSARV
SSSEKSSRSH KMLDSSGFPN INTRKAWSMR TSSISASQSS NSSQATCQEY ISVGYFLPNE
STPYVTKFSG RQISLKQFKQ LIPRKGNFRY FFQCASDELG TGMIQREVTD ENELLPIWEG
NKVVAKIVSV D
//
