ID A0A0V1CF80_TRIBR Unreviewed; 1012 AA.
AC A0A0V1CF80;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 28.
DE SubName: Full=Axin-1 {ECO:0000313|EMBL:KRY47646.1};
GN Name=axin1 {ECO:0000313|EMBL:KRY47646.1};
GN ORFNames=T03_7015 {ECO:0000313|EMBL:KRY47646.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY47646.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY47646.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY47646.1};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KRY47646.1}.
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DR EMBL; JYDI01000234; KRY47646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CF80; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
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; IPR014936; Axin_b-cat-bd.
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; PF08833; Axin_b-cat_bind; 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 Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|PROSITE-
KW ProRule:PRU00069}.
FT DOMAIN 131..235
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 929..1012
FT /note="DIX"
FT /evidence="ECO:0000259|PROSITE:PS50841"
FT REGION 34..118
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 396..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 631..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 559..586
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 37..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 721..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1012 AA; 110643 MW; 1974F057F80EC449 CRC64;
MAIKFVLFSE SRRGIITLGN IVLQALGLIK KKNSASSDPA 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 KSPGSKSPDR
RVISRMMTTS YPLPYAMSQT LPLQHQGGST AVMRGSLGQD QNQTMIQVPP NVPVHLSSKH
RATHASATSG SGGGGGGSHR SSSRTESTTA ASSGGGGGGT ATAATAAAAA AAAVAAAGSG
SSAAQRTSGS GKSSRQYSRY PVLTSDTSGI SSGTSSDPSL VSAKIPPMTA AYNRSSTNEQ
WILEERPSYE TESGRHRSRS SNQSGSVRTK VVPVILLHVC LALRRVVEVT KCWIPVVFQT
SIRTRKAWSM RTSSISASQS SNSSQATCQE YISVGYFLPN ESTPYVTKFS GRQISLKQFK
QLIPRKGNFR YFFQCASDEL GTGMIQREVT DENELLPIWE GNKVVAKIVS VD
//