ID A0A0V0UZ35_9BILA Unreviewed; 1018 AA.
AC A0A0V0UZ35;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Axin-1 {ECO:0000313|EMBL:KRX56553.1};
DE Flags: Fragment;
GN Name=axin1 {ECO:0000313|EMBL:KRX56553.1};
GN ORFNames=T09_3114 {ECO:0000313|EMBL:KRX56553.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX56553.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX56553.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX56553.1};
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:KRX56553.1}.
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DR EMBL; JYDN01000119; KRX56553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0UZ35; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UP000054681};
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..1018
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013130971"
FT DOMAIN 131..235
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 935..1018
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..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 554..581
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..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX56553.1"
SQ SEQUENCE 1018 AA; 110585 MW; 847147AACA3E8956 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
AETDGRIEQE QQQKSKQQQQ QKQSPKQQQQ QQQLKSQSLQ KHPAASGDEA TTSSSCSNKP
TKSAVGGGTA GPVVASSIPV VPTVTRTTFK SDERLRISGR DAAHPTTTSF TTTSVAPSSD
SQPTPVVMIK KKSSGSSGQS YGGRLTAGAL VATFEQRMAY SACSRGTRGG VPPNPYHTKY
VPYLPTSAQD SELQSMSSDA ATDSSFGNSR SRHKEKRIIR QHIEQNRDNV SSQIFIPRTQ
REVVARDMMD EEFKFQVVEK LENLRRERET YEKLNESLQR LSEPENNSNS HRAAVEKFCK
VEKSFRAAPE DAEAILDDYY NRVGWKDSPK QSPMRSPGFA FGSRKKSPGS KSPDRRVISR
MMTTSYPLPY AMSQTLPLQH QGGSTAVMRG SFGQDQNQTM IQVPPNVPVH LSSKHRATHA
SATSGSGGGG GGSHRSSSRT ESTTAASSGG GGGGGGTATA ATAAAAAAAV AAAGSGGSSA
AQRTSGSGKS SRQYSRYPVL TSDTSGISSG TSSDPSLVSA KIPPMTAAYN RSSTNEQWIL
EERPSYETES GRHRSRSSNQ SGSGLSSGKS HKTSSHKSGA SDSSARVSSS EKSSRSHKML
DSSGFPNINT RKAWSMRTSS ISASQSSNSS QATCQEYISV GYFLPNESTP YVTKFSGRQI
SLKQFKQLIP RKGNFRYFFQ CASDELGTGM IQREVTDENE LLPIWEGNKV VAKIVSVD
//
