ID A0A0V1M6K4_9BILA Unreviewed; 1104 AA.
AC A0A0V1M6K4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Axin-1 {ECO:0000313|EMBL:KRZ67244.1};
GN Name=axin1 {ECO:0000313|EMBL:KRZ67244.1};
GN ORFNames=T10_5335 {ECO:0000313|EMBL:KRZ67244.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ67244.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ67244.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ67244.1};
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:KRZ67244.1}.
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DR EMBL; JYDO01000204; KRZ67244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1M6K4; -.
DR STRING; 268474.A0A0V1M6K4; -.
DR Proteomes; UP000054843; 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:UP000054843};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|PROSITE-
KW ProRule:PRU00069}.
FT DOMAIN 198..302
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 1021..1104
FT /note="DIX"
FT /evidence="ECO:0000259|PROSITE:PS50841"
FT REGION 111..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 639..666
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 111..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1104 AA; 119308 MW; 8F476A4D7CE54992 CRC64;
MSTAGKLAEE AASEEFISCA TRPPAIGKAV FSGFICHVRF FIDARHAGLS KCLLCQKLDM
AIKKFVPFSE SRRGIITLGN ILLQALGLVK KKNSASSDPA DYANESSSSL SAVAEMKHSQ
QQQGGNTSPK SSKFNSRNHS PLLFTSRKSS RSASLSDFPK EGSEEAPLGG YVPCEEESDD
VSPYSERATP PYMRWAVDLQ NVLEDFEGLQ LFKKFLTNEG CENELDFWYA CKGLKQYSDK
EWSLVERVAH MIHQNYVRPQ GEYSLTCIRG ETRVEIQKRF VAKDICQGMF DTAQMEVEAF
LRIKHAAFVE SDLYISYLQA IQTGGWDSPR CYSNDSRSNS SSSNSADGQR PSSTLLPTVQ
EEVEVEVPET DGRTEQQEQQ QKQKHQQQQQ QQQQQQKQPP KQQQQVKSQS LQKHPPATGG
DEASSSGCSG GNNSKPTKSI AGGKVGPAPT PVPVVPTVTR ATLKSDERVK VSGRDVGHST
TTASFTTTAV APSTGVGDNS QPSVVMIKKK SSSSSSGGGG GSGQSYGGRL TAGALVATLE
QRMAYSACSR STRGGVPPNP YHTKYVPYLP TSAQDSELQS MSSDAATDSS FGNSRSRHKE
KRIIRQHIEQ NRDNVSSQIF IPRTQREVLA RDMMDEEFKF QVVEKLENLR RERETYEKLN
ESLQRLSEPE NNSNSHRAAV EKFCKVEKSF RAAPEDAEAI LDDYYNRVGW KDSPKQSPMR
SPGFAFGSRK KSPGSKSPDR RVISRMMTTS YPLPYAMSQT LPLQHQGGSA AAVMRGLGQE
QNQTMIQVPP IPVHLSSKHR AAHASASSGS GGGGAGSSGA GGGGGGGSGS HRSSSRAEIA
AASSGGGGGG TSAAAAAGSG GGSSAAQRSS GSGKSSRQYS RYPVLTSDTS GISSGTSSDP
SLVSAKIPPM TAAYNRSSTN EQWILEERPS YESESGRHRS RSSNQSGSGL SSGKSHKTSS
HKSGATDSSA RVSSSEKSSS RSHKMLDSSG FPSINTRKAW SMRTSNVSAS QSSNSSQATC
QEYISVGYFL PNESTPYVTR FSGRQISLKQ FKQLIPRKGN FRYFFQCASD ELGTGMIQRE
VTDENELLPI WEGNKVVAKI VSVD
//
