ID A0A0V1KUH9_9BILA Unreviewed; 1115 AA.
AC A0A0V1KUH9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Axin-1 {ECO:0000313|EMBL:KRZ51032.1};
GN Name=axin1 {ECO:0000313|EMBL:KRZ51032.1};
GN ORFNames=T02_7229 {ECO:0000313|EMBL:KRZ51032.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ51032.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ51032.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ51032.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ51032.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDW01000241; KRZ51032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1KUH9; -.
DR Proteomes; UP000054721; 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:UP000054721};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|PROSITE-
KW ProRule:PRU00069}.
FT DOMAIN 227..331
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 1032..1115
FT /note="DIX"
FT /evidence="ECO:0000259|PROSITE:PS50841"
FT REGION 130..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 656..683
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 133..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1115 AA; 121741 MW; CFA1F1F2703F2D00 CRC64;
MSTAGKLAEE AASEEFISCA TRPPAIGCNS VRTAPIADGA RCELSVHCSA MLVSVLTFDF
NLKKSKHLFQ IYFLVLFINS NENYKCENEH RISWTYMAIK FVLFSESRRG IITLGNIVLQ
ALGLIKKKNS ASSDPADYAN ESSTSGVVEM KHSHQGGGSP KSSKLNSRNH SPLLFTSKKS
SRSASLSDFP KEGSEEAPLG YVPCEESDDV SPYSERATPP YMRWAVDLQN VLEDFEGLQL
FKKFLTNEGC ENELDFWYAC KGLKQYSDKE WSLVERVAHM IHQNYVRPQG EYSLTCIRGE
TRVEIQKRFV AKDICQSMFD TAQMEVEAFL RIKHAAFVES DLYISYLQAI QTGGWDSPRC
YSNDSRSNSS SSNSADGQRP SSTLLPTVQE EVEIEVAETD GRIEQEQQQK SKQQQQQQQQ
QKQSPKQQQQ QLKSQSLQKH PAGSGDEATT SSSCSNKPTK STVGGGTAGP ASTPVAASSI
PVVPTVTRTT FKSDERLRIS GRDAAHPTTT SFTTTSVAPS SDSQPTAVVM IKKKSSGSSG
QSYGGRLTAG ALVATFEQRM AYSACSRGTR GGVPPNPYHT KYVPYLPTSA QDSELQSMSS
DAATDSSFGN SRSRHKEKRI IRQHIEQNRD NVSSQIFIPR TQREVVARDM MDEEFKFQVV
EKLENLRRER ETYEKLNESL QRLSEPENNS NSHRAAVEKF CKVEKSFRAA PEDAEAILDD
YYNRVGWKDS PKQSPMRSPG FAFGSRKKSP GSKSPDRRVI SRMMTTSYPL PYAMSQTLPL
QHQGGSTAVM RGSLGQDQNQ TMIQVPPNVP VHLSSKHRAT HASATSGSGG GGGGSHRSSS
RTESTTAASS GVGGGTATAA TAAAAAAVAA AGSGSSAAQR TGGSGKSSRQ YSRYPVLTSD
TSGISSGTSS DPSLVSAKIP PMTAAYNRSS TNEQWILEER PSYETESGRH RSRSSNQSGS
GLSSGKSHKT SSHKSGASDS SARVSSSEKS SRSHKMLDSS GFPNINTRKA WSMRTSSISA
SQSSNSSQAT CQEYISVGYF LPNESTPYVT KFSGRQISLK QFKQLIPRKG NFRYFFQCAS
DELGTGMIQR EVTDENELLP IWEGNKVVAK IVSVD
//
