ID A0A1S3IX94_LINUN Unreviewed; 980 AA.
AC A0A1S3IX94;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Axin-1 isoform X1 {ECO:0000313|RefSeq:XP_013402825.1};
GN Name=LOC106168343 {ECO:0000313|RefSeq:XP_013402825.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013402825.1};
RN [1] {ECO:0000313|RefSeq:XP_013402825.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013402825.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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 RefSeq; XP_013402825.1; XM_013547371.1.
DR AlphaFoldDB; A0A1S3IX94; -.
DR STRING; 7574.A0A1S3IX94; -.
DR EnsemblMetazoa; XM_013547371.1; XP_013402825.1; LOC106168343.
DR GeneID; 106168343; -.
DR KEGG; lak:106168343; -.
DR InParanoid; A0A1S3IX94; -.
DR OrthoDB; 4256282at2759; -.
DR Proteomes; UP000085678; Unplaced.
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; IPR032101; Axin_TNKS-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; PF16646; AXIN1_TNKS_BD; 1.
DR Pfam; PF08833; Axin_b-cat_bind; 1.
DR Pfam; PF00778; DIX; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
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 ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|PROSITE-
KW ProRule:PRU00069}.
FT DOMAIN 139..255
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 898..980
FT /note="DIX"
FT /evidence="ECO:0000259|PROSITE:PS50841"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 107746 MW; 9BCF188DB9D247CF CRC64;
MTERETASIN NMSIEVHQFV NDSGGHKFTE TAPRPPVPGE ENELQSNGGH STRSSGSHKS
HASHKSHSSS KSLKSDVSHS PAGTPRRSNL DKGGGSLTNS NKDLNAEEIE APLGFEPEGS
AANSPPFTET PPYLNWAKNF NLLLGDADGV KLFREFLEQE QTVNLLDFWF AVNGLKKQEK
AQETQIIKLI YKKYIRGDTG IQLSGEIRKE IQDKIANKKD IDGAIFDSAQ AEVEDIMRNE
TYQTFLKSDL YVQYLQNGGE SPKGGSSNSS GSNSARPLSV AGPLPTLHED SELLAESIPQ
TTVPIPLTTK SLTATRNTRL DSGFPPFKRP EAVAGLYLQP GGRVPHPYHV SYAPVSAQDS
ELQSLSSDAL TDDTMSLTDS SVDGIPPNRR YWRRHRKQMQ RSAAQNRDTA LSTHLIPRTE
RIKDFKERNI AETDPHRFAS MLIEKLKKVE RERDMQEEFN KKMTLISEGE ESEIELVPKT
AMASNPVFTM LMAQATQEQS DLDNSQSILD EHCSRIWDSS TGQTPSRSPG KQTPSRSKSP
ERAHRRSSGI GAATSLPGTM NRPKTKKDRG DHMSMVSCDS GVSSQEHQAV YYDQDTKTRH
VHHYHHYYHN MHSGKPRQHL EHHAEQRSMA HFHGDQTARS VGDNSGMDLS RGRTRDSGSK
RSGSKKSIDA SSADLQCDSG VSGVDQPPVP DLTNPANEKV MNWILENEKI RQSASTNTDS
ERSTERSSSK RSHHSKPSSS NAQQPHRQSA GSKSKPPVQY NVSRSGSLDR SGISSVINAQ
LAPMHVGRPS QPFAQDPSMP LLPPPNATTQ LEEARRRLEN EAHARQLAKE LAKGSRTCNT
GMPVGRQKYP ASSSVPPTHP LASMQQQVAS GADRPSSAPA PGPATSVPVV AASGTSSQEV
TVVGYYFCSE PIPYRTQLPG KSVTLAQFKS LLTKKGNYRY FFKCASDEFE TGVVHVEVIN
DNAILPLYEG KVVAKVEKVE
//
