ID A0A2U9BNE5_SCOMX Unreviewed; 891 AA.
AC A0A2U9BNE5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Axin-1 {ECO:0000256|ARBA:ARBA00013892};
DE AltName: Full=Axis inhibition protein 1 {ECO:0000256|ARBA:ARBA00032466};
GN ORFNames=SMAX5B_011353 {ECO:0000313|EMBL:AWP05330.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP05330.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP05330.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CP026250; AWP05330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BNE5; -.
DR STRING; 52904.ENSSMAP00000001170; -.
DR Proteomes; UP000246464; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; 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 CDD; cd11582; Axin_TNKS_binding; 1.
DR CDD; cd08707; RGS_Axin; 1.
DR Gene3D; 1.10.196.10; -; 2.
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:SF3; AXIN-1; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|PROSITE-
KW ProRule:PRU00069}.
FT DOMAIN 118..236
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 809..891
FT /note="DIX"
FT /evidence="ECO:0000259|PROSITE:PS50841"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 421..458
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 49..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 97962 MW; FF8CBB8CDDD89955 CRC64;
MSVVREIHGI GYRGGGGGGV VASLSGPSHF TEDAPRPPVP GEEGSDVDPP VQSANTRPNT
LSQTLGYPPS SSISKMGDPS SYTPSSSSAT PRRPDLDLGY EPEGSASPTP PYLKWAESLH
SLLDDQEGIQ LFRNFLCQEG CADLLDFWFA CSGFRKTSQD KRAKLAKAIY RKYIVDGSGI
VSRQIKAATK SFIRDCVGRP HPDPAMFEQA QTEIQAMMEE NTYPLFLKSD LYLEYTRTGG
ESPKPNPSDQ SPSSGPAKPV PGYLPTLAED EEWRCGGGGV REEEEDEKDE DECGDTPAGR
LTHSLLMPTA PQRVSTSRRR QDSREYRHWR EPVNPYYANM GYARAPATSA NDSEQQSMSS
DADTLSLPDS SVDGIPPYRY RKQHRKEMHE SAKANGRVPL PHIPRTYRMP KDIHVEPERF
AAELISRLET VLREREAQER LEERLKRVRL EEEGDEADIS VATSMSSHSI PLPLPSSFPP
LYGARYSETT ANTATVATYG GLVAMEDSQD DDPESILDEH VSRVMKTPGC QSPGATNSTL
GGVGGRHSPP KSSRSPDGGI GPPHYPPHRG GGHSLPPAGV KGTHHHKPPY HHRGREGQEE
AGSRAQPNFL WNGDPAGQYA GRSRNYADGA GASTIEGMGY SSKGSTLSRR GCKKTSETSG
KGDESGRGME TQVPLEDLER NQKILQWMME GDRQRKTTHG GSTSSSRRTG ASSESPRPTS
VERPGAVHPW VSAQLRNNPS SVSTAIPGSS STQVQPSHPF IQDPAMPPNP APNPLTQLEE
ARRRLEEERR RNALQQAKQR HKSGKRQGSE NMTVAYYFCG EPIPYRTSVK GRVVTLGQFK
ELLTKKGHYR FYFKKVSDEF DCGVVFEEVR DDEAVLPIFE EKIIGKVEKV D
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