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Database: UniProt
Entry: A0A3B4F4B4_9CICH
LinkDB: A0A3B4F4B4_9CICH
Original site: A0A3B4F4B4_9CICH 
ID   A0A3B4F4B4_9CICH        Unreviewed;       737 AA.
AC   A0A3B4F4B4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Axin-2-like {ECO:0000313|Ensembl:ENSPNYP00000005397.1};
GN   Name=AXIN2 {ECO:0000313|Ensembl:ENSPNYP00000005397.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000005397.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000005397.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   AlphaFoldDB; A0A3B4F4B4; -.
DR   STRING; 303518.ENSPNYP00000005397; -.
DR   Ensembl; ENSPNYT00000005538.1; ENSPNYP00000005397.1; ENSPNYG00000004181.1.
DR   GeneTree; ENSGT00940000157338; -.
DR   Proteomes; UP000261460; 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   CDD; cd11582; Axin_TNKS_binding; 1.
DR   CDD; cd08707; RGS_Axin; 1.
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:SF1; AXIN-2; 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   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|PROSITE-
KW   ProRule:PRU00069}.
FT   DOMAIN          86..205
FT                   /note="RGS"
FT                   /evidence="ECO:0000259|PROSITE:PS50132"
FT   DOMAIN          655..737
FT                   /note="DIX"
FT                   /evidence="ECO:0000259|PROSITE:PS50841"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          546..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..407
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   737 AA;  81696 MW;  53F598F05DC151DD CRC64;
     MSRALTEHIS SSFREDAPRP PVPGEEGEAS CYNPSRSAKM RAQSKVKDIP AASAPPGSTP
     RRNEDGLGEP EGSASPDSPL VRWTKSLHFL LGDQDGAHLF KTFLERENCV DTLDFWFACN
     GFRQMDLKDT KTLRVAKVIF KRYIENNSIV AKQLKPATKA FIRDSIKKQQ IDSSMFDQAQ
     TEIQSNMEEN AYQMFLTSDI YLEYVRTGCE NAAYMNHGGL GSLKLMCGYL PPLMEEEEWS
     CNDLKAKTLG SVVGLSAKNL RATATIRTAA EVLENSCRSH RRGDPASPYF VNSGYIFAPA
     TSANDSEISS DATTDDSMSM TDSSVDGIPP YKLGTKKQLQ REMHRSVKIN GQVTLPHFPR
     THRLPKEMTP VEPSAFAAQL IARLEKLKRE QETMSSLEER LQQIQEEEER EEGNDLISST
     SLQHPLLPSA SQCEEDPQAI LDEHLSRVLK TPGCQSPGVV RHSPRSRSPD RTGAVVSSGH
     GPFFGAYPGA SKVLMTGRQS TKHIHHHYIH HHHAGPKTKE QIEAEAAQRV QCLCPQGGAN
     YSDFTPATQG LKKSNPLDSK TLPGRTSSSW GGGGIGNGAH LRGHHPGHPF IQDPAMPPLP
     PPNTLAQLEE ACRRLEEVSK PPKQSNLQRD RNHPAAVFPT GSNSLASPGV QADESKELVV
     TYFFCGEEIP YRSMMKTHCL TLGHFKEQLS KKGNYRYYFK KASDEFECGA VFEEVWEDAT
     VLPMYEGKVL GKVERMD
//
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