ID M4AIA6_XIPMA Unreviewed; 603 AA.
AC M4AIA6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Segment polarity protein dishevelled homolog DVL-3 {ECO:0000313|Ensembl:ENSXMAP00000014200.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000014200.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000014200.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000014200.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the DSH family. {ECO:0000256|ARBA:ARBA00008735}.
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DR AlphaFoldDB; M4AIA6; -.
DR STRING; 8083.ENSXMAP00000014200; -.
DR Ensembl; ENSXMAT00000014219.2; ENSXMAP00000014200.2; ENSXMAG00000014155.2.
DR eggNOG; KOG3571; Eukaryota.
DR GeneTree; ENSGT00950000182903; -.
DR HOGENOM; CLU_012601_1_0_1; -.
DR InParanoid; M4AIA6; -.
DR OMA; HYSVHEE; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd04438; DEP_dishevelled; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.240.130; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR024580; Dishevelled_C-dom.
DR InterPro; IPR008339; Dishevelled_fam.
DR InterPro; IPR003351; Dishevelled_protein_dom.
DR InterPro; IPR001158; DIX.
DR InterPro; IPR038207; DIX_dom_sf.
DR InterPro; IPR015506; Dsh/Dvl-rel.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10878; SEGMENT POLARITY PROTEIN DISHEVELLED; 1.
DR PANTHER; PTHR10878:SF6; SEGMENT POLARITY PROTEIN DISHEVELLED HOMOLOG DVL-3; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF02377; Dishevelled; 1.
DR Pfam; PF00778; DIX; 1.
DR Pfam; PF12316; Dsh_C; 1.
DR Pfam; PF00595; PDZ; 1.
DR PRINTS; PR01760; DISHEVELLED.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50841; DIX; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Signal {ECO:0000256|SAM:SignalP};
KW Wnt signaling pathway {ECO:0000256|PROSITE-ProRule:PRU00069}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..603
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017473982"
FT DOMAIN 1..50
FT /note="DIX"
FT /evidence="ECO:0000259|PROSITE:PS50841"
FT DOMAIN 216..288
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 367..441
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT REGION 57..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..487
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 65516 MW; 69EA942980EBDA98 CRC64;
MMLVAMMMMI TLMMMMVMVC FRVVKEEISD DEARLPCVNG RVVCWVVSSD ACPPDFRGSD
TPSVATPSSL APPPIERTGG IGDSRPPSFH AAAVCHDDLQ GSEVKSPAPS SEKQRRRGGH
LNGHAHQAAD HKGAGPAGGG DSSSNQQSSE LETTSFCSSE EDSGGRFSQS TGQSSSSPRL
IRRQRRRHRK PKTPRMEKSA SFSSVTDSTM SLNIITVTLN MERYNFLGIS IVGQSNDRGD
GGIYIGSIMK GGAVAADGRI EPGDMLLQVN DINFENMSND DAVRVLREIV HQPGSVTLTV
AKCWDPNPRS CFTLPRSEPV RPIDPAAWVS HTAAMTGKLP PHYSVHEENH LNIHSDMTVV
VKAMANPESG LEVRDRMWLK ITIPNAFIGS DVVDWLHRNI EGFTDRREAR KYAGNLLKAG
FIRHTVNKVT FSEQCYYVFG DLCGDLAAMS LLDHEDGSSR EVGGGTDCDP PAFPYQYPVP
HPYSSPHPLQ QLPACGAGGG RSHHSEGSRS SQSDFSDDQE GKGGTQQESS NQEANAQHKM
ADCLSDGSAQ EPPTSFSGSH GDKDMPTPSR GQHRDFSSIQ PEISRQSFRL AMGNPSDLFV
DVM
//
