ID   WDR26_XENTR             Reviewed;         614 AA.
AC   Q28D01;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=WD repeat-containing protein 26;
GN   Name=wdr26; ORFNames=TGas059a07.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: G-beta-like protein involved in cell signal transduction.
CC       Acts as a negative regulator in MAPK signaling pathway. Functions as a
CC       scaffolding protein to promote G beta:gamma-mediated PLCB2 plasma
CC       membrane translocation and subsequent activation in leukocytes. Core
CC       component of the CTLH E3 ubiquitin-protein ligase complex that mediates
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins (By similarity). Acts as a negative regulator of the canonical
CC       Wnt signaling pathway through preventing ubiquitination of beta-catenin
CC       CTNNB1 by the beta-catenin destruction complex, thus negatively
CC       regulating CTNNB1 degradation. Serves as a scaffold to coordinate
CC       PI3K/AKT pathway-driven cell growth and migration. Protects cells from
CC       oxidative stress-induced apoptosis via the down-regulation of AP-1
CC       transcriptional activity as well as by inhibiting cytochrome c release
CC       from mitochondria (By similarity). Protects also cells by promoting
CC       hypoxia-mediated autophagy and mitophagy (By similarity).
CC       {ECO:0000250|UniProtKB:F1LTR1, ECO:0000250|UniProtKB:Q9H7D7}.
CC   -!- SUBUNIT: Forms homooligomers. Identified in the CTLH complex that
CC       contains at least MAEA, RMND5A (or alternatively its paralog RMND5B),
CC       GID8, WDR26, and RANBP9 and/or RANBP10. Interacts with DDB1-CUL4A/B E3
CC       ligase complexes. {ECO:0000250|UniProtKB:Q9H7D7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H7D7}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9H7D7}. Mitochondrion
CC       {ECO:0000250|UniProtKB:F1LTR1}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAJ81593.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR855782; CAJ81593.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001039080.1; NM_001045615.1.
DR   AlphaFoldDB; Q28D01; -.
DR   SMR; Q28D01; -.
DR   STRING; 8364.ENSXETP00000017750; -.
DR   PaxDb; Q28D01; -.
DR   DNASU; 733878; -.
DR   GeneID; 733878; -.
DR   KEGG; xtr:733878; -.
DR   CTD; 80232; -.
DR   Xenbase; XB-GENE-993726; wdr26.
DR   eggNOG; KOG0293; Eukaryota.
DR   InParanoid; Q28D01; -.
DR   OrthoDB; 349428at2759; -.
DR   Proteomes; UP000008143; Chromosome 5.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0034657; C:GID complex; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR006595; CTLH_C.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 5.
DR   SMART; SM00668; CTLH; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50897; CTLH; 1.
DR   PROSITE; PS50896; LISH; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Mitochondrion; Nucleus; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..614
FT                   /note="WD repeat-containing protein 26"
FT                   /id="PRO_0000280738"
FT   DOMAIN          67..99
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   DOMAIN          100..184
FT                   /note="CTLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT   REPEAT          306..345
FT                   /note="WD 1"
FT   REPEAT          352..391
FT                   /note="WD 2"
FT   REPEAT          397..437
FT                   /note="WD 3"
FT   REPEAT          477..516
FT                   /note="WD 4"
FT   REPEAT          519..561
FT                   /note="WD 5"
FT   REPEAT          564..604
FT                   /note="WD 6"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   614 AA;  68362 MW;  49A52349CEAB8BD5 CRC64;
     MQANGAAAAA AGEEPAGSGC LSAHNGESSE PAHSNGVLSS NNGLSGTGST GPTEQPGGRK
     KKRLSQADED VIRLIGQHLH GLGLNQTVDL LMQESGCRLE HPSATKFRNH VMEGEWDKAE
     NDLNELKSLV HSPHAVAACR PSSGGSGSEH SPTSCPTADV IRRMKFLLLQ QKYLEYLEDG
     KVLEALQVLR CELTPLKYNT ERIHVLSGYL MCSHADDLRA KAEWEGKGTA SRSKLLDKLQ
     TYLPPSVMLP PRRLQTLLRQ AVELQRDRCL YHNTKLDNNL DSVSLLIDHV CSRKQFPCFT
     QQVLTEHCNE VWFCKFSNDG TKLATGSKDT TVIIWQVDPD THQLKLLKTL EGHAYGVSYL
     AWSPDDNYLI ACGPDDCSEL WLWNVQTGEL RTKMSQSHED SLTSVAWNPD GKRFVTGGQR
     GQFYQCDLDG NLLDSWEGVR VQCLWCLSDG KTVLASDTHQ RIRGYNFEDL TDRNIVQEDH
     PIMSFTISRN GRLALLNVAT QGVHLWDLQD RVLVRKYQGV TQGFYTIHSC FGGHNEDFIA
     SGSEDHKVYV WHKRSELPIA ELTGHTRTVN CVSWNPQIPS LMASASDDGT VRIWGPAPYV
     DNQEFEEECS SMNS