ID   WDR26_DANRE             Reviewed;         576 AA.
AC   Q5SP67;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=WD repeat-containing protein 26;
GN   Name=wdr26; ORFNames=si:ch211-153j24.6;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18307296; DOI=10.1021/pr700667w;
RA   Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA   Slijper M., Heck A.J.R.;
RT   "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT   analysis down to a single embryo.";
RL   J. Proteome Res. 7:1555-1564(2008).
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}.
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DR   EMBL; AL929435; CAI11628.1; -; Genomic_DNA.
DR   EMBL; BX004824; CAI11628.1; JOINED; Genomic_DNA.
DR   EMBL; BX004824; CAI12019.1; -; Genomic_DNA.
DR   EMBL; AL929435; CAI12019.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_001189371.1; NM_001202442.1.
DR   RefSeq; XP_009293240.1; XM_009294965.2.
DR   AlphaFoldDB; Q5SP67; -.
DR   SMR; Q5SP67; -.
DR   STRING; 7955.ENSDARP00000036145; -.
DR   iPTMnet; Q5SP67; -.
DR   PaxDb; Q5SP67; -.
DR   Ensembl; ENSDART00000029894; ENSDARP00000036145; ENSDARG00000006812.
DR   Ensembl; ENSDART00000167398; ENSDARP00000132796; ENSDARG00000006812.
DR   GeneID; 564794; -.
DR   KEGG; dre:564794; -.
DR   CTD; 564794; -.
DR   ZFIN; ZDB-GENE-041014-277; wdr26b.
DR   eggNOG; KOG0293; Eukaryota.
DR   GeneTree; ENSGT00940000153634; -.
DR   InParanoid; Q5SP67; -.
DR   OMA; KHEFIRI; -.
DR   OrthoDB; 349428at2759; -.
DR   PhylomeDB; Q5SP67; -.
DR   TreeFam; TF314869; -.
DR   PRO; PR:Q5SP67; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 20.
DR   Bgee; ENSDARG00000006812; Expressed in mature ovarian follicle and 26 other tissues.
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; -; 2.
DR   InterPro; IPR006595; CTLH_C.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
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   PRINTS; PR00320; GPROTEINBRPT.
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   1: Evidence at protein level;
KW   Cytoplasm; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; WD repeat.
FT   CHAIN           1..576
FT                   /note="WD repeat-containing protein 26"
FT                   /id="PRO_0000280737"
FT   DOMAIN          51..83
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   DOMAIN          84..143
FT                   /note="CTLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT   REPEAT          265..304
FT                   /note="WD 1"
FT   REPEAT          311..350
FT                   /note="WD 2"
FT   REPEAT          356..396
FT                   /note="WD 3"
FT   REPEAT          436..475
FT                   /note="WD 4"
FT   REPEAT          478..520
FT                   /note="WD 5"
FT   REPEAT          523..563
FT                   /note="WD 6"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
SQ   SEQUENCE   576 AA;  64628 MW;  6D2D52B0D06373C9 CRC64;
     MQSNGTGQEQ NHPANTQNGD ANGLQSNAGS ASGASGTGSG SLKKKKRLSQ AEEDVIRLIG
     QHLHGLGLNQ TVDLLMQESG CRLEHSSATK FRNHVMEGEW DKAENDLNEL KALMHSPNAI
     VRMKFLLLQQ KYLEYLEDGK VLEALQVLRG ELTPLKYNTD RIHVLSGYLM CSHAEDLKAK
     AEWEGKGAGS RCRLLDKLQT YLPPSVMLPP RRLQTLLRQA VELQRDRCLY HNTKLDSSLD
     SVSLLLDHVC SRKQFPCYTQ QILTEHCNEV WFCKFSNDGT KLATGSKDTT VIIWQVEPDT
     HQLKLLRTLE GHAYGVSYLA WSPDDVYLIA CGPDDCSELW LWNVQTGELR TKMSQSHEDS
     LTSVAWNPDG KRFVTGGQRG QFYQCDLDGN LLESWEGVRV QCLWCMGDGR TVLASDTHQR
     IRGYSFEDLT DRNIVQEDHP IMSFTVSKNG RLALLNVATQ GVHLWDLQDR VLVRKYQGVT
     QGFYTIHSCF GGHNEDFIAS GSEDHKVYIW HKRSELPIVE LTGHTRTVNC VSWNPCIPSL
     MASASDDGTV RIWGPAPFLD AQELDGLTES CSSMDS