ID   WDR26_RAT               Reviewed;         514 AA.
AC   F1LTR1;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 2.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=WD repeat-containing protein 26 {ECO:0000250|UniProtKB:Q9H7D7};
GN   Name=Wdr26;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=22448652; DOI=10.3109/10715762.2012.678840;
RA   Feng Y., Zhang C., Luo Q., Wei X., Jiang B., Zhu H., Zhang L., Jiang L.,
RA   Liu M., Xiao X.;
RT   "A novel WD-repeat protein, WDR26, inhibits apoptosis of cardiomyocytes
RT   induced by oxidative stress.";
RL   Free Radic. Res. 46:777-784(2012).
RN   [3]
RP   FUNCTION.
RX   PubMed=27797717; DOI=10.1093/abbs/gmw104;
RA   Feng Y., Zhao J., Hou H., Zhang H., Jiao Y., Wang J., Wang Y., Sun Y.;
RT   "WDR26 promotes mitophagy of cardiomyocytes induced by hypoxia through
RT   Parkin translocation.";
RL   Acta Biochim. Biophys. Sin. 48:1075-1084(2016).
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
CC       selectively accepts ubiquitin from UBE2H and mediates ubiquitination
CC       and subsequent proteasomal degradation of the transcription factor HBP1
CC       (By similarity). Acts as a negative regulator of the canonical Wnt
CC       signaling pathway through preventing ubiquitination of beta-catenin
CC       CTNNB1 by the beta-catenin destruction complex, thus negatively
CC       regulating CTNNB1 degradation (By similarity). 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 (PubMed:22448652). Protects also cells by promoting
CC       hypoxia-mediated autophagy and mitophagy (PubMed:27797717).
CC       {ECO:0000250|UniProtKB:Q9H7D7, ECO:0000269|PubMed:22448652,
CC       ECO:0000269|PubMed:27797717}.
CC   -!- SUBUNIT: Forms homooligomers. Identified in the CTLH complex that
CC       contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or
CC       alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within
CC       this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8,
CC       WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4,
CC       MKLN1, ARMC8 and YPEL5 have ancillary roles. Interacts with DDB1-
CC       CUL4A/B E3 ligase complexes. Forms a complex composed of at least
CC       WDR26, a G-beta:gamma unit, and PLCB2. Interacts with AXIN1.
CC       {ECO:0000250|UniProtKB:Q9H7D7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H7D7}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9H7D7}. Mitochondrion
CC       {ECO:0000269|PubMed:22448652}.
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DR   EMBL; AABR07021932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F1LTR1; -.
DR   SMR; F1LTR1; -.
DR   STRING; 10116.ENSRNOP00000005059; -.
DR   jPOST; F1LTR1; -.
DR   PaxDb; F1LTR1; -.
DR   RGD; 1565589; Wdr26.
DR   VEuPathDB; HostDB:ENSRNOG00000003723; -.
DR   eggNOG; KOG0293; Eukaryota.
DR   HOGENOM; CLU_000288_57_25_1; -.
DR   InParanoid; F1LTR1; -.
DR   OMA; YCKFSPD; -.
DR   TreeFam; TF314869; -.
DR   PRO; PR:F1LTR1; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000003723; Expressed in esophagus and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0034657; C:GID complex; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0000151; C:ubiquitin ligase complex; ISO:RGD.
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; IPR020472; G-protein_beta_WD-40_rep.
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; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Mitochondrion; Nucleus; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..514
FT                   /note="WD repeat-containing protein 26"
FT                   /id="PRO_0000442421"
FT   DOMAIN          9..84
FT                   /note="CTLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT   REPEAT          206..245
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          252..291
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          297..337
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          377..416
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          419..461
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          464..504
FT                   /note="WD 6"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   514 AA;  58490 MW;  44F23D178278AFCA CRC64;
     MQKAGCRLEH PSATKFRNHV MEGDWDKAEN DLNELKPLVH SPHAIVVRGA LEISQTLLGI
     IVRMKFLLLQ QKYLEYLEDG KVLEALQVLR CELTPLKYNT ERIHVLSGYL MCSHAEDLRA
     KAEWEGKGAA SRSKLLDKLQ TYLPPSVMLP PRRLQTLLRQ AVELQRDRCL YHNTKLDNNL
     DSVSLLIDHV CSRRQFPCYT QQILTEHCNE VWFCKFSNDG TKLATGSKDT TVIVWQVDAD
     THLLKLLKTL EGHAYGVSYI AWSPDDSYLV ACGPDDCSEL WLWNVQTGEL RTKMSQSHED
     SLTSVAWNPD GKRFVTGGQR GQFYQCDLDG NLLDSWEGVR VQCLWCLSDG KTVLASDTHQ
     RIRGYNFEDL TDRNIVQEDH PIMSFTISKN GRLALLNVAT QGVHLWDLQD RVLVRKYQGV
     TQGFYTIHSC FGGHNEDFIA SGSEDHKVYI WHKRSELPIA ELTGHTRTVN CVSWNPQIPS
     MMASASDDGT VRIWGPAPFI DHQNIEEECS SMDS