WDR26_MOUSE
ID WDR26_MOUSE Reviewed; 641 AA.
AC Q8C6G8; E9PX83; Q3TK81; Q8C4F3; Q8VDZ6;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=WD repeat-containing protein 26;
GN Name=Wdr26;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-641.
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 156-641.
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Mammary tumor, and Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. 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 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:0000250|UniProtKB:F1LTR1}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC35923.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC113084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK075743; BAC35923.1; ALT_INIT; mRNA.
DR EMBL; AK167116; BAE39264.1; -; mRNA.
DR EMBL; AK167017; BAE39191.1; -; mRNA.
DR EMBL; BC020044; AAH20044.2; -; mRNA.
DR EMBL; BC058601; AAH58601.1; -; mRNA.
DR CCDS; CCDS15583.2; -.
DR RefSeq; NP_663489.4; NM_145514.5.
DR AlphaFoldDB; Q8C6G8; -.
DR SMR; Q8C6G8; -.
DR BioGRID; 230551; 11.
DR IntAct; Q8C6G8; 2.
DR STRING; 10090.ENSMUSP00000124592; -.
DR iPTMnet; Q8C6G8; -.
DR PhosphoSitePlus; Q8C6G8; -.
DR SwissPalm; Q8C6G8; -.
DR EPD; Q8C6G8; -.
DR jPOST; Q8C6G8; -.
DR MaxQB; Q8C6G8; -.
DR PaxDb; Q8C6G8; -.
DR PRIDE; Q8C6G8; -.
DR ProteomicsDB; 297640; -.
DR Antibodypedia; 34639; 97 antibodies from 18 providers.
DR DNASU; 226757; -.
DR Ensembl; ENSMUST00000162819; ENSMUSP00000124592; ENSMUSG00000038733.
DR GeneID; 226757; -.
DR KEGG; mmu:226757; -.
DR UCSC; uc007dxf.2; mouse.
DR CTD; 80232; -.
DR MGI; MGI:1923825; Wdr26.
DR VEuPathDB; HostDB:ENSMUSG00000038733; -.
DR eggNOG; KOG0293; Eukaryota.
DR GeneTree; ENSGT00940000153634; -.
DR InParanoid; Q8C6G8; -.
DR OMA; YCKFSPD; -.
DR OrthoDB; 349428at2759; -.
DR PhylomeDB; Q8C6G8; -.
DR TreeFam; TF314869; -.
DR BioGRID-ORCS; 226757; 9 hits in 75 CRISPR screens.
DR ChiTaRS; Wdr26; mouse.
DR PRO; PR:Q8C6G8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8C6G8; protein.
DR Bgee; ENSMUSG00000038733; Expressed in aortic valve and 250 other tissues.
DR ExpressionAtlas; Q8C6G8; baseline and differential.
DR Genevisible; Q8C6G8; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0034657; C:GID complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
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 1: Evidence at protein level;
KW Cytoplasm; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..641
FT /note="WD repeat-containing protein 26"
FT /id="PRO_0000051374"
FT DOMAIN 103..135
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 136..211
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REPEAT 333..372
FT /note="WD 1"
FT REPEAT 379..418
FT /note="WD 2"
FT REPEAT 424..464
FT /note="WD 3"
FT REPEAT 504..543
FT /note="WD 4"
FT REPEAT 546..588
FT /note="WD 5"
FT REPEAT 591..631
FT /note="WD 6"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 641 AA; 70543 MW; 053BAFF901088CFA CRC64;
MQANGAGGGG GGGGGGQGQT PELACLSAQN GESSPSATSA GDLAHANGLL PAAPSAAGNN
SNSLSVNNGV PGGAAAASAT AAAAQATPEL GSSLKKKKRL SQSDEDVIRL IGQHLNGLGL
NQTVDLLMQE SGCRLEHPSA TKFRNHVMEG DWDKAENDLN ELKPLVHSPH AIVVRGALEI
SQTLLGIIVR MKFLLLQQKY LEYLEDGKVL EALQVLRCEL TPLKYNTERI HVLSGYLMCS
HAEDLRAKAE WEGKGTASRS KLLDKLQTYL PPSVMLPPRR LQTLLRQAVE LQRDRCLYHN
TKLDNNLDSV SLLIDHVCSR RQFPCYTQQI LTEHCNEVWF CKFSNDGTKL ATGSKDTTVI
IWQVDPDTHL LKLLKTLEGH AYGVSYIAWS PDDSYLVACG PDDCSELWLW NVQTGELRTK
MSQSHEDSLT SVAWNPDGKR FVTGGQRGQF YQCDLDGNLL DSWEGVRVQC LWCLSDGKTV
LASDTHQRVR GYNFEDLTDR NIVQEDHPIM SFTISKNGRL ALLNVATQGV HLWDLQDRVL
VRKYQGVTQG FYTIHSCFGG HNEDFIASGS EDHKVYIWHK RSELPIAELT GHTRTVNCVS
WNPQIPSMMA SASDDGTVRI WGPAPFIDHQ NIEEECSSMD S
