WDR81_DANRE
ID WDR81_DANRE Reviewed; 2065 AA.
AC E7FEV0;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=WD repeat-containing protein 81 {ECO:0000250|UniProtKB:Q562E7};
GN Name=wdr81;
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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=27390838; DOI=10.1186/s12868-015-0229-4;
RA Doldur-Balli F., Ozel M.N., Gulsuner S., Tekinay A.B., Ozcelik T., Konu O.,
RA Adams M.M.;
RT "Characterization of a novel zebrafish (Danio rerio) gene, wdr81,
RT associated with cerebellar ataxia, mental retardation and dysequilibrium
RT syndrome (CAMRQ).";
RL BMC Neurosci. 16:96-96(2015).
CC -!- FUNCTION: Functions as a negative regulator of the PI3 kinase/PI3K
CC activity associated with endosomal membranes. By modifying the
CC phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal
CC membranes may regulate endosome fusion, recycling, sorting and early to
CC late endosome transport. May also play a role in aggrephagy, the
CC macroautophagic degradation of ubiquitinated protein aggregates. May
CC also be involved in maintenance of normal mitochondrial structure and
CC organization. {ECO:0000250|UniProtKB:Q562E7,
CC ECO:0000250|UniProtKB:Q5ND34}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q562E7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q562E7}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q562E7}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q562E7}. Cytoplasmic vesicle, autophagosome
CC membrane {ECO:0000250|UniProtKB:Q562E7}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q562E7}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q562E7}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:27390838}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed at 5 and 15 hpf. Expression is
CC higher in brain and eye. The expression drops after 72 hpf.
CC {ECO:0000269|PubMed:27390838}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR81 family. {ECO:0000305}.
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DR EMBL; CU861670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002664681.1; XM_002664635.4.
DR RefSeq; XP_005157714.1; XM_005157657.3.
DR AlphaFoldDB; E7FEV0; -.
DR SMR; E7FEV0; -.
DR STRING; 7955.ENSDARP00000129633; -.
DR PaxDb; E7FEV0; -.
DR PeptideAtlas; E7FEV0; -.
DR Ensembl; ENSDART00000156621; ENSDARP00000129633; ENSDARG00000079702.
DR Ensembl; ENSDART00000182609; ENSDARP00000151363; ENSDARG00000079702.
DR GeneID; 100333062; -.
DR KEGG; dre:100333062; -.
DR CTD; 124997; -.
DR ZFIN; ZDB-GENE-030131-3389; wdr81.
DR eggNOG; KOG1786; Eukaryota.
DR eggNOG; KOG4190; Eukaryota.
DR GeneTree; ENSGT00930000151039; -.
DR HOGENOM; CLU_001454_0_0_1; -.
DR InParanoid; E7FEV0; -.
DR OMA; AYEQFTP; -.
DR OrthoDB; 101142at2759; -.
DR PhylomeDB; E7FEV0; -.
DR TreeFam; TF323353; -.
DR Reactome; R-DRE-9013148; CDC42 GTPase cycle.
DR PRO; PR:E7FEV0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 15.
DR Bgee; ENSDARG00000079702; Expressed in white matter and 42 other tissues.
DR GO; GO:0000421; C:autophagosome membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0031313; C:extrinsic component of endosome membrane; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0035014; F:phosphatidylinositol 3-kinase regulator activity; ISS:UniProtKB.
DR GO; GO:0035973; P:aggrephagy; ISS:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR GO; GO:0043551; P:regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd06071; Beach; 1.
DR Gene3D; 1.10.1540.10; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR000409; BEACH_dom.
DR InterPro; IPR036372; BEACH_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF02138; Beach; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM01026; Beach; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81837; SSF81837; 1.
DR PROSITE; PS50197; BEACH; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; Endosome; Lysosome; Membrane;
KW Mitochondrion; Reference proteome; Repeat; Transit peptide; WD repeat.
FT CHAIN 1..2065
FT /note="WD repeat-containing protein 81"
FT /id="PRO_0000441869"
FT DOMAIN 325..617
FT /note="BEACH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00026"
FT REPEAT 1767..1806
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 1813..1853
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 1906..1945
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 1948..1986
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 2035..2065
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REGION 1082..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1595..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2065 AA; 228484 MW; 5E691A28BD594465 CRC64;
MEWLAPALER DLGIDQRQTA HSQRPNELVV LVPTRWVMAL RNKRVTRCAK YESFSEGEIC
TLLQRSQMKL PSGWTRVCIQ GLRKRKLGYR FARETGCHGE GLSQDSFMTL MQGVSQSNFR
NLWHEAYMTH VQPYADSVEQ TPVLALDAVR QALQKLFCSN FISTDRVSPS LSPAKEKEKD
CPFLSTCSAP KQSTESLCPN VLPAECLLES EEVLYVVFPY TQYTVHDIVT YSPAKLANSN
AKILFILYQL LIAMRECHAS GLLCGELSLL DIAVDEQLCS RLKISLAHYE KFKEYRDAVP
YALQNKVPMS VSTKDNHNNG VSGQLCRNCQ DELKSLVLDW VNGQVSNFQY LMELNRLAGR
REGDPNYHPV LPWVVDFTVP YGRFRDLKKS KFRLNKGDKQ LDFTYEMTKE ALAAVSGSGG
SNYPPDLGGP VVPGGPGQSD HLHVPHHISD VLSDITYYVY KARQTPKSVL CSHVRSQWEP
NEYPASMERI QSWTPDECIP EFYRDPSIFR SIHPDMPDLD VPPWCNSYEE FIAVHRQLLE
SREVSQQLHH WIDLTFGYKL SGKEAIKAKN VCLHLVDNHT HLTSYGVVQL FDHPHPPRLA
LYQYAPPEPP HFGRVNVTTW QIPPLETTMD GVDGLVPEAT GCESSGWSVV GRDEELEQAI
EALDLSGSSS STSASVSIPV VGSAAGKTSG ETIGLVVSPS HGSFPGEATG NVTNTLGSGI
RTAMLHRAAS VSKKPEASNL EDFKISLPDG FKPLQPLEEL EKLNTFLVKG LHSEIEHTMD
LGINKKDLRS VPKVPLSFTD LFQRDMQALG VLIAEIFYSS KLRGLRPETH LRDRFQAVLK
LCSTNLRDVP LPLHHALDTL LQVHKHCLKT ETIIMHPQGL PFLFKYDPIC EGLPPPNPWQ
LLSPIVSPLP FPEYFPTLHK FIFSYHSKME SINNIQGRDI VFNLWQQLET LLKGDITTEG
LEILLPFVLS LMSEESTAVY AAWYLFEPVS RVLGPRNASK YLIKPLVGVY ENPRCLRGRF
YLYTDCFVLQ LIVRLGLQVF LSSLLPHVLQ VMTGFESCNT AAGTEWEGMK VLRGAAGALD
EEEEEYECDD RRSSNATSSG KVGGGSGGGS GGVGVVGDQG LVDYSSGISL NDQVFLNEGE
DFQNGFYVNN SASGATTVGT KQQNQSTANK DQDQESLSVG KLSDKSSASE VSIGDRASLK
SADSSQDLKQ ASDGEDGGEL EDEEETVEDR EITVQRVPSL EMTLSVCTEE SEATVATLEG
DVMNGIVQED GEKNMEEEET EHDPLEDSEE KEHKILLDTV CKTVRWLSAK LGPTLTSRFI
ARNLLRLLTS CYIGLDKHQF MLSVNEENSL ECVGSVYEKK PVVGDQTARP VLECLIYIAH
LYGEPVLTYQ YLPYIGYLVS PPSSCRLNTR KEAGLLGAVV LTQKIIVFLS DTTLMDMLMK
INQEVLLPLL DLLTSTKMGF PSGVQTRSAV CLKTLSLMAL ICLRIGREMV QQHMAETLSR
FFQVFSLLQF LQNQIGSAPR REVAECTYLD LRIPDGAELT IELGVLEELQ AVFNPEMAYA
SYIPFYCLIG DSGIRKLVTN HELVWSLAQS YHERASPGSP ESNPVGGQRA SAVGLSPSMG
RQMSRSPFPA PSSTSTPLGG DILPESGTFG SHLVGNRIQV TRDTEACGSP NLSSLETWTH
GRPYGSNAPP MSLATTALSS AGPSFSHSSY SWVMGPTPED SALKQDLPRS SRSLQGNWLA
YWQYEIGLNQ QDSHFHFHQI RLQSFIGHSG TAKCLAPLAG EDYFLSGSKD KTVRLWPLYN
HGDGTREVEP RLTYTEHRKS IFYVGQLEAL QEVVSCDGTV HLWDQFTGKN IRCNEPLDGK
NPITAVTTMP APHCSVVFAS ADSVLRFIDP RKPGLQHEFR LAYSNLSAGL IRCLAVSPGG
RTIAAGFSTG FIVLLDARTG LVLRGWPGHE GDILQMKAAE GNLLVSSSSD HTLTVWKDVE
HKPLHQYRTP SDPIHAFDLY GAEIVAGTVA NKIGVYSILD STASLAGSTK LSTENFRGTL
TSLSVLPTKR LLLLGSDNGA IRLLA
