ID A0A663MJQ0_ATHCN Unreviewed; 1911 AA.
AC A0A663MJQ0;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 08-OCT-2025, entry version 25.
DE RecName: Full=WD repeat-containing protein 81 {ECO:0000256|ARBA:ARBA00070555};
GN Name=WDR81 {ECO:0000313|Ensembl:ENSACUP00000012139.1};
OS Athene cunicularia (Burrowing owl) (Speotyto cunicularia).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Strigiformes;
OC Strigidae; Athene.
OX NCBI_TaxID=194338 {ECO:0000313|Ensembl:ENSACUP00000012139.1, ECO:0000313|Proteomes:UP000472269};
RN [1] {ECO:0000313|Ensembl:ENSACUP00000012139.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2025) to UniProtKB.
CC -!- FUNCTION: Functions as a negative regulator of the PI3 kinase/PI3K
CC activity associated with endosomal membranes via BECN1, a core subunit
CC of the PI3K complex. By modifying the phosphatidylinositol 3-
CC phosphate/PtdInsP3 content of endosomal membranes may regulate endosome
CC fusion, recycling, sorting and early to late endosome transport. It is
CC for instance, required for the delivery of cargos like BST2/tetherin
CC from early to late endosome and thereby participates indirectly to
CC their degradation by the lysosome. May also play a role in aggrephagy,
CC the macroautophagic degradation of ubiquitinated protein aggregates. In
CC this process, may regulate the interaction of SQSTM1 with ubiquitinated
CC proteins and also recruit MAP1LC3C. May also be involved in maintenance
CC of normal mitochondrial structure and organization.
CC {ECO:0000256|ARBA:ARBA00058689}.
CC -!- SUBUNIT: Interacts with WDR91; involved in early to late endosome cargo
CC transport. Interacts with BECN1; negatively regulates the PI3
CC kinase/PI3K activity associated with endosomal membranes. Interacts
CC with SQSTM1; the interaction is direct and regulates the interaction of
CC SQSTM1 with ubiquitinated proteins. Interacts with MAP1LC3C; recruits
CC MAP1LC3C to ubiquitinated protein aggregates in the aggrephagy process.
CC {ECO:0000256|ARBA:ARBA00064041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, autophagosome
CC membrane {ECO:0000256|ARBA:ARBA00004652}. Early endosome membrane
CC {ECO:0000256|ARBA:ARBA00004220}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004220}. Late endosome membrane
CC {ECO:0000256|ARBA:ARBA00004414}. Lysosome membrane
CC {ECO:0000256|ARBA:ARBA00004656}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR81 family.
CC {ECO:0000256|ARBA:ARBA00060735}.
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DR RefSeq; XP_026717180.1; XM_026861379.1.
DR Ensembl; ENSACUT00000012961.1; ENSACUP00000012139.1; ENSACUG00000008197.1.
DR GeneID; 113487021; -.
DR CTD; 124997; -.
DR OMA; AYEQFTP; -.
DR OrthoDB; 29306at2759; -.
DR Proteomes; UP000472269; Unplaced.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0035014; F:phosphatidylinositol 3-kinase regulator activity; IEA:TreeGrafter.
DR GO; GO:0035973; P:aggrephagy; IEA:TreeGrafter.
DR CDD; cd06071; Beach; 1.
DR FunFam; 1.10.1540.10:FF:000003; WD repeat-containing protein 81 isoform X1; 1.
DR FunFam; 2.130.10.10:FF:000341; WD repeat-containing protein 81 isoform X1; 1.
DR FunFam; 2.130.10.10:FF:000355; WD repeat-containing protein 81 isoform X1; 1.
DR Gene3D; 1.10.1540.10; BEACH domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR000409; BEACH_dom.
DR InterPro; IPR036372; BEACH_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR052651; WDR81.
DR PANTHER; PTHR44662; WD REPEAT-CONTAINING PROTEIN 81; 1.
DR PANTHER; PTHR44662:SF1; WD REPEAT-CONTAINING PROTEIN 81; 1.
DR Pfam; PF02138; Beach; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM01026; Beach; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF81837; BEACH domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50197; BEACH; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000472269};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 312..588
FT /note="BEACH"
FT /evidence="ECO:0000259|PROSITE:PS50197"
FT REPEAT 1612..1643
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 646..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1498..1523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1117
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1141
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1173
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1911 AA; 211707 MW; ED5999899C11FB6A CRC64;
MDGFLQSVEK DLNIDRRQLA AAPERTHVTA FIPVKWLTSL KERRVLPGLC PRPEGLSDVE
VRTFLQHSVQ KLPAGWTRVE IHGLRKDRLA YPLQVQPPAC DQRNGNAETL HGFMQSVASQ
NYRNLWCRAH CLYVRPYRHA DTPTTVPALD ALRLALQKAY GCPILHVGKS VPGASPAKES
VAAPKGGPSC PNMLQAEALL ESANMLYIIY PYVQYCLHDI VTFSPAKLTN SHAKILFLLF
HVLQAMKACH QAGLACGAFS LRDVAVDEKL CSRLRVNFRE YEGPKKEEAN LEAGLERMSE
QSSAGVQGQE ARCTACQKDL RDLVLQWVHG QVSNFDYLMR LNSLAGRRMG DPNYHPVLPW
VVDFTTKNGK FRDLRKSKFR LNKGDKQLDF TYEMTKQAFV AGGSSGEQLH VPHHISDVLS
DITYYVYTAR RTPKAVLCCH VRSQWEPNEY PASMERMQSW TPDECIPEFY TDPSIFRSIH
PDMPDLDVPS WCSSYEEFIE VHRMLLESRE VSQDLHHWID LTFGYKLLGK DAVKEKNVCL
HLVDNHTHLT TYGVVQLFDQ PHPRRMVGPA YTPAEAPAIA RPLLQNIRET VFLEDIQGQV
TDVVNGLVLE ATPSETTWSG EKPIAGEDDL EQGTEALDSI SATTRAADQP CATVPSAQPS
TLPAYATEGK TSGVRPLRRS KGGAVDQADM KITLPEGFNP LQALEELEKL DNFLVKGLSS
EMQLTEQPWE EPPLGLSDLF QRDMQALGIL VAEIIFAPRI RPSKPDASLL ERFLMVHNLC
RYHPKEIPAP LQHVLHVLLQ LSVPVEKLLK TRLGKATVQL FEYKPISQGL PPPCPTQLLS
PFSSIVPFPT YFPALHKFIF TYQAKKIEDE GQGRELVFQL WQQVEGILSE ITPEGLEILL
PFILSLMSEE NTAVYAAWYL FEPIAKSLGP KNANKYLLKP LIGVYETPCY RHGRFYLYTD
CFVAQLIVRL GLQSFLLNLL PHILQILVGI ESSREESKSL LGTAEDDESG GESPVSCVFG
EEIKMDVEHS SAALDLLDYT SGVSFHDQAY LPESEDFQSG LYVGESLQPQ EQESLSLGRL
SDKSSASEVS LGEDRPADGD SQKDKSSLKS MDSSQDLKQS EDSEEEEEEH DEEEEHDDAT
VDAELTVAVD AGASVDVTLA DDSSEPEDGE GEELPDHSDD KEQTILLDTA CKMVRWLSAK
LGPTVTSRFI ARNLLRLLTS CYVGPTRQQF VPSSDENSPL STGNIYQKRP VLGDQVSKPV
LACLVHVAYL YGEPVLTYQY LPYISYLVAP SGGSGGGRLN SRKEAGLLAA VTLTQKIVVC
LSDTTLMDIL PKISQEVLLP VLGFLTSPAI GFPSGAQARI VLCVKTISLI ALICLRIGQE
MVQQHLSDTV RNFFGAFSLL QELQDQGLTA ESLSSCEVPV MEVPLSDGKL LALDPAVLLE
LQKVFNPEMA YVTYIPFSCL LGDVIRSVVP NHSLVEKLAS LHLENVNPKS LQVVSLEQTP
SAVGSDQETR GTEPFSSHHE DSHSGTFGSV LVGNRIQVPV DTQRECLGLL RLSAGTDGFI
PSSSSEENTL KHDLPRSTHM LCGNWLAYWQ YEIGVSQHDP RFHFHQIKLQ SFSGHSGAIK
CVAPLSSEDF FLSGSKDKTV RLWPLYNYGD GTSEVPPRFT YAEHKKSVFY VSQLEASQHV
VSCDGTVHIW DQFTGKLLRT FDELDSKVPI TAVTTMPPPY HSISVASADS VLRFIDHRKP
GLQHEFRLAS GVSAGLIRCL AVSPNGRSVM AGFSSGFIVL LDTRTGLIMR GWPAHEGDIL
QIKAAEGNVL ISSSSDHSLT VWKELEQKPL HHYKSASEPI HAFDLYGNEV VTGTVANKIG
VYSMLESSAL PISMTKLSSE NFRGTLTSLA VLPTKCHLLL GSDNGVIRLL A
//
