WDR81_RAT
ID WDR81_RAT Reviewed; 1933 AA.
AC D4A929;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=WD repeat-containing protein 81 {ECO:0000312|RGD:1311334};
GN Name=Wdr81 {ECO:0000312|RGD:1311334};
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].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q562E7, ECO:0000250|UniProtKB:Q5ND34}.
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:0000250|UniProtKB:Q562E7}.
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 -!- SIMILARITY: Belongs to the WD repeat WDR81 family. {ECO:0000305}.
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DR EMBL; CH473948; EDM05212.1; -; Genomic_DNA.
DR RefSeq; NP_001127832.1; NM_001134360.1.
DR AlphaFoldDB; D4A929; -.
DR SMR; D4A929; -.
DR STRING; 10116.ENSRNOP00000004365; -.
DR jPOST; D4A929; -.
DR PaxDb; D4A929; -.
DR PeptideAtlas; D4A929; -.
DR PRIDE; D4A929; -.
DR GeneID; 303312; -.
DR KEGG; rno:303312; -.
DR CTD; 124997; -.
DR RGD; 1311334; Wdr81.
DR VEuPathDB; HostDB:ENSRNOG00000003243; -.
DR eggNOG; KOG1786; Eukaryota.
DR eggNOG; KOG4190; Eukaryota.
DR HOGENOM; CLU_001454_0_0_1; -.
DR InParanoid; D4A929; -.
DR OMA; AYEQFTP; -.
DR OrthoDB; 101142at2759; -.
DR PhylomeDB; D4A929; -.
DR TreeFam; TF323353; -.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR PRO; PR:D4A929; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000003243; Expressed in spleen and 18 other tissues.
DR Genevisible; D4A929; RN.
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; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
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:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
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; IPR011009; Kinase-like_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; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF56112; SSF56112; 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 3: Inferred from homology;
KW Cytoplasm; Cytoplasmic vesicle; Endosome; Lysosome; Membrane;
KW Mitochondrion; Reference proteome; Repeat; Transit peptide; WD repeat.
FT CHAIN 1..1933
FT /note="WD repeat-containing protein 81"
FT /id="PRO_0000418625"
FT DOMAIN 333..610
FT /note="BEACH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00026"
FT REPEAT 1638..1677
FT /note="WD 1"
FT REPEAT 1684..1724
FT /note="WD 2"
FT REPEAT 1776..1815
FT /note="WD 3"
FT REPEAT 1818..1856
FT /note="WD 4"
FT REPEAT 1903..1933
FT /note="WD 5"
FT REGION 1..643
FT /note="Necessary and sufficient for the interaction with
FT SQSTM1"
FT /evidence="ECO:0000250|UniProtKB:Q562E7"
FT REGION 305..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1517..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1565..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1168
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1933 AA; 212260 MW; F10A45EFE0C1C478 CRC64;
MAQGSRRRKV VLTAGAEGCS SSSGPDMEEL LRCAERDLNI DARQLALAPG GTHVVALVST
RWLASLRERR LGPCPRAEGL GEAEVRTLLQ RSVQRLPQGW TRVEVHGLRK RRLSYPLSRV
LPFEEGSCSP ETLTRFMQEV AAQNYRNLWR HAYHTYGQPY SHSTAPSAIP ALDSIRQALQ
RVYGCTFLPV GESMQCLSNV RDGPSRGSSA CPSLLRAEAL LESPEMLYVV HPYVQFSLHD
VVTFSPAKLT NSQAKVLFIL FRVLRAMDAC HRQGLACGAL SLHHIAVDEK LCSELRLDLS
AYEMPSEDEN QEVSEEKDRT GVKSEKDGEG RPGCPTCQKE LRGLVLDWVH GRVSNFYYLM
QLNRLAGRRQ GDPNYHPVLP WVVDFTTPYG RFRDLRKSKF RLNKGDKQLD FTYEMTRQAF
VAGGAGSGEP LHVPHHISDV LSDITYYVYK ARRTPRSVLC GHVRAQWEPH EYPATMERMQ
TWTPDECIPE FYTDPSIFCS IHPDMPDLDV PAWCSSNQEF VTAHRALLES WEVSQDLHHW
IDLTFGYKLQ GKEAVKEKNV CLHLVDAHTH LTSYGVVQLF DQPHPQRLAG APALAPEPPL
IPRLLVQPIQ EATGQEDISG QLINGAGRHV VEVTPCESGW TRERPTAGED DLEQATEALD
SISIPGKAGD QPGSSSSQAS PGLLPFSAPS GSRPGRRSKA TGLDSGEGDE GKIVLPEGFS
PIQALEELEK VGNFLARGLG SQLEEPEKPQ AQPPVYLQSL FHRDMQVLGV LLAEMVFATR
VRILQPDAPL WVRFEAVRGL CTRHSKDIPV SLQPVLDTLL QLSGPKSPLV VKKGKLDPLF
EYRPVSQGLP PPSPAQLLSP FSSVVPFPTY FPALHKFILL YQARRVEDEV QGRELVFALW
QQLGAVLNEI TPEGLEILLP FVLSLMSEEH TAVYTAWYLF EPVAKALGPK NTIKYLLKPL
IGAYENPCRL HGRFYLYTDC FVAQLVVRLG LQAFLIHLLP HVLQVLAGVE ASQEEGKGLV
GTTEDEENEL PVPGPGSCAF GEEIQMGGQP AASSGLGLPD YRSGVSFHDQ ADLPDTEDFQ
AGLYVAESPQ PQEAEAVSLG QLSDKSSTSE ASQGEERGGD DGGAPVDKNS VKSGDSSQDL
KQSEGSEEEE EEEEGCVVLE EEEQDEVTGT SELTLSDTIL SMETVVAPGD GRDREEEEEP
LPEQTEGKEQ KILLDTACKM VRWLSAKLGP TVASRHVARN LLRLLTSCYV GPTRQQFTVS
CDDSPPLNAG NIYQKRPVLG DIVSGPVLSC LLHIAHLYGE PVLTYQYLPY ISYLVAPGSN
SSPSRLNSRK EAGLLAAVTL TQKIIVYLSD TTLMDILPRI SHEVLLPVLS FLTSFVTGFP
SGAQARTVLC VKTISLIALI CLRIGQEMVQ QHLSEPVATF FQVFSHLHEL RQQDLQLDLK
GCTEGQLPEA TFSDGQRRPV DPTLLEELQK VFTLEMAYTI YVPFSCLLGD IIRKIIPNHE
LVGELAGLYL ESMSPSSLRN PASMEPVTPS AGPEWNPQSG SCLQDDGHSG TFGSVLVGNR
IQIPDSQPQS SGPLGSISGV GSGGLSSRNE DNALKRELPR SAHGLSGNWL AYWQYEIGVS
QQDAHFHFHQ IRLQSFPGHT GAVKCVAALS SEDFFLSGSK DRTVRLWPLY NYGDGTSETA
PRLIYAQHRK SVFYVGQLEA PQYVVSCDGA VHVWDPFTGK TLRTVDPSDS RVPLTAVAVM
PAPHTSITMA SSDSTLRFVD CRKPGLQHEF RLGGGLNPGL VRSLAVSPSG RSVVAGFSSG
FMVLLDTRTG LVLRGWPAHE GDILQIKAVE GSVIVSSSSD HSLTVWKELE QKPTHHYKSA
SDPIHTFDLY GSEVVTGTVA NKIGVCSLLE PPSQATTKLS SENFRGTLTS LALLPTKRHL
LLGSDNGIIR LLA
