WDR91_BOVIN
ID WDR91_BOVIN Reviewed; 746 AA.
AC Q2HJE1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=WD repeat-containing protein 91 {ECO:0000250|UniProtKB:A4D1P6};
GN Name=WDR91 {ECO:0000250|UniProtKB:A4D1P6};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-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 play a role in meiosis.
CC {ECO:0000250|UniProtKB:A4D1P6, ECO:0000250|UniProtKB:Q7TMQ7}.
CC -!- SUBUNIT: Interacts with WDR81; involved in early to late endosome cargo
CC transport. Interacts with BECN1; negatively regulates the PI3
CC kinase/PI3K activity associated with endosomal membranes.
CC {ECO:0000250|UniProtKB:A4D1P6}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:A4D1P6}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:A4D1P6}. Late endosome membrane
CC {ECO:0000250|UniProtKB:A4D1P6}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR91 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC105528; AAI05529.1; -; mRNA.
DR EMBL; DV825576; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001039948.1; NM_001046483.1.
DR AlphaFoldDB; Q2HJE1; -.
DR SMR; Q2HJE1; -.
DR STRING; 9913.ENSBTAP00000023798; -.
DR iPTMnet; Q2HJE1; -.
DR PaxDb; Q2HJE1; -.
DR PRIDE; Q2HJE1; -.
DR GeneID; 540606; -.
DR KEGG; bta:540606; -.
DR CTD; 29062; -.
DR eggNOG; KOG1333; Eukaryota.
DR HOGENOM; CLU_022078_0_0_1; -.
DR InParanoid; Q2HJE1; -.
DR OrthoDB; 321271at2759; -.
DR TreeFam; TF317339; -.
DR Proteomes; UP000009136; Unplaced.
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:0035014; F:phosphatidylinositol 3-kinase regulator activity; 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 Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR039724; WDR91.
DR PANTHER; PTHR13083; PTHR13083; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 2: Evidence at transcript level;
KW Coiled coil; Endosome; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..746
FT /note="WD repeat-containing protein 91"
FT /id="PRO_0000295745"
FT REPEAT 405..444
FT /note="WD 1"
FT REPEAT 447..487
FT /note="WD 2"
FT REPEAT 514..554
FT /note="WD 3"
FT REPEAT 559..598
FT /note="WD 4"
FT REPEAT 601..640
FT /note="WD 5"
FT REPEAT 663..701
FT /note="WD 6"
FT REPEAT 708..746
FT /note="WD 7"
FT REGION 265..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 183..215
FT /evidence="ECO:0000255"
FT COMPBIAS 265..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A4D1P6"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A4D1P6"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TMQ7"
SQ SEQUENCE 746 AA; 83157 MW; 0ECA65285FD90F55 CRC64;
MAEAVERTDE MVREYLLFRG FTHTLRQLDA EIKADKEKGF RVDKIVDQLQ QLMQVYDLAA
LRDYWNYLER RLFSRLEDVY RPTINKLKTS LFRFYLVYTI QTNRSDKAQE FFAKQASELQ
NQAEWKDWFV LPFLPSPDTN PTFATYFSRQ WADTFIVSLH NFLSVLFQCM PVPVILNFDA
ECQRTNQVQE ENEVLRQKLF ALQAEIHRLK KEEQQPEEEE ALVQHKLPPY VSNMDRLGDS
ELAMVCSQRN ASLSQSPRVG FLSSLLPQSK KSPSRLSPAQ GPPQTQSSAK KESFGSQTTK
GREPAGAPKD GKSLFGGLAP GESSWSQHRQ RRLQDHGKER KELLSMTLQC AEKKPEAGGP
EAEPCPEPHV EALETLTRVP TAGPEGGGVR PEQPFIVLGQ EEYGEHHSSI MHCRVDCSGR
RVASLDVDGV IKVWSFNPIM QTKASSISKS PLLSLEWATK RDRLLLLGSG VGTVRLYDTE
AKKNLCEINI NDDMPRILSL ACSPSGASFV CSAAASSLTA HVDVLAPDIG SRGTNQVPGR
LLLWDTKTMK QQLQFSLDPE PIAINCTAFN HNGNLLVTGA ADGVIRLFDM QQHECAMSWK
AHCGEVYSVE FSYDENTVYS IGEDGKFIQW NIHKSGLKVS EYGLPADATG PFVLSGYSGY
KQVQVPRGRL FAFDSEGNYM LTCSATGGVI YKLGGDDKVL ESCVSLGGHR APVVTVDWST
AMDCGTCLTA SMDGKIKLTT LLAHKV
