ID   WDR91_PONAB             Reviewed;         712 AA.
AC   Q5R6T6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=WD repeat-containing protein 91 {ECO:0000250|UniProtKB:A4D1P6};
GN   Name=WDR91 {ECO:0000250|UniProtKB:A4D1P6};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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}.
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DR   EMBL; CR860398; CAH92524.1; -; mRNA.
DR   RefSeq; NP_001127560.1; NM_001134088.1.
DR   AlphaFoldDB; Q5R6T6; -.
DR   SMR; Q5R6T6; -.
DR   STRING; 9601.ENSPPYP00000020226; -.
DR   PRIDE; Q5R6T6; -.
DR   GeneID; 100174638; -.
DR   KEGG; pon:100174638; -.
DR   CTD; 29062; -.
DR   eggNOG; KOG1333; Eukaryota.
DR   InParanoid; Q5R6T6; -.
DR   Proteomes; UP000001595; 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; 5.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
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..712
FT                   /note="WD repeat-containing protein 91"
FT                   /id="PRO_0000295748"
FT   REPEAT          371..410
FT                   /note="WD 1"
FT   REPEAT          413..453
FT                   /note="WD 2"
FT   REPEAT          480..520
FT                   /note="WD 3"
FT   REPEAT          525..564
FT                   /note="WD 4"
FT   REPEAT          567..606
FT                   /note="WD 5"
FT   REPEAT          629..667
FT                   /note="WD 6"
FT   REPEAT          674..712
FT                   /note="WD 7"
FT   REGION          230..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          148..180
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        230..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A4D1P6"
FT   MOD_RES         253
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A4D1P6"
FT   MOD_RES         258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TMQ7"
SQ   SEQUENCE   712 AA;  79269 MW;  F6FFF26119815E39 CRC64;
     MIFHCEVDKI VDQLQQLMQV YDLAALRDYW SYLERRLFSR LEDIYRPTIH KLKTSLFRFY
     LVYTIQTNRN DKAQEFFAKQ ATELQNQAEW KDWFVLPFLP SPDTNPTFAT YFSRQWADTF
     IVSLHNFLSV LFQCMPVPVI LNFDAECRRT NQVQEENEVL RQKLFALQAE IHRLKKEEQQ
     PEEEEALVQH KLPPYVSNMD RLGDSELAMV CSQRNASLSQ SPRVGFLSSL LPQSKKSPSR
     LSPAQGPPQA QSSAKKESFG GQGTKGKDPT SGAKDGKGLL SGLATGESGW SQHRQRRLQD
     HGKERKELFS TTTSQCAEKK PEASGPEAEP CPELHTEPVE PLTRTSLAGP EGGGVRPEQP
     FIVLGQEEYG EHHSSIMHCR VDCSGRRVAS LDVDGVIKVW SFNPIMQTKA SSISKSPLLS
     LEWATKRDRL LLLGSGVGTV RLYDTEAKKN LCEININDDM PRILSLACSP NGASFVCSAA
     APSLTSQVDF SAPDIGSKGM NQVPGRLLLW DTKTMKQQLQ FSLDPEPIAI NCTAFNHNGN
     LLVTGAADGV IRLFDMQQHE CAMSWRAHYG EVYSVEFSYD ENTVYSIGED GKFIQWNIHK
     SGLKVSEYSL PSDATGPFVL SGYSGYKQVQ VPRGRLFAFD SEGNYMLTCS ATGGVIYKLG
     GDEKVLESCL SLGGHRAPVV TVDWSTAMDC GTCLTASMDG KIKLTTLLAH KA