ID   WDR91_CHICK             Reviewed;         751 AA.
AC   Q5ZLL7;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=WD repeat-containing protein 91 {ECO:0000250|UniProtKB:A4D1P6};
GN   Name=WDR91 {ECO:0000250|UniProtKB:A4D1P6};
GN   ORFNames=RCJMB04_5j14 {ECO:0000312|EMBL:CAG31376.1};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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. {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; AJ719717; CAG31376.1; -; mRNA.
DR   RefSeq; NP_001025923.1; NM_001030752.1.
DR   AlphaFoldDB; Q5ZLL7; -.
DR   SMR; Q5ZLL7; -.
DR   STRING; 9031.ENSGALP00000019133; -.
DR   PaxDb; Q5ZLL7; -.
DR   GeneID; 417939; -.
DR   KEGG; gga:417939; -.
DR   CTD; 29062; -.
DR   VEuPathDB; HostDB:geneid_417939; -.
DR   eggNOG; KOG1333; Eukaryota.
DR   InParanoid; Q5ZLL7; -.
DR   OrthoDB; 321271at2759; -.
DR   PhylomeDB; Q5ZLL7; -.
DR   PRO; PR:Q5ZLL7; -.
DR   Proteomes; UP000000539; 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; -; 3.
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; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..751
FT                   /note="WD repeat-containing protein 91"
FT                   /id="PRO_0000295749"
FT   REPEAT          410..449
FT                   /note="WD 1"
FT   REPEAT          452..492
FT                   /note="WD 2"
FT   REPEAT          497..559
FT                   /note="WD 3"
FT   REPEAT          564..603
FT                   /note="WD 4"
FT   REPEAT          606..645
FT                   /note="WD 5"
FT   REPEAT          668..706
FT                   /note="WD 6"
FT   REPEAT          713..751
FT                   /note="WD 7"
FT   REGION          264..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          188..212
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        264..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..347
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   751 AA;  83419 MW;  F9ED3E3FF2792EF8 CRC64;
     MAAATERTDE LVREYLLFRG FTAALKQLDA EIKADREKGF RVDKIVEQLQ QFVQSYDLAA
     LRDYWGYLDR RLFSRLEDMY RPTVNKLKTS LYRYYLVHTV QTGRNDKAQE FFLKQASELQ
     NQAEWKDWFV LPFLPAPDSN PTFATYFSRQ WADTFIVSLH NFLSVLFQCM PVPVILNLEA
     ECHRSSLIQE ENESLRHKLF ALQAESSRMK KEELEVEEAV VHHKLPAYVA NMDRLGDSEL
     DMTCSQRSTA HSLQSRGGFL SSLLSQSKKG PARPAQPSGA SPTQTGSVLL GKKEPANHQS
     AKGKEGTASS KDGKSHFSGL VAGESSSLQQ RQKRLQEHGK ERRELLSKGT SQVQSAEKKA
     DISTSEPEPC SEPQADQAET STKMPASSTE SVGVRQEQPF IVLSQEEYGE HHSSIMYCRV
     DCSGRRVASL DVDGVIKVWS FNPIMQTKAS SISKSPLLSL EWATKRDRLL LLGSGVGTVR
     LYDTEAKKNL CEISIDEDMP RILSLACSPS GASFVCSAAA QSPISHMDFS VVTSGGKSMN
     QVPGKLLLWD TKTMKQQLQF SLEPEPIAIN CTAFNHNGNL LVTGAADGIV RLFDMQQHEC
     AMSWKAHDGE VYSVEFSYDE NTVYSIGEDG KFIQWNIHKS GLKISEYALP SEATGPFVLS
     GYSGYKQVQF PRGRLFAFDS EGNYMLTCSS TGGVIFKLNG EDKVLESCLS LGGHRAPVVT
     VDWSTAMDCG TCLTASMDGK IKLTTLLAQK S