WDR91_DANRE
ID WDR91_DANRE Reviewed; 724 AA.
AC Q6TEN6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=WD repeat-containing protein 91 {ECO:0000250|UniProtKB:A4D1P6};
GN Name=wdr91; Synonyms=hspc049l;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ97989.1; Type=Erroneous initiation; Evidence={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; AY423013; AAQ97989.1; ALT_INIT; mRNA.
DR RefSeq; NP_991168.1; NM_205605.1.
DR AlphaFoldDB; Q6TEN6; -.
DR SMR; Q6TEN6; -.
DR STRING; 7955.ENSDARP00000126101; -.
DR iPTMnet; Q6TEN6; -.
DR PaxDb; Q6TEN6; -.
DR GeneID; 402898; -.
DR KEGG; dre:402898; -.
DR CTD; 29062; -.
DR ZFIN; ZDB-GENE-050113-2; wdr91.
DR eggNOG; KOG1333; Eukaryota.
DR InParanoid; Q6TEN6; -.
DR OrthoDB; 321271at2759; -.
DR PhylomeDB; Q6TEN6; -.
DR TreeFam; TF317339; -.
DR Reactome; R-DRE-9013148; CDC42 GTPase cycle.
DR PRO; PR:Q6TEN6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endosome; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..724
FT /note="WD repeat-containing protein 91"
FT /id="PRO_0000295750"
FT REPEAT 389..428
FT /note="WD 1"
FT REPEAT 431..471
FT /note="WD 2"
FT REPEAT 499..532
FT /note="WD 3"
FT REPEAT 537..576
FT /note="WD 4"
FT REPEAT 579..618
FT /note="WD 5"
FT REPEAT 641..679
FT /note="WD 6"
FT REPEAT 686..724
FT /note="WD 7"
FT REGION 249..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 178..207
FT /evidence="ECO:0000255"
FT COMPBIAS 269..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
SQ SEQUENCE 724 AA; 80767 MW; 008F055F47314E97 CRC64;
MASAVERTDD LVREYLIYRG FTSTLKHLDS EIKTDKEKGF RVDKIMDQLQ LLIQSCDLTG
LKEYWANLER RLFCRLEDVY KPTVSKLRTS LYRFYLIHTV QVKNVEKTQE FFQKQALELQ
AQAEWRDWFS LPFIPAPEQN PSFSAYFSRQ WADTFLVSLH NFLSVLFQCM PLPALLSFDS
EVQRITSLQE DNEQLRQTVF ALQGESRLKK DEQMVHHKLP PYVQHMDRLG DTELDLVSSQ
RNVNMATPSR NFFSTFLPQG RRAPGRTAPG PQSSPTQSAL GRKDAAASMQ SSKAKDKEVK
PPSVSSMTAE LSTSHPRQRR HQDHEKERKE LFSKHAAQGS EKKTDSDPDT QTEAPPDQTD
SANQTRVCDV GGAGAEQPFI KLSQEEYGEH HSSIMHCRVD CSGRRVASLD VDGVVKVWAF
NPIMQTKATI MSKSPLLSLE WAAKPDRLLL LGSGVGTVKL YDTDAKKCLY EMTIDDVHPR
ILSLACSPSG TSFVCSAAAH SGAVMESEPR GSAPVSGQLL LWDTKTVKQQ LQFALEPGPV
AINCTAFNHN GNLLVTGAAD GIIRLFDMQR YESALSWKAH DGEVYSVEFS YDENTVFSIG
EDGKFVQWNI HRCGVKQSEY SLSQDAVGPF VLSGYSGYKQ VQVPRGRLFA FDSEGQHVLT
CSSTGGNIYR LNKAEAGLES VLSLAGHKAP VVTVDWCSAM DCGTCLTASM DGKIKLSTLL
AQKP
