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WDR91_MOUSE
ID   WDR91_MOUSE             Reviewed;         748 AA.
AC   Q7TMQ7; Q80XN1;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=WD repeat-containing protein 91 {ECO:0000312|MGI:MGI:2141558};
GN   Name=Wdr91 {ECO:0000312|MGI:MGI:2141558};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and FVB/N-3; TISSUE=Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   FUNCTION.
RX   PubMed=27346680; DOI=10.1016/j.stemcr.2016.05.013;
RA   Wang S., Wang X., Ma L., Lin X., Zhang D., Li Z., Wu Y., Zheng C., Feng X.,
RA   Liao S., Feng Y., Chen J., Hu X., Wang M., Han C.;
RT   "Retinoic Acid is sufficient for the in vitro induction of mouse
RT   spermatocytes.";
RL   Stem Cell Reports 7:80-94(2016).
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 (By similarity). May play a role in
CC       meiosis (PubMed:27346680). {ECO:0000250|UniProtKB:A4D1P6,
CC       ECO:0000269|PubMed:27346680}.
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; BC043682; AAH43682.1; -; mRNA.
DR   EMBL; BC055046; AAH55046.1; -; mRNA.
DR   CCDS; CCDS39457.1; -.
DR   RefSeq; NP_001013384.1; NM_001013366.1.
DR   AlphaFoldDB; Q7TMQ7; -.
DR   SMR; Q7TMQ7; -.
DR   BioGRID; 221616; 2.
DR   IntAct; Q7TMQ7; 1.
DR   STRING; 10090.ENSMUSP00000079974; -.
DR   iPTMnet; Q7TMQ7; -.
DR   PhosphoSitePlus; Q7TMQ7; -.
DR   EPD; Q7TMQ7; -.
DR   jPOST; Q7TMQ7; -.
DR   MaxQB; Q7TMQ7; -.
DR   PaxDb; Q7TMQ7; -.
DR   PeptideAtlas; Q7TMQ7; -.
DR   PRIDE; Q7TMQ7; -.
DR   ProteomicsDB; 297554; -.
DR   Antibodypedia; 18119; 98 antibodies from 15 providers.
DR   DNASU; 101240; -.
DR   Ensembl; ENSMUST00000081214; ENSMUSP00000079974; ENSMUSG00000058486.
DR   GeneID; 101240; -.
DR   KEGG; mmu:101240; -.
DR   UCSC; uc009bhz.1; mouse.
DR   CTD; 29062; -.
DR   MGI; MGI:2141558; Wdr91.
DR   VEuPathDB; HostDB:ENSMUSG00000058486; -.
DR   eggNOG; KOG1333; Eukaryota.
DR   GeneTree; ENSGT00390000001566; -.
DR   HOGENOM; CLU_022078_0_0_1; -.
DR   InParanoid; Q7TMQ7; -.
DR   OMA; VLFQCML; -.
DR   OrthoDB; 321271at2759; -.
DR   PhylomeDB; Q7TMQ7; -.
DR   TreeFam; TF317339; -.
DR   Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR   BioGRID-ORCS; 101240; 5 hits in 75 CRISPR screens.
DR   ChiTaRS; Wdr91; mouse.
DR   PRO; PR:Q7TMQ7; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q7TMQ7; protein.
DR   Bgee; ENSMUSG00000058486; Expressed in animal zygote and 216 other tissues.
DR   ExpressionAtlas; Q7TMQ7; baseline and differential.
DR   Genevisible; Q7TMQ7; MM.
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   GO; GO:0042176; P:regulation of protein catabolic process; ISO:MGI.
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; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   Coiled coil; Endosome; Membrane; Phosphoprotein; Reference proteome;
KW   Repeat; WD repeat.
FT   CHAIN           1..748
FT                   /note="WD repeat-containing protein 91"
FT                   /id="PRO_0000295747"
FT   REPEAT          407..446
FT                   /note="WD 1"
FT   REPEAT          449..489
FT                   /note="WD 2"
FT   REPEAT          512..556
FT                   /note="WD 3"
FT   REPEAT          561..600
FT                   /note="WD 4"
FT   REPEAT          603..642
FT                   /note="WD 5"
FT   REPEAT          665..703
FT                   /note="WD 6"
FT   REPEAT          710..748
FT                   /note="WD 7"
FT   REGION          266..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          183..228
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        266..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         257
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A4D1P6"
FT   MOD_RES         289
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A4D1P6"
FT   MOD_RES         294
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   CONFLICT        590
FT                   /note="F -> L (in Ref. 1; AAH43682)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   748 AA;  83421 MW;  3973DC3AD76DFA13 CRC64;
     MAEAVERTDE LVREYLLFRG FTHTLRQLDA EIKADKEKGF RVDKIVDQLQ QLMQVYDLAA
     LRDYWSYLER RLFSRLEDIY RPTINKLKTS LFRFYLVYTI QTNRNDKAQE FFAKQATELQ
     NQAEWKDWFV LPFLPSPDTN PTFATYFSRQ WADTFIISLH NFLSVLFQCM PVPVILNFDA
     ECQRTNQVQE ENEVLRQKLF ALQAEIHRLK KEEQQQEEEA AALVQHKLPP YVSSMDRLGD
     SELALVCSQR PASLSQSPRV GFLSSLLPQS KKSPSRLSPA QGPPQAQSSA KKDSFSSQAT
     KGKDSVPGAK DGKSLLSGPV PGEASWTHQR QRRLQDHGKE RRELLSTSSS QSQCAERKPE
     VSGAEAEPCL ELHMGPVEVL ARVSTAGSEG DRPEQPFIVL SQEEYGEHHS SIMHCRVDCS
     GRRVASLDVD GVIKVWSFNP IMQTKASSIS KSPLLSLEWA TKRDRLLLLG SGVGTVRLYD
     TEAKKNLCEI NINDDMPRIL SLACSPNGAS FVCSAAAPSL TSQTDSSAPD IGSKGMNQVP
     GKLLLWDTKT MKQQLQFSLD PEPIAINCTA FNHNGNLLVT GAADGVIRLF DMQQHECAMS
     WKAHCGEVYS VEFSCDENAV YSIGEDRKFI QWNIHKSGLK VSESNLPSDA TGPFVLSGYS
     GYKQVQVPRG RLFAFDSEGN YMLTCSATGG LIYKLGSEEK VLENCLSLGG HRAPVVTVDW
     STAMDCGTCL TASMDGKIKL TTLLAHKL
 
 
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