QUI1_CAEEL
ID QUI1_CAEEL Reviewed; 1592 AA.
AC O62471; I2HAI7; N1NTL8;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protein qui-1 {ECO:0000305};
DE AltName: Full=Quinine non-avoider protein 1 {ECO:0000312|WormBase:Y45F10B.10a};
GN Name=qui-1 {ECO:0000312|WormBase:Y45F10B.10a};
GN ORFNames=Y45F10B.10 {ECO:0000312|WormBase:Y45F10B.10a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 250-GLN--LEU-1592 AND 1022-TRP--LEU-1592.
RX PubMed=14988722; DOI=10.1038/sj.emboj.7600107;
RA Hilliard M.A., Bergamasco C., Arbucci S., Plasterk R.H., Bazzicalupo P.;
RT "Worms taste bitter: ASH neurons, QUI-1, GPA-3 and ODR-3 mediate quinine
RT avoidance in Caenorhabditis elegans.";
RL EMBO J. 23:1101-1111(2004).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 250-GLN--LEU-1592 AND 848-TRP--LEU-1592.
RX PubMed=26976437; DOI=10.1534/g3.115.026450;
RA Neal S.J., Park J., DiTirro D., Yoon J., Shibuya M., Choi W.,
RA Schroeder F.C., Butcher R.A., Kim K., Sengupta P.;
RT "A Forward Genetic Screen for Molecules Involved in Pheromone-Induced Dauer
RT Formation in Caenorhabditis elegans.";
RL G3 (Bethesda) 6:1475-1487(2016).
CC -!- FUNCTION: Involved in the avoidance response to the noxious chemicals
CC and repellents such as quinine in ASH and ADL sensory neurons
CC (PubMed:14988722). In response to the noxious chemical quinine,
CC promotes dauer formation induced by pheromones such as the ascaroside
CC ascr#3 in ASH nociceptive neurons (PubMed:26976437).
CC {ECO:0000269|PubMed:14988722, ECO:0000269|PubMed:26976437}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14988722,
CC ECO:0000269|PubMed:26976437}. Perikaryon {ECO:0000269|PubMed:14988722}.
CC Nucleus {ECO:0000269|PubMed:14988722}. Cell projection, dendrite
CC {ECO:0000269|PubMed:14988722}. Cell projection, axon
CC {ECO:0000269|PubMed:14988722}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:Y45F10B.10a};
CC IsoId=O62471-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y45F10B.10b};
CC IsoId=O62471-2; Sequence=VSP_060901, VSP_060902;
CC Name=c {ECO:0000312|WormBase:Y45F10B.10c};
CC IsoId=O62471-3; Sequence=VSP_060900;
CC -!- TISSUE SPECIFICITY: Expressed in the nerve ring, neurons of the lateral
CC and ventral ganglia, including the sensory neuron ADL, neurons in the
CC retrovesicular ganglion and two neurons in the lumbar ganglion, PVQ and
CC the sensory neuron PHB (PubMed:14988722). Expressed in ASH nociceptive
CC chemosensory neurons (PubMed:14988722, PubMed:26976437). Not expressed
CC in ASK sensory neurons (PubMed:14988722). {ECO:0000269|PubMed:14988722,
CC ECO:0000269|PubMed:26976437}.
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DR EMBL; BX284604; CAA16357.2; -; Genomic_DNA.
DR EMBL; BX284604; CCH63915.1; -; Genomic_DNA.
DR EMBL; BX284604; CCW46000.1; -; Genomic_DNA.
DR PIR; T26919; T26919.
DR RefSeq; NP_001263809.1; NM_001276880.1. [O62471-2]
DR RefSeq; NP_001294084.1; NM_001307155.1. [O62471-3]
DR RefSeq; NP_502613.2; NM_070212.3. [O62471-1]
DR AlphaFoldDB; O62471; -.
DR SMR; O62471; -.
DR STRING; 6239.Y45F10B.10a; -.
DR EPD; O62471; -.
DR PaxDb; O62471; -.
DR EnsemblMetazoa; Y45F10B.10a.1; Y45F10B.10a.1; WBGene00004265. [O62471-1]
DR EnsemblMetazoa; Y45F10B.10b.1; Y45F10B.10b.1; WBGene00004265. [O62471-2]
DR EnsemblMetazoa; Y45F10B.10c.1; Y45F10B.10c.1; WBGene00004265. [O62471-3]
DR GeneID; 178326; -.
DR KEGG; cel:CELE_Y45F10B.10; -.
DR UCSC; Y45F10B.10; c. elegans. [O62471-1]
DR CTD; 178326; -.
DR WormBase; Y45F10B.10a; CE36361; WBGene00004265; qui-1. [O62471-1]
DR WormBase; Y45F10B.10b; CE47522; WBGene00004265; qui-1. [O62471-2]
DR WormBase; Y45F10B.10c; CE48377; WBGene00004265; qui-1. [O62471-3]
DR eggNOG; KOG4155; Eukaryota.
DR HOGENOM; CLU_001769_0_0_1; -.
DR InParanoid; O62471; -.
DR OMA; LKELPHH; -.
DR OrthoDB; 183408at2759; -.
DR PhylomeDB; O62471; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004265; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; O62471; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0043279; P:response to alkaloid; IMP:WormBase.
DR Gene3D; 2.130.10.10; -; 4.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 12.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; Nucleus;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1592
FT /note="Protein qui-1"
FT /id="PRO_0000452040"
FT REPEAT 909..948
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 951..992
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 993..1032
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 1035..1074
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 1077..1117
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 1119..1157
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 1162..1201
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REPEAT 1205..1244
FT /note="WD 8"
FT /evidence="ECO:0000255"
FT REPEAT 1247..1285
FT /note="WD 9"
FT /evidence="ECO:0000255"
FT REPEAT 1287..1328
FT /note="WD 10"
FT /evidence="ECO:0000255"
FT REPEAT 1333..1373
FT /note="WD 11"
FT /evidence="ECO:0000255"
FT REPEAT 1376..1415
FT /note="WD 12"
FT /evidence="ECO:0000255"
FT REPEAT 1417..1456
FT /note="WD 13"
FT /evidence="ECO:0000255"
FT REGION 1507..1592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..265
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_060900"
FT VAR_SEQ 108..115
FT /note="LLLGNRYG -> VRIGFGKL (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060901"
FT VAR_SEQ 116..1592
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060902"
FT MUTAGEN 250..1592
FT /note="Missing: In gb404; reduces ability to avoid the
FT noxious chemical quinine, chloroquine, amodiaquine,
FT primaquine, quinacrine, shikimic acid, denatonium, ethidium
FT bromide, zinc ions, sodium dodecyl sulfate and low pH
FT environments. Due to inability to avoid quinine, results in
FT enhanced pheromone-induced dauer formation in response to
FT the ascaroside ascr#3."
FT /evidence="ECO:0000269|PubMed:14988722,
FT ECO:0000269|PubMed:26976437"
FT MUTAGEN 848..1592
FT /note="Missing: In oy105; defects in pheromone-induced
FT dauer formation in response to the ascarosides ascr#3 and
FT icas#9."
FT /evidence="ECO:0000269|PubMed:26976437"
FT MUTAGEN 1022..1592
FT /note="Missing: In gb681; reduces ability to avoid the
FT noxious chemical quinine."
FT /evidence="ECO:0000269|PubMed:14988722"
SQ SEQUENCE 1592 AA; 177300 MW; 4FDCEF4ADC5581CB CRC64;
MFRGKGQQQV SSTDNIKAMM TAAIGNKLEK RLPLVSTIFV VGNDEEEFNI ERRTLWQDVL
PDLQNLAFQS NFDLEFCDVP LENGELTNSV AEHVLQMWKD NPRSWIVLLL GNRYGNVSVP
TSLRKEEYES IRSSIFEENG NVRVFEKAYT INRNGAVEEY RLVPSAIKDK KQLAEIIKAL
QAGAKAAHEE GSINQVHEQR QNRFFSSPLE TFVRSILQVS PCRCLFLLRK FDQLVADPNS
PNAFLETNDQ NSRKIEDLKN EITLKMNDRV MTHVLRPEST DINYFFNSRD GDKYREKIAR
QFNEKLKNHL ADINPPVRPE PPKSPMVLAA NEARTHQEFL ENQLALGNLK RDYDKRLDEL
ASVKVNRGVF LIQGTDLCGK TQALCRLYHK ISDKDAYKVI FFTNLTYSSN FAHEAWRTIC
LNICSISNID PKEVLEHFKL GGILKSLEEL VQKADKPVCI FIDDVHLLKF GHLLSQIGRR
TETAPDNLSL FMTSSNVAPV NAVFAVTQTV NVDVISENEV VGMVQKMAEK VDKKLTNEQI
SAIRPLMAAK DGILIAKSFT HEILFNGNSS MKGGMDGRMT RIEKEFGKLA VGNAVKFIAA
SSHGLTRLEI HDAISADREV LEEMNMSIVY SLLTLDGIIE ALGPILRKVI IDDRQIIGIA
HSGLISWLRN RYLTSSQDIR SAHLQLSDLF ADLLIDNEQS PRHEIAYQSF SQGIKRDNGS
PNFRRLRLLW YHCLHSGNLD RLKELSLCHF EYVDYVTRYF GISHLLSLYE ECATQILHHD
LQVISEQVLV PALVTMARDS EQLAAEVIGR LRFTRHENSH FLNSLVDQAM SWVDLYNRQP
LLVPLTCWIS PPATKVCRSF TLKDWKPGNT VLTLSANHQY ILISGNQSDP GVIYAYHIAS
EQLIGTFKGH TAAVTCLCSS NDSSLFVSTS FDKTVNVWVF SQSTPTMSLT HHTAKVTCAI
LTSDDQYLIT ASADSSAKMI KLETGEVMRS FNDHTGSVVS LQLTSNNQFL ITGSGDFVVQ
MWDVTNGKCI SRMGGLMAPV STLAITSNDA FVVVACEDET LKVFSTVGGQ ELHELMGHEG
KVNSLVCAQD DCQLFAATKS KVFCYDIHNG QMIDVLDTAQ PFPICSLKIS SDNYFLISPC
GPKVTIWNVT KRNHDAHDVH ADKEGFLTAV ALSNDDKYAA CGTNNGIVAL WDLEVCQCVF
TTIQNKGDPI TCIRYSVDSQ YCISGNQAGC ILILDAQNGG VVRELFMHSS EVLSIMSLVH
NKMISCDIQG KMVIWELFGD DDTPEMVATG VKPPIFVPPT GRIMVGHCSL SNKEMKIWAF
PEEGPPVTRA KLSHSDEITC FATSPKGGNF IATGSRDMSL KIWQIDKGFL TQVLVGHENV
VTCCCISFDE RLVVSGARDE KIIVWNVQSG DMVCTVNTTA AITSLSMTGD STVVFSTTED
GWVETWSTTK GRLLSTFNAH RPIKKLINSY ESHRMLLLLE NCAQLPILCL HNTPAVGVEA
TRRRSARAQS VSSASNEPVA STSAGEIKKD PILSSNNGGN AQSAPRATAP KPTFDMLERS
KSRTSLIEKD RTTTLTQSNA PPPQKSNMCT LL
