NRF6_CAEEL
ID NRF6_CAEEL Reviewed; 822 AA.
AC Q09225; Q9U4I8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Nose resistant to fluoxetine protein 6;
DE Short=Protein nrf-6;
DE Flags: Precursor;
GN Name=nrf-6; ORFNames=C08B11.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF PRO-787.
RC STRAIN=Bristol N2;
RX PubMed=10488330; DOI=10.1016/s1097-2765(00)80362-7;
RA Choy R.K.M., Thomas J.H.;
RT "Fluoxetine-resistant mutants in C. elegans define a novel family of
RT transmembrane proteins.";
RL Mol. Cell 4:143-152(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16487504; DOI=10.1016/j.ydbio.2006.01.013;
RA Watts J.L., Browse J.;
RT "Dietary manipulation implicates lipid signaling in the regulation of germ
RT cell maintenance in C. elegans.";
RL Dev. Biol. 292:381-392(2006).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16118202; DOI=10.1534/genetics.103.024869;
RA Choy R.K., Kemner J.M., Thomas J.H.;
RT "Fluoxetine-resistance genes in Caenorhabditis elegans function in the
RT intestine and may act in drug transport.";
RL Genetics 172:885-892(2006).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-236, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Plays a role in the uptake of a range of molecules including
CC lipids and xenobiotic compounds from the intestine to surrounding
CC tissues. Mediates transport of lipids from intestine to the
CC reproductive tract. Required for efficient yolk transport into oocytes.
CC Vital for embryonic development. {ECO:0000269|PubMed:10488330,
CC ECO:0000269|PubMed:16118202, ECO:0000269|PubMed:16487504}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In L1 larvae through to adult, hyp3 and hyp5, the
CC most anterior cells in the hypodermis, and in intestine. Other
CC hypodermal cells show weaker expression. {ECO:0000269|PubMed:10488330}.
CC -!- DISRUPTION PHENOTYPE: Increased resistance to fluoxetine-induced nose
CC muscle contraction. Slow development, embryonic lethality and defective
CC yolk transport to the oocytes leading to accumulation of yolk granules
CC in the pseudocoelomic fluid and appearance of pale eggs. Reduced level
CC of sensitivity to dihomo-gamma-linolenic acid-induced sterility.
CC {ECO:0000269|PubMed:10488330, ECO:0000269|PubMed:16118202,
CC ECO:0000269|PubMed:16487504}.
CC -!- SIMILARITY: Belongs to the acyltransferase 3 family. {ECO:0000305}.
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DR EMBL; AF173372; AAD51972.1; -; mRNA.
DR EMBL; Z46676; CAA86669.2; -; Genomic_DNA.
DR PIR; T19074; T19074.
DR RefSeq; NP_495680.1; NM_063279.3.
DR AlphaFoldDB; Q09225; -.
DR BioGRID; 39619; 1.
DR STRING; 6239.C08B11.4; -.
DR TCDB; 9.B.97.2.3; the acyltransferase-3/putative acetyl-coa transporter (atat) family.
DR iPTMnet; Q09225; -.
DR EPD; Q09225; -.
DR PaxDb; Q09225; -.
DR PeptideAtlas; Q09225; -.
DR EnsemblMetazoa; C08B11.4.1; C08B11.4.1; WBGene00003813.
DR GeneID; 174287; -.
DR KEGG; cel:CELE_C08B11.4; -.
DR UCSC; C08B11.4; c. elegans.
DR CTD; 174287; -.
DR WormBase; C08B11.4; CE27798; WBGene00003813; nrf-6.
DR eggNOG; KOG3700; Eukaryota.
DR GeneTree; ENSGT00530000063340; -.
DR HOGENOM; CLU_007874_3_2_1; -.
DR InParanoid; Q09225; -.
DR OMA; LIYMNNF; -.
DR OrthoDB; 1171418at2759; -.
DR PhylomeDB; Q09225; -.
DR PRO; PR:Q09225; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003813; Expressed in adult organism and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR InterPro; IPR002656; Acyl_transf_3_dom.
DR InterPro; IPR006621; Nose-resist-to-fluoxetine_N.
DR Pfam; PF01757; Acyl_transf_3; 1.
DR Pfam; PF20146; NRF; 1.
DR SMART; SM00703; NRF; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Glycoprotein; Lipid transport; Lipid-binding;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..822
FT /note="Nose resistant to fluoxetine protein 6"
FT /id="PRO_0000021856"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT MUTAGEN 787
FT /note="P->L: In allele nrg-6(SA526); fluoxetine induced
FT nose contraction, pale eggs, yolk accumulation and
FT embryonic lethality."
FT /evidence="ECO:0000269|PubMed:10488330"
SQ SEQUENCE 822 AA; 94206 MW; 5C685FF948A04F6E CRC64;
MGNMRRLLIF AVLVILTVIS NSKSSYKYDG SLFSSKELDY DETDTKAMGS VFSRYMSDSD
AQLILDLDFF RHFFNYAEAY RDGAEEGNLE LMKYAVEMVE KLKSFDISMA CVGDMMHLAW
TGVEYATHVE EHKNCSDCKC TPLFQQKKSE RHWIFNVFDA MGKVPAGIMS GNNLWVGSWS
TCRKIDVVKN AQGQKWKGQY CLATIDAYER DNPLVYFGNM MSGPPDKHCY DKTVKNVTDD
GFCFALFPVL KFGVCMPNTC TNHDVKQMLS FAIRATEGAV GTKSVCNVDV ECRAESYSDA
MSENGLAMFA LYLLIATVVL VTFGTLYDLF IVSKAPQDEK NSSAFNHPFI KFILAFSMYT
NGSEILQSKK NDREINSLHG VRFLSMCWII LGHTYYYIGT SLTTDNLVPT LINFPKQFHT
QIIVQAPLAV DSFFFLSGML AAFSFFKKTM KADPNHPPKL SAFNWQTWPM YYYKRYIRIT
PTYIIVMLFD VTLFTYISNG PFWRPIERQG CSIAWWTNLI YLNNFLLQDQ ECCMGWTWYL
ANDMQFHIFL MPLLVIVFLK WGMKVGLGLS TGLIALSSLI RLIITQIYGY PPAPILTAKL
QIVYQLNDYW NDVYVRPYIR CTPFIVGIVV AYLLNAWTTR EQKDLKIKLE RRTVIICWCT
STVLGLYSVF GLYWFAKTGD ISKPWEILYT IFGTPAYALA LGWVVFACTT GNGGPVDTIL
SWRLFVPLSK ITFCAYLLHP IMLQIYNLSR PQPFHFTTFI QMIRYTVEAV FASYTIAFFF
SLAFEKPLNK IDEMLFNSKK MMNGENGNTT EMVPLNKIRN SD
