NRF5_CAEEL
ID NRF5_CAEEL Reviewed; 551 AA.
AC Q93796; Q6RV00; Q6RV01;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Nose resistant to fluoxetine protein 5 {ECO:0000303|PubMed:16118202};
DE Short=Protein nrf-5 {ECO:0000303|PubMed:16118202};
DE Flags: Precursor;
GN Name=nrf-5 {ECO:0000312|EMBL:CAB02126.2, ECO:0000312|WormBase:F55B12.5};
GN ORFNames=F55B12.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:CAB02126.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB02126.2};
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, ECO:0000312|EMBL:AAS18682.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-551, TISSUE SPECIFICITY, AND DISRUPTION
RP 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 [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:10488330};
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 [4] {ECO:0000305}
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 [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH TTR-52, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22727700; DOI=10.1016/j.cub.2012.06.004;
RA Zhang Y., Wang H., Kage-Nakadai E., Mitani S., Wang X.;
RT "C. elegans secreted lipid-binding protein NRF-5 mediates PS appearance on
RT phagocytes for cell corpse engulfment.";
RL Curr. Biol. 22:1276-1284(2012).
CC -!- FUNCTION: Plays a role in the uptake of a range of molecules including
CC phosphatidylserine, lipids and xenobiotic compounds from the intestine
CC to surrounding tissues. Possesses lipid transfer activity. Mediates
CC transport of lipids from intestine to reproductive tract. Binds
CC phosphatidylserine. Plays a role in efficient clearance of cell corpses
CC by mediating phosphatidylserine appearance on phagocytic cells, thus
CC promoting phagocytic engulfment of apoptotic cells. Vital for embryonic
CC development. {ECO:0000269|PubMed:10488330, ECO:0000269|PubMed:16487504,
CC ECO:0000269|PubMed:22727700, ECO:0000305}.
CC -!- SUBUNIT: Interacts with ttr-52. {ECO:0000269|PubMed:22727700}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22727700}.
CC -!- TISSUE SPECIFICITY: Expressed in the body wall muscle cells and
CC detected at the basal surface of pharyngeal cells and basal-lateral
CC membranes of the intestine. {ECO:0000269|PubMed:16118202,
CC ECO:0000269|PubMed:22727700}.
CC -!- DISRUPTION PHENOTYPE: Increased resistance to fluoxetine-induced nose
CC muscle contraction. Slow development, embryonic lethality and defect in
CC yolk transport to oocytes leading to accumulation of yolk granules in
CC the pseudocoelomic fluid and appearance of pale eggs. Reduced level of
CC sensitivity to dihomo-gamma-linolenic acid-induced sterility. Cell
CC corpses persist significantly longer than in the wild-type, indicating
CC a cell corpse clearance defect. {ECO:0000269|PubMed:10488330,
CC ECO:0000269|PubMed:16118202, ECO:0000269|PubMed:16487504,
CC ECO:0000269|PubMed:22727700}.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000255}.
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DR EMBL; Z79757; CAB02126.2; -; Genomic_DNA.
DR EMBL; AY491012; AAS18681.1; -; mRNA.
DR EMBL; AY491013; AAS18682.1; -; mRNA.
DR PIR; T22700; T22700.
DR RefSeq; NP_506424.2; NM_074023.5.
DR AlphaFoldDB; Q93796; -.
DR SMR; Q93796; -.
DR BioGRID; 44893; 2.
DR STRING; 6239.F55B12.5.2; -.
DR SwissLipids; SLP:000000403; -.
DR TCDB; 1.C.40.1.5; the bactericidal permeability increasing protein (bpip) family.
DR EPD; Q93796; -.
DR PaxDb; Q93796; -.
DR PeptideAtlas; Q93796; -.
DR EnsemblMetazoa; F55B12.5.1; F55B12.5.1; WBGene00003812.
DR GeneID; 179879; -.
DR KEGG; cel:CELE_F55B12.5; -.
DR UCSC; F55B12.5.1; c. elegans.
DR CTD; 179879; -.
DR WormBase; F55B12.5; CE32438; WBGene00003812; nrf-5.
DR eggNOG; KOG4160; Eukaryota.
DR GeneTree; ENSGT01020000230460; -.
DR HOGENOM; CLU_017101_0_0_1; -.
DR InParanoid; Q93796; -.
DR OMA; CELQFIA; -.
DR OrthoDB; 489431at2759; -.
DR Reactome; R-CEL-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-CEL-5686938; Regulation of TLR by endogenous ligand.
DR PRO; PR:Q93796; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003812; Expressed in larva and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IDA:WormBase.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:WormBase.
DR GO; GO:0006869; P:lipid transport; IDA:WormBase.
DR GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IMP:WormBase.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR InterPro; IPR032942; BPI/LBP/Plunc.
DR InterPro; IPR001124; Lipid-bd_serum_glycop_C.
DR InterPro; IPR017942; Lipid-bd_serum_glycop_N.
DR PANTHER; PTHR10504; PTHR10504; 1.
DR Pfam; PF01273; LBP_BPI_CETP; 1.
DR Pfam; PF02886; LBP_BPI_CETP_C; 1.
DR SMART; SM00328; BPI1; 1.
DR SMART; SM00329; BPI2; 1.
DR SUPFAM; SSF55394; SSF55394; 2.
PE 1: Evidence at protein level;
KW Developmental protein; Disulfide bond; Lipid transport; Lipid-binding;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..551
FT /note="Nose resistant to fluoxetine protein 5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422699"
FT REGION 241..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 151..232
FT /evidence="ECO:0000250"
FT CONFLICT 452
FT /note="D -> DVSCIQEKLILKNFSCINLKVEQKFQ (in Ref. 1;
FT AAS18681/AAS18682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 551 AA; 60851 MW; D4FE291494D27680 CRC64;
MSRNFHIFFL LVSIIQVGNS ADSSEITHKP AGIYVRLNQK AVDYVADLAS DALPAILNNL
SPPDIVTDMA KITKLHISNV AKPNLSAKFI DGKGVAYNIS LASFRASAYA EISVFVWSYE
GDFTAELREL SIESELHFDY NGTTTVNASV CNVTHSELSL VFPPGSSLSA LQSEIKGQIV
SALRDAVCTT AVEALTFVMA QKPIPPESPN YQKPEAGDPN GFSVAELGAS LCQVDTVNGF
EDSEQEEGNV ETTVAPTPDD DNSTLTTEET QKSYWGVDLS VNHPPTFTDE DMIIGLDGGI
LFNGWKADSA QQLQILNKTR LDKKMVGILL SEYIPNTLFH HIYMYDLGNF KHRYTPSSLP
KILQKLSKAV CSKCYVEVSA NLTEQPILQI DAHLGARVQL SGNVSIMFHG REQLHDVLHA
NTKLHVTLKP TVRHSRIFGD VSLTNVDVNV FDLGLGGPLA APIEKLFSFV VPRVLWPQVK
KRLRFAMNRR GVKLPIFCGV ELEHTELDFV DHAVLLNTDF SFDLPLFLAK FKKYLDAKSK
INPNLPKYVI I
