FLD1_CAEEL
ID FLD1_CAEEL Reviewed; 350 AA.
AC G5EF48;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=TLC domain-containing protein fld-1 {ECO:0000305};
DE AltName: Full=Membrane fluidity homeostasis protein 1 {ECO:0000303|PubMed:30509349};
GN Name=fld-1 {ECO:0000303|PubMed:30509349, ECO:0000312|WormBase:Y63D3A.8};
GN ORFNames=Y63D3A.8 {ECO:0000312|WormBase:Y63D3A.8};
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, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF 46-TRP--VAL-350; HIS-116; ASP-160; GLU-207; HIS-214 AND
RP LEU-290.
RX PubMed=30509349; DOI=10.7554/elife.40686;
RA Ruiz M., Bodhicharla R., Svensk E., Devkota R., Busayavalasa K.,
RA Palmgren H., Staahlman M., Boren J., Pilon M.;
RT "Membrane fluidity is regulated by the C. elegans transmembrane protein
RT FLD-1 and its human homologs TLCD1/2.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Regulates the composition and fluidity of the plasma membrane
CC (PubMed:30509349). Inhibits the incorporation of membrane-fluidizing
CC phospholipids containing omega-3 long-chain polyunsaturated fatty acids
CC (LCPUFA) and thereby promotes membrane rigidity (PubMed:30509349). Does
CC not appear to have any effect on LCPUFA synthesis (PubMed:30509349).
CC {ECO:0000269|PubMed:30509349}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30509349};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:30509349}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:30509349}.
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DR EMBL; BX284601; CAA21712.2; -; Genomic_DNA.
DR PIR; T23273; T23273.
DR RefSeq; NP_493466.2; NM_061065.5.
DR AlphaFoldDB; G5EF48; -.
DR STRING; 6239.Y63D3A.8; -.
DR EPD; G5EF48; -.
DR PaxDb; G5EF48; -.
DR PeptideAtlas; G5EF48; -.
DR EnsemblMetazoa; Y63D3A.8.1; Y63D3A.8.1; WBGene00013407.
DR GeneID; 173280; -.
DR KEGG; cel:CELE_Y63D3A.8; -.
DR CTD; 173280; -.
DR WormBase; Y63D3A.8; CE39301; WBGene00013407; fld-1.
DR eggNOG; KOG4474; Eukaryota.
DR GeneTree; ENSGT01010000222313; -.
DR HOGENOM; CLU_056440_0_0_1; -.
DR InParanoid; G5EF48; -.
DR OMA; MAHYLLI; -.
DR OrthoDB; 1113854at2759; -.
DR PhylomeDB; G5EF48; -.
DR PRO; PR:G5EF48; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00013407; Expressed in embryo and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0071709; P:membrane assembly; IMP:UniProtKB.
DR GO; GO:0055091; P:phospholipid homeostasis; IMP:UniProtKB.
DR GO; GO:0007009; P:plasma membrane organization; IMP:UniProtKB.
DR GO; GO:0097035; P:regulation of membrane lipid distribution; IMP:UniProtKB.
DR InterPro; IPR006634; TLC-dom.
DR Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR SMART; SM00724; TLC; 1.
DR PROSITE; PS50922; TLC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..350
FT /note="TLC domain-containing protein fld-1"
FT /id="PRO_0000447257"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 102..279
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT REGION 65..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 46..350
FT /note="Missing: In gk653147; suppresses the saturated fatty
FT acid toxicity phenotypes of paqr-2 (tm3410) mutants
FT (specifically, withered tail tip morphology and glucose
FT intolerance)."
FT /evidence="ECO:0000269|PubMed:30509349"
FT MUTAGEN 116
FT /note="H->Y: In et50; suppresses the glucose intolerance
FT defects of paqr-2 (tm3410) and mdt-15 (et14) double
FT mutants."
FT /evidence="ECO:0000269|PubMed:30509349"
FT MUTAGEN 160
FT /note="D->N: In et45; suppresses the saturated fatty acid
FT toxicity phenotypes of paqr-2 (tm3410) mutants
FT (specifically, withered tail tip morphology and glucose
FT intolerance)."
FT /evidence="ECO:0000269|PubMed:30509349"
FT MUTAGEN 207
FT /note="E->K: In et47; suppresses the saturated fatty acid
FT toxicity phenotypes of paqr-2 (tm3410) mutants
FT (specifically, withered tail tip morphology and glucose
FT intolerance)."
FT /evidence="ECO:0000269|PubMed:30509349"
FT MUTAGEN 214
FT /note="H->P: In et51; suppresses the glucose intolerance
FT defects of paqr-2 (tm3410) mutants."
FT /evidence="ECO:0000269|PubMed:30509349"
FT MUTAGEN 290
FT /note="L->F: In et49; suppresses the saturated fatty acid
FT toxicity phenotypes of paqr-2 (tm3410) mutants
FT (specifically, withered tail tip morphology and glucose
FT intolerance)."
FT /evidence="ECO:0000269|PubMed:30509349"
SQ SEQUENCE 350 AA; 39824 MW; ADC726DE50520B18 CRC64;
MRQLAELLTD LLGPVPTMFL WVIVSFAFFR ALQFIVRWYL FGKWTWPNFN FFDIRNRIRR
RRRGGQEAEN TENPPENEAE AGEQVEQEPE PDSRDLSAIP PNKKWRISNE CVSLFHSVIS
GLWAAYALLY YKQLVQDLVN YRCDVAINLV LMSAGYLFHD LVDLLVNEQS ARIIELLFHH
VVVLSAFAVT MFFNRFLGVV VFGLLMELNS IFLHSRSLLN LYGVDKKSPS FRIIALLNMV
TLFAFRLCVS AYLVYFVVVS IPDLEWYVSI INGLVIASLA STNTVLTYRL LAADGLLGSR
RTRRTPAATA ETQVGDVESG PLRTQVEDED HHTIGVQTIH GTTEDATQTV
