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LDP1_CAEEL
ID   LDP1_CAEEL              Reviewed;         426 AA.
AC   Q9GZE9; Q8IA58;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Lipid droplet localized protein {ECO:0000312|WormBase:F22F7.1a};
GN   Name=ldp-1 {ECO:0000312|WormBase:F22F7.1a};
GN   ORFNames=F22F7.1 {ECO:0000312|WormBase:F22F7.1a};
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   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=26121959; DOI=10.1016/j.bbalip.2015.06.004;
RA   Vrablik T.L., Petyuk V.A., Larson E.M., Smith R.D., Watts J.L.;
RT   "Lipidomic and proteomic analysis of Caenorhabditis elegans lipid droplets
RT   and identification of ACS-4 as a lipid droplet-associated protein.";
RL   Biochim. Biophys. Acta 1851:1337-1345(2015).
RN   [3] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=26025681; DOI=10.1016/j.bbamcr.2015.05.020;
RA   Na H., Zhang P., Chen Y., Zhu X., Liu Y., Liu Y., Xie K., Xu N., Yang F.,
RA   Yu Y., Cichello S., Mak H.Y., Wang M.C., Zhang H., Liu P.;
RT   "Identification of lipid droplet structure-like/resident proteins in
RT   Caenorhabditis elegans.";
RL   Biochim. Biophys. Acta 1853:2481-2491(2015).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}. Lipid droplet {ECO:0000269|PubMed:26025681,
CC       ECO:0000269|PubMed:26121959}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a {ECO:0000312|WormBase:F22F7.1a};
CC         IsoId=Q9GZE9-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:F22F7.1b};
CC         IsoId=Q9GZE9-2; Sequence=VSP_059216;
CC   -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; BX284605; CCD67439.1; -; Genomic_DNA.
DR   EMBL; BX284605; CCD67440.2; -; Genomic_DNA.
DR   PIR; T33187; T33187.
DR   RefSeq; NP_503577.1; NM_071176.4. [Q9GZE9-1]
DR   RefSeq; NP_872194.2; NM_182394.5. [Q9GZE9-2]
DR   AlphaFoldDB; Q9GZE9; -.
DR   DIP; DIP-26138N; -.
DR   STRING; 6239.F22F7.1a; -.
DR   EPD; Q9GZE9; -.
DR   PaxDb; Q9GZE9; -.
DR   PeptideAtlas; Q9GZE9; -.
DR   EnsemblMetazoa; F22F7.1a.1; F22F7.1a.1; WBGene00017719. [Q9GZE9-1]
DR   EnsemblMetazoa; F22F7.1b.1; F22F7.1b.1; WBGene00017719. [Q9GZE9-2]
DR   GeneID; 178692; -.
DR   KEGG; cel:CELE_F22F7.1; -.
DR   UCSC; F22F7.1a.1; c. elegans.
DR   CTD; 178692; -.
DR   WormBase; F22F7.1a; CE17691; WBGene00017719; ldp-1. [Q9GZE9-1]
DR   WormBase; F22F7.1b; CE51032; WBGene00017719; ldp-1. [Q9GZE9-2]
DR   eggNOG; KOG2733; Eukaryota.
DR   GeneTree; ENSGT00390000004799; -.
DR   InParanoid; Q9GZE9; -.
DR   OMA; RTYFKMT; -.
DR   OrthoDB; 887497at2759; -.
DR   PhylomeDB; Q9GZE9; -.
DR   Reactome; R-CEL-114608; Platelet degranulation.
DR   PRO; PR:Q9GZE9; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00017719; Expressed in larva and 4 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0009247; P:glycolipid biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005097; Sacchrp_dh_NADP.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Lipid droplet; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..426
FT                   /note="Lipid droplet localized protein"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000442241"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..122
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_059216"
SQ   SEQUENCE   426 AA;  47294 MW;  4D9E6E891D6BB16A CRC64;
     MSRYDVVVYG ASGFTGAYVV EYLVNSEQFE GLSFAVAGRS EKKLREVLRN ISQKTGKDVS
     NAAVIVADSA DERSLNEMAR QANVVINAVG PYRLYGEAVV KAAVENGASH VDISGEPAWI
     EKMQQKYSKQ AKEQGVYVVS ACGWDSIPAD LGVNFLKKNF HGDLNHVESF VQLLTGPSGY
     SFNAGTYQTL ILGLSGAATD KLGAVRKEIM PEKIVRGAVK LPKRPTLWEI KEKELNGVAV
     PFPGADKSII NRSQYYDATS RQVRPIHMET YIRLSSQFYG YLIGLWIMFL SIFVKYPFTR
     RILQQYPDQC SFYMFKNSGP SARQMAEASF VYWFFGYGYK ETLPLDQQHE GKINRKVLAT
     CKGPDAGYIA TSGCVLSAAL TLIRDKDNLP KDGGVYTTAA AFGNSKIYDY LASFGITYQL
     ESEYDL
 
 
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