ID   LDF1B_XENLA             Reviewed;         162 AA.
AC   Q6GM19;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Lipid droplet assembly factor 1-B {ECO:0000250|UniProtKB:Q96B96};
DE   AltName: Full=Promethin-B;
DE   AltName: Full=Transmembrane protein 159-B;
GN   Name=ldaf1-b {ECO:0000250|UniProtKB:Q96B96}; Synonyms=tmem159-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in the formation of lipid droplets
CC       (LD) which are storage organelles at the center of lipid and energy
CC       homeostasis. {ECO:0000250|UniProtKB:Q96B96}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q96B96}; Multi-pass membrane protein
CC       {ECO:0000255}. Lipid droplet {ECO:0000250|UniProtKB:Q96B96}.
CC   -!- SIMILARITY: Belongs to the LDAF1 family. {ECO:0000305}.
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DR   EMBL; BC074271; AAH74271.1; -; mRNA.
DR   RefSeq; NP_001086158.1; NM_001092689.1.
DR   AlphaFoldDB; Q6GM19; -.
DR   DNASU; 444587; -.
DR   GeneID; 444587; -.
DR   KEGG; xla:444587; -.
DR   CTD; 444587; -.
DR   Xenbase; XB-GENE-6254876; ldaf1.S.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 444587; Expressed in muscle tissue and 18 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR   GO; GO:0140042; P:lipid droplet formation; ISS:UniProtKB.
DR   InterPro; IPR029709; LDAF1.
DR   PANTHER; PTHR14275; PTHR14275; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Lipid droplet; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..162
FT                   /note="Lipid droplet assembly factor 1-B"
FT                   /id="PRO_0000279539"
FT   TOPO_DOM        1..42
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q96B96"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..65
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q96B96"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q96B96"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        109
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q96B96"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        131..162
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q96B96"
SQ   SEQUENCE   162 AA;  17401 MW;  64BD974FFC0544D9 CRC64;
     MASAEKLYRE KMQELQKQLN KFMQTINNHS KVDAFLNSPF GQYLDEHPFV TLSLLVFVSL
     SVVPAGLFLT LVAGTAIAVC LAVLIIEGIV ISVSGIALLC ILCGLAVMSL GVAAILCVSY
     VAGSSVFNYM HAYRVAVGTR ERSGPISLNH KMTMAEKSLS SS