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LDAF1_RAT
ID   LDAF1_RAT               Reviewed;         161 AA.
AC   Q6UK00; Q6DGG2;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Lipid droplet assembly factor 1 {ECO:0000250|UniProtKB:Q96B96};
DE   AltName: Full=Promethin {ECO:0000303|PubMed:15589683};
DE   AltName: Full=Transmembrane protein 159;
GN   Name=Ldaf1 {ECO:0000312|RGD:727895}; Synonyms=Tmem159;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BDIX;
RX   PubMed=15589683; DOI=10.1016/j.biochi.2004.09.015;
RA   Yu S., Viswakarma N., Batra S.K., Sambasiva Rao M., Reddy J.K.;
RT   "Identification of promethin and PGLP as two novel up-regulated genes in
RT   PPARgamma1-induced adipogenic mouse liver.";
RL   Biochimie 86:743-761(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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 (By similarity). In association with BSCL2/seipin, defines
CC       the sites of LD formation in the endoplasmic reticulum (By similarity).
CC       {ECO:0000250|UniProtKB:Q96B96}.
CC   -!- SUBUNIT: Interacts with BSCL2/seipin to form an oligomeric complex.
CC       {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}. Note=Co-
CC       localizes with BSCL2/seipin in the ER, upon LD formation dissociates
CC       from BSCL2/seipin and relocalizes to LD surfaces during LD maturation.
CC       {ECO:0000250|UniProtKB:Q96B96}.
CC   -!- SIMILARITY: Belongs to the LDAF1 family. {ECO:0000305}.
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DR   EMBL; AY368496; AAQ74624.1; -; mRNA.
DR   EMBL; BC076384; AAH76384.1; -; mRNA.
DR   RefSeq; NP_919335.2; NM_194354.2.
DR   RefSeq; XP_006230200.1; XM_006230138.3.
DR   RefSeq; XP_017445000.1; XM_017589511.1.
DR   RefSeq; XP_017445001.1; XM_017589512.1.
DR   AlphaFoldDB; Q6UK00; -.
DR   SMR; Q6UK00; -.
DR   STRING; 10116.ENSRNOP00000065085; -.
DR   PaxDb; Q6UK00; -.
DR   GeneID; 378467; -.
DR   KEGG; rno:378467; -.
DR   CTD; 57146; -.
DR   RGD; 727895; Ldaf1.
DR   eggNOG; ENOG502S3TB; Eukaryota.
DR   InParanoid; Q6UK00; -.
DR   OrthoDB; 1492988at2759; -.
DR   PhylomeDB; Q6UK00; -.
DR   PRO; PR:Q6UK00; -.
DR   Proteomes; UP000002494; Unplaced.
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..161
FT                   /note="Lipid droplet assembly factor 1"
FT                   /id="PRO_0000279537"
FT   TOPO_DOM        1..43
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q96B96"
FT   TRANSMEM        44..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        62..67
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q96B96"
FT   TRANSMEM        68..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        88..93
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q96B96"
FT   TRANSMEM        94..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        111..116
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q96B96"
FT   TRANSMEM        117..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        134..161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q96B96"
FT   CONFLICT        7
FT                   /note="S -> P (in Ref. 2; AAH76384)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   161 AA;  17578 MW;  77D4738D3BAB07B5 CRC64;
     MAEEEPSSVS RDLQELQRKL GLLLESFQNN SKVVAFMKSP VGRFLDRHPF LVLTVLMFVT
     MSAIPVGFFL LIVVLTSLGA LMGAILLEGL VISVCGLSLL CILCGLGFVS LALSGITMMS
     YVVVSCLMSY WFSPSRPPTQ QHANIDSQLA MKFTESEKLG L
 
 
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