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