LDAF1_MOUSE
ID LDAF1_MOUSE Reviewed; 161 AA.
AC Q922Z1; Q8C5E0;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Lipid droplet assembly factor 1 {ECO:0000250|UniProtKB:Q96B96};
DE AltName: Full=Promethin {ECO:0000303|PubMed:15589683, ECO:0000303|PubMed:30901948};
DE AltName: Full=Transmembrane protein 159;
GN Name=Ldaf1 {ECO:0000250|UniProtKB:Q96B96};
GN Synonyms=Tmem159 {ECO:0000312|MGI:MGI:1925752};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 STRAIN=C57BL/6J; TISSUE=Bone marrow, Heart, Inner ear, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
RN [4]
RP INDUCTION.
RX PubMed=30901948; DOI=10.3390/cells8030268;
RA Castro I.G., Eisenberg-Bord M., Persiani E., Rochford J.J., Schuldiner M.,
RA Bohnert M.;
RT "Promethin Is a Conserved Seipin Partner Protein.";
RL Cells 8:0-0(2019).
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 -!- TISSUE SPECIFICITY: Prominently expressed in the heart and kidney.
CC Expressed at higher levels in white fat as compared to brown fat and
CC skeletal muscle. Expressed at lower levels in lung, liver and testis.
CC {ECO:0000269|PubMed:15589683}.
CC -!- INDUCTION: In liver with hepatic adiposis caused by PPAR gamma 1
CC overexpression (PubMed:15589683). Up-regulated during adipogenesis
CC (PubMed:30901948). {ECO:0000269|PubMed:15589683,
CC ECO:0000269|PubMed:30901948}.
CC -!- SIMILARITY: Belongs to the LDAF1 family. {ECO:0000305}.
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DR EMBL; AY167031; AAO11832.1; -; mRNA.
DR EMBL; AK078811; BAC37405.1; -; mRNA.
DR EMBL; AK087074; BAC39797.1; -; mRNA.
DR EMBL; AK142240; BAE24990.1; -; mRNA.
DR EMBL; AK150434; BAE29557.1; -; mRNA.
DR EMBL; AK158048; BAE34335.1; -; mRNA.
DR EMBL; AK158249; BAE34426.1; -; mRNA.
DR EMBL; AK167135; BAE39281.1; -; mRNA.
DR EMBL; AK167192; BAE39322.1; -; mRNA.
DR EMBL; AK171378; BAE42420.1; -; mRNA.
DR EMBL; BC006689; AAH06689.1; -; mRNA.
DR CCDS; CCDS21791.1; -.
DR RefSeq; NP_663561.1; NM_145586.1.
DR RefSeq; XP_006507745.1; XM_006507682.3.
DR AlphaFoldDB; Q922Z1; -.
DR SMR; Q922Z1; -.
DR STRING; 10090.ENSMUSP00000033210; -.
DR PhosphoSitePlus; Q922Z1; -.
DR MaxQB; Q922Z1; -.
DR PaxDb; Q922Z1; -.
DR PRIDE; Q922Z1; -.
DR ProteomicsDB; 259538; -.
DR Antibodypedia; 3080; 36 antibodies from 11 providers.
DR DNASU; 233806; -.
DR Ensembl; ENSMUST00000033210; ENSMUSP00000033210; ENSMUSG00000030917.
DR Ensembl; ENSMUST00000118737; ENSMUSP00000114085; ENSMUSG00000030917.
DR GeneID; 233806; -.
DR KEGG; mmu:233806; -.
DR UCSC; uc009jmh.1; mouse.
DR CTD; 233806; -.
DR MGI; MGI:1925752; Tmem159.
DR VEuPathDB; HostDB:ENSMUSG00000030917; -.
DR eggNOG; ENOG502S3TB; Eukaryota.
DR GeneTree; ENSGT00390000006420; -.
DR HOGENOM; CLU_142333_0_0_1; -.
DR InParanoid; Q922Z1; -.
DR OMA; FMNSRVG; -.
DR OrthoDB; 1492988at2759; -.
DR PhylomeDB; Q922Z1; -.
DR TreeFam; TF335782; -.
DR BioGRID-ORCS; 233806; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Tmem159; mouse.
DR PRO; PR:Q922Z1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q922Z1; protein.
DR Bgee; ENSMUSG00000030917; Expressed in lip and 203 other tissues.
DR Genevisible; Q922Z1; MM.
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_0000279536"
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 105
FT /note="G -> S (in Ref. 2; BAC37405)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 17643 MW; AB2527A56EEA6CF9 CRC64;
MAKEEPPSVS RDLQELQRKL GLLLESFLNN SKVVAFMKSP VGRFLDRHPF VTLTVLMFVT
MSAIPVGFFL LIVVLTSLGA LMGAILLEGL VISVCGLSLL CVLCGLGFLS LALSGIAMMS
YVVVSCLMSY WFSPSRPLTQ QNANVDCQLA MKFTESERLI F
