LDAF1_HUMAN
ID LDAF1_HUMAN Reviewed; 161 AA.
AC Q96B96; A6NMA9; B4DEC1; O00323;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Lipid droplet assembly factor 1 {ECO:0000303|PubMed:31708432};
DE AltName: Full=Promethin {ECO:0000303|PubMed:15589683, ECO:0000303|PubMed:30901948};
DE AltName: Full=Transmembrane protein 159;
GN Name=LDAF1 {ECO:0000312|HGNC:HGNC:30136}; Synonyms=TMEM159;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP ASP-154.
RC TISSUE=Heart;
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] (ISOFORMS 1 AND 2), AND VARIANT
RP ASP-154.
RC TISSUE=Cerebellum, and Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-107.
RC TISSUE=Skin;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP INTERACTION WITH BSCL2, AND SUBCELLULAR LOCATION.
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).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BSCL2, AND TOPOLOGY.
RX PubMed=31708432; DOI=10.1016/j.devcel.2019.10.006;
RA Chung J., Wu X., Lambert T.J., Lai Z.W., Walther T.C., Farese R.V. Jr.;
RT "LDAF1 and Seipin Form a Lipid Droplet Assembly Complex.";
RL Dev. Cell 0:0-0(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 (PubMed:31708432). In association with BSCL2/seipin,
CC defines the sites of LD formation in the endoplasmic reticulum
CC (PubMed:31708432). {ECO:0000269|PubMed:31708432}.
CC -!- SUBUNIT: Interacts with isoform 1 and isoform 3 of BSCL2/seipin to form
CC an oligomeric complex. {ECO:0000269|PubMed:30901948,
CC ECO:0000269|PubMed:31708432}.
CC -!- INTERACTION:
CC Q96B96; Q9UGQ2: CACFD1; NbExp=4; IntAct=EBI-7055862, EBI-8652492;
CC Q96B96; Q8NI60: COQ8A; NbExp=8; IntAct=EBI-7055862, EBI-745535;
CC Q96B96; Q05329: GAD2; NbExp=6; IntAct=EBI-7055862, EBI-9304251;
CC Q96B96; A8MRB1: S100B; NbExp=3; IntAct=EBI-7055862, EBI-16432654;
CC Q96B96; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-7055862, EBI-8652744;
CC Q96B96; Q6P1K1: SLC48A1; NbExp=3; IntAct=EBI-7055862, EBI-1222191;
CC Q96B96; Q17RD7: SYT16; NbExp=3; IntAct=EBI-7055862, EBI-10238936;
CC Q96B96; Q96HH6: TMEM19; NbExp=3; IntAct=EBI-7055862, EBI-741829;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:30901948, ECO:0000269|PubMed:31708432}; Multi-pass
CC membrane protein {ECO:0000255}. Lipid droplet
CC {ECO:0000269|PubMed:30901948, ECO:0000269|PubMed:31708432}. 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:0000269|PubMed:31708432}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96B96-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96B96-2; Sequence=VSP_056078;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the heart and skeletal
CC muscle. Expressed at low levels in kidney, small intestine, lung and
CC liver. {ECO:0000269|PubMed:15589683}.
CC -!- SIMILARITY: Belongs to the LDAF1 family. {ECO:0000305}.
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DR EMBL; AY212918; AAO52682.1; -; mRNA.
DR EMBL; AK074667; BAC11122.1; -; mRNA.
DR EMBL; AK293557; BAG57032.1; -; mRNA.
DR EMBL; AF001550; AAB67598.1; -; Genomic_DNA.
DR EMBL; AC008551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015812; AAH15812.1; -; mRNA.
DR CCDS; CCDS10595.1; -. [Q96B96-1]
DR CCDS; CCDS76841.1; -. [Q96B96-2]
DR RefSeq; NP_001288698.1; NM_001301769.1. [Q96B96-1]
DR RefSeq; NP_001288700.1; NM_001301771.1. [Q96B96-1]
DR RefSeq; NP_001288702.1; NM_001301773.1.
DR RefSeq; NP_001288703.1; NM_001301774.1.
DR RefSeq; NP_001288704.1; NM_001301775.1. [Q96B96-2]
DR RefSeq; NP_065155.3; NM_020422.5. [Q96B96-1]
DR RefSeq; XP_005255496.1; XM_005255439.4. [Q96B96-2]
DR RefSeq; XP_006721129.1; XM_006721066.2. [Q96B96-2]
DR AlphaFoldDB; Q96B96; -.
DR SMR; Q96B96; -.
DR BioGRID; 121403; 65.
DR IntAct; Q96B96; 15.
DR MINT; Q96B96; -.
DR STRING; 9606.ENSP00000233047; -.
DR iPTMnet; Q96B96; -.
DR PhosphoSitePlus; Q96B96; -.
DR BioMuta; TMEM159; -.
DR DMDM; 313104024; -.
DR EPD; Q96B96; -.
DR jPOST; Q96B96; -.
DR MassIVE; Q96B96; -.
DR MaxQB; Q96B96; -.
DR PaxDb; Q96B96; -.
DR PeptideAtlas; Q96B96; -.
DR PRIDE; Q96B96; -.
DR ProteomicsDB; 3940; -.
DR ProteomicsDB; 76056; -. [Q96B96-1]
DR Antibodypedia; 3080; 36 antibodies from 11 providers.
DR DNASU; 57146; -.
DR Ensembl; ENST00000233047.9; ENSP00000233047.4; ENSG00000011638.11. [Q96B96-1]
DR Ensembl; ENST00000261388.7; ENSP00000261388.3; ENSG00000011638.11. [Q96B96-1]
DR Ensembl; ENST00000451578.6; ENSP00000409879.2; ENSG00000011638.11. [Q96B96-2]
DR Ensembl; ENST00000572599.5; ENSP00000460687.1; ENSG00000011638.11. [Q96B96-1]
DR Ensembl; ENST00000638934.1; ENSP00000492501.1; ENSG00000283997.1. [Q96B96-1]
DR Ensembl; ENST00000639177.1; ENSP00000492842.1; ENSG00000283997.1. [Q96B96-2]
DR Ensembl; ENST00000640188.1; ENSP00000491056.1; ENSG00000283997.1. [Q96B96-1]
DR Ensembl; ENST00000640514.1; ENSP00000492164.1; ENSG00000283997.1. [Q96B96-1]
DR GeneID; 57146; -.
DR KEGG; hsa:57146; -.
DR MANE-Select; ENST00000233047.9; ENSP00000233047.4; NM_001301771.2; NP_001288700.1.
DR UCSC; uc002dif.5; human. [Q96B96-1]
DR CTD; 57146; -.
DR DisGeNET; 57146; -.
DR GeneCards; LDAF1; -.
DR HGNC; HGNC:30136; LDAF1.
DR HPA; ENSG00000011638; Tissue enhanced (skeletal).
DR MIM; 611304; gene.
DR neXtProt; NX_Q96B96; -.
DR OpenTargets; ENSG00000011638; -.
DR VEuPathDB; HostDB:ENSG00000011638; -.
DR eggNOG; ENOG502S3TB; Eukaryota.
DR GeneTree; ENSGT00390000006420; -.
DR InParanoid; Q96B96; -.
DR OMA; FMNSRVG; -.
DR OrthoDB; 1492988at2759; -.
DR PhylomeDB; Q96B96; -.
DR TreeFam; TF335782; -.
DR PathwayCommons; Q96B96; -.
DR SignaLink; Q96B96; -.
DR BioGRID-ORCS; 57146; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; TMEM159; human.
DR GenomeRNAi; 57146; -.
DR Pharos; Q96B96; Tdark.
DR PRO; PR:Q96B96; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96B96; protein.
DR Bgee; ENSG00000011638; Expressed in skin of leg and 106 other tissues.
DR ExpressionAtlas; Q96B96; baseline and differential.
DR Genevisible; Q96B96; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0140042; P:lipid droplet formation; IMP:UniProtKB.
DR InterPro; IPR029709; LDAF1.
DR PANTHER; PTHR14275; PTHR14275; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Lipid droplet; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..161
FT /note="Lipid droplet assembly factor 1"
FT /id="PRO_0000279535"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31708432"
FT TRANSMEM 44..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..67
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:31708432"
FT TRANSMEM 68..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31708432"
FT TRANSMEM 94..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..116
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:31708432"
FT TRANSMEM 117..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31708432"
FT VAR_SEQ 30
FT /note="N -> NSKLPQHSRISLDSDDGVSRLGSAG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056078"
FT VARIANT 97
FT /note="F -> L (in dbSNP:rs35345508)"
FT /id="VAR_057765"
FT VARIANT 107
FT /note="G -> S (in dbSNP:rs1046480)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030923"
FT VARIANT 154
FT /note="E -> D (in dbSNP:rs1063087)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15589683"
FT /id="VAR_030924"
SQ SEQUENCE 161 AA; 17522 MW; 196B502EE203BA7E CRC64;
MAKEEPQSIS RDLQELQKKL SLLIDSFQNN SKVVAFMKSP VGQYLDSHPF LAFTLLVFIV
MSAVPVGFFL LIVVLTTLAA LLGVIILEGL VISVGGFSLL CILCGLGFVS LAMSGMMIAS
YVVVSSLISC WFSPRPLTQQ NTSCDFLPAM KSAEFEGLYQ E
