LMF1_MOUSE
ID LMF1_MOUSE Reviewed; 574 AA.
AC Q3U3R4; Q3TDV1; Q8BM33; Q8BY75; Q8VDX3; Q9CWX8;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Lipase maturation factor 1;
DE AltName: Full=Transmembrane protein 112;
GN Name=Lmf1; Synonyms=Tmem112;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Dendritic cell, Embryo, and Embryonic stem cell;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP INVOLVEMENT IN CLD, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17994020; DOI=10.1038/ng.2007.24;
RA Peterfy M., Ben-Zeev O., Mao H.Z., Weissglas-Volkov D., Aouizerat B.E.,
RA Pullinger C.R., Frost P.H., Kane J.P., Malloy M.J., Reue K., Pajukanta P.,
RA Doolittle M.H.;
RT "Mutations in LMF1 cause combined lipase deficiency and severe
RT hypertriglyceridemia.";
RL Nat. Genet. 39:1483-1487(2007).
RN [4]
RP RETRACTED PAPER.
RX PubMed=19783858; DOI=10.1074/jbc.m109.049395;
RA Doolittle M.H., Neher S.B., Ben-Zeev O., Ling-Liao J., Gallagher C.M.,
RA Hosseini M., Yin F., Wong H., Walter P., Peterfy M.;
RT "Lipase maturation factor LMF1, membrane topology and interaction with
RT lipase proteins in the endoplasmic reticulum.";
RL J. Biol. Chem. 284:33623-33633(2009).
RN [5]
RP RETRACTION NOTICE OF PUBMED:19783858.
RX PubMed=31399538; DOI=10.1074/jbc.w119.010212;
RA Doolittle M.H., Neher S.B., Ben-Zeev O., Ling-Liao J., Gallagher C.M.,
RA Hosseini M., Yin F., Wong H., Walter P., Peterfy M.;
RL J. Biol. Chem. 294:12263-12263(2019).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH LPL AND SEL1L.
RX PubMed=25066055; DOI=10.1016/j.cmet.2014.06.015;
RA Sha H., Sun S., Francisco A.B., Ehrhardt N., Xue Z., Liu L., Lawrence P.,
RA Mattijssen F., Guber R.D., Panhwar M.S., Brenna J.T., Shi H., Xue B.,
RA Kersten S., Bensadoun A., Peterfy M., Long Q., Qi L.;
RT "The ER-associated degradation adaptor protein Sel1L regulates LPL
RT secretion and lipid metabolism.";
RL Cell Metab. 20:458-470(2014).
CC -!- FUNCTION: Involved in the maturation of specific proteins in the
CC endoplasmic reticulum. Required for maturation and transport of active
CC lipoprotein lipase (LPL) through the secretory pathway. Each LMF1
CC molecule chaperones 50 or more molecules of LPL.
CC {ECO:0000250|UniProtKB:Q96S06, ECO:0000269|PubMed:17994020}.
CC -!- SUBUNIT: Interacts with LPL and SEL1L. {ECO:0000269|PubMed:25066055}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17994020}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17994020}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q3U3R4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U3R4-2; Sequence=VSP_022974;
CC Name=3;
CC IsoId=Q3U3R4-3; Sequence=VSP_022973;
CC Name=4;
CC IsoId=Q3U3R4-4; Sequence=VSP_022975, VSP_022976;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues synthesizing lipoprotein
CC lipase (Lpl) and hepatic lipase (Lipc), including adipose tissue,
CC skeletal muscle, heart, and liver. Expressed at higher levels in
CC tissues that express little or no lipase activity such as testis and
CC pancreas suggesting additional functions in these tissues.
CC {ECO:0000269|PubMed:17994020}.
CC -!- DISEASE: Note=Defects in Lmf1 are the cause of combined lipase
CC deficiency (cld). Cld is characterized by severe hypertriglyceridemia
CC with accumulation of chylomicrons that gradually pack the lumina of
CC capillaries and sinusoids. Severe hypertriglyceridemia causes an
CC increase in blood viscosity, ischemia, and cyanosis, and the inability
CC of tissues to access circulating triglycerides results in starvation,
CC poor thermoregulation, and death 2 to 3 days after birth. The disorder
CC is caused by a decrease in the activity of lipoprotein lipase (Lpl) and
CC the related hepatic lipase (Lipc), caused by impaired maturation of
CC nascent Lpl and hepatic lipase polypeptides in the endoplasmic
CC reticulum.
CC -!- SIMILARITY: Belongs to the lipase maturation factor family.
CC {ECO:0000305}.
CC -!- CAUTION: Additional evidence for its localization to the endoplasmic
CC reticulum membrane was found. However this paper was retracted due to
CC manipulation of data. {ECO:0000305|PubMed:19783858,
CC ECO:0000305|PubMed:31399538}.
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DR EMBL; AK010312; BAB26844.1; -; mRNA.
DR EMBL; AK035119; BAC28952.1; -; mRNA.
DR EMBL; AK041659; BAC31022.1; -; mRNA.
DR EMBL; AK154622; BAE32721.1; -; mRNA.
DR EMBL; AK169983; BAE41497.1; -; mRNA.
DR EMBL; BC020104; AAH20104.1; -; mRNA.
DR CCDS; CCDS37502.2; -. [Q3U3R4-1]
DR RefSeq; NP_083900.3; NM_029624.4. [Q3U3R4-1]
DR RefSeq; XP_006525159.1; XM_006525096.3.
DR AlphaFoldDB; Q3U3R4; -.
DR BioGRID; 218147; 2.
DR STRING; 10090.ENSMUSP00000112340; -.
DR iPTMnet; Q3U3R4; -.
DR PhosphoSitePlus; Q3U3R4; -.
DR EPD; Q3U3R4; -.
DR jPOST; Q3U3R4; -.
DR MaxQB; Q3U3R4; -.
DR PaxDb; Q3U3R4; -.
DR PeptideAtlas; Q3U3R4; -.
DR PRIDE; Q3U3R4; -.
DR ProteomicsDB; 252478; -. [Q3U3R4-1]
DR ProteomicsDB; 252479; -. [Q3U3R4-2]
DR ProteomicsDB; 252480; -. [Q3U3R4-3]
DR ProteomicsDB; 252481; -. [Q3U3R4-4]
DR Antibodypedia; 5146; 46 antibodies from 16 providers.
DR DNASU; 76483; -.
DR Ensembl; ENSMUST00000116641; ENSMUSP00000112340; ENSMUSG00000002279. [Q3U3R4-1]
DR GeneID; 76483; -.
DR KEGG; mmu:76483; -.
DR UCSC; uc008bbf.3; mouse. [Q3U3R4-1]
DR CTD; 64788; -.
DR MGI; MGI:1923733; Lmf1.
DR VEuPathDB; HostDB:ENSMUSG00000002279; -.
DR eggNOG; ENOG502QT4H; Eukaryota.
DR GeneTree; ENSGT00530000063702; -.
DR HOGENOM; CLU_020557_2_0_1; -.
DR InParanoid; Q3U3R4; -.
DR OrthoDB; 759759at2759; -.
DR PhylomeDB; Q3U3R4; -.
DR TreeFam; TF314339; -.
DR Reactome; R-MMU-8963889; Assembly of active LPL and LIPC lipase complexes.
DR BioGRID-ORCS; 76483; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Lmf1; mouse.
DR PRO; PR:Q3U3R4; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3U3R4; protein.
DR Bgee; ENSMUSG00000002279; Expressed in spermatocyte and 216 other tissues.
DR ExpressionAtlas; Q3U3R4; baseline and differential.
DR Genevisible; Q3U3R4; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034382; P:chylomicron remnant clearance; IMP:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:MGI.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IDA:MGI.
DR GO; GO:0006486; P:protein glycosylation; IMP:MGI.
DR GO; GO:0051604; P:protein maturation; IDA:MGI.
DR GO; GO:0009306; P:protein secretion; IMP:MGI.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:MGI.
DR GO; GO:0090207; P:regulation of triglyceride metabolic process; IMP:MGI.
DR GO; GO:0006641; P:triglyceride metabolic process; ISS:UniProtKB.
DR InterPro; IPR009613; LMF.
DR PANTHER; PTHR14463; PTHR14463; 1.
DR Pfam; PF06762; LMF1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..574
FT /note="Lipase maturation factor 1"
FT /id="PRO_0000276740"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..127
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..292
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..574
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..217
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022973"
FT VAR_SEQ 1..7
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_022974"
FT VAR_SEQ 173..188
FT /note="WESQLLETGFLGIFLS -> AQGAITSYPQSRTERE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022975"
FT VAR_SEQ 189..574
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022976"
FT CONFLICT 551
FT /note="L -> Q (in Ref. 2; AAH20104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 65878 MW; 98ED20FA865ACDBB CRC64;
MRPDSLVMAA PEGSLRKRKV GGAEHSPASQ PSLARDPADS PARLHTGTFW LTRIVLLRAL
AFIYFVAFLV AFNQNKALIG DRGLLPCKLY LKNVQEYFQG STGWAAWTYA PTIMWLLDWS
DMNFNLDLIA LLGLGISSFV LVTGCANMIL MTALWALYMS LVNVGQIWYS FGWESQLLET
GFLGIFLSPL WTLSRLPKNT PTSQIVLWGF RWLIFRIMLG AGLIKVRGDK CWLDLTCMDF
HYETQPVPNP IAYYLHRSPW WFHRFETLSN HFVELLVPFF LFLGRRMRIL HGVLQILFQV
ILIISGNLSF LNWLTIVPSL ACFDDAALGF LFPSGPQGLK KQVLEIQRED TQRVQPKPRD
RGCLVRQVVN ISLGILVAWL SVPVVINLLS SRQIMNTSFN PLRIVNTYGA FGSVTKERTE
VILQGTVSPN ASAPDAVWED YEFKCKPGDP WRQPCLISPY HYRLDWLMWF AAFQTYEQNE
WILHLAGKLL AGDSEALALL AVNPFEGRTP PRWIRGEHYR YKFSLPGGQH ATQGKWWIRK
RIGPYFPPLR LEDLKEYFKT REWPLPEPPS RHTR
