LMF2_MOUSE
ID LMF2_MOUSE Reviewed; 702 AA.
AC Q8C3X8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Lipase maturation factor 2;
DE AltName: Full=Transmembrane protein 112B;
DE AltName: Full=Transmembrane protein 153;
GN Name=Lmf2; Synonyms=Tmem112b, Tmem153;
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].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Heart;
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].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and 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).
CC -!- FUNCTION: Involved in the maturation of specific proteins in the
CC endoplasmic reticulum. May be required for maturation and transport of
CC active lipoprotein lipase (LPL) through the secretory pathway (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lipase maturation factor family.
CC {ECO:0000305}.
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DR EMBL; AK084606; BAC39228.1; -; mRNA.
DR EMBL; AK149916; BAE29164.1; -; mRNA.
DR EMBL; AK149934; BAE29177.1; -; mRNA.
DR EMBL; AK171488; BAE42488.1; -; mRNA.
DR EMBL; BC079532; AAH79532.1; -; mRNA.
DR CCDS; CCDS27746.1; -.
DR RefSeq; NP_849250.1; NM_178919.4.
DR AlphaFoldDB; Q8C3X8; -.
DR BioGRID; 222935; 2.
DR STRING; 10090.ENSMUSP00000023283; -.
DR GlyGen; Q8C3X8; 1 site.
DR iPTMnet; Q8C3X8; -.
DR PhosphoSitePlus; Q8C3X8; -.
DR EPD; Q8C3X8; -.
DR jPOST; Q8C3X8; -.
DR MaxQB; Q8C3X8; -.
DR PaxDb; Q8C3X8; -.
DR PeptideAtlas; Q8C3X8; -.
DR PRIDE; Q8C3X8; -.
DR ProteomicsDB; 290049; -.
DR Antibodypedia; 28648; 128 antibodies from 21 providers.
DR Ensembl; ENSMUST00000023283; ENSMUSP00000023283; ENSMUSG00000022614.
DR GeneID; 105847; -.
DR KEGG; mmu:105847; -.
DR UCSC; uc007xgd.2; mouse.
DR CTD; 91289; -.
DR MGI; MGI:2146015; Lmf2.
DR VEuPathDB; HostDB:ENSMUSG00000022614; -.
DR eggNOG; ENOG502QTN6; Eukaryota.
DR GeneTree; ENSGT00530000063702; -.
DR HOGENOM; CLU_020557_1_0_1; -.
DR InParanoid; Q8C3X8; -.
DR OMA; FMWFQWD; -.
DR OrthoDB; 759759at2759; -.
DR PhylomeDB; Q8C3X8; -.
DR TreeFam; TF314339; -.
DR Reactome; R-MMU-8963889; Assembly of active LPL and LIPC lipase complexes.
DR BioGRID-ORCS; 105847; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Lmf2; mouse.
DR PRO; PR:Q8C3X8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8C3X8; protein.
DR Bgee; ENSMUSG00000022614; Expressed in humerus cartilage element and 207 other tissues.
DR ExpressionAtlas; Q8C3X8; baseline and differential.
DR Genevisible; Q8C3X8; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051604; P:protein maturation; IBA:GO_Central.
DR InterPro; IPR009613; LMF.
DR PANTHER; PTHR14463; PTHR14463; 1.
DR Pfam; PF06762; LMF1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..702
FT /note="Lipase maturation factor 2"
FT /id="PRO_0000324511"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 660..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 702 AA; 79997 MW; D6E880D37C517A17 CRC64;
MASSRVPQQL FLQGVAAVYL FAFASLYTQI PGLYGPEGIL PARRTLRPQG KGLWQQLWET
PTLLWEAPRL GLDTAQGLDL LTLLGTVLAL GALLLNSLRH PFVYLLLWVA YRSAYQVGQV
FLYFQWDSLL LETGFLAILV APLRGPSKHK ILQGRLAGAL PHEDLPFWLV RWLLFRLMFA
SGVVKLTSRC PTWWGLTALT YHYETQCLPT PAAWFAHHLP VWLHKLSVVA TFLIEIAVPP
LFFAPIRRLR LTAFYAQALL QVLIIITGNY NFFNLLTLVL TTALLDDRHL SAEPGLRCHK
KMPTSWPKAL LTALSLLLEL TVYGLLAYGT VYYFGLEVDW QQHIILSKTT FTFHQFSQWL
KTVTLPTVWL GTASLAWELL VVLWRWIQVQ GWSRKFSAGI QLSVLGTATV ALFLISLVPY
SYVEPGTHGR LWTGAHRLFG SVEHLQLANS YGLFRRMTGV GGRPEVVLEG SYDGQHWTEI
EFMYKPGNVS RPPPFLTPHQ PRLDWQMWFA ALGPHTHSPW FTGLVLRLLQ GKEPVIRLVQ
SHVANYPFHE RPPTYLRAQR YKYWFSKPGD QSRWWHRQWV EEFFPSVSLG DPTLETLLQQ
FGLKDKSPPR ARSPSNGLAQ TLNWVRTQLS PLEPPILLWG LFGAVVAIRV VQTLLAPRPL
QSSKQTREEK RKQTSKKDSR AASEQAAANS NSRDSWAPRR KK
