ID   MEST_MOUSE              Reviewed;         335 AA.
AC   Q07646; Q792T8; Q8BS88; Q8K463; Q99KT5;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 152.
DE   RecName: Full=Mesoderm-specific transcript protein;
DE            EC=3.-.-.-;
DE   AltName: Full=Paternally-expressed gene 1 protein;
GN   Name=Mest; Synonyms=Peg1; ORFNames=121a;
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] (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RA   Sado T., Nakajima N., Tada M., Takagi N.;
RT   "A novel mesoderm-specific cDNA isolated from a mouse embryonal carcinoma
RT   cell line.";
RL   Dev. Growth Differ. 35:551-560(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RC   STRAIN=C57BL/6J;
RX   PubMed=12095916; DOI=10.1093/hmg/11.15.1743;
RA   Nakabayashi K., Bentley L., Hitchins M.P., Mitsuya K., Meguro M.,
RA   Minagawa S., Bamforth J.S., Stanier P., Preece M., Weksberg R.,
RA   Oshimura M., Moore G.E., Scherer S.W.;
RT   "Identification and characterization of an imprinted antisense RNA
RT   (MESTIT1) in the human MEST locus on chromosome 7q32.";
RL   Hum. Mol. Genet. 11:1743-1756(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Amnion, Embryo, Heart, Kidney, and Wolffian duct;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; 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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
RC   STRAIN=129/Sv;
RX   PubMed=9302270; DOI=10.1093/hmg/6.11.1907;
RA   Lefebvre L., Viville S., Barton S.C., Ishino F., Surani M.A.;
RT   "Genomic structure and parent-of-origin-specific methylation of Peg1.";
RL   Hum. Mol. Genet. 6:1907-1915(1997).
RN   [6]
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
RC   STRAIN=129/Sv;
RX   PubMed=7550314; DOI=10.1038/ng0995-52;
RA   Kaneko-Ishino T., Kuroiwa Y., Miyoshi N., Kohda T., Suzuki R., Yokoyama M.,
RA   Viville S., Barton S.C., Ishino F., Surani M.A.;
RT   "Peg1/Mest imprinted gene on chromosome 6 identified by cDNA subtraction
RT   hybridization.";
RL   Nat. Genet. 11:52-59(1995).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18644838; DOI=10.1096/fj.08-108266;
RA   Nikonova L., Koza R.A., Mendoza T., Chao P.-M., Curley J.P., Kozak L.P.;
RT   "Mesoderm-specific transcript is associated with fat mass expansion in
RT   response to a positive energy balance.";
RL   FASEB J. 22:3925-3937(2008).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:18644838}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:18644838}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q07646-1; Sequence=Displayed;
CC       Name=2; Synonyms=MEST intronic transcript 1;
CC         IsoId=Q07646-2; Sequence=VSP_024534;
CC   -!- TISSUE SPECIFICITY: Expressed in mesodermal tissues. Isoform 1 is
CC       exclusively expressed from the paternal allele in all fetal tissues and
CC       cell lines examined, whereas isoform 2 is preferentially expressed from
CC       the paternal allele in a tissue-type-specific manner.
CC       {ECO:0000269|PubMed:7550314}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the nascent mesoderm of gastrulating
CC       embryos. At 7.0 dpc expression detected in both the intraembryonic
CC       mesoderm and the extraembryonic mesoderm cells of the amniotic fold. At
CC       8.5 dpc expressed predominantly in the head mesenchyme, allantois, and
CC       the mesodermal layer of the amnion, chorion and yolk. In 9.5 dpc
CC       embryos highly expressed in the mesenchymal tissues, presomitic
CC       paraxial mesoderm, heart and branchial arches. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; D16262; BAA03795.1; -; mRNA.
DR   EMBL; AF482999; AAM78507.1; -; mRNA.
DR   EMBL; AK032881; BAC28068.1; -; mRNA.
DR   EMBL; AK034949; BAC28891.1; -; mRNA.
DR   EMBL; AK168714; BAE40556.1; -; mRNA.
DR   EMBL; AK168732; BAE40573.1; -; mRNA.
DR   EMBL; AK168743; BAE40584.1; -; mRNA.
DR   EMBL; AK168995; BAE40794.1; -; mRNA.
DR   EMBL; AK169095; BAE40878.1; -; mRNA.
DR   EMBL; AK169266; BAE41027.1; -; mRNA.
DR   EMBL; BC004019; AAH04019.1; -; mRNA.
DR   EMBL; BC006639; AAH06639.1; -; mRNA.
DR   EMBL; AF017994; AAC53396.1; -; Genomic_DNA.
DR   CCDS; CCDS19979.1; -. [Q07646-1]
DR   CCDS; CCDS80513.1; -. [Q07646-2]
DR   RefSeq; NP_001239221.1; NM_001252292.1.
DR   RefSeq; NP_001239222.1; NM_001252293.1. [Q07646-2]
DR   RefSeq; NP_032616.1; NM_008590.2. [Q07646-1]
DR   AlphaFoldDB; Q07646; -.
DR   SMR; Q07646; -.
DR   BioGRID; 201402; 2.
DR   IntAct; Q07646; 1.
DR   MINT; Q07646; -.
DR   STRING; 10090.ENSMUSP00000117713; -.
DR   ESTHER; mouse-MEST; MEST-like.
DR   MEROPS; S33.972; -.
DR   GlyCosmos; Q07646; 1 site, No reported glycans.
DR   GlyGen; Q07646; 1 site.
DR   PhosphoSitePlus; Q07646; -.
DR   MaxQB; Q07646; -.
DR   PaxDb; 10090-ENSMUSP00000129639; -.
DR   PeptideAtlas; Q07646; -.
DR   ProteomicsDB; 295931; -. [Q07646-1]
DR   ProteomicsDB; 295932; -. [Q07646-2]
DR   Antibodypedia; 946; 138 antibodies from 32 providers.
DR   DNASU; 17294; -.
DR   Ensembl; ENSMUST00000157040.8; ENSMUSP00000119038.3; ENSMUSG00000051855.16. [Q07646-2]
DR   Ensembl; ENSMUST00000163949.9; ENSMUSP00000129639.3; ENSMUSG00000051855.16. [Q07646-1]
DR   GeneID; 17294; -.
DR   KEGG; mmu:17294; -.
DR   UCSC; uc009bfs.2; mouse. [Q07646-1]
DR   AGR; MGI:96968; -.
DR   CTD; 4232; -.
DR   MGI; MGI:96968; Mest.
DR   VEuPathDB; HostDB:ENSMUSG00000051855; -.
DR   eggNOG; KOG4178; Eukaryota.
DR   GeneTree; ENSGT00510000047602; -.
DR   InParanoid; Q07646; -.
DR   OrthoDB; 907220at2759; -.
DR   PhylomeDB; Q07646; -.
DR   TreeFam; TF329307; -.
DR   BioGRID-ORCS; 17294; 2 hits in 80 CRISPR screens.
DR   ChiTaRS; Mest; mouse.
DR   PRO; PR:Q07646; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q07646; Protein.
DR   Bgee; ENSMUSG00000051855; Expressed in humerus cartilage element and 284 other cell types or tissues.
DR   ExpressionAtlas; Q07646; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0010883; P:regulation of lipid storage; IMP:UniProtKB.
DR   GO; GO:0032526; P:response to retinoic acid; IDA:BHF-UCL.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR   PANTHER; PTHR43798:SF5; MONOACYLGLYCEROL LIPASE ABHD6; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   Genevisible; Q07646; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..335
FT                   /note="Mesoderm-specific transcript protein"
FT                   /id="PRO_0000284419"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          71..310
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   MOTIF           98..103
FT                   /note="RVIALD"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..9
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12095916"
FT                   /id="VSP_024534"
FT   CONFLICT        43
FT                   /note="W -> C (in Ref. 3; BAC28891)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="K -> N (in Ref. 2; AAM78507)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   335 AA;  38907 MW;  F5F394F46152E712 CRC64;
     MVRRDRLRRM REWWVQVGLL AVPLLAAYLH IPPPQLSPAL HSWKTSGKFF TYKGLRIFYQ
     DSVGVVGSPE IVVLLHGFPT SSYDWYKIWE GLTLRFHRVI ALDFLGFGFS DKPRPHQYSI
     FEQASIVESL LRHLGLQNRR INLLSHDYGD IVAQELLYRY KQNRSGRLTI KSLCLSNGGI
     FPETHRPLLL QKLLKDGGVL SPILTRLMNF FVFSRGLTPV FGPYTRPTES ELWDMWAVIR
     NNDGNLVIDS LLQYINQRKK FRRRWVGALA SVSIPIHFIY GPLDPINPYP EFLELYRKTL
     PRSTVSILDD HISHYPQLED PMGFLNAYMG FINSF
//