MSLN_MOUSE
ID MSLN_MOUSE Reviewed; 625 AA.
AC Q61468;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Mesothelin;
DE AltName: Full=Pre-pro-megakaryocyte-potentiating factor;
DE Contains:
DE RecName: Full=Megakaryocyte-potentiating factor;
DE Short=MPF;
DE Contains:
DE RecName: Full=Mesothelin, cleaved form;
DE Flags: Precursor;
GN Name=Msln; Synonyms=Mes, Mpf;
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].
RA Kojima T., Taniguchi Y., Hattori K., Oh-eda M.;
RT "Mouse megakaryocyte potentiating factor cDNA.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Seminal vesicle;
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 FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=10733593; DOI=10.1128/mcb.20.8.2902-2906.2000;
RA Bera T.K., Pastan I.;
RT "Mesothelin is not required for normal mouse development or reproduction.";
RL Mol. Cell. Biol. 20:2902-2906(2000).
RN [5]
RP INDUCTION BY WNT1.
RX PubMed=12697065; DOI=10.1186/1471-213x-3-2;
RA Prieve M.G., Moon R.T.;
RT "Stromelysin-1 and mesothelin are differentially regulated by Wnt-5a and
RT Wnt-1 in C57mg mouse mammary epithelial cells.";
RL BMC Dev. Biol. 3:2-2(2003).
RN [6]
RP INTERACTION WITH MUC16, DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=14676194; DOI=10.1074/jbc.m312372200;
RA Rump A., Morikawa Y., Tanaka M., Minami S., Umesaki N., Takeuchi M.,
RA Miyajima A.;
RT "Binding of ovarian cancer antigen CA125/MUC16 to mesothelin mediates cell
RT adhesion.";
RL J. Biol. Chem. 279:9190-9198(2004).
CC -!- FUNCTION: Membrane-anchored forms may play a role in cellular adhesion.
CC {ECO:0000269|PubMed:10733593, ECO:0000269|PubMed:14676194}.
CC -!- FUNCTION: Megakaryocyte-potentiating factor (MPF) may potentiate
CC megakaryocyte colony formation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MUC16. {ECO:0000269|PubMed:14676194}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}. Golgi apparatus {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Megakaryocyte-potentiating factor]: Secreted
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung and heart. Expressed at
CC low levels in spleen, liver, kidney and testis. Present in lung (at
CC protein level). {ECO:0000269|PubMed:10733593}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 7 dpc, down-regulated at 11 dpc, re-
CC expressed at 15 dpc and peaks at 17 dpc. Present in embryonic diaphragm
CC (at protein level). {ECO:0000269|PubMed:10733593,
CC ECO:0000269|PubMed:14676194}.
CC -!- INDUCTION: By WNT1 but not by WNT5A in mammary epithelial cells.
CC {ECO:0000269|PubMed:12697065}.
CC -!- PTM: Proteolytically cleaved by a furin-like convertase to generate
CC megakaryocyte-potentiating factor (MPF), and the cleaved form of
CC mesothelin. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice have normal growth and reproductive
CC function, and normal platelet counts. {ECO:0000269|PubMed:10733593}.
CC -!- SIMILARITY: Belongs to the mesothelin family. {ECO:0000305}.
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DR EMBL; D86370; BAA13077.1; -; mRNA.
DR EMBL; AK146799; BAE27441.1; -; mRNA.
DR EMBL; AK144391; BAE25864.1; -; mRNA.
DR EMBL; BC023753; AAH23753.1; -; mRNA.
DR CCDS; CCDS28526.1; -.
DR RefSeq; NP_061345.1; NM_018857.1.
DR RefSeq; XP_006524713.1; XM_006524650.3.
DR AlphaFoldDB; Q61468; -.
DR SMR; Q61468; -.
DR IntAct; Q61468; 1.
DR STRING; 10090.ENSMUSP00000075279; -.
DR GlyGen; Q61468; 4 sites.
DR PhosphoSitePlus; Q61468; -.
DR CPTAC; non-CPTAC-3929; -.
DR MaxQB; Q61468; -.
DR PaxDb; Q61468; -.
DR PeptideAtlas; Q61468; -.
DR PRIDE; Q61468; -.
DR ProteomicsDB; 295597; -.
DR ABCD; Q61468; 1 sequenced antibody.
DR Antibodypedia; 2310; 860 antibodies from 45 providers.
DR DNASU; 56047; -.
DR Ensembl; ENSMUST00000237359; ENSMUSP00000158474; ENSMUSG00000063011.
DR Ensembl; ENSMUST00000238120; ENSMUSP00000158357; ENSMUSG00000063011.
DR GeneID; 56047; -.
DR KEGG; mmu:56047; -.
DR UCSC; uc008bbo.1; mouse.
DR CTD; 10232; -.
DR MGI; MGI:1888992; Msln.
DR VEuPathDB; HostDB:ENSMUSG00000063011; -.
DR eggNOG; ENOG502QRX1; Eukaryota.
DR GeneTree; ENSGT00950000182957; -.
DR HOGENOM; CLU_014552_3_0_1; -.
DR InParanoid; Q61468; -.
DR OMA; DFTCTEV; -.
DR OrthoDB; 459771at2759; -.
DR PhylomeDB; Q61468; -.
DR TreeFam; TF331713; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 56047; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Msln; mouse.
DR PRO; PR:Q61468; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q61468; protein.
DR Bgee; ENSMUSG00000063011; Expressed in left lung lobe and 109 other tissues.
DR ExpressionAtlas; Q61468; baseline and differential.
DR Genevisible; Q61468; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR InterPro; IPR010335; Mesothelin.
DR InterPro; IPR026664; Stereocilin-rel.
DR PANTHER; PTHR23412; PTHR23412; 1.
DR Pfam; PF06060; Mesothelin; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW Disulfide bond; Glycoprotein; Golgi apparatus; GPI-anchor; Lipoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..600
FT /note="Mesothelin"
FT /id="PRO_0000253562"
FT CHAIN 36..288
FT /note="Megakaryocyte-potentiating factor"
FT /id="PRO_0000253563"
FT CHAIN 298..600
FT /note="Mesothelin, cleaved form"
FT /id="PRO_0000253564"
FT PROPEP 601..625
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000253565"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13421"
FT LIPID 600
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 304..328
FT /evidence="ECO:0000250"
SQ SEQUENCE 625 AA; 69423 MW; 9A5E9C3222C6983F CRC64;
MALPTARPLL GSCGSPICSR SFLLLLLSLG WIPRLQTQTT KTSQEATLLH AVNGAADFAS
LPTGLFLGLT CEEVSDLSME QAKGLAMAVR QKNITLRGHQ LRCLARRLPR HLTDEELNAL
PLDLLLFLNP AMFPGQQACA HFFSLISKAN VDVLPRRSLE RQRLLMEALK CQGVYGFQVS
EADVRALGGL ACDLPGKFVA RSSEVLLPWL AGCQGPLDQS QEKAVREVLR SGRTQYGPPS
KWSVSTLDAL QSLVAVLDES IVQSIPKDVK AEWLQHISRD PSRLGSKLTV IHPRFRRDAE
QKACPPGKEP YKVDEDLIFY QNWELEACVD GTMLARQMDL VNEIPFTYEQ LSIFKHKLDK
TYPQGYPESL IQQLGHFFRY VSPEDIHQWN VTSPDTVKTL LKVSKGQKMN AQAIALVACY
LRGGGQLDED MVKALGDIPL SYLCDFSPQD LHSVPSSVMW LVGPQDLDKC SQRHLGLLYQ
KACSAFQNVS GLEYFEKIKT FLGGASVKDL RALSQHNVSM DIATFKRLQV DSLVGLSVAE
VQKLLGPNIV DLKTEEDKSP VRDWLFRQHQ KDLDRLGLGL QGGIPNGYLV LDFNVREAFS
SRASLLGPGF VLIWIPALLP ALRLS
