MSLN_HUMAN
ID MSLN_HUMAN Reviewed; 630 AA.
AC Q13421; D3DU65; Q14859; Q4VQD5; Q96GR6; Q96KJ5; Q9BR17; Q9BTR2; Q9UCB2;
AC Q9UK57;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Mesothelin;
DE AltName: Full=CAK1 antigen;
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=MPF;
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 2), PROTEIN SEQUENCE OF 37-54 AND
RP 90-117, TISSUE SPECIFICITY, AND VARIANT VAL-601.
RC TISSUE=Pancreatic cancer;
RX PubMed=7665620; DOI=10.1074/jbc.270.37.21984;
RA Kojima T., Oh-Eda M., Hattori K., Taniguchi Y., Tamura M., Ochi N.,
RA Yamaguchi N.;
RT "Molecular cloning and expression of megakaryocyte potentiating factor
RT cDNA.";
RL J. Biol. Chem. 270:21984-21990(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, GPI-ANCHOR,
RP GLYCOSYLATION, CLEAVAGE, AND VARIANT VAL-601.
RC TISSUE=Carcinoma;
RX PubMed=8552591; DOI=10.1073/pnas.93.1.136;
RA Chang K., Pastan I.;
RT "Molecular cloning of mesothelin, a differentiation antigen present on
RT mesothelium, mesotheliomas, and ovarian cancers.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:136-140(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING (ISOFORMS
RP 2 AND 3).
RX PubMed=15140265; DOI=10.1186/1471-2407-4-19;
RA Muminova Z.E., Strong T.V., Shaw D.R.;
RT "Characterization of human mesothelin transcripts in ovarian and pancreatic
RT cancer.";
RL BMC Cancer 4:19-19(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), DISEASE, AND VARIANT VAL-601.
RC TISSUE=Lung, and Spleen;
RX PubMed=15897581; DOI=10.1158/1078-0432.ccr-04-2304;
RA Ho M., Hassan R., Zhang J., Wang Q.-C., Onda M., Bera T., Pastan I.;
RT "Humoral immune response to mesothelin in mesothelioma and ovarian cancer
RT patients.";
RL Clin. Cancer Res. 11:3814-3820(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-601.
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND VARIANTS
RP PRO-309 AND VAL-601.
RC TISSUE=Pancreas, and Placenta;
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 [9]
RP PROTEIN SEQUENCE OF 37-54 (ISOFORMS 1/2/3), GLYCOSYLATION, AND FUNCTION.
RC TISSUE=Pancreatic tumor;
RX PubMed=8288629; DOI=10.1016/s0021-9258(17)42180-6;
RA Yamaguchi N., Hattori K., Oh-eda M., Kojima T., Imai N., Ochi N.;
RT "A novel cytokine exhibiting megakaryocyte potentiating activity from a
RT human pancreatic tumor cell line HPC-Y5.";
RL J. Biol. Chem. 269:805-808(1994).
RN [10]
RP PROTEIN SEQUENCE OF 279-293, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Tear;
RX PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179;
RA Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I.,
RA Suarez T., Elortza F.;
RT "Human basal tear peptidome characterization by CID, HCD, and ETD followed
RT by in silico and in vitro analyses for antimicrobial peptide
RT identification.";
RL J. Proteome Res. 14:2649-2658(2015).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 297-630 (ISOFORM 3), PROTEIN SEQUENCE OF
RP 296-314, AND VARIANT VAL-601.
RX PubMed=10500211; DOI=10.1073/pnas.96.20.11531;
RA Scholler N., Fu N., Yang Y., Ye Z., Goodman G.E., Hellstroem K.E.,
RA Hellstroem I.;
RT "Soluble member(s) of the mesothelin/megakaryocyte potentiating factor
RT family are detectable in sera from patients with ovarian carcinoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11531-11536(1999).
RN [12]
RP INTERACTION WITH MUC16, 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).
RN [13]
RP GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=16857795; DOI=10.1158/1078-0432.ccr-06-0472;
RA Onda M., Nagata S., Ho M., Bera T.K., Hassan R., Alexander R.H., Pastan I.;
RT "Megakaryocyte potentiation factor cleaved from mesothelin precursor is a
RT useful tumor marker in the serum of patients with mesothelioma.";
RL Clin. Cancer Res. 12:4225-4231(2006).
RN [14]
RP PHOSPHORYLATION AT SER-200.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 302-359 IN COMPLEX WITH ANTIBODY,
RP SUBCELLULAR LOCATION, AND DISULFIDE BOND.
RX PubMed=22787150; DOI=10.1074/jbc.m112.381756;
RA Ma J., Tang W.K., Esser L., Pastan I., Xia D.;
RT "Recognition of mesothelin by the therapeutic antibody MORAb-009:
RT structural and mechanistic insights.";
RL J. Biol. Chem. 287:33123-33131(2012).
CC -!- FUNCTION: Membrane-anchored forms may play a role in cellular adhesion.
CC -!- FUNCTION: Megakaryocyte-potentiating factor (MPF) potentiates
CC megakaryocyte colony formation in vitro.
CC -!- SUBUNIT: Interacts with MUC16. {ECO:0000269|PubMed:14676194,
CC ECO:0000269|PubMed:22787150}.
CC -!- INTERACTION:
CC Q13421-3; Q92624: APPBP2; NbExp=3; IntAct=EBI-12303989, EBI-743771;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Golgi
CC apparatus.
CC -!- SUBCELLULAR LOCATION: [Megakaryocyte-potentiating factor]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q13421-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13421-3; Sequence=VSP_021059;
CC Name=3; Synonyms=SMRP;
CC IsoId=Q13421-2; Sequence=VSP_021059, VSP_021060;
CC Name=4;
CC IsoId=Q13421-4; Sequence=VSP_021058, VSP_021059;
CC -!- TISSUE SPECIFICITY: Expressed in lung. Expressed at low levels in
CC heart, placenta and kidney. Expressed in mesothelial cells. Highly
CC expressed in mesotheliomas, ovarian cancers, and some squamous cell
CC carcinomas (at protein level). {ECO:0000269|PubMed:16857795,
CC ECO:0000269|PubMed:7665620}.
CC -!- PTM: Both MPF and the cleaved form of mesothelin are N-glycosylated.
CC {ECO:0000269|PubMed:16857795, ECO:0000269|PubMed:8288629,
CC ECO:0000269|PubMed:8552591}.
CC -!- PTM: Proteolytically cleaved by a furin-like convertase to generate
CC megakaryocyte-potentiating factor (MPF), and the cleaved form of
CC mesothelin. {ECO:0000269|PubMed:8552591}.
CC -!- DISEASE: Note=Antibodies against MSLN are detected in patients with
CC mesothelioma and ovarian cancer. {ECO:0000269|PubMed:15897581}.
CC -!- MISCELLANEOUS: [Isoform 1]: Minor form.
CC -!- MISCELLANEOUS: [Isoform 2]: Major form. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Soluble form found in the sera from
CC patients with ovarian carcinoma. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the mesothelin family. {ECO:0000305}.
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DR EMBL; D49441; BAA08419.1; -; mRNA.
DR EMBL; U40434; AAC50348.1; -; mRNA.
DR EMBL; AY743922; AAV87530.1; -; mRNA.
DR EMBL; AE006464; AAK61253.1; -; Genomic_DNA.
DR EMBL; AL031258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85719.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85720.1; -; Genomic_DNA.
DR EMBL; BC003512; AAH03512.1; -; mRNA.
DR EMBL; BC009272; AAH09272.1; -; mRNA.
DR EMBL; AF180951; AAF01409.1; -; mRNA.
DR CCDS; CCDS32356.1; -. [Q13421-1]
DR CCDS; CCDS45370.1; -. [Q13421-3]
DR RefSeq; NP_001170826.1; NM_001177355.2. [Q13421-3]
DR RefSeq; NP_005814.2; NM_005823.5. [Q13421-3]
DR RefSeq; NP_037536.2; NM_013404.4. [Q13421-1]
DR RefSeq; XP_005255091.1; XM_005255034.4.
DR RefSeq; XP_011520650.1; XM_011522348.2.
DR RefSeq; XP_016878346.1; XM_017022857.1.
DR PDB; 4F3F; X-ray; 2.65 A; C=302-359.
DR PDBsum; 4F3F; -.
DR AlphaFoldDB; Q13421; -.
DR SMR; Q13421; -.
DR BioGRID; 115526; 78.
DR IntAct; Q13421; 4.
DR STRING; 9606.ENSP00000372313; -.
DR ChEMBL; CHEMBL3712878; -.
DR DrugBank; DB12845; Amatuximab.
DR GlyConnect; 1503; 22 N-Linked glycans (3 sites).
DR GlyGen; Q13421; 4 sites, 23 N-linked glycans (3 sites).
DR iPTMnet; Q13421; -.
DR PhosphoSitePlus; Q13421; -.
DR SwissPalm; Q13421; -.
DR BioMuta; MSLN; -.
DR DMDM; 116242654; -.
DR EPD; Q13421; -.
DR jPOST; Q13421; -.
DR MassIVE; Q13421; -.
DR MaxQB; Q13421; -.
DR PaxDb; Q13421; -.
DR PeptideAtlas; Q13421; -.
DR PRIDE; Q13421; -.
DR ProteomicsDB; 59397; -. [Q13421-1]
DR ProteomicsDB; 59398; -. [Q13421-2]
DR ProteomicsDB; 59399; -. [Q13421-3]
DR ProteomicsDB; 59400; -. [Q13421-4]
DR ABCD; Q13421; 93 sequenced antibodies.
DR Antibodypedia; 2310; 860 antibodies from 45 providers.
DR CPTC; Q13421; 2 antibodies.
DR DNASU; 10232; -.
DR Ensembl; ENST00000382862.7; ENSP00000372313.3; ENSG00000102854.16. [Q13421-1]
DR Ensembl; ENST00000545450.7; ENSP00000442965.2; ENSG00000102854.16. [Q13421-3]
DR Ensembl; ENST00000563941.5; ENSP00000456008.1; ENSG00000102854.16. [Q13421-3]
DR Ensembl; ENST00000566549.5; ENSP00000456702.1; ENSG00000102854.16. [Q13421-3]
DR GeneID; 10232; -.
DR KEGG; hsa:10232; -.
DR MANE-Select; ENST00000545450.7; ENSP00000442965.2; NM_005823.6; NP_005814.2. [Q13421-3]
DR UCSC; uc002cjt.2; human. [Q13421-1]
DR CTD; 10232; -.
DR DisGeNET; 10232; -.
DR GeneCards; MSLN; -.
DR HGNC; HGNC:7371; MSLN.
DR HPA; ENSG00000102854; Group enriched (fallopian tube, lung).
DR MIM; 601051; gene.
DR neXtProt; NX_Q13421; -.
DR OpenTargets; ENSG00000102854; -.
DR PharmGKB; PA31176; -.
DR VEuPathDB; HostDB:ENSG00000102854; -.
DR eggNOG; ENOG502QRX1; Eukaryota.
DR GeneTree; ENSGT00950000182957; -.
DR HOGENOM; CLU_014552_3_0_1; -.
DR InParanoid; Q13421; -.
DR OMA; DFTCTEV; -.
DR OrthoDB; 459771at2759; -.
DR PhylomeDB; Q13421; -.
DR TreeFam; TF331713; -.
DR PathwayCommons; Q13421; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; Q13421; -.
DR SIGNOR; Q13421; -.
DR BioGRID-ORCS; 10232; 11 hits in 1066 CRISPR screens.
DR ChiTaRS; MSLN; human.
DR GeneWiki; Mesothelin; -.
DR GenomeRNAi; 10232; -.
DR Pharos; Q13421; Tbio.
DR PRO; PR:Q13421; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q13421; protein.
DR Bgee; ENSG00000102854; Expressed in right uterine tube and 132 other tissues.
DR ExpressionAtlas; Q13421; baseline and differential.
DR Genevisible; Q13421; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0031016; P:pancreas development; IEA:Ensembl.
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 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Golgi apparatus; GPI-anchor; Lipoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000269|PubMed:7665620"
FT CHAIN 37..606
FT /note="Mesothelin"
FT /id="PRO_0000253559"
FT CHAIN 37..286
FT /note="Megakaryocyte-potentiating factor"
FT /id="PRO_0000253560"
FT CHAIN 296..606
FT /note="Mesothelin, cleaved form"
FT /id="PRO_0000253561"
FT PROPEP 607..630
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000021769"
FT REGION 262..286
FT /note="Required for megakaryocyte-potentiating factor
FT activity"
FT MOD_RES 200
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT LIPID 606
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 302..326
FT /evidence="ECO:0000269|PubMed:22787150"
FT VAR_SEQ 44
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021058"
FT VAR_SEQ 409..416
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10500211,
FT ECO:0000303|PubMed:15140265, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15897581, ECO:0000303|PubMed:7665620"
FT /id="VSP_021059"
FT VAR_SEQ 601..630
FT /note="MQEALSGTPCLLGPGPVLTVLALLLASTLA -> VQGGRGGQARAGGRAGGV
FT EVGALSHPSLCRGPLGDALPPRTWTCSHRPGTAPSLHPGLRAPLPC (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:10500211"
FT /id="VSP_021060"
FT VARIANT 72
FT /note="A -> V (in dbSNP:rs9927389)"
FT /id="VAR_028381"
FT VARIANT 309
FT /note="R -> P (in dbSNP:rs17850474)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028382"
FT VARIANT 497
FT /note="G -> E (in dbSNP:rs35935235)"
FT /id="VAR_054012"
FT VARIANT 601
FT /note="M -> V (in dbSNP:rs1135210)"
FT /evidence="ECO:0000269|PubMed:10500211,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15616553,
FT ECO:0000269|PubMed:15897581, ECO:0000269|PubMed:7665620,
FT ECO:0000269|PubMed:8552591"
FT /id="VAR_028383"
FT CONFLICT 4..11
FT /note="PTARPLLG -> QRLDPCW (in Ref. 2; AAC50348)"
FT /evidence="ECO:0000305"
FT CONFLICT 15..18
FT /note="TPAL -> DRP (in Ref. 2; AAC50348)"
FT /evidence="ECO:0000305"
FT CONFLICT 32..34
FT /note="QPS -> HPA (in Ref. 2; AAC50348)"
FT /evidence="ECO:0000305"
FT CONFLICT 43..45
FT /note="QEA -> TES (in Ref. 2; AAC50348)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="D -> G (in Ref. 2; AAC50348)"
FT /evidence="ECO:0000305"
FT CONFLICT 53..56
FT /note="ANPP -> TTPH (in Ref. 2; AAC50348)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="R -> H (in Ref. 4; AAV87530)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="N -> D (in Ref. 2; AAC50348)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="A -> T (in Ref. 2; AAC50348)"
FT /evidence="ECO:0000305"
FT HELIX 313..317
FT /evidence="ECO:0007829|PDB:4F3F"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:4F3F"
FT HELIX 329..334
FT /evidence="ECO:0007829|PDB:4F3F"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:4F3F"
FT HELIX 346..358
FT /evidence="ECO:0007829|PDB:4F3F"
SQ SEQUENCE 630 AA; 68986 MW; FA17E3609B6CC9CA CRC64;
MALPTARPLL GSCGTPALGS LLFLLFSLGW VQPSRTLAGE TGQEAAPLDG VLANPPNISS
LSPRQLLGFP CAEVSGLSTE RVRELAVALA QKNVKLSTEQ LRCLAHRLSE PPEDLDALPL
DLLLFLNPDA FSGPQACTRF FSRITKANVD LLPRGAPERQ RLLPAALACW GVRGSLLSEA
DVRALGGLAC DLPGRFVAES AEVLLPRLVS CPGPLDQDQQ EAARAALQGG GPPYGPPSTW
SVSTMDALRG LLPVLGQPII RSIPQGIVAA WRQRSSRDPS WRQPERTILR PRFRREVEKT
ACPSGKKARE IDESLIFYKK WELEACVDAA LLATQMDRVN AIPFTYEQLD VLKHKLDELY
PQGYPESVIQ HLGYLFLKMS PEDIRKWNVT SLETLKALLE VNKGHEMSPQ APRRPLPQVA
TLIDRFVKGR GQLDKDTLDT LTAFYPGYLC SLSPEELSSV PPSSIWAVRP QDLDTCDPRQ
LDVLYPKARL AFQNMNGSEY FVKIQSFLGG APTEDLKALS QQNVSMDLAT FMKLRTDAVL
PLTVAEVQKL LGPHVEGLKA EERHRPVRDW ILRQRQDDLD TLGLGLQGGI PNGYLVLDLS
MQEALSGTPC LLGPGPVLTV LALLLASTLA
