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   27-MAR-2024, entry version 185.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   PDB; 7U8C; X-ray; 1.74 A; BA2=590-606.
DR   PDB; 7U9J; X-ray; 2.09 A; A/B=296-509.
DR   PDB; 7UED; X-ray; 3.00 A; M=296-608.
DR   PDB; 8CX3; X-ray; 3.61 A; A/B/C/D/E/F=296-608.
DR   PDB; 8CXC; X-ray; 4.31 A; M=296-605.
DR   PDB; 8CYH; X-ray; 3.38 A; M=296-605.
DR   PDB; 8CZ8; X-ray; 2.60 A; E/M=434-590.
DR   PDBsum; 4F3F; -.
DR   PDBsum; 7U8C; -.
DR   PDBsum; 7U9J; -.
DR   PDBsum; 7UED; -.
DR   PDBsum; 8CX3; -.
DR   PDBsum; 8CXC; -.
DR   PDBsum; 8CYH; -.
DR   PDBsum; 8CZ8; -.
DR   AlphaFoldDB; Q13421; -.
DR   SMR; Q13421; -.
DR   BioGRID; 115526; 80.
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   GlyCosmos; Q13421; 4 sites, 23 glycans.
DR   GlyGen; Q13421; 5 sites, 23 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
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; 9606-ENSP00000372313; -.
DR   PeptideAtlas; Q13421; -.
DR   ProteomicsDB; 59397; -. [Q13421-1]
DR   ProteomicsDB; 59398; -. [Q13421-2]
DR   ProteomicsDB; 59399; -. [Q13421-3]
DR   ProteomicsDB; 59400; -. [Q13421-4]
DR   Pumba; Q13421; -.
DR   ABCD; Q13421; 93 sequenced antibodies.
DR   Antibodypedia; 2310; 1268 antibodies from 46 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   AGR; HGNC:7371; -.
DR   CTD; 10232; -.
DR   DisGeNET; 10232; -.
DR   GeneCards; MSLN; -.
DR   HGNC; HGNC:7371; MSLN.
DR   HPA; ENSG00000102854; Tissue enhanced (adipose tissue, fallopian tube).
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; GIPNGYI; -.
DR   OrthoDB; 4601115at2759; -.
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; 12 hits in 1146 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 cell types or tissues.
DR   ExpressionAtlas; Q13421; baseline and differential.
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: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:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR   GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR   Gene3D; 1.20.970.40; -; 1.
DR   InterPro; IPR010335; Mesothelin.
DR   InterPro; IPR026664; Stereocilin-rel.
DR   PANTHER; PTHR23412:SF6; MESOTHELIN; 1.
DR   PANTHER; PTHR23412; STEREOCILIN RELATED; 1.
DR   Pfam; PF06060; Mesothelin; 1.
DR   Genevisible; Q13421; HS.
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   STRAND          308..310
FT                   /evidence="ECO:0007829|PDB:8CYH"
FT   HELIX           313..317
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           320..326
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           329..334
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           336..338
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   TURN            339..341
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           346..359
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           366..369
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           373..378
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           381..385
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           392..401
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   TURN            402..404
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           419..430
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           435..444
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           449..451
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           454..458
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           462..467
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           470..473
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           478..491
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   TURN            492..494
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           497..504
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           505..507
FT                   /evidence="ECO:0007829|PDB:7U9J"
FT   HELIX           508..510
FT                   /evidence="ECO:0007829|PDB:7UED"
FT   HELIX           513..521
FT                   /evidence="ECO:0007829|PDB:8CZ8"
FT   HELIX           528..531
FT                   /evidence="ECO:0007829|PDB:8CZ8"
FT   HELIX           536..539
FT                   /evidence="ECO:0007829|PDB:8CZ8"
FT   HELIX           544..551
FT                   /evidence="ECO:0007829|PDB:8CZ8"
FT   HELIX           552..561
FT                   /evidence="ECO:0007829|PDB:8CZ8"
FT   STRAND          562..564
FT                   /evidence="ECO:0007829|PDB:7UED"
FT   HELIX           565..571
FT                   /evidence="ECO:0007829|PDB:8CZ8"
FT   HELIX           576..579
FT                   /evidence="ECO:0007829|PDB:8CZ8"
FT   HELIX           580..582
FT                   /evidence="ECO:0007829|PDB:8CZ8"
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
//