ID PON2_HUMAN Reviewed; 354 AA. AC Q15165; A4D1H7; B2RCP9; B4DJD5; O15114; O15115; O75856; Q5FBX7; Q86YL0; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 4. DT 27-MAR-2024, entry version 198. DE RecName: Full=Serum paraoxonase/arylesterase 2; DE Short=PON 2; DE EC=3.1.1.2; DE EC=3.1.1.81; DE AltName: Full=Aromatic esterase 2; DE Short=A-esterase 2; DE AltName: Full=Serum aryldialkylphosphatase 2; GN Name=PON2; 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 1), AND VARIANT CYS-311. RC TISSUE=Liver; RX PubMed=8661009; DOI=10.1006/geno.1996.0225; RA Primo-Parmo S.L., Sorenson R.C., Teiber J., La Du B.N.; RT "The human serum paraoxonase/arylesterase gene (PON1) is one member of a RT multigene family."; RL Genomics 33:498-507(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [GENOMIC DNA] RP OF 50-67, ALTERNATIVE SPLICING, AND VARIANT GLY-148. RX PubMed=9714608; DOI=10.1016/s0378-1119(98)00193-0; RA Mochizuki H., Scherer S.W., Xi T., Nickle D.C., Majer M., Huizenga J.J., RA Tsui L.-C., Prochazka M.; RT "Human PON2 gene at 7q21.3: cloning, multiple mRNA forms, and missense RT polymorphisms in the coding sequence."; RL Gene 213:149-157(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Sameshima E., Tabata Y., Hayashi A., Iida K., Mitsuyama M., Kanai S., RA Furuya T., Saito T.; RT "Paraoxonase mRNA,nirs splice variant1."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Subthalamic nucleus, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-148 AND LEU-172. RG SeattleSNPs variation discovery resource; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Skin; 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 FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=11579088; DOI=10.1074/jbc.m105660200; RA Ng C.J., Wadleigh D.J., Gangopadhyay A., Hama S., Grijalva V.R., Navab M., RA Fogelman A.M., Reddy S.T.; RT "Paraoxonase-2 is a ubiquitously expressed protein with antioxidant RT properties and is capable of preventing cell-mediated oxidative RT modification of low density lipoprotein."; RL J. Biol. Chem. 276:44444-44449(2001). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=15772423; DOI=10.1194/jlr.m400511-jlr200; RA Draganov D.I., Teiber J.F., Speelman A., Osawa Y., Sunahara R., La Du B.N.; RT "Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping RT and distinct substrate specificities."; RL J. Lipid Res. 46:1239-1247(2005). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-254. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [15] RP VARIANT GLY-148. RX PubMed=9329371; DOI=10.1210/jcem.82.10.4289; RA Hegele R.A., Connelly P.W., Scherer S.W., Hanley A.J.G., Harris S.B., RA Tsui L.-C., Zinman B.; RT "Paraoxonase-2 gene (PON2) G148 variant associated with elevated fasting RT plasma glucose in noninsulin-dependent diabetes mellitus."; RL J. Clin. Endocrinol. Metab. 82:3373-3377(1997). RN [16] RP POLYMORPHISM. RX PubMed=9443862; DOI=10.1086/301669; RA Sanghera D.K., Aston C.E., Saha N., Kamboh M.I.; RT "DNA polymorphisms in two paraoxonase genes (PON1 and PON2) are associated RT with the risk of coronary heart disease."; RL Am. J. Hum. Genet. 62:36-44(1998). CC -!- FUNCTION: Capable of hydrolyzing lactones and a number of aromatic CC carboxylic acid esters. Has antioxidant activity. Is not associated CC with high density lipoprotein. Prevents LDL lipid peroxidation, CC reverses the oxidation of mildly oxidized LDL, and inhibits the ability CC of MM-LDL to induce monocyte chemotaxis. {ECO:0000269|PubMed:11579088, CC ECO:0000269|PubMed:15772423}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+); CC Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2; CC Evidence={ECO:0000269|PubMed:15772423}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine CC + H(+); Xref=Rhea:RHEA:22576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:55474, ChEBI:CHEBI:58921; EC=3.1.1.81; CC Evidence={ECO:0000269|PubMed:15772423}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC Note=Binds 2 calcium ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:15772423}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11579088}; CC Peripheral membrane protein {ECO:0000269|PubMed:11579088}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=2; CC IsoId=Q15165-2; Sequence=Displayed; CC Name=1; CC IsoId=Q15165-1; Sequence=VSP_004533; CC Name=3; CC IsoId=Q15165-3; Sequence=VSP_040715; CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression in liver, CC lung, placenta, testis and heart. {ECO:0000269|PubMed:11579088}. CC -!- PTM: The signal sequence is not cleaved. {ECO:0000250}. CC -!- POLYMORPHISM: Ser-311 is associated with an increased risk of cornary CC heart disease. {ECO:0000269|PubMed:9443862}. CC -!- SIMILARITY: Belongs to the paraoxonase family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/pon2/"; 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; L48513; AAC41995.1; -; mRNA. DR EMBL; AF001601; AAC27944.1; -; mRNA. DR EMBL; AF001602; AAC27945.1; -; mRNA. DR EMBL; AF001603; AAC27946.1; -; Genomic_DNA. DR EMBL; AB102891; BAD89420.1; -; mRNA. DR EMBL; AK291103; BAF83792.1; -; mRNA. DR EMBL; AK296029; BAG58797.1; -; mRNA. DR EMBL; AK315209; BAG37646.1; -; mRNA. DR EMBL; AY210982; AAO18083.1; -; Genomic_DNA. DR EMBL; AC005021; AAC62431.1; -; Genomic_DNA. DR EMBL; CH236949; EAL24131.1; -; Genomic_DNA. DR EMBL; BC040010; AAH40010.1; -; mRNA. DR CCDS; CCDS47644.1; -. [Q15165-3] DR CCDS; CCDS5640.1; -. [Q15165-2] DR RefSeq; NP_000296.2; NM_000305.2. [Q15165-2] DR RefSeq; NP_001018171.1; NM_001018161.1. [Q15165-3] DR AlphaFoldDB; Q15165; -. DR SMR; Q15165; -. DR BioGRID; 111441; 252. DR DIP; DIP-61136N; -. DR IntAct; Q15165; 89. DR MINT; Q15165; -. DR STRING; 9606.ENSP00000488838; -. DR BindingDB; Q15165; -. DR ChEMBL; CHEMBL4295823; -. DR GlyConnect; 1741; 8 N-Linked glycans (2 sites). DR GlyCosmos; Q15165; 3 sites, 8 glycans. DR GlyGen; Q15165; 5 sites, 9 N-linked glycans (2 sites), 1 O-linked glycan (1 site). DR iPTMnet; Q15165; -. DR PhosphoSitePlus; Q15165; -. DR SwissPalm; Q15165; -. DR BioMuta; PON2; -. DR DMDM; 325511384; -. DR EPD; Q15165; -. DR jPOST; Q15165; -. DR MassIVE; Q15165; -. DR MaxQB; Q15165; -. DR PaxDb; 9606-ENSP00000222572; -. DR PeptideAtlas; Q15165; -. DR ProteomicsDB; 60475; -. [Q15165-2] DR ProteomicsDB; 60476; -. [Q15165-1] DR ProteomicsDB; 60477; -. [Q15165-3] DR Pumba; Q15165; -. DR Antibodypedia; 30147; 458 antibodies from 39 providers. DR DNASU; 5445; -. DR Ensembl; ENST00000222572.8; ENSP00000222572.3; ENSG00000105854.13. [Q15165-2] DR Ensembl; ENST00000433091.6; ENSP00000404622.2; ENSG00000105854.13. [Q15165-3] DR Ensembl; ENST00000633531.1; ENSP00000488838.1; ENSG00000105854.13. [Q15165-2] DR GeneID; 5445; -. DR KEGG; hsa:5445; -. DR MANE-Select; ENST00000222572.8; ENSP00000222572.3; NM_000305.3; NP_000296.2. DR UCSC; uc003unv.4; human. [Q15165-2] DR AGR; HGNC:9205; -. DR CTD; 5445; -. DR DisGeNET; 5445; -. DR GeneCards; PON2; -. DR HGNC; HGNC:9205; PON2. DR HPA; ENSG00000105854; Tissue enhanced (brain). DR MalaCards; PON2; -. DR MIM; 602447; gene. DR neXtProt; NX_Q15165; -. DR OpenTargets; ENSG00000105854; -. DR Orphanet; 803; Amyotrophic lateral sclerosis. DR PharmGKB; PA33530; -. DR VEuPathDB; HostDB:ENSG00000105854; -. DR eggNOG; ENOG502QUCT; Eukaryota. DR GeneTree; ENSGT00390000008932; -. DR HOGENOM; CLU_209318_0_0_1; -. DR InParanoid; Q15165; -. DR OMA; RIQNVHS; -. DR OrthoDB; 2874974at2759; -. DR PhylomeDB; Q15165; -. DR TreeFam; TF322436; -. DR BRENDA; 3.1.1.2; 2681. DR BRENDA; 3.1.1.25; 2681. DR PathwayCommons; Q15165; -. DR Reactome; R-HSA-2142688; Synthesis of 5-eicosatetraenoic acids. DR SignaLink; Q15165; -. DR SIGNOR; Q15165; -. DR BioGRID-ORCS; 5445; 9 hits in 1161 CRISPR screens. DR ChiTaRS; PON2; human. DR GeneWiki; PON2; -. DR GenomeRNAi; 5445; -. DR Pharos; Q15165; Tbio. DR PRO; PR:Q15165; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q15165; Protein. DR Bgee; ENSG00000105854; Expressed in right lung and 208 other cell types or tissues. DR ExpressionAtlas; Q15165; baseline and differential. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0004064; F:arylesterase activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IDA:BHF-UCL. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019439; P:aromatic compound catabolic process; IDA:BHF-UCL. DR GO; GO:0009636; P:response to toxic substance; IBA:GO_Central. DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR002640; Arylesterase. DR InterPro; IPR008364; Paraoxonase2. DR PANTHER; PTHR11799; PARAOXONASE; 1. DR PANTHER; PTHR11799:SF17; SERUM PARAOXONASE_ARYLESTERASE 2; 1. DR Pfam; PF01731; Arylesterase; 1. DR PRINTS; PR01785; PARAOXONASE. DR PRINTS; PR01787; PARAOXONASE2. DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1. DR Genevisible; Q15165; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Disulfide bond; Glycoprotein; Hydrolase; KW Membrane; Metal-binding; Reference proteome; Signal. FT CHAIN 1..354 FT /note="Serum paraoxonase/arylesterase 2" FT /id="PRO_0000223287" FT SIGNAL 1..? FT /note="Not cleaved" FT /evidence="ECO:0000250" FT ACT_SITE 114 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 53 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 54 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 116 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 167 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 168 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 223 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 268 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 269 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT CARBOHYD 254 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 269 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 323 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 42..352 FT /evidence="ECO:0000250" FT VAR_SEQ 1..16 FT /note="MGRLVAVGLLGIALAL -> MGAWVGCGLAGDRAGF (in isoform 1)" FT /evidence="ECO:0000303|PubMed:8661009" FT /id="VSP_004533" FT VAR_SEQ 123..134 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3" FT /id="VSP_040715" FT VARIANT 148 FT /note="A -> G (correlates with elevated mean fasting plasma FT glucose level; dbSNP:rs12026)" FT /evidence="ECO:0000269|PubMed:9329371, FT ECO:0000269|PubMed:9714608, ECO:0000269|Ref.5" FT /id="VAR_006045" FT VARIANT 172 FT /note="V -> L (in dbSNP:rs17876152)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_020786" FT VARIANT 311 FT /note="S -> C (in dbSNP:rs7493)" FT /evidence="ECO:0000269|PubMed:8661009" FT /id="VAR_006046" FT CONFLICT 49..50 FT /note="EA -> VW (in Ref. 2; AAC27945)" FT /evidence="ECO:0000305" FT CONFLICT 53 FT /note="E -> D (in Ref. 4; BAG37646)" FT /evidence="ECO:0000305" FT CONFLICT 63 FT /note="A -> V (in Ref. 4; BAG58797)" FT /evidence="ECO:0000305" FT CONFLICT 194 FT /note="E -> G (in Ref. 1; AAC41995)" FT /evidence="ECO:0000305" FT CONFLICT 282 FT /note="G -> V (in Ref. 2; AAC27944 and 3; BAD89420)" FT /evidence="ECO:0000305" SQ SEQUENCE 354 AA; 39381 MW; 05CEDC91C1B6BC2A CRC64; MGRLVAVGLL GIALALLGER LLALRNRLKA SREVESVDLP HCHLIKGIEA GSEDIDILPN GLAFFSVGLK FPGLHSFAPD KPGGILMMDL KEEKPRAREL RISRGFDLAS FNPHGISTFI DNDDTVYLFV VNHPEFKNTV EIFKFEEAEN SLLHLKTVKH ELLPSVNDIT AVGPAHFYAT NDHYFSDPFL KYLETYLNLH WANVVYYSPN EVKVVAEGFD SANGINISPD DKYIYVADIL AHEIHVLEKH TNMNLTQLKV LELDTLVDNL SIDPSSGDIW VGCHPNGQKL FVYDPNNPPS SEVLRIQNIL SEKPTVTTVY ANNGSVLQGS SVASVYDGKL LIGTLYHRAL YCEL //