PON2_HUMAN
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 03-AUG-2022, entry version 189.
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/";
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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; 239.
DR DIP; DIP-61136N; -.
DR IntAct; Q15165; 88.
DR MINT; Q15165; -.
DR STRING; 9606.ENSP00000222572; -.
DR BindingDB; Q15165; -.
DR ChEMBL; CHEMBL4295823; -.
DR GlyConnect; 1741; 8 N-Linked glycans (2 sites).
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; Q15165; -.
DR PeptideAtlas; Q15165; -.
DR PRIDE; Q15165; -.
DR ProteomicsDB; 60475; -. [Q15165-2]
DR ProteomicsDB; 60476; -. [Q15165-1]
DR ProteomicsDB; 60477; -. [Q15165-3]
DR Antibodypedia; 30147; 424 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 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; WSLTHVK; -.
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; 8 hits in 1079 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 206 other tissues.
DR ExpressionAtlas; Q15165; baseline and differential.
DR Genevisible; Q15165; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
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:0006979; P:response to oxidative stress; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IBA:GO_Central.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR002640; Arylesterase.
DR InterPro; IPR008364; Paraoxonase2.
DR Pfam; PF01731; Arylesterase; 1.
DR PRINTS; PR01785; PARAOXONASE.
DR PRINTS; PR01787; PARAOXONASE2.
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 (associated 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
