ID EST2_HUMAN Reviewed; 559 AA. AC O00748; A0A024R6X1; A8K367; Q16859; Q5MAB8; Q7Z366; Q8IUP4; Q8TCP8; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 13-FEB-2019, entry version 154. DE RecName: Full=Cocaine esterase; DE EC=3.1.1.84; DE AltName: Full=Carboxylesterase 2; DE Short=CE-2; DE Short=hCE-2; DE EC=3.1.1.1; DE AltName: Full=Methylumbelliferyl-acetate deacetylase 2; DE EC=3.1.1.56; DE Flags: Precursor; GN Name=CES2; Synonyms=ICE; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Small intestine; RX PubMed=9144407; DOI=10.1006/bbrc.1997.6413; RA Schwer H., Langmann T., Daig R., Becker A., Aslanidis C., Schmitz G.; RT "Molecular cloning and characterization of a novel putative RT carboxylesterase, present in human intestine and liver."; RL Biochem. Biophys. Res. Commun. 233:117-120(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 27-34; RP 57-70; 227-235; 300-305; 346-351; 447-454; 458-466; 535-540 AND RP 546-551, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, GLYCOSYLATION, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC TISSUE=Liver; RX PubMed=9169443; DOI=10.1074/jbc.272.23.14769; RA Pindel E.V., Kedishvili N.Y., Abraham T.L., Brzezinski M.R., Zhang J., RA Dean R.A., Bosron W.F.; RT "Purification and cloning of a broad substrate specificity human liver RT carboxylesterase that catalyzes the hydrolysis of cocaine and RT heroin."; RL J. Biol. Chem. 272:14769-14775(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RA Sone T., Ishida Y., Takabatake E., Wang C., Pohl L., Isobe M.; RT "Molecular cloning and expression of a human liver cDNA encoding a RT novel carboxylesterase."; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Endometrial adenocarcinoma, and Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA 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., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA 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 GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-111. 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 RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [11] RP SUBCELLULAR LOCATION. RX PubMed=22446793; DOI=10.1007/s00253-012-3994-3; RA Lamego J., Cunha B., Peixoto C., Sousa M.F., Alves P.M., RA Simplicio A.L., Coroadinha A.S.; RT "Carboxylesterase 2 production and characterization in human cells: RT new insights into enzyme oligomerization and activity."; RL Appl. Microbiol. Biotechnol. 97:1161-1173(2013). RN [12] RP REVIEW, AND ALTERNATIVE INITIATION (ISOFORMS 3 AND 4). RX PubMed=28677105; DOI=10.1007/s13238-017-0437-z; RA Lian J., Nelson R., Lehner R.; RT "Carboxylesterases in lipid metabolism: from mouse to human."; RL Protein Cell 9:178-195(2018). RN [13] 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., RA Buerckstuemmer T., 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 [14] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP VARIANT HIS-206. RX PubMed=12721789; DOI=10.1007/s10038-003-0021-7; RA Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C., RA Nakamura Y.; RT "Catalog of 680 variations among eight cytochrome p450 (CYP) genes, RT nine esterase genes, and two other genes in the Japanese population."; RL J. Hum. Genet. 48:249-270(2003). RN [16] RP VARIANT TRP-34. RX PubMed=15618752; DOI=10.2133/dmpk.18.327; RA Kim S.-R., Nakamura T., Saito Y., Sai K., Nakajima T., Saito H., RA Shirao K., Minami H., Ohtsu A., Yoshida T., Saijo N., Ozawa S., RA Sawada J.; RT "Twelve novel single nucleotide polymorphisms in the CES2 gene RT encoding human carboxylesterase 2 (hCE-2)."; RL Drug Metab. Pharmacokinet. 18:327-332(2003). CC -!- FUNCTION: Involved in the detoxification of xenobiotics and in the CC activation of ester and amide prodrugs (PubMed:9169443). Shows CC high catalytic efficiency for hydrolysis of cocaine, 4- CC methylumbelliferyl acetate, heroin and 6-monoacetylmorphine CC (PubMed:9169443). Hydrolyzes aspirin, substrates with large CC alcohol group and small acyl group and endogenous lipids such as CC triacylglycerol (PubMed:28677105). {ECO:0000269|PubMed:9169443, CC ECO:0000303|PubMed:28677105}. CC -!- CATALYTIC ACTIVITY: CC Reaction=cocaine + H2O = benzoate + ecgonine methyl ester + H(+); CC Xref=Rhea:RHEA:27506, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16150, ChEBI:CHEBI:59908, ChEBI:CHEBI:60056; CC EC=3.1.1.84; Evidence={ECO:0000269|PubMed:9169443}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + CC H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, CC ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10039, ECO:0000269|PubMed:9169443}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-methylumbelliferyl acetate + H2O = 4- CC methylumbelliferone + acetate + H(+); Xref=Rhea:RHEA:12208, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17224, CC ChEBI:CHEBI:17763, ChEBI:CHEBI:30089; EC=3.1.1.56; CC Evidence={ECO:0000269|PubMed:9169443}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.39 mM for cocaine {ECO:0000269|PubMed:9169443}; CC KM=0.15 mM for 4-methylumbelliferyl acetate CC {ECO:0000269|PubMed:9169443}; CC KM=6.8 mM for heroin {ECO:0000269|PubMed:9169443}; CC KM=0.13 mM for 6-monoacetylmorphine CC {ECO:0000269|PubMed:9169443}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9169443}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen CC {ECO:0000269|PubMed:22446793}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=4; CC Name=1; CC IsoId=O00748-1; Sequence=Displayed; CC Name=2; CC IsoId=O00748-2; Sequence=VSP_010161; CC Name=3; CC IsoId=O00748-4; Sequence=VSP_059804; CC Note=Probably produced by alternative initiation of isoform 1. CC Does not contain a signal peptide. The biological function of CC the extra amino acids in the N-terminus remains to be CC determined. {ECO:0000303|PubMed:28677105}; CC Name=4; CC IsoId=O00748-5; Sequence=VSP_059804, VSP_010161; CC Note=Probably produced by alternative initiation of isoform 2. CC Does not contain a signal peptide. The biological function of CC the extra amino acids in the N-terminus remains to be CC determined. {ECO:0000303|PubMed:28677105}; CC -!- TISSUE SPECIFICITY: Preferentially expressed in intestine with CC moderate expression in liver. Within the intestine, highest CC expression is found in small intestine with lower expression in CC colon and rectum. {ECO:0000269|PubMed:9144407}. CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:9169443}. CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/ces2/"; 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; Y09616; CAA70831.1; -; mRNA. DR EMBL; D50579; BAA23606.1; -; mRNA. DR EMBL; U60553; AAB03611.1; -; mRNA. DR EMBL; AL713761; CAD28531.1; -; mRNA. DR EMBL; AK290482; BAF83171.1; -; mRNA. DR EMBL; BX538086; CAD98009.1; -; mRNA. DR EMBL; AY851164; AAW29943.1; -; Genomic_DNA. DR EMBL; AC009084; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471092; EAW83058.1; -; Genomic_DNA. DR EMBL; CH471092; EAW83059.1; -; Genomic_DNA. DR EMBL; BC032095; AAH32095.1; -; mRNA. DR CCDS; CCDS10825.1; -. [O00748-1] DR CCDS; CCDS45507.1; -. [O00748-2] DR PIR; JC5408; JC5408. DR RefSeq; NP_003860.2; NM_003869.5. [O00748-1] DR RefSeq; NP_932327.1; NM_198061.2. [O00748-2] DR UniGene; Hs.282975; -. DR ProteinModelPortal; O00748; -. DR SMR; O00748; -. DR BioGrid; 114351; 1. DR IntAct; O00748; 2. DR STRING; 9606.ENSP00000317842; -. DR BindingDB; O00748; -. DR ChEMBL; CHEMBL3180; -. DR DrugBank; DB06695; Dabigatran etexilate. DR DrugBank; DB00762; Irinotecan. DR DrugBank; DB00688; Mycophenolate mofetil. DR DrugBank; DB06209; Prasugrel. DR SwissLipids; SLP:000001424; -. DR ESTHER; human-CES2; Carb_B_Chordata. DR MEROPS; S09.984; -. DR iPTMnet; O00748; -. DR PhosphoSitePlus; O00748; -. DR BioMuta; CES2; -. DR EPD; O00748; -. DR jPOST; O00748; -. DR MaxQB; O00748; -. DR PaxDb; O00748; -. DR PeptideAtlas; O00748; -. DR PRIDE; O00748; -. DR ProteomicsDB; 48014; -. DR ProteomicsDB; 48015; -. [O00748-2] DR DNASU; 8824; -. DR Ensembl; ENST00000317091; ENSP00000317842; ENSG00000172831. [O00748-4] DR Ensembl; ENST00000417689; ENSP00000394452; ENSG00000172831. [O00748-5] DR GeneID; 8824; -. DR KEGG; hsa:8824; -. DR UCSC; uc002eqq.4; human. [O00748-1] DR UCSC; uc002eqr.4; human. DR CTD; 8824; -. DR DisGeNET; 8824; -. DR EuPathDB; HostDB:ENSG00000172831.11; -. DR GeneCards; CES2; -. DR HGNC; HGNC:1864; CES2. DR HPA; HPA018897; -. DR MIM; 605278; gene. DR neXtProt; NX_O00748; -. DR OpenTargets; ENSG00000172831; -. DR PharmGKB; PA377; -. DR eggNOG; KOG1516; Eukaryota. DR eggNOG; COG2272; LUCA. DR GeneTree; ENSGT00940000153793; -. DR HOGENOM; HOG000091866; -. DR HOVERGEN; HBG008839; -. DR InParanoid; O00748; -. DR KO; K03927; -. DR OMA; GASAYWP; -. DR OrthoDB; 754103at2759; -. DR PhylomeDB; O00748; -. DR TreeFam; TF315470; -. DR BRENDA; 3.1.1.1; 2681. DR BRENDA; 3.1.1.84; 2681. DR Reactome; R-HSA-211945; Phase I - Functionalization of compounds. DR SABIO-RK; O00748; -. DR ChiTaRS; CES2; human. DR GeneWiki; Carboxylesterase_2; -. DR GenomeRNAi; 8824; -. DR PRO; PR:O00748; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000172831; Expressed in 236 organ(s), highest expression level in jejunal mucosa. DR ExpressionAtlas; O00748; baseline and differential. DR Genevisible; O00748; HS. DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:BHF-UCL. DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC. DR GO; GO:0047374; F:methylumbelliferyl-acetate deacetylase activity; IEA:UniProtKB-EC. DR GO; GO:0009056; P:catabolic process; TAS:ProtInc. DR GO; GO:0006693; P:prostaglandin metabolic process; IDA:BHF-UCL. DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR002018; CarbesteraseB. DR InterPro; IPR019826; Carboxylesterase_B_AS. DR InterPro; IPR019819; Carboxylesterase_B_CS. DR Pfam; PF00135; COesterase; 1. DR SUPFAM; SSF53474; SSF53474; 1. DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1. DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1. PE 1: Evidence at protein level; KW Alternative initiation; Alternative splicing; Complete proteome; KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; KW Glycoprotein; Hydrolase; Polymorphism; Pyrrolidone carboxylic acid; KW Reference proteome; Serine esterase; Signal. FT SIGNAL 1 26 {ECO:0000269|PubMed:9169443}. FT CHAIN 27 559 Cocaine esterase. FT /FTId=PRO_0000008572. FT MOTIF 556 559 Prevents secretion from ER. FT {ECO:0000255}. FT ACT_SITE 228 228 Acyl-ester intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU10039}. FT ACT_SITE 345 345 Charge relay system. {ECO:0000250}. FT ACT_SITE 457 457 Charge relay system. {ECO:0000250}. FT MOD_RES 27 27 Pyrrolidone carboxylic acid. FT {ECO:0000250|UniProtKB:P14943}. FT CARBOHYD 111 111 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 276 276 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 95 123 {ECO:0000250}. FT DISULFID 280 291 {ECO:0000250}. FT VAR_SEQ 1 1 M -> MTAQSRSPTTPTFPGPSQRTPLTPCPVQTPRLGKAL FT IHCWTDPGQPLGEQQRVRRQRTETSEPTM (in isoform FT 3 and isoform 4). FT {ECO:0000303|PubMed:28677105}. FT /FTId=VSP_059804. FT VAR_SEQ 458 474 GDELPFVFRSFFGGNYI -> V (in isoform 2 and FT isoform 4). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_010161. FT VARIANT 34 34 R -> W. {ECO:0000269|PubMed:15618752}. FT /FTId=VAR_018396. FT VARIANT 206 206 R -> H. {ECO:0000269|PubMed:12721789}. FT /FTId=VAR_018397. FT CONFLICT 2 10 Missing (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 180 180 G -> S (in Ref. 4; BAF83171). FT {ECO:0000305}. FT CONFLICT 239 239 V -> M (in Ref. 4; BAF83171). FT {ECO:0000305}. FT CONFLICT 385 385 F -> S (in Ref. 5; CAD98009). FT {ECO:0000305}. FT CONFLICT 519 519 Q -> R (in Ref. 5; CAD98009). FT {ECO:0000305}. SQ SEQUENCE 559 AA; 61807 MW; E2EBCABA2995339A CRC64; MRLHRLRARL SAVACGLLLL LVRGQGQDSA SPIRTTHTGQ VLGSLVHVKG ANAGVQTFLG IPFAKPPLGP LRFAPPEPPE SWSGVRDGTT HPAMCLQDLT AVESEFLSQF NMTFPSDSMS EDCLYLSIYT PAHSHEGSNL PVMVWIHGGA LVFGMASLYD GSMLAALENV VVVIIQYRLG VLGFFSTGDK HATGNWGYLD QVAALRWVQQ NIAHFGGNPD RVTIFGESAG GTSVSSLVVS PISQGLFHGA IMESGVALLP GLIASSADVI STVVANLSAC DQVDSEALVG CLRGKSKEEI LAINKPFKMI PGVVDGVFLP RHPQELLASA DFQPVPSIVG VNNNEFGWLI PKVMRIYDTQ KEMDREASQA ALQKMLTLLM LPPTFGDLLR EEYIGDNGDP QTLQAQFQEM MADSMFVIPA LQVAHFQCSR APVYFYEFQH QPSWLKNIRP PHMKADHGDE LPFVFRSFFG GNYIKFTEEE EQLSRKMMKY WANFARNGNP NGEGLPHWPL FDQEEQYLQL NLQPAVGRAL KAHRLQFWKK ALPQKIQELE EPEERHTEL //