NCEH1_HUMAN
ID NCEH1_HUMAN Reviewed; 408 AA.
AC Q6PIU2; B7Z2K4; B7Z3A1; B7Z5U2; B7Z906; B7ZAW6; F5H7K4; Q86WZ1; Q9P2I4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Neutral cholesterol ester hydrolase 1;
DE Short=NCEH;
DE EC=3.1.1.- {ECO:0000250|UniProtKB:Q8BLF1};
DE AltName: Full=Acetylalkylglycerol acetylhydrolase {ECO:0000305};
DE Short=2-acetyl MAGE hydrolase {ECO:0000303|PubMed:17052608};
DE EC=3.1.1.71 {ECO:0000269|PubMed:17052608};
DE AltName: Full=Arylacetamide deacetylase-like 1;
GN Name=NCEH1; Synonyms=AADACL1, KIAA1363;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, Hippocampus, Testis, Tongue, and Trachea;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-343.
RC TISSUE=Brain;
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 [5]
RP TISSUE SPECIFICITY, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=12149457; DOI=10.1073/pnas.162187599;
RA Jessani N., Liu Y., Humphrey M., Cravatt B.F.;
RT "Enzyme activity profiles of the secreted and membrane proteome that depict
RT cancer cell invasiveness.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10335-10340(2002).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=17052608; DOI=10.1016/j.chembiol.2006.08.008;
RA Chiang K.P., Niessen S., Saghatelian A., Cravatt B.F.;
RT "An enzyme that regulates ether lipid signaling pathways in cancer
RT annotated by multidimensional profiling.";
RL Chem. Biol. 13:1041-1050(2006).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=18782767; DOI=10.1074/jbc.m802686200;
RA Okazaki H., Igarashi M., Nishi M., Sekiya M., Tajima M., Takase S.,
RA Takanashi M., Ohta K., Tamura Y., Okazaki S., Yahagi N., Ohashi K.,
RA Amemiya-Kudo M., Nakagawa Y., Nagai R., Kadowaki T., Osuga J.,
RA Ishibashi S.;
RT "Identification of neutral cholesterol ester hydrolase, a key enzyme
RT removing cholesterol from macrophages.";
RL J. Biol. Chem. 283:33357-33364(2008).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-287.
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 [9]
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 [10]
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).
CC -!- FUNCTION: Hydrolyzes 2-acetyl monoalkylglycerol ether (1-O-alkyl-2-
CC acetyl-sn-glycerol), the penultimate precursor of the pathway for de
CC novo synthesis of platelet-activating factor (PubMed:17052608). May be
CC responsible for the hydrolysis of cholesterol esters (such as
CC cholesteryl (9Z-octadecenoate)) in macrophages (By similarity). Also
CC involved in organ detoxification by hydrolyzing exogenous
CC organophosphorus compounds (By similarity). May contribute to cancer
CC pathogenesis by promoting tumor cell migration (PubMed:17052608).
CC {ECO:0000250|UniProtKB:Q8BLF1, ECO:0000269|PubMed:17052608}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-O-alkyl-2-acetyl-sn-glycerol + H2O = 1-O-alkyl-sn-glycerol
CC + acetate + H(+); Xref=Rhea:RHEA:11552, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15850, ChEBI:CHEBI:16291,
CC ChEBI:CHEBI:30089; EC=3.1.1.71;
CC Evidence={ECO:0000269|PubMed:17052608};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11553;
CC Evidence={ECO:0000305|PubMed:17052608};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + H2O = 1-O-hexadecyl-sn-
CC glycerol + acetate + H(+); Xref=Rhea:RHEA:38563, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:34115,
CC ChEBI:CHEBI:75936; Evidence={ECO:0000269|PubMed:17052608};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38564;
CC Evidence={ECO:0000305|PubMed:17052608};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cholesterol ester + H2O = a fatty acid + cholesterol + H(+);
CC Xref=Rhea:RHEA:36403, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:17002, ChEBI:CHEBI:28868;
CC Evidence={ECO:0000250|UniProtKB:Q8BLF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36404;
CC Evidence={ECO:0000250|UniProtKB:Q8BLF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesteryl (9Z-octadecenoate) + H2O = (9Z)-octadecenoate +
CC cholesterol + H(+); Xref=Rhea:RHEA:33875, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:46898; Evidence={ECO:0000250|UniProtKB:Q8BLF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876;
CC Evidence={ECO:0000250|UniProtKB:Q8BLF1};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17052608,
CC ECO:0000305|PubMed:12149457}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:12149457}. Microsome
CC {ECO:0000250|UniProtKB:Q8BLF1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6PIU2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PIU2-2; Sequence=VSP_037519;
CC Name=3;
CC IsoId=Q6PIU2-3; Sequence=VSP_037518;
CC -!- TISSUE SPECIFICITY: Expressed in monocyte-derived macrophages. Up-
CC regulated in invasive melanoma and breast carcinoma cell lines.
CC {ECO:0000269|PubMed:12149457, ECO:0000269|PubMed:18782767}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12149457,
CC ECO:0000269|PubMed:19159218}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH28734.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH47588.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AC007919; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AC069237; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA92601.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAH13028.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAH14142.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAH14802.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB037784; BAA92601.1; ALT_INIT; mRNA.
DR EMBL; AK294811; BAH11890.1; -; mRNA.
DR EMBL; AK295641; BAH12137.1; -; mRNA.
DR EMBL; AK299422; BAH13028.1; ALT_INIT; mRNA.
DR EMBL; AK304253; BAH14142.1; ALT_INIT; mRNA.
DR EMBL; AK316431; BAH14802.1; ALT_INIT; mRNA.
DR EMBL; AC007919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028734; AAH28734.2; ALT_INIT; mRNA.
DR EMBL; BC047588; AAH47588.2; ALT_INIT; mRNA.
DR CCDS; CCDS33893.1; -. [Q6PIU2-1]
DR CCDS; CCDS54681.1; -. [Q6PIU2-3]
DR CCDS; CCDS54682.1; -. [Q6PIU2-2]
DR RefSeq; NP_001139748.1; NM_001146276.1. [Q6PIU2-2]
DR RefSeq; NP_001139749.1; NM_001146277.1. [Q6PIU2-3]
DR RefSeq; NP_001139750.1; NM_001146278.1. [Q6PIU2-3]
DR RefSeq; NP_065843.3; NM_020792.4. [Q6PIU2-1]
DR AlphaFoldDB; Q6PIU2; -.
DR SMR; Q6PIU2; -.
DR BioGRID; 121608; 111.
DR IntAct; Q6PIU2; 51.
DR MINT; Q6PIU2; -.
DR STRING; 9606.ENSP00000442464; -.
DR BindingDB; Q6PIU2; -.
DR ChEMBL; CHEMBL5048; -.
DR SwissLipids; SLP:000000634; -.
DR ESTHER; human-NCEH1; Arylacetamide_deacetylase.
DR MEROPS; S09.992; -.
DR GlyConnect; 1563; 3 N-Linked glycans (2 sites).
DR GlyGen; Q6PIU2; 3 sites, 3 N-linked glycans (2 sites).
DR iPTMnet; Q6PIU2; -.
DR PhosphoSitePlus; Q6PIU2; -.
DR SwissPalm; Q6PIU2; -.
DR BioMuta; NCEH1; -.
DR DMDM; 74737782; -.
DR EPD; Q6PIU2; -.
DR jPOST; Q6PIU2; -.
DR MassIVE; Q6PIU2; -.
DR MaxQB; Q6PIU2; -.
DR PaxDb; Q6PIU2; -.
DR PeptideAtlas; Q6PIU2; -.
DR PRIDE; Q6PIU2; -.
DR ProteomicsDB; 27511; -.
DR ProteomicsDB; 67177; -. [Q6PIU2-1]
DR ProteomicsDB; 67178; -. [Q6PIU2-2]
DR ProteomicsDB; 67179; -. [Q6PIU2-3]
DR Antibodypedia; 33731; 114 antibodies from 23 providers.
DR DNASU; 57552; -.
DR Ensembl; ENST00000475381.7; ENSP00000418571.4; ENSG00000144959.11. [Q6PIU2-1]
DR Ensembl; ENST00000543711.5; ENSP00000443227.1; ENSG00000144959.11. [Q6PIU2-3]
DR GeneID; 57552; -.
DR KEGG; hsa:57552; -.
DR MANE-Select; ENST00000475381.7; ENSP00000418571.4; NM_020792.6; NP_065843.4.
DR UCSC; uc003fig.4; human. [Q6PIU2-1]
DR CTD; 57552; -.
DR DisGeNET; 57552; -.
DR GeneCards; NCEH1; -.
DR HGNC; HGNC:29260; NCEH1.
DR HPA; ENSG00000144959; Low tissue specificity.
DR MIM; 613234; gene.
DR neXtProt; NX_Q6PIU2; -.
DR OpenTargets; ENSG00000144959; -.
DR PharmGKB; PA165697847; -.
DR VEuPathDB; HostDB:ENSG00000144959; -.
DR eggNOG; KOG1515; Eukaryota.
DR GeneTree; ENSGT00940000156699; -.
DR HOGENOM; CLU_012494_12_0_1; -.
DR InParanoid; Q6PIU2; -.
DR OMA; ISDPWKL; -.
DR OrthoDB; 1263520at2759; -.
DR PhylomeDB; Q6PIU2; -.
DR TreeFam; TF314978; -.
DR BRENDA; 3.1.1.13; 2681.
DR PathwayCommons; Q6PIU2; -.
DR Reactome; R-HSA-8964038; LDL clearance.
DR SignaLink; Q6PIU2; -.
DR BioGRID-ORCS; 57552; 11 hits in 1080 CRISPR screens.
DR ChiTaRS; NCEH1; human.
DR GeneWiki; NCEH1; -.
DR GenomeRNAi; 57552; -.
DR Pharos; Q6PIU2; Tchem.
DR PRO; PR:Q6PIU2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q6PIU2; protein.
DR Bgee; ENSG00000144959; Expressed in lateral nuclear group of thalamus and 171 other tissues.
DR ExpressionAtlas; Q6PIU2; baseline and differential.
DR Genevisible; Q6PIU2; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047378; F:acetylalkylglycerol acetylhydrolase activity; IEA:RHEA.
DR GO; GO:0042301; F:phosphate ion binding; IEA:Ensembl.
DR GO; GO:0017171; F:serine hydrolase activity; IBA:GO_Central.
DR GO; GO:0004771; F:sterol esterase activity; TAS:Reactome.
DR GO; GO:0046485; P:ether lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; TAS:Reactome.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:Ensembl.
DR GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR017157; Arylacetamide_deacetylase.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR Pfam; PF07859; Abhydrolase_3; 2.
DR PIRSF; PIRSF037251; Arylacetamide_deacetylase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Endoplasmic reticulum; Glycoprotein;
KW Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Microsome;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..408
FT /note="Neutral cholesterol ester hydrolase 1"
FT /id="PRO_0000265939"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..408
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOTIF 113..115
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 348
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..133
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037518"
FT VAR_SEQ 123
FT /note="K -> SASWSPSDE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037519"
FT VARIANT 19
FT /note="V -> F (in dbSNP:rs35316420)"
FT /id="VAR_047099"
FT VARIANT 71
FT /note="K -> Q (in dbSNP:rs2302815)"
FT /id="VAR_047100"
FT VARIANT 343
FT /note="L -> M (in dbSNP:rs17857335)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047101"
FT CONFLICT 16
FT /note="A -> T (in Ref. 1; BAA92601)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="H -> R (in Ref. 2; BAH13028)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="K -> R (in Ref. 2; BAH14802)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="Q -> K (in Ref. 4; AAH47588)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="D -> G (in Ref. 2; BAH14142)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="A -> S (in Ref. 2; BAH14142)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 45808 MW; E5754850BE9805B5 CRC64;
MRSSCVLLTA LVALAAYYVY IPLPGSVSDP WKLMLLDATF RGAQQVSNLI HYLGLSHHLL
ALNFIIVSFG KKSAWSSAQV KVTDTDFDGV EVRVFEGPPK PEEPLKRSVV YIHGGGWALA
SAKIRYYDEL CTAMAEELNA VIVSIEYRLV PKVYFPEQIH DVVRATKYFL KPEVLQKYMV
DPGRICISGD SAGGNLAAAL GQQFTQDASL KNKLKLQALI YPVLQALDFN TPSYQQNVNT
PILPRYVMVK YWVDYFKGNY DFVQAMIVNN HTSLDVEEAA AVRARLNWTS LLPASFTKNY
KPVVQTTGNA RIVQELPQLL DARSAPLIAD QAVLQLLPKT YILTCEHDVL RDDGIMYAKR
LESAGVEVTL DHFEDGFHGC MIFTSWPTNF SVGIRTRNSY IKWLDQNL
