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 27-MAR-2024, entry version 161. 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}; 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; 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; CCDS33893.2; -. [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; 117. DR IntAct; Q6PIU2; 52. 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 GlyCosmos; Q6PIU2; 3 sites, 3 glycans. DR GlyGen; Q6PIU2; 4 sites, 3 N-linked glycans (2 sites), 1 O-linked glycan (1 site). 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; 9606-ENSP00000442464; -. DR PeptideAtlas; Q6PIU2; -. DR ProteomicsDB; 27511; -. DR ProteomicsDB; 67177; -. [Q6PIU2-1] DR ProteomicsDB; 67178; -. [Q6PIU2-2] DR ProteomicsDB; 67179; -. [Q6PIU2-3] DR Pumba; Q6PIU2; -. DR Antibodypedia; 33731; 138 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 AGR; HGNC:29260; -. 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; DSWKLML; -. DR OrthoDB; 1144477at2759; -. 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; 12 hits in 1162 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 173 other cell types or tissues. DR ExpressionAtlas; Q6PIU2; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. 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:0006805; P:xenobiotic metabolic process; IEA:Ensembl. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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 PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1. DR PANTHER; PTHR48081:SF33; SIMILAR TO HYPOTHETICAL PROTEIN C130079G13; 1. DR Pfam; PF07859; Abhydrolase_3; 2. DR PIRSF; PIRSF037251; Arylacetamide_deacetylase; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR PROSITE; PS01174; LIPASE_GDXG_SER; 1. DR Genevisible; Q6PIU2; HS. 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 //