CETP_HUMAN
ID CETP_HUMAN Reviewed; 493 AA.
AC P11597; Q13987; Q13988; Q53YZ1;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Cholesteryl ester transfer protein {ECO:0000303|PubMed:3600759};
DE AltName: Full=Lipid transfer protein I {ECO:0000312|MIM:118470};
DE Flags: Precursor;
GN Name=CETP {ECO:0000312|HGNC:HGNC:1869};
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), PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP TISSUE SPECIFICITY, AND VARIANT ILE-422.
RX PubMed=3600759; DOI=10.1038/327632a0;
RA Drayna D., Jarnagin A.S., McLean J., Henzel W., Kohr W., Fielding C.,
RA Lawn R.;
RT "Cloning and sequencing of human cholesteryl ester transfer protein cDNA.";
RL Nature 327:632-634(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2334701; DOI=10.1021/bi00458a004;
RA Agellon L.B., Quinet E.M., Gillette T.G., Drayna D.T., Brown M.L.,
RA Tall A.R.;
RT "Organization of the human cholesteryl ester transfer protein gene.";
RL Biochemistry 29:1372-1376(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-422.
RA Rieder M.J., da Ponte S.H., Kuldanek S.A., Rajkumar N., Smith J.D.,
RA Toth E.J., Nickerson D.A.;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-422.
RC TISSUE=Pancreas, and Spleen;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RX PubMed=8943225; DOI=10.1074/jbc.271.50.31831;
RA Oliveira C.F.O., Chouinard R.A., Agellon L.B., Bruce C., Ma L., Walsh A.,
RA Breslow J.L., Tall A.R.;
RT "Human cholesteryl ester transfer protein gene proximal promoter contains
RT dietary cholesterol positive responsive elements and mediates expression in
RT small intestine and periphery while predominant liver and spleen expression
RT is controlled by 5'-distal sequences. Cis-acting sequences mapped in
RT transgenic mice.";
RL J. Biol. Chem. 271:31831-31838(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX PubMed=9332354; DOI=10.1016/s0378-1119(97)00247-3;
RA Williams S., Hayes L., Elsenboss L., Williams A., Andre C., Abramson R.,
RA Thompson J.F., Milos P.M.;
RT "Sequencing of the cholesteryl ester transfer protein 5' regulatory region
RT using artificial transposons.";
RL Gene 197:101-107(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-493 (ISOFORM 2), AND VARIANT ILE-422.
RC TISSUE=Liver;
RA Dinchuk J.E., Hart J.T., Wirak D.O.;
RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=3281933; DOI=10.1016/s0021-9258(18)60670-2;
RA Hesler C.B., Tall A.R., Swenson T.L., Weech P.K., Marcel Y.L., Milne R.W.;
RT "Monoclonal antibodies to the Mr 74,000 cholesteryl ester transfer protein
RT neutralize all of the cholesteryl ester and triglyceride transfer
RT activities in human plasma.";
RL J. Biol. Chem. 263:5020-5023(1988).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-257 AND ASN-358.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [10]
RP INVOLVEMENT IN HDLCQ10, AND POLYMORPHISM.
RX PubMed=17952847; DOI=10.1086/522497;
RA Spirin V., Schmidt S., Pertsemlidis A., Cooper R.S., Cohen J.C.,
RA Sunyaev S.R.;
RT "Common single-nucleotide polymorphisms act in concert to affect plasma
RT levels of high-density lipoprotein cholesterol.";
RL Am. J. Hum. Genet. 81:1298-1303(2007).
RN [11]
RP GLYCOSYLATION AT ASN-105.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=24293641; DOI=10.1194/jlr.m043646;
RA Morton R.E., Izem L.;
RT "Cholesteryl ester transfer proteins from different species do not have
RT equivalent activities.";
RL J. Lipid Res. 55:258-265(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 19-493 IN COMPLEX WITH LIPID,
RP FUNCTION, DISULFIDE BOND, AND MUTAGENESIS OF THR-155; VAL-215; ARG-218;
RP SER-247; PHE-282; PHE-287; PHE-309; LEU-313; TYR-392; LEU-399 AND VAL-433.
RX PubMed=17237796; DOI=10.1038/nsmb1197;
RA Qiu X., Mistry A., Ammirati M.J., Chrunyk B.A., Clark R.W., Cong Y.,
RA Culp J.S., Danley D.E., Freeman T.B., Geoghegan K.F., Griffor M.C.,
RA Hawrylik S.J., Hayward C.M., Hensley P., Hoth L.R., Karam G.A., Lira M.E.,
RA Lloyd D.B., McGrath K.M., Stutzman-Engwall K.J., Subashi A.K.,
RA Subashi T.A., Thompson J.F., Wang I.-K., Zhao H., Seddon A.P.;
RT "Crystal structure of cholesteryl ester transfer protein reveals a long
RT tunnel and four bound lipid molecules.";
RL Nat. Struct. Mol. Biol. 14:106-113(2007).
RN [14]
RP INVOLVEMENT IN HALP1.
RX PubMed=2215607; DOI=10.1056/nejm199011013231803;
RA Inazu A., Brown M.L., Hesler C.B., Agellon L.B., Koizumi J., Takata K.,
RA Maruhama Y., Mabuchi H., Tall A.R.;
RT "Increased high-density lipoprotein levels caused by a common cholesteryl-
RT ester transfer protein gene mutation.";
RL N. Engl. J. Med. 323:1234-1238(1990).
RN [15]
RP VARIANT HALP1 GLY-459.
RX PubMed=8408659; DOI=10.1172/jci116802;
RA Takahashi K., Jiang X.-C., Sakai N., Yamashita S., Hirano K., Bujo H.,
RA Yamazaki H., Kusunoki J., Miura T., Kussie P., Matsuzawa Y., Saito Y.,
RA Tall A.;
RT "A missense mutation in the cholesteryl ester transfer protein gene with
RT possible dominant effects on plasma high density lipoproteins.";
RL J. Clin. Invest. 92:2060-2064(1993).
RN [16]
RP VARIANTS SER-331; PRO-390; ILE-422 AND MET-486.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [17]
RP ERRATUM OF PUBMED:10391209.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
RN [18]
RP VARIANTS HALP1 PRO-168 AND CYS-299, AND CHARACTERIZATION OF VARIANTS HALP1
RP PRO-168 AND CYS-299.
RX PubMed=12091484; DOI=10.1194/jlr.m200024-jlr200;
RA Nagano M., Yamashita S., Hirano K., Ito M., Maruyama T., Ishihara M.,
RA Sagehashi Y., Oka T., Kujiraoka T., Hattori H., Nakajima N., Egashira T.,
RA Kondo M., Sakai N., Matsuzawa Y.;
RT "Two novel missense mutations in the CETP gene in Japanese
RT hyperalphalipoproteinemic subjects: high-throughput assay by Invader
RT assay.";
RL J. Lipid Res. 43:1011-1018(2002).
RN [19]
RP VARIANTS GLY-15; MET-385; PRO-390; ILE-422 AND GLN-468.
RX PubMed=12966036; DOI=10.1093/hmg/ddg314;
RA Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
RA Alvin G.B., Das K., Gilliam T.C.;
RT "Association of extreme blood lipid profile phenotypic variation with 11
RT reverse cholesterol transport genes and 10 non-genetic cardiovascular
RT disease risk factors.";
RL Hum. Mol. Genet. 12:2733-2743(2003).
CC -!- FUNCTION: Involved in the transfer of neutral lipids, including
CC cholesteryl ester and triglyceride, among lipoprotein particles. Allows
CC the net movement of cholesteryl ester from high density
CC lipoproteins/HDL to triglyceride-rich very low density
CC lipoproteins/VLDL, and the equimolar transport of triglyceride from
CC VLDL to HDL (PubMed:3600759, PubMed:24293641, PubMed:3281933).
CC Regulates the reverse cholesterol transport, by which excess
CC cholesterol is removed from peripheral tissues and returned to the
CC liver for elimination (PubMed:17237796). {ECO:0000269|PubMed:24293641,
CC ECO:0000269|PubMed:3281933, ECO:0000303|PubMed:17237796,
CC ECO:0000305|PubMed:3600759}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesteryl (9Z-octadecenoate)(in) = cholesteryl (9Z-
CC octadecenoate)(out); Xref=Rhea:RHEA:43348, ChEBI:CHEBI:46898;
CC Evidence={ECO:0000269|PubMed:24293641};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol(in) = 1,2,3-tri-(9Z-
CC octadecenoyl)-glycerol(out); Xref=Rhea:RHEA:43352, ChEBI:CHEBI:53753;
CC Evidence={ECO:0000269|PubMed:24293641, ECO:0000269|PubMed:3281933};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesteryl (9Z,12Z)-octadecadienoate(in) = cholesteryl
CC (9Z,12Z)-octadecadienoate(out); Xref=Rhea:RHEA:43356,
CC ChEBI:CHEBI:41509; Evidence={ECO:0000269|PubMed:3281933};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24293641,
CC ECO:0000269|PubMed:3281933}. Note=Secreted in plasma.
CC {ECO:0000269|PubMed:3281933}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P11597-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P11597-2; Sequence=VSP_023645;
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC {ECO:0000269|PubMed:3281933}.
CC -!- POLYMORPHISM: Genetic variations in CETP define the high density
CC lipoprotein cholesterol level quantitative trait locus 10 (HDLCQ10)
CC [MIM:143470]. {ECO:0000269|PubMed:17952847}.
CC -!- DISEASE: Hyperalphalipoproteinemia 1 (HALP1) [MIM:143470]: A condition
CC characterized by high levels of high density lipoprotein (HDL) and
CC increased HDL cholesterol levels. {ECO:0000269|PubMed:12091484,
CC ECO:0000269|PubMed:2215607, ECO:0000269|PubMed:8408659}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Cholesterylester transfer protein
CC entry;
CC URL="https://en.wikipedia.org/wiki/Cholesterylester_transfer_protein";
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DR EMBL; M30185; AAA51977.1; -; mRNA.
DR EMBL; M32998; AAA51978.1; -; Genomic_DNA.
DR EMBL; M32992; AAA51978.1; JOINED; Genomic_DNA.
DR EMBL; M32993; AAA51978.1; JOINED; Genomic_DNA.
DR EMBL; M32994; AAA51978.1; JOINED; Genomic_DNA.
DR EMBL; M32995; AAA51978.1; JOINED; Genomic_DNA.
DR EMBL; M32996; AAA51978.1; JOINED; Genomic_DNA.
DR EMBL; M32997; AAA51978.1; JOINED; Genomic_DNA.
DR EMBL; AY422211; AAR03500.1; -; Genomic_DNA.
DR EMBL; BC025739; AAH25739.1; -; mRNA.
DR EMBL; U71187; AAD14876.1; -; Genomic_DNA.
DR EMBL; AF027656; AAB86604.1; -; Genomic_DNA.
DR EMBL; M83573; AAB59388.1; -; mRNA.
DR CCDS; CCDS10772.1; -. [P11597-1]
DR CCDS; CCDS67032.1; -. [P11597-2]
DR PIR; A26941; A26941.
DR RefSeq; NP_000069.2; NM_000078.2. [P11597-1]
DR PDB; 2OBD; X-ray; 2.10 A; A=18-493.
DR PDB; 4EWS; X-ray; 2.59 A; A=18-493.
DR PDB; 4F2A; X-ray; 3.11 A; A=18-493.
DR PDBsum; 2OBD; -.
DR PDBsum; 4EWS; -.
DR PDBsum; 4F2A; -.
DR AlphaFoldDB; P11597; -.
DR SMR; P11597; -.
DR BioGRID; 107498; 3.
DR IntAct; P11597; 4.
DR STRING; 9606.ENSP00000200676; -.
DR BindingDB; P11597; -.
DR ChEMBL; CHEMBL3572; -.
DR DrugBank; DB06281; Torcetrapib.
DR SwissLipids; SLP:000000472; -.
DR TCDB; 1.C.40.1.8; the bactericidal permeability increasing protein (bpip) family.
DR GlyConnect; 1927; 8 N-Linked glycans (2 sites).
DR GlyGen; P11597; 5 sites, 8 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P11597; -.
DR PhosphoSitePlus; P11597; -.
DR SwissPalm; P11597; -.
DR BioMuta; CETP; -.
DR DMDM; 71153497; -.
DR jPOST; P11597; -.
DR MassIVE; P11597; -.
DR PaxDb; P11597; -.
DR PeptideAtlas; P11597; -.
DR PRIDE; P11597; -.
DR ProteomicsDB; 52795; -. [P11597-1]
DR ProteomicsDB; 52796; -. [P11597-2]
DR Antibodypedia; 28719; 385 antibodies from 35 providers.
DR DNASU; 1071; -.
DR Ensembl; ENST00000200676.8; ENSP00000200676.3; ENSG00000087237.12. [P11597-1]
DR Ensembl; ENST00000379780.6; ENSP00000369106.2; ENSG00000087237.12. [P11597-2]
DR GeneID; 1071; -.
DR KEGG; hsa:1071; -.
DR MANE-Select; ENST00000200676.8; ENSP00000200676.3; NM_000078.3; NP_000069.2.
DR UCSC; uc002eki.3; human. [P11597-1]
DR CTD; 1071; -.
DR DisGeNET; 1071; -.
DR GeneCards; CETP; -.
DR HGNC; HGNC:1869; CETP.
DR HPA; ENSG00000087237; Group enriched (adipose tissue, liver, lymphoid tissue, placenta).
DR MalaCards; CETP; -.
DR MIM; 118470; gene.
DR MIM; 143470; phenotype.
DR neXtProt; NX_P11597; -.
DR OpenTargets; ENSG00000087237; -.
DR Orphanet; 79506; Cholesterol-ester transfer protein deficiency.
DR PharmGKB; PA108; -.
DR VEuPathDB; HostDB:ENSG00000087237; -.
DR eggNOG; KOG4160; Eukaryota.
DR GeneTree; ENSGT01020000230460; -.
DR HOGENOM; CLU_043151_0_0_1; -.
DR InParanoid; P11597; -.
DR OMA; HLTENRM; -.
DR PhylomeDB; P11597; -.
DR TreeFam; TF333484; -.
DR PathwayCommons; P11597; -.
DR Reactome; R-HSA-8964041; LDL remodeling.
DR Reactome; R-HSA-8964058; HDL remodeling.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR SignaLink; P11597; -.
DR SIGNOR; P11597; -.
DR BioGRID-ORCS; 1071; 15 hits in 1070 CRISPR screens.
DR EvolutionaryTrace; P11597; -.
DR GeneWiki; Cholesterylester_transfer_protein; -.
DR GenomeRNAi; 1071; -.
DR Pharos; P11597; Tchem.
DR PRO; PR:P11597; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P11597; protein.
DR Bgee; ENSG00000087237; Expressed in lymph node and 100 other tissues.
DR ExpressionAtlas; P11597; baseline and differential.
DR Genevisible; P11597; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0031982; C:vesicle; IDA:BHF-UCL.
DR GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
DR GO; GO:0120020; F:cholesterol transfer activity; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IDA:BHF-UCL.
DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:BHF-UCL.
DR GO; GO:0005548; F:phospholipid transporter activity; IDA:BHF-UCL.
DR GO; GO:0017129; F:triglyceride binding; IDA:BHF-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
DR GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL.
DR GO; GO:0030301; P:cholesterol transport; IDA:UniProtKB.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IDA:BHF-UCL.
DR GO; GO:0006869; P:lipid transport; IDA:BHF-UCL.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IDA:BHF-UCL.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IC:BHF-UCL.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:BHF-UCL.
DR GO; GO:0055091; P:phospholipid homeostasis; IDA:BHF-UCL.
DR GO; GO:0032376; P:positive regulation of cholesterol transport; IDA:BHF-UCL.
DR GO; GO:2001140; P:positive regulation of phospholipid transport; IDA:BHF-UCL.
DR GO; GO:0010874; P:regulation of cholesterol efflux; IMP:BHF-UCL.
DR GO; GO:0043691; P:reverse cholesterol transport; IC:BHF-UCL.
DR GO; GO:0070328; P:triglyceride homeostasis; IDA:BHF-UCL.
DR GO; GO:0006641; P:triglyceride metabolic process; IDA:BHF-UCL.
DR GO; GO:0034197; P:triglyceride transport; IDA:UniProtKB.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IDA:UniProtKB.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR InterPro; IPR017130; Cholesteryl_ester_transfer.
DR InterPro; IPR001124; Lipid-bd_serum_glycop_C.
DR InterPro; IPR017954; Lipid-bd_serum_glycop_CS.
DR InterPro; IPR017942; Lipid-bd_serum_glycop_N.
DR PANTHER; PTHR47616; PTHR47616; 1.
DR Pfam; PF01273; LBP_BPI_CETP; 1.
DR Pfam; PF02886; LBP_BPI_CETP_C; 1.
DR PIRSF; PIRSF037185; Cholesteryl_ester_transf; 1.
DR SMART; SM00328; BPI1; 1.
DR SMART; SM00329; BPI2; 1.
DR SUPFAM; SSF55394; SSF55394; 2.
DR PROSITE; PS00400; LBP_BPI_CETP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Atherosclerosis;
KW Cholesterol metabolism; Direct protein sequencing; Disease variant;
KW Disulfide bond; Glycoprotein; Lipid metabolism; Lipid transport;
KW Reference proteome; Secreted; Signal; Steroid metabolism;
KW Sterol metabolism; Transport.
FT SIGNAL 1..17
FT CHAIN 18..493
FT /note="Cholesteryl ester transfer protein"
FT /id="PRO_0000017155"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19139490"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 160..201
FT /evidence="ECO:0000269|PubMed:17237796"
FT VAR_SEQ 251..310
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_023645"
FT VARIANT 15
FT /note="A -> G (in dbSNP:rs34065661)"
FT /evidence="ECO:0000269|PubMed:12966036"
FT /id="VAR_017018"
FT VARIANT 154
FT /note="R -> W (in dbSNP:rs34716057)"
FT /id="VAR_033098"
FT VARIANT 168
FT /note="L -> P (in HALP1; reduced secretion into plasma)"
FT /evidence="ECO:0000269|PubMed:12091484"
FT /id="VAR_033099"
FT VARIANT 299
FT /note="R -> C (in HALP1; reduced secretion into plasma;
FT dbSNP:rs142459781)"
FT /evidence="ECO:0000269|PubMed:12091484"
FT /id="VAR_033100"
FT VARIANT 331
FT /note="G -> S (in dbSNP:rs5881)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013919"
FT VARIANT 385
FT /note="V -> M (in dbSNP:rs34855278)"
FT /evidence="ECO:0000269|PubMed:12966036"
FT /id="VAR_017019"
FT VARIANT 390
FT /note="A -> P (in dbSNP:rs5880)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:12966036"
FT /id="VAR_013920"
FT VARIANT 422
FT /note="V -> I (in dbSNP:rs5882)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:12966036, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3600759, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.7"
FT /id="VAR_013921"
FT VARIANT 455
FT /note="V -> M (in dbSNP:rs2228667)"
FT /id="VAR_031127"
FT VARIANT 459
FT /note="D -> G (in HALP1; dbSNP:rs2303790)"
FT /evidence="ECO:0000269|PubMed:8408659"
FT /id="VAR_004172"
FT VARIANT 468
FT /note="R -> Q (in dbSNP:rs1800777)"
FT /evidence="ECO:0000269|PubMed:12966036"
FT /id="VAR_013922"
FT VARIANT 486
FT /note="V -> M (in dbSNP:rs5887)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013923"
FT MUTAGEN 155
FT /note="T->Y: Reduces triglyceride transfer and cholesteryl
FT ester transfer 5-fold."
FT /evidence="ECO:0000269|PubMed:17237796"
FT MUTAGEN 215
FT /note="V->W: Reduces triglyceride transfer 10-fold. No
FT effect on cholesteryl ester transfer."
FT /evidence="ECO:0000269|PubMed:17237796"
FT MUTAGEN 218
FT /note="R->S: Reduces triglyceride transfer 10-fold. Slight
FT reduction of cholesteryl ester transfer."
FT /evidence="ECO:0000269|PubMed:17237796"
FT MUTAGEN 247
FT /note="S->A: Reduces triglyceride transfer 5-fold. Slight
FT reduction of cholesteryl ester transfer."
FT /evidence="ECO:0000269|PubMed:17237796"
FT MUTAGEN 282
FT /note="F->R: Not secreted."
FT /evidence="ECO:0000269|PubMed:17237796"
FT MUTAGEN 287
FT /note="F->R: Not secreted."
FT /evidence="ECO:0000269|PubMed:17237796"
FT MUTAGEN 309
FT /note="F->D: Not secreted."
FT /evidence="ECO:0000269|PubMed:17237796"
FT MUTAGEN 313
FT /note="L->Q: Reduces cholesteryl ester transfer by 60%."
FT /evidence="ECO:0000269|PubMed:17237796"
FT MUTAGEN 392
FT /note="Y->S: Not secreted."
FT /evidence="ECO:0000269|PubMed:17237796"
FT MUTAGEN 399
FT /note="L->W: Not secreted."
FT /evidence="ECO:0000269|PubMed:17237796"
FT MUTAGEN 433
FT /note="V->R: Reduces activity by 60%."
FT /evidence="ECO:0000269|PubMed:17237796"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2OBD"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 70..94
FT /evidence="ECO:0007829|PDB:2OBD"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 98..120
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 128..149
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 152..171
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:4EWS"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 189..222
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 274..283
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 306..315
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 337..344
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 354..367
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 378..393
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 396..416
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 420..432
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 434..451
FT /evidence="ECO:0007829|PDB:2OBD"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 458..468
FT /evidence="ECO:0007829|PDB:2OBD"
FT STRAND 471..479
FT /evidence="ECO:0007829|PDB:2OBD"
FT HELIX 482..490
FT /evidence="ECO:0007829|PDB:2OBD"
SQ SEQUENCE 493 AA; 54756 MW; CD7762766A9B062E CRC64;
MLAATVLTLA LLGNAHACSK GTSHEAGIVC RITKPALLVL NHETAKVIQT AFQRASYPDI
TGEKAMMLLG QVKYGLHNIQ ISHLSIASSQ VELVEAKSID VSIQNVSVVF KGTLKYGYTT
AWWLGIDQSI DFEIDSAIDL QINTQLTCDS GRVRTDAPDC YLSFHKLLLH LQGEREPGWI
KQLFTNFISF TLKLVLKGQI CKEINVISNI MADFVQTRAA SILSDGDIGV DISLTGDPVI
TASYLESHHK GHFIYKNVSE DLPLPTFSPT LLGDSRMLYF WFSERVFHSL AKVAFQDGRL
MLSLMGDEFK AVLETWGFNT NQEIFQEVVG GFPSQAQVTV HCLKMPKISC QNKGVVVNSS
VMVKFLFPRP DQQHSVAYTF EEDIVTTVQA SYSKKKLFLS LLDFQITPKT VSNLTESSSE
SVQSFLQSMI TAVGIPEVMS RLEVVFTALM NSKGVSLFDI INPEIITRDG FLLLQMDFGF
PEHLLVDFLQ SLS
