CETP_CRIGR
ID CETP_CRIGR Reviewed; 492 AA.
AC G3HIK4;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 2.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Cholesteryl ester transfer protein {ECO:0000303|PubMed:24293641};
DE AltName: Full=Lipid transfer protein I {ECO:0000305};
DE Flags: Precursor;
GN Name=CETP {ECO:0000303|PubMed:24293641};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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).
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:24293641). Regulates the reverse cholesterol
CC transport, by which excess cholesterol is removed from peripheral
CC tissues and returned to the liver for elimination (By similarity).
CC {ECO:0000250|UniProtKB:P11597, ECO:0000269|PubMed:24293641}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesteryl (9Z-octadecenoate)(in) = cholesteryl (9Z-
CC octadecenoate)(out); Xref=Rhea:RHEA:43348, ChEBI:CHEBI:46898;
CC Evidence={ECO:0000250|UniProtKB:P11597};
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:0000250|UniProtKB:P11597};
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:0000250|UniProtKB:P11597};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11597}.
CC Note=Secreted in plasma. {ECO:0000250|UniProtKB:P11597}.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EGW00062.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; JH000405; EGW00062.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003503662.1; XM_003503614.2.
DR RefSeq; XP_007610321.1; XM_007612131.2.
DR AlphaFoldDB; G3HIK4; -.
DR SMR; G3HIK4; -.
DR STRING; 10029.XP_007610321.1; -.
DR SwissLipids; SLP:000000894; -.
DR eggNOG; KOG4160; Eukaryota.
DR InParanoid; G3HIK4; -.
DR OrthoDB; 484128at2759; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:InterPro.
DR GO; GO:0120020; F:cholesterol transfer activity; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030301; P:cholesterol transport; IDA:UniProtKB.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:UniProtKB.
DR GO; GO:0043691; P:reverse cholesterol transport; IEA:InterPro.
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 3: Inferred from homology;
KW Cholesterol metabolism; Disulfide bond; Glycoprotein; Lipid metabolism;
KW Lipid transport; Reference proteome; Secreted; Signal; Steroid metabolism;
KW Sterol metabolism; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..492
FT /note="Cholesteryl ester transfer protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431298"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 160..201
FT /evidence="ECO:0000250|UniProtKB:P11597"
FT CONFLICT 328..333
FT /note="VITGFP -> LFSGLLT (in Ref. 1; EGW00062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 54737 MW; 5CF8DFC79ED4FAEA CRC64;
MLAVTLLSLA LLGSTCACST STSYEAGIVC RITKAALLVL NQETAKVIQT AFQRASYPDI
KGERSMMLLG RVTYGLHNIQ ISHLSIASSQ VELVEAKSVD VSIQNASVIF KGTLNYGYKG
AWGLNIEQSV DFEIESAIDL QINTKLTCDS GHVRTDAPDC SISFHKLLLH LQGEREPGWT
KQLFTNIISF TLKMVLKGQV CKEINVISNI MADFVQTRAA NIISDRDIEV DISLTRSPII
TATYLESHHK GHFIYKNISE VLPLPAFSPT LLGDTRMLYF WFSEQVLDSL AKAAFQDGRL
QLNLAETELK VVLETWHFNP NQEIIPEVIT GFPSPGQVTV HCPRRPTISC QNKGVVVSSP
VVMEFLFPHK DGQDSVTHTF EEDIVATIQA SYSKKKLFLS LVDFQIKPKT TSNMAESSES
IQNFLQLMIT TVGIPEIMSR LEVALTTLMN SKGLDLFDII NPEIITRDGF LLLQMDFGFP
EHLLVDFLQS LN
