CETP_RABIT
ID CETP_RABIT Reviewed; 497 AA.
AC P22687;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Cholesteryl ester transfer protein {ECO:0000303|PubMed:24293641};
DE AltName: Full=Lipid transfer protein I {ECO:0000305};
DE Flags: Precursor; Fragment;
GN Name=CETP {ECO:0000303|PubMed:24293641};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=3244015;
RA Nagashima M., McLean J.W., Lawn R.M.;
RT "Cloning and mRNA tissue distribution of rabbit cholesteryl ester transfer
RT protein.";
RL J. Lipid Res. 29:1643-1649(1988).
RN [2]
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).
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: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};
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:0000269|PubMed:24293641}.
CC Note=Secreted in plasma. {ECO:0000250|UniProtKB:P47896}.
CC -!- TISSUE SPECIFICITY: Expressed by the liver.
CC {ECO:0000269|PubMed:3244015}.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000305}.
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DR EMBL; M27486; AAA31199.1; -; mRNA.
DR PIR; I46692; I46692.
DR AlphaFoldDB; P22687; -.
DR SMR; P22687; -.
DR STRING; 9986.ENSOCUP00000011306; -.
DR BindingDB; P22687; -.
DR ChEMBL; CHEMBL1163116; -.
DR SwissLipids; SLP:000000485; -.
DR TCDB; 1.C.40.1.3; the bactericidal permeability increasing protein (bpip) family.
DR PRIDE; P22687; -.
DR eggNOG; KOG4160; Eukaryota.
DR InParanoid; P22687; -.
DR Proteomes; UP000001811; Unplaced.
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 1: Evidence at protein level;
KW Cholesterol metabolism; Disulfide bond; Glycoprotein; Lipid metabolism;
KW Lipid transport; Reference proteome; Secreted; Signal; Steroid metabolism;
KW Sterol metabolism; Transport.
FT SIGNAL <1..1
FT CHAIN 2..497
FT /note="Cholesteryl ester transfer protein"
FT /id="PRO_0000017157"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 144..185
FT /evidence="ECO:0000250|UniProtKB:P11597"
FT NON_TER 1
SQ SEQUENCE 497 AA; 54514 MW; E82944E1821D0332 CRC64;
ACPKGASYEA GIVCRITKPA LLVLNQETAK VVQTAFQRAG YPDVSGERAV MLLGRVKYGL
HNLQISHLSI ASSQVELVDA KTIDVAIQNV SVVFKGTLNY SYTSAWGLGI NQSVDFEIDS
AIDLQINTEL TCDAGSVRTN APDCYLAFHK LLLHLQGERE PGWLKQLFTN FISFTLKLIL
KRQVCNEINT ISNIMADFVQ TRAASILSDG DIGVDISVTG APVITATYLE SHHKGHFTHK
NVSEAFPLRA FPPGLLGDSR MLYFWFSDQV LNSLARAAFQ EGRLVLSLTG DEFKKVLETQ
GFDTNQEIFQ ELSRGLPTGQ AQVAVHCLKV PKISCQNRGV VVSSSVAVTF RFPRPDGREA
VAYRFEEDII TTVQASYSQK KLFLHLLDFQ CVPASGRAGS SANLSVALRT EAKAVSNLTE
SRSESLQSSL RSLIATVGIP EVMSRLEVAF TALMNSKGLD LFEIINPEII TLDGCLLLQM
DFGFPKHLLV DFLQSLS
