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CETP_CHICK
ID   CETP_CHICK              Reviewed;         505 AA.
AC   Q3V6R6;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Cholesteryl ester transfer protein {ECO:0000303|PubMed:17574888};
DE   Flags: Precursor;
GN   Name=CETP {ECO:0000305};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND INDUCTION.
RX   PubMed=17574888; DOI=10.1016/j.cbpb.2007.05.003;
RA   Sato K., Ohuchi A., Sato T., Schneider W.J., Akiba Y.;
RT   "Molecular characterization and expression of the cholesteryl ester
RT   transfer protein gene in chickens.";
RL   Comp. Biochem. Physiol. 148B:117-123(2007).
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:17574888). 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:17574888}.
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   -!- TISSUE SPECIFICITY: Highly expressed in liver brain, heart, and spleen.
CC       Secreted in plasma. {ECO:0000269|PubMed:17574888}.
CC   -!- DEVELOPMENTAL STAGE: Expression is significantly lower in mature (egg-
CC       laying) females than in immature female, but unaffected by age in
CC       males. {ECO:0000269|PubMed:17574888}.
CC   -!- INDUCTION: Expression increases following dietary supplementation with
CC       cholesterol. Expression decreases following dietary supplementation
CC       with estradiol. {ECO:0000269|PubMed:17574888}.
CC   -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC       {ECO:0000305}.
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DR   EMBL; AB205527; BAE43960.1; -; mRNA.
DR   AlphaFoldDB; Q3V6R6; -.
DR   SMR; Q3V6R6; -.
DR   STRING; 9031.ENSGALP00000001869; -.
DR   PaxDb; Q3V6R6; -.
DR   VEuPathDB; HostDB:geneid_415645; -.
DR   eggNOG; KOG4160; Eukaryota.
DR   InParanoid; Q3V6R6; -.
DR   PhylomeDB; Q3V6R6; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:InterPro.
DR   GO; GO:0120020; F:cholesterol transfer activity; ISS: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; ISS:UniProtKB.
DR   GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISS:UniProtKB.
DR   GO; GO:0043691; P:reverse cholesterol transport; IEA:InterPro.
DR   GO; GO:0034197; P:triglyceride transport; ISS:UniProtKB.
DR   GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; ISS: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; 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.
PE   2: Evidence at transcript 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..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..505
FT                   /note="Cholesteryl ester transfer protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000394151"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        344
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        169..210
FT                   /evidence="ECO:0000250|UniProtKB:P11597"
SQ   SEQUENCE   505 AA;  56716 MW;  0957AA18588224DD CRC64;
     MLWAGGMRLG MARILLMLVH AAAACEFGPM PYSVTGIVFR MTKPAALLLN QETARLIQAS
     FKHAKFPNIT GERSMRFLGT VAYTLANIQV SDLSIEQSEV ELKENDAIDI AIKNVTAFFR
     GTLTYGYAGA WFLQLFHSVD FEIQSSIDLQ INIKLLCQEE QVAADASDCY LSFHKLMLHL
     QGDKEPGWLK QLFTDFISFT LKFVLKRELC KEINLLAQVM ANFVHNVAEN FVQDEAIGLD
     ISLASDPLIK ANYLESHHEG LVLYKNYSDV LSDSVFSPSL LSESRMLYFW ISEHILNSLA
     SAAFLDGRLV LAIRGEKLQA LFEFEDTEAQ QKAVHLIFQG NSYNDSVAKV WSLALPEISL
     QPEGTVVKSL VAVEISIFPP GEEPLTALYM EEEITVTIQA AYVEKKLILR PVDSQIEFKV
     FNCTADPSGN DQSVRNFLQK MISAVGIPEV ISKIEPALTS LMNSKGLHLF EIKNPEIITR
     KRYLIVQLDF SFPNHLLLDF LEKTL
 
 
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