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Database: UniProt
Entry: A0A094KKZ6_ANTCR
LinkDB: A0A094KKZ6_ANTCR
Original site: A0A094KKZ6_ANTCR 
ID   A0A094KKZ6_ANTCR        Unreviewed;       505 AA.
AC   A0A094KKZ6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Cholesteryl ester transfer protein {ECO:0000256|ARBA:ARBA00022354, ECO:0000256|PIRNR:PIRNR037185};
GN   ORFNames=N321_06687 {ECO:0000313|EMBL:KFZ58082.1};
OS   Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC   Caprimulgidae; Antrostomus.
OX   NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ58082.1, ECO:0000313|Proteomes:UP000053620};
RN   [1] {ECO:0000313|EMBL:KFZ58082.1, ECO:0000313|Proteomes:UP000053620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ58082.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|PIRNR:PIRNR037185}.
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:0000256|ARBA:ARBA00001417};
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:0000256|ARBA:ARBA00001140};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cholesteryl (9Z-octadecenoate)(in) = cholesteryl (9Z-
CC         octadecenoate)(out); Xref=Rhea:RHEA:43348, ChEBI:CHEBI:46898;
CC         Evidence={ECO:0000256|ARBA:ARBA00000222};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|PIRNR:PIRNR037185}.
CC       Note=Secreted in plasma. {ECO:0000256|PIRNR:PIRNR037185}.
CC   -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC       {ECO:0000256|PIRNR:PIRNR037185}.
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DR   EMBL; KL349613; KFZ58082.1; -; Genomic_DNA.
DR   RefSeq; XP_010166072.1; XM_010167770.1.
DR   AlphaFoldDB; A0A094KKZ6; -.
DR   GeneID; 104524786; -.
DR   KEGG; acar:104524786; -.
DR   CTD; 1071; -.
DR   OrthoDB; 5355726at2759; -.
DR   Proteomes; UP000053620; Unassembled WGS sequence.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-UniRule.
DR   GO; GO:0120020; F:cholesterol transfer activity; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:UniProtKB-UniRule.
DR   GO; GO:0043691; P:reverse cholesterol transport; IEA:InterPro.
DR   GO; GO:0034197; P:triglyceride transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IEA:UniProtKB-UniRule.
DR   CDD; cd00025; BPI1; 1.
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; CHOLESTERYL ESTER TRANSFER PROTEIN; 1.
DR   PANTHER; PTHR47616:SF1; CHOLESTERYL ESTER TRANSFER PROTEIN; 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; Bactericidal permeability-increasing protein, BPI; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548,
KW   ECO:0000256|PIRNR:PIRNR037185};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR037185-50};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|PIRNR:PIRNR037185};
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055,
KW   ECO:0000256|PIRNR:PIRNR037185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053620};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR037185};
KW   Signal {ECO:0000256|PIRNR:PIRNR037185};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023221,
KW   ECO:0000256|PIRNR:PIRNR037185};
KW   Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037185}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|PIRNR:PIRNR037185"
FT   CHAIN           25..505
FT                   /note="Cholesteryl ester transfer protein"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR037185"
FT                   /id="PRO_5015219182"
FT   DOMAIN          40..267
FT                   /note="Lipid-binding serum glycoprotein N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00328"
FT   DOMAIN          281..488
FT                   /note="Lipid-binding serum glycoprotein C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00329"
FT   DISULFID        169..210
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037185-50"
SQ   SEQUENCE   505 AA;  56949 MW;  73959B23ACBF337D CRC64;
     MLWAGRMRLG TFGILLMLVH ASAACEFEPF PYSVTGIVCR MTKPAALLLN QETAQVIQAA
     FRNAKFPNIT GERSMRLLGK VAYGLTNIQV NDLSIEQSEV ELKENDAIYI AIKNVTAFFK
     GTLTYGYAGA WFLQLFHSVD FEIESSIDLQ INIKLMCQKD QVAADASDCY LSFHKLILHL
     QGEKEPGWLK QLFTDFISFT LKLVLKSEVC NEINFLAQVL ANFVHDLAAN FVQDEDISVD
     ISLASVPLIK ANYLESHHKG LVLYKNYSDV FSDSVFSPLL LTESRMLYFW LSEHILNSLA
     SAAFLDKRLM LTIKGEKLQA LFEMEDTDAQ RKAVQMIFQG ASYNDSMAKV WSLAQPQISL
     QPEGTVVKSL VAVEVSIFPL GEEPLMVLYM EKEIMVTIQA AYAEKKLILH PLDSRIEFKV
     FKCTADPSGN DPSIRNFLQT MISVVGIPEV ISRIEPALTS LMNSKGLHLF EIRNPEIITR
     KGYVIVQLDF SFPNHLLLDF LEKRL
//
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