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Database: UniProt
Entry: A0A091TCF3_PHALP
LinkDB: A0A091TCF3_PHALP
Original site: A0A091TCF3_PHALP 
ID   A0A091TCF3_PHALP        Unreviewed;       505 AA.
AC   A0A091TCF3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Cholesteryl ester transfer protein {ECO:0000256|ARBA:ARBA00022354, ECO:0000256|PIRNR:PIRNR037185};
GN   ORFNames=N335_12175 {ECO:0000313|EMBL:KFQ71542.1};
OS   Phaethon lepturus (White-tailed tropicbird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC   Phaethontidae; Phaethon.
OX   NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ71542.1, ECO:0000313|Proteomes:UP000053638};
RN   [1] {ECO:0000313|EMBL:KFQ71542.1, ECO:0000313|Proteomes:UP000053638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ71542.1};
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; KK445605; KFQ71542.1; -; Genomic_DNA.
DR   RefSeq; XP_010280945.1; XM_010282643.1.
DR   AlphaFoldDB; A0A091TCF3; -.
DR   GeneID; 104617357; -.
DR   KEGG; plet:104617357; -.
DR   CTD; 1071; -.
DR   OrthoDB; 5355726at2759; -.
DR   PhylomeDB; A0A091TCF3; -.
DR   Proteomes; UP000053638; 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.
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:UP000053638};
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_5015219133"
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;  56982 MW;  6576D808F6BDAFF8 CRC64;
     MLWAGRMRLG TFGILLMLVR ASAACEFGPF PYSVTGIVCR MTKPAALLLN QETAQVIQAA
     FRNAKFPNIT GERSMRLLGK VAYGLTNIQV NDLSIEQSEV ELKENDAIHI AIKNVTAFFK
     GTLNYGYAGA WFLQLFHSVD FEIESSIDLQ INIKLTCQKD QVAADASDCY LTFHKLTLHL
     QGDKEPGWLK QLFTDFISFT LKLVLKREVC NEINFLAQVL ANFVHDLAAN FVRDEDISVD
     ISLASAPLIK ANYLESYHKG LIRYKNYSDV FSDSVFSPSL LTESRMLYFW LSEHILNSLA
     TAAFLDKRLA LTIRGEKLQA LFEMEDTETQ RKVVQMIFQG TSYNDSVAKV WSLAHPQISL
     QPEGTVVKSL VAVEISIFPP GEESLMVLYM EKEITVTIQA AYTEKKLILH PLDSRIEFKV
     FKCTADPSGN DPSIRNFLQT MISVVGIPEV ISRIEPALTS LMNSKGLNLF EIRNPEIITR
     KGYIIVQLDF SFPNHLLLDF LEKML
//
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