PPCT_BOVIN
ID PPCT_BOVIN Reviewed; 213 AA.
AC P02720; Q1LZA5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Phosphatidylcholine transfer protein;
DE Short=PC-TP;
DE AltName: Full=START domain-containing protein 2;
DE Short=StARD2;
DE AltName: Full=StAR-related lipid transfer protein 2;
GN Name=PCTP; Synonyms=STARD2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7590292; DOI=10.1016/0378-1119(95)00382-g;
RA Cohen D.E., Green R.M.;
RT "Cloning and characterization of a cDNA encoding the specific
RT phosphatidylcholine transfer protein from bovine liver.";
RL Gene 163:327-328(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8645232; DOI=10.1042/bj3160049;
RA Geijtenbeek T.B.H., Smith A.J., Borst P., Wirtz K.W.A.;
RT "cDNA cloning and tissue-specific expression of the phosphatidylcholine
RT transfer protein gene.";
RL Biochem. J. 316:49-55(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 1-122, AND ACETYLATION AT MET-1.
RX PubMed=7042332;
RA Moonen P., Akeroyd R., Westerman J., Puyk W.C., Smits P., Wirtz K.W.A.;
RT "The primary structure of the phosphatidylcholine-exchange protein from
RT bovine liver. Isolation and characterization of the staphylococcal protease
RT peptides and the amino-acid sequence of the N-terminal half (residues 1-
RT 122).";
RL Eur. J. Biochem. 106:279-290(1980).
RN [5]
RP PROTEIN SEQUENCE OF 110-213.
RX PubMed=7011810; DOI=10.1111/j.1432-1033.1981.tb05158.x;
RA Akeroyd R., Moonen P., Westerman J., Puyk W.C., Wirtz K.W.A.;
RT "The complete primary structure of the phosphatidylcholine-transfer protein
RT from bovine liver. Isolation and characterization of the cyanogen bromide
RT peptides.";
RL Eur. J. Biochem. 114:385-391(1981).
RN [6]
RP PROTEIN SEQUENCE OF 146-183.
RX PubMed=499208; DOI=10.1111/j.1432-1033.1979.tb13274.x;
RA Moonen P., Haagsman H.P., van Deenen L.L.M., Wirtz K.W.A.;
RT "Determination of the hydrophobic binding site of phosphatidylcholine
RT exchange protein with photosensitive phosphatidylcholine.";
RL Eur. J. Biochem. 99:439-445(1979).
RN [7]
RP MUTAGENESIS OF LYS-55.
RX PubMed=11551535; DOI=10.1016/s0009-3084(01)00171-2;
RA de Brouwer A.P., Bouma B., van Tiel C.M., Heerma W., Brouwers J.F.,
RA Bevers L.E., Westerman J., Roelofsen B., Wirtz K.W.;
RT "The binding of phosphatidylcholine to the phosphatidylcholine transfer
RT protein: affinity and role in folding.";
RL Chem. Phys. Lipids 112:109-119(2001).
CC -!- FUNCTION: Catalyzes the transfer of phosphatidylcholine between
CC membranes. Binds phosphatidylcholine in a tight 1:1 stoichiometric
CC complex.
CC -!- SUBUNIT: Interacts with ACOT13/THEM2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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DR EMBL; U21660; AAA87003.1; -; mRNA.
DR EMBL; Z50026; CAA90330.1; -; mRNA.
DR EMBL; BC116120; AAI16121.1; -; mRNA.
DR PIR; A91092; EPBO.
DR RefSeq; NP_777260.1; NM_174835.2.
DR AlphaFoldDB; P02720; -.
DR SMR; P02720; -.
DR STRING; 9913.ENSBTAP00000024898; -.
DR iPTMnet; P02720; -.
DR PaxDb; P02720; -.
DR PRIDE; P02720; -.
DR Ensembl; ENSBTAT00000024898; ENSBTAP00000024898; ENSBTAG00000018706.
DR GeneID; 317656; -.
DR KEGG; bta:317656; -.
DR CTD; 58488; -.
DR VEuPathDB; HostDB:ENSBTAG00000018706; -.
DR eggNOG; KOG2761; Eukaryota.
DR GeneTree; ENSGT00940000156843; -.
DR HOGENOM; CLU_042209_1_0_1; -.
DR InParanoid; P02720; -.
DR OMA; FRKQWDQ; -.
DR OrthoDB; 973910at2759; -.
DR TreeFam; TF320705; -.
DR Reactome; R-BTA-1483191; Synthesis of PC.
DR Reactome; R-BTA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000018706; Expressed in liver and 106 other tissues.
DR ExpressionAtlas; P02720; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISS:UniProtKB.
DR GO; GO:0008525; F:phosphatidylcholine transporter activity; ISS:UniProtKB.
DR GO; GO:0015914; P:phospholipid transport; ISS:UniProtKB.
DR CDD; cd08910; START_STARD2-like; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR041950; STARD2_START.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR Pfam; PF01852; START; 1.
DR SMART; SM00234; START; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Lipid transport;
KW Lipid-binding; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..213
FT /note="Phosphatidylcholine transfer protein"
FT /id="PRO_0000220657"
FT DOMAIN 1..212
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT REGION 171..176
FT /note="Part of the binding site for phosphatidylcholine"
FT BINDING 72
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT /ligand_id="ChEBI:CHEBI:57643"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT /ligand_id="ChEBI:CHEBI:57643"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT /ligand_id="ChEBI:CHEBI:57643"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:7042332"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKL6"
FT MUTAGEN 55
FT /note="K->I: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11551535"
FT CONFLICT 167
FT /note="R -> K (in Ref. 2; CAA90330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 213 AA; 24643 MW; 3BDEE6E54567EF10 CRC64;
MDPGAGAFSE EQFREACAEL QRPALSGAAW ELLVETQGIS VYRLLDQQTG LYAYKVFGVL
EDCLPDLLAD VYMDLAYRKQ WDQYVKELYE KECSGETVVY WQVKYPFPMS NRDYVYVRQR
QELDFEGQKV HVILAQSTSE PQFPEKSGVI RVKHYKQRLA IQSDGKRGSK VFMYYFDNPG
GQIPSWVINW AAKNGVPNFL KDMVKACQNY KKT
