PPCT_RAT
ID PPCT_RAT Reviewed; 214 AA.
AC P53809; Q9Z2N9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 120.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10415339; DOI=10.1016/s0378-1119(99)00204-8;
RA Wu M.K., Boylan M.O., Cohen D.E.;
RT "Cloning and gene structure of rat phosphatidylcholine transfer protein,
RT Pctp.";
RL Gene 235:111-120(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 100-179.
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).
CC -!- FUNCTION: Lipid transfer protein that promotes intermembrane transfer
CC of phosphatidylcholines but no other phospholipids. Binds a single
CC lipid molecule. May play a role in hepatocellular selection and
CC transport of phosphatidylcholines during bile formation.
CC -!- SUBUNIT: Interacts with ACOT13/THEM2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF040267; AAC98930.1; -; Genomic_DNA.
DR EMBL; AF040262; AAC98930.1; JOINED; Genomic_DNA.
DR EMBL; AF040263; AAC98930.1; JOINED; Genomic_DNA.
DR EMBL; AF040264; AAC98930.1; JOINED; Genomic_DNA.
DR EMBL; AF040265; AAC98930.1; JOINED; Genomic_DNA.
DR EMBL; AF040266; AAC98930.1; JOINED; Genomic_DNA.
DR EMBL; AF040261; AAC98929.1; -; mRNA.
DR EMBL; BC078854; AAH78854.1; -; mRNA.
DR EMBL; Z50025; CAA90329.1; -; mRNA.
DR RefSeq; NP_058921.1; NM_017225.3.
DR AlphaFoldDB; P53809; -.
DR SMR; P53809; -.
DR STRING; 10116.ENSRNOP00000003295; -.
DR PaxDb; P53809; -.
DR Ensembl; ENSRNOT00000003295; ENSRNOP00000003295; ENSRNOG00000002425.
DR GeneID; 29510; -.
DR KEGG; rno:29510; -.
DR CTD; 58488; -.
DR RGD; 3276; Pctp.
DR eggNOG; KOG2761; Eukaryota.
DR GeneTree; ENSGT00940000156843; -.
DR HOGENOM; CLU_042209_1_0_1; -.
DR InParanoid; P53809; -.
DR OMA; FRKQWDQ; -.
DR OrthoDB; 973910at2759; -.
DR PhylomeDB; P53809; -.
DR TreeFam; TF320705; -.
DR Reactome; R-RNO-1483191; Synthesis of PC.
DR Reactome; R-RNO-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR PRO; PR:P53809; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000002425; Expressed in liver and 19 other tissues.
DR Genevisible; P53809; RN.
DR GO; GO:0005829; C:cytosol; TAS:RGD.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISS:UniProtKB.
DR GO; GO:0008525; F:phosphatidylcholine transporter activity; ISS:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Lipid transport; Lipid-binding; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..214
FT /note="Phosphatidylcholine transfer protein"
FT /id="PRO_0000220660"
FT DOMAIN 1..212
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
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:0000250|UniProtKB:P02720"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKL6"
FT CONFLICT 102
FT /note="E -> Q (in Ref. 3; CAA90329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 24734 MW; 35D26960235C2374 CRC64;
MAGPAAHFSD EQFREACAEL QKPALTGADW QLLVEASGIT IYRLLDQSTG LYEYKVFGVL
ESCIPSLLAD VYMDLDYRKK WDQYVKELYE KSFDGQMVAY WEVKYPFPLS NRDYVYTRQR
RDLDVDGRKI YVVLAQNISV PQFPEKSGVI RVKQYKQSLA IESDGKKGSR VFMYYFDNPG
GQIPSWLINW AAKNGVPSFL KDMVKACQNY HKKT
