ID   PPCT_MOUSE              Reviewed;         214 AA.
AC   P53808; Q9QZX0; Q9R058;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   08-NOV-2023, entry version 134.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=129/Ola; TISSUE=Liver;
RX   PubMed=10500206; DOI=10.1073/pnas.96.20.11501;
RA   van Helvoort A., de Brouwer A., Ottenhoff R., Brouwers J.F.H.M.,
RA   Wijnholds J., Beijnen J.H., Rijneveld A., van der Poll T.,
RA   van der Valk M.A., Majoor D., Voorhout W., Wirtz K.W.A.,
RA   Oude Elferink R.P.J., Borst P.;
RT   "Mice without phosphatidylcholine transfer protein have no defects in the
RT   secretion of PC into bile or into the lung airspaces.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:11501-11506(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 41-214.
RC   TISSUE=Lung;
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 [MRNA] OF 82-214.
RC   STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX   PubMed=10542325; DOI=10.1016/s0167-4781(99)00163-3;
RA   Cohen D.E., Green R.M., Wu M.K., Beier D.R.;
RT   "Cloning, tissue-specific expression, gene structure and chromosomal
RT   localization of human phosphatidylcholine transfer protein.";
RL   Biochim. Biophys. Acta 1447:265-270(1999).
RN   [4]
RP   INTERACTION WITH ACOT13/THEM2 AND PAX3.
RX   PubMed=17704541; DOI=10.1074/jbc.m703745200;
RA   Kanno K., Wu M.K., Agate D.S., Fanelli B.J., Wagle N., Scapa E.F.,
RA   Ukomadu C., Cohen D.E.;
RT   "Interacting proteins dictate function of the minimal START domain
RT   phosphatidylcholine transfer protein/StarD2.";
RL   J. Biol. Chem. 282:30728-30736(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, Lung, Pancreas, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Catalyzes the transfer of phosphatidylcholine between
CC       membranes. Binds a single lipid molecule.
CC   -!- SUBUNIT: Interacts with ACOT13/THEM2. {ECO:0000269|PubMed:17704541}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10500206}.
CC   -!- TISSUE SPECIFICITY: Abundant in liver of pups but levels in liver
CC       decrease 10-fold about 2 weeks after birth. In adult, highly expressed
CC       in epididymis, testis, kidney and bone-marrow derived mast cells.
CC       {ECO:0000269|PubMed:10500206}.
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DR   EMBL; AF151639; AAF02537.1; -; mRNA.
DR   EMBL; Z50024; CAA90328.1; -; mRNA.
DR   EMBL; AF114437; AAF08346.1; -; mRNA.
DR   CCDS; CCDS25238.1; -.
DR   PIR; S68246; S68246.
DR   AlphaFoldDB; P53808; -.
DR   SMR; P53808; -.
DR   BioGRID; 202066; 2.
DR   STRING; 10090.ENSMUSP00000020864; -.
DR   iPTMnet; P53808; -.
DR   PhosphoSitePlus; P53808; -.
DR   SwissPalm; P53808; -.
DR   EPD; P53808; -.
DR   jPOST; P53808; -.
DR   MaxQB; P53808; -.
DR   PaxDb; 10090-ENSMUSP00000020864; -.
DR   PeptideAtlas; P53808; -.
DR   ProteomicsDB; 289803; -.
DR   Pumba; P53808; -.
DR   DNASU; 18559; -.
DR   AGR; MGI:107375; -.
DR   MGI; MGI:107375; Pctp.
DR   eggNOG; KOG2761; Eukaryota.
DR   InParanoid; P53808; -.
DR   PhylomeDB; P53808; -.
DR   Reactome; R-MMU-1483191; Synthesis of PC.
DR   Reactome; R-MMU-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   SABIO-RK; P53808; -.
DR   PRO; PR:P53808; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P53808; Protein.
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:0008203; P:cholesterol metabolic process; IMP:MGI.
DR   GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:0015914; P:phospholipid transport; ISS:UniProtKB.
DR   Gene3D; 3.30.530.20; -; 1.
DR   InterPro; IPR023393; START-like_dom_sf.
DR   InterPro; IPR002913; START_lipid-bd_dom.
DR   PANTHER; PTHR19308; PHOSPHATIDYLCHOLINE TRANSFER PROTEIN; 1.
DR   PANTHER; PTHR19308:SF39; PHOSPHATIDYLCHOLINE TRANSFER PROTEIN; 1.
DR   Pfam; PF01852; START; 1.
DR   SMART; SM00234; START; 1.
DR   SUPFAM; SSF55961; Bet v1-like; 1.
DR   PROSITE; PS50848; START; 1.
PE   1: Evidence at protein 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_0000220659"
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        90
FT                   /note="E -> D (in Ref. 3; AAF08346)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="R -> G (in Ref. 3; AAF08346)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   214 AA;  24785 MW;  8BE2B046314DAE70 CRC64;
     MAGAACCFSD EQFREACAEL QKPALTGADW QLLVEASGIT IYRLLDQPSG LYEYKVFGVL
     EGCSPALLTD VYMDLDYRKQ WDQYVKELYE KESDEQMVAY WEVKYPFPLS NRDYVYTRQR
     RDLDVDRRKI YVVLAQSISA PQFPEKSGVI RVKQYKQSLA IESDGKKGSR VFMYYFDNPG
     GQIPSWLINW AAKNGVPNFL KDMVKACQNY HKKT
//