ID   PPCT_HUMAN              Reviewed;         214 AA.
AC   Q9UKL6; Q9BSC9; Q9UIT3; Q9UKW7;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 179.
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Kidney;
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Uterus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=B-cell;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   PubMed=11983415; DOI=10.1016/s0167-4838(01)00318-1;
RA   Chan W.W., Roderick S.L., Cohen D.E.;
RT   "Human phosphatidylcholine transfer protein: purification, crystallization
RT   and preliminary X-ray diffraction data.";
RL   Biochim. Biophys. Acta 1596:1-5(2002).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEXES WITH
RP   PHOSPHATIDYLCHOLINE, FUNCTION, AND MUTAGENESIS OF CYS-63.
RX   PubMed=12055623; DOI=10.1038/nsb812;
RA   Roderick S.L., Chan W.W., Agate D.S., Olsen L.R., Vetting M.W.,
RA   Rajashankar K.R., Cohen D.E.;
RT   "Structure of human phosphatidylcholine transfer protein in complex with
RT   its ligand.";
RL   Nat. Struct. Biol. 9:507-511(2002).
CC   -!- FUNCTION: Catalyzes the transfer of phosphatidylcholine between
CC       membranes. Binds a single lipid molecule.
CC       {ECO:0000269|PubMed:12055623}.
CC   -!- SUBUNIT: Interacts with ACOT13/THEM2. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9UKL6; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-4402391, EBI-741181;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53808}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UKL6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UKL6-2; Sequence=VSP_041363;
CC   -!- TISSUE SPECIFICITY: Highest expression in liver, placenta, testis,
CC       kidney and heart. Low levels in brain and lung. No expression detected
CC       in thymus. {ECO:0000269|PubMed:10542325}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH05112.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF114436; AAF08347.1; -; Genomic_DNA.
DR   EMBL; AF114431; AAF08347.1; JOINED; Genomic_DNA.
DR   EMBL; AF114432; AAF08347.1; JOINED; Genomic_DNA.
DR   EMBL; AF114433; AAF08347.1; JOINED; Genomic_DNA.
DR   EMBL; AF114434; AAF08347.1; JOINED; Genomic_DNA.
DR   EMBL; AF114435; AAF08347.1; JOINED; Genomic_DNA.
DR   EMBL; AF114430; AAF08345.1; -; mRNA.
DR   EMBL; AF151638; AAF02536.1; -; mRNA.
DR   EMBL; AC009837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC091155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005112; AAH05112.1; ALT_INIT; mRNA.
DR   EMBL; BC012084; AAH12084.1; -; mRNA.
DR   CCDS; CCDS11588.1; -. [Q9UKL6-1]
DR   CCDS; CCDS45741.1; -. [Q9UKL6-2]
DR   RefSeq; NP_001095872.1; NM_001102402.2. [Q9UKL6-2]
DR   RefSeq; NP_001317307.1; NM_001330378.1.
DR   RefSeq; NP_067036.2; NM_021213.3. [Q9UKL6-1]
DR   PDB; 1LN1; X-ray; 2.40 A; A=1-214.
DR   PDB; 1LN2; X-ray; 2.90 A; A/B=1-214.
DR   PDB; 1LN3; X-ray; 2.90 A; A/B=1-214.
DR   PDB; 7U9D; X-ray; 2.18 A; A=1-214.
DR   PDBsum; 1LN1; -.
DR   PDBsum; 1LN2; -.
DR   PDBsum; 1LN3; -.
DR   PDBsum; 7U9D; -.
DR   AlphaFoldDB; Q9UKL6; -.
DR   SMR; Q9UKL6; -.
DR   BioGRID; 121818; 12.
DR   IntAct; Q9UKL6; 2.
DR   STRING; 9606.ENSP00000460437; -.
DR   ChEMBL; CHEMBL4523490; -.
DR   DrugBank; DB04372; L-Dilinoleoyllecithin.
DR   DrugBank; DB09568; Omega-3-carboxylic acids.
DR   DrugBank; DB02306; Palmitoyl-Linoleoyl Phosphatidylcholine.
DR   SwissLipids; SLP:000001541; -.
DR   iPTMnet; Q9UKL6; -.
DR   MetOSite; Q9UKL6; -.
DR   PhosphoSitePlus; Q9UKL6; -.
DR   BioMuta; PCTP; -.
DR   DMDM; 15214192; -.
DR   EPD; Q9UKL6; -.
DR   MassIVE; Q9UKL6; -.
DR   MaxQB; Q9UKL6; -.
DR   PaxDb; 9606-ENSP00000268896; -.
DR   PeptideAtlas; Q9UKL6; -.
DR   ProteomicsDB; 84818; -. [Q9UKL6-1]
DR   ProteomicsDB; 84819; -. [Q9UKL6-2]
DR   Pumba; Q9UKL6; -.
DR   Antibodypedia; 30858; 227 antibodies from 23 providers.
DR   DNASU; 58488; -.
DR   Ensembl; ENST00000268896.10; ENSP00000268896.4; ENSG00000141179.14. [Q9UKL6-1]
DR   Ensembl; ENST00000325214.10; ENSP00000325181.5; ENSG00000141179.14. [Q9UKL6-2]
DR   GeneID; 58488; -.
DR   KEGG; hsa:58488; -.
DR   MANE-Select; ENST00000268896.10; ENSP00000268896.4; NM_021213.4; NP_067036.2.
DR   UCSC; uc002iul.5; human. [Q9UKL6-1]
DR   AGR; HGNC:8752; -.
DR   CTD; 58488; -.
DR   DisGeNET; 58488; -.
DR   GeneCards; PCTP; -.
DR   HGNC; HGNC:8752; PCTP.
DR   HPA; ENSG00000141179; Tissue enhanced (liver).
DR   MIM; 606055; gene.
DR   neXtProt; NX_Q9UKL6; -.
DR   OpenTargets; ENSG00000141179; -.
DR   PharmGKB; PA33098; -.
DR   VEuPathDB; HostDB:ENSG00000141179; -.
DR   eggNOG; KOG2761; Eukaryota.
DR   GeneTree; ENSGT00940000156843; -.
DR   HOGENOM; CLU_042209_1_0_1; -.
DR   InParanoid; Q9UKL6; -.
DR   OMA; GETVTYW; -.
DR   OrthoDB; 1346920at2759; -.
DR   PhylomeDB; Q9UKL6; -.
DR   TreeFam; TF320705; -.
DR   PathwayCommons; Q9UKL6; -.
DR   Reactome; R-HSA-1483191; Synthesis of PC.
DR   Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   SignaLink; Q9UKL6; -.
DR   BioGRID-ORCS; 58488; 20 hits in 1160 CRISPR screens.
DR   ChiTaRS; PCTP; human.
DR   EvolutionaryTrace; Q9UKL6; -.
DR   GeneWiki; Phosphatidylcholine_transfer_protein; -.
DR   GenomeRNAi; 58488; -.
DR   Pharos; Q9UKL6; Tbio.
DR   PRO; PR:Q9UKL6; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9UKL6; Protein.
DR   Bgee; ENSG00000141179; Expressed in secondary oocyte and 174 other cell types or tissues.
DR   ExpressionAtlas; Q9UKL6; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR   GO; GO:0031210; F:phosphatidylcholine binding; IDA:UniProtKB.
DR   GO; GO:0008525; F:phosphatidylcholine transporter activity; IDA:UniProtKB.
DR   GO; GO:0006869; P:lipid transport; NAS:UniProtKB.
DR   GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0015914; P:phospholipid transport; IDA: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   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.
DR   Genevisible; Q9UKL6; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Lipid transport; Lipid-binding; Phosphoprotein; Reference proteome;
KW   Transport.
FT   CHAIN           1..214
FT                   /note="Phosphatidylcholine transfer protein"
FT                   /id="PRO_0000220658"
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   BINDING         78
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:57643"
FT   BINDING         157
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:57643"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P02720"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..72
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_041363"
FT   VARIANT         10
FT                   /note="E -> A (in dbSNP:rs12941739)"
FT                   /id="VAR_052070"
FT   MUTAGEN         63
FT                   /note="C->A: Reduces activity by 20%."
FT                   /evidence="ECO:0000269|PubMed:12055623"
FT   CONFLICT        52
FT                   /note="Y -> H (in Ref. 1; AAF08347)"
FT                   /evidence="ECO:0000305"
FT   HELIX           10..16
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   HELIX           18..21
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   TURN            26..29
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   STRAND          31..36
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   STRAND          39..45
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   STRAND          52..61
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   HELIX           65..73
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   HELIX           75..81
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   STRAND          85..103
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:1LN2"
FT   STRAND          111..125
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   STRAND          128..137
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   STRAND          149..152
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   STRAND          154..163
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   STRAND          165..177
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   HELIX           185..193
FT                   /evidence="ECO:0007829|PDB:7U9D"
FT   HELIX           195..208
FT                   /evidence="ECO:0007829|PDB:7U9D"
SQ   SEQUENCE   214 AA;  24843 MW;  E40204B7C0A9AF83 CRC64;
     MELAAGSFSE EQFWEACAEL QQPALAGADW QLLVETSGIS IYRLLDKKTG LYEYKVFGVL
     EDCSPTLLAD IYMDSDYRKQ WDQYVKELYE QECNGETVVY WEVKYPFPMS NRDYVYLRQR
     RDLDMEGRKI HVILARSTSM PQLGERSGVI RVKQYKQSLA IESDGKKGSK VFMYYFDNPG
     GQIPSWLINW AAKNGVPNFL KDMARACQNY LKKT
//