PPCT_HUMAN
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 03-AUG-2022, entry version 171.
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 PDBsum; 1LN1; -.
DR PDBsum; 1LN2; -.
DR PDBsum; 1LN3; -.
DR AlphaFoldDB; Q9UKL6; -.
DR SMR; Q9UKL6; -.
DR BioGRID; 121818; 10.
DR IntAct; Q9UKL6; 2.
DR STRING; 9606.ENSP00000268896; -.
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; Q9UKL6; -.
DR PeptideAtlas; Q9UKL6; -.
DR PRIDE; Q9UKL6; -.
DR ProteomicsDB; 84818; -. [Q9UKL6-1]
DR ProteomicsDB; 84819; -. [Q9UKL6-2]
DR Antibodypedia; 30858; 207 antibodies from 24 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 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; FRKQWDQ; -.
DR OrthoDB; 973910at2759; -.
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; 17 hits in 1082 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 172 other tissues.
DR ExpressionAtlas; Q9UKL6; baseline and differential.
DR Genevisible; Q9UKL6; HS.
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 Pfam; PF01852; START; 1.
DR SMART; SM00234; START; 1.
DR PROSITE; PS50848; START; 1.
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..15
FT /evidence="ECO:0007829|PDB:1LN1"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:1LN1"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:1LN1"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:1LN1"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1LN1"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1LN1"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:1LN1"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:1LN1"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:1LN1"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:1LN1"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1LN1"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1LN2"
FT STRAND 112..123
FT /evidence="ECO:0007829|PDB:1LN1"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1LN2"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:1LN1"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1LN1"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:1LN1"
FT STRAND 165..177
FT /evidence="ECO:0007829|PDB:1LN1"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:1LN1"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:1LN1"
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
