Q9UKL6 (PPCT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphatidylcholine transfer protein
Short name=PC-TP

Alternative name(s):
START domain-containing protein 2
Short name=StARD2
StAR-related lipid transfer protein 2

Gene names

Name:	PCTP
Synonyms:	STARD2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	214 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of phosphatidylcholine between membranes. Binds a single lipid molecule. Ref.7
Subunit structure	Interacts with ACOT13/THEM2 By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Highest expression in liver, placenta, testis, kidney and heart. Low levels in brain and lung. No expression detected in thymus. Ref.1
Sequence similarities	Contains 1 START domain.
Sequence caution	The sequence AAH05112.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Lipid transport Transport
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Lipid-binding
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cholesterol metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	phosphatidylcholine binding Inferred from direct assay Ref.7. Source: UniProtKB phosphatidylcholine transporter activity Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UKL6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UKL6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 214

214

Phosphatidylcholine transfer protein

PRO_0000220658

Regions

Domain

1 – 212

212

START

Sites

Binding site

72

1

Phosphatidylcholine

Binding site

78

1

Phosphatidylcholine

Binding site

157

1

Phosphatidylcholine

Amino acid modifications

Modified residue

1

1

N-acetylmethionine By similarity

Natural variations

Alternative sequence

1 – 72

72

Missing in isoform 2.

VSP_041363

Natural variant

10

1

E → A.
Corresponds to variant rs12941739 [ dbSNP | Ensembl ].

VAR_052070

Experimental info

Mutagenesis

63

1

C → A: Reduces activity by 20%. Ref.7

Sequence conflict

52

1

Y → H in AAF08347. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

214

Helix Strand Turn

Details...

Helix

10 – 15

6

Helix

18 – 21

4

Turn

26 – 29

4

Beta strand

31 – 36

6

Beta strand

39 – 45

7

Turn

47 – 49

3

Beta strand

52 – 60

9

Helix

65 – 73

9

Helix

75 – 81

7

Beta strand

85 – 93

9

Beta strand

96 – 103

8

Beta strand

107 – 109

3

Beta strand

112 – 123

12

Helix

125 – 127

3

Beta strand

130 – 137

8

Beta strand

149 – 152

4

Beta strand

155 – 163

9

Beta strand

165 – 177

13

Helix

185 – 193

9

Helix

195 – 208

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: E40204B7C0A9AF83	FASTA	214	24,843
	10 20 30 40 50 60 MELAAGSFSE EQFWEACAEL QQPALAGADW QLLVETSGIS IYRLLDKKTG LYEYKVFGVL 70 80 90 100 110 120 EDCSPTLLAD IYMDSDYRKQ WDQYVKELYE QECNGETVVY WEVKYPFPMS NRDYVYLRQR 130 140 150 160 170 180 RDLDMEGRKI HVILARSTSM PQLGERSGVI RVKQYKQSLA IESDGKKGSK VFMYYFDNPG 190 200 210 GQIPSWLINW AAKNGVPNFL KDMARACQNY LKKT
	Isoform 2 [UniParc]. Checksum: 1BA1CE03358BAB59	FASTA	142	16,824
	10 20 30 40 50 60 MDSDYRKQWD QYVKELYEQE CNGETVVYWE VKYPFPMSNR DYVYLRQRRD LDMEGRKIHV 70 80 90 100 110 120 ILARSTSMPQ LGERSGVIRV KQYKQSLAIE SDGKKGSKVF MYYFDNPGGQ IPSWLINWAA 130 140 KNGVPNFLKD MARACQNYLK KT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, tissue-specific expression, gene structure and chromosomal localization of human phosphatidylcholine transfer protein." Cohen D.E., Green R.M., Wu M.K., Beier D.R. Biochim. Biophys. Acta 1447:265-270(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Kidney.
[2]	"Mice without phosphatidylcholine transfer protein have no defects in the secretion of PC into bile or into the lung airspaces." van Helvoort A., de Brouwer A., Ottenhoff R., Brouwers J.F.H.M., Wijnholds J., Beijnen J.H., Rijneveld A., van der Poll T., van der Valk M.A., Majoor D., Voorhout W., Wirtz K.W.A., Oude Elferink R.P.J., Borst P. Proc. Natl. Acad. Sci. U.S.A. 96:11501-11506(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Uterus.
[3]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: B-cell.
[5]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]	"Human phosphatidylcholine transfer protein: purification, crystallization and preliminary X-ray diffraction data." Chan W.W., Roderick S.L., Cohen D.E. Biochim. Biophys. Acta 1596:1-5(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[7]	"Structure of human phosphatidylcholine transfer protein in complex with its ligand." Roderick S.L., Chan W.W., Agate D.S., Olsen L.R., Vetting M.W., Rajashankar K.R., Cohen D.E. Nat. Struct. Biol. 9:507-511(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEXES WITH PHOSPHATIDYLCHOLINE, FUNCTION, MUTAGENESIS OF CYS-63.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF114436 , AF114431, AF114432, AF114433, AF114434, AF114435 Genomic DNA. Translation: AAF08347.1.
AF114430 mRNA. Translation: AAF08345.1.
AF151638 mRNA. Translation: AAF02536.1.
AC009837 Genomic DNA. No translation available.
AC091155 Genomic DNA. No translation available.
BC005112 mRNA. Translation: AAH05112.1. Different initiation.
BC012084 mRNA. Translation: AAH12084.1.

IPI

IPI00296927.
IPI00645437.

RefSeq

NP_001095872.1. NM_001102402.2.
NP_067036.2. NM_021213.3.

UniGene

Hs.285218.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LN1	X-ray	2.40	A	1-214	[»]
1LN2	X-ray	2.90	A/B	1-214	[»]
1LN3	X-ray	2.90	A/B	1-214	[»]

ProteinModelPortal

Q9UKL6.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000268896.

PTM databases

PhosphoSite

Q9UKL6.

Polymorphism databases

DMDM

15214192.

Proteomic databases

PaxDb

Q9UKL6.

PRIDE

Q9UKL6.

Protocols and materials databases

DNASU

58488.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000268896; ENSP00000268896; ENSG00000141179.
ENST00000325214; ENSP00000325181; ENSG00000141179.

GeneID

58488.

KEGG

hsa:58488.

UCSC

uc002iul.4. human.

Organism-specific databases

CTD

58488.

GeneCards

GC17P053828.

HGNC

HGNC:8752. PCTP.

HPA

HPA022979.

MIM

606055. gene.

neXtProt

NX_Q9UKL6.

PharmGKB

PA33098.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG264966.

HOGENOM

HOG000261644.

HOVERGEN

HBG008237.

InParanoid

Q9UKL6.

OMA

CADVYMD.

OrthoDB

EOG47SSFK.

PhylomeDB

Q9UKL6.

Gene expression databases

ArrayExpress

Q9UKL6.

Bgee

Q9UKL6.

CleanEx

HS_PCTP.

Genevestigator

Q9UKL6.

GermOnline

ENSG00000141179. Homo sapiens.

Family and domain databases

Gene3D

3.30.530.20. 1 hit.

InterPro

IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]

Pfam

PF01852. START. 1 hit.
[Graphical view]

SMART

SM00234. START. 1 hit.
[Graphical view]

PROSITE

PS50848. START. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9UKL6.

GenomeRNAi

58488.

NextBio

64950.

SOURCE

Search...

Entry information

Entry name

PPCT_HUMAN

Accession

Primary (citable) accession number: Q9UKL6
Secondary accession number(s): Q9BSC9, Q9UIT3, Q9UKW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.