Q00169 (PIPNA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphatidylinositol transfer protein alpha isoform
Short name=PI-TP-alpha
Short name=PtdIns transfer protein alpha
Short name=PtdInsTP alpha

Gene names

Name:	PITPNA
Synonyms:	PITPN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.
Subcellular location	Cytoplasm.
Tissue specificity	Expressed in a wide range of tissues.
Sequence similarities	Belongs to the PtdIns transfer protein family. PI transfer class I subfamily.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm
Ligand	Lipid-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	axon guidance Traceable author statement. Source: Reactome lipid metabolic process Non-traceable author statement. Source: ProtInc visual perception Traceable author statement. Source: ProtInc
Molecular function	phosphatidylcholine transporter activity Traceable author statement. Source: ProtInc phosphatidylinositol transporter activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 270

269

Phosphatidylinositol transfer protein alpha isoform

PRO_0000191639

Sites

Binding site

58

1

Phosphatidylinositol lipid headgroup

Binding site

60

1

Phosphatidylinositol lipid headgroup

Binding site

85

1

Phosphatidylinositol lipid headgroup

Binding site

89

1

Phosphatidylinositol lipid headgroup

Binding site

96

1

Phosphatidylinositol lipid headgroup

Binding site

194

1

Phosphatidylinositol lipid headgroup

Amino acid modifications

Modified residue

57

1

Phosphotyrosine Ref.5

Modified residue

215

1

N6-acetyllysine Ref.6

Experimental info

Sequence conflict

45

1

N → P in BAA06276. Ref.2

Secondary structure

1

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270

Helix Strand Turn

Details...

Beta strand

3 – 13

11

Helix

15 – 33

19

Beta strand

38 – 49

12

Beta strand

54 – 65

12

Helix

70 – 73

4

Beta strand

81 – 90

10

Beta strand

93 – 99

7

Helix

101 – 103

3

Beta strand

106 – 120

15

Turn

123 – 126

4

Helix

130 – 133

4

Beta strand

137 – 141

5

Helix

146 – 148

3

Helix

151 – 153

3

Helix

156 – 158

3

Helix

160 – 162

3

Turn

166 – 168

3

Helix

177 – 182

6

Beta strand

190 – 200

11

Turn

203 – 205

3

Helix

206 – 230

25

Helix

232 – 235

4

Helix

240 – 260

21

Sequences

	Sequence		Length	Mass (Da)
	Q00169 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 4531E6E38697C93B	FASTA	270	31,806
	10 20 30 40 50 60 MVLLKEYRVI LPVSVDEYQV GQLYSVAEAS KNETGGGEGV EVLVNEPYEK DGEKGQYTHK 70 80 90 100 110 120 IYHLQSKVPT FVRMLAPEGA LNIHEKAWNA YPYCRTVITN EYMKEDFLIK IETWHKPDLG 130 140 150 160 170 180 TQENVHKLEP EAWKHVEAVY IDIADRSQVL SKDYKAEEDP AKFKSIKTGR GPLGPNWKQE 190 200 210 220 230 240 LVNQKDCPYM CAYKLVTVKF KWWGLQNKVE NFIHKQERRL FTNFHRQLFC WLDKWVDLTM 250 260 270 DDIRRMEEET KRQLDEMRQK DPVKGMTADD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of a human cDNA encoding phosphatidylinositol transfer protein and occurrence of a related sequence in widely divergent eukaryotes." Dickeson S.K., Helmkamp G.M. Jr., Yarbrough L.R. Gene 142:301-305(1994) [PubMed: 8194769] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[2]	Tanaka S., Yamashita S., Hosaka K. Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Ovary.
[4]	Lubec G., Afjehi-Sadat L. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 135-146, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[5]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-57, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[6]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215, MASS SPECTROMETRY.
[7]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"Structure-function analysis of human phosphatidylinositol transfer protein alpha bound to phosphatidylinositol." Tilley S.J., Skippen A., Murray-Rust J., Swigart P.M., Stewart A., Morgan C.P., Cockcroft S., McDonald N.Q. Structure 12:317-326(2004) [PubMed: 14962392] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH PHOSPHATIDYLINOSITOL.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M73704 mRNA. Translation: AAA36441.1.
D30036 mRNA. Translation: BAA06276.1.
BC082976 mRNA. Translation: AAH82976.1.
BC045108 mRNA. Translation: AAH45108.1.

IPI

IPI00216048.

PIR

I53775.

RefSeq

NP_006215.1. NM_006224.3.

UniGene

Hs.429819.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UW5	X-ray	2.90	A/B/C/D	1-270	[»]

ProteinModelPortal

Q00169.

SMR

Q00169. Positions 1-269.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q00169. 2 interactions.

STRING

Q00169.

PTM databases

PhosphoSite

Q00169.

Polymorphism databases

DMDM

130770.

Proteomic databases

PRIDE

Q00169.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000313486; ENSP00000316809; ENSG00000174238.

GeneID

5306.

KEGG

hsa:5306.

Organism-specific databases

CTD

5306.

GeneCards

GC17M001368.

H-InvDB

HIX0202467.

HGNC

HGNC:9001. PITPNA.

HPA

HPA000528.

MIM

600174. gene.

neXtProt

NX_Q00169.

PharmGKB

PA33335.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05057.

HOVERGEN

HBG058915.

InParanoid

Q00169.

OMA

KLEPEAW.

OrthoDB

EOG42JNS2.

PhylomeDB

Q00169.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

Q00169.

Bgee

Q00169.

CleanEx

HS_PITPNA.

Genevestigator

Q00169.

GermOnline

ENSG00000174238. Homo sapiens.

Family and domain databases

InterPro

IPR001666. PI_transfer.
IPR023393. START-like_dom.
[Graphical view]

Gene3D

G3DSA:3.30.530.20. G3DSA:3.30.530.20. 1 hit.

PANTHER

PTHR10658. PI_transfer. 1 hit.

Pfam

PF02121. IP_trans. 1 hit.
[Graphical view]

PRINTS

PR00391. PITRANSFER.

ProtoNet

Search...

Other

NextBio

20510.

SOURCE

Search...

Entry information

Entry name

PIPNA_HUMAN

Accession

Primary (citable) accession number: Q00169

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 110 of the entry and version 2 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.