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Q00169

- PIPNA_HUMAN

UniProt

Q00169 - PIPNA_HUMAN

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Protein

Phosphatidylinositol transfer protein alpha isoform

Gene

PITPNA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei58 – 581Phosphatidylinositol lipid headgroup1 Publication
Binding sitei60 – 601Phosphatidylinositol lipid headgroup1 Publication
Binding sitei85 – 851Phosphatidylinositol lipid headgroup1 Publication
Binding sitei89 – 891Phosphatidylinositol lipid headgroup1 Publication
Binding sitei96 – 961Phosphatidylinositol lipid headgroup1 Publication
Binding sitei194 – 1941Phosphatidylinositol lipid headgroup1 Publication

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW
  2. phosphatidylcholine transporter activity Source: ProtInc
  3. phosphatidylinositol transporter activity Source: ProtInc

GO - Biological processi

  1. axon guidance Source: Reactome
  2. lipid metabolic process Source: ProtInc
  3. phospholipid transport Source: GOC
  4. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_22228. Role of second messengers in netrin-1 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol transfer protein alpha isoform
Short name:
PI-TP-alpha
Short name:
PtdIns transfer protein alpha
Short name:
PtdInsTP alpha
Gene namesi
Name:PITPNA
Synonyms:PITPN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:9001. PITPNA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33335.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 270269Phosphatidylinositol transfer protein alpha isoformPRO_0000191639Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei215 – 2151N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ00169.
PaxDbiQ00169.
PRIDEiQ00169.

PTM databases

PhosphoSiteiQ00169.

Expressioni

Tissue specificityi

Expressed in a wide range of tissues.

Gene expression databases

BgeeiQ00169.
CleanExiHS_PITPNA.
ExpressionAtlasiQ00169. baseline and differential.
GenevestigatoriQ00169.

Organism-specific databases

HPAiHPA000528.

Interactioni

Protein-protein interaction databases

BioGridi111323. 6 interactions.
IntActiQ00169. 3 interactions.
STRINGi9606.ENSP00000316809.

Structurei

Secondary structure

1
270
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1311
Helixi15 – 3319
Beta strandi38 – 4912
Beta strandi54 – 6512
Helixi70 – 734
Beta strandi81 – 9010
Beta strandi93 – 997
Helixi101 – 1033
Beta strandi106 – 12015
Turni123 – 1264
Helixi130 – 1334
Beta strandi137 – 1415
Helixi146 – 1483
Helixi151 – 1533
Helixi156 – 1583
Helixi160 – 1623
Turni166 – 1683
Helixi177 – 1826
Beta strandi190 – 20011
Turni203 – 2053
Helixi206 – 23025
Helixi232 – 2354
Helixi240 – 26021

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UW5X-ray2.90A/B/C/D1-270[»]
ProteinModelPortaliQ00169.
SMRiQ00169. Positions 1-269.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00169.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG250489.
HOVERGENiHBG058915.
InParanoidiQ00169.
OMAiMVLLKEY.
OrthoDBiEOG7PGDRB.
PhylomeDBiQ00169.
TreeFamiTF313279.

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
InterProiIPR001666. PI_transfer.
IPR023393. START-like_dom.
[Graphical view]
PANTHERiPTHR10658. PTHR10658. 1 hit.
PfamiPF02121. IP_trans. 1 hit.
[Graphical view]
PRINTSiPR00391. PITRANSFER.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00169-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVLLKEYRVI LPVSVDEYQV GQLYSVAEAS KNETGGGEGV EVLVNEPYEK
60 70 80 90 100
DGEKGQYTHK IYHLQSKVPT FVRMLAPEGA LNIHEKAWNA YPYCRTVITN
110 120 130 140 150
EYMKEDFLIK IETWHKPDLG TQENVHKLEP EAWKHVEAVY IDIADRSQVL
160 170 180 190 200
SKDYKAEEDP AKFKSIKTGR GPLGPNWKQE LVNQKDCPYM CAYKLVTVKF
210 220 230 240 250
KWWGLQNKVE NFIHKQERRL FTNFHRQLFC WLDKWVDLTM DDIRRMEEET
260 270
KRQLDEMRQK DPVKGMTADD
Length:270
Mass (Da):31,806
Last modified:January 23, 2007 - v2
Checksum:i4531E6E38697C93B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451N → P in BAA06276. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M73704 mRNA. Translation: AAA36441.1.
D30036 mRNA. Translation: BAA06276.1.
BC082976 mRNA. Translation: AAH82976.1.
BC045108 mRNA. Translation: AAH45108.1.
CCDSiCCDS45563.1.
PIRiI53775.
RefSeqiNP_006215.1. NM_006224.3.
UniGeneiHs.429819.

Genome annotation databases

EnsembliENST00000313486; ENSP00000316809; ENSG00000174238.
GeneIDi5306.
KEGGihsa:5306.
UCSCiuc010cjt.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M73704 mRNA. Translation: AAA36441.1 .
D30036 mRNA. Translation: BAA06276.1 .
BC082976 mRNA. Translation: AAH82976.1 .
BC045108 mRNA. Translation: AAH45108.1 .
CCDSi CCDS45563.1.
PIRi I53775.
RefSeqi NP_006215.1. NM_006224.3.
UniGenei Hs.429819.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UW5 X-ray 2.90 A/B/C/D 1-270 [» ]
ProteinModelPortali Q00169.
SMRi Q00169. Positions 1-269.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111323. 6 interactions.
IntActi Q00169. 3 interactions.
STRINGi 9606.ENSP00000316809.

PTM databases

PhosphoSitei Q00169.

Proteomic databases

MaxQBi Q00169.
PaxDbi Q00169.
PRIDEi Q00169.

Protocols and materials databases

DNASUi 5306.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000313486 ; ENSP00000316809 ; ENSG00000174238 .
GeneIDi 5306.
KEGGi hsa:5306.
UCSCi uc010cjt.3. human.

Organism-specific databases

CTDi 5306.
GeneCardsi GC17M001421.
HGNCi HGNC:9001. PITPNA.
HPAi HPA000528.
MIMi 600174. gene.
neXtProti NX_Q00169.
PharmGKBi PA33335.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG250489.
HOVERGENi HBG058915.
InParanoidi Q00169.
OMAi MVLLKEY.
OrthoDBi EOG7PGDRB.
PhylomeDBi Q00169.
TreeFami TF313279.

Enzyme and pathway databases

Reactomei REACT_22228. Role of second messengers in netrin-1 signaling.

Miscellaneous databases

ChiTaRSi PITPNA. human.
EvolutionaryTracei Q00169.
GeneWikii Phosphatidylinositol_transfer_protein,_alpha.
GenomeRNAii 5306.
NextBioi 20510.
PROi Q00169.
SOURCEi Search...

Gene expression databases

Bgeei Q00169.
CleanExi HS_PITPNA.
ExpressionAtlasi Q00169. baseline and differential.
Genevestigatori Q00169.

Family and domain databases

Gene3Di 3.30.530.20. 1 hit.
InterProi IPR001666. PI_transfer.
IPR023393. START-like_dom.
[Graphical view ]
PANTHERi PTHR10658. PTHR10658. 1 hit.
Pfami PF02121. IP_trans. 1 hit.
[Graphical view ]
PRINTSi PR00391. PITRANSFER.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  5. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. 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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH PHOSPHATIDYLINOSITOL.

Entry informationi

Entry nameiPIPNA_HUMAN
AccessioniPrimary (citable) accession number: Q00169
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3