P53810 (PIPNA_MOUSE) 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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	271 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.
Involvement in disease	Note=Defects in Pitpna are the cause of the vibrator phenotype which is characterized by early-onset progressive action tremor, degeneration of brain stem and spinal cord neurons, and juvenile death. The mutation is due to the insertion of an intracisternal A particle retrotransposon in intron 4 which results in a 5-fold reduction in protein levels. Ref.2
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)
Cellular component	cytosol Traceable author statement. Source: Reactome
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 – 271

270

Phosphatidylinositol transfer protein alpha isoform

PRO_0000191640

Sites

Binding site

59

1

Phosphatidylinositol lipid headgroup By similarity

Binding site

61

1

Phosphatidylinositol lipid headgroup By similarity

Binding site

86

1

Phosphatidylinositol lipid headgroup By similarity

Binding site

90

1

Phosphatidylinositol lipid headgroup By similarity

Binding site

97

1

Phosphatidylinositol lipid headgroup By similarity

Binding site

195

1

Phosphatidylinositol lipid headgroup By similarity

Amino acid modifications

Modified residue

58

1

Phosphotyrosine By similarity

Modified residue

216

1

N6-acetyllysine By similarity

Secondary structure

1

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271

Helix Strand Turn

Details...

Beta strand

3 – 13

11

Helix

15 – 30

16

Turn

36 – 39

4

Beta strand

40 – 49

10

Beta strand

55 – 64

10

Helix

66 – 68

3

Helix

71 – 74

4

Turn

79 – 82

4

Beta strand

83 – 91

9

Beta strand

94 – 101

8

Turn

102 – 104

3

Helix

105 – 107

3

Beta strand

108 – 121

14

Helix

131 – 134

4

Beta strand

138 – 142

5

Helix

147 – 149

3

Helix

152 – 154

3

Helix

157 – 159

3

Turn

161 – 163

3

Turn

167 – 169

3

Helix

178 – 182

5

Beta strand

191 – 201

11

Helix

207 – 231

25

Helix

233 – 236

4

Helix

241 – 253

13

Sequences

	Sequence		Length	Mass (Da)
	P53810 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E9561EE5BBBADC3A	FASTA	271	31,893
	10 20 30 40 50 60 MVLLKEYRVI LPVSVDEYQV GQLYSVAEAS KNETGGGEGV EVLVNEPYEK DDGEKGQYTH 70 80 90 100 110 120 KIYHLQSKVP TFVRMLAPEG ALNIHEKAWN AYPYCRTVIT NEYMKEDFLI KIETWHKPDL 130 140 150 160 170 180 GTQENVHKLE PEAWKHVEAI YIDIADRSQV LSKDYKAEED PAKFKSVKTG RGPLGPNWKQ 190 200 210 220 230 240 ELVNQKDCPY MCAYKLVTVK FKWWGLQNKV ENFIHKQEKR LFTNFHRQLF CWLDKWVDLT 250 260 270 MDDIRRMEEE TKRQLDEMRQ KDPVKGMTAD D

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of mouse phosphatidylinositol transfer protein expressed in Escherichia coli." Geijtenbeek T.B.H., de Groot E., van Baal J., Brunink F., Westerman J., Snoek G.T., Wirtz K.W. Biochim. Biophys. Acta 1213:309-318(1994) [PubMed: 8049244] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Swiss.
[2]	"The vibrator mutation causes neurodegeneration via reduced expression of PITP alpha: positional complementation cloning and extragenic suppression." Hamilton B.A., Smith D.J., Mueller K.L., Kerrebrock A.W., Bronson R.T., van Berkel V., Daly M.J., Kruglyak L., Reeve M.P., Nemhauser J.L., Hawkins T.L., Rubin E.M., Lander E.S. Neuron 18:711-722(1997) [PubMed: 9182797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DISEASE. Strain: DBA/2J. 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]. Strain: C57BL/6. Tissue: Brain.
[4]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 9-50; 88-96; 112-128 AND 136-147, MASS SPECTROMETRY. Tissue: Hippocampus.
[5]	"Structure of apo-phosphatidylinositol transfer protein alpha provides insight into membrane association." Schouten A., Agianian B., Westerman J., Kroon J., Wirtz K.W., Gros P. EMBO J. 21:2117-2121(2002) [PubMed: 11980708] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S72681 mRNA. Translation: AAC60690.1.
U96725 mRNA. Translation: AAC53266.1.
U96726 Genomic DNA. Translation: AAC60756.1.
BC056171 mRNA. Translation: AAH56171.1.

IPI

IPI00230003.

RefSeq

NP_032876.1. NM_008850.1.

UniGene

Mm.3128.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KCM	X-ray	2.00	A	2-271	[»]

ProteinModelPortal

P53810.

SMR

P53810. Positions 2-257.

ModBase

Search...

Protein-protein interaction databases

STRING

P53810.

PTM databases

PhosphoSite

P53810.

2D gel databases

REPRODUCTION-2DPAGE

P53810.

Proteomic databases

PRIDE

P53810.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000143219; ENSMUSP00000115723; ENSMUSG00000017781.

GeneID

18738.

KEGG

mmu:18738.

Organism-specific databases

CTD

5306.

MGI

MGI:99887. Pitpna.

Phylogenomic databases

eggNOG

roNOG09025.

GeneTree

ENSGT00550000074351.

HOVERGEN

HBG058915.

InParanoid

P53810.

OMA

KLEPEAW.

Enzyme and pathway databases

Reactome

REACT_115492. Developmental Biology.

Gene expression databases

ArrayExpress

P53810.

Bgee

P53810.

CleanEx

MM_PITPNA.

Genevestigator

P53810.

GermOnline

ENSMUSG00000017781. Mus musculus.

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

294873.

SOURCE

Search...

Entry information

Entry name

PIPNA_MOUSE

Accession

Primary (citable) accession number: P53810

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program