PIPNA_MOUSE
ID PIPNA_MOUSE Reviewed; 271 AA.
AC P53810;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Phosphatidylinositol transfer protein alpha isoform;
DE Short=PI-TP-alpha;
DE Short=PtdIns transfer protein alpha;
DE Short=PtdInsTP alpha;
GN Name=Pitpna; Synonyms=Pitpn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-25, FUNCTION, CATALYTIC
RP ACTIVITY, AND PHOSPHORYLATION.
RC STRAIN=SWR/J;
RX PubMed=8049244; DOI=10.1016/0005-2760(94)00063-8;
RA Geijtenbeek T.B.H., de Groot E., van Baal J., Brunink F., Westerman J.,
RA Snoek G.T., Wirtz K.W.;
RT "Characterization of mouse phosphatidylinositol transfer protein expressed
RT in Escherichia coli.";
RL Biochim. Biophys. Acta 1213:309-318(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND DISEASE.
RC STRAIN=DBA/2J; TISSUE=Brain;
RX PubMed=9182797; DOI=10.1016/s0896-6273(00)80312-8;
RA Hamilton B.A., Smith D.J., Mueller K.L., Kerrebrock A.W., Bronson R.T.,
RA van Berkel V., Daly M.J., Kruglyak L., Reeve M.P., Nemhauser J.L.,
RA Hawkins T.L., Rubin E.M., Lander E.S.;
RT "The vibrator mutation causes neurodegeneration via reduced expression of
RT PITP alpha: positional complementation cloning and extragenic
RT suppression.";
RL Neuron 18:711-722(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP PROTEIN SEQUENCE OF 9-50; 88-96; 112-128 AND 136-147, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=7654206; DOI=10.1042/bj3100643;
RA de Vries K.J., Heinrichs A.A., Cunningham E., Brunink F., Westerman J.,
RA Somerharju P.J., Cockcroft S., Wirtz K.W., Snoek G.T.;
RT "An isoform of the phosphatidylinositol-transfer protein transfers
RT sphingomyelin and is associated with the Golgi system.";
RL Biochem. J. 310:643-649(1995).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=11980708; DOI=10.1093/emboj/21.9.2117;
RA Schouten A., Agianian B., Westerman J., Kroon J., Wirtz K.W., Gros P.;
RT "Structure of apo-phosphatidylinositol transfer protein alpha provides
RT insight into membrane association.";
RL EMBO J. 21:2117-2121(2002).
CC -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol (PI) and
CC phosphatidylcholine (PC) between membranes (PubMed:8049244). Shows a
CC preference for PI and PC containing shorter saturated or monosaturated
CC acyl chains at the sn-1 and sn-2 positions (By similarity). Preference
CC order for PC is C16:1 > C16:0 > C18:1 > C18:0 > C20:4 and for PI is
CC C16:1 > C16:0 > C18:1 > C18:0 > C20:4 > C20:3 (By similarity).
CC {ECO:0000250|UniProtKB:Q00169, ECO:0000269|PubMed:8049244}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:8049244};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572;
CC Evidence={ECO:0000305|PubMed:8049244};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out);
CC Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880;
CC Evidence={ECO:0000269|PubMed:8049244};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000305|PubMed:8049244};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7654206}. Nucleus
CC {ECO:0000269|PubMed:7654206}.
CC -!- PTM: Phosphorylated by PKC in a calcium and phosphatidylserine-
CC dependent manner. {ECO:0000269|PubMed:8049244}.
CC -!- DISEASE: Note=Defects in Pitpna are the cause of the vibrator phenotype
CC which is characterized by early-onset progressive action tremor,
CC degeneration of brain stem and spinal cord neurons, and juvenile death.
CC The mutation is due to the insertion of an intracisternal A particle
CC retrotransposon in intron 4 which results in a 5-fold reduction in
CC protein levels. {ECO:0000269|PubMed:9182797}.
CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI transfer
CC class I subfamily. {ECO:0000305}.
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DR EMBL; S72681; AAC60690.1; -; mRNA.
DR EMBL; U96725; AAC53266.1; -; mRNA.
DR EMBL; U96726; AAC60756.1; -; Genomic_DNA.
DR EMBL; BC056171; AAH56171.1; -; mRNA.
DR CCDS; CCDS25052.1; -.
DR RefSeq; NP_032876.1; NM_008850.2.
DR PDB; 1KCM; X-ray; 2.00 A; A=2-271.
DR PDBsum; 1KCM; -.
DR AlphaFoldDB; P53810; -.
DR SMR; P53810; -.
DR BioGRID; 202184; 5.
DR STRING; 10090.ENSMUSP00000115723; -.
DR iPTMnet; P53810; -.
DR PhosphoSitePlus; P53810; -.
DR REPRODUCTION-2DPAGE; P53810; -.
DR EPD; P53810; -.
DR jPOST; P53810; -.
DR PaxDb; P53810; -.
DR PeptideAtlas; P53810; -.
DR PRIDE; P53810; -.
DR ProteomicsDB; 289578; -.
DR Antibodypedia; 5311; 193 antibodies from 33 providers.
DR DNASU; 18738; -.
DR Ensembl; ENSMUST00000143219; ENSMUSP00000115723; ENSMUSG00000017781.
DR GeneID; 18738; -.
DR KEGG; mmu:18738; -.
DR UCSC; uc007kei.1; mouse.
DR CTD; 5306; -.
DR MGI; MGI:99887; Pitpna.
DR VEuPathDB; HostDB:ENSMUSG00000017781; -.
DR eggNOG; KOG3668; Eukaryota.
DR GeneTree; ENSGT00940000157119; -.
DR HOGENOM; CLU_046509_0_0_1; -.
DR InParanoid; P53810; -.
DR OrthoDB; 951268at2759; -.
DR PhylomeDB; P53810; -.
DR TreeFam; TF313279; -.
DR BioGRID-ORCS; 18738; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Pitpna; mouse.
DR EvolutionaryTrace; P53810; -.
DR PRO; PR:P53810; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P53810; protein.
DR Bgee; ENSMUSG00000017781; Expressed in small intestine Peyer's patch and 262 other tissues.
DR ExpressionAtlas; P53810; baseline and differential.
DR Genevisible; P53810; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; ISS:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:UniProtKB.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; IDA:UniProtKB.
DR GO; GO:0008525; F:phosphatidylcholine transporter activity; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0070540; F:stearic acid binding; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:BHF-UCL.
DR GO; GO:0015914; P:phospholipid transport; ISO:MGI.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR001666; PI_transfer.
DR InterPro; IPR023393; START-like_dom_sf.
DR PANTHER; PTHR10658; PTHR10658; 1.
DR Pfam; PF02121; IP_trans; 1.
DR PRINTS; PR00391; PITRANSFER.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Lipid transport; Lipid-binding; Nucleus; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7654206"
FT CHAIN 2..271
FT /note="Phosphatidylinositol transfer protein alpha isoform"
FT /id="PRO_0000191640"
FT REGION 251..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q00169"
FT BINDING 61
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q00169"
FT BINDING 86
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q00169"
FT BINDING 90
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q00169"
FT BINDING 97
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q00169"
FT BINDING 195
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q00169"
FT MOD_RES 216
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00169"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:1KCM"
FT HELIX 15..30
FT /evidence="ECO:0007829|PDB:1KCM"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:1KCM"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:1KCM"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:1KCM"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1KCM"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:1KCM"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:1KCM"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:1KCM"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:1KCM"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1KCM"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1KCM"
FT STRAND 108..121
FT /evidence="ECO:0007829|PDB:1KCM"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:1KCM"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1KCM"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1KCM"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:1KCM"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1KCM"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1KCM"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1KCM"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:1KCM"
FT STRAND 191..201
FT /evidence="ECO:0007829|PDB:1KCM"
FT HELIX 207..231
FT /evidence="ECO:0007829|PDB:1KCM"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:1KCM"
FT HELIX 241..253
FT /evidence="ECO:0007829|PDB:1KCM"
SQ SEQUENCE 271 AA; 31893 MW; E9561EE5BBBADC3A CRC64;
MVLLKEYRVI LPVSVDEYQV GQLYSVAEAS KNETGGGEGV EVLVNEPYEK DDGEKGQYTH
KIYHLQSKVP TFVRMLAPEG ALNIHEKAWN AYPYCRTVIT NEYMKEDFLI KIETWHKPDL
GTQENVHKLE PEAWKHVEAI YIDIADRSQV LSKDYKAEED PAKFKSVKTG RGPLGPNWKQ
ELVNQKDCPY MCAYKLVTVK FKWWGLQNKV ENFIHKQEKR LFTNFHRQLF CWLDKWVDLT
MDDIRRMEEE TKRQLDEMRQ KDPVKGMTAD D
