PIPNA_RAT
ID PIPNA_RAT Reviewed; 271 AA.
AC P16446;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=2777797; DOI=10.1016/s0021-9258(19)84743-9;
RA Dickeson S.K., Lim C.N., Schuyler G.T., Dalton T.P., Helmkamp G.M. Jr.,
RA Yarbrough L.R.;
RT "Isolation and sequence of cDNA clones encoding rat phosphatidylinositol
RT transfer protein.";
RL J. Biol. Chem. 264:16557-16564(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [3]
RP PROTEIN SEQUENCE OF 2-21.
RC TISSUE=Lung;
RX PubMed=3606604; DOI=10.1016/0006-291x(87)91580-4;
RA Funkhouser J.D.;
RT "Amino-terminal sequence of a phospholipid transfer protein from rat
RT lung.";
RL Biochem. Biophys. Res. Commun. 145:1310-1314(1987).
RN [4]
RP PROTEIN SEQUENCE OF 9-31; 88-96; 136-147 AND 235-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L., Shim K.;
RL Submitted (DEC-2006) to UniProtKB.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-25; THR-59; HIS-60;
RP PRO-78; THR-198 AND GLU-248.
RX PubMed=7568025; DOI=10.1073/pnas.92.19.8826;
RA Alb J.G. Jr., Gedvilaite A., Cartee R.T., Skinner H.B., Bankaitis V.A.;
RT "Mutant rat phosphatidylinositol/phosphatidylcholine transfer proteins
RT specifically defective in phosphatidylinositol transfer: implications for
RT the regulation of phospholipid transfer activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8826-8830(1995).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=18636990; DOI=10.1111/j.1600-0854.2008.00794.x;
RA Shadan S., Holic R., Carvou N., Ee P., Li M., Murray-Rust J., Cockcroft S.;
RT "Dynamics of lipid transfer by phosphatidylinositol transfer proteins in
RT cells.";
RL Traffic 9:1743-1756(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=11104777; DOI=10.1074/jbc.m010131200;
RA Yoder M.D., Thomas L.M., Tremblay J.M., Oliver R.L., Yarbrough L.R.,
RA Helmkamp G.M. Jr.;
RT "Structure of a multifunctional protein. Mammalian phosphatidylinositol
RT transfer protein complexed with phosphatidylcholine.";
RL J. Biol. Chem. 276:9246-9252(2001).
CC -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol (PI) and
CC phosphatidylcholine (PC) between membranes (PubMed:7568025,
CC PubMed:18636990). Shows a preference for PI and PC containing shorter
CC saturated or monosaturated acyl chains at the sn-1 and sn-2 positions
CC (By similarity). Preference order for PC is C16:1 > C16:0 > C18:1 >
CC C18:0 > C20:4 and for PI is C16:1 > C16:0 > C18:1 > C18:0 > C20:4 >
CC C20:3 (By similarity). {ECO:0000250|UniProtKB:Q00169,
CC ECO:0000269|PubMed:18636990, ECO:0000269|PubMed:7568025}.
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:7568025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572;
CC Evidence={ECO:0000305|PubMed:7568025};
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:18636990, ECO:0000269|PubMed:7568025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000305|PubMed:7568025};
CC -!- ACTIVITY REGULATION: Phosphatidylinositol transfer activity is
CC inhibited by N-ethylmaleimide. {ECO:0000269|PubMed:18636990}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53810}. Nucleus
CC {ECO:0000250|UniProtKB:P53810}.
CC -!- TISSUE SPECIFICITY: Expressed in a wide range of tissues.
CC {ECO:0000269|PubMed:2777797}.
CC -!- PTM: Phosphorylated by PKC in a calcium and phosphatidylserine-
CC dependent manner. {ECO:0000250|UniProtKB:P53810}.
CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI transfer
CC class I subfamily. {ECO:0000305}.
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DR EMBL; M25758; AAA41984.1; -; mRNA.
DR EMBL; BC070945; AAH70945.1; -; mRNA.
DR PIR; A34391; A34391.
DR RefSeq; NP_058927.1; NM_017231.1.
DR PDB; 1T27; X-ray; 2.20 A; A=1-271.
DR PDBsum; 1T27; -.
DR AlphaFoldDB; P16446; -.
DR SMR; P16446; -.
DR BioGRID; 248161; 1.
DR STRING; 10116.ENSRNOP00000005368; -.
DR iPTMnet; P16446; -.
DR PhosphoSitePlus; P16446; -.
DR SwissPalm; P16446; -.
DR World-2DPAGE; 0004:P16446; -.
DR jPOST; P16446; -.
DR PaxDb; P16446; -.
DR PRIDE; P16446; -.
DR Ensembl; ENSRNOT00000005368; ENSRNOP00000005368; ENSRNOG00000003846.
DR GeneID; 29525; -.
DR KEGG; rno:29525; -.
DR CTD; 5306; -.
DR RGD; 61885; Pitpna.
DR eggNOG; KOG3668; Eukaryota.
DR HOGENOM; CLU_046509_0_0_1; -.
DR InParanoid; P16446; -.
DR OrthoDB; 951268at2759; -.
DR PhylomeDB; P16446; -.
DR TreeFam; TF313279; -.
DR EvolutionaryTrace; P16446; -.
DR PRO; PR:P16446; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003846; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; P16446; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:UniProtKB.
DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:BHF-UCL.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; IMP:UniProtKB.
DR GO; GO:0008525; F:phosphatidylcholine transporter activity; IDA:BHF-UCL.
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; IDA:MGI.
DR GO; GO:0070540; F:stearic acid binding; IDA:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0015914; P:phospholipid transport; IDA:UniProtKB.
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:3606604"
FT CHAIN 2..271
FT /note="Phosphatidylinositol transfer protein alpha isoform"
FT /id="PRO_0000191642"
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:0000305|PubMed:7568025"
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 MUTAGEN 25
FT /note="S->F: Loss of phosphatidylinositol transfer activity
FT but no significant effect on phosphatidylcholine transfer
FT activity."
FT /evidence="ECO:0000269|PubMed:7568025"
FT MUTAGEN 59
FT /note="T->A: Reduced phosphatidylinositol and
FT phosphatidylcholine transfer activity."
FT /evidence="ECO:0000269|PubMed:7568025"
FT MUTAGEN 59
FT /note="T->S,Q,V,I,N,D,E: Loss of phosphatidylinositol
FT transfer activity but no significant effect on
FT phosphatidylcholine transfer activity."
FT /evidence="ECO:0000269|PubMed:7568025"
FT MUTAGEN 60
FT /note="H->Q: No significant effect on phosphatidylinositol
FT and phosphatidylcholine transfer activity."
FT /evidence="ECO:0000269|PubMed:7568025"
FT MUTAGEN 78
FT /note="P->L: Loss of phosphatidylinositol transfer activity
FT but no significant effect on phosphatidylcholine transfer
FT activity."
FT /evidence="ECO:0000269|PubMed:7568025"
FT MUTAGEN 198
FT /note="T->I: No significant effect on phosphatidylinositol
FT and phosphatidylcholine transfer activity."
FT /evidence="ECO:0000269|PubMed:7568025"
FT MUTAGEN 248
FT /note="E->K: Loss of phosphatidylinositol transfer activity
FT but no significant effect on phosphatidylcholine transfer
FT activity."
FT /evidence="ECO:0000269|PubMed:7568025"
FT CONFLICT 14
FT /note="S -> H (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:1T27"
FT HELIX 15..32
FT /evidence="ECO:0007829|PDB:1T27"
FT STRAND 38..49
FT /evidence="ECO:0007829|PDB:1T27"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:1T27"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:1T27"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:1T27"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:1T27"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:1T27"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1T27"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1T27"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1T27"
FT STRAND 108..119
FT /evidence="ECO:0007829|PDB:1T27"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:1T27"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:1T27"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1T27"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1T27"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1T27"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1T27"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1T27"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1T27"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:1T27"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1T27"
FT STRAND 191..201
FT /evidence="ECO:0007829|PDB:1T27"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1T27"
FT HELIX 207..231
FT /evidence="ECO:0007829|PDB:1T27"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:1T27"
FT HELIX 241..260
FT /evidence="ECO:0007829|PDB:1T27"
SQ SEQUENCE 271 AA; 31907 MW; F06794CD1930EDA9 CRC64;
MVLLKEYRVI LPVSVDEYQV GQLYSVAEAS KNETGGGEGV EVLVNEPYEK DDGEKGQYTH
KIYHLQSKVP TFVRMLAPEG ALNIHEKAWN AYPYCRTVIT NEYMKEDFLI KIETWHKPDL
GTQENVHKLE PEAWKHVEAI YIDIADRSQV LSKDYKAEED PAKFKSIKTG RGPLGPNWKQ
ELVNQKDCPY MCAYKLVTVK FKWWGLQNKV ENFIHKQEKR LFTNFHRQLF CWLDKWVDLT
MDDIRRMEEE TKRQLDEMRQ KDPVKGMTAD D
