PIPNA_BOVIN
ID PIPNA_BOVIN Reviewed; 270 AA.
AC Q2HJ54; Q9TR37;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Phosphatidylinositol transfer protein alpha isoform;
DE Short=PI-TP-alpha;
DE Short=PtdIns transfer protein alpha;
DE Short=PtdInsTP alpha;
DE AltName: Full=Phosphatidylinositol-transfer protein 35 kDa isoform;
DE Short=PI-TP 35 kda isoform;
GN Name=PITPNA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-22, FUNCTION, AND CATALYTIC ACTIVITY.
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).
CC -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol (PI) and
CC phosphatidylcholine (PC) between membranes (PubMed:7654206). 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:7654206}.
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:7654206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572;
CC Evidence={ECO:0000305|PubMed:7654206};
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:7654206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000305|PubMed:7654206};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53810}. Nucleus
CC {ECO:0000250|UniProtKB:P53810}.
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; BC113306; AAI13307.1; -; mRNA.
DR PIR; A48214; A48214.
DR PIR; S58431; S58431.
DR RefSeq; NP_001040047.1; NM_001046582.1.
DR AlphaFoldDB; Q2HJ54; -.
DR SMR; Q2HJ54; -.
DR STRING; 9913.ENSBTAP00000043732; -.
DR SwissLipids; SLP:000000988; -.
DR PaxDb; Q2HJ54; -.
DR PRIDE; Q2HJ54; -.
DR Ensembl; ENSBTAT00000046430; ENSBTAP00000043732; ENSBTAG00000011480.
DR GeneID; 616550; -.
DR KEGG; bta:616550; -.
DR CTD; 5306; -.
DR VEuPathDB; HostDB:ENSBTAG00000011480; -.
DR VGNC; VGNC:32919; PITPNA.
DR eggNOG; KOG3668; Eukaryota.
DR GeneTree; ENSGT00940000157119; -.
DR HOGENOM; CLU_046509_0_0_1; -.
DR InParanoid; Q2HJ54; -.
DR OMA; VQPVMTC; -.
DR OrthoDB; 951268at2759; -.
DR TreeFam; TF313279; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000011480; Expressed in corpus epididymis and 106 other tissues.
DR ExpressionAtlas; Q2HJ54; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; IDA:UniProtKB.
DR GO; GO:0008525; F:phosphatidylcholine transporter activity; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; 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 Acetylation; Cytoplasm; Direct protein sequencing; Lipid transport;
KW Lipid-binding; Nucleus; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7654206"
FT CHAIN 2..270
FT /note="Phosphatidylinositol transfer protein alpha isoform"
FT /id="PRO_0000269200"
FT BINDING 58
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 60
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 85
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 89
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 96
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 194
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 215
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00169"
SQ SEQUENCE 270 AA; 31849 MW; FFE53A8F4D9F87CD CRC64;
MVLLKEYRVI LPVSVEEYQV GQLYSVAEAS KNETGGGEGV EVLVNEPYEK DGEKGQYTHK
IYHLQSKVPT FVRMLAPEGA LNIHEKAWNA YPYCRTVITN EYMKEDFLIK IETWHKPDLG
TLENVHKLEP EAWKHVEVIY IDIADRSQVL SKDYKAEEDP AKYKSIKTGR GPLGPNWKQE
LVNQKDCPYM CAYKLVTVKF KWWGLQNKVE NFIHKQERRL FTNFHRQLFC WLDKWVDLTM
DDIRRMEDET KRQLDEMRQK DPVKGMTADD
