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 29-MAY-2024, entry version 99. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSBTAP00000074228; -. DR SwissLipids; SLP:000000988; -. DR PaxDb; 9913-ENSBTAP00000043732; -. DR Ensembl; ENSBTAT00000116103.1; ENSBTAP00000082114.1; ENSBTAG00000011480.7. 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; QHNVHEL; -. DR OrthoDB; 3946034at2759; -. DR TreeFam; TF313279; -. DR Proteomes; UP000009136; Chromosome 19. DR Bgee; ENSBTAG00000011480; Expressed in corpus epididymis and 106 other cell types or 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 CDD; cd08888; SRPBCC_PITPNA-B_like; 1. DR Gene3D; 3.30.530.20; -; 1. DR InterPro; IPR001666; PI_transfer. DR InterPro; IPR023393; START-like_dom_sf. DR PANTHER; PTHR10658; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN; 1. DR PANTHER; PTHR10658:SF28; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN ALPHA ISOFORM; 1. DR Pfam; PF02121; IP_trans; 1. DR PRINTS; PR00391; PITRANSFER. DR SUPFAM; SSF55961; Bet v1-like; 1. 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 //