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 16-OCT-2019, entry version 83. 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; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; 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. RC TISSUE=Brain; RX PubMed=7654206; DOI=10.1042/bj3100643; RA de Vries K.J., Heinrichs A.A., Cunningham E., Brunink F., RA Westerman J., 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 PtdIns and phosphatidylcholine CC between membranes. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI CC transfer 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 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 VGNC; VGNC:32919; PITPNA. DR eggNOG; KOG3668; Eukaryota. DR eggNOG; COG5083; LUCA. DR GeneTree; ENSGT00940000157119; -. DR HOGENOM; HOG000006717; -. DR InParanoid; Q2HJ54; -. DR OMA; EPDVWKN; -. DR OrthoDB; 951268at2759; -. DR TreeFam; TF313279; -. DR Proteomes; UP000009136; Chromosome 19. DR Bgee; ENSBTAG00000011480; Expressed in 10 organ(s), highest expression level in brain. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central. 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; IBA:GO_Central. 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; Complete proteome; Cytoplasm; Direct protein sequencing; KW Lipid-binding; Reference proteome; Transport. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7654206}. FT CHAIN 2 270 Phosphatidylinositol transfer protein FT alpha isoform. FT /FTId=PRO_0000269200. FT BINDING 58 58 Phosphatidylinositol lipid headgroup. FT {ECO:0000250}. FT BINDING 60 60 Phosphatidylinositol lipid headgroup. FT {ECO:0000250}. FT BINDING 85 85 Phosphatidylinositol lipid headgroup. FT {ECO:0000250}. FT BINDING 89 89 Phosphatidylinositol lipid headgroup. FT {ECO:0000250}. FT BINDING 96 96 Phosphatidylinositol lipid headgroup. FT {ECO:0000250}. FT BINDING 194 194 Phosphatidylinositol lipid headgroup. FT {ECO:0000250}. FT MOD_RES 215 215 N6-acetyllysine. FT {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 //