ID PIPNA_HUMAN Reviewed; 270 AA. AC Q00169; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 25-JAN-2012, entry version 110. 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Testis; RX MEDLINE=94252585; PubMed=8194769; DOI=10.1016/0378-1119(94)90279-8; RA Dickeson S.K., Helmkamp G.M. Jr., Yarbrough L.R.; RT "Sequence of a human cDNA encoding phosphatidylinositol transfer RT protein and occurrence of a related sequence in widely divergent RT eukaryotes."; RL Gene 142:301-305(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RA Tanaka S., Yamashita S., Hosaka K.; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Ovary; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 135-146, AND MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-57, AND MASS RP SPECTROMETRY. RC TISSUE=Lung carcinoma; RX PubMed=18083107; DOI=10.1016/j.cell.2007.11.025; RA Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., RA Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., RA Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., RA Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., RA Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; RT "Global survey of phosphotyrosine signaling identifies oncogenic RT kinases in lung cancer."; RL Cell 131:1190-1203(2007). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH RP PHOSPHATIDYLINOSITOL. RX PubMed=14962392; DOI=10.1016/S0969-2126(04)00025-5; RA Tilley S.J., Skippen A., Murray-Rust J., Swigart P.M., Stewart A., RA Morgan C.P., Cockcroft S., McDonald N.Q.; RT "Structure-function analysis of human phosphatidylinositol transfer RT protein alpha bound to phosphatidylinositol."; RL Structure 12:317-326(2004). CC -!- FUNCTION: Catalyzes the transfer of PtdIns and phosphatidylcholine CC between membranes. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed in a wide range of tissues. CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI CC transfer class I subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M73704; AAA36441.1; -; mRNA. DR EMBL; D30036; BAA06276.1; -; mRNA. DR EMBL; BC082976; AAH82976.1; -; mRNA. DR EMBL; BC045108; AAH45108.1; -; mRNA. DR IPI; IPI00216048; -. DR PIR; I53775; I53775. DR RefSeq; NP_006215.1; NM_006224.3. DR UniGene; Hs.429819; -. DR PDB; 1UW5; X-ray; 2.90 A; A/B/C/D=1-270. DR PDBsum; 1UW5; -. DR ProteinModelPortal; Q00169; -. DR SMR; Q00169; 1-269. DR IntAct; Q00169; 2. DR STRING; Q00169; -. DR PhosphoSite; Q00169; -. DR DMDM; 130770; -. DR PRIDE; Q00169; -. DR Ensembl; ENST00000313486; ENSP00000316809; ENSG00000174238. DR GeneID; 5306; -. DR KEGG; hsa:5306; -. DR CTD; 5306; -. DR GeneCards; GC17M001368; -. DR H-InvDB; HIX0202467; -. DR HGNC; HGNC:9001; PITPNA. DR HPA; HPA000528; -. DR MIM; 600174; gene. DR neXtProt; NX_Q00169; -. DR PharmGKB; PA33335; -. DR eggNOG; prNOG05057; -. DR HOVERGEN; HBG058915; -. DR InParanoid; Q00169; -. DR OMA; KLEPEAW; -. DR OrthoDB; EOG42JNS2; -. DR PhylomeDB; Q00169; -. DR Reactome; REACT_111045; Developmental Biology. DR NextBio; 20510; -. DR ArrayExpress; Q00169; -. DR Bgee; Q00169; -. DR CleanEx; HS_PITPNA; -. DR Genevestigator; Q00169; -. DR GermOnline; ENSG00000174238; Homo sapiens. DR GO; GO:0008525; F:phosphatidylcholine transporter activity; TAS:ProtInc. DR GO; GO:0008526; F:phosphatidylinositol transporter activity; TAS:ProtInc. DR GO; GO:0007411; P:axon guidance; TAS:Reactome. DR GO; GO:0006629; P:lipid metabolic process; NAS:ProtInc. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR InterPro; IPR001666; PI_transfer. DR InterPro; IPR023393; START-like_dom. DR Gene3D; G3DSA:3.30.530.20; G3DSA:3.30.530.20; 1. DR PANTHER; PTHR10658; PI_transfer; 1. DR Pfam; PF02121; IP_trans; 1. DR PRINTS; PR00391; PITRANSFER. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; KW Direct protein sequencing; Lipid-binding; Phosphoprotein; KW Reference proteome; Transport. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 270 Phosphatidylinositol transfer protein FT alpha isoform. FT /FTId=PRO_0000191639. FT BINDING 58 58 Phosphatidylinositol lipid headgroup. FT BINDING 60 60 Phosphatidylinositol lipid headgroup. FT BINDING 85 85 Phosphatidylinositol lipid headgroup. FT BINDING 89 89 Phosphatidylinositol lipid headgroup. FT BINDING 96 96 Phosphatidylinositol lipid headgroup. FT BINDING 194 194 Phosphatidylinositol lipid headgroup. FT MOD_RES 57 57 Phosphotyrosine. FT MOD_RES 215 215 N6-acetyllysine. FT CONFLICT 45 45 N -> P (in Ref. 2; BAA06276). FT STRAND 3 13 FT HELIX 15 33 FT STRAND 38 49 FT STRAND 54 65 FT HELIX 70 73 FT STRAND 81 90 FT STRAND 93 99 FT HELIX 101 103 FT STRAND 106 120 FT TURN 123 126 FT HELIX 130 133 FT STRAND 137 141 FT HELIX 146 148 FT HELIX 151 153 FT HELIX 156 158 FT HELIX 160 162 FT TURN 166 168 FT HELIX 177 182 FT STRAND 190 200 FT TURN 203 205 FT HELIX 206 230 FT HELIX 232 235 FT HELIX 240 260 SQ SEQUENCE 270 AA; 31806 MW; 4531E6E38697C93B CRC64; MVLLKEYRVI LPVSVDEYQV GQLYSVAEAS KNETGGGEGV EVLVNEPYEK DGEKGQYTHK IYHLQSKVPT FVRMLAPEGA LNIHEKAWNA YPYCRTVITN EYMKEDFLIK IETWHKPDLG TQENVHKLEP EAWKHVEAVY IDIADRSQVL SKDYKAEEDP AKFKSIKTGR GPLGPNWKQE LVNQKDCPYM CAYKLVTVKF KWWGLQNKVE NFIHKQERRL FTNFHRQLFC WLDKWVDLTM DDIRRMEEET KRQLDEMRQK DPVKGMTADD //