ID PIPNB_HUMAN Reviewed; 271 AA. AC P48739; B3KYB8; B7Z7Q0; Q8N5W1; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 190. DE RecName: Full=Phosphatidylinositol transfer protein beta isoform; DE Short=PI-TP-beta; DE Short=PtdIns transfer protein beta; DE Short=PtdInsTP beta; GN Name=PITPNB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=8541325; DOI=10.1016/0005-2760(95)00192-1; RA Tanaka S., Yamashita S., Hosaka K.; RT "Cloning and expression of human cDNA encoding phosphatidylinositol RT transfer protein beta."; RL Biochim. Biophys. Acta 1259:199-202(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Lymph, and Skin; 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 [7] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=10531358; DOI=10.1074/jbc.274.44.31553; RA Fullwood Y., dos Santos M., Hsuan J.J.; RT "Cloning and characterization of a novel human phosphatidylinositol RT transfer protein, rdgBbeta."; RL J. Biol. Chem. 274:31553-31558(1999). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF RP CYS-94; CYS-187 AND 202-TRP-TRP-203. 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 [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., 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 [10] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-60; ASN-89; CYS-94 AND RP 202-TRP-TRP-203. RX PubMed=20332109; DOI=10.1242/jcs.061986; RA Carvou N., Holic R., Li M., Futter C., Skippen A., Cockcroft S.; RT "Phosphatidylinositol- and phosphatidylcholine-transfer activity of RT PITPbeta is essential for COPI-mediated retrograde transport from the Golgi RT to the endoplasmic reticulum."; RL J. Cell Sci. 123:1262-1273(2010). RN [11] 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., Buerckstuemmer T., RA 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol and CC phosphatidylcholine between membranes (PubMed:10531358, CC PubMed:18636990, PubMed:20332109). Also catalyzes the transfer of CC sphingomyelin (By similarity). Required for COPI-mediated retrograde CC transport from the Golgi to the endoplasmic reticulum; CC phosphatidylinositol and phosphatidylcholine transfer activity is CC essential for this function (PubMed:20332109). CC {ECO:0000250|UniProtKB:Q9TR36, ECO:0000269|PubMed:10531358, CC ECO:0000269|PubMed:18636990, ECO:0000269|PubMed:20332109}. 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:18636990, CC ECO:0000269|PubMed:20332109}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572; CC Evidence={ECO:0000305|PubMed:20332109}; 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:10531358, ECO:0000269|PubMed:18636990, CC ECO:0000269|PubMed:20332109}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692; CC Evidence={ECO:0000305|PubMed:10531358}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-(acyl)-sphingosylphosphocholine(in) = an N-(acyl)- CC sphingosylphosphocholine(out); Xref=Rhea:RHEA:43776, CC ChEBI:CHEBI:64583; Evidence={ECO:0000250|UniProtKB:Q9TR36}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43777; CC Evidence={ECO:0000250|UniProtKB:Q9TR36}; CC -!- ACTIVITY REGULATION: Phosphatidylinositol transfer activity is CC inhibited by N-ethylmaleimide. {ECO:0000269|PubMed:18636990}. CC -!- INTERACTION: CC P48739; P55212: CASP6; NbExp=3; IntAct=EBI-1047143, EBI-718729; CC P48739; P13473-2: LAMP2; NbExp=3; IntAct=EBI-1047143, EBI-21591415; CC P48739; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-1047143, EBI-5280197; CC P48739; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-1047143, EBI-2623095; CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P53811}. CC Golgi apparatus membrane {ECO:0000250|UniProtKB:P53812}. Endoplasmic CC reticulum membrane {ECO:0000250|UniProtKB:P53812}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P48739-1; Sequence=Displayed; CC Name=2; CC IsoId=P48739-2; Sequence=VSP_012762; CC Name=3; CC IsoId=P48739-3; Sequence=VSP_055132; CC -!- TISSUE SPECIFICITY: Widely expressed in various tissues including CC brain. CC -!- PTM: Constitutive phosphorylation of Ser-262 has no effect on CC phospholipid transfer activity but is required for Golgi targeting. CC {ECO:0000250|UniProtKB:P53811}. 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; D30037; BAA06277.1; -; mRNA. DR EMBL; CR456541; CAG30427.1; -; mRNA. DR EMBL; AK302367; BAH13686.1; -; mRNA. DR EMBL; AL031591; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471095; EAW59743.1; -; Genomic_DNA. DR EMBL; BC018704; AAH18704.1; -; mRNA. DR EMBL; BC031427; AAH31427.1; -; mRNA. DR CCDS; CCDS13842.1; -. [P48739-1] DR CCDS; CCDS63432.1; -. [P48739-3] DR CCDS; CCDS63433.1; -. [P48739-2] DR RefSeq; NP_001271206.1; NM_001284277.1. [P48739-2] DR RefSeq; NP_001271207.1; NM_001284278.1. [P48739-3] DR RefSeq; NP_036531.1; NM_012399.4. [P48739-1] DR AlphaFoldDB; P48739; -. DR SMR; P48739; -. DR BioGRID; 117261; 48. DR IntAct; P48739; 12. DR MINT; P48739; -. DR STRING; 9606.ENSP00000487693; -. DR SwissLipids; SLP:000000416; -. DR GlyGen; P48739; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P48739; -. DR MetOSite; P48739; -. DR PhosphoSitePlus; P48739; -. DR SwissPalm; P48739; -. DR BioMuta; PITPNB; -. DR DMDM; 1346772; -. DR EPD; P48739; -. DR jPOST; P48739; -. DR MassIVE; P48739; -. DR MaxQB; P48739; -. DR PaxDb; 9606-ENSP00000321266; -. DR PeptideAtlas; P48739; -. DR ProteomicsDB; 55934; -. [P48739-1] DR ProteomicsDB; 55935; -. [P48739-2] DR ProteomicsDB; 6893; -. DR Pumba; P48739; -. DR Antibodypedia; 24304; 331 antibodies from 28 providers. DR DNASU; 23760; -. DR Ensembl; ENST00000320996.14; ENSP00000321266.10; ENSG00000180957.19. [P48739-2] DR Ensembl; ENST00000335272.10; ENSP00000334738.5; ENSG00000180957.19. [P48739-1] DR Ensembl; ENST00000634017.1; ENSP00000487693.1; ENSG00000180957.19. [P48739-3] DR GeneID; 23760; -. DR KEGG; hsa:23760; -. DR MANE-Select; ENST00000335272.10; ENSP00000334738.5; NM_012399.5; NP_036531.1. DR UCSC; uc003adk.5; human. [P48739-1] DR AGR; HGNC:9002; -. DR CTD; 23760; -. DR DisGeNET; 23760; -. DR GeneCards; PITPNB; -. DR HGNC; HGNC:9002; PITPNB. DR HPA; ENSG00000180957; Low tissue specificity. DR MIM; 606876; gene. DR neXtProt; NX_P48739; -. DR OpenTargets; ENSG00000180957; -. DR PharmGKB; PA33336; -. DR VEuPathDB; HostDB:ENSG00000180957; -. DR eggNOG; KOG3668; Eukaryota. DR GeneTree; ENSGT00940000155101; -. DR HOGENOM; CLU_046509_0_0_1; -. DR InParanoid; P48739; -. DR OMA; NELKPDC; -. DR OrthoDB; 3946034at2759; -. DR PhylomeDB; P48739; -. DR TreeFam; TF313279; -. DR PathwayCommons; P48739; -. DR Reactome; R-HSA-1483196; PI and PC transport between ER and Golgi membranes. DR SignaLink; P48739; -. DR BioGRID-ORCS; 23760; 44 hits in 1160 CRISPR screens. DR ChiTaRS; PITPNB; human. DR GeneWiki; PITPNB; -. DR GenomeRNAi; 23760; -. DR Pharos; P48739; Tbio. DR PRO; PR:P48739; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; P48739; Protein. DR Bgee; ENSG00000180957; Expressed in gingival epithelium and 218 other cell types or tissues. DR ExpressionAtlas; P48739; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; ISS: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:BHF-UCL. DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IDA:UniProtKB. DR GO; GO:0140338; F:sphingomyelin transfer activity; ISS:UniProtKB. DR GO; GO:0006629; P:lipid metabolic process; NAS:ProtInc. DR GO; GO:0006997; P:nucleus organization; TAS:BHF-UCL. DR GO; GO:0015914; P:phospholipid transport; IDA:BHF-UCL. DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP: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:SF27; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN BETA ISOFORM; 1. DR Pfam; PF02121; IP_trans; 1. DR PRINTS; PR00391; PITRANSFER. DR SUPFAM; SSF55961; Bet v1-like; 1. DR Genevisible; P48739; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Endoplasmic reticulum; Golgi apparatus; KW Lipid transport; Lipid-binding; Membrane; Phosphoprotein; KW Reference proteome; Transport. FT CHAIN 1..271 FT /note="Phosphatidylinositol transfer protein beta isoform" FT /id="PRO_0000191643" FT MOD_RES 215 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 262 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P53811" FT VAR_SEQ 1..7 FT /note="MVLIKEF -> MGDLLMEKC (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055132" FT VAR_SEQ 257..271 FT /note="MRKRGSVRGTSAADV -> LRNQGQVRGTSAASDE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_012762" FT MUTAGEN 60 FT /note="K->A: Loss of phosphatidylinositol transfer activity FT but no effect on phosphatidylcholine transfer activity. FT Fails to rescue the retrograde transport defect from the FT Golgi to endoplasmic reticulum in PITPNB-deficient cells." FT /evidence="ECO:0000269|PubMed:20332109" FT MUTAGEN 89 FT /note="N->F: Loss of phosphatidylinositol transfer activity FT but no effect on phosphatidylcholine transfer activity. FT Fails to rescue the retrograde transport defect from the FT Golgi to endoplasmic reticulum in PITPNB-deficient cells." FT /evidence="ECO:0000269|PubMed:20332109" FT MUTAGEN 94 FT /note="C->T,A: Loss of phosphatidylcholine transfer FT activity but no effect on phosphatidylinositol transfer FT activity. Not inhibited by N-ethylmaleimide. Fails to FT rescue the retrograde transport defect from the Golgi to FT endoplasmic reticulum in PITPNB-deficient cells." FT /evidence="ECO:0000269|PubMed:18636990, FT ECO:0000269|PubMed:20332109" FT MUTAGEN 187 FT /note="C->A: No effect on phosphatidylinositol transfer FT activity." FT /evidence="ECO:0000269|PubMed:18636990" FT MUTAGEN 202..203 FT /note="WW->AA: Loss of phosphatidylinositol transfer FT activity. Fails to rescue the retrograde transport defect FT from the Golgi to endoplasmic reticulum in PITPNB-deficient FT cells." FT /evidence="ECO:0000269|PubMed:18636990, FT ECO:0000269|PubMed:20332109" SQ SEQUENCE 271 AA; 31540 MW; AC5333FBC0F6CA06 CRC64; MVLIKEFRVV LPCSVQEYQV GQLYSVAEAS KNETGGGEGI EVLKNEPYEK DGEKGQYTHK IYHLKSKVPA FVRMIAPEGS LVFHEKAWNA YPYCRTIVTN EYMKDDFFIK IETWHKPDLG TLENVHGLDP NTWKTVEIVH IDIADRSQVE PADYKADEDP ALFQSVKTKR GPLGPNWKKE LANSPDCPQM CAYKLVTIKF KWWGLQSKVE NFIQKQEKRI FTNFHRQLFC WIDKWIDLTM EDIRRMEDET QKELETMRKR GSVRGTSAAD V //