PIPNB_HUMAN
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 03-AUG-2022, entry version 181.
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}.
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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; 37.
DR IntAct; P48739; 9.
DR MINT; P48739; -.
DR STRING; 9606.ENSP00000321266; -.
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; P48739; -.
DR PeptideAtlas; P48739; -.
DR PRIDE; P48739; -.
DR ProteomicsDB; 55934; -. [P48739-1]
DR ProteomicsDB; 55935; -. [P48739-2]
DR ProteomicsDB; 6893; -.
DR Antibodypedia; 24304; 292 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 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; YCRTSKY; -.
DR OrthoDB; 951268at2759; -.
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; 39 hits in 1078 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 216 other tissues.
DR ExpressionAtlas; P48739; baseline and differential.
DR Genevisible; P48739; HS.
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 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; 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
