PIPNB_MOUSE
ID PIPNB_MOUSE Reviewed; 271 AA.
AC P53811;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SWR/J;
RA Geijtenbeek T.B.H., der Helm H.A., Snoek G.T., Wirtz K.W.A.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP SUBCELLULAR LOCATION.
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).
RN [4]
RP PHOSPHORYLATION AT SER-262, MUTAGENESIS OF SER-165 AND SER-262, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11953429; DOI=10.1074/jbc.m201532200;
RA van Tiel C.M., Westerman J., Paasman M.A., Hoebens M.M., Wirtz K.W.,
RA Snoek G.T.;
RT "The Golgi localization of phosphatidylinositol transfer protein beta
RT requires the protein kinase C-dependent phosphorylation of serine 262 and
RT is essential for maintaining plasma membrane sphingomyelin levels.";
RL J. Biol. Chem. 277:22447-22452(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol,
CC phosphatidylcholine and sphingomyelin between membranes (By
CC similarity). Required for COPI-mediated retrograde transport from the
CC Golgi to the endoplasmic reticulum; phosphatidylinositol and
CC phosphatidylcholine transfer activity is essential for this function
CC (By similarity). {ECO:0000250|UniProtKB:P48739,
CC ECO:0000250|UniProtKB:Q9TR36}.
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:0000250|UniProtKB:Q9TR36};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572;
CC Evidence={ECO:0000250|UniProtKB:Q9TR36};
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:0000250|UniProtKB:Q9TR36};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000250|UniProtKB:Q9TR36};
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 -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:7654206}.
CC Golgi apparatus membrane {ECO:0000250|UniProtKB:P53812}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P53812}.
CC -!- PTM: Constitutive phosphorylation of Ser-262 has no effect on
CC phospholipid transfer activity but is required for Golgi targeting.
CC {ECO:0000269|PubMed:11953429}.
CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI transfer
CC class I subfamily. {ECO:0000305}.
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DR EMBL; U46934; AAA87593.1; -; mRNA.
DR EMBL; AK028235; BAC25830.1; -; mRNA.
DR CCDS; CCDS39213.1; -.
DR RefSeq; NP_001288573.1; NM_001301644.1.
DR RefSeq; NP_062614.1; NM_019640.5.
DR AlphaFoldDB; P53811; -.
DR SMR; P53811; -.
DR BioGRID; 207889; 1.
DR STRING; 10090.ENSMUSP00000083835; -.
DR iPTMnet; P53811; -.
DR PhosphoSitePlus; P53811; -.
DR SwissPalm; P53811; -.
DR EPD; P53811; -.
DR jPOST; P53811; -.
DR MaxQB; P53811; -.
DR PaxDb; P53811; -.
DR PeptideAtlas; P53811; -.
DR PRIDE; P53811; -.
DR ProteomicsDB; 287734; -.
DR Antibodypedia; 24304; 292 antibodies from 28 providers.
DR DNASU; 56305; -.
DR Ensembl; ENSMUST00000086635; ENSMUSP00000083835; ENSMUSG00000050017.
DR GeneID; 56305; -.
DR KEGG; mmu:56305; -.
DR UCSC; uc008ysb.2; mouse.
DR CTD; 23760; -.
DR MGI; MGI:1927542; Pitpnb.
DR VEuPathDB; HostDB:ENSMUSG00000050017; -.
DR eggNOG; KOG3668; Eukaryota.
DR GeneTree; ENSGT00940000155101; -.
DR HOGENOM; CLU_046509_0_0_1; -.
DR InParanoid; P53811; -.
DR OMA; YCRTSKY; -.
DR PhylomeDB; P53811; -.
DR TreeFam; TF313279; -.
DR Reactome; R-MMU-1483196; PI and PC transport between ER and Golgi membranes.
DR BioGRID-ORCS; 56305; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Pitpnb; mouse.
DR PRO; PR:P53811; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P53811; protein.
DR Bgee; ENSMUSG00000050017; Expressed in condyle and 256 other tissues.
DR ExpressionAtlas; P53811; baseline and differential.
DR Genevisible; P53811; MM.
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; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:MGI.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; ISS:UniProtKB.
DR GO; GO:0008525; F:phosphatidylcholine transporter activity; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISO:MGI.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISA:MGI.
DR GO; GO:0140338; F:sphingomyelin transfer activity; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0015914; P:phospholipid transport; ISO:MGI.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISS: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; Endoplasmic reticulum; Golgi apparatus; Lipid transport;
KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..271
FT /note="Phosphatidylinositol transfer protein beta isoform"
FT /id="PRO_0000191644"
FT MOD_RES 215
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48739"
FT MOD_RES 262
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:11953429"
FT MUTAGEN 165
FT /note="S->A: No effect on phosphorylation by PKC; abolishes
FT phospholipid transfer activity."
FT /evidence="ECO:0000269|PubMed:11953429"
FT MUTAGEN 262
FT /note="S->A: Abolishes phosphorylation by PKC and impairs
FT Golgi targeting; no effect on phospholipid transfer
FT activity."
FT /evidence="ECO:0000269|PubMed:11953429"
SQ SEQUENCE 271 AA; 31487 MW; 9111B615909548CD CRC64;
MVLIKEFRVV LPCSVQEYQV GQLYSVAEAS KNETGGGEGI EVLKNEPYEN DGEKGQYTHK
IYHLKSKVPA FVRMIAPEGS LVFHEKAWNA YPYCRTIVTN EYMKDDFFIK IETWHKPDLG
TLENVHGLDP NTWKTVEIVH IDIADRSQVE PADYKADEDP ALFHSVKTKR GPLGPNWKKE
LANTPDCPRM CAYKLVTIKF KWWGLQSKVE NFIQKQEKRI FTNLHRQLFC WIDKWIDLTM
EDIRRMEDET QKELETMRKK GSVRGTSAAD A
