ID Q8JZZ5_MOUSE Unreviewed; 272 AA. AC Q8JZZ5; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=Phosphatidylinositol transfer protein beta isoform {ECO:0000256|ARBA:ARBA00041171}; GN Name=Pitpnb {ECO:0000313|EMBL:AAH34676.1, GN ECO:0000313|Ensembl:ENSMUSP00000142732.2, GN ECO:0000313|MGI:MGI:1927542}; 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 {ECO:0000313|EMBL:AAH34676.1}; RN [1] {ECO:0000313|EMBL:AAH34676.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye {ECO:0000313|EMBL:AAH34676.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; 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 [2] {ECO:0000313|Ensembl:ENSMUSP00000142732.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000142732.2, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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). RN [4] {ECO:0000313|Ensembl:ENSMUSP00000142732.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000142732.2}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. 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:0000256|ARBA:ARBA00024146}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692; CC Evidence={ECO:0000256|ARBA:ARBA00024146}; 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:0000256|ARBA:ARBA00023723}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572; CC Evidence={ECO:0000256|ARBA:ARBA00023723}; 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:0000256|ARBA:ARBA00036388}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43777; CC Evidence={ECO:0000256|ARBA:ARBA00036388}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004586}. Golgi apparatus membrane CC {ECO:0000256|ARBA:ARBA00004394}. CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI transfer CC class I subfamily. {ECO:0000256|ARBA:ARBA00038104}. 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; BC034676; AAH34676.1; -; mRNA. DR RefSeq; NP_001288572.1; NM_001301643.1. DR RefSeq; NP_001288573.1; NM_001301644.1. DR RefSeq; NP_001288595.1; NM_001301666.1. DR RefSeq; NP_062614.1; NM_019640.5. DR ProteomicsDB; 337136; -. DR Antibodypedia; 24304; 331 antibodies from 28 providers. DR DNASU; 56305; -. DR Ensembl; ENSMUST00000200298.2; ENSMUSP00000142732.2; ENSMUSG00000050017.12. DR GeneID; 56305; -. DR KEGG; mmu:56305; -. DR UCSC; uc008ysc.2; mouse. DR AGR; MGI:1927542; -. DR CTD; 23760; -. DR MGI; MGI:1927542; Pitpnb. DR VEuPathDB; HostDB:ENSMUSG00000050017; -. DR GeneTree; ENSGT00940000155101; -. DR OrthoDB; 3946034at2759; -. DR BioGRID-ORCS; 56305; 5 hits in 80 CRISPR screens. DR ChiTaRS; Pitpnb; mouse. DR Proteomes; UP000000589; Chromosome 5. DR Bgee; ENSMUSG00000050017; Expressed in condyle and 259 other cell types or tissues. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031210; F:phosphatidylcholine binding; IEA:Ensembl. DR GO; GO:0120019; F:phosphatidylcholine transfer activity; IEA:Ensembl. DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:Ensembl. DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IEA:Ensembl. DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:Ensembl. 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. PE 1: Evidence at protein level; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW Proteomics identification {ECO:0007829|EPD:Q8JZZ5, KW ECO:0007829|MaxQB:Q8JZZ5}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}. SQ SEQUENCE 272 AA; 31616 MW; BFD6672C097CED49 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 QKELETLRSQ GQVRGTSAAC DD //