ID   PIPNB_PONAB             Reviewed;         272 AA.
AC   Q5R6F0;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 71.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P53811}.
CC       Golgi apparatus membrane {ECO:0000250|UniProtKB:P53812}. Endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P53812}.
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; CR860540; CAH92666.1; -; mRNA.
DR   RefSeq; NP_001126559.1; NM_001133087.1.
DR   AlphaFoldDB; Q5R6F0; -.
DR   SMR; Q5R6F0; -.
DR   STRING; 9601.ENSPPYP00000013019; -.
DR   GeneID; 100173550; -.
DR   KEGG; pon:100173550; -.
DR   CTD; 23760; -.
DR   eggNOG; KOG3668; Eukaryota.
DR   InParanoid; Q5R6F0; -.
DR   OrthoDB; 951268at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0008526; F:phosphatidylinositol transfer activity; ISS:UniProtKB.
DR   GO; GO:0140338; F:sphingomyelin transfer activity; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Acetylation; Endoplasmic reticulum; Golgi apparatus; Lipid transport;
KW   Lipid-binding; Membrane; Reference proteome; Transport.
FT   CHAIN           1..272
FT                   /note="Phosphatidylinositol transfer protein beta isoform"
FT                   /id="PRO_0000191645"
FT   MOD_RES         215
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P48739"
SQ   SEQUENCE   272 AA;  31578 MW;  14C2F93FAD993419 CRC64;
     MVLIKEFRVV LPCSVQEYQV GQLYSVAEAS KNETGGGEGI EVLKNEPYEK DGEKGQYTHK
     IYHLKSKVPA FVRMIAPEGS LVFHEKAWNA YPYCRTIVTN ECMKDDFFIK IETWHKPDLG
     TLENVHGLDP NTWKTVEIVH IDIADRSQVE PADYKADEDP ALFQSVKTKR GPLGPNWKKE
     LANSPDCPQM CAYKLVTIKF KWWGLQSKVE NFIQKQEKRI FTNFHRQLFC WIDKWIDLTM
     EDIRRMEDET QKELETLRNQ GQVRGTSAAS DE