PIPNB_BOVIN
ID PIPNB_BOVIN Reviewed; 271 AA.
AC Q9TR36; A0JN44;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Phosphatidylinositol transfer protein beta isoform;
DE Short=PI-TP-beta;
DE Short=PtdIns transfer protein beta;
DE Short=PtdInsTP beta;
DE AltName: Full=Phosphatidylinositol-transfer protein 36 kDa isoform;
DE Short=PI-TP 36 kda isoform;
GN Name=PITPNB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-22, FUNCTION, AND CATALYTIC ACTIVITY.
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).
CC -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol,
CC phosphatidylcholine and sphingomyelin between membranes
CC (PubMed:7654206). Required for COPI-mediated retrograde transport from
CC the 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:0000269|PubMed:7654206}.
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:7654206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572;
CC Evidence={ECO:0000305|PubMed:7654206};
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:7654206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000305|PubMed:7654206};
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:0000269|PubMed:7654206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43777;
CC Evidence={ECO:0000305|PubMed:7654206};
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 -!- 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; BC126510; AAI26511.1; -; mRNA.
DR RefSeq; NP_001071508.1; NM_001078040.1.
DR AlphaFoldDB; Q9TR36; -.
DR SMR; Q9TR36; -.
DR STRING; 9913.ENSBTAP00000048516; -.
DR SwissLipids; SLP:000000989; -.
DR PaxDb; Q9TR36; -.
DR PRIDE; Q9TR36; -.
DR Ensembl; ENSBTAT00000081439; ENSBTAP00000061142; ENSBTAG00000017799.
DR GeneID; 613773; -.
DR KEGG; bta:613773; -.
DR CTD; 23760; -.
DR VEuPathDB; HostDB:ENSBTAG00000017799; -.
DR VGNC; VGNC:32920; PITPNB.
DR eggNOG; KOG3668; Eukaryota.
DR GeneTree; ENSGT00940000155101; -.
DR HOGENOM; CLU_046509_0_0_1; -.
DR InParanoid; Q9TR36; -.
DR OMA; YCRTSKY; -.
DR OrthoDB; 951268at2759; -.
DR TreeFam; TF313279; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000017799; Expressed in ruminant reticulum and 108 other tissues.
DR ExpressionAtlas; Q9TR36; 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; IBA:GO_Central.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; IDA:UniProtKB.
DR GO; GO:0008525; F:phosphatidylcholine transporter activity; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IDA:UniProtKB.
DR GO; GO:0140338; F:sphingomyelin transfer activity; IDA: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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Endoplasmic reticulum;
KW Golgi apparatus; Lipid transport; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7654206"
FT CHAIN 2..271
FT /note="Phosphatidylinositol transfer protein beta isoform"
FT /id="PRO_0000269201"
FT MOD_RES 215
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48739"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53811"
SQ SEQUENCE 271 AA; 31539 MW; 114FE229E13BCA13 CRC64;
MVLIKEFRVV LPCSVQEYQV GQLYSVAEAS KNETGGGEGI EVLKNEPYEK DGEKGQYTHK
IYHLKSKVPA FVRMIAPEGS LVFHEKAWNA YPYCRTIVTN EYMKDDFFIK IETWHKPDLG
TLENVHGLDP NTWKTVEIVH IDIADRSQVE PADYKADEDP ALFQSVKTKR GPLGPNWKKE
LANNPDCPQM CAYKLVTIKF KWWGLQSKVE NFIQKQEKRI FTNFHRQLFC WIDKWIDLTM
EDIRRMEDET QKELETMRKK GSVRGTSAAD V
