PIPNB_RAT
ID PIPNB_RAT Reviewed; 271 AA.
AC P53812; Q6P7S3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=7961615; DOI=10.1093/oxfordjournals.jbchem.a124448;
RA Tanaka S., Hosaka K.;
RT "Cloning of a cDNA encoding a second phosphatidylinositol transfer protein
RT of rat brain by complementation of the yeast sec14 mutation.";
RL J. Biochem. 115:981-984(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIVITY REGULATION,
RP AND MUTAGENESIS OF 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).
CC -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol between
CC membranes (PubMed:18636990). Also catalyzes the transfer of
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, ECO:0000269|PubMed:18636990}.
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:0000269|PubMed:18636990};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000305|PubMed:18636990};
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 -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P53811}.
CC Golgi apparatus membrane {ECO:0000269|PubMed:18636990}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:18636990}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P53812-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53812-2; Sequence=VSP_012763;
CC -!- TISSUE SPECIFICITY: Expressed abundantly in brain, kidney, liver, and
CC lung, but in a lesser amount in testis. {ECO:0000269|PubMed:7961615}.
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; D21132; BAA04669.1; -; mRNA.
DR EMBL; BC061538; AAH61538.1; -; mRNA.
DR PIR; JX0316; JX0316.
DR RefSeq; NP_446194.1; NM_053742.1. [P53812-1]
DR RefSeq; XP_006249584.1; XM_006249522.3. [P53812-2]
DR PDB; 2A1L; X-ray; 2.18 A; A=2-271.
DR PDBsum; 2A1L; -.
DR AlphaFoldDB; P53812; -.
DR SMR; P53812; -.
DR STRING; 10116.ENSRNOP00000050368; -.
DR iPTMnet; P53812; -.
DR PhosphoSitePlus; P53812; -.
DR jPOST; P53812; -.
DR PaxDb; P53812; -.
DR Ensembl; ENSRNOT00000052202; ENSRNOP00000050368; ENSRNOG00000000665. [P53812-2]
DR Ensembl; ENSRNOT00000115325; ENSRNOP00000078649; ENSRNOG00000000665. [P53812-1]
DR GeneID; 114561; -.
DR KEGG; rno:114561; -.
DR UCSC; RGD:620143; rat. [P53812-1]
DR CTD; 23760; -.
DR RGD; 620143; Pitpnb.
DR eggNOG; KOG3668; Eukaryota.
DR GeneTree; ENSGT00940000155101; -.
DR HOGENOM; CLU_046509_0_0_1; -.
DR InParanoid; P53812; -.
DR OrthoDB; 951268at2759; -.
DR Reactome; R-RNO-1483196; PI and PC transport between ER and Golgi membranes.
DR EvolutionaryTrace; P53812; -.
DR PRO; PR:P53812; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000000665; Expressed in heart and 19 other tissues.
DR ExpressionAtlas; P53812; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:BHF-UCL.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; ISS: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:BHF-UCL.
DR GO; GO:0140338; F:sphingomyelin transfer activity; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0015914; P:phospholipid transport; IDA:BHF-UCL.
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 3D-structure; Acetylation; Alternative splicing; Endoplasmic reticulum;
KW Golgi apparatus; Lipid transport; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..271
FT /note="Phosphatidylinositol transfer protein beta isoform"
FT /id="PRO_0000191646"
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"
FT VAR_SEQ 257..271
FT /note="MRKKGSVRGTSAADA -> LRSQGQVRGTSAACDD (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_012763"
FT MUTAGEN 202..203
FT /note="WW->AA: Loss of Golgi membrane localization."
FT /evidence="ECO:0000269|PubMed:18636990"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:2A1L"
FT HELIX 15..31
FT /evidence="ECO:0007829|PDB:2A1L"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:2A1L"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:2A1L"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2A1L"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:2A1L"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:2A1L"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:2A1L"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:2A1L"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2A1L"
FT STRAND 107..120
FT /evidence="ECO:0007829|PDB:2A1L"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:2A1L"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:2A1L"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2A1L"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:2A1L"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2A1L"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:2A1L"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:2A1L"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:2A1L"
FT STRAND 190..200
FT /evidence="ECO:0007829|PDB:2A1L"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:2A1L"
FT HELIX 206..230
FT /evidence="ECO:0007829|PDB:2A1L"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:2A1L"
FT HELIX 240..257
FT /evidence="ECO:0007829|PDB:2A1L"
SQ SEQUENCE 271 AA; 31450 MW; 936F9C5E068422B6 CRC64;
MVLIKEFRVV LPCSVQEYQV GQLYSVAEAS KNETGGGEGI EVLKNEPYEN DGEKGQYTHK
IYHLKSKVPA FVRMIAPEGS LVFHEKAWNA YPYCRTIVTN EYMKDDFFIK IETWHKPDLG
TLENVHGLDP NTWKTVEIVH IDIADRSQVE PADYKADEDP ALFQSVKTKR GPLGPNWKKE
LANTPDCPKM CAYKLVTIKF KWWGLQSKVE NFIQKQEKRI FTNLHRQLFC WIDKWIDLTM
EDIRRMEDET QKELETMRKK GSVRGTSAAD A
