ID   PITC1_XENTR             Reviewed;         329 AA.
AC   Q28CA0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Cytoplasmic phosphatidylinositol transfer protein 1;
DE   AltName: Full=Retinal degeneration B homolog beta;
DE            Short=RdgBbeta;
GN   Name=pitpnc1; ORFNames=TGas018n09.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol (PI) and
CC       phosphatidic acid (PA) between membranes (By similarity). Binds PA
CC       derived from the phospholipase D signaling pathway and among the
CC       cellular PA species, preferably binds to the C16:0/16:1 and C16:1/18:1
CC       PA species (By similarity). {ECO:0000250|UniProtKB:Q9UKF7}.
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:Q9UKF7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC         Evidence={ECO:0000250|UniProtKB:Q9UKF7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphate(in) = a 1,2-diacyl-sn-
CC         glycero-3-phosphate(out); Xref=Rhea:RHEA:36435, ChEBI:CHEBI:58608;
CC         Evidence={ECO:0000250|UniProtKB:Q9UKF7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36436;
CC         Evidence={ECO:0000250|UniProtKB:Q9UKF7};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K4R4}.
CC   -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI transfer
CC       class IIB subfamily. {ECO:0000305}.
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DR   EMBL; CR942381; CAJ82527.1; -; mRNA.
DR   RefSeq; NP_001039199.1; NM_001045734.1.
DR   AlphaFoldDB; Q28CA0; -.
DR   SMR; Q28CA0; -.
DR   STRING; 8364.ENSXETP00000060192; -.
DR   GeneID; 734057; -.
DR   KEGG; xtr:734057; -.
DR   CTD; 26207; -.
DR   Xenbase; XB-GENE-959703; pitpnc1.
DR   eggNOG; KOG3668; Eukaryota.
DR   InParanoid; Q28CA0; -.
DR   OrthoDB; 951268at2759; -.
DR   Proteomes; UP000008143; Chromosome 10.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:1990050; F:phosphatidic acid transfer activity; ISS:UniProtKB.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR   GO; GO:0008526; F:phosphatidylinositol transfer activity; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; 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   Cytoplasm; Lipid transport; Lipid-binding; Reference proteome; Transport.
FT   CHAIN           1..329
FT                   /note="Cytoplasmic phosphatidylinositol transfer protein 1"
FT                   /id="PRO_0000287532"
FT   REGION          267..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   329 AA;  37841 MW;  0905017E432CEC2C CRC64;
     MLLKEYRICM PLTVEEYRIG QLYMISKHSH EQSERGEGVE VVQNEPYEDP VHGQGQLTEK
     RVYLNSKLPS WARAVVPKIF YVTEKAWNYY PYTITEYTCS FLPKFSIHIE TKYEDNKGSN
     DNIFESEAKD AEREICFVDI ACDEIPERYY KESEDPKNFV SEKTGRGQLK EGWREAQEPI
     MCSYKLVAVK FEVWGLQSRV EQFVHKVVRD ILLIGHRQAF AWVDEWYDMT MDEVREYERT
     TQEATNRKIG VFPPAISISD ITLPSHSHGG YSSAPSTPLA TDAPEFLSVP KDRPRKKSAP
     ETLTLPDPSQ ICLNVQPGAG NKPSLAKPE