PIPNA_RABIT
ID PIPNA_RABIT Reviewed; 270 AA.
AC P48738;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Phosphatidylinositol transfer protein alpha isoform;
DE Short=PI-TP-alpha;
DE Short=PtdIns transfer protein alpha;
DE Short=PtdInsTP alpha;
GN Name=PITPNA; Synonyms=PITPN;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lung;
RX PubMed=8682321; DOI=10.1016/0378-1119(96)00098-4;
RA Tsao F.H.C., Cheng W., Chen X.R., Chen X.M.;
RT "Isolation and sequencing of the cDNA encoding phosphatidylinositol
RT transfer protein from rabbit lung.";
RL Gene 172:299-302(1996).
CC -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol (PI) and
CC phosphatidylcholine (PC) between membranes (By similarity). Shows a
CC preference for PI and PC containing shorter saturated or monosaturated
CC acyl chains at the sn-1 and sn-2 positions (By similarity). Preference
CC order for PC is C16:1 > C16:0 > C18:1 > C18:0 > C20:4 and for PI is
CC C16:1 > C16:0 > C18:1 > C18:0 > C20:4 > C20:3 (By similarity).
CC {ECO:0000250|UniProtKB:Q00169}.
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:Q00169};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572;
CC Evidence={ECO:0000250|UniProtKB:Q00169};
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:Q00169};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000250|UniProtKB:Q00169};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53810}. Nucleus
CC {ECO:0000250|UniProtKB:P53810}.
CC -!- PTM: Phosphorylated by PKC in a calcium and phosphatidylserine-
CC dependent manner. {ECO:0000250|UniProtKB:P53810}.
CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI transfer
CC class I subfamily. {ECO:0000305}.
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DR EMBL; U12558; AAB08971.1; -; Genomic_DNA.
DR PIR; JC4854; JC4854.
DR RefSeq; NP_001164622.1; NM_001171151.1.
DR RefSeq; XP_008268889.1; XM_008270667.2.
DR AlphaFoldDB; P48738; -.
DR SMR; P48738; -.
DR STRING; 9986.ENSOCUP00000016962; -.
DR Ensembl; ENSOCUT00000022040; ENSOCUP00000016962; ENSOCUG00000000075.
DR GeneID; 100328961; -.
DR KEGG; ocu:100328961; -.
DR CTD; 5306; -.
DR eggNOG; KOG3668; Eukaryota.
DR GeneTree; ENSGT00940000157119; -.
DR InParanoid; P48738; -.
DR OrthoDB; 951268at2759; -.
DR Proteomes; UP000001811; Chromosome 19.
DR Bgee; ENSOCUG00000000075; Expressed in autopod skin and 17 other tissues.
DR ExpressionAtlas; P48738; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISS:UniProtKB.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; ISS:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; 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 3: Inferred from homology;
KW Acetylation; Cytoplasm; Lipid transport; Lipid-binding; Nucleus;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q2HJ54"
FT CHAIN 2..270
FT /note="Phosphatidylinositol transfer protein alpha isoform"
FT /id="PRO_0000191641"
FT REGION 250..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q00169"
FT BINDING 60
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q00169"
FT BINDING 85
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q00169"
FT BINDING 89
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q00169"
FT BINDING 96
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q00169"
FT BINDING 194
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q00169"
FT MOD_RES 215
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00169"
SQ SEQUENCE 270 AA; 31906 MW; 9287AE1EB9800A8A CRC64;
MVLLKEYRVI LPVSVDEYQV GQLYSVAEAS KNETGGGEGV EVLVNEPYEK DGERGQYTHK
IYHLQSKVPT FVRMLAPEGA LNIHEKAWNA YPYCRTVITN EYMKEDFLIK IETWHKPDLG
TQENVHKLEP ETWKHVEVIY IDIADRSQVL SKDYKAEEDP AKFKSIKTGR GPLGPNWKQE
LVNQKDCPYM CAYKLVTVKF KWWGLQNKVE NFIHKQERRL FTNFHRQLFC WLDKWVDLTM
DDIRRMEEET KRQLDEMRQK DPVKGMTADD
