TTPA_RAT
ID TTPA_RAT Reviewed; 278 AA.
AC P41034;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Alpha-tocopherol transfer protein;
DE Short=Alpha-TTP;
GN Name=Ttpa; Synonyms=Tpp1;
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], AND PROTEIN SEQUENCE OF 77-87; 156-165; 178-182
RP AND 212-216.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8349655; DOI=10.1016/s0021-9258(17)46761-5;
RA Sato Y., Arai H., Miyata A., Tokita S., Yamamoto K., Tanabe T., Inoue K.;
RT "Primary structure of alpha-tocopherol transfer protein from rat liver.
RT Homology with cellular retinaldehyde-binding protein.";
RL J. Biol. Chem. 268:17705-17710(1993).
CC -!- FUNCTION: Binds alpha-tocopherol, enhances its transfer between
CC separate membranes, and stimulates its release from liver cells. Binds
CC both phosphatidylinositol 3,4-bisphosphate and
CC phosphatidylinositolphosphatidylinol 4,5-bisphosphate; the resulting
CC conformation change is important for the release of the bound alpha-
CC tocopherol (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer and homotetramer. Phosphatidylinositol 4,5-
CC bisphosphate binding induces the formation of homotetramers.
CC Phosphatidylinositol 3,4-bisphosphate is less efficient in inducing
CC tetramerization (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Liver.
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DR EMBL; D16339; BAA03843.1; -; mRNA.
DR PIR; A47404; A47404.
DR RefSeq; NP_037180.1; NM_013048.2.
DR AlphaFoldDB; P41034; -.
DR SMR; P41034; -.
DR IntAct; P41034; 1.
DR STRING; 10116.ENSRNOP00000009611; -.
DR iPTMnet; P41034; -.
DR PhosphoSitePlus; P41034; -.
DR PaxDb; P41034; -.
DR PRIDE; P41034; -.
DR GeneID; 25571; -.
DR KEGG; rno:25571; -.
DR UCSC; RGD:3915; rat.
DR CTD; 7274; -.
DR RGD; 3915; Ttpa.
DR VEuPathDB; HostDB:ENSRNOG00000007139; -.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_046597_1_2_1; -.
DR InParanoid; P41034; -.
DR OMA; WTDFIMA; -.
DR OrthoDB; 1053004at2759; -.
DR PhylomeDB; P41034; -.
DR Reactome; R-RNO-8877627; Vitamin E.
DR PRO; PR:P41034; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007139; Expressed in liver and 17 other tissues.
DR Genevisible; P41034; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005770; C:late endosome; IDA:RGD.
DR GO; GO:0120013; F:lipid transfer activity; ISO:RGD.
DR GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; IBA:GO_Central.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0019842; F:vitamin binding; IDA:RGD.
DR GO; GO:0008431; F:vitamin E binding; IDA:RGD.
DR GO; GO:0032502; P:developmental process; IEP:RGD.
DR GO; GO:0001892; P:embryonic placenta development; ISO:RGD.
DR GO; GO:0120009; P:intermembrane lipid transfer; ISS:UniProtKB.
DR GO; GO:0051452; P:intracellular pH reduction; IDA:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IDA:RGD.
DR GO; GO:0090212; P:negative regulation of establishment of blood-brain barrier; ISO:RGD.
DR GO; GO:0001890; P:placenta development; ISO:RGD.
DR GO; GO:1900223; P:positive regulation of amyloid-beta clearance; ISO:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0009268; P:response to pH; IDA:RGD.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
DR GO; GO:0042360; P:vitamin E metabolic process; IDA:RGD.
DR GO; GO:0051180; P:vitamin transport; ISS:UniProtKB.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Lipid-binding; Reference proteome;
KW Transport.
FT CHAIN 1..278
FT /note="Alpha-tocopherol transfer protein"
FT /id="PRO_0000210766"
FT DOMAIN 88..253
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57658"
FT /evidence="ECO:0000250|UniProtKB:Q8BWP5"
FT BINDING 187
FT /ligand="(+)-alpha-tocopherol"
FT /ligand_id="ChEBI:CHEBI:18145"
FT /evidence="ECO:0000250|UniProtKB:Q8BWP5"
FT BINDING 190..192
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57658"
FT /evidence="ECO:0000250|UniProtKB:Q8BWP5"
FT BINDING 208..211
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:Q8BWP5"
FT BINDING 217
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57658"
FT /evidence="ECO:0000250|UniProtKB:Q8BWP5"
FT BINDING 221
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57658"
FT /evidence="ECO:0000250|UniProtKB:Q8BWP5"
SQ SEQUENCE 278 AA; 31846 MW; 96F16E3F227F140C CRC64;
MAEMRPGPVV GKQLNEQPDH SPLVQPGLAE LRRRAQEEGV PETPQPLTDA FLLRFLRARD
FDLDLAWRLM KNYYKWRAEC PELSADLHPR SILGLLKAGY HGVLRSRDPT GSRVLIYRIS
YWDPKVFTAY DVFRVSLITS ELIVQEVETQ RNGVKAIFDL EGWQISHAFQ ITPSVAKKIA
AVVTDSFPLK VRGIHLINEP VIFHAVFSMI KPFLTEKIKG RIHLHGNNYK SSLLQHFPDI
LPLEYGGNES SMEDICQEWT NFIMKSEDYL SSISETIQ
