P60815
uniprot
P60815
canonical
amino_acid_sequence
MVNESLNQEESNDRPVPESEFQADTSYSTQPSVSIHPSVSGHPSVSIHPSVSGHPSVSIDPSVSVHPSSSAHPSTLAQPSGLTHPNELVKEDSVIKVSKRRWAVVLVFSCYSLCNAFQWIQYGSINNIFMNFYGVSAFAIDWLSMCYMLTYIPLLLPVAWMLEKFGLRTIAITGSALNCLGAWVKLGSLEPHLFPVTMVGQVICSVAQVFILGMPSRIASVWFGANEVSTACSMAVFGNQLGIAIGFLVPPVLVPNIKDQEKLAYHISIMFYIIGGVATLLFILVIIVFKEKPKYPPSRAQSLSYALATTDASYLSSIVRLFKNLNFVLLVITYGLNAGAFYALSTLLNRMVIMHFPGQEVNAGRIGLTIVIAGMFGAMISGIWLDKSKTYKETTLVVYIMTLVGMVVYTFTLNLNHLWIVFITADSLGFFMTGYLPLGFEFAVELTYPESEGVSSGLLNVSAQVFGIIFTISQGQIIDNYGSVPGNIFLCVFLALGSALTAFIKSDLRRQRANKDAPETKVQEEEEEEEESNTSKVPTVLSEAHL
uniprot
proteins
function
FUNCTION: Choline uniporter that specifically mediates choline uptake at the blood-brain-barrier. Responsible for the majority of choline uptake across the blood-brain-barrier from the circulation into the brain (By similarity). Choline, a nutrient critical for brain development, is a precursor of phosphatidylcholine, as well as betaine (By similarity). Also mediates transport of ethanolamine (By similarity). Choline and ethanolamine transport is not coupled with proton transport and is exclusively driven by the choline gradient across the plasma membrane (By similarity). However, the presence of an inwardly directed proton gradient enhances choline uptake (By similarity). Also acts as a heme b transporter (By similarity). Required to regulate mitochondrial respiration processes, ATP synthesis and thermogenesis (By similarity). At low heme levels, interacts with components of electron transfer chain (ETC) complexes and ATP2A2, leading to ubiquitin-mediated degradation of ATP2A2 and inhibition of thermogenesis (By similarity). Upon heme binding, dissociates from ETC complexes to allow switching from mitochondrial ATP synthesis to thermogenesis (By similarity). {ECO:0000250|UniProtKB:Q91X85, ECO:0000250|UniProtKB:Q9UPI3}.
uniprot
proteins
mass_dalton
59742
uniprot
proteins
protein_family
Feline leukemia virus subgroup C receptor (TC 2.A.1.28.1) family
uniprot
proteins
protein_family
Major facilitator superfamily
uniprot
proteins
pubmed
14729055
uniprot
proteins
sequence_length
546
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q91X85}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q91X85}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UPI3}; Multi-pass membrane protein {ECO:0000255}. Note=Present on both luminal (blood-facing) and abluminal (brain-facing) sides of brain endothelial cell plasma membranes, with higher luminal membrane expression (By similarity). Also localizes in mitochondria where it interacts with components of the electron transfer complexes III, IV and V. Colocalizes with ATP2A2 at the mitochondrial-ER contact junction (By similarity). {ECO:0000250|UniProtKB:Q91X85, ECO:0000250|UniProtKB:Q9UPI3}.
uniprot
proteins
transmembrane_region
TRANSMEM 94..118; /note="Helical; Name=TM1"; /evidence="ECO:0000250|UniProtKB:Q91X85"; TRANSMEM 137..164; /note="Helical; Name=TM2"; /evidence="ECO:0000250|UniProtKB:Q91X85"; TRANSMEM 167..186; /note="Helical; Name=TM3"; /evidence="ECO:0000250|UniProtKB:Q91X85"; TRANSMEM 194..222; /note="Helical; Name=TM4"; /evidence="ECO:0000250|UniProtKB:Q91X85"; TRANSMEM 228..253; /note="Helical; Name=TM5"; /evidence="ECO:0000250|UniProtKB:Q91X85"; TRANSMEM 259..288; /note="Helical; Name=TM6"; /evidence="ECO:0000250|UniProtKB:Q91X85"; TRANSMEM 325..355; /note="Helical; Name=TM7"; /evidence="ECO:0000250|UniProtKB:Q91X85"; TRANSMEM 360..388; /note="Helical; Name=TM8"; /evidence="ECO:0000250|UniProtKB:Q91X85"; TRANSMEM 391..413; /note="Helical; Name=TM9"; /evidence="ECO:0000250|UniProtKB:Q91X85"; TRANSMEM 417..446; /note="Helical; Name=TM10"; /evidence="ECO:0000250|UniProtKB:Q91X85"; TRANSMEM 455..480; /note="Helical; Name=TM11"; /evidence="ECO:0000250|UniProtKB:Q91X85"; TRANSMEM 483..505; /note="Helical; Name=TM12"; /evidence="ECO:0000250|UniProtKB:Q91X85
uniprot
proteins