Flvcr2
entrez
217721
canonical
uniprot
Q91X85
canonical
ensembl
ENSMUSG00000034258
resolver
ensp
ENSMUSP00000035569
resolver
enst
ENSMUST00000040461
resolver
genesymbol
Flvcr2
resolver
genesymbol_syn
BC011209
resolver
genesymbol_syn
Mfsd7c
resolver
uniprot
A0A0R4J0E9
resolver
uniprot
Q3UL56
resolver
uniprot_entry
FLVC2_MOUSE
resolver
uniprot_entry
Q3UL56_MOUSE
resolver
uniprot_sec
A0A0R4J0E9
resolver
amino_acid_sequence
MVNESLNQEESNDRPAPESEFQMDTSYSTQPSGSIHPSVSGHPSVSGHPSVSGHPSVSIHPSVSIDPSVSVRPSSSALPSTLAQPSGLTHHSSLVREDSVIKVSKRRWVVVLVFSCYSLCNAFQWIQYGSINNIFMNFYGVSAFAIDWLSMCYMLTYIPLLLPVAWMLEKFGLRTIAITGSALNCLGAWVKLGSLEPHLFPVTMVGQVICSVAQVFILGMPSRIASVWFGADEVSTACSVAVFGNQLGIAIGFLVPPVLVPNIKDPEKLAYHISIMFYIIGGVATFLFILVIIVFKEKPKHPPSRAQSLSYALATTDASYLSSIVRLFKNLNFVLLVITYGLNAGAFYALSTLLNRMVILHFPGEEVNAGRIGLTIVIAGMFGAMISGIWLDKSKTYKETTLVVYIMTLVGMVVYTFTLNLNHLWVVFITAGTLGFFMTGYLPLGFEFAVELTYPESEGVSSGLLNVSAQVFGIVFTISQGQIIDNHGTMFGNIFLCVFLALGSALTAFIKSDLRRQRANKDAPETKVQEEEEEEEGSNTSKVPVVSEAHL
uniprot
proteins
function
FUNCTION: Choline uniporter that specifically mediates choline uptake at the blood-brain-barrier (PubMed:38302740, PubMed:38693257). Responsible for the majority of choline uptake across the blood-brain-barrier from the circulation into the brain (PubMed:38693257). Choline, a nutrient critical for brain development, is a precursor of phosphatidylcholine, as well as betaine (PubMed:38693257). 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 (PubMed:38693257). However, the presence of an inwardly directed proton gradient enhances choline uptake (PubMed:38693257). 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 (PubMed:32973183). Upon heme binding, dissociates from ETC complexes to allow switching from mitochondrial ATP synthesis to thermogenesis (PubMed:32973183). {ECO:0000250|UniProtKB:Q9UPI3, ECO:0000269|PubMed:32973183, ECO:0000269|PubMed:38302740, ECO:0000269|PubMed:38693257}.
uniprot
proteins
mass_dalton
60059
uniprot
proteins
mutagenesis
MUTAGEN 1..80; /note="Missing: Present at mitochondrial membrane. Impairs interaction with HMOX1. Abolishes the response to heme."; /evidence="ECO:0000269|PubMed:32973183
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
pubmed
15489334
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
32369449
uniprot
proteins
pubmed
32369453
uniprot
proteins
pubmed
32973183
uniprot
proteins
pubmed
38302740
uniprot
proteins
pubmed
38693257
uniprot
proteins
sequence_length
551
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:38693257}; Multi-pass membrane protein {ECO:0000269|PubMed:38693257}. Mitochondrion membrane {ECO:0000269|PubMed:32973183}; 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 (PubMed:38693257). Also localizes in mitochondria where it interacts with components of the electron transfer complexes III, IV and V (By similarity). Colocalizes with ATP2A2 at the mitochondrial-ER contact junction (By similarity). {ECO:0000250|UniProtKB:Q9UPI3, ECO:0000269|PubMed:38693257}.
uniprot
proteins
transmembrane_region
TRANSMEM 100..124; /note="Helical; Name=TM1"; /evidence="ECO:0000269|PubMed:38693257, ECO:0007744|PDB:8VZN, ECO:0007744|PDB:8VZO"; TRANSMEM 143..170; /note="Helical; Name=TM2"; /evidence="ECO:0000269|PubMed:38693257, ECO:0007744|PDB:8VZN, ECO:0007744|PDB:8VZO"; TRANSMEM 173..192; /note="Helical; Name=TM3"; /evidence="ECO:0000269|PubMed:38693257, ECO:0007744|PDB:8VZN, ECO:0007744|PDB:8VZO"; TRANSMEM 200..228; /note="Helical; Name=TM4"; /evidence="ECO:0000269|PubMed:38693257, ECO:0007744|PDB:8VZN, ECO:0007744|PDB:8VZO"; TRANSMEM 234..259; /note="Helical; Name=TM5"; /evidence="ECO:0000269|PubMed:38693257, ECO:0007744|PDB:8VZN, ECO:0007744|PDB:8VZO"; TRANSMEM 265..294; /note="Helical; Name=TM6"; /evidence="ECO:0000269|PubMed:38693257, ECO:0007744|PDB:8VZN, ECO:0007744|PDB:8VZO"; TRANSMEM 331..361; /note="Helical; Name=TM7"; /evidence="ECO:0000269|PubMed:38693257, ECO:0007744|PDB:8VZN, ECO:0007744|PDB:8VZO"; TRANSMEM 366..394; /note="Helical; Name=TM8"; /evidence="ECO:0000269|PubMed:38693257, ECO:0007744|PDB:8VZN, ECO:0007744|PDB:8VZO"; TRANSMEM 397..419; /note="Helical; Name=TM9"; /evidence="ECO:0000269|PubMed:38693257, ECO:0007744|PDB:8VZN, ECO:0007744|PDB:8VZO"; TRANSMEM 423..452; /note="Helical; Name=TM10"; /evidence="ECO:0000269|PubMed:38693257, ECO:0007744|PDB:8VZN, ECO:0007744|PDB:8VZO"; TRANSMEM 461..486; /note="Helical; Name=TM11"; /evidence="ECO:0000269|PubMed:38693257, ECO:0007744|PDB:8VZN, ECO:0007744|PDB:8VZO"; TRANSMEM 489..511; /note="Helical; Name=TM12"; /evidence="ECO:0000269|PubMed:38693257, ECO:0007744|PDB:8VZN, ECO:0007744|PDB:8VZO
uniprot
proteins