Flvcr1
entrez
226844
canonical
uniprot
B2RXV4
canonical
ensembl
ENSMUSG00000066595
resolver
ensp
ENSMUSP00000082777
resolver
ensp
ENSMUSP00000141578
resolver
enst
ENSMUST00000191946
resolver
genesymbol
Flvcr1
resolver
genesymbol_syn
Mfsd7b
resolver
uniprot
A0A0A6YWJ7
resolver
uniprot_entry
A0A0A6YWJ7_MOUSE
resolver
uniprot_entry
FLVC1_MOUSE
resolver
amino_acid_sequence
MARPDDEVGPAVAPGHPLGKGYLPVPKGAPDGEARLVPQNGPEALNGGPGLGPLIAGAQGGPQALIAAEEETQARLLPAGDGEDVPCPACPPRTALSPRRFVVLLIFSLYSLVNAFQWIQYSSISNVFEDFYEVSPLHINWLSMVYMVAYVPLIFPATWLLDTRGLRLTALLGSGLNCLGAWVKCGSVQRHLFWVTMLGQILCSVAQVFILGLPSPVASVWFGPKEVSTACATAVLGNQLGTAVGFLLPPVLVPALGTQNSTGLLAHTQNNTDLLAHNINTMFYGTAFISTFLFFLTIIAFKEKPPLPPSQAQAVLRDSPPEEYSYKSSIWNLCRNIPFVLLLVSYGIMTGAFYSISTLLNQIILTYYVGEEVNAGRIGLTLVVAGMVGSILCGLWLDYTKTYKQTTLIVYVLSFIGMLIFTFTLNLGYIIVVFFTGGILGFFMTGYLPLGFEFAVEITYPESEGMSSGLLNTAAQILGIFFTLAQGKITTDYNSPEAGNIFLCAWMFVGIILTALIKSDLRRHNINTGLTNIDVKAVPVDSRVDPKPKVMVSIQSESSL
uniprot
proteins
function
FUNCTION: Uniporter that mediates the transport of extracellular choline and ethanolamine into cells, thereby playing a key role in phospholipid biosynthesis (PubMed:37100056). Choline and ethanolamine are the precursors of phosphatidylcholine and phosphatidylethanolamine, respectively, the two most abundant phospholipids (By similarity). Transport is not coupled with proton transport and is exclusively driven by the choline (or ethanolamine) gradient across the plasma membrane (By similarity). Also acts as a heme b transporter that mediates heme efflux from the cytoplasm to the extracellular compartment (PubMed:18258918, PubMed:23187127). {ECO:0000250|UniProtKB:Q9Y5Y0, ECO:0000269|PubMed:18258918, ECO:0000269|PubMed:23187127, ECO:0000269|PubMed:37100056}.; FUNCTION: [Isoform 1]: Uniporter that mediates the transport of extracellular choline and ethanolamine into cells (By similarity). Choline and ethanolamine are the precursors of phosphatidylcholine and phosphatidylethanolamine, respectively, the two most abundant phospholipids (By similarity). Transport is not coupled with proton transport and is exclusively driven by the choline (or ethanolamine) gradient across the plasma membrane (By similarity). Also acts as a heme b transporter that mediates heme efflux from the cytoplasm to the extracellular compartment (PubMed:18258918, PubMed:23187127). Heme export depends on the presence of HPX and is required to maintain intracellular free heme balance, protecting cells from heme toxicity (By similarity). Heme export provides protection from heme or ferrous iron toxicities in liver, brain, sensory neurons and during erythropoiesis, a process in which heme synthesis intensifies (By similarity). Possibly export coproporphyrin and protoporphyrin IX, which are both intermediate products in the heme biosynthetic pathway (By similarity). Does not export bilirubin. The molecular mechanism of heme transport, whether electrogenic, electroneutral or coupled to other ions, remains to be elucidated (By similarity). {ECO:0000250|UniProtKB:Q9Y5Y0, ECO:0000269|PubMed:18258918, ECO:0000269|PubMed:23187127}.; FUNCTION: [Isoform 2]: Heme transporter that promotes heme efflux from the mitochondrion to the cytoplasm. Essential for erythroid differentiation. {ECO:0000269|PubMed:23187127}.
uniprot
proteins
mass_dalton
60469
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
15489334
uniprot
proteins
pubmed
18258918
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
23187127
uniprot
proteins
pubmed
24021674
uniprot
proteins
pubmed
37100056
uniprot
proteins
sequence_length
560
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:23187127}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion membrane {ECO:0000269|PubMed:23187127}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with HADHA. {ECO:0000269|PubMed:23187127}.
uniprot
proteins
transmembrane_region
TRANSMEM 93..117; /note="Helical; Name=TM1"; /evidence="ECO:0000250|UniProtKB:Q9Y5Y0"; TRANSMEM 136..163; /note="Helical; Name=TM2"; /evidence="ECO:0000250|UniProtKB:Q9Y5Y0"; TRANSMEM 166..185; /note="Helical; Name=TM3"; /evidence="ECO:0000250|UniProtKB:Q9Y5Y0"; TRANSMEM 193..221; /note="Helical; Name=TM4"; /evidence="ECO:0000250|UniProtKB:Q9Y5Y0"; TRANSMEM 227..252; /note="Helical; Name=TM5"; /evidence="ECO:0000250|UniProtKB:Q9Y5Y0"; TRANSMEM 271..300; /note="Helical; Name=TM6"; /evidence="ECO:0000250|UniProtKB:Q9Y5Y0"; TRANSMEM 337..367; /note="Helical; Name=TM7"; /evidence="ECO:0000250|UniProtKB:Q9Y5Y0"; TRANSMEM 372..400; /note="Helical; Name=TM8"; /evidence="ECO:0000250|UniProtKB:Q9Y5Y0"; TRANSMEM 403..425; /note="Helical; Name=TM9"; /evidence="ECO:0000250|UniProtKB:Q9Y5Y0"; TRANSMEM 429..458; /note="Helical; Name=TM10"; /evidence="ECO:0000250|UniProtKB:Q9Y5Y0"; TRANSMEM 467..492; /note="Helical; Name=TM11"; /evidence="ECO:0000250|UniProtKB:Q9Y5Y0"; TRANSMEM 496..518; /note="Helical; Name=TM12"; /evidence="ECO:0000250|UniProtKB:Q9Y5Y0
uniprot
proteins