FLVCR2
entrez
55640
canonical
uniprot
Q9UPI3
canonical
ensembl
ENSG00000119686
resolver
ensp
ENSP00000238667
resolver
ensp
ENSP00000443439
resolver
genesymbol
FLVCR2
resolver
genesymbol_syn
C14orf58
resolver
hgnc
HGNC:20105
resolver
uniprot
B7Z485
resolver
uniprot
Q53ZT9
resolver
uniprot
Q96JY3
resolver
uniprot
Q9NX90
resolver
uniprot_entry
FLVC2_HUMAN
resolver
uniprot_sec
B7Z485
resolver
uniprot_sec
Q53ZT9
resolver
uniprot_sec
Q96JY3
resolver
uniprot_sec
Q9NX90
resolver
amino_acid_sequence
MVNEGPNQEESDDTPVPESALQADPSVSVHPSVSVHPSVSINPSVSVHPSSSAHPSALAQPSGLAHPSSSGPEDLSVIKVSRRRWAVVLVFSCYSMCNSFQWIQYGSINNIFMHFYGVSAFAIDWLSMCYMLTYIPLLLPVAWLLEKFGLRTIALTGSALNCLGAWVKLGSLKPHLFPVTVVGQLICSVAQVFILGMPSRIASVWFGANEVSTACSVAVFGNQLGIAIGFLVPPVLVPNIEDRDELAYHISIMFYIIGGVATLLLILVIIVFKEKPKYPPSRAQSLSYALTSPDASYLGSIARLFKNLNFVLLVITYGLNAGAFYALSTLLNRMVIWHYPGEEVNAGRIGLTIVIAGMLGAVISGIWLDRSKTYKETTLVVYIMTLVGMVVYTFTLNLGHLWVVFITAGTMGFFMTGYLPLGFEFAVELTYPESEGISSGLLNISAQVFGIIFTISQGQIIDNYGTKPGNIFLCVFLTLGAALTAFIKADLRRQKANKETLENKLQEEEEESNTSKVPTAVSEDHL
uniprot
proteins
disease_involvement
DISEASE: Proliferative vasculopathy and hydranencephaly-hydrocephaly syndrome (PVHH) [MIM:225790]: A rare prenatally lethal disorder characterized by hydranencephaly, a distinctive glomerular vasculopathy in the central nervous system and retina, and diffuse ischemic lesions of the brain stem, basal ganglia, and spinal cord with calcifications. Hydranencephaly is a condition where the greater portions of the cerebral hemispheres and corpus striatum are replaced by cerebrospinal fluid and glial tissue. {ECO:0000269|PubMed:20206334, ECO:0000269|PubMed:20518025, ECO:0000269|PubMed:20690116, ECO:0000269|PubMed:25677735, ECO:0000269|PubMed:38302740}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Choline uniporter that specifically mediates choline uptake at the blood-brain-barrier (PubMed:38302740, PubMed:38778100, PubMed:40972734). 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 (PubMed:38778100). Choline and ethanolamine transport is not coupled with proton transport and is exclusively driven by the choline gradient across the plasma membrane (PubMed:38778100). However, the presence of an inwardly directed proton gradient enhances choline uptake (By similarity). Also acts as a heme b transporter (PubMed:20823265, PubMed:32973183). Required to regulate mitochondrial respiration processes, ATP synthesis and thermogenesis (PubMed:32973183). 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:Q91X85, ECO:0000269|PubMed:20823265, ECO:0000269|PubMed:32973183, ECO:0000269|PubMed:38302740, ECO:0000269|PubMed:38778100}.
uniprot
proteins
mass_dalton
57241
uniprot
proteins
mutagenesis
MUTAGEN 30..66; /note="HPSVSVHPSVSINPSVSVHPSSSAHPSALAQPSGLAH->APSVSVAPSVSINPSVSVAPSSSAAPSALAQPSGLAA: Loss of heme-binding activity."; /evidence="ECO:0000269|PubMed:32973183"; MUTAGEN 102; /note="W->A: Reduced transport of choline and ethanolamine."; /evidence="ECO:0000269|PubMed:38778100"; MUTAGEN 191; /note="Q->A: Reduced transport of choline and ethanolamine."; /evidence="ECO:0000269|PubMed:38778100"; MUTAGEN 222; /note="N->A: Reduced transport of choline and ethanolamine."; /evidence="ECO:0000269|PubMed:38778100"; MUTAGEN 325; /note="Y->A: Slightly reduced transport of choline and ethanolamine."; /evidence="ECO:0000269|PubMed:38778100"; MUTAGEN 447; /note="Q->A: Reduced transport of choline and ethanolamine."; /evidence="ECO:0000269|PubMed:38778100
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
12508121
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14729055
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
20206334
uniprot
proteins
pubmed
20518025
uniprot
proteins
pubmed
20690116
uniprot
proteins
pubmed
20823265
uniprot
proteins
pubmed
25677735
uniprot
proteins
pubmed
32973183
uniprot
proteins
pubmed
38302740
uniprot
proteins
pubmed
38778100
uniprot
proteins
pubmed
40972734
uniprot
proteins
sequence_length
526
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14729055, ECO:0000269|PubMed:38302740, ECO:0000269|PubMed:38778100}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:32973183}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:32973183}; 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 (PubMed:32973183). Colocalizes with ATP2A2 at the mitochondrial-ER contact junction (PubMed:32973183). {ECO:0000250|UniProtKB:Q91X85, ECO:0000269|PubMed:32973183}.
uniprot
proteins
transmembrane_region
TRANSMEM 77..101; /note="Helical; Name=TM1"; /evidence="ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCX, ECO:0007744|PDB:8QCY, ECO:0007744|PDB:8QD0"; TRANSMEM 120..147; /note="Helical; Name=TM2"; /evidence="ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCX, ECO:0007744|PDB:8QCY, ECO:0007744|PDB:8QD0"; TRANSMEM 150..169; /note="Helical; Name=TM3"; /evidence="ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCX, ECO:0007744|PDB:8QCY, ECO:0007744|PDB:8QD0"; TRANSMEM 177..205; /note="Helical; Name=TM4"; /evidence="ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCX, ECO:0007744|PDB:8QCY, ECO:0007744|PDB:8QD0"; TRANSMEM 211..236; /note="Helical; Name=TM5"; /evidence="ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCX, ECO:0007744|PDB:8QCY, ECO:0007744|PDB:8QD0"; TRANSMEM 242..271; /note="Helical; Name=TM6"; /evidence="ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCX, ECO:0007744|PDB:8QCY, ECO:0007744|PDB:8QD0"; TRANSMEM 308..338; /note="Helical; Name=TM7"; /evidence="ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCX, ECO:0007744|PDB:8QCY, ECO:0007744|PDB:8QD0"; TRANSMEM 343..371; /note="Helical; Name=TM8"; /evidence="ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCX, ECO:0007744|PDB:8QCY, ECO:0007744|PDB:8QD0"; TRANSMEM 374..396; /note="Helical; Name=TM9"; /evidence="ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCX, ECO:0007744|PDB:8QCY, ECO:0007744|PDB:8QD0"; TRANSMEM 400..429; /note="Helical; Name=TM10"; /evidence="ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCX, ECO:0007744|PDB:8QCY, ECO:0007744|PDB:8QD0"; TRANSMEM 438..463; /note="Helical; Name=TM11"; /evidence="ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCX, ECO:0007744|PDB:8QCY, ECO:0007744|PDB:8QD0"; TRANSMEM 466..488; /note="Helical; Name=TM12"; /evidence="ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCX, ECO:0007744|PDB:8QCY, ECO:0007744|PDB:8QD0
uniprot
proteins