FLVCR1
entrez
28982
canonical
uniprot
Q9Y5Y0
canonical
ensembl
ENSG00000162769
resolver
ensp
ENSP00000355938
resolver
ensp
ENSP00000700306
resolver
ensp
ENSP00000733862
resolver
genesymbol
FLVCR1
resolver
genesymbol_syn
FLVCR
resolver
hgnc
HGNC:24682
resolver
uniprot
B2RB38
resolver
uniprot
Q1HE16
resolver
uniprot
Q86XY9
resolver
uniprot
Q9NVR9
resolver
uniprot_entry
B2RB38_HUMAN
resolver
uniprot_entry
FLVC1_HUMAN
resolver
uniprot_sec
Q1HE16
resolver
uniprot_sec
Q86XY9
resolver
uniprot_sec
Q9NVR9
resolver
amino_acid_sequence
MARPDDEEGAAVAPGHPLAKGYLPLPRGAPVGKESVELQNGPKAGTFPVNGAPRDSLAAASGVLGGPQTPLAPEEETQARLLPAGAGAETPGAESSPLPLTALSPRRFVVLLIFSLYSLVNAFQWIQYSIISNVFEGFYGVTLLHIDWLSMVYMLAYVPLIFPATWLLDTRGLRLTALLGSGLNCLGAWIKCGSVQQHLFWVTMLGQCLCSVAQVFILGLPSRIASVWFGPKEVSTACATAVLGNQLGTAVGFLLPPVLVPNTQNDTNLLACNISTMFYGTSAVATLLFILTAIAFKEKPRYPPSQAQAALQDSPPEEYSYKKSIRNLFKNIPFVLLLITYGIMTGAFYSVSTLLNQMILTYYEGEEVNAGRIGLTLVVAGMVGSILCGLWLDYTKTYKQTTLIVYILSFIGMVIFTFTLDLRYIIIVFVTGGVLGFFMTGYLPLGFEFAVEITYPESEGTSSGLLNASAQIFGILFTLAQGKLTSDYGPKAGNIFLCVWMFIGIILTALIKSDLRRHNINIGITNVDVKAIPADSPTDQEPKTVMLSKQSESAI
uniprot
proteins
disease_involvement
DISEASE: Retinopathy-sensory neuropathy syndrome (RETSNS) [MIM:609033]: An autosomal recessive neurodegenerative syndrome beginning in infancy with areflexia and retinitis pigmentosa. Nyctalopia (night blindness) and peripheral visual field loss are usually evident during late childhood or teenage years, with subsequent progressive constriction of the visual fields and loss of central retinal function over time. A sensory ataxia caused by degeneration of the posterior columns of the spinal cord results in a loss of proprioceptive sensation that is clinically evident in the second decade of life and gradually progresses. Scoliosis, camptodactyly, achalasia, gastrointestinal dysmotility, and a sensory peripheral neuropathy are variable features of the disease. Affected individuals have no clinical or radiological evidence of cerebral or cerebellar involvement. Some patients have pain insensitivity and commonly manifest self-injury, ulcers and amputations. {ECO:0000269|PubMed:21070897, ECO:0000269|PubMed:21267618, ECO:0000269|PubMed:22483575, ECO:0000269|PubMed:27923065, ECO:0000269|PubMed:28766925, ECO:0000269|PubMed:30444160, ECO:0000269|PubMed:39306721}. Note=The disease is caused by variants affecting the gene represented in this entry. Defective neuronal heme transmembrane export due to FLVCR1 mutations may abrogate the neuroprotective effects of neuroglobin and initiate an apoptotic cascade that results in the selective degeneration of photoreceptors in the neurosensory retina and sensory neurons in the posterior spinal cord. {ECO:0000269|PubMed:21070897}.; DISEASE: Neurodevelopmental disorder with microcephaly, absent speech, and hypotonia (NEDMISH) [MIM:621060]: A severe, autosomal recessive disorder characterized by profound global developmental delay, impaired intellectual development, absent speech, microcephaly, brain malformations, epilepsy, spasticity, and premature death. Brain malformations range from mild brain volume reduction to hydranencephaly. Additional features may include cortical visual impairment, sensory neuropathy, limb and digital malformations, and macrocytic anemia. {ECO:0000269|PubMed:39306721}. Note=The disease is caused by variants affecting the gene represented in this entry.
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, PubMed:38693265, PubMed:38778100, PubMed:39306721, PubMed:40972734). Choline and ethanolamine are the precursors of phosphatidylcholine and phosphatidylethanolamine, respectively, the two most abundant phospholipids (PubMed:38693265, PubMed:38778100). Transport is not coupled with proton transport and is exclusively driven by the choline (or ethanolamine) gradient across the plasma membrane (PubMed:38693265, PubMed:38778100). Also acts as a heme b transporter that mediates heme efflux from the cytoplasm to the extracellular compartment (PubMed:15369674, PubMed:20610401, PubMed:22483575, PubMed:23187127, PubMed:27923065). {ECO:0000269|PubMed:15369674, ECO:0000269|PubMed:20610401, ECO:0000269|PubMed:22483575, ECO:0000269|PubMed:23187127, ECO:0000269|PubMed:27923065, ECO:0000269|PubMed:37100056, ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100, ECO:0000269|PubMed:39306721}.; FUNCTION: [Isoform 1]: Uniporter that mediates the transport of extracellular choline and ethanolamine into cells (PubMed:37100056, PubMed:38693265). Choline and ethanolamine are the precursors of phosphatidylcholine and phosphatidylethanolamine, respectively, the two most abundant phospholipids (PubMed:38693265). Transport is not coupled with proton transport and is exclusively driven by the choline (or ethanolamine) gradient across the plasma membrane (PubMed:38693265). Also acts as a heme b transporter that mediates heme efflux from the cytoplasm to the extracellular compartment (PubMed:15369674, PubMed:20610401, PubMed:22483575, PubMed:23187127, PubMed:27923065). Heme export depends on the presence of HPX and is required to maintain intracellular free heme balance, protecting cells from heme toxicity (PubMed:20610401). 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 (PubMed:20610401, PubMed:23187127). Possibly export coproporphyrin and protoporphyrin IX, which are both intermediate products in the heme biosynthetic pathway (PubMed:20610401). Does not export bilirubin (PubMed:20610401). The molecular mechanism of heme transport, whether electrogenic, electroneutral or coupled to other ions, remains to be elucidated (PubMed:20610401, PubMed:23187127). {ECO:0000269|PubMed:15369674, ECO:0000269|PubMed:20610401, ECO:0000269|PubMed:22483575, ECO:0000269|PubMed:23187127, ECO:0000269|PubMed:27923065, ECO:0000269|PubMed:37100056, ECO:0000269|PubMed:38693265}.; FUNCTION: [Isoform 2]: Heme b transporter that promotes heme efflux from the mitochondrion to the cytoplasm. Essential for erythroid differentiation. {ECO:0000269|PubMed:23187127}.; FUNCTION: [Isoform 1]: (Microbial infection) Confers susceptibility to feline leukemia virus subgroup C (FeLV-C) infection in vitro. {ECO:0000269|PubMed:10400745}.
uniprot
proteins
mass_dalton
59863
uniprot
proteins
mutagenesis
MUTAGEN 125; /note="W->A: Reduced transport of choline and ethanolamine."; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100"; MUTAGEN 151; /note="M->V: No effect on choline transmembrane transporter activity. No effect on ethanolamine transmembrane transporter activity."; /evidence="ECO:0000269|PubMed:39306721"; MUTAGEN 153; /note="Y->A: Reduced transport of choline and ethanolamine."; /evidence="ECO:0000269|PubMed:38693265"; MUTAGEN 214; /note="Q->A: Reduced transport of choline and nearly abolished transport of ethanolamine."; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100"; MUTAGEN 245; /note="N->A: Slightly reduced transport of choline and ethanolamine."; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100"; MUTAGEN 349; /note="Y->A: Reduced transport of choline and ethanolamine."; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100"; MUTAGEN 443; /note="L->P: Decreased choline and ethanolamine transmembrane transporter activity."; /evidence="ECO:0000269|PubMed:39306721"; MUTAGEN 471; /note="Q->A: Slightly reduced transport of choline and ethanolamine."; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100
uniprot
proteins
post_translational_modification
PTM: N-Glycosylated. {ECO:0000269|PubMed:16439531}.
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
10400745
uniprot
proteins
pubmed
11943475
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15369674
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16439531
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20610401
uniprot
proteins
pubmed
21070897
uniprot
proteins
pubmed
21267618
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22483575
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23187127
uniprot
proteins
pubmed
27923065
uniprot
proteins
pubmed
28766925
uniprot
proteins
pubmed
30444160
uniprot
proteins
pubmed
37100056
uniprot
proteins
pubmed
38693265
uniprot
proteins
pubmed
38778100
uniprot
proteins
pubmed
39306721
uniprot
proteins
pubmed
40972734
uniprot
proteins
sequence_length
555
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:15369674, ECO:0000269|PubMed:22483575, ECO:0000269|PubMed:37100056, ECO:0000269|PubMed:38778100}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion membrane {ECO:0000269|PubMed:23187127}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 100..124; /note="Helical; Name=TM1"; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCS, ECO:0007744|PDB:8QCT, ECO:0007744|PDB:8R8T, ECO:0007744|PDB:8UBW, ECO:0007744|PDB:8UBX, ECO:0007744|PDB:8UBZ"; TRANSMEM 143..170; /note="Helical; Name=TM2"; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCS, ECO:0007744|PDB:8QCT, ECO:0007744|PDB:8R8T, ECO:0007744|PDB:8UBW, ECO:0007744|PDB:8UBX, ECO:0007744|PDB:8UBZ"; TRANSMEM 173..192; /note="Helical; Name=TM3"; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCS, ECO:0007744|PDB:8QCT, ECO:0007744|PDB:8R8T, ECO:0007744|PDB:8UBW, ECO:0007744|PDB:8UBX, ECO:0007744|PDB:8UBZ"; TRANSMEM 200..228; /note="Helical; Name=TM4"; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCS, ECO:0007744|PDB:8QCT, ECO:0007744|PDB:8R8T, ECO:0007744|PDB:8UBW, ECO:0007744|PDB:8UBX, ECO:0007744|PDB:8UBZ"; TRANSMEM 234..259; /note="Helical; Name=TM5"; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCS, ECO:0007744|PDB:8QCT, ECO:0007744|PDB:8R8T, ECO:0007744|PDB:8UBW, ECO:0007744|PDB:8UBX, ECO:0007744|PDB:8UBZ"; TRANSMEM 266..295; /note="Helical; Name=TM6"; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCS, ECO:0007744|PDB:8QCT, ECO:0007744|PDB:8R8T, ECO:0007744|PDB:8UBW, ECO:0007744|PDB:8UBX, ECO:0007744|PDB:8UBZ"; TRANSMEM 332..362; /note="Helical; Name=TM7"; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCS, ECO:0007744|PDB:8QCT, ECO:0007744|PDB:8R8T, ECO:0007744|PDB:8UBW, ECO:0007744|PDB:8UBX, ECO:0007744|PDB:8UBZ"; TRANSMEM 367..395; /note="Helical; Name=TM8"; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCS, ECO:0007744|PDB:8QCT, ECO:0007744|PDB:8R8T, ECO:0007744|PDB:8UBW, ECO:0007744|PDB:8UBX, ECO:0007744|PDB:8UBZ"; TRANSMEM 398..420; /note="Helical; Name=TM9"; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCS, ECO:0007744|PDB:8QCT, ECO:0007744|PDB:8R8T, ECO:0007744|PDB:8UBW, ECO:0007744|PDB:8UBX, ECO:0007744|PDB:8UBZ"; TRANSMEM 424..453; /note="Helical; Name=TM10"; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCS, ECO:0007744|PDB:8QCT, ECO:0007744|PDB:8R8T, ECO:0007744|PDB:8UBW, ECO:0007744|PDB:8UBX, ECO:0007744|PDB:8UBZ"; TRANSMEM 462..487; /note="Helical; Name=TM11"; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCS, ECO:0007744|PDB:8QCT, ECO:0007744|PDB:8R8T, ECO:0007744|PDB:8UBW, ECO:0007744|PDB:8UBX, ECO:0007744|PDB:8UBZ"; TRANSMEM 490..512; /note="Helical; Name=TM12"; /evidence="ECO:0000269|PubMed:38693265, ECO:0000269|PubMed:38778100, ECO:0007744|PDB:8QCS, ECO:0007744|PDB:8QCT, ECO:0007744|PDB:8R8T, ECO:0007744|PDB:8UBW, ECO:0007744|PDB:8UBX, ECO:0007744|PDB:8UBZ
uniprot
proteins