FLVC1_MUSTR
ID FLVC1_MUSTR Reviewed; 560 AA.
AC Q9ES43;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Feline leukemia virus subgroup C receptor-related protein 1;
GN Name=Flvcr1;
OS Mus terricolor (Earth-colored mouse) (Mus dunni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=254704;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11000257; DOI=10.1128/jvi.74.20.9797-9801.2000;
RA Tailor C.S., Nouri A., Kabat D.;
RT "Cellular and species resistance to murine amphotropic, gibbon ape, and
RT feline subgroup C leukemia viruses is strongly influenced by receptor
RT expression levels and by receptor masking mechanisms.";
RL J. Virol. 74:9797-9801(2000).
CC -!- FUNCTION: Heme transporter that exports cytoplasmic heme. It can also
CC export coproporphyrin and protoporphyrin IX, which are both
CC intermediate products in the heme biosynthetic pathway. Does not export
CC bilirubin. Heme export depends on the presence of HPX and is required
CC to maintain intracellular free heme balance, protecting cells from heme
CC toxicity. Heme export provides protection from heme or ferrous iron
CC toxicities in liver, brain, sensory neurons and during erythtopoiesis,
CC a process in which heme synthesis intensifies. Causes susceptibility to
CC FeLV-C in vitro. {ECO:0000250|UniProtKB:B2RXV4,
CC ECO:0000250|UniProtKB:Q9Y5Y0}.
CC -!- SUBUNIT: Interacts with HPX. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: N-Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Feline
CC leukemia virus subgroup C receptor (TC 2.A.1.28.1) family.
CC {ECO:0000305}.
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DR EMBL; AF239767; AAG21946.1; -; mRNA.
DR AlphaFoldDB; Q9ES43; -.
DR SMR; Q9ES43; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Erythrocyte maturation; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..560
FT /note="Feline leukemia virus subgroup C receptor-related
FT protein 1"
FT /id="PRO_0000084845"
FT TOPO_DOM 1..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..280
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..377
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..437
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..496
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Y0"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 560 AA; 60584 MW; 573F404F590B7D9F CRC64;
MARPDDEVGP AVAPGHPLGK GYLPVPKGAP DGEARLVPQN GPEALNGGPV LDPLVAGAQD
GPQALIAAEE ETQARLLPAG DGEDVPCPAC PPRTALSPRR FVVLLIFSLY SLVNAFQWIQ
YSSISNVFED FYEVSPLHIN WLSMVYMVAY VPLIFPATWL LDTRGLRLTA LLGSGLNCLG
AWVKCGSVQR HLFWVTMLGQ ILCSVAQVFI LGLPSPVASV WFGPKEVSTA CATAVLGNQL
GTAVGFLLPP VLVPALGTQN NTGLLAHTQN NTDLLAHNIN TMFYGTAFIS TFLFFLTVIA
FKEKPPLPPS QAQAILRDSP PEEYSYKSSI WNLCRNIPFV LLLVSYGIMT GAFYSISTLL
NQIILTYYVG EEVNAGRIGL TLVVAGMVGS ILCGLWLDYT KTYKQTTLIV YVLSFIGMLI
FTFTLNLGYI VALFFTGGIL GFFMTGYLPL GFEFAVEITY PESEGMSSGL LNTAAQILGI
FFTLAQGKIT TDYNSPEAGN IFLCAWMFVG IILTALIKSD LRRHNINTGL TNIDVKAVPV
DSRVDPKPKA MVSIQSESSL
