FLVC1_FELCA
ID FLVC1_FELCA Reviewed; 560 AA.
AC Q9N1F2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Feline leukemia virus subgroup C receptor-related protein 1;
GN Name=FLVCR1;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION OF FELV-C RECEPTOR
RP FUNCTION.
RC TISSUE=T-cell;
RX PubMed=10648427;
RA Quigley J.G., Burns C.C., Anderson M.M., Lynch E.D., Sabo K.M.,
RA Overbaugh J., Abkowitz J.L.;
RT "Cloning of the cellular receptor for feline leukemia virus subgroup C
RT (FeLV-C), a retrovirus that induces red cell aplasia.";
RL Blood 95:1093-1099(2000).
RN [2]
RP ERRATUM OF PUBMED:10648427.
RA Quigley J.G., Burns C.C., Anderson M.M., Lynch E.D., Sabo K.M.,
RA Overbaugh J., Abkowitz J.L.;
RL Blood 96:8-8(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 (By similarity). Confers
CC susceptibility to Feline leukemia virus subgroup C (FeLV-C) infection,
CC which is associated with fatal erythroid aplasia, also known as
CC aplastic anemia (PubMed:10648427). {ECO:0000250|UniProtKB:Q9Y5Y0,
CC ECO:0000269|PubMed:10648427}.
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; AF192387; AAF37351.1; -; mRNA.
DR RefSeq; NP_001009302.1; NM_001009302.1.
DR AlphaFoldDB; Q9N1F2; -.
DR SMR; Q9N1F2; -.
DR STRING; 9685.ENSFCAP00000000192; -.
DR TCDB; 2.A.1.28.7; the major facilitator superfamily (mfs).
DR Ensembl; ENSFCAT00000000207; ENSFCAP00000000192; ENSFCAG00000000207.
DR GeneID; 493854; -.
DR KEGG; fca:493854; -.
DR CTD; 28982; -.
DR VGNC; VGNC:97439; FLVCR1.
DR eggNOG; KOG2563; Eukaryota.
DR GeneTree; ENSGT01030000234625; -.
DR HOGENOM; CLU_023132_0_0_1; -.
DR InParanoid; Q9N1F2; -.
DR OrthoDB; 702737at2759; -.
DR Proteomes; UP000011712; Chromosome F1.
DR Bgee; ENSFCAG00000000207; Expressed in embryonic head and 10 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0015232; F:heme transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0030218; P:erythrocyte differentiation; IBA:GO_Central.
DR GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR GO; GO:0060323; P:head morphogenesis; IEA:Ensembl.
DR GO; GO:0097037; P:heme export; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006839; P:mitochondrial transport; IBA:GO_Central.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0046620; P:regulation of organ growth; IEA:Ensembl.
DR GO; GO:0048536; P:spleen development; IEA:Ensembl.
DR Gene3D; 1.20.1250.20; -; 2.
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 1: Evidence at protein level;
KW Cell membrane; Erythrocyte maturation; Glycoprotein;
KW Host cell receptor for virus entry; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..560
FT /note="Feline leukemia virus subgroup C receptor-related
FT protein 1"
FT /id="PRO_0000084843"
FT TOPO_DOM 1..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..147
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..372
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..432
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..490
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Y0"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Y0"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 560 AA; 60422 MW; 2A289B5AFE45EE5A CRC64;
MVKLNDEEGA AMAPGHQPTN GYLLVPGGEP PGKVSAELQN GPKAVCLTLN GVSRDSLAAA
AEALCRPQTP LAPEEETQTR LLPTGPGEET PGTEGSPAPQ TALSARRFVV LLIFSLYSLV
NAFQWIQYSV ISNVFEGFYG VSSLHIDWLS MVYMLAYVPL IFPATWLLDT RGLRLTALLG
SGLNCLGAWV KCASVQQHLF WVTMLGQCLC SVAQVFILGL PSRIASVWFG PKEVSTACAT
AVLGNQLGAA IGFLLPPVLV PNTQNNTDLL ACNISTMFYG TSSVATFLCF LTIIAFKEKP
QYPPSQAQAA LQNSPPAKYS YKKSIRNLFR NVPFVLLLIT YGIITGAFYS VSTLLNQMIL
TYYKGEEVSA GKIGLTLVVA GMVGSILCGF WLDYTKIYKQ TTLIVYILSF LGMVIFTFTL
DLGYGIVVFV TGGVLGFFMT GYLPLGFEFA VEITYPESEG TSSGLLNAAA QIFGILFTLA
QGKLTTDYSP KAGNIFLCVW LFLGIILTAL IKSDLRRHNI NIGIANGDIK AVPVEDTVED
SPTDKESKTI VMSKQSESAI
