FLVC1_HUMAN
ID FLVC1_HUMAN Reviewed; 555 AA.
AC Q9Y5Y0; Q1HE16; Q86XY9; Q9NVR9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Feline leukemia virus subgroup C receptor-related protein 1;
DE Short=Feline leukemia virus subgroup C receptor;
DE Short=hFLVCR;
GN Name=FLVCR1; Synonyms=FLVCR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP CHARACTERIZATION OF FELV-C RECEPTOR FUNCTION.
RC TISSUE=Lymphocyte;
RX PubMed=10400745; DOI=10.1128/jvi.73.8.6500-6505.1999;
RA Tailor C.S., Willett B.J., Kabat D.;
RT "A putative cell surface receptor for anemia-inducing feline leukemia virus
RT subgroup C is a member of a transporter superfamily.";
RL J. Virol. 73:6500-6505(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS PRO-52 AND
RP MET-544.
RC TISSUE=Duodenum;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP GENE STRUCTURE.
RX PubMed=11943475; DOI=10.1016/s0378-1119(02)00457-2;
RA Lipovich L., Hughes A.L., King M.-C., Abkowitz J.L., Quigley J.G.;
RT "Genomic structure and evolutionary context of the human feline leukemia
RT virus subgroup C receptor (hFLVCR) gene: evidence for block duplications
RT and de novo gene formation within duplicons of the hFLVCR locus.";
RL Gene 286:203-213(2002).
RN [7]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15369674; DOI=10.1016/j.cell.2004.08.014;
RA Quigley J.G., Yang Z., Worthington M.T., Phillips J.D., Sabo K.M.,
RA Sabath D.E., Berg C.L., Sassa S., Wood B.L., Abkowitz J.L.;
RT "Identification of a human heme exporter that is essential for
RT erythropoiesis.";
RL Cell 118:757-766(2004).
RN [8]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION.
RX PubMed=16439531; DOI=10.1128/jvi.80.4.1742-1751.2006;
RA Brown J.K., Fung C., Tailor C.S.;
RT "Comprehensive mapping of receptor-functioning domains in feline leukemia
RT virus subgroup C receptor FLVCR1.";
RL J. Virol. 80:1742-1751(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP FUNCTION, AND INTERACTION WITH HPX.
RX PubMed=20610401; DOI=10.1074/jbc.m110.119131;
RA Yang Z., Philips J.D., Doty R.T., Giraudi P., Ostrow J.D., Tiribelli C.,
RA Smith A., Abkowitz J.L.;
RT "Kinetics and specificity of feline leukemia virus subgroup C receptor
RT (FLVCR) export function and its dependence on hemopexin.";
RL J. Biol. Chem. 285:28874-28882(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION (ISOFORM 2), AND SUBCELLULAR
RP LOCATION (ISOFORM 2).
RX PubMed=23187127; DOI=10.1172/jci62422;
RA Chiabrando D., Marro S., Mercurio S., Giorgi C., Petrillo S., Vinchi F.,
RA Fiorito V., Fagoonee S., Camporeale A., Turco E., Merlo G.R., Silengo L.,
RA Altruda F., Pinton P., Tolosano E.;
RT "The mitochondrial heme exporter FLVCR1b mediates erythroid
RT differentiation.";
RL J. Clin. Invest. 122:4569-4579(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP FUNCTION, INVOLVEMENT IN SENSORY NEUROPATHY, AND VARIANTS ARG-192 AND
RP SER-221.
RX PubMed=27923065; DOI=10.1371/journal.pgen.1006461;
RA Chiabrando D., Castori M., di Rocco M., Ungelenk M., Giesselmann S.,
RA Di Capua M., Madeo A., Grammatico P., Bartsch S., Huebner C.A., Altruda F.,
RA Silengo L., Tolosano E., Kurth I.;
RT "Mutations in the heme exporter FLVCR1 cause sensory neurodegeneration with
RT loss of pain perception.";
RL PLoS Genet. 12:E1006461-E1006461(2016).
RN [18]
RP VARIANTS PCARP ASP-121; ARG-192 AND THR-241.
RX PubMed=21070897; DOI=10.1016/j.ajhg.2010.10.013;
RA Rajadhyaksha A.M., Elemento O., Puffenberger E.G., Schierberl K.C.,
RA Xiang J.Z., Putorti M.L., Berciano J., Poulin C., Brais B., Michaelides M.,
RA Weleber R.G., Higgins J.J.;
RT "Mutations in FLVCR1 cause posterior column ataxia and retinitis
RT pigmentosa.";
RL Am. J. Hum. Genet. 87:643-654(2010).
RN [19]
RP VARIANT PCARP ARG-493.
RX PubMed=21267618; DOI=10.1007/s10048-010-0271-4;
RA Ishiura H., Fukuda Y., Mitsui J., Nakahara Y., Ahsan B., Takahashi Y.,
RA Ichikawa Y., Goto J., Sakai T., Tsuji S.;
RT "Posterior column ataxia with retinitis pigmentosa in a Japanese family
RT with a novel mutation in FLVCR1.";
RL Neurogenetics 12:117-121(2011).
CC -!- FUNCTION: [Isoform 1]: Heme transporter that exports cytoplasmic heme.
CC It can also 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:0000269|PubMed:10400745,
CC ECO:0000269|PubMed:15369674, ECO:0000269|PubMed:20610401,
CC ECO:0000269|PubMed:27923065}.
CC -!- FUNCTION: [Isoform 2]: Heme transporter that promotes heme efflux from
CC the mitochondrion to the cytoplasm. Essential for erythroid
CC differentiation.
CC -!- SUBUNIT: Interacts with HPX. {ECO:0000269|PubMed:20610401}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=FLVC1a;
CC IsoId=Q9Y5Y0-1; Sequence=Displayed;
CC Name=2; Synonyms=FLVC1b, mitochondrial;
CC IsoId=Q9Y5Y0-2; Sequence=VSP_047866;
CC -!- TISSUE SPECIFICITY: Found all hematopoietic tissues including
CC peripheral blood lymphocytes. Some expression is found in pancreas and
CC kidney. {ECO:0000269|PubMed:10400745}.
CC -!- DEVELOPMENTAL STAGE: Down-regulated in haemopoietic progenitor cells
CC undergoing differentiation and hemoglobinization. Abundant in fetal
CC liver. {ECO:0000269|PubMed:15369674}.
CC -!- PTM: N-Glycosylated. {ECO:0000269|PubMed:16439531}.
CC -!- DISEASE: Posterior column ataxia with retinitis pigmentosa (PCARP)
CC [MIM:609033]: A neurodegenerative syndrome beginning in infancy with
CC areflexia and retinitis pigmentosa. Nyctalopia (night blindness) and
CC peripheral visual field loss are usually evident during late childhood
CC or teenage years, with subsequent progressive constriction of the
CC visual fields and loss of central retinal function over time. A sensory
CC ataxia caused by degeneration of the posterior columns of the spinal
CC cord results in a loss of proprioceptive sensation that is clinically
CC evident in the second decade of life and gradually progresses.
CC Scoliosis, camptodactyly, achalasia, gastrointestinal dysmotility, and
CC a sensory peripheral neuropathy are variable features of the disease.
CC Affected individuals have no clinical or radiological evidence of
CC cerebral or cerebellar involvement. {ECO:0000269|PubMed:21070897,
CC ECO:0000269|PubMed:21267618}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. Defective neuronal heme
CC transmembrane export due to FLVCR1 mutations may abrogate the
CC neuroprotective effects of neuroglobin and initiate an apoptotic
CC cascade that results in the selective degeneration of photoreceptors in
CC the neurosensory retina and sensory neurons in the posterior spinal
CC cord.
CC -!- DISEASE: Note=Defects in FLVCR1 are a cause of a sensory neuropathy
CC resulting in pain insensitivity. Patients have decreased sensing of
CC pain, temperature and touch. Self-injury, ulcers and amputations are
CC commonly observed in affected individuals.
CC {ECO:0000269|PubMed:27923065}.
CC -!- MISCELLANEOUS: [Isoform 2]: Has a probable mitochondrial transit
CC peptide at positions 1-38. {ECO:0000305}.
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; AF118637; AAD45243.1; -; mRNA.
DR EMBL; AK001419; BAA91679.1; -; mRNA.
DR EMBL; DQ496107; ABF47096.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93374.1; -; Genomic_DNA.
DR EMBL; BC048312; AAH48312.1; -; mRNA.
DR CCDS; CCDS1510.1; -. [Q9Y5Y0-1]
DR RefSeq; NP_054772.1; NM_014053.3. [Q9Y5Y0-1]
DR AlphaFoldDB; Q9Y5Y0; -.
DR SMR; Q9Y5Y0; -.
DR BioGRID; 118803; 129.
DR IntAct; Q9Y5Y0; 28.
DR MINT; Q9Y5Y0; -.
DR STRING; 9606.ENSP00000355938; -.
DR TCDB; 2.A.1.28.1; the major facilitator superfamily (mfs).
DR GlyGen; Q9Y5Y0; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y5Y0; -.
DR PhosphoSitePlus; Q9Y5Y0; -.
DR BioMuta; FLVCR1; -.
DR DMDM; 46396053; -.
DR EPD; Q9Y5Y0; -.
DR jPOST; Q9Y5Y0; -.
DR MassIVE; Q9Y5Y0; -.
DR MaxQB; Q9Y5Y0; -.
DR PaxDb; Q9Y5Y0; -.
DR PeptideAtlas; Q9Y5Y0; -.
DR PRIDE; Q9Y5Y0; -.
DR ProteomicsDB; 86537; -. [Q9Y5Y0-1]
DR Antibodypedia; 20720; 180 antibodies from 32 providers.
DR DNASU; 28982; -.
DR Ensembl; ENST00000366971.9; ENSP00000355938.4; ENSG00000162769.13. [Q9Y5Y0-1]
DR GeneID; 28982; -.
DR KEGG; hsa:28982; -.
DR MANE-Select; ENST00000366971.9; ENSP00000355938.4; NM_014053.4; NP_054772.1.
DR UCSC; uc001hjt.3; human. [Q9Y5Y0-1]
DR CTD; 28982; -.
DR DisGeNET; 28982; -.
DR GeneCards; FLVCR1; -.
DR HGNC; HGNC:24682; FLVCR1.
DR HPA; ENSG00000162769; Tissue enhanced (intestine).
DR MalaCards; FLVCR1; -.
DR MIM; 609033; phenotype.
DR MIM; 609144; gene.
DR neXtProt; NX_Q9Y5Y0; -.
DR OpenTargets; ENSG00000162769; -.
DR Orphanet; 88628; Posterior column ataxia-retinitis pigmentosa syndrome.
DR PharmGKB; PA162388695; -.
DR VEuPathDB; HostDB:ENSG00000162769; -.
DR eggNOG; KOG2563; Eukaryota.
DR GeneTree; ENSGT01030000234625; -.
DR InParanoid; Q9Y5Y0; -.
DR OMA; TYYKGEE; -.
DR PhylomeDB; Q9Y5Y0; -.
DR TreeFam; TF314292; -.
DR PathwayCommons; Q9Y5Y0; -.
DR Reactome; R-HSA-189451; Heme biosynthesis.
DR Reactome; R-HSA-917937; Iron uptake and transport. [Q9Y5Y0-1]
DR SignaLink; Q9Y5Y0; -.
DR BioGRID-ORCS; 28982; 30 hits in 1083 CRISPR screens.
DR ChiTaRS; FLVCR1; human.
DR GeneWiki; FLVCR1; -.
DR GenomeRNAi; 28982; -.
DR Pharos; Q9Y5Y0; Tbio.
DR PRO; PR:Q9Y5Y0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y5Y0; protein.
DR Bgee; ENSG00000162769; Expressed in jejunal mucosa and 172 other tissues.
DR ExpressionAtlas; Q9Y5Y0; baseline and differential.
DR Genevisible; Q9Y5Y0; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0015232; F:heme transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
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; IDA:MGI.
DR GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR GO; GO:0060323; P:head morphogenesis; IEA:Ensembl.
DR GO; GO:0006783; P:heme biosynthetic process; TAS:Reactome.
DR GO; GO:0097037; P:heme export; IMP:UniProtKB.
DR GO; GO:0015886; P:heme transport; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006839; P:mitochondrial transport; IDA:MGI.
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; -; 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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disease variant;
KW Erythrocyte maturation; Glycoprotein; Membrane; Mitochondrion;
KW Neurodegeneration; Neuropathy; Phosphoprotein; Receptor;
KW Reference proteome; Retinitis pigmentosa; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..555
FT /note="Feline leukemia virus subgroup C receptor-related
FT protein 1"
FT /id="PRO_0000084844"
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..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..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..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..424
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..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..555
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
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"
FT VAR_SEQ 1..276
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_047866"
FT VARIANT 52
FT /note="A -> P (in dbSNP:rs11120047)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_050297"
FT VARIANT 121
FT /note="N -> D (in PCARP; dbSNP:rs267606820)"
FT /evidence="ECO:0000269|PubMed:21070897"
FT /id="VAR_065158"
FT VARIANT 192
FT /note="C -> R (in PCARP; also found in a patient with
FT sensory neuropathy and pain insensitivity;
FT dbSNP:rs267606821)"
FT /evidence="ECO:0000269|PubMed:21070897,
FT ECO:0000269|PubMed:27923065"
FT /id="VAR_065159"
FT VARIANT 221
FT /note="P -> S (probable disease-associated variant found in
FT a patient with sensory neuropathy and pain insensitivity;
FT dbSNP:rs753000469)"
FT /evidence="ECO:0000269|PubMed:27923065"
FT /id="VAR_077884"
FT VARIANT 241
FT /note="A -> T (in PCARP; dbSNP:rs267606819)"
FT /evidence="ECO:0000269|PubMed:21070897"
FT /id="VAR_065160"
FT VARIANT 493
FT /note="G -> R (in PCARP; dbSNP:rs1558121050)"
FT /evidence="ECO:0000269|PubMed:21267618"
FT /id="VAR_065161"
FT VARIANT 544
FT /note="T -> M (in dbSNP:rs3207090)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_050298"
SQ SEQUENCE 555 AA; 59863 MW; D0EBA9886CC8E747 CRC64;
MARPDDEEGA AVAPGHPLAK GYLPLPRGAP VGKESVELQN GPKAGTFPVN GAPRDSLAAA
SGVLGGPQTP LAPEEETQAR LLPAGAGAET PGAESSPLPL TALSPRRFVV LLIFSLYSLV
NAFQWIQYSI ISNVFEGFYG VTLLHIDWLS MVYMLAYVPL IFPATWLLDT RGLRLTALLG
SGLNCLGAWI KCGSVQQHLF WVTMLGQCLC SVAQVFILGL PSRIASVWFG PKEVSTACAT
AVLGNQLGTA VGFLLPPVLV PNTQNDTNLL ACNISTMFYG TSAVATLLFI LTAIAFKEKP
RYPPSQAQAA LQDSPPEEYS YKKSIRNLFK NIPFVLLLIT YGIMTGAFYS VSTLLNQMIL
TYYEGEEVNA GRIGLTLVVA GMVGSILCGL WLDYTKTYKQ TTLIVYILSF IGMVIFTFTL
DLRYIIIVFV TGGVLGFFMT GYLPLGFEFA VEITYPESEG TSSGLLNASA QIFGILFTLA
QGKLTSDYGP KAGNIFLCVW MFIGIILTAL IKSDLRRHNI NIGITNVDVK AIPADSPTDQ
EPKTVMLSKQ SESAI
