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 23-FEB-2022, entry version 155. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q9Y5Y0; -. DR BioGRID; 118803; 87. DR IntAct; Q9Y5Y0; 26. 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; 178 antibodies from 32 providers. DR DNASU; 28982; -. DR Ensembl; ENST00000366971; ENSP00000355938; ENSG00000162769. 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; EKPQYPP; -. 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; 24 hits in 1051 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 202 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 //