XPR1_HUMAN
ID XPR1_HUMAN Reviewed; 696 AA.
AC Q9UBH6; O95719; Q7L8K9; Q8IW20; Q9NT19; Q9UFB9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Xenotropic and polytropic retrovirus receptor 1;
DE AltName: Full=Protein SYG1 homolog;
DE AltName: Full=Xenotropic and polytropic murine leukemia virus receptor X3;
DE Short=X-receptor;
GN Name=XPR1; Synonyms=SYG1, XR;
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).
RX PubMed=9988277; DOI=10.1038/6005;
RA Yang Y.-L., Guo L., Xu S., Holland C.A., Kitamura T., Hunter K.,
RA Cunningham J.M.;
RT "Receptors for polytropic and xenotropic mouse leukaemia viruses encoded by
RT a single gene at Rmc1.";
RL Nat. Genet. 21:216-219(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Lymphocyte;
RX PubMed=9927670; DOI=10.1073/pnas.96.3.927;
RA Tailor C.S., Nouri A., Lee C.G., Kozak C., Kabat D.;
RT "Cloning and characterization of a cell surface receptor for xenotropic and
RT polytropic murine leukemia viruses.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:927-932(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND VARIANT ALA-491.
RC TISSUE=Cervix carcinoma;
RX PubMed=9990033; DOI=10.1073/pnas.96.4.1385;
RA Battini J.-L., Rasko J.E.J., Miller A.D.;
RT "A human cell-surface receptor for xenotropic and polytropic murine
RT leukemia viruses: possible role in G protein-coupled signal transduction.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1385-1390(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-696 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-690, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668 AND THR-690, AND
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 THR-690, AND IDENTIFICATION BY
RP 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 [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23791524; DOI=10.1016/j.celrep.2013.05.035;
RA Giovannini D., Touhami J., Charnet P., Sitbon M., Battini J.L.;
RT "Inorganic phosphate export by the retrovirus receptor XPR1 in metazoans.";
RL Cell Rep. 3:1866-1873(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668, 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 [14]
RP FUNCTION, INVOLVEMENT IN IBGC6, VARIANTS IBGC6 ASN-136; PRO-140; PRO-145
RP AND SER-218, AND CHARACTERIZATION OF VARIANTS IBGC6 ASN-136; PRO-140;
RP PRO-145 AND SER-218.
RX PubMed=25938945; DOI=10.1038/ng.3289;
RA Legati A., Giovannini D., Nicolas G., Lopez-Sanchez U., Quintans B.,
RA Oliveira J.R., Sears R.L., Ramos E.M., Spiteri E., Sobrido M.J.,
RA Carracedo A., Castro-Fernandez C., Cubizolle S., Fogel B.L., Goizet C.,
RA Jen J.C., Kirdlarp S., Lang A.E., Miedzybrodzka Z., Mitarnun W., Paucar M.,
RA Paulson H., Pariente J., Richard A.C., Salins N.S., Simpson S.A.,
RA Striano P., Svenningsson P., Tison F., Unni V.K., Vanakker O.,
RA Wessels M.W., Wetchaphanphesat S., Yang M., Boller F., Campion D.,
RA Hannequin D., Sitbon M., Geschwind D.H., Battini J.L., Coppola G.;
RT "Mutations in XPR1 cause primary familial brain calcification associated
RT with altered phosphate export.";
RL Nat. Genet. 47:579-581(2015).
RN [15] {ECO:0007744|PDB:5IJH}
RP X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF 1-207, DOMAIN, AND FUNCTION.
RX PubMed=27080106; DOI=10.1126/science.aad9858;
RA Wild R., Gerasimaite R., Jung J.Y., Truffault V., Pavlovic I., Schmidt A.,
RA Saiardi A., Jessen H.J., Poirier Y., Hothorn M., Mayer A.;
RT "Control of eukaryotic phosphate homeostasis by inositol polyphosphate
RT sensor domains.";
RL Science 352:986-990(2016).
CC -!- FUNCTION: Plays a role in phosphate homeostasis. Mediates phosphate
CC export from the cell (PubMed:23791524, PubMed:25938945). Binds inositol
CC hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as
CC 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important
CC intracellular signaling molecules (PubMed:27080106).
CC {ECO:0000250|UniProtKB:Q9Z0U0, ECO:0000269|PubMed:23791524,
CC ECO:0000269|PubMed:25938945, ECO:0000269|PubMed:27080106}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23791524};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UBH6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBH6-2; Sequence=VSP_030748;
CC -!- TISSUE SPECIFICITY: Widely expressed. Detected in spleen, lymph node,
CC thymus, leukocytes, bone marrow, heart, kidney, pancreas and skeletal
CC muscle. {ECO:0000269|PubMed:9927670, ECO:0000269|PubMed:9990033}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal liver.
CC {ECO:0000269|PubMed:9927670, ECO:0000269|PubMed:9990033}.
CC -!- DOMAIN: The SPX domain has high affinity for inositol polyphosphates,
CC such as myo-inositol hexakisphosphate and 5-diphospho-myo-inositol
CC pentakisphosphate (5-InsP7). Its affinity for inorganic phosphate is
CC tow to three orders of magnitude lower. {ECO:0000269|PubMed:27080106}.
CC -!- DISEASE: Basal ganglia calcification, idiopathic, 6 (IBGC6)
CC [MIM:616413]: A form of basal ganglia calcification, an autosomal
CC dominant condition characterized by symmetric calcification in the
CC basal ganglia and other brain regions. Affected individuals can either
CC be asymptomatic or show a wide spectrum of neuropsychiatric symptoms,
CC including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis,
CC seizures, and chronic headache. Serum levels of calcium, phosphate,
CC alkaline phosphatase and parathyroid hormone are normal. The
CC neuropathological hallmark of the disease is vascular and pericapillary
CC calcification, mainly of calcium phosphate, in the affected brain
CC areas. {ECO:0000269|PubMed:25938945}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family. {ECO:0000305}.
CC -!- CAUTION: It is unclear whether its ability to act as a receptor for
CC xenotropic and polytropic murine leukemia retroviruses is relevant in
CC vivo and whether such viruses can infect human. {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; AF115389; AAD17211.1; -; mRNA.
DR EMBL; AF089744; AAD10196.1; -; mRNA.
DR EMBL; AF099082; AAD08928.1; -; mRNA.
DR EMBL; AL590085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91086.1; -; Genomic_DNA.
DR EMBL; BC041142; AAH41142.1; -; mRNA.
DR EMBL; AL133058; CAB61383.1; -; mRNA.
DR EMBL; AL137583; CAB70825.1; -; mRNA.
DR CCDS; CCDS1340.1; -. [Q9UBH6-1]
DR CCDS; CCDS44284.1; -. [Q9UBH6-2]
DR PIR; T42660; T42660.
DR RefSeq; NP_001129141.1; NM_001135669.1. [Q9UBH6-2]
DR RefSeq; NP_004727.2; NM_004736.3. [Q9UBH6-1]
DR PDB; 5IJH; X-ray; 2.43 A; A/B=1-207.
DR PDBsum; 5IJH; -.
DR AlphaFoldDB; Q9UBH6; -.
DR SMR; Q9UBH6; -.
DR BioGRID; 114647; 117.
DR IntAct; Q9UBH6; 43.
DR MINT; Q9UBH6; -.
DR STRING; 9606.ENSP00000356562; -.
DR TCDB; 2.A.94.1.6; the phosphate permease (pho1) family.
DR iPTMnet; Q9UBH6; -.
DR PhosphoSitePlus; Q9UBH6; -.
DR BioMuta; XPR1; -.
DR DMDM; 74753221; -.
DR EPD; Q9UBH6; -.
DR jPOST; Q9UBH6; -.
DR MassIVE; Q9UBH6; -.
DR MaxQB; Q9UBH6; -.
DR PaxDb; Q9UBH6; -.
DR PeptideAtlas; Q9UBH6; -.
DR PRIDE; Q9UBH6; -.
DR ProteomicsDB; 83970; -. [Q9UBH6-1]
DR ProteomicsDB; 83971; -. [Q9UBH6-2]
DR Antibodypedia; 20589; 195 antibodies from 29 providers.
DR DNASU; 9213; -.
DR Ensembl; ENST00000367589.3; ENSP00000356561.3; ENSG00000143324.14. [Q9UBH6-2]
DR Ensembl; ENST00000367590.9; ENSP00000356562.4; ENSG00000143324.14. [Q9UBH6-1]
DR GeneID; 9213; -.
DR KEGG; hsa:9213; -.
DR MANE-Select; ENST00000367590.9; ENSP00000356562.4; NM_004736.4; NP_004727.2.
DR UCSC; uc001goi.4; human. [Q9UBH6-1]
DR CTD; 9213; -.
DR DisGeNET; 9213; -.
DR GeneCards; XPR1; -.
DR GeneReviews; XPR1; -.
DR HGNC; HGNC:12827; XPR1.
DR HPA; ENSG00000143324; Low tissue specificity.
DR MalaCards; XPR1; -.
DR MIM; 605237; gene.
DR MIM; 616413; phenotype.
DR neXtProt; NX_Q9UBH6; -.
DR OpenTargets; ENSG00000143324; -.
DR Orphanet; 1980; Bilateral striopallidodentate calcinosis.
DR PharmGKB; PA37420; -.
DR VEuPathDB; HostDB:ENSG00000143324; -.
DR eggNOG; KOG1162; Eukaryota.
DR GeneTree; ENSGT00500000044895; -.
DR HOGENOM; CLU_006116_3_0_1; -.
DR InParanoid; Q9UBH6; -.
DR OMA; GNWTEAR; -.
DR PhylomeDB; Q9UBH6; -.
DR TreeFam; TF314643; -.
DR PathwayCommons; Q9UBH6; -.
DR SignaLink; Q9UBH6; -.
DR BioGRID-ORCS; 9213; 61 hits in 1086 CRISPR screens.
DR ChiTaRS; XPR1; human.
DR GenomeRNAi; 9213; -.
DR Pharos; Q9UBH6; Tbio.
DR PRO; PR:Q9UBH6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UBH6; protein.
DR Bgee; ENSG00000143324; Expressed in cortical plate and 190 other tissues.
DR ExpressionAtlas; Q9UBH6; baseline and differential.
DR Genevisible; Q9UBH6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IDA:UniProtKB.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0001618; F:virus receptor activity; IMP:UniProtKB.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; IMP:UniProtKB.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0006817; P:phosphate ion transport; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR InterPro; IPR004342; EXS_C.
DR InterPro; IPR004331; SPX_dom.
DR Pfam; PF03124; EXS; 1.
DR Pfam; PF03105; SPX; 3.
DR PROSITE; PS51380; EXS; 1.
DR PROSITE; PS51382; SPX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Host cell receptor for virus entry; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..696
FT /note="Xenotropic and polytropic retrovirus receptor 1"
FT /id="PRO_0000315853"
FT TOPO_DOM 1..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..345
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497..507
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 529..696
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..177
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT DOMAIN 439..643
FT /note="EXS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00712"
FT REGION 158..165
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P43585"
FT REGION 673..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 22
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000305|PubMed:27080106"
FT SITE 26
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000305|PubMed:27080106"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 690
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT VAR_SEQ 437..501
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030748"
FT VARIANT 136
FT /note="S -> N (in IBGC6; phosphate efflux is impaired;
FT present at the plasma membrane; dbSNP:rs786205902)"
FT /evidence="ECO:0000269|PubMed:25938945"
FT /id="VAR_073840"
FT VARIANT 140
FT /note="L -> P (in IBGC6; phosphate efflux is impaired;
FT present at the plasma membrane; dbSNP:rs786205903)"
FT /evidence="ECO:0000269|PubMed:25938945"
FT /id="VAR_073841"
FT VARIANT 145
FT /note="L -> P (in IBGC6; dominant negative; phosphate
FT efflux is impaired; loss of localization to the plasma
FT membrane; dbSNP:rs786205901)"
FT /evidence="ECO:0000269|PubMed:25938945"
FT /id="VAR_073842"
FT VARIANT 218
FT /note="L -> S (in IBGC6; present at the plasma membrane;
FT phosphate efflux is impaired; dbSNP:rs786205904)"
FT /evidence="ECO:0000269|PubMed:25938945"
FT /id="VAR_073843"
FT VARIANT 491
FT /note="T -> A (in dbSNP:rs1061012)"
FT /evidence="ECO:0000269|PubMed:9990033"
FT /id="VAR_038350"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:5IJH"
FT HELIX 13..18
FT /evidence="ECO:0007829|PDB:5IJH"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:5IJH"
FT HELIX 44..98
FT /evidence="ECO:0007829|PDB:5IJH"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:5IJH"
FT HELIX 125..167
FT /evidence="ECO:0007829|PDB:5IJH"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:5IJH"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:5IJH"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:5IJH"
FT HELIX 191..204
FT /evidence="ECO:0007829|PDB:5IJH"
SQ SEQUENCE 696 AA; 81535 MW; B5B4BABF5CA2503A CRC64;
MKFAEHLSAH ITPEWRKQYI QYEAFKDMLY SAQDQAPSVE VTDEDTVKRY FAKFEEKFFQ
TCEKELAKIN TFYSEKLAEA QRRFATLQNE LQSSLDAQKE STGVTTLRQR RKPVFHLSHE
ERVQHRNIKD LKLAFSEFYL SLILLQNYQN LNFTGFRKIL KKHDKILETS RGADWRVAHV
EVAPFYTCKK INQLISETEA VVTNELEDGD RQKAMKRLRV PPLGAAQPAP AWTTFRVGLF
CGIFIVLNIT LVLAAVFKLE TDRSIWPLIR IYRGGFLLIE FLFLLGINTY GWRQAGVNHV
LIFELNPRSN LSHQHLFEIA GFLGILWCLS LLACFFAPIS VIPTYVYPLA LYGFMVFFLI
NPTKTFYYKS RFWLLKLLFR VFTAPFHKVG FADFWLADQL NSLSVILMDL EYMICFYSLE
LKWDESKGLL PNNSEESGIC HKYTYGVRAI VQCIPAWLRF IQCLRRYRDT KRAFPHLVNA
GKYSTTFFMV TFAALYSTHK ERGHSDTMVF FYLWIVFYII SSCYTLIWDL KMDWGLFDKN
AGENTFLREE IVYPQKAYYY CAIIEDVILR FAWTIQISIT STTLLPHSGD IIATVFAPLE
VFRRFVWNFF RLENEHLNNC GEFRAVRDIS VAPLNADDQT LLEQMMDQDD GVRNRQKNRS
WKYNQSISLR RPRLASQSKA RDTKVLIEDT DDEANT
