XPR1_DANRE
ID XPR1_DANRE Reviewed; 693 AA.
AC A8DZH4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Xenotropic and polytropic retrovirus receptor 1 homolog;
GN Name=xpr1; ORFNames=si:dkey-60b12.7;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
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).
CC -!- FUNCTION: Plays a role in phosphate homeostasis. Mediates phosphate
CC export from the cell (PubMed:23791524). Binds inositol hexakisphosphate
CC (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-
CC inositol pentakisphosphate (5-InsP7); these are important intracellular
CC signaling molecules (By similarity). {ECO:0000250|UniProtKB:Q9UBH6,
CC ECO:0000269|PubMed:23791524}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23791524};
CC Multi-pass membrane protein {ECO:0000305}.
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:0000250|UniProtKB:Q9UBH6}.
CC -!- SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family. {ECO:0000305}.
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DR EMBL; AL953893; CAP09231.1; -; Genomic_DNA.
DR RefSeq; NP_001119862.1; NM_001126390.1.
DR AlphaFoldDB; A8DZH4; -.
DR SMR; A8DZH4; -.
DR STRING; 7955.ENSDARP00000050596; -.
DR PaxDb; A8DZH4; -.
DR Ensembl; ENSDART00000050597; ENSDARP00000050596; ENSDARG00000029671.
DR GeneID; 558034; -.
DR KEGG; dre:558034; -.
DR CTD; 558034; -.
DR ZFIN; ZDB-GENE-060503-266; xpr1b.
DR eggNOG; KOG1162; Eukaryota.
DR GeneTree; ENSGT00940000164519; -.
DR HOGENOM; CLU_006116_3_0_1; -.
DR InParanoid; A8DZH4; -.
DR OMA; HETENIV; -.
DR OrthoDB; 536327at2759; -.
DR PhylomeDB; A8DZH4; -.
DR TreeFam; TF314643; -.
DR PRO; PR:A8DZH4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000029671; Expressed in retina and 23 other tissues.
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; ISS: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:0000822; F:inositol hexakisphosphate binding; ISS:UniProtKB.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IDA:ZFIN.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; ISS:UniProtKB.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IBA:GO_Central.
DR GO; GO:0030225; P:macrophage differentiation; IMP:ZFIN.
DR GO; GO:0014004; P:microglia differentiation; IMP:ZFIN.
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:0001501; P:skeletal system development; IMP:ZFIN.
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 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..693
FT /note="Xenotropic and polytropic retrovirus receptor 1
FT homolog"
FT /id="PRO_0000315860"
FT TOPO_DOM 1..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..267
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..477
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..506
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..560
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..693
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..176
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT DOMAIN 441..642
FT /note="EXS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00712"
FT REGION 157..164
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P43585"
FT REGION 674..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 22
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P43585"
FT SITE 26
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P43585"
SQ SEQUENCE 693 AA; 81281 MW; 5B5575CAD59DFF4D CRC64;
MKFTEHLSAH ITPEWRKQYI QYEAFKEMLY SAQDQAPSIE VTDEDTVKRY YAKFEEKFFQ
TCEKELAKIN TFYSEKLAEA QRRFATLQNE LQSSLDAQRE SSRAAGLRHR RTVFHLSQQE
RCKHRNIKDL QLAFSEFYLS LILLQNYQNL NFTGFRKILK KHDKIFETSR GADWRVAHVE
VAPFYTCKKI TQLISETETL VTTELEGGDR QKAMKRLRVP PLGAAQPAPA WTTFRVGLYC
GVFVALTVTV IIAGVVKLVE HFGDNTDVWP LIRIYRGGFL LIEFLFLLGI NTYGWRQAGV
NHVLIFELNP RNNLSHQHLF EIAGFLGVLW CVSILSCLFA ENTLIPIHMN PLALYGFFFL
FLINPLKTCY YKSRFWLLKL LFRVVTAPFH RVGFADFWLA DQLNSLVVVL MDLEYMICFY
SLELNWTMSE GELWIKEGER ICYSYSYGVR AVIKCLPAWF RFVQCLRRYR DTKRAFPHLV
NAGKYSTTFF VVIFEALFKT HSGDERFVFL YIMIACRIVN SCYTLLWDLK MDWGLFDRNA
GENTLLREEI VYPQKAYYYC AIVEDVILRF AWTIPLSLEV VYDRPVISNI LGTVLPPLEV
FRRFVWNFFR LENEHLNNCG EFRAVRDISV APLNADDQTL LEQMMDQEDG VRNRLGKKNW
KRSYSMSLRR PRLSSQSKVR DTKVLIEDTD DDT
