XPR1_MOUSE
ID XPR1_MOUSE Reviewed; 695 AA.
AC Q9Z0U0; Q3UHG6; Q3UR99; Q8CCC8; Q8CCT2; Q9QZ72; Q9R034; Q9R036;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Xenotropic and polytropic retrovirus receptor 1;
DE AltName: Full=Protein SYG1 homolog;
DE AltName: Full=Rmc-1;
GN Name=Xpr1; Synonyms=Syg1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS RECEPTOR FOR MURINE
RP RETROVIRUSES, AND MUTAGENESIS OF THR-582.
RC STRAIN=NIH Swiss; TISSUE=Kidney;
RX PubMed=10516044; DOI=10.1128/jvi.73.11.9362-9368.1999;
RA Marin M., Tailor C.S., Nouri A., Kozak S.L., Kabat D.;
RT "Polymorphisms of the cell surface receptor control mouse susceptibilities
RT to xenotropic and polytropic leukemia viruses.";
RL J. Virol. 73:9362-9368(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS RECEPTOR FOR MURINE
RP RETROVIRUSES.
RC TISSUE=Fibroblast;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Battini J.-L., Rasko J.E.J., Miller A.D.;
RT "Xenotropic and polytropic murine leukemia virus receptors from different
RT species.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Colon, Embryo, and Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 RECEPTOR FOR MURINE RETROVIRUSES, AND MUTAGENESIS OF GLU-500.
RX PubMed=17634227; DOI=10.1128/jvi.00933-07;
RA Yan Y., Knoper R.C., Kozak C.A.;
RT "Wild mouse variants of envelope genes of xenotropic/polytropic mouse
RT gammaretroviruses and their XPR1 receptors elucidate receptor determinants
RT of virus entry.";
RL J. Virol. 81:10550-10557(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667 AND THR-689, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-689, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in phosphate homeostasis. Mediates phosphate
CC export from the cell. Binds inositol hexakisphosphate (Ins6P) and
CC similar inositol polyphosphates, such as 5-diphospho-inositol
CC pentakisphosphate (5-InsP7); these are important intracellular
CC signaling molecules (By similarity). Potential receptor for xenotropic
CC and polytropic murine leukemia retroviruses (PubMed:10516044,
CC PubMed:9988277). {ECO:0000250|UniProtKB:Q9UBH6,
CC ECO:0000269|PubMed:10516044, ECO:0000269|PubMed:9988277}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UBH6};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UBH6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z0U0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z0U0-2; Sequence=VSP_030749;
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; AF131096; AAF03482.1; -; mRNA.
DR EMBL; AF131098; AAF03484.1; -; mRNA.
DR EMBL; AF114753; AAD17206.1; -; mRNA.
DR EMBL; AF198104; AAF13256.1; -; mRNA.
DR EMBL; AK032148; BAC27724.1; -; mRNA.
DR EMBL; AK033421; BAC28279.1; -; mRNA.
DR EMBL; AK141660; BAE24789.1; -; mRNA.
DR EMBL; AK147403; BAE27891.1; -; mRNA.
DR EMBL; BC153872; AAI53873.1; -; mRNA.
DR CCDS; CCDS15384.1; -. [Q9Z0U0-1]
DR RefSeq; NP_035403.1; NM_011273.2. [Q9Z0U0-1]
DR AlphaFoldDB; Q9Z0U0; -.
DR SMR; Q9Z0U0; -.
DR STRING; 10090.ENSMUSP00000027741; -.
DR iPTMnet; Q9Z0U0; -.
DR PhosphoSitePlus; Q9Z0U0; -.
DR MaxQB; Q9Z0U0; -.
DR PaxDb; Q9Z0U0; -.
DR PeptideAtlas; Q9Z0U0; -.
DR PRIDE; Q9Z0U0; -.
DR ProteomicsDB; 299800; -. [Q9Z0U0-1]
DR ProteomicsDB; 299801; -. [Q9Z0U0-2]
DR Antibodypedia; 20589; 195 antibodies from 29 providers.
DR DNASU; 19775; -.
DR Ensembl; ENSMUST00000027741; ENSMUSP00000027741; ENSMUSG00000026469. [Q9Z0U0-1]
DR Ensembl; ENSMUST00000111774; ENSMUSP00000107404; ENSMUSG00000026469. [Q9Z0U0-2]
DR GeneID; 19775; -.
DR KEGG; mmu:19775; -.
DR UCSC; uc007dbf.1; mouse. [Q9Z0U0-1]
DR UCSC; uc007dbh.1; mouse. [Q9Z0U0-2]
DR CTD; 9213; -.
DR MGI; MGI:97932; Xpr1.
DR VEuPathDB; HostDB:ENSMUSG00000026469; -.
DR eggNOG; KOG1162; Eukaryota.
DR GeneTree; ENSGT00500000044895; -.
DR HOGENOM; CLU_006116_3_0_1; -.
DR InParanoid; Q9Z0U0; -.
DR OMA; HETENIV; -.
DR OrthoDB; 536327at2759; -.
DR PhylomeDB; Q9Z0U0; -.
DR TreeFam; TF314643; -.
DR BioGRID-ORCS; 19775; 8 hits in 72 CRISPR screens.
DR ChiTaRS; Xpr1; mouse.
DR PRO; PR:Q9Z0U0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9Z0U0; protein.
DR Bgee; ENSMUSG00000026469; Expressed in median eminence of neurohypophysis and 256 other tissues.
DR ExpressionAtlas; Q9Z0U0; baseline and differential.
DR Genevisible; Q9Z0U0; MM.
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; ISS:UniProtKB.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; ISS:UniProtKB.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; IDA:MGI.
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:0035435; P:phosphate ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006817; P:phosphate ion transport; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; IDA:MGI.
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 Alternative splicing; Cell membrane; Host cell receptor for virus entry;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..695
FT /note="Xenotropic and polytropic retrovirus receptor 1"
FT /id="PRO_0000315854"
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..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..340
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..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..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..507
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 529..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..177
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT DOMAIN 439..642
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 671..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..695
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:0000250|UniProtKB:P43585"
FT SITE 26
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P43585"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 689
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 677..695
FT /note="SKARDTKVLIEDTDDEANT -> YVE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030749"
FT MUTAGEN 500
FT /note="E->K: Gives susceptibility to xenotropic murine
FT leukemia retroviruses infection."
FT /evidence="ECO:0000269|PubMed:17634227"
FT MUTAGEN 582
FT /note="T->TT: Gives susceptibility to xenotropic murine
FT leukemia retroviruses infection."
FT /evidence="ECO:0000269|PubMed:10516044"
FT CONFLICT 59
FT /note="F -> S (in Ref. 3; AAF13256)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="F -> L (in Ref. 1; AAF03484)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="G -> A (in Ref. 1; AAF03484)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="T -> A (in Ref. 1; AAF03484)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="K -> E (in Ref. 4; BAE27891)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="F -> L (in Ref. 1; AAF03482)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="L -> P (in Ref. 1; AAF03484)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="D -> N (in Ref. 1; AAF03482)"
FT /evidence="ECO:0000305"
FT CONFLICT 500..503
FT /note="EEQN -> KERG (in Ref. 1; AAF03484)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="V -> M (in Ref. 1; AAF03484)"
FT /evidence="ECO:0000305"
FT CONFLICT 515..518
FT /note="VFFC -> IVFY (in Ref. 1; AAF03484)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="I -> T (in Ref. 3; AAF13256)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="T -> TT (in Ref. 1; AAF03484)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="N -> D (in Ref. 1; AAF03484)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="I -> S (in Ref. 4; BAE27891)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="W -> L (in Ref. 1; AAF03484)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="Q -> R (in Ref. 4; BAE24789)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 695 AA; 81751 MW; B2E76CFE29C72258 CRC64;
MKFAEHLSAH ITPEWRKQYI QYEAFKDMLY SAQDQAPSVE VTDEDTVKRY FAKFEEKFFQ
TCEKELAKIN TFYSEKLAEA QRRFATLQNE LQSSLDVQKE SSGVTTLRQR RKPVFHLSHE
ERVQHRNIKD LKLAFSEFYL SLILLQNYQN LNFTGFRKIL KKHDKILETS RGADWRVIHV
EVAPFYTCKK INQLISETEA VVTNELEDGD RQKAMKRLRV PPLGAAQPAP AWTTFRVGLF
CGIFIVLNIT LVFAAVFKLE TDRTVWPLIR IYRGGFLLIE FLFLLGINTY GWRQAGVNHV
LIFELNPRNN LSHQHLFEIA GFLGILWCLS LLACFFAPIS IIPIYVYPLA LYGFMVFFLI
NPTKTFYYKS RFWLLKLLFR VFTAPFHKVG FADFWLADQL NSLSVILMDL EYMICFYSFE
LKWDESKGLL PNDPQEPEFC HKYSYGVRAI VQCIPAWLRF IQCLRRYRDT RRAFPHLVNA
GKYSTTFFTV TFAALYSTHE EQNHSDTVVF FYLWVFFCII SSCYTLIWDL KMDWGLFDKN
AGENTFLREE IVYPQKAYYY CAIIEDVILR FAWTIQISIT ATFKPHVGNI IATVFAPLEV
FRRFVWNFFR LENEHLNNCG EFRAVRDISV APLNADDQTL LEQMMDQEDG VRNRQKNRSW
KYNQSISLRR PRLASQSKAR DTKVLIEDTD DEANT
