ID   XPR1_MUSMC              Reviewed;         691 AA.
AC   Q9R031;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Xenotropic and polytropic retrovirus receptor 1 homolog;
GN   Name=Xpr1;
OS   Mus musculus castaneus (Southeastern Asian house mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   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).
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. {ECO:0000250|UniProtKB:Q9UBH6,
CC       ECO:0000250|UniProtKB:Q9Z0U0}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UBH6};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UBH6}.
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   -!- MISCELLANEOUS: In contrast to the ortholog protein in related Mus
CC       species, does not act as a receptor for xenotropic and polytropic
CC       murine leukemia retroviruses.
CC   -!- SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family. {ECO:0000305}.
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DR   EMBL; AF131102; AAF03488.1; -; mRNA.
DR   AlphaFoldDB; Q9R031; -.
DR   SMR; Q9R031; -.
DR   PRIDE; Q9R031; -.
DR   MGI; MGI:97932; Xpr1.
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: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   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   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..691
FT                   /note="Xenotropic and polytropic retrovirus receptor 1
FT                   homolog"
FT                   /id="PRO_0000315856"
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..371
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        393
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        415..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..691
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1..177
FT                   /note="SPX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT   DOMAIN          439..638
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          667..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..691
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         663
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBH6"
FT   MOD_RES         685
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBH6"
SQ   SEQUENCE   691 AA;  81228 MW;  5B9172B85E263CA6 CRC64;
     MKFAEHLSAH ITPEWRKQYI QYEAFKDMLY SAQDQAPSVE VTDEDTVKRY FAKFEEKFFQ
     TCEKELAKIN TFYSEKLAEA QRRFATLQNE LQSSLDVQKE SSAVTALRQR RKPVFHLSHE
     ERVQHRNIKD LKLAFSEFYL SLILLQNYQN LNFTGFRKIL KKHDKILETS RGADWRVIHV
     EVAPFYTCKK INQLISETEA VVTNELEDGD RQKAMKRLRV PPLGAAQPAP AWTIFRVGLF
     CGIFIVLNIT LVFAAVFKLE TDRTVWPLIR IYRGGFLLIE FLFLLGINTY GWRQAGVNHV
     LIFELNPRNN LSHQHLFEIA GFLGILWCLS LLACFFAPIS IIPIYVYPLA LYGFMVFFLI
     NPTKTFYYKS RFWLLKLLFR VFTAPFHKVG FADFWLAGQL NSLSVILMDL EYMICFYSFE
     LKWDESKGLL PNDPQEPEFC HKYSYGVRAI VQCIPAWLRF IQCLRRYRDT RRAFPHLVNA
     GKYSTTFFTV TFAALYSTHK EQNHSDTVVF FYLWVFFCII SSCYTLIWDL KMDWGLFDKN
     AGENTFLREE IVYPQKAYYY CAIIEDVILR FAWIIQISIT AHVGDIIATV FAPLEVFRRF
     VWNFFRLENE HLNNCGEFRA VRDISVAPLN ADDQTLLEQM MDQEDGVRNR QKNRSWKYNQ
     SISLRRPRLA SQSKARDTKV LIEDTDDEAN T