XPR1_MUSSP
ID XPR1_MUSSP Reviewed; 696 AA.
AC Q9R032;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Xenotropic and polytropic retrovirus receptor 1;
GN Name=Xpr1;
OS Mus spretus (Western Mediterranean mouse) (Algerian mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10096;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION AS RECEPTOR FOR MURINE
RP RETROVIRUSES.
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 (By similarity). Potential receptor for xenotropic
CC and polytropic murine leukemia retroviruses.
CC {ECO:0000250|UniProtKB:Q9UBH6, ECO:0000269|PubMed:10516044}.
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 -!- SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family. {ECO:0000305}.
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DR EMBL; AF131101; AAF03487.1; -; mRNA.
DR AlphaFoldDB; Q9R032; -.
DR SMR; Q9R032; -.
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:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Cell membrane; Host cell receptor for virus entry; Membrane;
KW Phosphoprotein; Receptor; Transmembrane; Transmembrane helix.
FT CHAIN 1..696
FT /note="Xenotropic and polytropic retrovirus receptor 1"
FT /id="PRO_0000315858"
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..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..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..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 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 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBH6"
FT MOD_RES 690
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBH6"
SQ SEQUENCE 696 AA; 81757 MW; 74A1B2B9783310CA CRC64;
MKFAEHLSAH ITPEWRKQYT QYEAFKDMLY SAQDQAPSVE VTDEDTVKRY FAKFEEKFFQ
TCEKELAKIN TFYSEKLAEA QRRFATLQNE LQSSLDVQKE SSGVTTLRQR RKPVFHLSHE
ERVQHRNIKD LKLAFSEFYL SLILLQNYQN LNFTGFRKIL KKHDKILETS RGADWRVIHV
EVAPFYTCKK INQLISETEA VVTNELEDGD RQKAMKRLRV PPLGAAQPAP AWTTFRVGLF
CGIFIGLNIT LGFAAVFKLE TDRTVWPLIR IYRGGFLLIE FLFLLGINTY GWRQAGVNHV
LIFELNPRNN LSHQHLFEIA GFLGILWCLS LLACFFAPIS IIPIYVYPLA LYGFMVFFLI
NPTKTFYYKS RFWLLKLLFR VFTAPFHKVG FADFWLADQL NSLSVILMDL EYMICFYSFE
LKWDESKGLL PNDPQEPEFC HKYSYGVRAI VQCIPAWLRF IQCLRRYRDT RRAFPHLVNA
GKYSTTFFTV TFAALYSTHK EQNHSDTVVF FYLWVFFCII SSCYTLIWDL KMDWGLFDKN
AGENTFLREE IVYPQKAYYY CAIIEDVILR FAWTIQISIT ATTFKPHVGD IIATVFAPLE
VFRRFVWNFF RLENEHLDNC GEFRAVRDIS VAPLNADDQT LLEQMMDQED GVRNRQKNRS
WKYNQSISLR RPRLASQSKA RDTKVLIEDT DDEANT
