XPR1_CRIGR
ID XPR1_CRIGR Reviewed; 696 AA.
AC Q9QZ70; Q9R033;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Xenotropic and polytropic retrovirus receptor 1 homolog;
GN Name=XPR1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
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].
RC TISSUE=Ovary;
RX PubMed=16354307; DOI=10.1186/1742-4690-2-76;
RA Van Hoeven N.S., Miller A.D.;
RT "Use of different but overlapping determinants in a retrovirus receptor
RT accounts for non-reciprocal interference between xenotropic and polytropic
RT murine leukemia viruses.";
RL Retrovirology 2:76-76(2005).
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 -!- SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family. {ECO:0000305}.
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DR EMBL; AF131099; AAF03485.1; -; mRNA.
DR EMBL; AF198106; AAF13258.1; -; mRNA.
DR RefSeq; NP_001231014.1; NM_001244085.1.
DR AlphaFoldDB; Q9QZ70; -.
DR SMR; Q9QZ70; -.
DR STRING; 10029.NP_001231014.1; -.
DR PRIDE; Q9QZ70; -.
DR Ensembl; ENSCGRT00001027531; ENSCGRP00001023285; ENSCGRG00001021543.
DR GeneID; 100689082; -.
DR KEGG; cge:100689082; -.
DR CTD; 9213; -.
DR eggNOG; KOG1162; Eukaryota.
DR GeneTree; ENSGT00500000044895; -.
DR OrthoDB; 536327at2759; -.
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: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:Ensembl.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; ISS:UniProtKB.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cell membrane; Membrane; Phosphoprotein; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..696
FT /note="Xenotropic and polytropic retrovirus receptor 1
FT homolog"
FT /id="PRO_0000315852"
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..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..343
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..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..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..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 672..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: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"
FT CONFLICT 40
FT /note="E -> K (in Ref. 1; AAF03485)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="F -> L (in Ref. 1; AAF03485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 696 AA; 81767 MW; 406F7D7A4EB1D266 CRC64;
MKFAEHLSAH ITPEWRKQYI QYEAFKDMLY SAQDQAPSVE VTDEDTVKRY FAKFEEKFFQ
TCEKELAKIN TFYSEKLAEA QRRFATLQNE LQSSLDAQRE SIGVTTLRQR RKPVFHLSHE
ERVQHRNIKD LKLAFSEFYL SLILLQNYQN LNFTGFRKIL KKHDKILETS RGADWRVGHV
EVAPFYTCKK INQLISETEA VVTNELEDGD RQKAMKRLRV PPLGAAQPAP AWTTFRVGLF
CGIFIVLNIT LVLAAVFKLE TDRTVWPLIR IYRGGFLLIE FLFLLGINTY GWRQAGVNHV
LIFELNPRNN LSHQHLFEIA GFLGILWCLS LLACFFAPIS VVPIYVYPLA LYGFMVFFLI
NPTKTFYYKS RFWLLKLLFR VFTAPFHKVG FADFWLADQL NSLSVILMDL EYMICFYSFE
LKWDENKSLL PNDLQEPEFC HRYTYGVRAI VQCIPAWLRF IQCLRRYRDT KRAFPHLVNA
GKYSTTFFTV TFAALYSTHK ERQHSDTMVF LYLWVVFCAI SSCYTLIWDL KMDWGLFDKN
AGENTFLREE IVYPQKAYYY CAIIEDVILR FAWTIQISIT ATAFQPHVGD IIATVFAPLE
VFRRFVWNFF RLENEHLNNC GEFRAVRDIS VAPLNADDQT LLEQMMDQED GVRNRQKNRS
WKYNQSISLR RPRLASQSKA RDTKVLIEDT DDEANT
