XPR1_XENLA
ID XPR1_XENLA Reviewed; 692 AA.
AC Q6DD44;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Xenotropic and polytropic retrovirus receptor 1 homolog;
GN Name=xpr1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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; BC077785; AAH77785.1; -; mRNA.
DR RefSeq; NP_001086930.1; NM_001093461.1.
DR AlphaFoldDB; Q6DD44; -.
DR SMR; Q6DD44; -.
DR PRIDE; Q6DD44; -.
DR DNASU; 446765; -.
DR GeneID; 446765; -.
DR KEGG; xla:446765; -.
DR CTD; 446765; -.
DR Xenbase; XB-GENE-1015951; xpr1.L.
DR OMA; GNWTEAR; -.
DR OrthoDB; 536327at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 446765; Expressed in brain and 19 other tissues.
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:0030643; P:cellular phosphate ion homeostasis; ISS:UniProtKB.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; ISS:UniProtKB.
DR InterPro; IPR004342; EXS_C.
DR InterPro; IPR004331; SPX_dom.
DR Pfam; PF03124; EXS; 1.
DR Pfam; PF03105; SPX; 2.
DR PROSITE; PS51380; EXS; 1.
DR PROSITE; PS51382; SPX; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..692
FT /note="Xenotropic and polytropic retrovirus receptor 1
FT homolog"
FT /id="PRO_0000315861"
FT TOPO_DOM 1..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..503
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 525..692
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..177
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT DOMAIN 435..639
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 660..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..692
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"
SQ SEQUENCE 692 AA; 80939 MW; 082A31BD3F59CCB2 CRC64;
MKFTEHLSAH ITPEWRKQYI QYEAFKEMLY AAQDQAPSIE VTDEDTVKRY YAKFEEKFFQ
TCEKELAKIN TFYSEKLAEA QRRSATLQNE LQSSLDAQRE SSVVPGLRQR RKAVFALTHE
ERVQHRNIKD LKLAFSEFYL SLILLQNYQN LNFTGFRKIL KKHDKILETS RGADWRVAHV
EVAPFYTCKK INQLISETET VVTNELESGD RQKAMKRLRV PPLGAAQPAP AWTTFRVGLY
CGIFMVVNLA VVMAGYHFLQ GKNVWPMVRI YRGGFLLIEF LFLLGINTYG WRQAGVNHVL
IFELNPRNNL SHQHLFEIAG FLGILWCFSL FSCIFGLSIN LQMHLNPLIL YGIMLVFLVN
PTKTFYYKSR FWLLKLLFRV FTAPFHKVGF ADFWLADQLN SLAIILMDLE FMICFYSFEL
NWGKSEGLVE SAKSVCNSYS YGVRAVVQCI PAWLRFIQCL RRYRDTKRAF PHLVNAGKYS
TTFFMVTFAA LYSTHKERNH SDAQVFFYLW IVFYFISSCY TLIWDLKMDW GLFDRNAGEN
TFLREEIVYP QKAYYYCAII QDVILRFAWT IQISVTSLNL FTDAGDVIST VLAPLEVFRR
FVWNFFRLEN EHLNNCGEFR AVRDISVAPL NADDQTMLEQ MMDQDDGVKN RVKSRIWKRS
QSMSLRRPRL SSQSKMKDAK ILIDDTDDEA NT
