XPR1_XENTR
ID XPR1_XENTR Reviewed; 692 AA.
AC Q28CY9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Xenotropic and polytropic retrovirus receptor 1 homolog;
GN Name=xpr1; ORFNames=TGas047j19.2;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) 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; CR855800; CAJ83793.1; -; mRNA.
DR RefSeq; NP_001016753.1; NM_001016753.2.
DR AlphaFoldDB; Q28CY9; -.
DR SMR; Q28CY9; -.
DR PaxDb; Q28CY9; -.
DR GeneID; 549507; -.
DR KEGG; xtr:549507; -.
DR CTD; 9213; -.
DR Xenbase; XB-GENE-1015946; xpr1.
DR eggNOG; KOG1162; Eukaryota.
DR InParanoid; Q28CY9; -.
DR OrthoDB; 536327at2759; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
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; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..692
FT /note="Xenotropic and polytropic retrovirus receptor 1
FT homolog"
FT /id="PRO_0000315862"
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..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..344
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..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..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..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; 80881 MW; EDF80B8141C390DB CRC64;
MKFAEHLSAH ITPEWRKQYI QYEAFKEMLY AAQDQAPSIE VTDEDTVKRY YAKFEEIFFQ
TCEKELAKIN TFYSEKLAEA QRRSATLQNE LQSSLDAQRE SSAIPGLRQR RKAVFALTHE
ERVQHRNIKD LKLAFSEFYL SLILLQNYQN LNFTGFRKIL KKHDKILETS RGADWRVAHV
EVAPFYTCKK INQLISETET VVTNELESGD RQKAMKRLRV PPLGAAQPAP AWTTFRVGLY
CGIFIVLNMA IIMAGSHYLL GKDVWPMVRI YRGGFLLIEF LFLLGINTYG WRQAGVNHVL
IFELNPRNNL SHQHLFEIAG FLGILWCFSL FSCIFGLWIN LQMHLNPLIL YGLMLLFLVN
PTKTFYYKSR FWLLKLLFRV FTAPFHKVGF ADFWLADQLN SLAVILMDLE FMICFYSFEL
KWGDSDGLVN SANSVCNSYS YGVRAVVQCI PAWLRFIQCL RRYRDTKRAF PHLVNAGKYS
TTFFMVTFAA LYSTHKERNH SDAQVFFYLW IIFYLISSCY TLIWDLKMDW GLFDRNAGEN
TFLREEIVYP QKAYYYCAII QDVILRFAWT IQISVTSLNL FTDAGDIIST VLAPLEVFRR
FVWNFFRLEN EHLNNCGEFR AVRDISVAPL NADDQTLLEQ MMDQDDGVKN RVKSRIWKRS
QSMSLRRPRL SSQSKMKDAK ILIDDTDDEA NT
