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Protein

Xenotropic and polytropic retrovirus receptor 1

Gene

Xpr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in phosphate homeostasis. Mediates phosphate export from the cell. Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules (By similarity). Potential receptor for xenotropic and polytropic murine leukemia retroviruses (PubMed:10516044, PubMed:9988277).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei22Important for inositol polyphosphate bindingBy similarity1
Sitei26Important for inositol polyphosphate bindingBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Receptor

Names & Taxonomyi

Protein namesi
Recommended name:
Xenotropic and polytropic retrovirus receptor 1
Alternative name(s):
Protein SYG1 homolog
Rmc-1
Gene namesi
Name:Xpr1
Synonyms:Syg1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:97932. Xpr1.

Subcellular locationi

  • Cell membrane By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 236CytoplasmicSequence analysisAdd BLAST236
Transmembranei237 – 257HelicalSequence analysisAdd BLAST21
Topological domaini258 – 264ExtracellularSequence analysis7
Transmembranei265 – 285HelicalSequence analysisAdd BLAST21
Topological domaini286 – 314CytoplasmicSequence analysisAdd BLAST29
Transmembranei315 – 337HelicalSequence analysisAdd BLAST23
Topological domaini338 – 340ExtracellularSequence analysis3
Transmembranei341 – 360HelicalSequence analysisAdd BLAST20
Topological domaini361 – 376CytoplasmicSequence analysisAdd BLAST16
Transmembranei377 – 397HelicalSequence analysisAdd BLAST21
Topological domaini398 – 402ExtracellularSequence analysis5
Transmembranei403 – 423HelicalSequence analysisAdd BLAST21
Topological domaini424 – 475CytoplasmicSequence analysisAdd BLAST52
Transmembranei476 – 498HelicalSequence analysisAdd BLAST23
Topological domaini499 – 507ExtracellularSequence analysis9
Transmembranei508 – 528HelicalSequence analysisAdd BLAST21
Topological domaini529 – 695CytoplasmicSequence analysisAdd BLAST167

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi500E → K: Gives susceptibility to xenotropic murine leukemia retroviruses infection. 1 Publication1
Mutagenesisi582T → TT: Gives susceptibility to xenotropic murine leukemia retroviruses infection. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003158541 – 695Xenotropic and polytropic retrovirus receptor 1Add BLAST695

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei667PhosphoserineCombined sources1
Modified residuei689PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9Z0U0.
PeptideAtlasiQ9Z0U0.
PRIDEiQ9Z0U0.

PTM databases

iPTMnetiQ9Z0U0.
PhosphoSitePlusiQ9Z0U0.

Expressioni

Gene expression databases

BgeeiENSMUSG00000026469.
ExpressionAtlasiQ9Z0U0. baseline and differential.
GenevisibleiQ9Z0U0. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027741.

Structurei

3D structure databases

ProteinModelPortaliQ9Z0U0.
SMRiQ9Z0U0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 177SPXPROSITE-ProRule annotationAdd BLAST177
Domaini439 – 642EXSPROSITE-ProRule annotationAdd BLAST204

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni158 – 165Important for inositol polyphosphate bindingBy similarity8

Domaini

The SPX domain has high affinity for inositol polyphosphates, such as myo-inositol hexakisphosphate and 5-diphospho-myo-inositol pentakisphosphate (5-InsP7). Its affinity for inorganic phosphate is tow to three orders of magnitude lower.By similarity

Sequence similaritiesi

Contains 1 EXS domain.PROSITE-ProRule annotation
Contains 1 SPX domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1162. Eukaryota.
COG5409. LUCA.
GeneTreeiENSGT00500000044895.
HOVERGENiHBG108684.
InParanoidiQ9Z0U0.
OMAiWTVQISI.
OrthoDBiEOG091G02HT.
PhylomeDBiQ9Z0U0.
TreeFamiTF314643.

Family and domain databases

InterProiIPR004342. EXS_C.
IPR004331. SPX_dom.
[Graphical view]
PfamiPF03124. EXS. 1 hit.
PF03105. SPX. 3 hits.
[Graphical view]
PROSITEiPS51380. EXS. 1 hit.
PS51382. SPX. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Z0U0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKFAEHLSAH ITPEWRKQYI QYEAFKDMLY SAQDQAPSVE VTDEDTVKRY
60 70 80 90 100
FAKFEEKFFQ TCEKELAKIN TFYSEKLAEA QRRFATLQNE LQSSLDVQKE
110 120 130 140 150
SSGVTTLRQR RKPVFHLSHE ERVQHRNIKD LKLAFSEFYL SLILLQNYQN
160 170 180 190 200
LNFTGFRKIL KKHDKILETS RGADWRVIHV EVAPFYTCKK INQLISETEA
210 220 230 240 250
VVTNELEDGD RQKAMKRLRV PPLGAAQPAP AWTTFRVGLF CGIFIVLNIT
260 270 280 290 300
LVFAAVFKLE TDRTVWPLIR IYRGGFLLIE FLFLLGINTY GWRQAGVNHV
310 320 330 340 350
LIFELNPRNN LSHQHLFEIA GFLGILWCLS LLACFFAPIS IIPIYVYPLA
360 370 380 390 400
LYGFMVFFLI NPTKTFYYKS RFWLLKLLFR VFTAPFHKVG FADFWLADQL
410 420 430 440 450
NSLSVILMDL EYMICFYSFE LKWDESKGLL PNDPQEPEFC HKYSYGVRAI
460 470 480 490 500
VQCIPAWLRF IQCLRRYRDT RRAFPHLVNA GKYSTTFFTV TFAALYSTHE
510 520 530 540 550
EQNHSDTVVF FYLWVFFCII SSCYTLIWDL KMDWGLFDKN AGENTFLREE
560 570 580 590 600
IVYPQKAYYY CAIIEDVILR FAWTIQISIT ATFKPHVGNI IATVFAPLEV
610 620 630 640 650
FRRFVWNFFR LENEHLNNCG EFRAVRDISV APLNADDQTL LEQMMDQEDG
660 670 680 690
VRNRQKNRSW KYNQSISLRR PRLASQSKAR DTKVLIEDTD DEANT
Length:695
Mass (Da):81,751
Last modified:May 1, 1999 - v1
Checksum:iB2E76CFE29C72258
GO
Isoform 2 (identifier: Q9Z0U0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     677-695: SKARDTKVLIEDTDDEANT → YVE

Note: No experimental confirmation available.
Show »
Length:679
Mass (Da):80,040
Checksum:i1E79B7D83133CC1B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti59F → S in AAF13256 (Ref. 3) Curated1
Sequence conflicti72F → L in AAF03484 (PubMed:10516044).Curated1
Sequence conflicti103G → A in AAF03484 (PubMed:10516044).Curated1
Sequence conflicti106T → A in AAF03484 (PubMed:10516044).Curated1
Sequence conflicti158K → E in BAE27891 (PubMed:16141072).Curated1
Sequence conflicti372F → L in AAF03482 (PubMed:10516044).Curated1
Sequence conflicti377L → P in AAF03484 (PubMed:10516044).Curated1
Sequence conflicti469D → N in AAF03482 (PubMed:10516044).Curated1
Sequence conflicti500 – 503EEQN → KERG in AAF03484 (PubMed:10516044).Curated4
Sequence conflicti508V → M in AAF03484 (PubMed:10516044).Curated1
Sequence conflicti515 – 518VFFC → IVFY in AAF03484 (PubMed:10516044).Curated4
Sequence conflicti564I → T in AAF13256 (Ref. 3) Curated1
Sequence conflicti582T → TT in AAF03484 (PubMed:10516044).Curated1
Sequence conflicti589N → D in AAF03484 (PubMed:10516044).Curated1
Sequence conflicti591I → S in BAE27891 (PubMed:16141072).Curated1
Sequence conflicti606W → L in AAF03484 (PubMed:10516044).Curated1
Sequence conflicti647Q → R in BAE24789 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_030749677 – 695SKARD…DEANT → YVE in isoform 2. 1 PublicationAdd BLAST19

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF131096 mRNA. Translation: AAF03482.1.
AF131098 mRNA. Translation: AAF03484.1.
AF114753 mRNA. Translation: AAD17206.1.
AF198104 mRNA. Translation: AAF13256.1.
AK032148 mRNA. Translation: BAC27724.1.
AK033421 mRNA. Translation: BAC28279.1.
AK141660 mRNA. Translation: BAE24789.1.
AK147403 mRNA. Translation: BAE27891.1.
BC153872 mRNA. Translation: AAI53873.1.
CCDSiCCDS15384.1. [Q9Z0U0-1]
RefSeqiNP_035403.1. NM_011273.2. [Q9Z0U0-1]
UniGeneiMm.266215.

Genome annotation databases

EnsembliENSMUST00000027741; ENSMUSP00000027741; ENSMUSG00000026469. [Q9Z0U0-1]
ENSMUST00000111774; ENSMUSP00000107404; ENSMUSG00000026469. [Q9Z0U0-2]
GeneIDi19775.
KEGGimmu:19775.
UCSCiuc007dbf.1. mouse. [Q9Z0U0-1]
uc007dbh.1. mouse. [Q9Z0U0-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF131096 mRNA. Translation: AAF03482.1.
AF131098 mRNA. Translation: AAF03484.1.
AF114753 mRNA. Translation: AAD17206.1.
AF198104 mRNA. Translation: AAF13256.1.
AK032148 mRNA. Translation: BAC27724.1.
AK033421 mRNA. Translation: BAC28279.1.
AK141660 mRNA. Translation: BAE24789.1.
AK147403 mRNA. Translation: BAE27891.1.
BC153872 mRNA. Translation: AAI53873.1.
CCDSiCCDS15384.1. [Q9Z0U0-1]
RefSeqiNP_035403.1. NM_011273.2. [Q9Z0U0-1]
UniGeneiMm.266215.

3D structure databases

ProteinModelPortaliQ9Z0U0.
SMRiQ9Z0U0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027741.

PTM databases

iPTMnetiQ9Z0U0.
PhosphoSitePlusiQ9Z0U0.

Proteomic databases

PaxDbiQ9Z0U0.
PeptideAtlasiQ9Z0U0.
PRIDEiQ9Z0U0.

Protocols and materials databases

DNASUi19775.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027741; ENSMUSP00000027741; ENSMUSG00000026469. [Q9Z0U0-1]
ENSMUST00000111774; ENSMUSP00000107404; ENSMUSG00000026469. [Q9Z0U0-2]
GeneIDi19775.
KEGGimmu:19775.
UCSCiuc007dbf.1. mouse. [Q9Z0U0-1]
uc007dbh.1. mouse. [Q9Z0U0-2]

Organism-specific databases

CTDi9213.
MGIiMGI:97932. Xpr1.

Phylogenomic databases

eggNOGiKOG1162. Eukaryota.
COG5409. LUCA.
GeneTreeiENSGT00500000044895.
HOVERGENiHBG108684.
InParanoidiQ9Z0U0.
OMAiWTVQISI.
OrthoDBiEOG091G02HT.
PhylomeDBiQ9Z0U0.
TreeFamiTF314643.

Miscellaneous databases

ChiTaRSiXpr1. mouse.
PROiQ9Z0U0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026469.
ExpressionAtlasiQ9Z0U0. baseline and differential.
GenevisibleiQ9Z0U0. MM.

Family and domain databases

InterProiIPR004342. EXS_C.
IPR004331. SPX_dom.
[Graphical view]
PfamiPF03124. EXS. 1 hit.
PF03105. SPX. 3 hits.
[Graphical view]
PROSITEiPS51380. EXS. 1 hit.
PS51382. SPX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXPR1_MOUSE
AccessioniPrimary (citable) accession number: Q9Z0U0
Secondary accession number(s): Q3UHG6
, Q3UR99, Q8CCC8, Q8CCT2, Q9QZ72, Q9R034, Q9R036
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 1, 1999
Last modified: November 2, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.