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Protein

Xenotropic and polytropic retrovirus receptor 1

Gene

Xpr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in phosphate homeostasis. Mediates phosphate export from the cell (By similarity). May function in G-protein coupled signal transduction (By similarity). Potential receptor for xenotropic and polytropic murine leukemia retroviruses (PubMed:10516044, PubMed:9988277).By similarity2 Publications

GO - Molecular functioni

  • receptor activity Source: MGI
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  • cellular phosphate ion homeostasis Source: UniProtKB
  • response to virus Source: MGI
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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 236236CytoplasmicSequence analysisAdd
BLAST
Transmembranei237 – 25721HelicalSequence analysisAdd
BLAST
Topological domaini258 – 2647ExtracellularSequence analysis
Transmembranei265 – 28521HelicalSequence analysisAdd
BLAST
Topological domaini286 – 31429CytoplasmicSequence analysisAdd
BLAST
Transmembranei315 – 33723HelicalSequence analysisAdd
BLAST
Topological domaini338 – 3403ExtracellularSequence analysis
Transmembranei341 – 36020HelicalSequence analysisAdd
BLAST
Topological domaini361 – 37616CytoplasmicSequence analysisAdd
BLAST
Transmembranei377 – 39721HelicalSequence analysisAdd
BLAST
Topological domaini398 – 4025ExtracellularSequence analysis
Transmembranei403 – 42321HelicalSequence analysisAdd
BLAST
Topological domaini424 – 47552CytoplasmicSequence analysisAdd
BLAST
Transmembranei476 – 49823HelicalSequence analysisAdd
BLAST
Topological domaini499 – 5079ExtracellularSequence analysis
Transmembranei508 – 52821HelicalSequence analysisAdd
BLAST
Topological domaini529 – 695167CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi500 – 5001E → K: Gives susceptibility to xenotropic murine leukemia retroviruses infection. 1 Publication
Mutagenesisi582 – 5821T → TT: Gives susceptibility to xenotropic murine leukemia retroviruses infection. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 695695Xenotropic and polytropic retrovirus receptor 1PRO_0000315854Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei667 – 6671PhosphoserineCombined sources
Modified residuei689 – 6891PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Z0U0.
MaxQBiQ9Z0U0.
PaxDbiQ9Z0U0.
PRIDEiQ9Z0U0.

PTM databases

iPTMnetiQ9Z0U0.
PhosphoSiteiQ9Z0U0.

Expressioni

Gene expression databases

BgeeiQ9Z0U0.
ExpressionAtlasiQ9Z0U0. baseline and differential.
GenevisibleiQ9Z0U0. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027741.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 177177SPXPROSITE-ProRule annotationAdd
BLAST
Domaini439 – 642204EXSPROSITE-ProRule annotationAdd
BLAST

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.
OMAiVLYGFMV.
OrthoDBiEOG7VQJCG.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591F → S in AAF13256 (Ref. 3) Curated
Sequence conflicti72 – 721F → L in AAF03484 (PubMed:10516044).Curated
Sequence conflicti103 – 1031G → A in AAF03484 (PubMed:10516044).Curated
Sequence conflicti106 – 1061T → A in AAF03484 (PubMed:10516044).Curated
Sequence conflicti158 – 1581K → E in BAE27891 (PubMed:16141072).Curated
Sequence conflicti372 – 3721F → L in AAF03482 (PubMed:10516044).Curated
Sequence conflicti377 – 3771L → P in AAF03484 (PubMed:10516044).Curated
Sequence conflicti469 – 4691D → N in AAF03482 (PubMed:10516044).Curated
Sequence conflicti500 – 5034EEQN → KERG in AAF03484 (PubMed:10516044).Curated
Sequence conflicti508 – 5081V → M in AAF03484 (PubMed:10516044).Curated
Sequence conflicti515 – 5184VFFC → IVFY in AAF03484 (PubMed:10516044).Curated
Sequence conflicti564 – 5641I → T in AAF13256 (Ref. 3) Curated
Sequence conflicti582 – 5821T → TT in AAF03484 (PubMed:10516044).Curated
Sequence conflicti589 – 5891N → D in AAF03484 (PubMed:10516044).Curated
Sequence conflicti591 – 5911I → S in BAE27891 (PubMed:16141072).Curated
Sequence conflicti606 – 6061W → L in AAF03484 (PubMed:10516044).Curated
Sequence conflicti647 – 6471Q → R in BAE24789 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei677 – 69519SKARD…DEANT → YVE in isoform 2. 1 PublicationVSP_030749Add
BLAST

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

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027741.

PTM databases

iPTMnetiQ9Z0U0.
PhosphoSiteiQ9Z0U0.

Proteomic databases

EPDiQ9Z0U0.
MaxQBiQ9Z0U0.
PaxDbiQ9Z0U0.
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.
OMAiVLYGFMV.
OrthoDBiEOG7VQJCG.
PhylomeDBiQ9Z0U0.
TreeFamiTF314643.

Miscellaneous databases

ChiTaRSiXpr1. mouse.
PROiQ9Z0U0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z0U0.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Polymorphisms of the cell surface receptor control mouse susceptibilities to xenotropic and polytropic leukemia viruses."
    Marin M., Tailor C.S., Nouri A., Kozak S.L., Kabat D.
    J. Virol. 73:9362-9368(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS RECEPTOR FOR MURINE RETROVIRUSES, MUTAGENESIS OF THR-582.
    Strain: NIH Swiss.
    Tissue: Kidney.
  2. "Receptors for polytropic and xenotropic mouse leukaemia viruses encoded by a single gene at Rmc1."
    Yang Y.-L., Guo L., Xu S., Holland C.A., Kitamura T., Hunter K., Cunningham J.M.
    Nat. Genet. 21:216-219(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS RECEPTOR FOR MURINE RETROVIRUSES.
    Tissue: Fibroblast.
  3. "Xenotropic and polytropic murine leukemia virus receptors from different species."
    Battini J.-L., Rasko J.E.J., Miller A.D.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Colon, Embryo and Olfactory bulb.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "Wild mouse variants of envelope genes of xenotropic/polytropic mouse gammaretroviruses and their XPR1 receptors elucidate receptor determinants of virus entry."
    Yan Y., Knoper R.C., Kozak C.A.
    J. Virol. 81:10550-10557(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECEPTOR FOR MURINE RETROVIRUSES, MUTAGENESIS OF GLU-500.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667 AND THR-689, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-689, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

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: June 8, 2016
This is version 90 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.