XPR1_NEOVI
ID XPR1_NEOVI Reviewed; 696 AA.
AC Q9TU72;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Xenotropic and polytropic retrovirus receptor 1;
GN Name=XPR1;
OS Neovison vison (American mink) (Mustela vison).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC Neogale.
OX NCBI_TaxID=452646;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RECEPTOR FOR MURINE RETROVIRUSES.
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).
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 (By similarity). Potential receptor for xenotropic
CC and polytropic murine leukemia retroviruses.
CC {ECO:0000250|UniProtKB:Q9UBH6, ECO:0000269|PubMed:10516044}.
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; AF131100; AAF03486.1; -; mRNA.
DR AlphaFoldDB; Q9TU72; -.
DR SMR; Q9TU72; -.
DR PRIDE; Q9TU72; -.
DR Proteomes; UP000694425; Unplaced.
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:UniProtKB-KW.
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; 3.
DR PROSITE; PS51380; EXS; 1.
DR PROSITE; PS51382; SPX; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Host cell receptor for virus entry; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..696
FT /note="Xenotropic and polytropic retrovirus receptor 1"
FT /id="PRO_0000315859"
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..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..345
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..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..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497..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 648..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"
SQ SEQUENCE 696 AA; 81581 MW; 479997D73DB5837B CRC64;
MKFAEHLSAH ITPEWRKQYI QYEAFKDMLY SAQDQAPSVE VTDEDTVKRY FAKFEEKFFQ
TCEKELAKIN TFYSEKLAEA QRRFATLQNE LQSSLDAQKE STGVTTLRQR RMPVFHLSHE
ERVQHRNIKD LKLAFSEFYL SLILLQNYQN LNFTEFRKIL KKHDKILETS RGADWRVAHV
EVAPFYTCKK INQLISETEA VVTNELEDGD PQKAMKRLRV PSLGAAQPAP AWTTFRVGLF
CGIFIVLNIT LVLAAVFKLE TDRSIWPLIR IYRGGFLLIE FLFLLGINTY GWRQAGVNHV
LIFELNPRNN LSHQHLFEIA GFLGILWCLS LLACFFAPIS VIPTYVYPLV LYGFMVFFLI
NPTKTFYYKS RFWLLKLLFR VFTAPFHKVG FADFWLADQL NSLSVILMDL EYMICFYSFE
LKWDESGGLL PNNSEEPEIC HKYSYGVRAI VQCVPAWLRF IQCLRRYRDT KRAFPHLVNA
GKYSTTFFTV TFAALYSTHK ERGHSDTMVF FYLWIVFCII SSCYTLIWDL KMDWGLFDKN
AGENTFLREE IVYPQRAYYY CTIIEDVILR FAWTVQISIT SMTLLPHSGD IIATVFAPLE
VFRRFVWNFF RLENEHLNNC GEFRAVRDIS VAPLNADDQT LLEQMMDQDD GVRDRQKNRP
WKYSQSISLR RPRLASQSKA RDTKVLIEDT DDEANT
