S20A2_CRIGR
ID S20A2_CRIGR Reviewed; 650 AA.
AC Q9ES44; Q60421; Q9WTV3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Sodium-dependent phosphate transporter 2;
DE AltName: Full=Amphotropic murine leukemia virus receptor;
DE AltName: Full=Amphotropic murine retrovirus receptor;
DE AltName: Full=Phosphate transporter 2;
DE Short=ChoPit2;
DE Short=HaPit2;
DE Short=PiT-2;
DE AltName: Full=Solute carrier family 20 member 2;
GN Name=SLC20A2; Synonyms=PIT2;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION AS RETROVIRAL RECEPTOR.
RC TISSUE=Lung;
RX PubMed=7966559; DOI=10.1128/jvi.68.12.7697-7703.1994;
RA Wilson C.A., Farrell K.B., Eiden M.V.;
RT "Properties of a unique form of the murine amphotropic leukemia virus
RT receptor expressed on hamster cells.";
RL J. Virol. 68:7697-7703(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10074140; DOI=10.1128/jvi.73.4.2916-2920.1999;
RA Chaudry G.J., Farrell K.B., Ting Y.-T., Schmitz C., Lie S.Y.,
RA Petropoulos C.J., Eiden M.V.;
RT "Gibbon ape leukemia virus receptor functions of type III phosphate
RT transporters from CHOK1 cells are disrupted by two distinct mechanisms.";
RL J. Virol. 73:2916-2920(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION AS RETROVIRAL RECEPTOR.
RC TISSUE=Ovary;
RX PubMed=11000257; DOI=10.1128/jvi.74.20.9797-9801.2000;
RA Tailor C.S., Nouri A., Kabat D.;
RT "Cellular and species resistance to murine amphotropic, gibbon ape, and
RT feline subgroup C leukemia viruses is strongly influenced by receptor
RT expression levels and by receptor masking mechanisms.";
RL J. Virol. 74:9797-9801(2000).
CC -!- FUNCTION: Sodium-phosphate symporter which seems to play a fundamental
CC housekeeping role in phosphate transport by absorbing phosphate from
CC interstitial fluid for normal cellular functions such as cellular
CC metabolism, signal transduction, and nucleic acid and lipid synthesis.
CC In vitro, sodium-dependent phosphate uptake is not significantly
CC affected by acidic and alkaline conditions, however sodium-independent
CC phosphate uptake occurs at acidic conditions. May play a role in
CC extracellular matrix, cartilage calcification and vascular
CC calcification (By similarity). Functions as a retroviral receptor and
CC confers hamster cells susceptibility to infection to Gibbon Ape
CC Leukemia Virus (GaLV) and amphotropic murine leukemia virus (A-MuLV).
CC {ECO:0000250, ECO:0000269|PubMed:11000257, ECO:0000269|PubMed:7966559}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) (TC
CC 2.A.20) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U13945; AAA57032.1; -; mRNA.
DR EMBL; AF063025; AAD28693.1; -; mRNA.
DR EMBL; AF239675; AAG21945.1; -; mRNA.
DR RefSeq; NP_001230939.1; NM_001244010.1.
DR AlphaFoldDB; Q9ES44; -.
DR SMR; Q9ES44; -.
DR STRING; 10029.NP_001230939.1; -.
DR GeneID; 100689023; -.
DR KEGG; cge:100689023; -.
DR CTD; 6575; -.
DR eggNOG; KOG2493; Eukaryota.
DR OrthoDB; 712010at2759; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR001204; Phos_transporter.
DR PANTHER; PTHR11101; PTHR11101; 1.
DR Pfam; PF01384; PHO4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Host cell receptor for virus entry;
KW Host-virus interaction; Ion transport; Membrane; Phosphate transport;
KW Phosphoprotein; Receptor; Sodium; Sodium transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..650
FT /note="Sodium-dependent phosphate transporter 2"
FT /id="PRO_0000341266"
FT TOPO_DOM 1..5
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..83
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..142
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..530
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..571
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..593
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..609
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 610..621
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..650
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 268..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63488"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08357"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08357"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08357"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08357"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08357"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 1..2
FT /note="Missing (in Ref. 2; AAD28693)"
FT /evidence="ECO:0000305"
FT CONFLICT 5
FT /note="G -> E (in Ref. 1; AAA57032)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="V -> L (in Ref. 3; AAG21945)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="W -> G (in Ref. 3; AAG21945)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="K -> M (in Ref. 2; AAD28693)"
FT /evidence="ECO:0000305"
FT CONFLICT 415..416
FT /note="KL -> NV (in Ref. 1; AAA57032)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="S -> F (in Ref. 1; AAA57032)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="R -> K (in Ref. 3; AAG21945)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="A -> Q (in Ref. 1; AAA57032)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="A -> S (in Ref. 1; AAA57032)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="G -> R (in Ref. 1; AAA57032)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="S -> PYV (in Ref. 1; AAA57032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 70279 MW; A59BF4444D608CE4 CRC64;
MAMDGYLWMV ILGFIIAFIL AFSVGANDVA NSFGTAVGSG VVTLRQACIL ASIFETTGSV
LLGAKVGETI RKGIIDVNLY NDTVVTLMAG EVSAMVGSAV WQLIASFLRL PISGTHCIVG
STIGFSLVAN GTKGVQWMEL VKIVASWFIS PLLSGFMSGV LFVLIRMFIL TKEDPVPNGL
QALPLFYAAT IAINVFSIMY TGAPVLGLSL PIWAIALISF GVALLFAFFV WLFVCPWMRR
KIAGKLEKES ALSRTSDESL SKVQEVESPF KELPGAKASD DSAVPLTNPT GEAVGPSEGT
STGNHPRTAY GRALSMTHGS AKSPISNGTF SFEGHMRNDG HVYHTVHKDS GLYKDLLHKI
HVDKGPEEKL SQENNYRLLR RNNSYTCYTA AICGMPVHTT FRATDASSAP EDSEKLVGDT
VSYSKKRLRY DSYSSYCNAV AEAEIEAEEG GVEMRLASEL ADPDQPHDDP TEEEKEEKDT
AEVHLLFHFL QVLTACFGSF AHGGNDVSNA IGPLVALWLI YEQGGVMQEA ATPVWLLFYG
GVGICTGLWV WGRRVIQTMG KDLTPITPSS GFTIELASAF TVVIASNIGL PVSTTHCKVG
SVVAVGWIRS RKAVDWHLFR NIFVAWFVTV PVAGLFSAAI MAIFMYGILS
