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Database: UniProt
Entry: Q28722
LinkDB: Q28722
Original site: Q28722 
ID   NPT1_RABIT              Reviewed;         465 AA.
AC   Q28722;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-NOV-2023, entry version 105.
DE   RecName: Full=Sodium-dependent phosphate transport protein 1;
DE   AltName: Full=NAPI-1;
DE   AltName: Full=Na(+)/PI cotransporter 1;
DE   AltName: Full=Renal Na(+)-dependent phosphate cotransporter 1;
DE   AltName: Full=Renal sodium-dependent phosphate transport protein 1;
DE            Short=Renal sodium-phosphate transport protein 1;
DE   AltName: Full=Sodium/phosphate cotransporter 1;
DE   AltName: Full=Solute carrier family 17 member 1;
GN   Name=SLC17A1; Synonyms=NPT1;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney cortex;
RX   PubMed=1946375; DOI=10.1073/pnas.88.21.9608;
RA   Werner A., Moore M.L., Mantei N., Biber J., Semenza G., Murer H.;
RT   "Cloning and expression of cDNA for a Na/Pi cotransport system of kidney
RT   cortex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:9608-9612(1991).
CC   -!- FUNCTION: Important for the resorption of phosphate by the kidney. May
CC       be involved in actively transporting phosphate into cells via Na(+)
CC       cotransport in the renal brush border membrane. Plays a role in urate
CC       transport in the kidney. {ECO:0000250|UniProtKB:Q14916}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in);
CC         Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474;
CC         Evidence={ECO:0000250|UniProtKB:Q14916};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=urate(out) = urate(in); Xref=Rhea:RHEA:60368,
CC         ChEBI:CHEBI:17775; Evidence={ECO:0000250|UniProtKB:Q14916};
CC   -!- SUBUNIT: Interacts with PDZK1. {ECO:0000250|UniProtKB:Q61983}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q14916}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Kidney cortex and liver.
CC       {ECO:0000269|PubMed:1946375}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion
CC       cotransporter family. {ECO:0000305}.
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DR   EMBL; M76466; AAA31461.1; -; mRNA.
DR   PIR; A56410; A56410.
DR   RefSeq; NP_001075776.1; NM_001082307.1.
DR   AlphaFoldDB; Q28722; -.
DR   SMR; Q28722; -.
DR   STRING; 9986.ENSOCUP00000012050; -.
DR   GlyCosmos; Q28722; 2 sites, No reported glycans.
DR   PaxDb; 9986-ENSOCUP00000012050; -.
DR   GeneID; 100009144; -.
DR   KEGG; ocu:100009144; -.
DR   CTD; 6568; -.
DR   eggNOG; KOG2532; Eukaryota.
DR   InParanoid; Q28722; -.
DR   OrthoDB; 2685946at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0044341; P:sodium-dependent phosphate transport; ISS:UniProtKB.
DR   GO; GO:0015747; P:urate transport; ISS:UniProtKB.
DR   CDD; cd17318; MFS_SLC17; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004745; Pi_cotranspt.
DR   NCBIfam; TIGR00894; 2A0114euk; 1.
DR   PANTHER; PTHR11662:SF26; SODIUM-DEPENDENT PHOSPHATE TRANSPORT PROTEIN 1; 1.
DR   PANTHER; PTHR11662; SOLUTE CARRIER FAMILY 17; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Ion transport; Membrane; Reference proteome;
KW   Sodium; Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..465
FT                   /note="Sodium-dependent phosphate transport protein 1"
FT                   /id="PRO_0000220938"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   465 AA;  51798 MW;  29B33FB1EADDCBAD CRC64;
     MDNQFPSRKG PCFCSFRYVL ALFMHFCNIV IIAQRMCLSL TMVAMVNNTN LHGSPNTSAE
     KRLDNTKNPV YNWSPDVQGI IFSSIFYGAF LIQIPVGYIS GIYSIKKLIG FALFLSSLVS
     IFIPQAAAVG ETWIIVCRVV QGITQGTVTT AQHEIWVKWA PPLERGRLTS MSLSGFLLGP
     FIVLLVTGII CESLGWPMVF YIFGACGCAV CLLWFVLYYD DPKDHPCVSL HEKEYITSSL
     IQQGSSTRQS LPIKAMIKSL PLWAISFCCF AYLWTYSRLI VYTPTLINSM LHVDIRENGL
     LSSLPYLFAW ICGVIAGHTA DFLMSRNMLS LTAIRKLFTA IGLLLPIVFS MCLLYLSSGF
     YSTITFLILA NASSSFCLGG ALINALDLAP RYYVFIKGVT TLIGMTGGMT SSTVAGLFLS
     QDPESSWFKI FLLMSIINVI SVIFYLIFAK AEIQDWAKEK QHTRL
//
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