NPT2A_RABIT
ID NPT2A_RABIT Reviewed; 642 AA.
AC Q28620;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Sodium-dependent phosphate transport protein 2A;
DE Short=Sodium-phosphate transport protein 2A;
DE AltName: Full=Na(+)-dependent phosphate cotransporter 2A;
DE AltName: Full=NaPi-6 {ECO:0000303|PubMed:7733319};
DE AltName: Full=Sodium/phosphate cotransporter 2A;
DE Short=Na(+)/Pi cotransporter 2A;
DE Short=NaPi-2a;
DE AltName: Full=Solute carrier family 34 member 1 {ECO:0000250|UniProtKB:Q06495};
GN Name=SLC34A1 {ECO:0000250|UniProtKB:Q06495};
GN Synonyms=SLC17A2 {ECO:0000250|UniProtKB:Q06495};
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], FUNCTION, TRANSPORTER ACTIVITY, TISSUE
RP SPECIFICITY, ACTIVITY REGULATION, AND INDUCTION.
RC TISSUE=Kidney;
RX PubMed=7733319; DOI=10.1152/ajprenal.1995.268.4.f626;
RA Verri T., Markovich D., Perego C., Norbis F., Stange G., Sorribas V.,
RA Biber J., Murer H.;
RT "Cloning of a rabbit renal Na-Pi cotransporter, which is regulated by
RT dietary phosphate.";
RL Am. J. Physiol. 268:F626-F633(1995).
CC -!- FUNCTION: Involved in actively transporting phosphate into cells via
CC Na(+) cotransport in the renal brush border membrane (PubMed:7733319).
CC The cotransport has a Na(+):Pi stoichiometry of 3:1 and is electrogenic
CC (By similarity). {ECO:0000250|UniProtKB:Q06496,
CC ECO:0000269|PubMed:7733319}.
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:0000269|PubMed:7733319};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71256;
CC Evidence={ECO:0000305|PubMed:7733319};
CC -!- ACTIVITY REGULATION: Transport activity is significantly increased in
CC response to dietary phosphate deprivation.
CC {ECO:0000269|PubMed:7733319}.
CC -!- SUBUNIT: Interacts via its C-terminal region with PDZK2. Interacts with
CC SLC9A3R1. {ECO:0000250|UniProtKB:Q06495, ECO:0000250|UniProtKB:Q60825}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q06495}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q06496}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Localized at the brush border
CC membranes of the proximal tubules. {ECO:0000250|UniProtKB:Q06496}.
CC -!- TISSUE SPECIFICITY: Expressed in the kidney cortex.
CC {ECO:0000269|PubMed:7733319}.
CC -!- INDUCTION: Up-regulated by a low-phosphate diet.
CC {ECO:0000269|PubMed:7733319}.
CC -!- SIMILARITY: Belongs to the SLC34A transporter family. {ECO:0000305}.
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DR EMBL; U20793; AAA77682.1; -; mRNA.
DR PIR; I46534; I46534.
DR RefSeq; NP_001076142.1; NM_001082673.2.
DR AlphaFoldDB; Q28620; -.
DR STRING; 9986.ENSOCUP00000002416; -.
DR PRIDE; Q28620; -.
DR Ensembl; ENSOCUT00000002784; ENSOCUP00000002416; ENSOCUG00000002783.
DR GeneID; 100009392; -.
DR KEGG; ocu:100009392; -.
DR CTD; 6569; -.
DR eggNOG; ENOG502QQ3I; Eukaryota.
DR GeneTree; ENSGT00950000183177; -.
DR HOGENOM; CLU_025063_0_0_1; -.
DR InParanoid; Q28620; -.
DR OMA; TWDFLPA; -.
DR OrthoDB; 976094at2759; -.
DR TreeFam; TF313981; -.
DR Proteomes; UP000001811; Chromosome 3.
DR Bgee; ENSOCUG00000002783; Expressed in kidney and 12 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005436; F:sodium:phosphate symporter activity; IDA:UniProtKB.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IDA:UniProtKB.
DR GO; GO:0055062; P:phosphate ion homeostasis; ISS:UniProtKB.
DR GO; GO:0006817; P:phosphate ion transport; ISS:UniProtKB.
DR GO; GO:0044341; P:sodium-dependent phosphate transport; IEA:InterPro.
DR InterPro; IPR003841; Na/Pi_transpt.
DR InterPro; IPR029848; Na/Pi_transpt_2A.
DR PANTHER; PTHR10010; PTHR10010; 1.
DR PANTHER; PTHR10010:SF21; PTHR10010:SF21; 1.
DR Pfam; PF02690; Na_Pi_cotrans; 2.
DR TIGRFAMs; TIGR01013; 2a58; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Sodium; Sodium transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..642
FT /note="Sodium-dependent phosphate transport protein 2A"
FT /id="PRO_0000068609"
FT TOPO_DOM 1..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 107..128
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..148
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 149..166
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 169..188
FT /note="Helical; Name=M3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..350
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 351..373
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 416..439
FT /note="Helical; Name=M5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..469
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 470..490
FT /note="Helical; Name=M6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..516
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 517..537
FT /note="Helical; Name=M7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 538..542
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 543..564
FT /note="Helical; Name=M8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60825"
FT MOD_RES 511
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT MOD_RES 626
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q60825"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60825"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 228..525
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT DISULFID 309..339
FT /evidence="ECO:0000250|UniProtKB:Q06496"
SQ SEQUENCE 642 AA; 69432 MW; A48B85C001642A8B CRC64;
MISYGEQLSS PAVSPPLVRA GLRGPMMHGA TFAYVPSPQA LHRIPGTSAY AFPSLSPVAL
TEHGCPYGEA RERHEPLPAK LALEEEQKPE SGWAQELRRT AMTLLKLPLM VTFLYLFVCS
LDVLSSAFQL AGGKVAGDIF KDNAILANPV AGLVVGILVT VLVQSSSTAT SIIVSMVSSG
LLEVSSAIPI IMGSNIGTSV TNTIVALMQA GDRTDFRRAF AGATVHDCFN WLSVLVLLPL
EAATGYLHHV TGLVVASFNI RGGRDAPDLL KTITEPFTKL IIQLDRSVIT SIATGDESLR
NHSLIRIWCH RDPVEASTSM ARAETNISRT HGNATMEKCN HIFVDTQLPD LAVGLILLAG
SLVLLCTCLI LLVKMLNSLL KGQVAKVIQK VINTDLPAPF TWVTGYFAMV VGAAMTFIVQ
SSSVFTSAIT PLVGLGVISI ERAYPLTLGS NIGTTTTAIL AALASPREKL SSSFQIALCH
FFFNISGILL WYPLPCTRLP IRMAKALGKR TAKYRWFAVL YLLVCFLLLP SLVFGISMAG
WRAMVGVGAP FGALLAFVVL INVLQSRSPG RLPKWLQTWD FLPHWMHSLQ PLDHLITHAT
LCCSRSEPRS PQLPARVFLE ELPPATPSPR LALPAHHNAT RL
