NPT2A_SHEEP
ID NPT2A_SHEEP Reviewed; 639 AA.
AC O97704;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=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=NPT2 {ECO:0000250|UniProtKB:Q60825},
GN SLC17A2 {ECO:0000250|UniProtKB:Q06495};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney cortex;
RA Wood I.S., Ford L.T., Penny J.I., Shirazi-Beechey S.P.;
RT "Characterisation of a Na+-dependent phosphate cotransporter from ovine
RT renal outer cortex.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in actively transporting phosphate into cells via
CC Na(+) cotransport in the renal brush border membrane. The cotransport
CC has a Na(+):Pi stoichiometry of 3:1 and is electrogenic.
CC {ECO:0000250|UniProtKB:Q06496}.
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:Q06496};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71256;
CC Evidence={ECO:0000250|UniProtKB:Q06496};
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 -!- SIMILARITY: Belongs to the SLC34A transporter family. {ECO:0000305}.
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DR EMBL; AJ001385; CAA04715.1; -; mRNA.
DR RefSeq; NP_001009450.1; NM_001009450.1.
DR AlphaFoldDB; O97704; -.
DR STRING; 9940.ENSOARP00000005056; -.
DR GeneID; 443505; -.
DR KEGG; oas:443505; -.
DR CTD; 6569; -.
DR eggNOG; ENOG502QQ3I; Eukaryota.
DR OrthoDB; 976094at2759; -.
DR Proteomes; UP000002356; Unplaced.
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; ISS: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..639
FT /note="Sodium-dependent phosphate transport protein 2A"
FT /id="PRO_0000068611"
FT TOPO_DOM 1..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 104..125
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..145
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 146..163
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 166..185
FT /note="Helical; Name=M3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..347
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 348..370
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 413..436
FT /note="Helical; Name=M5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..466
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 467..487
FT /note="Helical; Name=M6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 514..534
FT /note="Helical; Name=M7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 535..539
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 540..561
FT /note="Helical; Name=M8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..639
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 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60825"
FT MOD_RES 508
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT MOD_RES 623
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q60825"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60825"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 225..522
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT DISULFID 306..336
FT /evidence="ECO:0000250|UniProtKB:Q06496"
SQ SEQUENCE 639 AA; 69023 MW; 713EA39C54EC3A1F CRC64;
MISYGENLGG RAVSPLPVRG GHMMHGAAFA YVPSPQVLHR IPGTSAYGFP SVGPMALPEH
GCPYGEVVEH HDPLPAKLAL EDERKPEPGL IQKLRRAGVT LLKVPLMLSF LYLFVCSLDV
LSSAFQLAGG KVAGDIFKDN AILSNPVAGL VVGILVTVLV QSSSTSTSIV VSMVSSGLLE
VSSAIPIIMG SNIGTSVTNT IVALMQAGDR TDFRRAFAGA TVHDCFNWLS VLVLLPLEAA
TGYLHHITRL VVASFNIRGG RDAPDLLKII TEPFTKLIIQ LDKSVITSLA SGDESLRNHS
LIRVWCYPNP TEVPTPMPRA EANTSRMLRN ATLEKCNHIF VDTGLPDLAV GLILLAGSLA
LLCTCLILLV KMLNSLLKGQ VAKVIQKVIN TDFPTPFTWA TGYFAMVVGA SMTFVVQSSS
VFTSAITPLI GLGVISIERA YPLTLGSNIG TTTTAILAAL ASPREKLSSA FQIALCHFFF
NISGILLWYP VPCTRLPIRM AKALGKRTAK YRWFAVLYLL LCFLLLPSMV FGLSMAGWRA
MVGVGAPFGA LLAFVVLVSA LQHRSPGCLP KWLQTWDFLP LWVHSLKPLD HLITRATLCC
ARPEPRSPPL PTRVFLEELP PATPSPRLAM PHHHDATRL
