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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
 
 
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