Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Sodium-dependent phosphate transport protein 2A (Sodium-phosphate transport protein 2A) (Na( )-dependent phosphate cotransporter 2A) (NaPi-3) (Sodium/phosphate cotransporter 2A) (Na( )/Pi cotransporter 2A) (NaPi-2a) (Solute carrier family 34 member 1)

 NPT2A_HUMAN             Reviewed;         639 AA.
Q06495; B4DPE3;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
30-AUG-2017, entry version 156.
RecName: Full=Sodium-dependent phosphate transport protein 2A;
Short=Sodium-phosphate transport protein 2A;
AltName: Full=Na(+)-dependent phosphate cotransporter 2A;
AltName: Full=NaPi-3 {ECO:0000303|PubMed:8327470};
AltName: Full=Sodium/phosphate cotransporter 2A;
Short=Na(+)/Pi cotransporter 2A;
Short=NaPi-2a;
AltName: Full=Solute carrier family 34 member 1 {ECO:0000312|HGNC:HGNC:11019};
Name=SLC34A1 {ECO:0000312|HGNC:HGNC:11019};
Synonyms=NPT2 {ECO:0000250|UniProtKB:Q60825},
SLC17A2 {ECO:0000312|HGNC:HGNC:11019};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
TISSUE=Kidney;
PubMed=8327470; DOI=10.1073/pnas.90.13.5979;
Magagnin S., Werner A., Markovich D., Sorribas V., Stange G.,
Biber J., Murer H.;
"Expression cloning of human and rat renal cortex Na/Pi cotransport.";
Proc. Natl. Acad. Sci. U.S.A. 90:5979-5983(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[4]
INTERACTION WITH SLC9A3R1.
PubMed=22506049; DOI=10.1371/journal.pone.0034764;
Courbebaisse M., Leroy C., Bakouh N., Salaun C., Beck L.,
Grandchamp B., Planelles G., Hall R.A., Friedlander G., Prie D.;
"A new human NHERF1 mutation decreases renal phosphate transporter
NPT2a expression by a PTH-independent mechanism.";
PLoS ONE 7:E34764-E34764(2012).
[5]
FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN HCINF2, VARIANTS HCINF2
91-VAL--ALA-97 DEL; ALA-153; VAL-153; PRO-155; TRP-215; GLY-336;
GLU-408 AND ARG-488, AND CHARACTERIZATION OF VARIANTS HCINF2
91-VAL--ALA-97 DEL; ALA-153; VAL-153; PRO-155; GLY-336; GLU-408 AND
ARG-488.
PubMed=26047794; DOI=10.1681/ASN.2014101025;
Schlingmann K.P., Ruminska J., Kaufmann M., Dursun I., Patti M.,
Kranz B., Pronicka E., Ciara E., Akcay T., Bulus D., Cornelissen E.A.,
Gawlik A., Sikora P., Patzer L., Galiano M., Boyadzhiev V., Dumic M.,
Vivante A., Kleta R., Dekel B., Levtchenko E., Bindels R.J., Rust S.,
Forster I.C., Hernando N., Jones G., Wagner C.A., Konrad M.;
"Autosomal-recessive mutations in SLC34A1 encoding sodium-phosphate
cotransporter 2A cause idiopathic infantile hypercalcemia.";
J. Am. Soc. Nephrol. 27:604-614(2016).
[6]
VARIANTS NPHLOP1 PHE-48 AND MET-147, AND CHARACTERIZATION OF VARIANTS
NPHLOP1 PHE-48 AND MET-147.
PubMed=12324554; DOI=10.1056/NEJMoa020028;
Prie D., Huart V., Bakouh N., Planelles G., Dellis O., Gerard B.,
Hulin P., Benque-Blanchet F., Silve C., Grandchamp B., Friedlander G.;
"Nephrolithiasis and osteoporosis associated with hypophosphatemia
caused by mutations in the type 2a sodium-phosphate cotransporter.";
N. Engl. J. Med. 347:983-991(2002).
[7]
VARIANT FRTS2 ILE-LEU-VAL-THR-VAL-LEU-VAL-160 INS, AND
CHARACTERIZATION OF VARIANT FRTS2 ILE-LEU-VAL-THR-VAL-LEU-VAL-160 INS.
PubMed=20335586; DOI=10.1056/NEJMoa0905647;
Magen D., Berger L., Coady M.J., Ilivitzki A., Militianu D.,
Tieder M., Selig S., Lapointe J.Y., Zelikovic I., Skorecki K.;
"A loss-of-function mutation in NaPi-IIa and renal Fanconi's
syndrome.";
N. Engl. J. Med. 362:1102-1109(2010).
-!- FUNCTION: Involved in actively transporting phosphate into cells
via Na(+) cotransport in the renal brush border membrane. Probably
mediates 70-80% of the apical influx.
{ECO:0000269|PubMed:26047794, ECO:0000269|PubMed:8327470}.
-!- SUBUNIT: Interacts via its C-terminal region with PDZK2 (By
similarity). Interacts with SLC9A3R1 (PubMed:22506049).
{ECO:0000250|UniProtKB:Q60825, ECO:0000269|PubMed:22506049}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:26047794}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q06495-1; Sequence=Displayed;
Name=2;
IsoId=Q06495-2; Sequence=VSP_042311;
-!- TISSUE SPECIFICITY: Kidney and lung.
-!- DISEASE: Nephrolithiasis/osteoporosis, hypophosphatemic, 1
(NPHLOP1) [MIM:612286]: A disease characterized by decreased renal
phosphate absorption, renal phosphate wasting, hypophosphatemia,
hyperphosphaturia, hypercalciuria, nephrolithiasis and
osteoporosis. {ECO:0000269|PubMed:12324554}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Fanconi renotubular syndrome 2 (FRTS2) [MIM:613388]: A
disease due to a generalized dysfunction of the proximal kidney
tubule resulting in decreased solute and water reabsorption.
Patients have polydipsia and polyuria with phosphaturia,
glycosuria and aminoaciduria. They may develop hypophosphatemic
rickets or osteomalacia, acidosis and a tendency toward
dehydration. Some eventually develop renal insufficiency.
{ECO:0000269|PubMed:20335586}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Hypercalcemia, infantile, 2 (HCINF2) [MIM:616963]: An
autosomal recessive form of hypercalcemia, a disorder
characterized by abnormally high level of calcium in the blood,
failure to thrive, vomiting, dehydration, and nephrocalcinosis.
{ECO:0000269|PubMed:26047794}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the SLC34A transporter family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L13258; AAA36354.1; -; mRNA.
EMBL; AK298299; BAG60555.1; -; mRNA.
EMBL; AC145098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS4418.1; -. [Q06495-1]
CCDS; CCDS54953.1; -. [Q06495-2]
PIR; B48189; B48189.
RefSeq; NP_001161051.1; NM_001167579.1. [Q06495-2]
RefSeq; NP_003043.3; NM_003052.4. [Q06495-1]
UniGene; Hs.936; -.
ProteinModelPortal; Q06495; -.
BioGrid; 112457; 1.
STRING; 9606.ENSP00000321424; -.
ChEMBL; CHEMBL3769299; -.
TCDB; 2.A.58.1.5; the phosphate:na(+) symporter (pnas) family.
iPTMnet; Q06495; -.
PhosphoSitePlus; Q06495; -.
BioMuta; SLC34A1; -.
DMDM; 730113; -.
PaxDb; Q06495; -.
PeptideAtlas; Q06495; -.
PRIDE; Q06495; -.
Ensembl; ENST00000324417; ENSP00000321424; ENSG00000131183. [Q06495-1]
Ensembl; ENST00000512593; ENSP00000423022; ENSG00000131183. [Q06495-2]
GeneID; 6569; -.
KEGG; hsa:6569; -.
UCSC; uc003mgk.5; human. [Q06495-1]
CTD; 6569; -.
DisGeNET; 6569; -.
GeneCards; SLC34A1; -.
HGNC; HGNC:11019; SLC34A1.
HPA; HPA051255; -.
MalaCards; SLC34A1; -.
MIM; 182309; gene.
MIM; 612286; phenotype.
MIM; 613388; phenotype.
MIM; 616963; phenotype.
neXtProt; NX_Q06495; -.
OpenTargets; ENSG00000131183; -.
Orphanet; 244305; Dominant hypophosphatemia with nephrolithiasis or osteoporosis.
Orphanet; 3337; Primary Fanconi syndrome.
PharmGKB; PA35887; -.
eggNOG; ENOG410IE8P; Eukaryota.
eggNOG; COG1283; LUCA.
GeneTree; ENSGT00390000005032; -.
HOGENOM; HOG000006550; -.
HOVERGEN; HBG079110; -.
InParanoid; Q06495; -.
KO; K14683; -.
OMA; CPYGEVL; -.
OrthoDB; EOG091G0DR5; -.
PhylomeDB; Q06495; -.
TreeFam; TF313981; -.
Reactome; R-HSA-427589; Type II Na+/Pi cotransporters.
Reactome; R-HSA-5683826; Surfactant metabolism.
SignaLink; Q06495; -.
GeneWiki; Sodium/phosphate_cotransporter; -.
GenomeRNAi; 6569; -.
PRO; PR:Q06495; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000131183; -.
CleanEx; HS_SLC17A2; -.
CleanEx; HS_SLC34A1; -.
ExpressionAtlas; Q06495; baseline and differential.
Genevisible; Q06495; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0005903; C:brush border; IBA:GO_Central.
GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005768; C:endosome; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0031982; C:vesicle; IBA:GO_Central.
GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0015321; F:sodium-dependent phosphate transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0005436; F:sodium:phosphate symporter activity; IBA:GO_Central.
GO; GO:1901684; P:arsenate ion transmembrane transport; IEA:Ensembl.
GO; GO:0030643; P:cellular phosphate ion homeostasis; IBA:GO_Central.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0071248; P:cellular response to metal ion; IEA:Ensembl.
GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl.
GO; GO:0072734; P:cellular response to staurosporine; IEA:Ensembl.
GO; GO:0097187; P:dentinogenesis; IEA:Ensembl.
GO; GO:1901128; P:gentamycin metabolic process; IEA:Ensembl.
GO; GO:0009100; P:glycoprotein metabolic process; IEA:Ensembl.
GO; GO:0042431; P:indole metabolic process; IEA:Ensembl.
GO; GO:0001822; P:kidney development; IEA:Ensembl.
GO; GO:0001503; P:ossification; IEA:Ensembl.
GO; GO:0055062; P:phosphate ion homeostasis; IDA:UniProtKB.
GO; GO:0006817; P:phosphate ion transport; IDA:UniProtKB.
GO; GO:0045838; P:positive regulation of membrane potential; IEA:Ensembl.
GO; GO:2000187; P:positive regulation of phosphate transmembrane transport; IEA:Ensembl.
GO; GO:2000120; P:positive regulation of sodium-dependent phosphate transport; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0046686; P:response to cadmium ion; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
GO; GO:0010288; P:response to lead ion; IDA:UniProtKB.
GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
GO; GO:0046689; P:response to mercury ion; IDA:UniProtKB.
GO; GO:0035864; P:response to potassium ion; IEA:Ensembl.
GO; GO:0097066; P:response to thyroid hormone; IEA:Ensembl.
GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
GO; GO:0072350; P:tricarboxylic acid metabolic process; IEA:Ensembl.
InterPro; IPR003841; Na/Pi_transpt.
InterPro; IPR029848; Na/Pi_transpt_2A.
PANTHER; PTHR10010; PTHR10010; 1.
PANTHER; PTHR10010:SF41; PTHR10010:SF41; 1.
Pfam; PF02690; Na_Pi_cotrans; 2.
TIGRFAMs; TIGR01013; 2a58; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disease mutation; Disulfide bond; Glycoprotein; Ion transport;
Membrane; Phosphoprotein; Reference proteome; Sodium;
Sodium transport; Symport; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 639 Sodium-dependent phosphate transport
protein 2A.
/FTId=PRO_0000068607.
TOPO_DOM 1 103 Cytoplasmic. {ECO:0000255}.
TRANSMEM 104 125 Helical; Name=M1. {ECO:0000255}.
TOPO_DOM 126 145 Extracellular. {ECO:0000255}.
TRANSMEM 146 163 Helical; Name=M2. {ECO:0000255}.
TOPO_DOM 164 165 Cytoplasmic. {ECO:0000255}.
TRANSMEM 166 185 Helical; Name=M3. {ECO:0000255}.
TOPO_DOM 186 347 Extracellular. {ECO:0000255}.
TRANSMEM 348 370 Helical; Name=M4. {ECO:0000255}.
TOPO_DOM 371 412 Cytoplasmic. {ECO:0000255}.
TRANSMEM 413 436 Helical; Name=M5. {ECO:0000255}.
TOPO_DOM 437 466 Extracellular. {ECO:0000255}.
TRANSMEM 467 487 Helical; Name=M6. {ECO:0000255}.
TOPO_DOM 488 513 Cytoplasmic. {ECO:0000255}.
TRANSMEM 514 534 Helical; Name=M7. {ECO:0000255}.
TOPO_DOM 535 539 Extracellular. {ECO:0000255}.
TRANSMEM 540 561 Helical; Name=M8. {ECO:0000255}.
TOPO_DOM 562 639 Cytoplasmic. {ECO:0000255}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000250|UniProtKB:Q06496}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000250|UniProtKB:Q60825}.
MOD_RES 508 508 Phosphothreonine; by PKC. {ECO:0000255}.
MOD_RES 607 607 Phosphoserine.
{ECO:0000250|UniProtKB:Q06496}.
MOD_RES 623 623 Phosphothreonine.
{ECO:0000250|UniProtKB:Q60825}.
MOD_RES 625 625 Phosphoserine.
{ECO:0000250|UniProtKB:Q60825}.
CARBOHYD 298 298 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 225 522 {ECO:0000250}.
DISULFID 306 336 {ECO:0000250}.
VAR_SEQ 313 639 APTSMSRAEANSSQTLGNATMEKCNHIFVDTGLPDLAVGLI
LLAGSLVLLCTCLILLVKMLNSLLKGQVAKVIQKVINTDFP
APFTWVTGYFAMVVGASMTFVVQSSSVFTSAITPLIGLGVI
SIERAYPLTLGSNIGTTTTAILAALASPREKLSSAFQIALC
HFFFNISGILLWYPVPCTRLPIRMAKALGKRTAKYRWFAVL
YLLVCFLLLPSLVFGISMAGWQVMVGVGTPFGALLAFVVLI
NVLQSRSPGHLPKWLQTWDFLPRWMHSLKPLDHLITRATLC
CARPEPRSPPLPPRVFLEELPPATPSPRLALPAHHNATRL
-> QNLEGREITHFDLRKKQAMEDSSVPHCP (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042311.
VARIANT 48 48 A -> F (in NPHLOP1; causes
hypophosphatemic urolithiasis; requires 2
nucleotide substitutions; results in
lower phosphate current, decreases
affinity for phosphate and decreases
phosphate uptake compared to wild-type;
shows a dominant-negative effect;
dbSNP:rs121918610).
{ECO:0000269|PubMed:12324554}.
/FTId=VAR_024765.
VARIANT 91 97 Missing (in HCINF2; no change in
phosphate transport activity; changed
localization to the apical plasma
membrane; partial retention inside the
cell). {ECO:0000269|PubMed:26047794}.
/FTId=VAR_077913.
VARIANT 147 147 V -> M (in NPHLOP1; causes
hypophosphatemic osteoporosis; results in
lower phosphate current, decreases
affinity for phosphate and decreases
phosphate uptake compared to wild-type;
shows a dominant-negative effect;
dbSNP:rs121918611).
{ECO:0000269|PubMed:12324554}.
/FTId=VAR_024766.
VARIANT 153 153 G -> A (in HCINF2; loss of phosphate
transport activity; loss of localization
to apical plasma membrane; display a
complete intracellular retention and no
detectable actin colocalization).
{ECO:0000269|PubMed:26047794}.
/FTId=VAR_077914.
VARIANT 153 153 G -> V (in HCINF2; loss of phosphate
transport activity; loss of localization
to apical plasma membrane; display a
complete intracellular retention and no
detectable actin colocalization;
dbSNP:rs769409705).
{ECO:0000269|PubMed:26047794}.
/FTId=VAR_077915.
VARIANT 155 155 L -> P (in HCINF2; loss of phosphate
transport activity; loss of localization
to apical plasma membrane; display a
complete intracellular retention and no
detectable actin colocalization;
dbSNP:rs369770760).
{ECO:0000269|PubMed:26047794}.
/FTId=VAR_077916.
VARIANT 160 160 V -> VILVTVLV (in FRTS2; loss of function
in the homozygous state).
{ECO:0000269|PubMed:20335586}.
/FTId=VAR_063812.
VARIANT 215 215 R -> W (in HCINF2; dbSNP:rs577273266).
{ECO:0000269|PubMed:26047794}.
/FTId=VAR_077917.
VARIANT 336 336 C -> G (in HCINF2; loss of phosphate
transport activity; loss of localization
to apical plasma membrane; display a
complete intracellular retention and no
detectable actin colocalization;
dbSNP:rs876661338).
{ECO:0000269|PubMed:26047794}.
/FTId=VAR_077918.
VARIANT 408 408 V -> E (in HCINF2; loss of phosphate
transport activity; loss of localization
to apical plasma membrane; a complete
intracellular retention and no detectable
actin colocalization; dbSNP:rs140649226).
{ECO:0000269|PubMed:26047794}.
/FTId=VAR_077919.
VARIANT 488 488 W -> R (in HCINF2; loss of phosphate
transport activity; loss of localization
to apical plasma membrane; display a
complete intracellular retention and no
detectable actin colocalization).
{ECO:0000269|PubMed:26047794}.
/FTId=VAR_077920.
SEQUENCE 639 AA; 68937 MW; 65D21D968C35D61B CRC64;
MLSYGERLGS PAVSPLPVRG GHVMRGTAFA YVPSPQVLHR IPGTSAYAFP SLGPVALAEH
TCPCGEVLER HEPLPAKLAL EEEQKPESRL VPKLRQAGAM LLKVPLMLTF LYLFVCSLDM
LSSAFQLAGG KVAGDIFKDN AILSNPVAGL VVGILVTVLV QSSSTSTSII VSMVSSGLLE
VSSAIPIIMG SNIGTSVTNT IVALMQAGDR TDFRRAFAGA TVHDCFNWLS VLVLLPLEAA
TGYLHHITRL VVASFNIHGG RDAPDLLKII TEPFTKLIIQ LDESVITSIA TGDESLRNHS
LIQIWCHPDS LQAPTSMSRA EANSSQTLGN ATMEKCNHIF VDTGLPDLAV GLILLAGSLV
LLCTCLILLV KMLNSLLKGQ VAKVIQKVIN TDFPAPFTWV TGYFAMVVGA SMTFVVQSSS
VFTSAITPLI GLGVISIERA YPLTLGSNIG TTTTAILAAL ASPREKLSSA FQIALCHFFF
NISGILLWYP VPCTRLPIRM AKALGKRTAK YRWFAVLYLL VCFLLLPSLV FGISMAGWQV
MVGVGTPFGA LLAFVVLINV LQSRSPGHLP KWLQTWDFLP RWMHSLKPLD HLITRATLCC
ARPEPRSPPL PPRVFLEELP PATPSPRLAL PAHHNATRL


Related products :

Catalog number Product name Quantity
EIAAB27713 Homo sapiens,Human,Na(+)_Pi cotransporter 2B,Na(+)-dependent phosphate cotransporter 2B,NaPi-2b,NaPi3b,SLC34A2,Sodium_phosphate cotransporter 2B,Sodium-dependent phosphate transport protein 2B,Sodium-
EIAAB27717 Na(+)_Pi cotransporter 2C,Na(+)-dependent phosphate cotransporter 2C,NaPi-2c,Rat,Rattus norvegicus,Slc34a3,Sodium_phosphate cotransporter 2C,Sodium-dependent phosphate transport protein 2C,Sodium-phos
EIAAB27716 Mouse,Mus musculus,Na(+)_Pi cotransporter 2C,Na(+)-dependent phosphate cotransporter 2C,NaPi-2c,Npt2c,Slc34a3,Sodium_phosphate cotransporter 2C,Sodium-dependent phosphate transport protein 2C,Sodium-p
EIAAB27711 Mouse,Mus musculus,Na(+)_Pi cotransporter 2B,Na(+)-dependent phosphate cotransporter 2B,NaPi-2b,Npt2b,Slc34a2,Sodium_phosphate cotransporter 2B,Sodium-dependent phosphate transport protein 2B,Sodium-p
EIAAB27712 Bos taurus,Bovine,Na(+)_Pi cotransporter 2B,Na(+)-dependent phosphate cotransporter 2B,NaPi-2b,SLC34A2,Sodium_phosphate cotransporter 2B,Sodium-dependent phosphate transport protein 2B,Sodium-phosphat
EIAAB27708 Homo sapiens,Human,Na(+)_Pi cotransporter 2A,Na(+)-dependent phosphate cotransporter 2A,NaPi-2a,NaPi-3,NPT2,SLC17A2,SLC34A1,Sodium_phosphate cotransporter 2A,Sodium-dependent phosphate transport prote
EIAAB27710 Mouse,Mus musculus,Na(+)_Pi cotransporter 2A,Na(+)-dependent phosphate cotransporter 2A,NaPi-2a,NaPi-7,Npt2,Slc17a2,Slc34a1,Sodium_phosphate cotransporter 2A,Sodium-dependent phosphate transport prote
EIAAB27707 Na(+)_Pi cotransporter 2A,Na(+)-dependent phosphate cotransporter 2A,NaPi-2a,NaPi-6,Oryctolagus cuniculus,Rabbit,SLC17A2,SLC34A1,Sodium_phosphate cotransporter 2A,Sodium-dependent phosphate transport
EIAAB27709 Na(+)_Pi cotransporter 2A,Na(+)-dependent phosphate cotransporter 2A,NaPi-2a,Rat,Rattus norvegicus,Slc17a2,Slc34a1,Sodium_phosphate cotransporter 2A,Sodium-dependent phosphate transport protein 2A,Sod
EIAAB27714 Na(+)_Pi cotransporter 2B,Na(+)-dependent phosphate cotransporter 2B,NaPi-2b,Rat,Rattus norvegicus,rNaPi IIb,Slc34a2,Sodium_phosphate cotransporter 2B,Sodium-dependent phosphate transport protein 2B,S
EIAAB27706 Na(+)_PI cotransporter 1,NAPI-1,NPT1,Oryctolagus cuniculus,Rabbit,Renal Na(+)-dependent phosphate cotransporter 1,Renal sodium-dependent phosphate transport protein 1,Renal sodium-phosphate transport
18-003-42439 Sodium-dependent phosphate transport protein 3 - Sodium_phosphate cotransporter 3; Na(+)_PI cotransporter 3; Solute carrier family 18 member 2 Polyclonal 0.05 mg Aff Pur
EIAAB27718 Bos taurus,Bovine,Na(+)_PI cotransporter 3,NPT3,SLC17A2,Sodium_phosphate cotransporter 3,Sodium-dependent phosphate transport protein 3,Solute carrier family 17 member 3
EIAAB27719 Mouse,Mus musculus,Na(+)_PI cotransporter 3,Npt3,Slc17a2,Sodium_phosphate cotransporter 3,Sodium-dependent phosphate transport protein 3,Solute carrier family 17 member 2
EIAAB27720 Homo sapiens,Human,Na(+)_PI cotransporter 3,NPT3,SLC17A2,Sodium_phosphate cotransporter 3,Sodium-dependent phosphate transport protein 3,Solute carrier family 17 member 2
EIAAB27721 Homo sapiens,Human,Na(+)_PI cotransporter 4,NPT4,SLC17A3,Sodium_phosphate cotransporter 4,Sodium-dependent phosphate transport protein 4,Solute carrier family 17 member 3
EIAAB27704 Homo sapiens,Human,Na(+)_PI cotransporter 1,Na_Pi-4,NPT1,Renal Na(+)-dependent phosphate cotransporter 1,Renal sodium-dependent phosphate transport protein 1,Renal sodium-phosphate transport protein 1
EIAAB27703 Na(+)_PI cotransporter 1,Npt1,Rat,Rattus norvegicus,Renal Na(+)-dependent phosphate cotransporter 1,Renal sodium-dependent phosphate transport protein 1,Renal sodium-phosphate transport protein 1,Slc1
EIAAB27705 Mouse,Mus musculus,Na(+)_PI cotransporter 1,Npt1,Renal Na(+)-dependent phosphate cotransporter 1,Renal sodium-dependent phosphate transport protein 1,Renal sodium-phosphate transport protein 1,Slc17a1
EIAAB27715 Homo sapiens,Human,Na(+)_Pi cotransporter 2C,Na(+)-dependent phosphate cotransporter 2C,NaPi-2c,NPT2C,NPTIIC,SLC34A3,Sodium_inorganic phosphate cotransporter IIC,Sodium_phosphate cotransporter 2C,Sodi
EIAAB36690 Mouse,Mus musculus,Phosphate transporter 2,Pit2,PiT-2,Slc20a2,Sodium-dependent phosphate transporter 2,Solute carrier family 20 member 2,Type III sodium-dependent phosphate transporter
CSB-EL021422RA Rat solute carrier family 17 (sodium-dependent inorganic phosphate cotransporter), member 6 (SLC17A6) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL021424RA Rat solute carrier family 17 (sodium-dependent inorganic phosphate cotransporter), member 8 (SLC17A8) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL021423RA Rat solute carrier family 17 (sodium-dependent inorganic phosphate cotransporter), member 7 (SLC17A7) ELISA kit, Species Rat, Sample Type serum, plasma 96T
SLC17A6 SLC17A6 Gene solute carrier family 17 (sodium-dependent inorganic phosphate cotransporter), member 6


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur