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Na( )/H( ) exchange regulatory cofactor NHE-RF1 (NHERF-1) (Ezrin-radixin-moesin-binding phosphoprotein 50) (EBP50) (Regulatory cofactor of Na( )/H( ) exchanger) (Sodium-hydrogen exchanger regulatory factor 1) (Solute carrier family 9 isoform A3 regulatory factor 1)

 NHRF1_HUMAN             Reviewed;         358 AA.
O14745; B3KY21; O43552; Q86WQ5;
02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 187.
RecName: Full=Na(+)/H(+) exchange regulatory cofactor NHE-RF1;
Short=NHERF-1;
AltName: Full=Ezrin-radixin-moesin-binding phosphoprotein 50;
Short=EBP50;
AltName: Full=Regulatory cofactor of Na(+)/H(+) exchanger;
AltName: Full=Sodium-hydrogen exchanger regulatory factor 1;
AltName: Full=Solute carrier family 9 isoform A3 regulatory factor 1;
Name=SLC9A3R1; Synonyms=NHERF, NHERF1;
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), PROTEIN SEQUENCE OF 19-32 AND
341-350, PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND INTERACTION WITH EZR AND MSN.
PubMed=9314537; DOI=10.1083/jcb.139.1.169;
Reczek D., Berryman M., Bretscher A.;
"Identification of EBP50: a PDZ-containing phosphoprotein that
associates with members of the ezrin-radixin-moesin family.";
J. Cell Biol. 139:169-179(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND INTERACTION WITH EZR; RDX AND MSN.
TISSUE=Fetal brain;
PubMed=9430655; DOI=10.1074/jbc.273.3.1273;
Murthy A., Gonzalez-Agosti C., Cordero E., Pinney D., Candia C.,
Solomon F., Gusella J., Ramesh V.;
"NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common
interactor for merlin and ERM (MERM) proteins.";
J. Biol. Chem. 273:1273-1276(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Liver;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Blood, Lymph, Pancreas, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-13.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[8]
PROTEIN SEQUENCE OF 2-12; 39-49 AND 89-100, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=T-cell;
Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
Submitted (MAY-2006) to UniProtKB.
[9]
FUNCTION, INTERACTION WITH SLC9A3, AND TISSUE SPECIFICITY.
PubMed=9096337; DOI=10.1073/pnas.94.7.3010;
Yun C.H.C., Oh S., Zizak M., Steplock D., Tsao S., Tse C.-M.,
Weinman E.J., Donowitz M.;
"cAMP-mediated inhibition of the epithelial brush border Na+/H+
exchanger, NHE3, requires an associated regulatory protein.";
Proc. Natl. Acad. Sci. U.S.A. 94:3010-3015(1997).
[10]
FUNCTION, AND INTERACTION WITH ADRB2.
PubMed=10499588; DOI=10.1038/45816;
Cao T.T., Deacon H.W., Reczek D., Bretscher A., von Zastrow M.;
"A kinase-regulated PDZ-domain interaction controls endocytic sorting
of the beta2-adrenergic receptor.";
Nature 401:286-290(1999).
[11]
INTERACTION WITH PAG1, AND SUBCELLULAR LOCATION.
PubMed=11684085; DOI=10.1016/S0014-5793(01)02955-6;
Brdickova N., Brdicka T., Andera L., Spicka J., Angelisova P.,
Milgram S.L., Horejsi V.;
"Interaction between two adapter proteins, PAG and EBP50: a possible
link between membrane rafts and actin cytoskeleton.";
FEBS Lett. 507:133-136(2001).
[12]
INTERACTION WITH EPI64; ARHGAP17; PLCB3 AND EZR.
PubMed=11285285; DOI=10.1083/jcb.153.1.191;
Reczek D., Bretscher A.;
"Identification of EPI64, a TBC/rabGAP domain-containing microvillar
protein that binds to the first PDZ domain of EBP50 and E3KARP.";
J. Cell Biol. 153:191-206(2001).
[13]
INTERACTION WITH RACK1.
PubMed=11956211; DOI=10.1074/jbc.M201917200;
Liedtke C.M., Yun C.H.C., Kyle N., Wang D.;
"Protein kinase C epsilon-dependent regulation of cystic fibrosis
transmembrane regulator involves binding to a receptor for activated C
kinase (RACK1) and RACK1 binding to Na+/H+ exchange regulatory
factor.";
J. Biol. Chem. 277:22925-22933(2002).
[14]
INTERACTION WITH OPRK1.
PubMed=12004055; DOI=10.1074/jbc.M200058200;
Li J.-G., Chen C., Liu-Chen L.-Y.;
"Ezrin-radixin-moesin-binding phosphoprotein-50/Na+/H+ exchanger
regulatory factor (EBP50/NHERF) blocks U50,488H-induced down-
regulation of the human kappa opioid receptor by enhancing its
recycling rate.";
J. Biol. Chem. 277:27545-27552(2002).
[15]
INTERACTION WITH NOS2.
PubMed=12080081; DOI=10.1074/jbc.M205764200;
Glynne P.A., Darling K.E.A., Picot J., Evans T.J.;
"Epithelial inducible nitric-oxide synthase is an apical EBP50-binding
protein that directs vectorial nitric oxide output.";
J. Biol. Chem. 277:33132-33138(2002).
[16]
INTERACTION WITH GNAQ.
PubMed=12193606; DOI=10.1074/jbc.M207910200;
Rochdi M.D., Watier V., La Madeleine C., Nakata H., Kozasa T.,
Parent J.-L.;
"Regulation of GTP-binding protein alpha q (Galpha q) signaling by the
ezrin-radixin-moesin-binding phosphoprotein-50 (EBP50).";
J. Biol. Chem. 277:40751-40759(2002).
[17]
INTERACTION WITH SLC4A7 AND CFTR.
PubMed=12403779; DOI=10.1074/jbc.M201862200;
Park M., Ko S.B.H., Choi J.Y., Muallem G., Thomas P.J., Pushkin A.,
Lee M.-S., Kim J.Y., Lee M.G., Muallem S., Kurtz I.;
"The cystic fibrosis transmembrane conductance regulator interacts
with and regulates the activity of the HCO3- salvage transporter human
Na+-HCO3-cotransport isoform 3.";
J. Biol. Chem. 277:50503-50509(2002).
[18]
INTERACTION WITH TRPC4.
PubMed=12154080;
Mery L., Strauss B., Dufour J.F., Krause K.H., Hoth M.;
"The PDZ-interacting domain of TRPC4 controls its localization and
surface expression in HEK293 cells.";
J. Cell Sci. 115:3497-3508(2002).
[19]
INDUCTION BY ESTROGEN.
PubMed=12145337; DOI=10.1210/me.2001-0290;
Ediger T.R., Park S.-E., Katzenellenbogen B.S.;
"Estrogen receptor inducibility of the human Na+/H+ exchanger
regulatory factor/ezrin-radixin-moesin binding protein 50 (NHE-
RF/EBP50) gene involving multiple half-estrogen response elements.";
Mol. Endocrinol. 16:1828-1839(2002).
[20]
INTERACTION WITH SLC4A7 AND ATP6V1B1.
PubMed=12444018; DOI=10.1152/ajpcell.00225.2002;
Pushkin A., Abuladze N., Newman D., Muronets V., Sassani P.,
Tatishchev S., Kurtz I.;
"The COOH termini of NBC3 and the 56-kDa H+-ATPase subunit are PDZ
motifs involved in their interaction.";
Am. J. Physiol. 284:C667-C673(2003).
[21]
INTERACTION WITH SLC26A6.
PubMed=12444019; DOI=10.1152/ajpcell.00270.2002;
Lohi H., Lamprecht G., Markovich D., Heil A., Kujala M., Seidler U.,
Kere J.;
"Isoforms of SLC26A6 mediate anion transport and have functional PDZ
interaction domains.";
Am. J. Physiol. 284:C769-C779(2003).
[22]
INTERACTION WITH CTNNB1.
PubMed=12830000; DOI=10.1053/jhep.2003.50270;
Shibata T., Chuma M., Kokubu A., Sakamoto M., Hirohashi S.;
"EBP50, a beta-catenin-associating protein, enhances Wnt signaling and
is over-expressed in hepatocellular carcinoma.";
Hepatology 38:178-186(2003).
[23]
INTERACTION WITH CLCN3.
PubMed=12471024; DOI=10.1074/jbc.M211050200;
Gentzsch M., Cui L., Mengos A., Chang X.-B., Chen J.-H., Riordan J.R.;
"The PDZ-binding chloride channel ClC-3B localizes to the Golgi and
associates with cystic fibrosis transmembrane conductance regulator-
interacting PDZ proteins.";
J. Biol. Chem. 278:6440-6449(2003).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[31]
INTERACTION WITH MCC.
PubMed=19555689; DOI=10.1016/j.febslet.2009.06.034;
Arnaud C., Sebbagh M., Nola S., Audebert S., Bidaut G., Hermant A.,
Gayet O., Dusetti N.J., Ollendorff V., Santoni M.J., Borg J.P.,
Lecine P.;
"MCC, a new interacting protein for Scrib, is required for cell
migration in epithelial cells.";
FEBS Lett. 583:2326-2332(2009).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-280, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-269 AND
SER-280, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[36]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[37]
INTERACTION WITH SLC34A1, VARIANT NPHLOP2 ALA-68, AND CHARACTERIZATION
OF VARIANT NPHLOP2 ALA-68.
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).
[38]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-46 AND SER-280,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; SER-280 AND
SER-294, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[41]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[42]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 11-99 IN COMPLEX WITH CFTR.
PubMed=11304524; DOI=10.1074/jbc.C100154200;
Karthikeyan S., Leung T., Ladias J.A.A.;
"Structural basis of the Na+/H+ exchanger regulatory factor PDZ1
interaction with the carboxyl-terminal region of the cystic fibrosis
transmembrane conductance regulator.";
J. Biol. Chem. 276:19683-19686(2001).
[43]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 11-99, AND HOMODIMERIZATION.
PubMed=11352585; DOI=10.1006/jmbi.2001.4634;
Karthikeyan S., Leung T., Birrane G., Webster G., Ladias J.A.A.;
"Crystal structure of the PDZ1 domain of human Na(+)/H(+) exchanger
regulatory factor provides insights into the mechanism of carboxyl-
terminal leucine recognition by class I PDZ domains.";
J. Mol. Biol. 308:963-973(2001).
[44]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 11-99 IN COMPLEX WITH PDGFRA;
PDGFRB OR ADRB2.
PubMed=11882663; DOI=10.1074/jbc.M201507200;
Karthikeyan S., Leung T., Ladias J.A.A.;
"Structural determinants of the Na+/H+ exchanger regulatory factor
interaction with the beta 2 adrenergic and platelet-derived growth
factor receptors.";
J. Biol. Chem. 277:18973-18978(2002).
[45]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 321-358 IN COMPLEX WITH MSX,
AND MUTAGENESIS OF PHE-355 AND LEU-358.
PubMed=15020681; DOI=10.1242/jcs.01038;
Finnerty C.M., Chambers D., Ingraffea J., Faber H.R., Karplus P.A.,
Bretscher A.;
"The EBP50-moesin interaction involves a binding site regulated by
direct masking on the FERM domain.";
J. Cell Sci. 117:1547-1552(2004).
[46]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 331-358 IN COMPLEX WITH RDX.
PubMed=16615918; DOI=10.1016/j.str.2006.01.015;
Terawaki S., Maesaki R., Hakoshima T.;
"Structural basis for NHERF recognition by ERM proteins.";
Structure 14:777-789(2006).
[47]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 150-236.
Structural genomics consortium (SGC);
"The crystal structure of the 2nd PDZ domain of the human NHERF-1
(SLC9A3R1).";
Submitted (MAR-2007) to the PDB data bank.
[48]
FUNCTION IN RENAL PHOSPHATE ABSORPTION, VARIANTS NPHLOP2 VAL-110;
GLN-153 AND LYS-225, AND CHARACTERIZATION OF VARIANTS NPHLOP2 VAL-110;
GLN-153 AND LYS-225.
PubMed=18784102; DOI=10.1056/NEJMoa0802836;
Karim Z., Gerard B., Bakouh N., Alili R., Leroy C., Beck L., Silve C.,
Planelles G., Urena-Torres P., Grandchamp B., Friedlander G., Prie D.;
"NHERF1 mutations and responsiveness of renal parathyroid hormone.";
N. Engl. J. Med. 359:1128-1135(2008).
-!- FUNCTION: Scaffold protein that connects plasma membrane proteins
with members of the ezrin/moesin/radixin family and thereby helps
to link them to the actin cytoskeleton and to regulate their
surface expression. Necessary for recycling of internalized ADRB2.
Was first known to play a role in the regulation of the activity
and subcellular location of SLC9A3. Necessary for cAMP-mediated
phosphorylation and inhibition of SLC9A3. May enhance Wnt
signaling. May participate in HTR4 targeting to microvilli (By
similarity). Involved in the regulation of phosphate reabsorption
in the renal proximal tubules. Involved in sperm capacitation. May
participate in the regulation of the chloride and bicarbonate
homeostasis in spermatozoa. {ECO:0000250,
ECO:0000269|PubMed:10499588, ECO:0000269|PubMed:18784102,
ECO:0000269|PubMed:9096337, ECO:0000269|PubMed:9430655}.
-!- SUBUNIT: Homodimer, and heterodimer with SLC9A3R2. Binds the N-
termini of EZR, RDX and MSN. Binds the C-termini of PDGFRA,
PDGFRB, ADRB2, NOS2 and CFTR. Binds ARHGAP17, EPI64, RACK1, OPRK1,
GNAQ, CTNNB1 and PLCB3. Binds PDZK1 (By similarity). Interacts
with CLCN3. Binds the C-terminus of PAG1. In resting T-cells, part
of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR
activation. Forms a complex with CFTR and SLC4A7. Forms a complex
with SLC4A7 and ATP6V1B1. Interacts with TRPC4 (via the PDZ-
binding domain). Directly interacts with HTR4 (By similarity).
Interacts (via the PDZ 1 domain) with PODXL (via the C-terminal
PDZ-binding motif DTHL); interaction is not detected in glomerular
epithelium cells. Interacts (via the PDZ 1 domain) with PODXL (via
the C-terminal PDZ-binding motif DTHL); the interaction take place
early in the secretory pathway and is necessary for its apical
membrane sorting (By similarity). Interacts with SLC26A3 (By
similarity). Interacts with MCC. Interacts with SLC34A1. Interacts
(via the PDZ domains) with SLC26A6 isoform 4 and isoform 5.
{ECO:0000250, ECO:0000269|PubMed:10499588,
ECO:0000269|PubMed:11285285, ECO:0000269|PubMed:11304524,
ECO:0000269|PubMed:11684085, ECO:0000269|PubMed:11882663,
ECO:0000269|PubMed:11956211, ECO:0000269|PubMed:12004055,
ECO:0000269|PubMed:12080081, ECO:0000269|PubMed:12154080,
ECO:0000269|PubMed:12193606, ECO:0000269|PubMed:12403779,
ECO:0000269|PubMed:12444018, ECO:0000269|PubMed:12444019,
ECO:0000269|PubMed:12471024, ECO:0000269|PubMed:12830000,
ECO:0000269|PubMed:15020681, ECO:0000269|PubMed:16615918,
ECO:0000269|PubMed:19555689, ECO:0000269|PubMed:22506049,
ECO:0000269|PubMed:9096337, ECO:0000269|PubMed:9314537,
ECO:0000269|PubMed:9430655}.
-!- INTERACTION:
P07550:ADRB2; NbExp=6; IntAct=EBI-349787, EBI-491169;
P13569:CFTR; NbExp=5; IntAct=EBI-349787, EBI-349854;
P15311:EZR; NbExp=2; IntAct=EBI-349787, EBI-1056902;
Q9R0W0:mGluR1a (xeno); NbExp=2; IntAct=EBI-349787, EBI-8505383;
P26038:MSN; NbExp=4; IntAct=EBI-349787, EBI-528768;
P35240-1:NF2; NbExp=4; IntAct=EBI-349787, EBI-1014500;
P47900:P2RY1; NbExp=2; IntAct=EBI-349787, EBI-8677223;
P09619:PDGFRB; NbExp=5; IntAct=EBI-349787, EBI-641237;
O60346:PHLPP1; NbExp=2; IntAct=EBI-349787, EBI-2511516;
O60346-2:PHLPP1; NbExp=5; IntAct=EBI-349787, EBI-11165225;
Q6ZVD8:PHLPP2; NbExp=5; IntAct=EBI-349787, EBI-2511496;
P60484:PTEN; NbExp=7; IntAct=EBI-349787, EBI-696162;
P26043:Rdx (xeno); NbExp=2; IntAct=EBI-349787, EBI-647737;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Apical cell
membrane {ECO:0000250}. Endomembrane system; Peripheral membrane
protein. Cell projection, filopodium. Cell projection, ruffle.
Cell projection, microvillus. Note=Translocates from the cytoplasm
to the apical cell membrane in a PODXL-dependent manner.
Colocalizes with CFTR at the midpiece of sperm tail (By
similarity). Colocalizes with actin in microvilli-rich apical
regions of the syncytiotrophoblast. Found in microvilli, ruffling
membrane and filopodia of HeLa cells. Present in lipid rafts of T-
cells. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O14745-1; Sequence=Displayed;
Name=2;
IsoId=O14745-2; Sequence=VSP_055497;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in liver, kidney, pancreas, prostate,
spleen, small intestine and placenta, in particular in the
syncytiotrophoblast. {ECO:0000269|PubMed:9096337,
ECO:0000269|PubMed:9314537}.
-!- INDUCTION: By estrogen. {ECO:0000269|PubMed:12145337}.
-!- PTM: Phosphorylated on serine residues.
{ECO:0000269|PubMed:9314537}.
-!- DISEASE: Nephrolithiasis/osteoporosis, hypophosphatemic, 2
(NPHLOP2) [MIM:612287]: A disease characterized by decreased renal
phosphate absorption, renal phosphate wasting, hypophosphatemia,
hyperphosphaturia, hypercalciuria, nephrolithiasis and
osteoporosis. {ECO:0000269|PubMed:18784102,
ECO:0000269|PubMed:22506049}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAH49220.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SLC9A3R1ID46023ch17q25.html";
-----------------------------------------------------------------------
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EMBL; AF015926; AAC52084.1; -; mRNA.
EMBL; AF036241; AAC04572.1; -; mRNA.
EMBL; AK128474; BAG54683.1; -; mRNA.
EMBL; AC016888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471099; EAW89189.1; -; Genomic_DNA.
EMBL; BC001443; AAH01443.1; -; mRNA.
EMBL; BC003361; AAH03361.1; -; mRNA.
EMBL; BC011777; AAH11777.1; -; mRNA.
EMBL; BC049220; AAH49220.1; ALT_INIT; mRNA.
EMBL; BC053350; AAH53350.1; -; mRNA.
CCDS; CCDS11705.1; -. [O14745-1]
RefSeq; NP_004243.1; NM_004252.4. [O14745-1]
UniGene; Hs.724482; -.
UniGene; Hs.744126; -.
PDB; 1G9O; X-ray; 1.50 A; A=11-99.
PDB; 1GQ4; X-ray; 1.90 A; A=11-94.
PDB; 1GQ5; X-ray; 2.20 A; A=11-94.
PDB; 1I92; X-ray; 1.70 A; A=11-94.
PDB; 1SGH; X-ray; 3.50 A; B=321-358.
PDB; 2D10; X-ray; 2.50 A; E/F/G/H=331-358.
PDB; 2JXO; NMR; -; A=150-240.
PDB; 2KJD; NMR; -; A=150-270.
PDB; 2KRG; NMR; -; A=150-358.
PDB; 2M0T; NMR; -; A=11-120.
PDB; 2M0U; NMR; -; A=11-120.
PDB; 2M0V; NMR; -; A=150-270.
PDB; 2OZF; X-ray; 1.50 A; A=150-235.
PDB; 4JL7; X-ray; 1.16 A; A=11-95.
PDB; 4LMM; X-ray; 1.10 A; A=11-94.
PDB; 4MPA; X-ray; 1.10 A; A=11-94.
PDB; 4N6X; X-ray; 1.05 A; A=11-94.
PDB; 4PQW; X-ray; 1.47 A; A=11-94.
PDB; 4Q3H; X-ray; 1.44 A; A/B=150-234.
PDBsum; 1G9O; -.
PDBsum; 1GQ4; -.
PDBsum; 1GQ5; -.
PDBsum; 1I92; -.
PDBsum; 1SGH; -.
PDBsum; 2D10; -.
PDBsum; 2JXO; -.
PDBsum; 2KJD; -.
PDBsum; 2KRG; -.
PDBsum; 2M0T; -.
PDBsum; 2M0U; -.
PDBsum; 2M0V; -.
PDBsum; 2OZF; -.
PDBsum; 4JL7; -.
PDBsum; 4LMM; -.
PDBsum; 4MPA; -.
PDBsum; 4N6X; -.
PDBsum; 4PQW; -.
PDBsum; 4Q3H; -.
ProteinModelPortal; O14745; -.
SMR; O14745; -.
BioGrid; 114769; 107.
CORUM; O14745; -.
DIP; DIP-29092N; -.
ELM; O14745; -.
IntAct; O14745; 33.
MINT; MINT-4998796; -.
STRING; 9606.ENSP00000262613; -.
TCDB; 8.A.24.1.1; the ezrin/radixin/moesin-binding phosphoprotein 50 (ebp50) family.
iPTMnet; O14745; -.
PhosphoSitePlus; O14745; -.
BioMuta; SLC9A3R1; -.
EPD; O14745; -.
MaxQB; O14745; -.
PaxDb; O14745; -.
PeptideAtlas; O14745; -.
PRIDE; O14745; -.
Ensembl; ENST00000262613; ENSP00000262613; ENSG00000109062. [O14745-1]
Ensembl; ENST00000413388; ENSP00000464982; ENSG00000109062. [O14745-2]
GeneID; 9368; -.
KEGG; hsa:9368; -.
UCSC; uc002jlo.5; human. [O14745-1]
CTD; 9368; -.
DisGeNET; 9368; -.
EuPathDB; HostDB:ENSG00000109062.9; -.
GeneCards; SLC9A3R1; -.
HGNC; HGNC:11075; SLC9A3R1.
HPA; CAB001962; -.
HPA; HPA009672; -.
HPA; HPA027247; -.
MalaCards; SLC9A3R1; -.
MIM; 604990; gene.
MIM; 612287; phenotype.
neXtProt; NX_O14745; -.
OpenTargets; ENSG00000109062; -.
Orphanet; 244305; Dominant hypophosphatemia with nephrolithiasis or osteoporosis.
PharmGKB; PA35931; -.
eggNOG; ENOG410ITAB; Eukaryota.
eggNOG; ENOG4110SZZ; LUCA.
GeneTree; ENSGT00530000062999; -.
HOGENOM; HOG000089940; -.
HOVERGEN; HBG052616; -.
InParanoid; O14745; -.
KO; K13365; -.
OMA; LCAMKKG; -.
OrthoDB; EOG091G086H; -.
PhylomeDB; O14745; -.
TreeFam; TF350449; -.
SignaLink; O14745; -.
SIGNOR; O14745; -.
ChiTaRS; SLC9A3R1; human.
EvolutionaryTrace; O14745; -.
GeneWiki; Sodium-hydrogen_antiporter_3_regulator_1; -.
GenomeRNAi; 9368; -.
PRO; PR:O14745; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000109062; -.
CleanEx; HS_SLC9A3R1; -.
ExpressionAtlas; O14745; baseline and differential.
Genevisible; O14745; HS.
GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005902; C:microvillus; IDA:UniProtKB.
GO; GO:0031528; C:microvillus membrane; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
GO; GO:0032426; C:stereocilium tip; IEA:Ensembl.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0031698; F:beta-2 adrenergic receptor binding; IPI:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
GO; GO:0017081; F:chloride channel regulator activity; IDA:UniProtKB.
GO; GO:0050780; F:dopamine receptor binding; IEA:Ensembl.
GO; GO:0070851; F:growth factor receptor binding; IPI:UniProtKB.
GO; GO:0045159; F:myosin II binding; IEA:Ensembl.
GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0032947; F:protein complex scaffold activity; IEA:Ensembl.
GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IEA:Ensembl.
GO; GO:0060088; P:auditory receptor cell stereocilium organization; IEA:Ensembl.
GO; GO:0032782; P:bile acid secretion; ISS:UniProtKB.
GO; GO:0030643; P:cellular phosphate ion homeostasis; IEA:Ensembl.
GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:UniProtKB.
GO; GO:0051683; P:establishment of Golgi localization; IMP:UniProtKB.
GO; GO:0022612; P:gland morphogenesis; IMP:UniProtKB.
GO; GO:0034635; P:glutathione transport; ISS:UniProtKB.
GO; GO:0030033; P:microvillus assembly; IMP:UniProtKB.
GO; GO:0035414; P:negative regulation of catenin import into nucleus; IMP:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:0032416; P:negative regulation of sodium:proton antiporter activity; IEA:Ensembl.
GO; GO:0007097; P:nuclear migration; IMP:UniProtKB.
GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IEA:Ensembl.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0008361; P:regulation of cell size; IMP:UniProtKB.
GO; GO:0044062; P:regulation of excretion; IEA:Ensembl.
GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0032415; P:regulation of sodium:proton antiporter activity; NAS:UniProtKB.
GO; GO:0070293; P:renal absorption; ISS:UniProtKB.
GO; GO:0097291; P:renal phosphate ion absorption; IMP:UniProtKB.
GO; GO:0003096; P:renal sodium ion transport; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR015098; EBP50_C-term.
InterPro; IPR031199; NHERF-1.
InterPro; IPR017300; NHERF-1/NHERF-2.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
PANTHER; PTHR14191:SF7; PTHR14191:SF7; 1.
Pfam; PF09007; EBP50_C; 1.
Pfam; PF00595; PDZ; 2.
PIRSF; PIRSF037866; EBP50; 1.
ProDom; PD283022; EBP50_C-term; 1.
SMART; SM00228; PDZ; 2.
SUPFAM; SSF50156; SSF50156; 2.
PROSITE; PS50106; PDZ; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell membrane;
Cell projection; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Membrane; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Wnt signaling pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.8}.
CHAIN 2 358 Na(+)/H(+) exchange regulatory cofactor
NHE-RF1.
/FTId=PRO_0000096799.
DOMAIN 14 94 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 154 234 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.8}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 269 269 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000250|UniProtKB:Q28619}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000250|UniProtKB:P70441}.
MOD_RES 293 293 Phosphothreonine.
{ECO:0000250|UniProtKB:P70441}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 299 299 Phosphoserine.
{ECO:0000250|UniProtKB:P70441}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000250|UniProtKB:P70441}.
VAR_SEQ 1 156 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055497.
VARIANT 68 68 E -> A (in NPHLOP2; impairs the
interaction with SLC34A1; causes a
reduction of SLC34A1 amount on cell
membrane and affects SLC34A1-dependent
phosphate uptake; dbSNP:rs139622189).
{ECO:0000269|PubMed:22506049}.
/FTId=VAR_067661.
VARIANT 110 110 L -> V (in NPHLOP2; the mutant expressed
in cultured renal cells increases the
generation of cyclic AMP (cAMP) by
parathyroid hormone (PTH) and inhibits
phosphate transport; dbSNP:rs35910969).
{ECO:0000269|PubMed:18784102}.
/FTId=VAR_034899.
VARIANT 153 153 R -> Q (in NPHLOP2; the mutant expressed
in cultured renal cells increases the
generation of cAMP by PTH and inhibits
phosphate transport; dbSNP:rs41282065).
{ECO:0000269|PubMed:18784102}.
/FTId=VAR_048021.
VARIANT 225 225 E -> K (in NPHLOP2; the mutant expressed
in cultured renal cells increases the
generation of cAMP by PTH and inhibits
phosphate transport; dbSNP:rs119486097).
{ECO:0000269|PubMed:18784102}.
/FTId=VAR_048022.
MUTAGEN 355 355 F->R: Loss of MSX binding.
{ECO:0000269|PubMed:15020681}.
MUTAGEN 358 358 Missing: Reduces MSX binding.
{ECO:0000269|PubMed:15020681}.
STRAND 13 18 {ECO:0000244|PDB:4N6X}.
STRAND 23 25 {ECO:0000244|PDB:4PQW}.
STRAND 27 30 {ECO:0000244|PDB:4N6X}.
STRAND 32 40 {ECO:0000244|PDB:4N6X}.
HELIX 47 50 {ECO:0000244|PDB:4N6X}.
STRAND 58 62 {ECO:0000244|PDB:4N6X}.
HELIX 72 81 {ECO:0000244|PDB:4N6X}.
STRAND 82 91 {ECO:0000244|PDB:4N6X}.
TURN 93 95 {ECO:0000244|PDB:4N6X}.
TURN 101 103 {ECO:0000244|PDB:2M0T}.
TURN 106 108 {ECO:0000244|PDB:2M0T}.
HELIX 109 112 {ECO:0000244|PDB:2M0T}.
STRAND 115 118 {ECO:0000244|PDB:2M0T}.
STRAND 153 158 {ECO:0000244|PDB:4Q3H}.
TURN 160 162 {ECO:0000244|PDB:2JXO}.
STRAND 166 170 {ECO:0000244|PDB:4Q3H}.
STRAND 172 182 {ECO:0000244|PDB:4Q3H}.
STRAND 184 186 {ECO:0000244|PDB:2M0V}.
HELIX 187 190 {ECO:0000244|PDB:4Q3H}.
STRAND 198 202 {ECO:0000244|PDB:4Q3H}.
HELIX 212 221 {ECO:0000244|PDB:4Q3H}.
TURN 222 224 {ECO:0000244|PDB:4Q3H}.
STRAND 225 231 {ECO:0000244|PDB:4Q3H}.
HELIX 233 238 {ECO:0000244|PDB:2JXO}.
HELIX 248 251 {ECO:0000244|PDB:2KJD}.
STRAND 286 289 {ECO:0000244|PDB:2KRG}.
HELIX 297 299 {ECO:0000244|PDB:2KRG}.
STRAND 300 302 {ECO:0000244|PDB:2KRG}.
STRAND 313 315 {ECO:0000244|PDB:2KRG}.
HELIX 323 328 {ECO:0000244|PDB:2KRG}.
HELIX 329 333 {ECO:0000244|PDB:2KRG}.
HELIX 348 355 {ECO:0000244|PDB:2D10}.
SEQUENCE 358 AA; 38868 MW; E33AF87016D37A65 CRC64;
MSADAAAGAP LPRLCCLEKG PNGYGFHLHG EKGKLGQYIR LVEPGSPAEK AGLLAGDRLV
EVNGENVEKE THQQVVSRIR AALNAVRLLV VDPETDEQLQ KLGVQVREEL LRAQEAPGQA
EPPAAAEVQG AGNENEPREA DKSHPEQREL RPRLCTMKKG PSGYGFNLHS DKSKPGQFIR
SVDPDSPAEA SGLRAQDRIV EVNGVCMEGK QHGDVVSAIR AGGDETKLLV VDRETDEFFK
KCRVIPSQEH LNGPLPVPFT NGEIQKENSR EALAEAALES PRPALVRSAS SDTSEELNSQ
DSPPKQDSTA PSSTSSSDPI LDFNISLAMA KERAHQKRSS KRAPQMDWSK KNELFSNL


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