NHRF1_MOUSE
ID NHRF1_MOUSE Reviewed; 355 AA.
AC P70441; Q8BYD8;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Na(+)/H(+) exchange regulatory cofactor NHE-RF1;
DE Short=NHERF-1;
DE AltName: Full=Ezrin-radixin-moesin-binding phosphoprotein 50;
DE Short=EBP50;
DE AltName: Full=Regulatory cofactor of Na(+)/H(+) exchanger;
DE AltName: Full=Sodium-hydrogen exchanger regulatory factor 1;
DE AltName: Full=Solute carrier family 9 isoform A3 regulatory factor 1;
GN Name=Slc9a3r1; Synonyms=Nherf, Nherf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=10500246; DOI=10.1016/s0167-4781(99)00100-1;
RA Weinman E.J., Steplock D., Zhang X., Akhter S., Shenolikar S.;
RT "Molecular cloning of the cDNA and promoter sequences for the mouse sodium-
RT hydrogen exchanger regulatory factor.";
RL Biochim. Biophys. Acta 1447:71-76(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND INTERACTION WITH ADRB2.
RX PubMed=9560162; DOI=10.1038/33458;
RA Hall R.A., Premont R.T., Chow C.-W., Blitzer J.T., Pitcher J.A., Claing A.,
RA Stoffel R.H., Barak L.S., Shenolikar S., Weinman E.J., Grinstein S.,
RA Lefkowitz R.J.;
RT "The beta2-adrenergic receptor interacts with the Na+/H+-exchanger
RT regulatory factor to control Na+/H+ exchange.";
RL Nature 392:626-630(1998).
RN [5]
RP INTERACTION WITH PAG1, AND IDENTIFICATION IN A COMPLEX WITH PAG1 AND MSN.
RX PubMed=11777944; DOI=10.4049/jimmunol.168.2.541;
RA Itoh K., Sakakibara M., Yamasaki S., Takeuchi A., Arase H., Miyazaki M.,
RA Nakajima N., Okada M., Saito T.;
RT "Negative regulation of immune synapse formation by anchoring lipid raft to
RT cytoskeleton through Cbp-EBP50-ERM assembly.";
RL J. Immunol. 168:541-544(2002).
RN [6]
RP INTERACTION WITH PDZK1.
RX PubMed=14531806; DOI=10.1046/j.1523-1755.2003.00266.x;
RA Gisler S.M., Pribanic S., Bacic D., Forrer P., Gantenbein A.,
RA Sabourin L.A., Tsuji A., Zhao Z.-S., Manser E., Biber J., Murer H.;
RT "PDZK1: I. a major scaffolder in brush borders of proximal tubular cells.";
RL Kidney Int. 64:1733-1745(2003).
RN [7]
RP INTERACTION WITH HTR4.
RX PubMed=15466885; DOI=10.1242/jcs.01379;
RA Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA Marin P., Dumuis A., Bockaert J.;
RT "New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a
RT receptor splice variant: roles in receptor targeting.";
RL J. Cell Sci. 117:5367-5379(2004).
RN [8]
RP PHOSPHORYLATION AT SER-286.
RX PubMed=15378723; DOI=10.1002/rcm.1604;
RA Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
RT "Phosphoproteome analysis of mouse liver using immobilized metal affinity
RT purification and linear ion trap mass spectrometry.";
RL Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17311105; DOI=10.1371/journal.pone.0000237;
RA Nielsen J.S., Graves M.L., Chelliah S., Vogl A.W., Roskelley C.D.,
RA McNagny K.M.;
RT "The CD34-related molecule podocalyxin is a potent inducer of microvillus
RT formation.";
RL PLoS ONE 2:E237-E237(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-297, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286; THR-288; SER-289;
RP SER-294 AND SER-297, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP FUNCTION, INTERACTION WITH CFTR; SLC26A3 AND SLC26A6, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=21976599; DOI=10.1095/biolreprod.111.094037;
RA Chavez J.C., Hernandez-Gonzalez E.O., Wertheimer E., Visconti P.E.,
RA Darszon A., Trevino C.L.;
RT "Participation of the Cl-/HCO(3)- exchangers SLC26A3 and SLC26A6, the
RT Cl- channel CFTR, and the regulatory factor SLC9A3R1 in mouse sperm
RT capacitation.";
RL Biol. Reprod. 86:1-14(2012).
CC -!- FUNCTION: Scaffold protein that connects plasma membrane proteins with
CC members of the ezrin/moesin/radixin family and thereby helps to link
CC them to the actin cytoskeleton and to regulate their surface
CC expression. Necessary for recycling of internalized ADRB2. Was first
CC known to play a role in the regulation of the activity and subcellular
CC location of SLC9A3. Necessary for cAMP-mediated phosphorylation and
CC inhibition of SLC9A3. May enhance Wnt signaling (By similarity). May
CC participate in HTR4 targeting to microvilli. Involved in the regulation
CC of phosphate reabsorption in the renal proximal tubules (By
CC similarity). Involved in sperm capacitation. May participate in the
CC regulation of the chloride and bicarbonate homeostasis in spermatozoa.
CC {ECO:0000250, ECO:0000269|PubMed:21976599, ECO:0000269|PubMed:9560162}.
CC -!- SUBUNIT: Homodimer, and heterodimer with SLC9A3R2. Binds the N-termini
CC of EZR, RDX and MSN. Binds the C-termini of PDGFRA, PDGFRB, ADRB2 and
CC NOS2. Binds ARHGAP17, EPI64, RACK1, OPRK1, GNAQ, CTNNB1, PLCB3 and
CC CLCN3. Forms a complex with CFTR and SLC4A7. Forms a complex with
CC SLC4A7 and ATP6V1B1 (By similarity). Binds PDZK1. Binds the C-terminus
CC of PAG1. In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which
CC is disrupted upon TCR activation. Directly interacts with HTR4.
CC Interacts with MCC (By similarity). Interacts with TRPC4 (via the PDZ-
CC binding domain) (By similarity). Interacts (via the PDZ 1 domain) with
CC PODXL (via the C-terminal PDZ-binding motif DTHL); interaction is not
CC detected in glomerular epithelium cells (By similarity). Interacts (via
CC the PDZ 1 domain) with PODXL (via the C-terminal PDZ-binding motif
CC DTHL); the interaction take place early in the secretory pathway and is
CC necessary for its apical membrane sorting (By similarity). Interacts
CC with SLC34A1 (By similarity). Interacts with CFTR, SLC26A3 and SLC26A6.
CC Interacts (via PDZ domains) with ACE2 (via PDZ-binding motif); the
CC interaction may enhance ACE2 membrane residence (By similarity).
CC {ECO:0000250|UniProtKB:O14745, ECO:0000269|PubMed:11777944,
CC ECO:0000269|PubMed:14531806, ECO:0000269|PubMed:15466885,
CC ECO:0000269|PubMed:21976599, ECO:0000269|PubMed:9560162}.
CC -!- INTERACTION:
CC P70441; P26361: Cftr; NbExp=3; IntAct=EBI-1184085, EBI-6115317;
CC P70441; Q9WVC8: Slc26a3; NbExp=2; IntAct=EBI-1184085, EBI-6895537;
CC P70441; Q8CIW6: Slc26a6; NbExp=2; IntAct=EBI-1184085, EBI-6895517;
CC P70441; Q80ZA5-3: Slc4a10; Xeno; NbExp=3; IntAct=EBI-1184085, EBI-8613086;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Apical cell membrane. Cell projection,
CC filopodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cell
CC projection, microvillus {ECO:0000250}. Endomembrane system
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=Colocalizes with actin in microvilli-rich apical regions of the
CC syncytiotrophoblast. Present in lipid rafts of T-cells (By similarity).
CC Translocates from the cytoplasm to the apical cell membrane in a PODXL-
CC dependent manner. Colocalizes with CFTR at the midpiece of sperm tail.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P70441-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P70441-2; Sequence=VSP_027877, VSP_027878;
CC -!- TISSUE SPECIFICITY: Expressed in spermatogenic cells.
CC {ECO:0000269|PubMed:21976599}.
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DR EMBL; U74079; AAB17569.1; -; mRNA.
DR EMBL; AK040371; BAC30573.2; -; mRNA.
DR EMBL; BC085141; AAH85141.1; -; mRNA.
DR CCDS; CCDS36370.1; -. [P70441-1]
DR RefSeq; NP_036160.1; NM_012030.2. [P70441-1]
DR AlphaFoldDB; P70441; -.
DR SMR; P70441; -.
DR BioGRID; 205077; 28.
DR CORUM; P70441; -.
DR IntAct; P70441; 10.
DR MINT; P70441; -.
DR STRING; 10090.ENSMUSP00000021077; -.
DR iPTMnet; P70441; -.
DR PhosphoSitePlus; P70441; -.
DR SwissPalm; P70441; -.
DR EPD; P70441; -.
DR jPOST; P70441; -.
DR MaxQB; P70441; -.
DR PaxDb; P70441; -.
DR PeptideAtlas; P70441; -.
DR PRIDE; P70441; -.
DR ProteomicsDB; 287423; -. [P70441-1]
DR ProteomicsDB; 287424; -. [P70441-2]
DR Antibodypedia; 1525; 347 antibodies from 37 providers.
DR DNASU; 26941; -.
DR Ensembl; ENSMUST00000021077; ENSMUSP00000021077; ENSMUSG00000020733. [P70441-1]
DR GeneID; 26941; -.
DR KEGG; mmu:26941; -.
DR UCSC; uc007mgp.1; mouse. [P70441-1]
DR CTD; 9368; -.
DR MGI; MGI:1349482; Slc9a3r1.
DR VEuPathDB; HostDB:ENSMUSG00000020733; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00950000182849; -.
DR HOGENOM; CLU_038627_1_0_1; -.
DR InParanoid; P70441; -.
DR OMA; NGQIHGH; -.
DR PhylomeDB; P70441; -.
DR TreeFam; TF350449; -.
DR BioGRID-ORCS; 26941; 1 hit in 75 CRISPR screens.
DR PRO; PR:P70441; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P70441; protein.
DR Bgee; ENSMUSG00000020733; Expressed in small intestine Peyer's patch and 288 other tissues.
DR ExpressionAtlas; P70441; baseline and differential.
DR Genevisible; P70441; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0031526; C:brush border membrane; IDA:MGI.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098797; C:plasma membrane protein complex; ISO:MGI.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0097225; C:sperm midpiece; IDA:UniProtKB.
DR GO; GO:0032420; C:stereocilium; IDA:MGI.
DR GO; GO:0032426; C:stereocilium tip; IDA:MGI.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0017081; F:chloride channel regulator activity; ISS:UniProtKB.
DR GO; GO:0050780; F:dopamine receptor binding; IDA:MGI.
DR GO; GO:0015185; F:gamma-aminobutyric acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0070851; F:growth factor receptor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR GO; GO:0045159; F:myosin II binding; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0031799; F:type 2 metabotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0031800; F:type 3 metabotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IMP:MGI.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:0032782; P:bile acid secretion; IMP:UniProtKB.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; IMP:MGI.
DR GO; GO:0090660; P:cerebrospinal fluid circulation; IDA:ARUK-UCL.
DR GO; GO:0044782; P:cilium organization; IMP:ARUK-UCL.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISO:MGI.
DR GO; GO:0051683; P:establishment of Golgi localization; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0010761; P:fibroblast migration; IGI:MGI.
DR GO; GO:0051939; P:gamma-aminobutyric acid import; ISO:MGI.
DR GO; GO:0022612; P:gland morphogenesis; ISO:MGI.
DR GO; GO:0034635; P:glutathione transport; IMP:UniProtKB.
DR GO; GO:0098739; P:import across plasma membrane; ISO:MGI.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IMP:ARUK-UCL.
DR GO; GO:0030033; P:microvillus assembly; ISO:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:2000146; P:negative regulation of cell motility; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0010764; P:negative regulation of fibroblast migration; IGI:MGI.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
DR GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0010766; P:negative regulation of sodium ion transport; IMP:MGI.
DR GO; GO:0032416; P:negative regulation of sodium:proton antiporter activity; IMP:MGI.
DR GO; GO:0007097; P:nuclear migration; ISO:MGI.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IMP:MGI.
DR GO; GO:0007009; P:plasma membrane organization; IMP:ARUK-UCL.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0034767; P:positive regulation of ion transmembrane transport; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0008361; P:regulation of cell size; ISO:MGI.
DR GO; GO:0045859; P:regulation of protein kinase activity; IMP:UniProtKB.
DR GO; GO:1903402; P:regulation of renal phosphate excretion; IMP:MGI.
DR GO; GO:0070293; P:renal absorption; IMP:UniProtKB.
DR GO; GO:0097291; P:renal phosphate ion absorption; ISS:UniProtKB.
DR GO; GO:0003096; P:renal sodium ion transport; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0006814; P:sodium ion transport; IMP:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR015098; EBP50_C-term.
DR InterPro; IPR031199; NHERF-1.
DR InterPro; IPR017300; NHERF-1/NHERF-2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR14191:SF7; PTHR14191:SF7; 1.
DR Pfam; PF09007; EBP50_C; 1.
DR Pfam; PF00595; PDZ; 2.
DR PIRSF; PIRSF037866; EBP50; 1.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS50106; PDZ; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O14745"
FT CHAIN 2..355
FT /note="Na(+)/H(+) exchange regulatory cofactor NHE-RF1"
FT /id="PRO_0000096800"
FT DOMAIN 14..94
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 149..229
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 110..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O14745"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14745"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14745"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14745"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14745"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28619"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15378723,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 288
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..317
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027877"
FT VAR_SEQ 318
FT /note="L -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027878"
SQ SEQUENCE 355 AA; 38600 MW; 331F6BEE31DA0A11 CRC64;
MSADAAAGEP LPRLCCLEKG PNGYGFHLHG EKGKVGQFIR LVEPGSPAEK SGLLAGDRLV
EVNGENVEKE THQQVVSRIR AALNAVRLLV VDPETDERLK KLGVSIREEL LRPQEKSEQA
EPPAAADTHE AGDQNEAEKS HLRELRPRLC TMKKGPNGYG FNLHSDKSKP GQFIRAVDPD
SPAEASGLRA QDRIVEVNGV CMEGKQHGDV VSAIKGGGDE AKLLVVDKET DEFFKKCKVI
PSQEHLDGPL PEPFSNGEIQ KESSREALVE PASESPRPAL ARSASSDTSE ELNSQDSPKR
QVSTEPSSTS SSSSDPILDL NISLAVAKER AHQKRSSKRA PQMDWSKKNE LFSNL
