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Na( )/H( ) exchange regulatory cofactor NHE-RF4 (NHERF-4) (Intestinal and kidney-enriched PDZ protein) (Natrium-phosphate cotransporter IIa C-terminal-associated protein 2) (Na/Pi cotransporter C-terminal-associated protein 2) (NaPi-Cap2) (PDZ domain-containing protein 2) (PDZ domain-containing protein 3) (Sodium-hydrogen exchanger regulatory factor 4)

 NHRF4_HUMAN             Reviewed;         571 AA.
Q86UT5; Q8N6R4; Q8NAW7; Q8NEX7; Q9H5Z3;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 2.
25-OCT-2017, entry version 126.
RecName: Full=Na(+)/H(+) exchange regulatory cofactor NHE-RF4;
Short=NHERF-4;
AltName: Full=Intestinal and kidney-enriched PDZ protein;
AltName: Full=Natrium-phosphate cotransporter IIa C-terminal-associated protein 2;
Short=Na/Pi cotransporter C-terminal-associated protein 2;
Short=NaPi-Cap2;
AltName: Full=PDZ domain-containing protein 2;
AltName: Full=PDZ domain-containing protein 3;
AltName: Full=Sodium-hydrogen exchanger regulatory factor 4;
Name=PDZD3; Synonyms=IKEPP, NHERF4, PDZK2; ORFNames=DLNB27;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAL10686.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
GUCY2C, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Intestinal epithelium {ECO:0000269|PubMed:11950846};
PubMed=11950846; DOI=10.1074/jbc.M202434200;
Scott R.O., Thelin W.R., Milgram S.L.;
"A novel PDZ protein regulates the activity of guanylyl cyclase C, the
heat-stable enterotoxin receptor.";
J. Biol. Chem. 277:22934-22941(2002).
[2] {ECO:0000305, ECO:0000312|EMBL:BAC76050.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Kubo T., Arai Y., Ohira M., Gamou T., Maeno G., Sakiyama T.,
Toyoda A., Hattori M., Sakaki Y., Nakagawara A., Ohki M.;
"Identification of a 500-kb region of common allelic loss in
chromosome 11q23 in non-MYCN amplified type of neuroblastoma.";
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000305, ECO:0000312|EMBL:BAC03780.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
TISSUE=Ileal mucosa {ECO:0000312|EMBL:BAB15474.1}, and
Kidney {ECO:0000312|EMBL:BAC03780.1};
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=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5] {ECO:0000305, ECO:0000312|EMBL:AAH29042.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SLC9A3.
PubMed=19088451; DOI=10.1159/000185553;
Zachos N.C., Hodson C., Kovbasnjuk O., Li X., Thelin W.R., Cha B.,
Milgram S., Donowitz M.;
"Elevated intracellular calcium stimulates NHE3 activity by an IKEPP
(NHERF4) dependent mechanism.";
Cell. Physiol. Biochem. 22:693-704(2008).
[7] {ECO:0000305, ECO:0000312|EMBL:BAC76050.1}
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 326-415.
Structural genomics consortium (SGC);
"Crystal structure of the 3rd PDZ domain of intestine- and kidney-
enriched PDZ domain IKEPP (PDZD3).";
Submitted (JUL-2011) to the PDB data bank.
[8]
INTERACTION WITH USP2.
PubMed=26756164; DOI=10.1371/journal.pone.0145155;
Pouly D., Chenaux S., Martin V., Babis M., Koch R., Nagoshi E.,
Katanaev V.L., Gachon F., Staub O.;
"USP2-45 is a circadian clock output effector regulating calcium
absorption at the post-translational level.";
PLoS ONE 11:E0145155-E0145155(2016).
-!- FUNCTION: Acts as a regulatory protein that associates with GUCY2C
and negatively modulates its heat-stable enterotoxin-mediated
activation (PubMed:11950846). Stimulates SLC9A3 activity in the
presence of elevated calcium ions (PubMed:19088451).
{ECO:0000269|PubMed:11950846, ECO:0000269|PubMed:19088451}.
-!- SUBUNIT: Interacts with the C-terminal region of GUCY2C
(PubMed:11950846). Interacts with the C-terminal region SLC9A3 and
the interactions decrease in response to elevated calcium ion
levels (PubMed:19088451). Interacts with the C-terminal region of
SLC34A1 (By similarity). Interacts with USP2 isoform 4
(PubMed:26756164). {ECO:0000250|UniProtKB:Q99MJ6,
ECO:0000269|PubMed:11950846, ECO:0000269|PubMed:19088451,
ECO:0000269|PubMed:26756164}.
-!- INTERACTION:
Q8TDY4:ASAP3; NbExp=3; IntAct=EBI-8744528, EBI-2609717;
Q13698:CACNA1S; NbExp=3; IntAct=EBI-8744528, EBI-5329490;
P25092:GUCY2C; NbExp=4; IntAct=EBI-8299496, EBI-2816795;
Q96GZ6:SLC41A3; NbExp=3; IntAct=EBI-8744528, EBI-7225508;
Q5W111:SPRYD7; NbExp=3; IntAct=EBI-8744528, EBI-10248098;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11950846,
ECO:0000269|PubMed:19088451}; Peripheral membrane protein
{ECO:0000269|PubMed:11950846, ECO:0000269|PubMed:19088451}.
Cytoplasm {ECO:0000269|PubMed:19088451}. Note=Preferentially
accumulates at the apical surface and ileal brush border of
intestinal epithelial cells (PubMed:11950846, PubMed:19088451).
{ECO:0000269|PubMed:11950846, ECO:0000269|PubMed:19088451}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1 {ECO:0000269|Ref.2};
IsoId=Q86UT5-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:11950846};
IsoId=Q86UT5-2; Sequence=VSP_051786, VSP_051787;
Name=3 {ECO:0000305};
IsoId=Q86UT5-3; Sequence=VSP_051786, VSP_051787, VSP_051788;
Note=No experimental confirmation available. {ECO:0000305};
Name=4 {ECO:0000305};
IsoId=Q86UT5-4; Sequence=VSP_051790, VSP_051791;
Note=No experimental confirmation available. {ECO:0000305};
Name=5 {ECO:0000305};
IsoId=Q86UT5-5; Sequence=VSP_051786, VSP_051787, VSP_051789;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in kidney and the gastrointestinal
tract. Not detected in brain, heart, skeletal muscle or cells of
hematopoietic origin. {ECO:0000269|PubMed:11950846}.
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EMBL; AY047359; AAL10686.1; -; mRNA.
EMBL; AB094096; BAC76050.1; -; mRNA.
EMBL; AK026409; BAB15474.1; -; mRNA.
EMBL; AK091966; BAC03780.1; -; mRNA.
EMBL; AP002956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC029042; AAH29042.1; -; mRNA.
CCDS; CCDS53719.1; -. [Q86UT5-2]
CCDS; CCDS8417.1; -. [Q86UT5-3]
RefSeq; NP_001161940.1; NM_001168468.1. [Q86UT5-2]
RefSeq; NP_079067.3; NM_024791.3. [Q86UT5-3]
RefSeq; XP_011541302.1; XM_011543000.2. [Q86UT5-1]
RefSeq; XP_011541303.1; XM_011543001.2. [Q86UT5-1]
RefSeq; XP_011541304.1; XM_011543002.2. [Q86UT5-1]
UniGene; Hs.374726; -.
PDB; 2V90; X-ray; 2.00 A; A/B/C/D/E/F=326-415.
PDBsum; 2V90; -.
ProteinModelPortal; Q86UT5; -.
SMR; Q86UT5; -.
BioGrid; 122940; 8.
IntAct; Q86UT5; 6.
STRING; 9606.ENSP00000347742; -.
iPTMnet; Q86UT5; -.
PhosphoSitePlus; Q86UT5; -.
BioMuta; PDZD3; -.
DMDM; 308153467; -.
MaxQB; Q86UT5; -.
PaxDb; Q86UT5; -.
PeptideAtlas; Q86UT5; -.
PRIDE; Q86UT5; -.
TopDownProteomics; Q86UT5-4; -. [Q86UT5-4]
Ensembl; ENST00000322712; ENSP00000327107; ENSG00000172367. [Q86UT5-3]
Ensembl; ENST00000355547; ENSP00000347742; ENSG00000172367. [Q86UT5-2]
Ensembl; ENST00000531114; ENSP00000431164; ENSG00000172367. [Q86UT5-1]
GeneID; 79849; -.
KEGG; hsa:79849; -.
UCSC; uc001pvy.4; human. [Q86UT5-1]
CTD; 79849; -.
DisGeNET; 79849; -.
EuPathDB; HostDB:ENSG00000172367.15; -.
GeneCards; PDZD3; -.
H-InvDB; HIX0201614; -.
HGNC; HGNC:19891; PDZD3.
MIM; 607146; gene.
neXtProt; NX_Q86UT5; -.
OpenTargets; ENSG00000172367; -.
PharmGKB; PA134911718; -.
eggNOG; ENOG410ITA7; Eukaryota.
eggNOG; ENOG410XURS; LUCA.
GeneTree; ENSGT00530000062999; -.
HOGENOM; HOG000048712; -.
HOVERGEN; HBG080760; -.
InParanoid; Q86UT5; -.
OMA; GVRPRLC; -.
OrthoDB; EOG091G0KAL; -.
PhylomeDB; Q86UT5; -.
TreeFam; TF350449; -.
Reactome; R-HSA-8942233; Intestinal infectious diseases.
EvolutionaryTrace; Q86UT5; -.
GenomeRNAi; 79849; -.
PRO; PR:Q86UT5; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000172367; -.
CleanEx; HS_PDZD3; -.
ExpressionAtlas; Q86UT5; baseline and differential.
Genevisible; Q86UT5; HS.
GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
GO; GO:0005903; C:brush border; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:UniProtKB.
GO; GO:0035003; C:subapical complex; IDA:UniProtKB.
GO; GO:0030251; F:guanylate cyclase inhibitor activity; IDA:UniProtKB.
GO; GO:0008200; F:ion channel inhibitor activity; TAS:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:UniProtKB.
GO; GO:0019934; P:cGMP-mediated signaling; NAS:UniProtKB.
GO; GO:0006811; P:ion transport; NAS:UniProtKB.
GO; GO:0030827; P:negative regulation of cGMP biosynthetic process; TAS:UniProtKB.
GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IC:UniProtKB.
GO; GO:0009636; P:response to toxic substance; TAS:UniProtKB.
GO; GO:0006833; P:water transport; NAS:UniProtKB.
InterPro; IPR031200; NHERF-4.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
PANTHER; PTHR14191:SF20; PTHR14191:SF20; 1.
Pfam; PF00595; PDZ; 4.
SMART; SM00228; PDZ; 4.
SUPFAM; SSF50156; SSF50156; 4.
PROSITE; PS50106; PDZ; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Cytoplasm; Membrane; Reference proteome; Repeat.
CHAIN 1 571 Na(+)/H(+) exchange regulatory cofactor
NHE-RF4.
/FTId=PRO_0000058292.
DOMAIN 115 196 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 223 301 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 329 412 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 467 548 PDZ 4. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
VAR_SEQ 1 66 Missing (in isoform 2, isoform 3 and
isoform 5). {ECO:0000303|PubMed:11950846,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_051786.
VAR_SEQ 67 105 TRQKLPSTLSGHRVCQAHGEPVLGLCPLLPLFCCPPHPP
-> MEKAADLQDTASLTLKFKFNPKLGIDNPVLSLAEDHDP
Y (in isoform 2, isoform 3 and isoform
5). {ECO:0000303|PubMed:11950846,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_051787.
VAR_SEQ 272 285 Missing (in isoform 3).
{ECO:0000303|PubMed:11950846,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_051788.
VAR_SEQ 287 571 Missing (in isoform 5).
{ECO:0000303|PubMed:11950846,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_051789.
VAR_SEQ 355 386 QFLWEVDPGLPAKKAGMQAGDRLVAVAGESVE -> EWEPW
GRWGKVGLGVGTQAYIHLSVHRRGVPV (in isoform
4). {ECO:0000303|PubMed:11950846,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_051790.
VAR_SEQ 387 571 Missing (in isoform 4).
{ECO:0000303|PubMed:11950846,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_051791.
CONFLICT 112 112 R -> P (in Ref. 3; BAB15474).
{ECO:0000305}.
CONFLICT 125 125 S -> G (in Ref. 3; BAC03780).
{ECO:0000305}.
CONFLICT 286 286 L -> V (in Ref. 3; BAB15474).
{ECO:0000305}.
CONFLICT 438 438 R -> Q (in Ref. 2; BAC76050 and 5;
AAH29042). {ECO:0000305}.
STRAND 328 333 {ECO:0000244|PDB:2V90}.
STRAND 341 347 {ECO:0000244|PDB:2V90}.
STRAND 353 360 {ECO:0000244|PDB:2V90}.
HELIX 365 368 {ECO:0000244|PDB:2V90}.
STRAND 375 380 {ECO:0000244|PDB:2V90}.
HELIX 390 398 {ECO:0000244|PDB:2V90}.
TURN 399 402 {ECO:0000244|PDB:2V90}.
STRAND 403 409 {ECO:0000244|PDB:2V90}.
SEQUENCE 571 AA; 61032 MW; B56CDC91348EE592 CRC64;
MVTPSPPGNH SLSLEAPRLH TASDLLGNHS LGLPLITALV GSRDRRGRVF SPVPVPLPTN
PTTQHPTRQK LPSTLSGHRV CQAHGEPVLG LCPLLPLFCC PPHPPDPWSL ERPRFCLLSK
EEGKSFGFHL QQELGRAGHV VCRVDPGTSA QRQGLQEGDR ILAVNNDVVE HEDYAVVVRR
IRASSPRVLL TVLARHAHDV ARAQLGEDAH LCPTLGPGVR PRLCHIVKDE GGFGFSVTHG
NQGPFWLVLS TGGAAERAGV PPGARLLEVN GVSVEKFTHN QLTRKLWQSG QQVTLLVAGP
EVEEQCRQLG LPLAAPLAEG WALPTKPRCL HLEKGPQGFG FLLREEKGLD GRPGQFLWEV
DPGLPAKKAG MQAGDRLVAV AGESVEGLGH EETVSRIQGQ GSCVSLTVVD PEADRFFSMV
RLSPLLFLEN TEAPASPRGS SSASLVETED PSLEDTSVPS VPLGSRQCFL YPGPGGSYGF
RLSCVASGPR LFISQVTPGG SAARAGLQVG DVILEVNGYP VGGQNDLERL QQLPEAEPPL
CLKLAARSLR GLEAWIPPGA AEDWALASDL L


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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
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
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


 

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