NHRF3_HUMAN
ID NHRF3_HUMAN Reviewed; 519 AA.
AC Q5T2W1; B4DPB9; E7EU02; O60450; Q5T5P6; Q9BQ41;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Na(+)/H(+) exchange regulatory cofactor NHE-RF3;
DE Short=NHERF-3;
DE AltName: Full=CFTR-associated protein of 70 kDa;
DE AltName: Full=Na(+)/H(+) exchanger regulatory factor 3;
DE AltName: Full=Na/Pi cotransporter C-terminal-associated protein 1;
DE Short=NaPi-Cap1;
DE AltName: Full=PDZ domain-containing protein 1;
DE AltName: Full=Sodium-hydrogen exchanger regulatory factor 3;
GN Name=PDZK1; Synonyms=CAP70, NHERF3, PDZD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INTERACTION
RP WITH PDZK1IP1.
RX PubMed=9461128;
RA Kocher O., Comella N., Tognazzi K., Brown L.F.;
RT "Identification and partial characterization of PDZK1: a novel protein
RT containing PDZ interaction domains.";
RL Lab. Invest. 78:117-125(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [5]
RP TISSUE SPECIFICITY, AND INTERACTION WITH ABCC2.
RX PubMed=10496535;
RA Kocher O., Comella N., Gilchrist A., Pal R., Tognazzi K., Brown L.F.,
RA Knoll J.H.;
RT "PDZK1, a novel PDZ domain-containing protein up-regulated in carcinomas
RT and mapped to chromosome 1q21, interacts with cMOAT (MRP2), the multidrug
RT resistance-associated protein.";
RL Lab. Invest. 79:1161-1170(1999).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=11051556; DOI=10.1016/s0092-8674(00)00096-9;
RA Wang S., Yue H., Derin R.B., Guggino W.B., Li M.;
RT "Accessory protein facilitated CFTR-CFTR interaction, a molecular mechanism
RT to potentiate the chloride channel activity.";
RL Cell 103:169-179(2000).
RN [7]
RP INTERACTION WITH BCR.
RX PubMed=15494376; DOI=10.1242/jcs.01472;
RA Malmberg E.K., Andersson C.X., Gentzsch M., Chen J.H., Mengos A., Cui L.,
RA Hansson G.C., Riordan J.R.;
RT "Bcr (breakpoint cluster region) protein binds to PDZ-domains of scaffold
RT protein PDZK1 and vesicle coat protein Mint3.";
RL J. Cell Sci. 117:5535-5541(2004).
RN [8]
RP INTERACTION WITH SLC26A3.
RX PubMed=15766278; DOI=10.1021/bi048828b;
RA Rossmann H., Jacob P., Baisch S., Hassoun R., Meier J., Natour D.,
RA Yahya K., Yun C., Biber J., Lackner K.J., Fiehn W., Gregor M., Seidler U.,
RA Lamprecht G.;
RT "The CFTR associated protein CAP70 interacts with the apical Cl-/HCO3-
RT exchanger DRA in rabbit small intestinal mucosa.";
RL Biochemistry 44:4477-4487(2005).
RN [9]
RP INTERACTION WITH SLC9A3.
RX PubMed=16141316; DOI=10.1073/pnas.0506578102;
RA Thomson R.B., Wang T., Thomson B.R., Tarrats L., Girardi A., Mentone S.,
RA Soleimani M., Kocher O., Aronson P.S.;
RT "Role of PDZK1 in membrane expression of renal brush border ion
RT exchangers.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13331-13336(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP STRUCTURE BY NMR OF 132-224 AND 376-458.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of PDZ domains of PDZ domain containing protein 1.";
RL Submitted (FEB-2008) to the PDB data bank.
CC -!- FUNCTION: A scaffold protein that connects plasma membrane proteins and
CC regulatory components, regulating their surface expression in
CC epithelial cells apical domains. May be involved in the coordination of
CC a diverse range of regulatory processes for ion transport and second
CC messenger cascades. In complex with SLC9A3R1, may cluster proteins that
CC are functionally dependent in a mutual fashion and modulate the
CC trafficking and the activity of the associated membrane proteins. May
CC play a role in the cellular mechanisms associated with multidrug
CC resistance through its interaction with ABCC2 and PDZK1IP1. May
CC potentiate the CFTR chloride channel activity. Required for normal
CC cell-surface expression of SCARB1. Plays a role in maintaining normal
CC plasma cholesterol levels via its effects on SCARB1. Plays a role in
CC the normal localization and function of the chloride-anion exchanger
CC SLC26A6 to the plasma membrane in the brush border of the proximal
CC tubule of the kidney. May be involved in the regulation of proximal
CC tubular Na(+)-dependent inorganic phosphate cotransport therefore
CC playing an important role in tubule function (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PDZK1IP1 and ABCC2. Interacts (via PDZ domains
CC 1 and 3) with SCARB1 (C-terminal domain). Forms a heterodimeric complex
CC with SLC9A3R1. Interacts with AKAP2, BCR, CFTR, SLC22A12, SLC22A4,
CC SLC22A5, SLC9A3R2 and SLC17A1. Component of a complex, composed of
CC PDZK1, SYNGAP1, KLHL17 and NMDA receptors. Interacts (via PDZ1 domain)
CC directly with KLHL17; the interaction is important for integrity of
CC actin cytoskeleton structures in neurons. Interacts (via the first PDZ
CC domain) with PTGIR (via non-isoprenylated C-terminus) (By similarity).
CC Interacts (via C-terminal PDZ domain) with SLC26A6 (via C-terminal
CC domain) (By similarity). Interacts (via C-terminal PDZ domain) with
CC SLC9A3 (via C-terminal domain). {ECO:0000250,
CC ECO:0000269|PubMed:10496535, ECO:0000269|PubMed:15494376,
CC ECO:0000269|PubMed:15766278, ECO:0000269|PubMed:16141316,
CC ECO:0000269|PubMed:9461128}.
CC -!- INTERACTION:
CC Q5T2W1; Q9BYF1: ACE2; NbExp=3; IntAct=EBI-349819, EBI-7730807;
CC Q5T2W1; P13569: CFTR; NbExp=3; IntAct=EBI-349819, EBI-349854;
CC Q5T2W1; P51790-2: CLCN3; NbExp=2; IntAct=EBI-349819, EBI-25495635;
CC Q5T2W1; P14136: GFAP; NbExp=4; IntAct=EBI-349819, EBI-744302;
CC Q5T2W1; P19404: NDUFV2; NbExp=3; IntAct=EBI-349819, EBI-713665;
CC Q5T2W1; P29474: NOS3; NbExp=3; IntAct=EBI-349819, EBI-1391623;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9JJ40};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JJ40}. Cell
CC membrane {ECO:0000250|UniProtKB:Q9JIL4}. Note=Associated with
CC peripheral membranes. Localizes to the apical compartment of proximal
CC tubular cells and to sinusoidal liver membranes.
CC {ECO:0000250|UniProtKB:Q9JJ40}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5T2W1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T2W1-2; Sequence=VSP_044637;
CC -!- TISSUE SPECIFICITY: Expression is limited to epithelial cells.
CC Expressed in the kidney (brush border of proximal tubule), pancreas,
CC liver, and small intestine. Expressed at a lower level in the adrenal
CC cortex, testis and stomach. Overexpressed in breast, renal and lung
CC carcinomas. {ECO:0000269|PubMed:10496535, ECO:0000269|PubMed:11051556,
CC ECO:0000269|PubMed:9461128}.
CC -!- DOMAIN: The PDZ 2 and 3 domains seem to be involved in the interaction
CC with SLC26A3. {ECO:0000250}.
CC -!- DOMAIN: Interaction with the C-terminus of CFTR could be mediated
CC through independent binding of PDZ 1, 3 and 4 domains. {ECO:0000250}.
CC -!- DOMAIN: The PDZ 1 and 3 domains seem to be involved in the interaction
CC with SLCO1A1. {ECO:0000250}.
CC -!- DOMAIN: The PDZ 1 domain interacts with BCR.
CC -!- DOMAIN: The PDZ 2 and 4 domains do not interact with the C-terminal
CC region of SCARB1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NHER family. {ECO:0000305}.
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DR EMBL; AF012281; AAC12264.1; -; mRNA.
DR EMBL; AK298269; BAG60531.1; -; mRNA.
DR EMBL; AL390725; CAI13715.1; -; Genomic_DNA.
DR EMBL; AL390725; CAI13716.1; -; Genomic_DNA.
DR EMBL; BC006496; AAH06496.1; -; mRNA.
DR EMBL; BC006518; AAH06518.1; -; mRNA.
DR CCDS; CCDS72859.1; -. [Q5T2W1-2]
DR CCDS; CCDS72860.1; -. [Q5T2W1-1]
DR RefSeq; NP_001188254.1; NM_001201325.1. [Q5T2W1-1]
DR RefSeq; NP_001188255.1; NM_001201326.1. [Q5T2W1-2]
DR RefSeq; NP_002605.2; NM_002614.4. [Q5T2W1-1]
DR RefSeq; XP_016856953.1; XM_017001464.1.
DR PDB; 2EEI; NMR; -; A=132-224.
DR PDB; 2EEJ; NMR; -; A=376-458.
DR PDB; 2VSP; X-ray; 2.60 A; A/B/C/D=375-459.
DR PDB; 3TMH; X-ray; 3.80 A; A/E/I=375-459.
DR PDB; 4Q2P; X-ray; 2.05 A; A/B/C=132-215.
DR PDB; 6EZI; X-ray; 1.50 A; A=374-460.
DR PDBsum; 2EEI; -.
DR PDBsum; 2EEJ; -.
DR PDBsum; 2VSP; -.
DR PDBsum; 3TMH; -.
DR PDBsum; 4Q2P; -.
DR PDBsum; 6EZI; -.
DR AlphaFoldDB; Q5T2W1; -.
DR SMR; Q5T2W1; -.
DR BioGRID; 111200; 63.
DR CORUM; Q5T2W1; -.
DR IntAct; Q5T2W1; 24.
DR MINT; Q5T2W1; -.
DR STRING; 9606.ENSP00000394485; -.
DR iPTMnet; Q5T2W1; -.
DR PhosphoSitePlus; Q5T2W1; -.
DR BioMuta; PDZK1; -.
DR DMDM; 73621372; -.
DR jPOST; Q5T2W1; -.
DR MassIVE; Q5T2W1; -.
DR MaxQB; Q5T2W1; -.
DR PaxDb; Q5T2W1; -.
DR PeptideAtlas; Q5T2W1; -.
DR PRIDE; Q5T2W1; -.
DR ProteomicsDB; 18326; -.
DR ProteomicsDB; 64362; -. [Q5T2W1-1]
DR Antibodypedia; 1599; 421 antibodies from 32 providers.
DR DNASU; 5174; -.
DR Ensembl; ENST00000344770.6; ENSP00000342143.2; ENSG00000174827.14. [Q5T2W1-1]
DR Ensembl; ENST00000417171.6; ENSP00000394485.1; ENSG00000174827.14. [Q5T2W1-1]
DR Ensembl; ENST00000451928.6; ENSP00000403422.2; ENSG00000174827.14. [Q5T2W1-2]
DR GeneID; 5174; -.
DR KEGG; hsa:5174; -.
DR MANE-Select; ENST00000417171.6; ENSP00000394485.1; NM_001201325.2; NP_001188254.1.
DR UCSC; uc001eoo.3; human. [Q5T2W1-1]
DR CTD; 5174; -.
DR DisGeNET; 5174; -.
DR GeneCards; PDZK1; -.
DR HGNC; HGNC:8821; PDZK1.
DR HPA; ENSG00000174827; Tissue enriched (kidney).
DR MIM; 603831; gene.
DR neXtProt; NX_Q5T2W1; -.
DR OpenTargets; ENSG00000174827; -.
DR PharmGKB; PA33165; -.
DR VEuPathDB; HostDB:ENSG00000174827; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00950000182849; -.
DR HOGENOM; CLU_031712_1_0_1; -.
DR InParanoid; Q5T2W1; -.
DR OMA; TSVTFHI; -.
DR OrthoDB; 880632at2759; -.
DR PhylomeDB; Q5T2W1; -.
DR TreeFam; TF350449; -.
DR PathwayCommons; Q5T2W1; -.
DR SignaLink; Q5T2W1; -.
DR BioGRID-ORCS; 5174; 26 hits in 1066 CRISPR screens.
DR ChiTaRS; PDZK1; human.
DR EvolutionaryTrace; Q5T2W1; -.
DR GeneWiki; PDZK1; -.
DR GenomeRNAi; 5174; -.
DR Pharos; Q5T2W1; Tbio.
DR PRO; PR:Q5T2W1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5T2W1; protein.
DR Bgee; ENSG00000174827; Expressed in adult mammalian kidney and 98 other tissues.
DR ExpressionAtlas; Q5T2W1; baseline and differential.
DR Genevisible; Q5T2W1; HS.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0031528; C:microvillus membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR GO; GO:0005124; F:scavenger receptor binding; IEA:Ensembl.
DR GO; GO:0015879; P:carnitine transport; IDA:BHF-UCL.
DR GO; GO:1904064; P:positive regulation of cation transmembrane transport; IDA:BHF-UCL.
DR GO; GO:0032414; P:positive regulation of ion transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:1905477; P:positive regulation of protein localization to membrane; IMP:ARUK-UCL.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0044070; P:regulation of anion transport; ISS:UniProtKB.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; NAS:UniProtKB.
DR Gene3D; 2.30.42.10; -; 4.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF17820; PDZ_6; 1.
DR SMART; SM00228; PDZ; 4.
DR SUPFAM; SSF50156; SSF50156; 4.
DR PROSITE; PS50106; PDZ; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Membrane;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..519
FT /note="Na(+)/H(+) exchange regulatory cofactor NHE-RF3"
FT /id="PRO_0000058287"
FT DOMAIN 9..90
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 134..215
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 243..323
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 378..458
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 347..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJ40"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIL4"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIL4"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIL4"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIL4"
FT MOD_RES 451
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIL4"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIL4"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIL4"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIL4"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIL4"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIL4"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIL4"
FT VAR_SEQ 154..264
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044637"
FT CONFLICT 195
FT /note="E -> K (in Ref. 1; AAC12264)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="D -> G (in Ref. 2; BAG60531)"
FT /evidence="ECO:0000305"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:4Q2P"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2EEI"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4Q2P"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:4Q2P"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:4Q2P"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:4Q2P"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:4Q2P"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:4Q2P"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:4Q2P"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:2EEI"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:6EZI"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:2EEJ"
FT STRAND 391..395
FT /evidence="ECO:0007829|PDB:6EZI"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:6EZI"
FT HELIX 411..415
FT /evidence="ECO:0007829|PDB:6EZI"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:6EZI"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:2EEJ"
FT HELIX 436..444
FT /evidence="ECO:0007829|PDB:6EZI"
FT STRAND 448..455
FT /evidence="ECO:0007829|PDB:6EZI"
SQ SEQUENCE 519 AA; 57129 MW; 98BF707F87CD77A6 CRC64;
MTSTFNPREC KLSKQEGQNY GFFLRIEKDT EGHLVRVVEK CSPAEKAGLQ DGDRVLRING
VFVDKEEHMQ VVDLVRKSGN SVTLLVLDGD SYEKAVKTRV DLKELGQSQK EQGLSDNILS
PVMNGGVQTW TQPRLCYLVK EGGSYGFSLK TVQGKKGVYM TDITPQGVAM RAGVLADDHL
IEVNGENVED ASHEEVVEKV KKSGSRVMFL LVDKETDKRH VEQKIQFKRE TASLKLLPHQ
PRIVEMKKGS NGYGFYLRAG SEQKGQIIKD IDSGSPAEEA GLKNNDLVVA VNGESVETLD
HDSVVEMIRK GGDQTSLLVV DKETDNMYRL AHFSPFLYYQ SQELPNGSVK EAPAPTPTSL
EVSSPPDTTE EVDHKPKLCR LAKGENGYGF HLNAIRGLPG SFIKEVQKGG PADLAGLEDE
DVIIEVNGVN VLDEPYEKVV DRIQSSGKNV TLLVCGKKAY DYFQAKKIPI VSSLADPLDT
PPDSKEGIVV ESNHDSHMAK ERAHSTASHS SSNSEDTEM
