NHRF2_RABIT
ID NHRF2_RABIT Reviewed; 316 AA.
AC Q8SQG9;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Na(+)/H(+) exchange regulatory cofactor NHE-RF2;
DE AltName: Full=PDZ domain-containing protein NHERF-2;
DE AltName: Full=Sodium-hydrogen exchanger regulatory factor 2;
DE AltName: Full=Solute carrier family 9 isoform A3 regulatory factor 2;
GN Name=SLC9A3R2; Synonyms=NHERF2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH PODXL.
RC TISSUE=Renal glomerulus;
RX PubMed=11997330; DOI=10.1152/ajprenal.00131.2001;
RA Li Y., Li J., Straight S.W., Kershaw D.B.;
RT "PDZ domain-mediated interaction of rabbit podocalyxin and Na(+)/H(+)
RT exchange regulatory factor-2.";
RL Am. J. Physiol. 282:F1129-F1139(2002).
RN [2]
RP DIMERIZATION.
RX PubMed=11456497; DOI=10.1021/bi0103516;
RA Lau A.G., Hall R.A.;
RT "Oligomerization of NHERF-1 and NHERF-2 PDZ domains: differential
RT regulation by association with receptor carboxyl-termini and by
RT phosphorylation.";
RL Biochemistry 40:8572-8580(2001).
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 cAMP-mediated phosphorylation and inhibition
CC of SLC9A3. May also act as scaffold protein in the nucleus (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer, and heterodimer with SLC9A3R1. Binds ADRB2, SLC9A3,
CC P2RY1, P2YR2, SRY, RDX, PDZK1 and LPAR2 (By similarity). Found in a
CC complex with EZR, PODXL and SLC9A3R2 (By similarity). Interacts (via
CC the PDZ domains) with PODXL (via the C-terminal PDZ-binding motif
CC DTHL); interaction is detected in glomerular epithelium cells (By
CC similarity). Binds PODXL. Interacts with SGK1 and KCNJ1/ROMK1 (By
CC similarity). Interacts (via the PDZ domains) with SLC26A6 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8SQG9; Q28645: PODXL; NbExp=7; IntAct=EBI-1174758, EBI-8375591;
CC Q8SQG9; Q01814-1: ATP2B2; Xeno; NbExp=3; IntAct=EBI-1174758, EBI-1174262;
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Apical cell
CC membrane {ECO:0000250}. Note=Localizes with EZR and PODXL at the apical
CC cell membrane of glomerular epithelium cells and the sides of the food
CC processes. Nuclear, in a punctate pattern (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in kidney glomeruli.
CC {ECO:0000269|PubMed:11997330}.
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DR EMBL; AF358433; AAL78310.1; -; mRNA.
DR RefSeq; NP_001075576.1; NM_001082107.1.
DR AlphaFoldDB; Q8SQG9; -.
DR SMR; Q8SQG9; -.
DR IntAct; Q8SQG9; 2.
DR MINT; Q8SQG9; -.
DR GeneID; 100008813; -.
DR KEGG; ocu:100008813; -.
DR CTD; 9351; -.
DR InParanoid; Q8SQG9; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:InterPro.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0031799; F:type 2 metabotropic glutamate receptor binding; IPI:ARUK-UCL.
DR GO; GO:0031800; F:type 3 metabotropic glutamate receptor binding; IPI:ARUK-UCL.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR015098; EBP50_C-term.
DR InterPro; IPR017300; NHERF-1/NHERF-2.
DR InterPro; IPR031197; NHERF-2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR14191:SF4; PTHR14191:SF4; 2.
DR Pfam; PF09007; EBP50_C; 2.
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 Cell membrane; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..316
FT /note="Na(+)/H(+) exchange regulatory cofactor NHE-RF2"
FT /id="PRO_0000096807"
FT DOMAIN 11..91
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 151..231
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 109..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHL1"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15599"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15599"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15599"
SQ SEQUENCE 316 AA; 35320 MW; F496FAD64156BCED CRC64;
MAAPEPLRPR LCRLVRGEQG YGFHLHGEKG RRGQFIRRVE PGSPAEAAAL RAGDRLVEVN
GVNVEGETHH QVVQRIKAVE GETRLLVVDK ETDEELRRRQ LTCTEDMAQR GLPPAHDPWE
PKPDWARAGS LSSDAGQKDV NGPPRELRPR LCHLRKGPQG YGFNLHSDKS RPGQYIRSVD
PGSPAAHSGL CAQDRLIEVN GQNVEGLRHA EVVARIKAKE DEARLLLVDP ETDEYFKRLR
VTPTEEHVEG PLPSPITNGT SPAQDASAWK RDPFQESGLH LSPTAAEAKE KARATRVNKR
APQMDWNRKR EIFSNF
