ID   FXYD4_RAT               Reviewed;          87 AA.
AC   Q63113;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=FXYD domain-containing ion transport regulator 4;
DE   AltName: Full=Channel-inducing factor;
DE            Short=CHIF;
DE   AltName: Full=Corticosteroid-induced protein;
DE   Flags: Precursor;
GN   Name=Fxyd4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Colon;
RX   PubMed=7597086; DOI=10.1073/pnas.92.13.6092;
RA   Attali B., Latter H., Rachamim N., Garty H.;
RT   "A corticosteroid-induced gene expressing an 'IsK-like' K+ channel activity
RT   in Xenopus oocytes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:6092-6096(1995).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=8843704; DOI=10.1152/ajpcell.1996.271.3.c753;
RA   Capurro C., Coutry N., Bonvalet J.-P., Escoubet B., Garty H., Farman N.;
RT   "Cellular localization and regulation of CHIF in kidney and colon.";
RL   Am. J. Physiol. 271:C753-C762(1996).
RN   [3]
RP   STRUCTURE BY NMR OF 21-87.
RX   PubMed=17567018; DOI=10.1021/ja0728371;
RA   Franzin C.M., Teriete P., Marassi F.M.;
RT   "Structural similarity of a membrane protein in micelles and membranes.";
RL   J. Am. Chem. Soc. 129:8078-8079(2007).
CC   -!- FUNCTION: Induces a potassium channel when expressed in Xenopus
CC       oocytes.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Selectively present in the distal parts of the
CC       nephron (medullary and papillary collecting ducts and end portions of
CC       cortical collecting tubule) and in the epithelial cells of the distal
CC       colon. No expression is found in renal proximal tubule, loop of henle
CC       and distal tubule, proximal colon, small intestine, lung, choroid
CC       plexus, salivary glands, or brain. {ECO:0000269|PubMed:8843704}.
CC   -!- INDUCTION: By corticosteroids.
CC   -!- SIMILARITY: Belongs to the FXYD family. {ECO:0000305}.
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DR   EMBL; L41254; AAA74691.1; -; mRNA.
DR   PIR; I59391; I59391.
DR   RefSeq; NP_071783.1; NM_022388.1.
DR   RefSeq; XP_006237268.1; XM_006237206.2.
DR   RefSeq; XP_017448357.1; XM_017592868.1.
DR   PDB; 2JP3; NMR; -; A=21-87.
DR   PDBsum; 2JP3; -.
DR   AlphaFoldDB; Q63113; -.
DR   SMR; Q63113; -.
DR   STRING; 10116.ENSRNOP00000019649; -.
DR   TCDB; 1.A.27.1.4; the phospholemman (plm) family.
DR   PaxDb; Q63113; -.
DR   Ensembl; ENSRNOT00000019649; ENSRNOP00000019649; ENSRNOG00000014578.
DR   GeneID; 64190; -.
DR   UCSC; RGD:70998; rat.
DR   CTD; 53828; -.
DR   RGD; 70998; Fxyd4.
DR   eggNOG; ENOG502TDGY; Eukaryota.
DR   GeneTree; ENSGT00940000153062; -.
DR   HOGENOM; CLU_171208_0_1_1; -.
DR   InParanoid; Q63113; -.
DR   OMA; QLGGMIC; -.
DR   OrthoDB; 1606794at2759; -.
DR   PhylomeDB; Q63113; -.
DR   TreeFam; TF333443; -.
DR   Reactome; R-RNO-5578775; Ion homeostasis.
DR   Reactome; R-RNO-936837; Ion transport by P-type ATPases.
DR   EvolutionaryTrace; Q63113; -.
DR   PRO; PR:Q63113; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000014578; Expressed in kidney and 10 other tissues.
DR   Genevisible; Q63113; RN.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:RGD.
DR   GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:InterPro.
DR   GO; GO:0005267; F:potassium channel activity; IDA:RGD.
DR   GO; GO:0098662; P:inorganic cation transmembrane transport; IDA:RGD.
DR   GO; GO:0043269; P:regulation of ion transport; IEA:InterPro.
DR   InterPro; IPR000272; Ion-transport_regulator_FXYD.
DR   Pfam; PF02038; ATP1G1_PLM_MAT8; 1.
DR   PROSITE; PS01310; FXYD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Ion channel; Ion transport; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..87
FT                   /note="FXYD domain-containing ion transport regulator 4"
FT                   /id="PRO_0000010368"
FT   TOPO_DOM        21..38
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        60..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          67..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           29..34
FT                   /evidence="ECO:0007829|PDB:2JP3"
FT   HELIX           35..57
FT                   /evidence="ECO:0007829|PDB:2JP3"
FT   HELIX           60..65
FT                   /evidence="ECO:0007829|PDB:2JP3"
FT   TURN            69..71
FT                   /evidence="ECO:0007829|PDB:2JP3"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:2JP3"
FT   HELIX           77..80
FT                   /evidence="ECO:0007829|PDB:2JP3"
SQ   SEQUENCE   87 AA;  9084 MW;  5D0DE1FFC6B1BCCA CRC64;
     MEGITCAFLL VLAGLPVLEA NGPVDKGSPF YYDWESLQLG GMIFGGLLCI AGIAMALSGK
     CKCRRNHTPS SLPEKVTPLI TPGSAST