FXYD domain-containing ion transport regulator 2; FXYD domain-containing ion transport regulator 2 (FXYD2), also known as sodium/potassium-transporting ATPase subunit gamma, or Na(+)/K(+) ATPase subunit gamma, or sodium pump gamma chain, is the regulatory subunit of the sodium/potassium-transporting ATPase (Na,K-ATPase). Na+,K+-ATPase is a heteromeric complex consisting of a large alpha-subunit, which is responsible for ATP hydrolysis, ion transport, and CTS binding, and a beta-subunit, acting as a chaperone. Although the Na,K-ATPase does not depend on the gamma subunit to be functional, it is thought that the gamma subunit modulates the enzyme's activity by inducing ion channel activity. Mutations in this gene have been associated with renal hypomagnesaemia.

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gi 11125764  8 GSPKGDVDPFYYDYETVRNGGLIFAGLAFIVGLLILLSRRFRC 50
Cdd:cd20318  1 GSPEGSEDPFTYDYETVRNGGLIFAAVAFVVGLLIILSKRFRC 43

FXYD domain-containing ion transport regulator 2; FXYD domain-containing ion transport regulator 2 (FXYD2), also known as sodium/potassium-transporting ATPase subunit gamma, or Na(+)/K(+) ATPase subunit gamma, or sodium pump gamma chain, is the regulatory subunit of the sodium/potassium-transporting ATPase (Na,K-ATPase). Na+,K+-ATPase is a heteromeric complex consisting of a large alpha-subunit, which is responsible for ATP hydrolysis, ion transport, and CTS binding, and a beta-subunit, acting as a chaperone. Although the Na,K-ATPase does not depend on the gamma subunit to be functional, it is thought that the gamma subunit modulates the enzyme's activity by inducing ion channel activity. Mutations in this gene have been associated with renal hypomagnesaemia.

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gi 11125764  8 GSPKGDVDPFYYDYETVRNGGLIFAGLAFIVGLLILLSRRFRC 50
Cdd:cd20318  1 GSPEGSEDPFTYDYETVRNGGLIFAAVAFVVGLLIILSKRFRC 43

FXYD domain-containing ion transport regulator 2; FXYD domain-containing ion transport regulator 2 (FXYD2), also known as sodium/potassium-transporting ATPase subunit gamma, or Na(+)/K(+) ATPase subunit gamma, or sodium pump gamma chain, is the regulatory subunit of the sodium/potassium-transporting ATPase (Na,K-ATPase). Na+,K+-ATPase is a heteromeric complex consisting of a large alpha-subunit, which is responsible for ATP hydrolysis, ion transport, and CTS binding, and a beta-subunit, acting as a chaperone. Although the Na,K-ATPase does not depend on the gamma subunit to be functional, it is thought that the gamma subunit modulates the enzyme's activity by inducing ion channel activity. Mutations in this gene have been associated with renal hypomagnesaemia.

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gi 11125764  8 GSPKGDVDPFYYDYETVRNGGLIFAGLAFIVGLLILLSRRFRC 50
Cdd:cd20318  1 GSPEGSEDPFTYDYETVRNGGLIFAAVAFVVGLLIILSKRFRC 43

FXYD domain-containing ion transport regulator 1; FXYD domain-containing ion transport regulator 1 (FXYD1), also known as phospholemman (PLM), or sodium/potassium-transporting ATPase subunit FXYD1, associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na+ out of the cell and K+ into the cell. It is a plasma membrane substrate for several kinases, including protein kinase A, protein kinase C, NIMA kinase, and myotonic dystrophy kinase. It is thought to form an ion channel or regulate ion channel activity. Transcript variants with different 5' UTR sequences have been described in the literature.

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gi 11125764 15 DPFYYDYETVRNGGLIFAGLAFIVGLLILLSRRFRCGGNKKRRQINEDEP 64
Cdd:cd20317  5 DPFTYDYQSLRIGGLIIAGILFILGILIILSRRCRCKFNQQQRTGEPDEE 54

phenylalanine-X-tyrosine-aspartate (FXYD) family; FXYDs are small single-transmembrane proteins that act as novel regulators of Na+/K+-ATPase (NKA). The transmembrane domain and the conserved Phe-X-Tyr-Asp motif of FXYD play a role in the binding of FXYD to the alpha- and beta-subunits of NKA. PFXYD (proline-phenylalanine-X-tyrosine-aspartate) at the beginning of the signature sequence is invariant in all known examples in mammals and identical except for the proline in other vertebrates; X is usually Y (tyrosine), but can also be E, T, or H (glutamate, threonine, or histidine). The FXYD protein family contains at least twelve members that have the extracellular FXYD motif, transmembrane domain, and intracellular domain. Members share a 35-amino acid signature sequence domain, beginning with PFXYD and containing 7 invariant and 6 highly conserved amino acids. In mammals, members of the FXYD family include FXYD1 (phospholemman, PLM), FXYD2 (the gamma-subunit of NKA), FXYD3 (mammary tumor marker Mat-8), FXYD4 (corticosteroid hormone-induced factor, CHIF), FXYD5 (dysadherin), FXYD6 (phosphohippolin), and FXYD7. In elasmobranchs, FXYD10 (phospholemman-like protein from shark, PLMS) was first identified in the rectal glands of Squalus acanthias. In addition, studies on sharks reported that the functions of FXYD10 via its C-terminal cysteine residue interactions were associated with negative regulation of shark NKA activity. Teleostean FXYD proteins (FXYD2, 5-9, 11, and 12) have been reported in certain teleosts such as the Tetraodon nigroviridis, Salmo salar, Danio rerio, and Oryzias dancena. Recent studies have demonstrated that several teleost FXYD isoforms are expressed in the gills and kidneys of the fish, and their expression levels are altered in response to salinity changes, suggesting that these FXYDs may regulate electrolyte homeostasis and body fluid of the fish.

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gi 11125764 17 FYYDYETVRNGGLIFAGLAFIVGLLILLSR 46
Cdd:cd20277  1 FYYDYETLRIGGLVFAAVLFIVGILILLSG 30

FXYD domain-containing ion transport regulator 4; FXYD domain-containing ion transport regulator 4 (FXYD4), also known as CHIF (channel-inducing factor or corticosteroid hormone-induced factor), evokes K+ conductance in oocytes and is localized in the distal parts of the nephron and in the colon. CHIF, a putative K channel regulator, is regulated by aldosterone in the colon and by K+ intake in the kidney.

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gi 11125764 15 DPFYYDYETVRNGGLIFAGLAFIVGLLILLSRRFRCGGNKK 55
Cdd:cd20322  8 SPFYYDWESLQLGGMICAGLLCIAGIAFALSGKCKCKHSQK 48

FXYD domain-containing ion transport regulator 3 and similar proteins; This subfamily includes FXYD domain-containing ion transport regulator 3 (FXYD3), FXYD9, and FXYD10, also called PLMS/Phospholemman-like protein. FXYD3, also known as mammary tumor 8 kDa protein (MAT-8), or chloride conductance inducer protein Mat-8, or phospholemman-like (PLML), may function as a chloride channel or as a chloride channel regulator. It associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na+ out of the cell and K+ into the cell. Two transcript variants encode two different isoforms of the protein; in addition, transcripts utilizing alternative polyA signals have been described in the literature. Members here include mammalians and reptiles. FXYD9 is present in teleosts including: Danio rerio, Atlantic salmon, and Japanese Medaka fish. In general, the FXYD9 isoform has the highest degree of conservation among the examined teleost species, indicating that it may be involved in physiological processes that are not evolving within this group of vertebrates. FXYD10, present in shark, associates with and modifies the activity of Na,K-ATPase in vitro through interactions mediated by its transmembrane and cytoplasmic C-terminal domains. It is important in the phosphorylation and potassium deocclusion reactions, which are known to be controlled by A domain movements. It is thought that FXYD10 interacts with the A domain of the shark Na,K-ATPase alpha-subunit.

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gi 11125764 15 DPFYYDYETVRNGGLIFAGLAFIVGLLILLSRRFRCGGNKKRR 57
Cdd:cd20328  9 SPFYYDWHRLRVGGLICAAVLCAIGIIVLLSGKCKCKFNQKKR 51

FXYD domain of FXYD domain-containing ion transport regulator 5; FXYD domain-containing ion transport regulator 5 (FXYD5) is also called dysadherin in humans or related to ion channel (RIC) in mice. Two transcript variants have been found for this gene, and they are both predicted to encode the same protein. Dysadherin is the gamma subunit the human Na,K-ATPase and is the only member that has a large extracellular sequence of 140 amino acids. Dysadherin has been observed to be over-expressed on the surface of cells that have down regulated levels of surface E-cadherin. CCL2 (bone homing cytokine) is a protein that is highly affected by silencing dysadherin expression. Dysadherin interferes with cell adhesion via beta1 subunit interactions and is a target for an extracellular antibody drug conjugate where the antibody to dysadherin is attached to a cardiac glycoside. FXYD5 expression in mouse is mainly in the kidney, intestine, spleen, and lung. Confocal immunofluorescence microscopy of mouse kidney detected FXYD5 on basolateral membranes of connecting tubules, collecting tubules, intercalated cells of collecting duct, and on apical membranes in long thin limb of Henle loop.

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gi 11125764 10 PKGDvDPFYYDYETVRNGGLIFAGLAFIVGLLILLSRRFRC 50
Cdd:cd20323  2 PKWD-EPFTYDYETLRKAGLIIAAVLFITGILVLTCGKVCR 41