Fxyd1
entrez
56188
canonical
uniprot
Q9Z239
canonical
ensembl
ENSMUSG00000036570
resolver
ensp
ENSMUSP00000048460
resolver
ensp
ENSMUSP00000071617
resolver
ensp
ENSMUSP00000103745
resolver
ensp
ENSMUSP00000145589
resolver
ensp
ENSMUSP00000145712
resolver
ensp
ENSMUSP00000145818
resolver
ensp
ENSMUSP00000145920
resolver
ensp
ENSMUSP00000146064
resolver
ensp
ENSMUSP00000146288
resolver
ensp
ENSMUSP00000146295
resolver
ensp
ENSMUSP00000357512
resolver
enst
ENSMUST00000039909
resolver
enst
ENSMUST00000071697
resolver
enst
ENSMUST00000108110
resolver
enst
ENSMUST00000205439
resolver
enst
ENSMUST00000205778
resolver
enst
ENSMUST00000206012
resolver
enst
ENSMUST00000206305
resolver
enst
ENSMUST00000206328
resolver
enst
ENSMUST00000206474
resolver
enst
ENSMUST00000206860
resolver
genesymbol
Fxyd1
resolver
genesymbol_syn
Plm
resolver
uniprot_entry
PLM_MOUSE
resolver
amino_acid_sequence
MASPGHILALCVCLLSMASAEAPQEPDPFTYDYHTLRIGGLTIAGILFILGILIILSKRCRCKFNQQQRTGEPDEEEGTFRSSIRRLSSRRR
uniprot
proteins
function
FUNCTION: 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 (PubMed:15563542, PubMed:18065526). Inhibits NKA activity in its unphosphorylated state and stimulates activity when phosphorylated (By similarity). Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1 (PubMed:21454534). Contributes to female sexual development by maintaining the excitability of neurons which secrete gonadotropin-releasing hormone (PubMed:19187398). {ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:P56513, ECO:0000269|PubMed:19187398, ECO:0000269|PubMed:21454534}.
uniprot
proteins
mass_dalton
10323
uniprot
proteins
post_translational_modification
PTM: Major plasma membrane substrate for cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) in several different tissues. Phosphorylated in response to insulin and adrenergic stimulation. Phosphorylation at Ser-88 stimulates sodium/potassium-transporting ATPase activity while the unphosphorylated form inhibits sodium/potassium-transporting ATPase activity. Phosphorylation increases tetramerization, decreases binding to ATP1A1 and reduces inhibition of ATP1A1 activity. Phosphorylation at Ser-83 leads to greatly reduced interaction with ATP1A1, ATP1A2 and ATP1A3. May be phosphorylated by DMPK. {ECO:0000250|UniProtKB:O00168, ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:P56513}.; PTM: Palmitoylation increases half-life and stability and is enhanced upon phosphorylation at Ser-88 by PKA. {ECO:0000250|UniProtKB:O00168}.
uniprot
proteins
protein_family
FXYD family
uniprot
proteins
pubmed
11410367
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15563542
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17283221
uniprot
proteins
pubmed
18065526
uniprot
proteins
pubmed
18630941
uniprot
proteins
pubmed
19187398
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21454534
uniprot
proteins
pubmed
23532852
uniprot
proteins
sequence_length
92
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P56513}; Single-pass type I membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O08589}; Single-pass type I membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:O08589}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O08589}. Note=Detected in the apical cell membrane in brain. In myocytes, localizes to sarcolemma, t-tubules and intercalated disks. {ECO:0000250|UniProtKB:O08589}.
uniprot
proteins
transmembrane_region
TRANSMEM 36..56; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins