PLM_BOVIN
ID PLM_BOVIN Reviewed; 92 AA.
AC Q3SZX0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Phospholemman {ECO:0000250|UniProtKB:P56513};
DE AltName: Full=FXYD domain-containing ion transport regulator 1 {ECO:0000250|UniProtKB:O00168};
DE AltName: Full=Sodium/potassium-transporting ATPase subunit FXYD1 {ECO:0000305};
DE Flags: Precursor;
GN Name=FXYD1 {ECO:0000250|UniProtKB:O00168};
GN Synonyms=PLM {ECO:0000250|UniProtKB:O00168};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, IDENTIFICATION IN SODIUM/POTASSIUM-TRANSPORTING ATPASE COMPLEX,
RP INTERACTION WITH ATP1A1; ATP1A2 AND ATP1A3, AND TISSUE SPECIFICITY.
RX PubMed=12657675; DOI=10.1523/jneurosci.23-06-02161.2003;
RA Feschenko M.S., Donnet C., Wetzel R.K., Asinovski N.K., Jones L.R.,
RA Sweadner K.J.;
RT "Phospholemman, a single-span membrane protein, is an accessory protein of
RT Na,K-ATPase in cerebellum and choroid plexus.";
RL J. Neurosci. 23:2161-2169(2003).
CC -!- FUNCTION: Associates with and regulates the activity of the
CC sodium/potassium-transporting ATPase (NKA) which transports Na(+) out
CC of the cell and K(+) into the cell (PubMed:12657675). Inhibits NKA
CC activity in its unphosphorylated state and stimulates activity when
CC phosphorylated (By similarity). Reduces glutathionylation of the NKA
CC beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated
CC inhibition of ATP1B1 (By similarity). Contributes to female sexual
CC development by maintaining the excitability of neurons which secrete
CC gonadotropin-releasing hormone (By similarity).
CC {ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:P56513,
CC ECO:0000250|UniProtKB:Q9Z239, ECO:0000269|PubMed:12657675}.
CC -!- SUBUNIT: Homotetramer (By similarity). Monomer (By similarity).
CC Regulatory subunit of the sodium/potassium-transporting ATPase (NKA)
CC which is composed of a catalytic alpha subunit, an auxiliary non-
CC catalytic beta subunit and an additional regulatory subunit
CC (PubMed:12657675). The monomeric form associates with NKA while the
CC oligomeric form does not (By similarity). Interacts with the catalytic
CC alpha-1 subunit ATP1A1 (PubMed:12657675). Also interacts with the
CC catalytic alpha-2 and alpha-3 subunits ATP1A2 and ATP1A3
CC (PubMed:12657675). Very little interaction with ATP1A1, ATP1A2 or
CC ATP1A3 when phosphorylated at Ser-83 (By similarity). Interacts with
CC the non-catalytic beta-1 subunit ATP1B1 (By similarity). Oxidative
CC stress decreases interaction with ATP1A1 but increases interaction with
CC ATP1B1 (By similarity). {ECO:0000250|UniProtKB:O00168,
CC ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:P56513,
CC ECO:0000250|UniProtKB:Q9Z239, ECO:0000269|PubMed:12657675}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P56513}; Single-pass type I membrane protein
CC {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O08589};
CC Single-pass type I membrane protein {ECO:0000255}. Membrane, caveola
CC {ECO:0000250|UniProtKB:O08589}. Cell membrane, sarcolemma, T-tubule
CC {ECO:0000250|UniProtKB:O08589}. Note=Detected in the apical cell
CC membrane in brain. In myocytes, localizes to sarcolemma, t-tubules and
CC intercalated disks. {ECO:0000250|UniProtKB:O08589}.
CC -!- TISSUE SPECIFICITY: In the brain, detected in cerebellum and choroid
CC plexus (at protein level). {ECO:0000269|PubMed:12657675}.
CC -!- DOMAIN: The cytoplasmic domain is sufficient to regulate
CC sodium/potassium-transporting ATPase activity.
CC {ECO:0000250|UniProtKB:O08589}.
CC -!- PTM: Major plasma membrane substrate for cAMP-dependent protein kinase
CC (PKA) and protein kinase C (PKC) in several different tissues.
CC Phosphorylated in response to insulin and adrenergic stimulation.
CC Phosphorylation at Ser-88 stimulates sodium/potassium-transporting
CC ATPase activity while the unphosphorylated form inhibits
CC sodium/potassium-transporting ATPase activity. Phosphorylation
CC increases tetramerization, decreases binding to ATP1A1 and reduces
CC inhibition of ATP1A1 activity. Phosphorylation at Ser-83 leads to
CC greatly reduced interaction with ATP1A1, ATP1A2 and ATP1A3. May be
CC phosphorylated by DMPK. {ECO:0000250|UniProtKB:O00168,
CC ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:P56513}.
CC -!- PTM: Palmitoylation increases half-life and stability and is enhanced
CC upon phosphorylation at Ser-88 by PKA. {ECO:0000250|UniProtKB:O00168}.
CC -!- SIMILARITY: Belongs to the FXYD family. {ECO:0000305}.
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DR EMBL; BC102671; AAI02672.1; -; mRNA.
DR RefSeq; NP_001069878.1; NM_001076410.1.
DR RefSeq; XP_005219074.1; XM_005219017.2.
DR RefSeq; XP_005219076.1; XM_005219019.3.
DR RefSeq; XP_005219077.1; XM_005219020.3.
DR RefSeq; XP_010813107.1; XM_010814805.2.
DR AlphaFoldDB; Q3SZX0; -.
DR SMR; Q3SZX0; -.
DR STRING; 9913.ENSBTAP00000042049; -.
DR PaxDb; Q3SZX0; -.
DR PRIDE; Q3SZX0; -.
DR Ensembl; ENSBTAT00000044563; ENSBTAP00000042049; ENSBTAG00000017816.
DR GeneID; 616139; -.
DR KEGG; bta:616139; -.
DR CTD; 5348; -.
DR VEuPathDB; HostDB:ENSBTAG00000017816; -.
DR VGNC; VGNC:29156; FXYD1.
DR eggNOG; ENOG502S5XM; Eukaryota.
DR GeneTree; ENSGT00940000153062; -.
DR HOGENOM; CLU_171208_2_0_1; -.
DR InParanoid; Q3SZX0; -.
DR OMA; FTMANAE; -.
DR OrthoDB; 1621616at2759; -.
DR TreeFam; TF333443; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000017816; Expressed in laryngeal cartilage and 102 other tissues.
DR ExpressionAtlas; Q3SZX0; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:UniProtKB.
DR GO; GO:0030315; C:T-tubule; ISS:UniProtKB.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:InterPro.
DR GO; GO:0010734; P:negative regulation of protein glutathionylation; ISS:UniProtKB.
DR GO; GO:1903278; P:positive regulation of sodium ion export across plasma membrane; IDA:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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 Cell membrane; Glutathionylation; Ion transport; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Potassium; Potassium transport;
KW Reference proteome; Signal; Sodium; Sodium transport;
KW Sodium/potassium transport; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000250|UniProtKB:P56513"
FT CHAIN 21..92
FT /note="Phospholemman"
FT /id="PRO_0000283050"
FT TOPO_DOM 21..35
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 65..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56513"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z239"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z239"
FT MOD_RES 83
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000250|UniProtKB:P56513"
FT MOD_RES 88
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P56513"
FT MOD_RES 89
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P56513"
FT LIPID 60
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O00168"
FT LIPID 62
FT /note="S-palmitoyl cysteine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O00168"
SQ SEQUENCE 92 AA; 10447 MW; 42244DD050C60A3B CRC64;
MASLSHILVL CVGLLAMVNA EAPQEHDPFT YDYQSLRIGG LIIAGILFIL GILIVLSRRC
RCKFNQQQRT GEPDEEEGTF RSSIRRLSTR RR
