ID PLM_CANLF Reviewed; 92 AA. AC P56513; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 17-FEB-2016, entry version 87. DE RecName: Full=Phospholemman; DE AltName: Full=FXYD domain-containing ion transport regulator 1; DE Flags: Precursor; GN Name=FXYD1; Synonyms=PLM; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 21-92. RC TISSUE=Heart ventricle; RX PubMed=1710217; RA Palmer C.J., Scott B.T., Jones L.R.; RT "Purification and complete sequence determination of the major plasma RT membrane substrate for cAMP-dependent protein kinase and protein RT kinase C in myocardium."; RL J. Biol. Chem. 266:11126-11130(1991). CC -!- FUNCTION: May have a functional role in muscle contraction. CC Induces a hyperpolarization-activated chloride current when CC exogenously expressed. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- TISSUE SPECIFICITY: Present in heart, esophagus, stomach, aorta, CC skeletal muscle, smooth muscle, and liver but absent from brain CC and kidney. CC -!- PTM: Major plasma membrane substrate for cAMP-dependent protein CC kinase (PK-A) and protein kinase C (PK-C) in several different CC tissues. Phosphorylated in response to insulin and adrenergic CC stimulation. May be phosphorylated by DMPK (By similarity). CC {ECO:0000250}. CC -!- PTM: Palmitoylation increases half-life and stability, it is CC enhanced upon phosphorylation at Ser-88 by PKA. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FXYD family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M63934; -; NOT_ANNOTATED_CDS; mRNA. DR PIR; A40533; A40533. DR ProteinModelPortal; P56513; -. DR SMR; P56513; 21-92. DR STRING; 9615.ENSCAFP00000010530; -. DR TCDB; 1.A.27.1.1; the phospholemman (plm) family. DR PaxDb; P56513; -. DR eggNOG; ENOG410J08K; Eukaryota. DR eggNOG; ENOG410YYN6; LUCA. DR HOGENOM; HOG000234467; -. DR HOVERGEN; HBG008212; -. DR InParanoid; P56513; -. DR Proteomes; UP000002254; Unplaced. DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW. DR GO; GO:0017080; F:sodium channel regulator activity; IBA:GO_Central. DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IBA:GO_Central. DR InterPro; IPR000272; Ion-transport_regulator_FXYD. DR Pfam; PF02038; ATP1G1_PLM_MAT8; 1. DR ProDom; PD005989; PD005989; 1. DR PROSITE; PS01310; FXYD; 1. PE 1: Evidence at protein level; KW Chloride; Chloride channel; Complete proteome; KW Direct protein sequencing; Ion channel; Ion transport; Lipoprotein; KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1 20 {ECO:0000269|PubMed:1710217}. FT CHAIN 21 92 Phospholemman. FT /FTId=PRO_0000010358. FT TOPO_DOM 21 35 Extracellular. {ECO:0000255}. FT TRANSMEM 36 56 Helical. {ECO:0000255}. FT TOPO_DOM 57 92 Cytoplasmic. {ECO:0000255}. FT MOD_RES 79 79 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q9Z239}. FT MOD_RES 82 82 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9Z239}. FT MOD_RES 83 83 Phosphoserine; by PKA and PKC. FT {ECO:0000250}. FT MOD_RES 88 88 Phosphoserine; by PKA. {ECO:0000250}. FT LIPID 60 60 S-palmitoyl cysteine. {ECO:0000250}. FT LIPID 62 62 S-palmitoyl cysteine. {ECO:0000250}. SQ SEQUENCE 92 AA; 10500 MW; 890DE301BF8E740A CRC64; MAPLHHILVL CVGFLTTATA EAPQEHDPFT YDYQSLRIGG LIIAGILFIL GILIVLSRRC RCKFNQQQRT GEPDEEEGTF RSSIRRLSTR RR //