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Cardiac phospholamban (PLB)

 PPLA_HUMAN              Reviewed;          52 AA.
P26678;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
25-OCT-2017, entry version 174.
RecName: Full=Cardiac phospholamban;
Short=PLB;
Name=PLN; Synonyms=PLB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1828805;
Fujii J., Zarain-Herzberg A., Willard H.F., Tada M., Maclennan D.H.;
"Structure of the rabbit phospholamban gene, cloning of the human
cDNA, and assignment of the gene to human chromosome 6.";
J. Biol. Chem. 266:11669-11675(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Salvatore C.A., Jacobson M.A.;
"Cloning of human cardiac phospholamban.";
Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10198197; DOI=10.1006/jmcc.1998.0904;
McTiernan C.F., Frye C.S., Lemster B.H., Kinder E.A.,
Ogletree-Hughes M.L., Moravec C.S., Feldman A.M.;
"The human phospholamban gene: structure and expression.";
J. Mol. Cell. Cardiol. 31:679-692(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INVOLVEMENT IN CMH18.
PubMed=12705874; DOI=10.1016/S0006-291X(03)00526-6;
Minamisawa S., Sato Y., Tatsuguchi Y., Fujino T., Imamura S.,
Uetsuka Y., Nakazawa M., Matsuoka R.;
"Mutation of the phospholamban promoter associated with hypertrophic
cardiomyopathy.";
Biochem. Biophys. Res. Commun. 304:1-4(2003).
[6]
PHOSPHORYLATION AT SER-16 BY DMPK, AND SUBCELLULAR LOCATION.
PubMed=15598648; DOI=10.1074/jbc.M412845200;
Kaliman P., Catalucci D., Lam J.T., Kondo R., Gutierrez J.C.,
Reddy S., Palacin M., Zorzano A., Chien K.R., Ruiz-Lozano P.;
"Myotonic dystrophy protein kinase phosphorylates phospholamban and
regulates calcium uptake in cardiomyocyte sarcoplasmic reticulum.";
J. Biol. Chem. 280:8016-8021(2005).
[7]
PHOSPHORYLATION AT THR-17 BY CAMK2.
PubMed=16690701; DOI=10.1113/jphysiol.2006.111757;
Rose A.J., Kiens B., Richter E.A.;
"Ca2+-calmodulin-dependent protein kinase expression and signalling in
skeletal muscle during exercise.";
J. Physiol. (Lond.) 574:889-903(2006).
[8]
INTERACTION WITH HAX1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17241641; DOI=10.1016/j.jmb.2006.10.057;
Vafiadaki E., Sanoudou D., Arvanitis D.A., Catino D.H., Kranias E.G.,
Kontrogianni-Konstantopoulos A.;
"Phospholamban interacts with HAX-1, a mitochondrial protein with
anti-apoptotic function.";
J. Mol. Biol. 367:65-79(2007).
[9]
FUNCTION, CHARACTERIZATION OF VARIANTS CMD1P HIS-9; LEU-9; CYS-9 AND
ARG-14 DEL, PHOSPHORYLATION AT SER-16, AND MUTAGENESIS OF ARG-13;
ARG-14; SER-16 AND THR-17.
PubMed=22707725; DOI=10.1074/jbc.M112.382713;
Ceholski D.K., Trieber C.A., Holmes C.F., Young H.S.;
"Lethal, hereditary mutants of phospholamban elude phosphorylation by
protein kinase A.";
J. Biol. Chem. 287:26596-26605(2012).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
STRUCTURE BY NMR OF 1-25.
PubMed=7779806; DOI=10.1021/bi00023a006;
Mortishire-Smith R.J., Pitzenberger S.M., Burke C.J., Middaugh C.R.,
Garsky V.M., Johnson R.G.;
"Solution structure of the cytoplasmic domain of phospholamban:
phosphorylation leads to a local perturbation in secondary
structure.";
Biochemistry 34:7603-7613(1995).
[12]
3D-STRUCTURE MODELING.
PubMed=7749920; DOI=10.1038/nsb0295-154;
Adams P.D., Arkin I.T., Engelman D.M., Bruenger A.T.;
"Computational searching and mutagenesis suggest a structure for the
pentameric transmembrane domain of phospholamban.";
Nat. Struct. Biol. 2:154-162(1995).
[13]
3D-STRUCTURE MODELING.
PubMed=9512019; DOI=10.1016/S0006-3495(98)77835-X;
Herzyk P., Hubbard R.E.;
"Using experimental information to produce a model of the
transmembrane domain of the ion channel phospholamban.";
Biophys. J. 74:1203-1214(1998).
[14]
STRUCTURE BY NMR, AND SUBUNIT.
PubMed=16043693; DOI=10.1073/pnas.0504920102;
Oxenoid K., Chou J.J.;
"The structure of phospholamban pentamer reveals a channel-like
architecture in membranes.";
Proc. Natl. Acad. Sci. U.S.A. 102:10870-10875(2005).
[15]
STRUCTURE BY NMR, AND SUBUNIT.
PubMed=16897780; DOI=10.1002/prot.21091;
Potluri S., Yan A.K., Chou J.J., Donald B.R., Bailey-Kellogg C.;
"Structure determination of symmetric homo-oligomers by a complete
search of symmetry configuration space, using NMR restraints and van
der Waals packing.";
Proteins 65:203-219(2006).
[16]
VARIANT CMD1P CYS-9, AND CHARACTERIZATION OF VARIANT CMD1P CYS-9.
PubMed=12610310; DOI=10.1126/science.1081578;
Schmitt J.P., Kamisago M., Asahi M., Li G.H., Ahmad F., Mende U.,
Kranias E.G., MacLennan D.H., Seidman J.G., Seidman C.E.;
"Dilated cardiomyopathy and heart failure caused by a mutation in
phospholamban.";
Science 299:1410-1413(2003).
[17]
VARIANT CMD1P ARG-14 DEL, AND CHARACTERIZATION OF VARIANT CMD1P ARG-14
DEL.
PubMed=16432188; DOI=10.1073/pnas.0510519103;
Haghighi K., Kolokathis F., Gramolini A.O., Waggoner J.R., Pater L.,
Lynch R.A., Fan G.C., Tsiapras D., Parekh R.R., Dorn G.W. II,
MacLennan D.H., Kremastinos D.T., Kranias E.G.;
"A mutation in the human phospholamban gene, deleting arginine 14,
results in lethal, hereditary cardiomyopathy.";
Proc. Natl. Acad. Sci. U.S.A. 103:1388-1393(2006).
[18]
VARIANTS CMD1P HIS-9 AND LEU-9.
PubMed=22137083; DOI=10.1016/j.ahj.2011.07.028;
Medeiros A., Biagi D.G., Sobreira T.J., de Oliveira P.S., Negrao C.E.,
Mansur A.J., Krieger J.E., Brum P.C., Pereira A.C.;
"Mutations in the human phospholamban gene in patients with heart
failure.";
Am. Heart J. 162:1088-1095(2011).
[19]
CHARACTERIZATION OF VARIANTS CMD1P CYS-9 AND ARG-14 DEL, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=22427649; DOI=10.1074/jbc.M112.360859;
Ceholski D.K., Trieber C.A., Young H.S.;
"Hydrophobic imbalance in the cytoplasmic domain of phospholamban is a
determinant for lethal dilated cardiomyopathy.";
J. Biol. Chem. 287:16521-16529(2012).
-!- FUNCTION: Reversibly inhibits the activity of ATP2A2 in cardiac
sarcoplasmic reticulum by decreasing the apparent affinity of the
ATPase for Ca(2+). Modulates the contractility of the heart muscle
in response to physiological stimuli via its effects on ATP2A2.
Modulates calcium re-uptake during muscle relaxation and plays an
important role in calcium homeostasis in the heart muscle. The
degree of ATP2A2 inhibition depends on the oligomeric state of
PLN. ATP2A2 inhibition is alleviated by PLN phosphorylation.
{ECO:0000269|PubMed:22427649, ECO:0000269|PubMed:22707725}.
-!- SUBUNIT: Homopentamer (PubMed:16043693, PubMed:16897780).
Interacts with HAX1 and ATP2A2 (PubMed:17241641).
{ECO:0000269|PubMed:16043693, ECO:0000269|PubMed:16897780,
ECO:0000269|PubMed:17241641}.
-!- INTERACTION:
Q9BXK5:BCL2L13; NbExp=5; IntAct=EBI-692836, EBI-747430;
O43889-2:CREB3; NbExp=3; IntAct=EBI-692836, EBI-625022;
Q96BA8:CREB3L1; NbExp=3; IntAct=EBI-692836, EBI-6942903;
Q09013:DMPK; NbExp=4; IntAct=EBI-692836, EBI-692774;
Q92838:EDA; NbExp=8; IntAct=EBI-692836, EBI-529425;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:17241641}; Single-pass membrane protein
{ECO:0000255}. Sarcoplasmic reticulum membrane
{ECO:0000269|PubMed:15598648, ECO:0000269|PubMed:22427649};
Single-pass membrane protein {ECO:0000255}. Mitochondrion membrane
{ECO:0000250|UniProtKB:A4IFH6}; Single-pass membrane protein
{ECO:0000255}. Membrane {ECO:0000250|UniProtKB:P61014}; Single-
pass membrane protein {ECO:0000255}. Note=Colocalizes with HAX1 at
the endoplasmic reticulum (PubMed:17241641). Colocalizes with DMPK
a the sarcoplasmic reticulum (PubMed:15598648).
{ECO:0000269|PubMed:15598648, ECO:0000269|PubMed:17241641}.
-!- TISSUE SPECIFICITY: Heart muscle (at protein level).
{ECO:0000269|PubMed:17241641}.
-!- PTM: Phosphorylation by PKA abolishes the inhibition of ATP2A2-
mediated calcium uptake. Phosphorylated at Thr-17 by CaMK2, and in
response to beta-adrenergic stimulation. Phosphorylation by DMPK
may stimulate sarcoplasmic reticulum calcium uptake in
cardiomyocytes. {ECO:0000269|PubMed:15598648,
ECO:0000269|PubMed:16690701, ECO:0000269|PubMed:22707725}.
-!- DISEASE: Cardiomyopathy, dilated 1P (CMD1P) [MIM:609909]: A
disorder characterized by ventricular dilation and impaired
systolic function, resulting in congestive heart failure and
arrhythmia. Patients are at risk of premature death.
{ECO:0000269|PubMed:12610310, ECO:0000269|PubMed:16432188,
ECO:0000269|PubMed:22137083, ECO:0000269|PubMed:22427649,
ECO:0000269|PubMed:22707725}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cardiomyopathy, familial hypertrophic 18 (CMH18)
[MIM:613874]: A hereditary heart disorder characterized by
ventricular hypertrophy, which is usually asymmetric and often
involves the interventricular septum. The symptoms include
dyspnea, syncope, collapse, palpitations, and chest pain. They can
be readily provoked by exercise. The disorder has inter- and
intrafamilial variability ranging from benign to malignant forms
with high risk of cardiac failure and sudden cardiac death.
{ECO:0000269|PubMed:12705874}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: For practical reasons, PLN activity is most often
studied with ATP2A1 instead of ATP2A2.
-!- SIMILARITY: Belongs to the phospholamban family. {ECO:0000305}.
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EMBL; M63603; AAA60083.1; -; mRNA.
EMBL; M60411; AAA60109.1; -; mRNA.
EMBL; AF177764; AAD55950.1; -; Genomic_DNA.
EMBL; BC005269; AAH05269.1; -; mRNA.
CCDS; CCDS5120.1; -.
PIR; A40424; A40424.
RefSeq; NP_002658.1; NM_002667.4.
UniGene; Hs.170839; -.
UniGene; Hs.745010; -.
PDB; 1K9N; Model; -; A/B/C/D/E=35-52.
PDB; 1KCH; Model; -; A/B/C/D/E=35-52.
PDB; 1PLN; Model; -; A/B/C/D/E=35-52.
PDB; 1PLP; NMR; -; A=1-24.
PDB; 1PSL; Model; -; A/B/C/D/E=1-52.
PDB; 1ZLL; NMR; -; A/B/C/D/E=1-52.
PDB; 2HYN; NMR; -; A/B/C/D/E=1-52.
PDBsum; 1K9N; -.
PDBsum; 1KCH; -.
PDBsum; 1PLN; -.
PDBsum; 1PLP; -.
PDBsum; 1PSL; -.
PDBsum; 1ZLL; -.
PDBsum; 2HYN; -.
ProteinModelPortal; P26678; -.
SMR; P26678; -.
BioGrid; 111365; 8.
CORUM; P26678; -.
DIP; DIP-33582N; -.
ELM; P26678; -.
IntAct; P26678; 24.
STRING; 9606.ENSP00000350132; -.
TCDB; 1.A.50.1.1; the phospholamban (ca(2+)-channel and ca(2+)-atpase regulator) (plb) family.
iPTMnet; P26678; -.
PhosphoSitePlus; P26678; -.
BioMuta; PLN; -.
DMDM; 130774; -.
PaxDb; P26678; -.
PeptideAtlas; P26678; -.
PRIDE; P26678; -.
TopDownProteomics; P26678; -.
DNASU; 5350; -.
Ensembl; ENST00000357525; ENSP00000350132; ENSG00000198523.
GeneID; 5350; -.
KEGG; hsa:5350; -.
CTD; 5350; -.
DisGeNET; 5350; -.
EuPathDB; HostDB:ENSG00000198523.5; -.
GeneCards; PLN; -.
GeneReviews; PLN; -.
HGNC; HGNC:9080; PLN.
HPA; CAB005597; -.
HPA; HPA026900; -.
MalaCards; PLN; -.
MIM; 172405; gene.
MIM; 609909; phenotype.
MIM; 613874; phenotype.
neXtProt; NX_P26678; -.
OpenTargets; ENSG00000198523; -.
Orphanet; 154; Familial isolated dilated cardiomyopathy.
Orphanet; 155; Familial isolated hypertrophic cardiomyopathy.
PharmGKB; PA272; -.
eggNOG; ENOG410J7H0; Eukaryota.
eggNOG; ENOG4111BFT; LUCA.
GeneTree; ENSGT00390000002403; -.
HOGENOM; HOG000115660; -.
HOVERGEN; HBG108280; -.
InParanoid; P26678; -.
KO; K05852; -.
OMA; MERVQHM; -.
PhylomeDB; P26678; -.
TreeFam; TF330750; -.
Reactome; R-HSA-5578775; Ion homeostasis.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
SIGNOR; P26678; -.
EvolutionaryTrace; P26678; -.
GeneWiki; Phospholamban; -.
GenomeRNAi; 5350; -.
PRO; PR:P26678; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000198523; -.
CleanEx; HS_PLN; -.
ExpressionAtlas; P26678; baseline and differential.
Genevisible; P26678; HS.
GO; GO:0090534; C:calcium ion-transporting ATPase complex; IDA:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0031982; C:vesicle; IEA:Ensembl.
GO; GO:0051117; F:ATPase binding; ISS:BHF-UCL.
GO; GO:0042030; F:ATPase inhibitor activity; IDA:BHF-UCL.
GO; GO:0005246; F:calcium channel regulator activity; IEA:InterPro.
GO; GO:0004857; F:enzyme inhibitor activity; ISS:BHF-UCL.
GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL.
GO; GO:0086023; P:adrenergic receptor signaling pathway involved in heart process; IEA:Ensembl.
GO; GO:0008015; P:blood circulation; NAS:ProtInc.
GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
GO; GO:0048738; P:cardiac muscle tissue development; IEA:Ensembl.
GO; GO:0032780; P:negative regulation of ATPase activity; IDA:BHF-UCL.
GO; GO:1901877; P:negative regulation of calcium ion binding; IDA:BHF-UCL.
GO; GO:0090281; P:negative regulation of calcium ion import; ISS:BHF-UCL.
GO; GO:1902081; P:negative regulation of calcium ion import into sarcoplasmic reticulum; ISS:BHF-UCL.
GO; GO:1901020; P:negative regulation of calcium ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0051926; P:negative regulation of calcium ion transport; IDA:BHF-UCL.
GO; GO:1901895; P:negative regulation of calcium-transporting ATPase activity; IDA:BHF-UCL.
GO; GO:0043086; P:negative regulation of catalytic activity; ISS:BHF-UCL.
GO; GO:0010459; P:negative regulation of heart rate; IMP:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0051924; P:regulation of calcium ion transport; IDA:UniProtKB.
GO; GO:1901894; P:regulation of calcium-transporting ATPase activity; IDA:UniProtKB.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IC:BHF-UCL.
GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; IC:BHF-UCL.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IEA:Ensembl.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IC:BHF-UCL.
GO; GO:0008016; P:regulation of heart contraction; IMP:BHF-UCL.
GO; GO:1901897; P:regulation of relaxation of cardiac muscle; IC:BHF-UCL.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IEA:Ensembl.
GO; GO:0002026; P:regulation of the force of heart contraction; IC:BHF-UCL.
GO; GO:0086092; P:regulation of the force of heart contraction by cardiac conduction; IEA:Ensembl.
GO; GO:0055119; P:relaxation of cardiac muscle; TAS:BHF-UCL.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
InterPro; IPR005984; PLB.
PANTHER; PTHR21194; PTHR21194; 1.
Pfam; PF04272; Phospholamban; 1.
PIRSF; PIRSF001665; PLB; 1.
ProDom; PD014689; P_lamban; 1.
TIGRFAMs; TIGR01294; P_lamban; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cardiomyopathy; Complete proteome;
Disease mutation; Endoplasmic reticulum; Membrane; Mitochondrion;
Phosphoprotein; Reference proteome; Sarcoplasmic reticulum;
Transmembrane; Transmembrane helix.
CHAIN 1 52 Cardiac phospholamban.
/FTId=PRO_0000191244.
TOPO_DOM 1 31 Cytoplasmic. {ECO:0000305}.
TRANSMEM 32 52 Helical. {ECO:0000305}.
REGION 16 22 Involved in HAX1 binding.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:A4IFH6}.
MOD_RES 16 16 Phosphoserine; by PKA and DMPK.
{ECO:0000269|PubMed:15598648,
ECO:0000269|PubMed:22707725}.
MOD_RES 17 17 Phosphothreonine; by CaMK2.
{ECO:0000269|PubMed:16690701}.
VARIANT 9 9 R -> C (in CMD1P; impairs phosphorylation
by PKA and inhibition of ATP2A1-mediated
calcium uptake; dbSNP:rs111033559).
{ECO:0000269|PubMed:12610310,
ECO:0000269|PubMed:22427649,
ECO:0000269|PubMed:22707725}.
/FTId=VAR_025989.
VARIANT 9 9 R -> H (in CMD1P; impairs phosphorylation
by PKA and inhibition of ATP2A1-mediated
calcium uptake; dbSNP:rs754782171).
{ECO:0000269|PubMed:22137083,
ECO:0000269|PubMed:22707725}.
/FTId=VAR_072925.
VARIANT 9 9 R -> L (in CMD1P; impairs phosphorylation
by PKA and inhibition of ATP2A1-mediated
calcium uptake).
{ECO:0000269|PubMed:22137083,
ECO:0000269|PubMed:22707725}.
/FTId=VAR_072926.
VARIANT 14 14 Missing (in CMD1P; impairs
phosphorylation by PKA, destabilizes the
homopentamer and mildly reduces
inhibition of ATP2A1-mediated calcium
uptake). {ECO:0000269|PubMed:16432188,
ECO:0000269|PubMed:22427649,
ECO:0000269|PubMed:22707725}.
/FTId=VAR_025990.
MUTAGEN 13 13 R->A: Abolishes phosphorylation by PKA.
{ECO:0000269|PubMed:22707725}.
MUTAGEN 14 14 R->A: Abolishes phosphorylation by PKA.
{ECO:0000269|PubMed:22707725}.
MUTAGEN 16 16 S->A: Abolishes phosphorylation by PKA.
{ECO:0000269|PubMed:22707725}.
MUTAGEN 17 17 T->A: No effect on phosphorylation by
PKA. {ECO:0000269|PubMed:22707725}.
HELIX 4 14 {ECO:0000244|PDB:1PLP}.
STRAND 18 20 {ECO:0000244|PDB:1PLP}.
HELIX 23 50 {ECO:0000244|PDB:1ZLL}.
SEQUENCE 52 AA; 6109 MW; 0766304A76A854D3 CRC64;
MEKVQYLTRS AIRRASTIEM PQQARQKLQN LFINFCLILI CLLLICIIVM LL


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