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P61014 (PPLA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cardiac phospholamban

Short name=PLB
Gene names
Name:Pln
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length52 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca2+. 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. Ref.4

Subunit structure

Homopentamer. Interacts with HAX1 and ATP2A2 By similarity.

Subcellular location

Sarcoplasmic reticulum membrane; Single-pass membrane protein By similarity. Mitochondrion membrane; Single-pass membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass membrane protein By similarity. Membrane; Single-pass membrane protein Ref.5.

Post-translational modification

Phosphorylated at Thr-17 by CaMK2, and in response to beta-adrenergic stimulation. Phosphorylation by DMPK may stimulate sarcoplasmic reticulum calcium uptake in cardiomyocytes By similarity. Phosphorylation by PKA abolishes the inhibition of ATP2A2-mediated calcium uptake. Ref.4 Ref.5

Sequence similarities

Belongs to the phospholamban family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Mitochondrion
Sarcoplasmic reticulum
   DomainTransmembrane
Transmembrane helix
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadrenergic receptor signaling pathway involved in heart process

Inferred from mutant phenotype PubMed 10471356. Source: MGI

calcium ion transport

Inferred from electronic annotation. Source: Ensembl

cardiac muscle tissue development

Inferred from genetic interaction PubMed 10555147. Source: MGI

cellular calcium ion homeostasis

Inferred from genetic interaction PubMed 10555147. Source: MGI

negative regulation of calcium ion transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of calcium-transporting ATPase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of heart contraction

Inferred from mutant phenotype PubMed 8062415. Source: MGI

negative regulation of heart rate

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of calcium ion import

Inferred from mutant phenotype PubMed 8620604. Source: MGI

regulation of calcium ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cardiac muscle cell contraction

Inferred from mutant phenotype PubMed 8620604. Source: MGI

regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion

Inferred from mutant phenotype PubMed 8831698. Source: MGI

regulation of heart contraction

Inferred from mutant phenotype PubMed 8831698. Source: MGI

regulation of relaxation of muscle

Inferred from mutant phenotype PubMed 10024311. Source: MGI

regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Inferred from mutant phenotype PubMed 9118481. Source: MGI

regulation of ryanodine-sensitive calcium-release channel activity

Inferred from mutant phenotype PubMed 10603936. Source: MGI

regulation of the force of heart contraction

Inferred from mutant phenotype PubMed 9118481. Source: MGI

regulation of the force of heart contraction by cardiac conduction

Inferred from mutant phenotype PubMed 10644605. Source: MGI

response to testosterone

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcalcium ion-transporting ATPase complex

Inferred from electronic annotation. Source: Ensembl

mitochondrial membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

sarcoplasmic reticulum

Inferred from direct assay PubMed 9038922. Source: MGI

sarcoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATPase inhibitor activity

Inferred from electronic annotation. Source: Ensembl

calcium channel regulator activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5252Cardiac phospholamban
PRO_0000191245

Regions

Topological domain1 – 3131Cytoplasmic Potential
Transmembrane32 – 5221Helical; Potential

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue161Phosphoserine; by DMPK; alternate By similarity
Modified residue161Phosphoserine; by PKA; alternate Ref.4 Ref.5
Modified residue171Phosphothreonine; by CaMK2 By similarity

Experimental info

Mutagenesis20 – 223MPQ → GGG: No effect on inhibition of ATP2A1-mediated calcium uptake. Ref.4
Mutagenesis20 – 212MP → GG: Nearly abolishes inhibition of ATP2A1-mediated calcium uptake. Ref.4
Mutagenesis211P → G: Reduces inhibition of ATP2A1-mediated calcium uptake. Ref.4
Mutagenesis221Q → G: Strongly reduces inhibition of ATP2A1-mediated calcium uptake. Ref.4

Secondary structure

... 52
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61014 [UniParc].

Last modified April 26, 2004. Version 1.
Checksum: 0763601F76A854D3

FASTA526,095
        10         20         30         40         50 
MEKVQYLTRS AIRRASTIEM PQQARQNLQN LFINFCLILI CLLLICIIVM LL 

« Hide

References

« Hide 'large scale' references
[1]"Mouse phospholamban gene expression during development in vivo and in vitro."
Ganim J.R., Luo W., Ponniah S., Grupp I., Kim H.W., Ferguson D.G., Kadambi V., Neumann J.C., Doetschman T., Kranias E.G.
Circ. Res. 71:1021-1030(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Aorta, Heart and Kidney.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]"Tuning the structural coupling between the transmembrane and cytoplasmic domains of phospholamban to control sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) function."
Ha K.N., Gustavsson M., Veglia G.
J. Muscle Res. Cell Motil. 33:485-492(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 20-MET--GLN-22; PRO-21 AND GLN-22.
[5]"Dynamics connect substrate recognition to catalysis in protein kinase A."
Masterson L.R., Cheng C., Yu T., Tonelli M., Kornev A., Taylor S.S., Veglia G.
Nat. Chem. Biol. 6:821-828(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4-18 IN COMPLEX WITH PRKACA, PHOSPHORYLATION AT SER-16, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S46792 mRNA. Translation: AAB23706.1.
AK002622 mRNA. Translation: BAB22237.1.
AK040718 mRNA. Translation: BAC30680.1.
AK052199 mRNA. Translation: BAC34880.1.
AK142708 mRNA. Translation: BAE25168.1.
BC061097 mRNA. Translation: AAH61097.1.
PIRA49057.
RefSeqNP_001135399.1. NM_001141927.1.
NP_075618.1. NM_023129.5.
UniGeneMm.34145.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3O7LX-ray2.80I4-18[»]
ProteinModelPortalP61014.
SMRP61014. Positions 1-52.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202252. 1 interaction.
STRING10090.ENSMUSP00000045709.

PTM databases

PhosphoSiteP61014.

Proteomic databases

PaxDbP61014.
PRIDEP61014.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000046221; ENSMUSP00000045709; ENSMUSG00000038583.
ENSMUST00000163319; ENSMUSP00000132743; ENSMUSG00000038583.
GeneID18821.
KEGGmmu:18821.
UCSCuc007fbo.2. mouse.

Organism-specific databases

CTD5350.
MGIMGI:97622. Pln.

Phylogenomic databases

eggNOGNOG44917.
GeneTreeENSGT00390000002403.
HOGENOMHOG000115660.
HOVERGENHBG049447.
InParanoidP61014.
KOK05852.
OMAQHMTRSA.
TreeFamTF330750.

Gene expression databases

BgeeP61014.
CleanExMM_PLN.
GenevestigatorP61014.

Family and domain databases

InterProIPR005984. P_lamban.
[Graphical view]
PANTHERPTHR21194. PTHR21194. 1 hit.
PfamPF04272. Phospholamban. 1 hit.
[Graphical view]
PIRSFPIRSF001665. PLB. 1 hit.
ProDomPD014689. P_lamban. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01294. P_lamban. 1 hit.
ProtoNetSearch...

Other

NextBio295180.
PROP61014.
SOURCESearch...

Entry information

Entry namePPLA_MOUSE
AccessionPrimary (citable) accession number: P61014
Secondary accession number(s): P20006, Q3UQ75
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: April 16, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot