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P61014

- PPLA_MOUSE

UniProt

P61014 - PPLA_MOUSE

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Protein

Cardiac phospholamban

Gene

Pln

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. ATPase inhibitor activity Source: Ensembl
  2. calcium channel regulator activity Source: InterPro

GO - Biological processi

  1. adrenergic receptor signaling pathway involved in heart process Source: MGI
  2. calcium ion transport Source: Ensembl
  3. cardiac muscle tissue development Source: MGI
  4. cellular calcium ion homeostasis Source: MGI
  5. negative regulation of calcium ion transport Source: Ensembl
  6. negative regulation of calcium-transporting ATPase activity Source: Ensembl
  7. negative regulation of heart contraction Source: MGI
  8. negative regulation of heart rate Source: Ensembl
  9. protein homooligomerization Source: Ensembl
  10. regulation of calcium ion import Source: MGI
  11. regulation of calcium ion transport Source: UniProtKB
  12. regulation of cardiac muscle cell contraction Source: MGI
  13. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: MGI
  14. regulation of heart contraction Source: MGI
  15. regulation of relaxation of muscle Source: MGI
  16. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: MGI
  17. regulation of ryanodine-sensitive calcium-release channel activity Source: MGI
  18. regulation of the force of heart contraction Source: MGI
  19. regulation of the force of heart contraction by cardiac conduction Source: MGI
  20. response to testosterone Source: Ensembl
  21. response to zinc ion Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Cardiac phospholamban
Short name:
PLB
Gene namesi
Name:Pln
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:97622. Pln.

Subcellular locationi

Sarcoplasmic reticulum membrane By similarity; Single-pass membrane protein By similarity. Mitochondrion membrane By similarity; Single-pass membrane protein By similarity. Endoplasmic reticulum membrane By similarity; Single-pass membrane protein By similarity. Membrane 1 Publication; Single-pass membrane protein 1 Publication

GO - Cellular componenti

  1. calcium ion-transporting ATPase complex Source: Ensembl
  2. mitochondrion Source: UniProtKB-KW
  3. sarcoplasmic reticulum Source: MGI
  4. vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Sarcoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 223MPQ → GGG: No effect on inhibition of ATP2A1-mediated calcium uptake. 1 Publication
Mutagenesisi20 – 212MP → GG: Nearly abolishes inhibition of ATP2A1-mediated calcium uptake.
Mutagenesisi21 – 211P → G: Reduces inhibition of ATP2A1-mediated calcium uptake. 1 Publication
Mutagenesisi22 – 221Q → G: Strongly reduces inhibition of ATP2A1-mediated calcium uptake. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5252Cardiac phospholambanPRO_0000191245Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei16 – 161Phosphoserine; by DMPK; alternateBy similarity
Modified residuei16 – 161Phosphoserine; by PKA; alternate2 Publications
Modified residuei17 – 171Phosphothreonine; by CaMK2By similarity

Post-translational modificationi

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.By similarity2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP61014.
PRIDEiP61014.

PTM databases

PhosphoSiteiP61014.

Expressioni

Gene expression databases

BgeeiP61014.
CleanExiMM_PLN.
GenevestigatoriP61014.

Interactioni

Subunit structurei

Homopentamer. Interacts with HAX1 and ATP2A2 By similarity.By similarity

Protein-protein interaction databases

BioGridi202252. 1 interaction.
STRINGi10090.ENSMUSP00000045709.

Structurei

Secondary structure

1
52
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni9 – 113Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3O7LX-ray2.80I4-18[»]
ProteinModelPortaliP61014.
SMRiP61014. Positions 1-52.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3131CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei32 – 5221HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholamban family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG44917.
GeneTreeiENSGT00390000002403.
HOGENOMiHOG000115660.
HOVERGENiHBG049447.
InParanoidiP61014.
KOiK05852.
OMAiQHARQNL.
TreeFamiTF330750.

Family and domain databases

InterProiIPR005984. P_lamban.
[Graphical view]
PANTHERiPTHR21194. PTHR21194. 1 hit.
PfamiPF04272. Phospholamban. 1 hit.
[Graphical view]
PIRSFiPIRSF001665. PLB. 1 hit.
ProDomiPD014689. P_lamban. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR01294. P_lamban. 1 hit.

Sequencei

Sequence statusi: Complete.

P61014-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEKVQYLTRS AIRRASTIEM PQQARQNLQN LFINFCLILI CLLLICIIVM

LL
Length:52
Mass (Da):6,095
Last modified:April 26, 2004 - v1
Checksum:i0763601F76A854D3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS35899.1.
PIRiA49057.
RefSeqiNP_001135399.1. NM_001141927.1.
NP_075618.1. NM_023129.5.
UniGeneiMm.34145.

Genome annotation databases

EnsembliENSMUST00000046221; ENSMUSP00000045709; ENSMUSG00000038583.
ENSMUST00000163319; ENSMUSP00000132743; ENSMUSG00000038583.
GeneIDi18821.
KEGGimmu:18821.
UCSCiuc007fbo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS35899.1.
PIRi A49057.
RefSeqi NP_001135399.1. NM_001141927.1.
NP_075618.1. NM_023129.5.
UniGenei Mm.34145.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3O7L X-ray 2.80 I 4-18 [» ]
ProteinModelPortali P61014.
SMRi P61014. Positions 1-52.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202252. 1 interaction.
STRINGi 10090.ENSMUSP00000045709.

PTM databases

PhosphoSitei P61014.

Proteomic databases

PaxDbi P61014.
PRIDEi P61014.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000046221 ; ENSMUSP00000045709 ; ENSMUSG00000038583 .
ENSMUST00000163319 ; ENSMUSP00000132743 ; ENSMUSG00000038583 .
GeneIDi 18821.
KEGGi mmu:18821.
UCSCi uc007fbo.2. mouse.

Organism-specific databases

CTDi 5350.
MGIi MGI:97622. Pln.

Phylogenomic databases

eggNOGi NOG44917.
GeneTreei ENSGT00390000002403.
HOGENOMi HOG000115660.
HOVERGENi HBG049447.
InParanoidi P61014.
KOi K05852.
OMAi QHARQNL.
TreeFami TF330750.

Miscellaneous databases

NextBioi 295180.
PROi P61014.
SOURCEi Search...

Gene expression databases

Bgeei P61014.
CleanExi MM_PLN.
Genevestigatori P61014.

Family and domain databases

InterProi IPR005984. P_lamban.
[Graphical view ]
PANTHERi PTHR21194. PTHR21194. 1 hit.
Pfami PF04272. Phospholamban. 1 hit.
[Graphical view ]
PIRSFi PIRSF001665. PLB. 1 hit.
ProDomi PD014689. P_lamban. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
TIGRFAMsi TIGR01294. P_lamban. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPPLA_MOUSE
AccessioniPrimary (citable) accession number: P61014
Secondary accession number(s): P20006, Q3UQ75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: October 29, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3