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P61015 (PPLA_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

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

General annotation (Comments)

Function

Phospholamban has been postulated to regulate the activity of the calcium pump of cardiac sarcoplasmic reticulum.

Subunit structure

Homopentamer. Interacts with HAX1 By similarity.

Subcellular location

Mitochondrion membrane; Single-pass membrane protein. Sarcoplasmic reticulum By similarity.

Tissue specificity

Heart.

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.

Sequence similarities

Belongs to the phospholamban family.

Ontologies

Keywords
   Cellular componentMembrane
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 electronic annotation. Source: Compara

calcium ion transport

Inferred from electronic annotation. Source: InterPro

cardiac muscle tissue development

Inferred from electronic annotation. Source: Compara

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Compara

negative regulation of calcium ion binding

Inferred from direct assay PubMed 12032137PubMed 16432188. Source: BHF-UCL

negative regulation of calcium ion import

Inferred from direct assay PubMed 12032137. Source: BHF-UCL

negative regulation of calcium ion transmembrane transporter activity

Inferred from direct assay PubMed 12032137. Source: BHF-UCL

negative regulation of heart contraction

Inferred from electronic annotation. Source: Compara

regulation of cardiac muscle cell contraction

Inferred from electronic annotation. Source: Compara

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

Inferred from electronic annotation. Source: Compara

regulation of relaxation of muscle

Inferred from electronic annotation. Source: Compara

regulation of ryanodine-sensitive calcium-release channel activity

Inferred from electronic annotation. Source: Compara

regulation of the force of heart contraction by cardiac conduction

Inferred from electronic annotation. Source: Compara

   Cellular_componentendoplasmic reticulum

Inferred from direct assay PubMed 16432188. Source: BHF-UCL

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from direct assay PubMed 16432188. Source: BHF-UCL

sarcoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATPase binding

Inferred from direct assay PubMed 12032137. Source: BHF-UCL

ATPase inhibitor activity

Inferred by curator PubMed 16432188. Source: BHF-UCL

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_0000191247

Regions

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

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue161Phosphoserine; by PKA and DMPK By similarity
Modified residue171Phosphothreonine; by CaMK2 By similarity

Secondary structure

..... 52
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61015 [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

[1]"Structure of the rabbit phospholamban gene, cloning of the human cDNA, and assignment of the gene to human chromosome 6."
Fujii J., Zarain-Herzberg A., Willard H.F., Tada M., Maclennan D.H.
J. Biol. Chem. 266:11669-11675(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Rabbit cardiac and slow-twitch muscle express the same phospholamban gene."
Fujii J., Lytton J., Tada M., Maclennan D.H.
FEBS Lett. 227:51-55(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles."
Zamoon J., Mascioni A., Thomas D.D., Veglia G.
Biophys. J. 85:2589-2598(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[4]"Phospholamban pentamer quaternary conformation determined by in-gel fluorescence anisotropy."
Robia S.L., Flohr N.C., Thomas D.D.
Biochemistry 44:4302-4311(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63600 Genomic DNA. No translation available.
M63601 Genomic DNA. Translation: AAA31445.1.
Y00761 mRNA. Translation: CAA68730.1.
PIRB40424.
RefSeqNP_001076090.1. NM_001082621.1.
UniGeneOcu.3266.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N7LNMR-A1-52[»]
1XNUmodel-A/B/C/D/E1-52[»]
2LPFNMR-A1-52[»]
ProteinModelPortalP61015.
SMRP61015. Positions 1-52.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-31022N.
IntActP61015. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009299.

Organism-specific databases

CTD5350.

Phylogenomic databases

eggNOGNOG44917.
HOVERGENHBG049447.
OMAQHMTRSA.

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

EvolutionaryTraceP61015.
NextBio295180.

Entry information

Entry namePPLA_RABIT
AccessionPrimary (citable) accession number: P61015
Secondary accession number(s): P20006
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families