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PPLA_BOVIN
ID   PPLA_BOVIN              Reviewed;          52 AA.
AC   A4IFH6;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Cardiac phospholamban;
DE            Short=PLB;
GN   Name=PLN;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SUBCELLULAR LOCATION, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
RX   PubMed=17060615; DOI=10.1073/pnas.0607719103;
RA   Carroll J., Fearnley I.M., Walker J.E.;
RT   "Definition of the mitochondrial proteome by measurement of molecular
RT   masses of membrane proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:16170-16175(2006).
CC   -!- FUNCTION: Reversibly inhibits the activity of ATP2A2 in cardiac
CC       sarcoplasmic reticulum by decreasing the apparent affinity of the
CC       ATPase for Ca(2+). Modulates the contractility of the heart muscle in
CC       response to physiological stimuli via its effects on ATP2A2. Modulates
CC       calcium re-uptake during muscle relaxation and plays an important role
CC       in calcium homeostasis in the heart muscle. The degree of ATP2A2
CC       inhibition depends on the oligomeric state of PLN. ATP2A2 inhibition is
CC       alleviated by PLN phosphorylation (By similarity).
CC       {ECO:0000250|UniProtKB:P26678}.
CC   -!- SUBUNIT: Homopentamer. Interacts with HAX1. Interact with ATP2A2; the
CC       inhibition decreases ATP2A2 Ca(2+) affinity. Interacts with VMP1; VMP1
CC       competes with PLN and SLN to prevent them from forming an inhibitory
CC       complex with ATP2A2. Interacts with S100A1 in a Ca(2+)-dependent
CC       manner. {ECO:0000250|UniProtKB:P26678}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P26678}; Single-pass membrane protein
CC       {ECO:0000255}. Sarcoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P26678}; Single-pass membrane protein
CC       {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:17060615};
CC       Single-pass membrane protein {ECO:0000255}. Membrane
CC       {ECO:0000250|UniProtKB:P61014}; Single-pass membrane protein
CC       {ECO:0000255}. Note=Colocalizes with HAX1 at the endoplasmic reticulum.
CC       Colocalizes with DMPK a the sarcoplasmic reticulum.
CC       {ECO:0000250|UniProtKB:P26678}.
CC   -!- PTM: Phosphorylation by PKA abolishes the inhibition of ATP2A2-mediated
CC       calcium uptake. Phosphorylated at Thr-17 by CaMK2, and in response to
CC       beta-adrenergic stimulation. Phosphorylation by DMPK may stimulate
CC       sarcoplasmic reticulum calcium uptake in cardiomyocytes (By
CC       similarity). {ECO:0000250|UniProtKB:P26678}.
CC   -!- PTM: Palmitoylated by ZDHHC16, promoting formation of the homopentamer.
CC       {ECO:0000250|UniProtKB:P61014}.
CC   -!- MASS SPECTROMETRY: Mass=6122.7; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17060615};
CC   -!- SIMILARITY: Belongs to the phospholamban family. {ECO:0000305}.
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DR   EMBL; BC134584; AAI34585.1; -; mRNA.
DR   RefSeq; NP_001096789.1; NM_001103319.1.
DR   AlphaFoldDB; A4IFH6; -.
DR   SMR; A4IFH6; -.
DR   CORUM; A4IFH6; -.
DR   STRING; 9913.ENSBTAP00000017182; -.
DR   iPTMnet; A4IFH6; -.
DR   PaxDb; A4IFH6; -.
DR   GeneID; 100125240; -.
DR   KEGG; bta:100125240; -.
DR   CTD; 5350; -.
DR   eggNOG; ENOG502S97F; Eukaryota.
DR   InParanoid; A4IFH6; -.
DR   OrthoDB; 1643351at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0042030; F:ATPase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:1901895; P:negative regulation of ATPase-coupled calcium transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:1902081; P:negative regulation of calcium ion import into sarcoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0010459; P:negative regulation of heart rate; IBA:GO_Central.
DR   CDD; cd20250; Phospholamban; 1.
DR   InterPro; IPR005984; PLB.
DR   PANTHER; PTHR21194; PTHR21194; 1.
DR   Pfam; PF04272; Phospholamban; 1.
DR   PIRSF; PIRSF001665; PLB; 1.
DR   TIGRFAMs; TIGR01294; P_lamban; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Endoplasmic reticulum; Lipoprotein; Membrane; Mitochondrion;
KW   Palmitate; Phosphoprotein; Reference proteome; Sarcoplasmic reticulum;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..52
FT                   /note="Cardiac phospholamban"
FT                   /id="PRO_0000353186"
FT   TOPO_DOM        1..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:17060615"
FT   MOD_RES         16
FT                   /note="Phosphoserine; by PKA and DMPK"
FT                   /evidence="ECO:0000250|UniProtKB:P61012"
FT   MOD_RES         17
FT                   /note="Phosphothreonine; by CaMK2"
FT                   /evidence="ECO:0000250|UniProtKB:P61012"
FT   LIPID           36
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P61014"
SQ   SEQUENCE   52 AA;  6054 MW;  076361D9ADDC87D3 CRC64;
     MDKVQYLTRS AIRRASTIEM PQQARQNLQN LFINFCLISI CLLLICIIVM LL
 
 
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