ID   PPLA_MOUSE              Reviewed;          52 AA.
AC   P61014; P20006; Q3UQ75;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 1.
DT   24-JAN-2024, entry version 157.
DE   RecName: Full=Cardiac phospholamban {ECO:0000305};
DE            Short=PLB;
GN   Name=Pln {ECO:0000312|MGI:MGI:97622};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=1394867; DOI=10.1161/01.res.71.5.1021;
RA   Ganim J.R., Luo W., Ponniah S., Grupp I., Kim H.W., Ferguson D.G.,
RA   Kadambi V., Neumann J.C., Doetschman T., Kranias E.G.;
RT   "Mouse phospholamban gene expression during development in vivo and in
RT   vitro.";
RL   Circ. Res. 71:1021-1030(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Aorta, Heart, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   FUNCTION, PHOSPHORYLATION AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY,
RP   AND MUTAGENESIS OF 20-MET--GLN-22; PRO-21 AND GLN-22.
RX   PubMed=22971924; DOI=10.1007/s10974-012-9319-4;
RA   Ha K.N., Gustavsson M., Veglia G.;
RT   "Tuning the structural coupling between the transmembrane and cytoplasmic
RT   domains of phospholamban to control sarcoplasmic reticulum Ca(2+)-ATPase
RT   (SERCA) function.";
RL   J. Muscle Res. Cell Motil. 33:485-492(2012).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4-18 IN COMPLEX WITH PRKACA,
RP   PHOSPHORYLATION AT SER-16, AND SUBCELLULAR LOCATION.
RX   PubMed=20890288; DOI=10.1038/nchembio.452;
RA   Masterson L.R., Cheng C., Yu T., Tonelli M., Kornev A., Taylor S.S.,
RA   Veglia G.;
RT   "Dynamics connect substrate recognition to catalysis in protein kinase A.";
RL   Nat. Chem. Biol. 6:821-828(2010).
RN   [7]
RP   PALMITOYLATION AT CYS-36, PHOSPHORYLATION AT SER-16, SUBUNIT, AND
RP   MUTAGENESIS OF CYS-36; CYS-41 AND CYS-46.
RX   PubMed=26644582; DOI=10.1073/pnas.1518368112;
RA   Zhou T., Li J., Zhao P., Liu H., Jia D., Jia H., He L., Cang Y., Boast S.,
RA   Chen Y.H., Thibault H., Scherrer-Crosbie M., Goff S.P., Li B.;
RT   "Palmitoyl acyltransferase Aph2 in cardiac function and the development of
RT   cardiomyopathy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:15666-15671(2015).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=26816378; DOI=10.1126/science.aad4076;
RA   Nelson B.R., Makarewich C.A., Anderson D.M., Winders B.R., Troupes C.D.,
RA   Wu F., Reese A.L., McAnally J.R., Chen X., Kavalali E.T., Cannon S.C.,
RA   Houser S.R., Bassel-Duby R., Olson E.N.;
RT   "Muscle physiology. A peptide encoded by a transcript annotated as long
RT   noncoding RNA enhances SERCA activity in muscle.";
RL   Science 351:271-275(2016).
RN   [9]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   32-PHE--CYS-36; 36-CYS--CYS-46 AND 42-LEU--CYS-46.
RX   PubMed=30733280; DOI=10.15252/embr.201846449;
RA   Niemeyer J., Mentrup T., Heidasch R., Mueller S.A., Biswas U., Meyer R.,
RA   Papadopoulou A.A., Dederer V., Haug-Kroeper M., Adamski V.,
RA   Luellmann-Rauch R., Bergmann M., Mayerhofer A., Saftig P., Wennemuth G.,
RA   Jessberger R., Fluhrer R., Lichtenthaler S.F., Lemberg M.K., Schroeder B.;
RT   "The intramembrane protease SPPL2c promotes male germ cell development by
RT   cleaving phospholamban.";
RL   EMBO Rep. 20:0-0(2019).
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 (PubMed:22971924, PubMed:26816378).
CC       Controls intracellular Ca(2+) levels in elongated spermatids. May play
CC       a role in germ cell differentiation (PubMed:30733280).
CC       {ECO:0000269|PubMed:22971924, ECO:0000269|PubMed:26816378,
CC       ECO:0000269|PubMed:30733280}.
CC   -!- SUBUNIT: Homopentamer (PubMed:26644582). Interacts with HAX1. Interact
CC       with ATP2A2; the inhibition decreases ATP2A2 Ca(2+) affinity. Interacts
CC       with VMP1; VMP1 competes with PLN and SLN to prevent them from forming
CC       an inhibitory complex with ATP2A2. Interacts with S100A1 in a Ca(2+)-
CC       dependent manner. {ECO:0000250|UniProtKB:P26678,
CC       ECO:0000269|PubMed:26644582}.
CC   -!- INTERACTION:
CC       P61014; P05132: Prkaca; NbExp=2; IntAct=EBI-10148373, EBI-400564;
CC       P61014; Q13557: CAMK2D; Xeno; NbExp=2; IntAct=EBI-10148373, EBI-351018;
CC       P61014; P61981: YWHAG; Xeno; NbExp=3; IntAct=EBI-10148373, EBI-359832;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:26816378, ECO:0000269|PubMed:30733280}; Single-pass
CC       membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P26678}; Single-pass membrane protein
CC       {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:A4IFH6};
CC       Single-pass membrane protein {ECO:0000255}. Membrane
CC       {ECO:0000269|PubMed:20890288}; 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   -!- TISSUE SPECIFICITY: Expressed in testis (at protein level).
CC       {ECO:0000269|PubMed:30733280}.
CC   -!- PTM: Phosphorylated at Thr-17 by CaMK2, and in response to beta-
CC       adrenergic stimulation. Phosphorylation by DMPK may stimulate
CC       sarcoplasmic reticulum calcium uptake in cardiomyocytes (By
CC       similarity). Phosphorylation by PKA abolishes the inhibition of ATP2A2-
CC       mediated calcium uptake. {ECO:0000250|UniProtKB:P26678,
CC       ECO:0000269|PubMed:20890288, ECO:0000269|PubMed:22971924}.
CC   -!- PTM: Palmitoylated by ZDHHC16, promoting formation of the homopentamer.
CC       {ECO:0000269|PubMed:26644582}.
CC   -!- PTM: In elongated spermatids, proteolytically cleaved by SPPL2C which
CC       modulates intracellular Ca(2+) homeostasis.
CC       {ECO:0000269|PubMed:1394867}.
CC   -!- SIMILARITY: Belongs to the phospholamban family. {ECO:0000305}.
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DR   EMBL; S46792; AAB23706.1; -; mRNA.
DR   EMBL; AK002622; BAB22237.1; -; mRNA.
DR   EMBL; AK040718; BAC30680.1; -; mRNA.
DR   EMBL; AK052199; BAC34880.1; -; mRNA.
DR   EMBL; AK142708; BAE25168.1; -; mRNA.
DR   EMBL; BC061097; AAH61097.1; -; mRNA.
DR   CCDS; CCDS35899.1; -.
DR   PIR; A49057; A49057.
DR   RefSeq; NP_001135399.1; NM_001141927.1.
DR   RefSeq; NP_075618.1; NM_023129.5.
DR   PDB; 3O7L; X-ray; 2.80 A; I=4-18.
DR   PDBsum; 3O7L; -.
DR   AlphaFoldDB; P61014; -.
DR   BMRB; P61014; -.
DR   SMR; P61014; -.
DR   BioGRID; 202252; 1.
DR   ComplexPortal; CPX-55; Cardiac phospholamban complex.
DR   IntAct; P61014; 6.
DR   STRING; 10090.ENSMUSP00000045709; -.
DR   GlyGen; P61014; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P61014; -.
DR   PhosphoSitePlus; P61014; -.
DR   SwissPalm; P61014; -.
DR   PaxDb; 10090-ENSMUSP00000132743; -.
DR   ProteomicsDB; 289809; -.
DR   ABCD; P61014; 2 sequenced antibodies.
DR   Antibodypedia; 3353; 558 antibodies from 39 providers.
DR   DNASU; 18821; -.
DR   Ensembl; ENSMUST00000046221.8; ENSMUSP00000045709.7; ENSMUSG00000038583.14.
DR   Ensembl; ENSMUST00000163319.9; ENSMUSP00000132743.2; ENSMUSG00000038583.14.
DR   Ensembl; ENSMUST00000218468.2; ENSMUSP00000151745.2; ENSMUSG00000038583.14.
DR   Ensembl; ENSMUST00000219491.2; ENSMUSP00000151641.2; ENSMUSG00000038583.14.
DR   Ensembl; ENSMUST00000219921.2; ENSMUSP00000151860.2; ENSMUSG00000038583.14.
DR   Ensembl; ENSMUST00000220197.2; ENSMUSP00000151966.2; ENSMUSG00000038583.14.
DR   GeneID; 18821; -.
DR   KEGG; mmu:18821; -.
DR   UCSC; uc007fbo.2; mouse.
DR   AGR; MGI:97622; -.
DR   CTD; 5350; -.
DR   MGI; MGI:97622; Pln.
DR   VEuPathDB; HostDB:ENSMUSG00000038583; -.
DR   eggNOG; ENOG502S97F; Eukaryota.
DR   GeneTree; ENSGT00390000002403; -.
DR   HOGENOM; CLU_214576_0_0_1; -.
DR   InParanoid; P61014; -.
DR   OMA; YITRSAM; -.
DR   TreeFam; TF330750; -.
DR   Reactome; R-MMU-5578775; Ion homeostasis.
DR   Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR   BioGRID-ORCS; 18821; 1 hit in 74 CRISPR screens.
DR   ChiTaRS; Pln; mouse.
DR   PRO; PR:P61014; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; P61014; Protein.
DR   Bgee; ENSMUSG00000038583; Expressed in interventricular septum and 118 other cell types or tissues.
DR   GO; GO:0090534; C:calcium ion-transporting ATPase complex; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0031982; C:vesicle; ISO:MGI.
DR   GO; GO:0042030; F:ATPase inhibitor activity; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0001675; P:acrosome assembly; IDA:UniProtKB.
DR   GO; GO:0086023; P:adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process; IMP:MGI.
DR   GO; GO:0006816; P:calcium ion transport; ISO:MGI.
DR   GO; GO:0048738; P:cardiac muscle tissue development; IGI:MGI.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IDA:UniProtKB.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IGI:MGI.
DR   GO; GO:1901895; P:negative regulation of ATPase-coupled calcium transmembrane transporter activity; IMP:UniProtKB.
DR   GO; GO:1902081; P:negative regulation of calcium ion import into sarcoplasmic reticulum; IMP:UniProtKB.
DR   GO; GO:0051926; P:negative regulation of calcium ion transport; ISO:MGI.
DR   GO; GO:0045822; P:negative regulation of heart contraction; IMP:MGI.
DR   GO; GO:0010459; P:negative regulation of heart rate; ISO:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR   GO; GO:0090279; P:regulation of calcium ion import; IMP:MGI.
DR   GO; GO:0051924; P:regulation of calcium ion transport; ISS:UniProtKB.
DR   GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IMP:MGI.
DR   GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IMP:MGI.
DR   GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR   GO; GO:1901077; P:regulation of relaxation of muscle; IMP:MGI.
DR   GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IMP:MGI.
DR   GO; GO:0002026; P:regulation of the force of heart contraction; IMP:MGI.
DR   GO; GO:0086092; P:regulation of the force of heart contraction by cardiac conduction; IMP:MGI.
DR   GO; GO:0033574; P:response to testosterone; ISO:MGI.
DR   GO; GO:0010043; P:response to zinc ion; ISO:MGI.
DR   CDD; cd20250; Phospholamban; 1.
DR   Gene3D; 1.20.5.290; Phospholamban; 1.
DR   InterPro; IPR005984; PLB.
DR   NCBIfam; TIGR01294; P_lamban; 1.
DR   PANTHER; PTHR21194; CARDIAC PHOSPHOLAMBAN; 1.
DR   PANTHER; PTHR21194:SF1; CARDIAC PHOSPHOLAMBAN; 1.
DR   Pfam; PF04272; Phospholamban; 1.
DR   PIRSF; PIRSF001665; PLB; 1.
DR   Genevisible; P61014; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Endoplasmic reticulum; Lipoprotein; Membrane;
KW   Mitochondrion; Palmitate; Phosphoprotein; Reference proteome;
KW   Sarcoplasmic reticulum; Transmembrane; Transmembrane helix.
FT   CHAIN           1..52
FT                   /note="Cardiac phospholamban"
FT                   /id="PRO_0000191245"
FT   TOPO_DOM        1..31
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:A4IFH6"
FT   MOD_RES         16
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000269|PubMed:20890288,
FT                   ECO:0000269|PubMed:22971924, ECO:0000269|PubMed:26644582,
FT                   ECO:0007744|PubMed:21183079"
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:0000269|PubMed:26644582"
FT   MUTAGEN         20..22
FT                   /note="MPQ->GGG: No effect on inhibition of ATP2A1-mediated
FT                   calcium uptake."
FT                   /evidence="ECO:0000269|PubMed:22971924"
FT   MUTAGEN         20..21
FT                   /note="MP->GG: Nearly abolishes inhibition of
FT                   ATP2A1-mediated calcium uptake."
FT   MUTAGEN         21
FT                   /note="P->G: Reduces inhibition of ATP2A1-mediated calcium
FT                   uptake."
FT                   /evidence="ECO:0000269|PubMed:22971924"
FT   MUTAGEN         22
FT                   /note="Q->G: Strongly reduces inhibition of ATP2A1-mediated
FT                   calcium uptake."
FT                   /evidence="ECO:0000269|PubMed:22971924"
FT   MUTAGEN         32..36
FT                   /note="FINFC->AAAAA: Cleaved by SPPL2c."
FT                   /evidence="ECO:0000269|PubMed:30733280"
FT   MUTAGEN         36..46
FT                   /note="CLILICLLLIC->ALILIALLLIA: Not cleaved by SPPL2c."
FT                   /evidence="ECO:0000269|PubMed:30733280"
FT   MUTAGEN         36
FT                   /note="C->A: Abolishes palmitoylation."
FT                   /evidence="ECO:0000269|PubMed:26644582"
FT   MUTAGEN         41
FT                   /note="C->A: Does not affect palmitoylation."
FT                   /evidence="ECO:0000269|PubMed:26644582"
FT   MUTAGEN         42..46
FT                   /note="LLLIC->AAAAA: Cleaved by SPPL2c."
FT                   /evidence="ECO:0000269|PubMed:30733280"
FT   MUTAGEN         46
FT                   /note="C->A: Does not affect palmitoylation."
FT                   /evidence="ECO:0000269|PubMed:26644582"
FT   TURN            9..11
FT                   /evidence="ECO:0007829|PDB:3O7L"
SQ   SEQUENCE   52 AA;  6095 MW;  0763601F76A854D3 CRC64;
     MEKVQYLTRS AIRRASTIEM PQQARQNLQN LFINFCLILI CLLLICIIVM LL
//