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 02-SEP-2026, entry version 166. DE RecName: Full=Phospholamban {ECO:0000303|PubMed:1394867, ECO:0000312|MGI:MGI:97622}; 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, INTERACTION WITH ATP2A2, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=27923914; DOI=10.1126/scisignal.aaj1460; RA Anderson D.M., Makarewich C.A., Anderson K.M., Shelton J.M., RA Bezprozvannaya S., Bassel-Duby R., Olson E.N.; RT "Widespread control of calcium signaling by a family of SERCA-inhibiting RT micropeptides."; RL Sci. Signal. 9:ra119-ra119(2016). RN [10] 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). RN [11] RP FUNCTION, SUBUNIT, AND INTERACTION WITH ATP2A2. RX PubMed=31449798; DOI=10.1016/j.jmb.2019.07.037; RA Singh D.R., Dalton M.P., Cho E.E., Pribadi M.P., Zak T.J., Seflova J., RA Makarewich C.A., Olson E.N., Robia S.L.; RT "Newly Discovered Micropeptide Regulators of SERCA Form Oligomers but Bind RT to the Pump as Monomers."; RL J. Mol. Biol. 431:4429-4443(2019). RN [12] RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=38493225; DOI=10.1038/s41598-024-56447-x; RA Klocke B., Britzolaki A., Saurine J., Ott H., Krone K., Bahamonde K., RA Thelen C., Tzimas C., Sanoudou D., Kranias E.G., Pitychoutis P.M.; RT "A novel role for phospholamban in the thalamic reticular nucleus."; RL Sci. Rep. 14:6376-6376(2024). CC -!- FUNCTION: Reversibly inhibits the activity of ATP2A2/SERCA2 in cardiac CC sarcoplasmic reticulum by decreasing the apparent affinity of the CC ATPase for Ca(2+) (PubMed:22971924, PubMed:27923914, PubMed:31449798). CC Binds preferentially to the ATP-bound E1 conformational form of ATP2A2 CC which predominates at low Ca(2+) concentrations during the diastolic CC phase of the cardiac cycle (By similarity). Inhibits ATP2A2 Ca(2+) CC affinity by disrupting its allosteric activation by ATP (By CC similarity). 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 Also inhibits the activity of ATP2A3/SERCA3 (PubMed:27923914). Controls CC intracellular Ca(2+) levels in elongated spermatids and may play a role CC in germ cell differentiation (PubMed:30733280). In the thalamic CC reticular nucleus of the brain, plays a role in the regulation of sleep CC patterns and executive functioning (PubMed:38493225). CC {ECO:0000250|UniProtKB:P61012, ECO:0000269|PubMed:22971924, CC ECO:0000269|PubMed:26816378, ECO:0000269|PubMed:27923914, CC ECO:0000269|PubMed:30733280, ECO:0000269|PubMed:31449798, CC ECO:0000269|PubMed:38493225}. CC -!- SUBUNIT: Homopentamer (PubMed:26644582). Can also form heterooligomers CC with other sarcoplasmic/endoplasmic reticulum calcium ATPase (SERCA) CC regulators ARLN, ERLN, SLN and STRIT1/DWORF (By similarity). Monomer CC (PubMed:31449798). Interacts with HAX1. Interacts as a monomer with CC ATP2A2; the interaction decreases ATP2A2 Ca(2+) affinity CC (PubMed:27923914, PubMed:31449798). Interacts with VMP1; VMP1 competes CC with PLN and SLN to prevent them from forming an inhibitory complex CC with ATP2A2. Interacts with S100A1 in a Ca(2+)-dependent manner. CC {ECO:0000250|UniProtKB:P26678, ECO:0000269|PubMed:26644582, CC ECO:0000269|PubMed:27923914, ECO:0000269|PubMed:31449798}. 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:27923914, CC ECO:0000269|PubMed:30733280}; 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: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 at the sarcoplasmic reticulum. CC {ECO:0000250|UniProtKB:P26678}. CC -!- TISSUE SPECIFICITY: Expressed in testis (at protein level) CC (PubMed:30733280). In brain, expressed specifically in GABAergic GAD67+ CC neurons of the thalamic reticular nucleus where it colocalizes with CC ATP2A2/SERCA2 (at protein level) (PubMed:38493225). Expressed in the CC bladder and in the atria and ventricles of the heart (PubMed:27923914). CC {ECO:0000269|PubMed:27923914, ECO:0000269|PubMed:30733280, CC ECO:0000269|PubMed:38493225}. 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 -!- DISRUPTION PHENOTYPE: Hyperactivity and impaired spatial working memory CC with no effect on sociability or preference for social novelty CC (PubMed:38493225). Conditional knockout in GABAergic neurons of the CC thalamic reticular nucleus results in hyperactivity, altered sleep CC architecture and impaired executive functioning which gives rise to CC impulsivity (PubMed:38493225). {ECO:0000269|PubMed:38493225}. CC -!- SIMILARITY: Belongs to the phospholamban family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 AlphaFoldDB; P61014; -. DR BMRB; P61014; -. DR SMR; P61014; -. DR BioGRID; 202252; 1. DR ComplexPortal; CPX-55; Cardiac phospholamban complex. DR FunCoup; P61014; 565. 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-ENSMUSP00000045709; -. DR ProteomicsDB; 289809; -. DR ABCD; P61014; 2 sequenced antibodies. DR Antibodypedia; 3353; 522 antibodies from 41 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; QHTMRSA; -. 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 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:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; EXP:UniProtKB. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:1990629; C:phospholamban complex; ISO:GO_Central. DR GO; GO:0032991; C:protein-containing complex; ISO:GO_Central. 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:GO_Central. DR GO; GO:0042030; F:ATPase inhibitor activity; IDA:UniProt. DR GO; GO:0042802; F:identical protein binding; ISO:GO_Central. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0044325; F:transmembrane transporter binding; ISO:GO_Central. DR GO; GO:0141110; F:transporter inhibitor activity; ISO:GO_Central. DR GO; GO:0001675; P:acrosome assembly; IDA:UniProtKB. DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IMP:MGI. DR GO; GO:0006816; P:calcium ion transport; ISO:GO_Central. DR GO; GO:0048738; P:cardiac muscle tissue development; IGI:MGI. DR GO; GO:0050802; P:circadian sleep/wake cycle, sleep; IMP:UniProtKB. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IDA:UniProtKB. DR GO; GO:0045475; P:locomotor rhythm; IMP:UniProtKB. DR GO; GO:1901895; P:negative regulation of ATPase-coupled calcium transmembrane transporter activity; IDA:MGI. 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:GO_Central. DR GO; GO:0045822; P:negative regulation of heart contraction; IMP:MGI. DR GO; GO:0010459; P:negative regulation of heart rate; ISO:GO_Central. DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI. DR GO; GO:1901894; P:regulation of ATPase-coupled calcium transmembrane transporter activity; ISO:GO_Central. 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:0051480; P:regulation of cytosolic calcium ion concentration; ISO:GO_Central. 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:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; 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:0032868; P:response to insulin; IEA:Ensembl. DR GO; GO:0033574; P:response to testosterone; ISO:GO_Central. DR GO; GO:0010043; P:response to zinc ion; ISO:GO_Central. DR GO; GO:0007283; P:spermatogenesis; IDA:UniProt. DR GO; GO:0008542; P:visual learning; IMP:UniProtKB. DR CDD; cd20250; Phospholamban; 1. DR FunFam; 1.20.5.290:FF:000001; Cardiac 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 PDBsum; 3O7L; -. 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="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" FT HELIX 13..16 FT /evidence="ECO:0007829|PDB:3O7L" SQ SEQUENCE 52 AA; 6095 MW; 0763601F76A854D3 CRC64; MEKVQYLTRS AIRRASTIEM PQQARQNLQN LFINFCLILI CLLLICIIVM LL //