POPD2_MOUSE
ID POPD2_MOUSE Reviewed; 367 AA.
AC Q9ES82;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Popeye domain-containing protein 2;
DE Short=Popeye protein 2;
GN Name=Popdc2; Synonyms=Pop2;
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], POSSIBLE FUNCTION, DEVELOPMENTAL STAGE, AND
RP TISSUE SPECIFICITY.
RX PubMed=10882522; DOI=10.1006/dbio.2000.9751;
RA Andree B., Hillemann T., Kessler-Icekson G., Schmitt-John T., Jockusch H.,
RA Arnold H.-H., Brand T.;
RT "Isolation and characterization of the novel popeye gene family expressed
RT in skeletal muscle and heart.";
RL Dev. Biol. 223:371-382(2000).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-364, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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 [3]
RP FUNCTION, DISRUPTION PHENOTYPE, CAMP-BINDING, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF ASP-184.
RX PubMed=22354168; DOI=10.1172/jci59410;
RA Froese A., Breher S.S., Waldeyer C., Schindler R.F., Nikolaev V.O.,
RA Rinne S., Wischmeyer E., Schlueter J., Becher J., Simrick S., Vauti F.,
RA Kuhtz J., Meister P., Kreissl S., Torlopp A., Liebig S.K., Laakmann S.,
RA Mueller T.D., Neumann J., Stieber J., Ludwig A., Maier S.K., Decher N.,
RA Arnold H.H., Kirchhof P., Fabritz L., Brand T.;
RT "Popeye domain containing proteins are essential for stress-mediated
RT modulation of cardiac pacemaking in mice.";
RL J. Clin. Invest. 122:1119-1130(2012).
CC -!- FUNCTION: Important for the maintenance of cardiac function. Plays a
CC regulatory function in heart rate dynamics mediated, at least in part,
CC through cAMP-binding and, probably, by increasing cell surface
CC expression of the potassium channel KCNK2 and enhancing current
CC density. {ECO:0000250|UniProtKB:Q6JWV8, ECO:0000269|PubMed:22354168}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q9HBU9}.
CC -!- TISSUE SPECIFICITY: Expressed in the developing and adult heart, with
CC high expression levels in the sinus and atrioventricular nodes. Also
CC expressed in the bladder and skeletal muscle.
CC {ECO:0000269|PubMed:10882522, ECO:0000269|PubMed:22354168}.
CC -!- DEVELOPMENTAL STAGE: Expression was first detected at 7.5 dpc in the
CC cardiac crescent. Expression was observed in the myocardial layer but
CC not in the endocardium. Expression was homogeneous in all heart
CC segments with the exception of the outflow tract. Between 9.5 dpc and
CC 10.5 dpc expression was also observed in the trabeculated areas. In
CC more advanced stages of myocardial differentiation, expression in the
CC ventricle was largely restricted to the compact layer.
CC {ECO:0000269|PubMed:10882522}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice are deficient to adapt heart rate
CC to physiological stress, this deficiency develops in older mice. They
CC show severe sinus node dysfunction with long pauses and intercurrent
CC periods of normal synus rhythm. The sinus node structure is abnormal
CC with a loss of pacemaker tissue from the inferior part of the sinus
CC node and a compact structure of the superior sinus node.
CC {ECO:0000269|PubMed:22354168}.
CC -!- SIMILARITY: Belongs to the popeye family. {ECO:0000305}.
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DR EMBL; AF204175; AAG23408.1; -; mRNA.
DR CCDS; CCDS37342.1; -.
DR RefSeq; NP_071713.1; NM_022318.3.
DR AlphaFoldDB; Q9ES82; -.
DR SMR; Q9ES82; -.
DR STRING; 10090.ENSMUSP00000023494; -.
DR GlyGen; Q9ES82; 2 sites.
DR iPTMnet; Q9ES82; -.
DR PhosphoSitePlus; Q9ES82; -.
DR PaxDb; Q9ES82; -.
DR PRIDE; Q9ES82; -.
DR ProteomicsDB; 289790; -.
DR Antibodypedia; 16586; 60 antibodies from 15 providers.
DR DNASU; 64082; -.
DR Ensembl; ENSMUST00000114739; ENSMUSP00000110387; ENSMUSG00000022803.
DR GeneID; 64082; -.
DR KEGG; mmu:64082; -.
DR UCSC; uc007zeu.2; mouse.
DR CTD; 64091; -.
DR MGI; MGI:1930150; Popdc2.
DR VEuPathDB; HostDB:ENSMUSG00000022803; -.
DR eggNOG; ENOG502R0XG; Eukaryota.
DR GeneTree; ENSGT00390000002563; -.
DR HOGENOM; CLU_048494_2_0_1; -.
DR InParanoid; Q9ES82; -.
DR OrthoDB; 1369469at2759; -.
DR PhylomeDB; Q9ES82; -.
DR BioGRID-ORCS; 64082; 1 hit in 57 CRISPR screens.
DR ChiTaRS; Cnot7; mouse.
DR PRO; PR:Q9ES82; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9ES82; protein.
DR Bgee; ENSMUSG00000022803; Expressed in interventricular septum and 116 other tissues.
DR ExpressionAtlas; Q9ES82; baseline and differential.
DR Genevisible; Q9ES82; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0030552; F:cAMP binding; IDA:MGI.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IGI:MGI.
DR GO; GO:0060931; P:sinoatrial node cell development; IMP:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; IBA:GO_Central.
DR GO; GO:0051146; P:striated muscle cell differentiation; IBA:GO_Central.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR006916; Popeye_prot.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR12101; PTHR12101; 1.
DR Pfam; PF04831; Popeye; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
PE 1: Evidence at protein level;
KW cAMP; cAMP-binding; Cell membrane; Glycoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..367
FT /note="Popeye domain-containing protein 2"
FT /id="PRO_0000046794"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 273..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..329
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 364
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 184
FT /note="D->A: Almost abolishes cAMP-binding."
FT /evidence="ECO:0000269|PubMed:22354168"
SQ SEQUENCE 367 AA; 41252 MW; 74D89B4062C85CBA CRC64;
MSANGSSVAQ LLWQPPVCRS WKPDVEGAVY HLANCFLLMG FMAGSGVYGC FYLFGILGPG
YLCCVLWGWF DACGLDIVLW NVLLTVACLL QLAQLVYRVR VNTLPEEFNL LYRTLCLPLQ
VPLQVYKEIV HCCHEQVLTL ATEQTYAVEG ETPINRLSLL LSGRVRVSQD GQFLHYIFPY
QFMDSPEWES LHPSEEGTFQ VTLTAETECS YISWPRKNLY LLLNRERYIS RLFSALLGYD
ISEKLYTLND KLFAKFGLRF DIRLPSLYHV LSPSASDGEP ESEKDDEEAL EAAVSPAQAR
PICIVPTPPC SAPPATTNFP VPLPRARMPR MPRPDSGNLA SRRPLQNSSQ VMSRSQAPLA
PIHTPEL
