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Blood vessel epicardial substance (mBVES) (Popeye domain-containing protein 1) (Popeye protein 1)

 POPD1_MOUSE             Reviewed;         358 AA.
Q9ES83; A2RS91; Q8C8L3;
31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-SEP-2018, entry version 123.
RecName: Full=Blood vessel epicardial substance {ECO:0000312|MGI:MGI:1346013};
Short=mBVES;
AltName: Full=Popeye domain-containing protein 1;
Short=Popeye protein 1;
Name=Bves {ECO:0000312|MGI:MGI:1346013};
Synonyms=Pop1 {ECO:0000312|MGI:MGI:1346013},
Popdc1 {ECO:0000312|MGI:MGI:1346013};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, DEVELOPMENTAL STAGE,
AND TISSUE SPECIFICITY.
PubMed=10882522; DOI=10.1006/dbio.2000.9751;
Andree B., Hillemann T., Kessler-Icekson G., Schmitt-John T.,
Jockusch H., Arnold H.-H., Brand T.;
"Isolation and characterization of the novel popeye gene family
expressed in skeletal muscle and heart.";
Dev. Biol. 223:371-382(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-358.
PubMed=10208750; DOI=10.1006/dbio.1999.9246;
Reese D.E., Zavaljevski M., Streiff N.L., Bader D.;
"bves: a novel gene expressed during coronary blood vessel
development.";
Dev. Biol. 209:159-171(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 259-358.
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=11839816; DOI=10.1128/MCB.22.5.1504-1512.2002;
Andree B., Fleige A., Arnold H.H., Brand T.;
"Mouse Pop1 is required for muscle regeneration in adult skeletal
muscle.";
Mol. Cell. Biol. 22:1504-1512(2002).
[6]
FUNCTION, INTERACTION WITH TJP1, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=16188940; DOI=10.1242/jcs.02588;
Osler M.E., Chang M.S., Bader D.M.;
"Bves modulates epithelial integrity through an interaction at the
tight junction.";
J. Cell Sci. 118:4667-4678(2005).
[7]
FUNCTION, INTERACTION WITH ARHGEF25, AND TISSUE SPECIFICITY.
PubMed=18541910; DOI=10.1073/pnas.0802345105;
Smith T.K., Hager H.A., Francis R., Kilkenny D.M., Lo C.W.,
Bader D.M.;
"Bves directly interacts with GEFT, and controls cell shape and
movement through regulation of Rac1/Cdc42 activity.";
Proc. Natl. Acad. Sci. U.S.A. 105:8298-8303(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, INTERACTION WITH VAMP3, AND SUBCELLULAR LOCATION.
PubMed=20057356; DOI=10.1038/emboj.2009.379;
Hager H.A., Roberts R.J., Cross E.E., Proux-Gillardeaux V.,
Bader D.M.;
"Identification of a novel Bves function: regulation of vesicular
transport.";
EMBO J. 29:532-545(2010).
[10]
FUNCTION, DISRUPTION PHENOTYPE, CAMP-BINDING, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF ASP-200; PRO-202; GLU-203 AND VAL-217.
PubMed=22354168; DOI=10.1172/JCI59410;
Froese A., Breher S.S., Waldeyer C., Schindler R.F., Nikolaev V.O.,
Rinne S., Wischmeyer E., Schlueter J., Becher J., Simrick S.,
Vauti F., Kuhtz J., Meister P., Kreissl S., Torlopp A., Liebig S.K.,
Laakmann S., Mueller T.D., Neumann J., Stieber J., Ludwig A.,
Maier S.K., Decher N., Arnold H.H., Kirchhof P., Fabritz L., Brand T.;
"Popeye domain containing proteins are essential for stress-mediated
modulation of cardiac pacemaking in mice.";
J. Clin. Invest. 122:1119-1130(2012).
[11]
FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CAV3, AND SUBCELLULAR
LOCATION.
PubMed=24066022; DOI=10.1371/journal.pone.0071100;
Alcalay Y., Hochhauser E., Kliminski V., Dick J., Zahalka M.A.,
Parnes D., Schlesinger H., Abassi Z., Shainberg A., Schindler R.F.,
Brand T., Kessler-Icekson G.;
"Popeye domain containing 1 (Popdc1/Bves) is a caveolae-associated
protein involved in ischemia tolerance.";
PLoS ONE 8:E71100-E71100(2013).
[12]
INTERACTION WITH KCNK2.
PubMed=26642364; DOI=10.1172/JCI79562;
Schindler R.F., Scotton C., Zhang J., Passarelli C., Ortiz-Bonnin B.,
Simrick S., Schwerte T., Poon K.L., Fang M., Rinne S., Froese A.,
Nikolaev V.O., Grunert C., Mueller T., Tasca G., Sarathchandra P.,
Drago F., Dallapiccola B., Rapezzi C., Arbustini E., Di Raimo F.R.,
Neri M., Selvatici R., Gualandi F., Fattori F., Pietrangelo A., Li W.,
Jiang H., Xu X., Bertini E., Decher N., Wang J., Brand T., Ferlini A.;
"POPDC1S201F causes muscular dystrophy and arrhythmia by affecting
protein trafficking.";
J. Clin. Invest. 126:239-253(2016).
-!- FUNCTION: Cell adhesion molecule involved in the establishment
and/or maintenance of cell integrity. Involved in the formation
and regulation of the tight junction (TJ) paracellular
permeability barrier in epithelial cells (PubMed:16188940). Plays
a role in VAMP3-mediated vesicular transport and recycling of
different receptor molecules through its interaction with VAMP3
(PubMed:20057356). Plays a role in the regulation of cell shape
and movement by modulating the Rho-family GTPase activity through
its interaction with ARHGEF25/GEFT (PubMed:18541910). Induces
primordial adhesive contact and aggregation of epithelial cells in
a Ca(2+)-independent manner. Also involved in striated muscle
regeneration and repair and in the regulation of cell spreading
(PubMed:11839816). Important for the maintenance of cardiac
function. Plays a regulatory function in heart rate dynamics
mediated, at least in part, through cAMP-binding and, probably, by
increasing cell surface expression of the potassium channel KCNK2
and enhancing current density (PubMed:26642364). Is a caveolae-
associated protein important for the preservation of caveolae
structural and functional integrity as well as for heart
protection against ischemia injury (PubMed:24066022).
{ECO:0000250|UniProtKB:Q8NE79, ECO:0000269|PubMed:10882522,
ECO:0000269|PubMed:11839816, ECO:0000269|PubMed:16188940,
ECO:0000269|PubMed:18541910, ECO:0000269|PubMed:20057356,
ECO:0000269|PubMed:22354168, ECO:0000269|PubMed:24066022}.
-!- SUBUNIT: Homodimer. Homodimerization requires the C-terminus
cytoplasmic region (By similarity). Interacts (via the C-terminus
cytoplasmic tail) with TJP1. Interacts (via the C-terminus
cytoplasmic tail) with ARHGEF25/GEFT (via the DH domain).
Interacts (via the C-terminus cytoplasmic tail) with VAMP3.
Interacts with KCNK2; the interaction enhances KCNK2 surface
expression and is inhibited by cAMP (PubMed:22354168,
PubMed:26642364). Interacts with CAV3 (PubMed:24066022).
{ECO:0000250|UniProtKB:Q9DG23, ECO:0000269|PubMed:16188940,
ECO:0000269|PubMed:18541910, ECO:0000269|PubMed:20057356,
ECO:0000269|PubMed:24066022, ECO:0000269|PubMed:26642364}.
-!- INTERACTION:
Q9CWR0:Arhgef25; NbExp=2; IntAct=EBI-7705661, EBI-15708245;
P63025:Vamp3 (xeno); NbExp=3; IntAct=EBI-7705661, EBI-7705696;
-!- SUBCELLULAR LOCATION: Lateral cell membrane
{ECO:0000250|UniProtKB:Q8NE79}. Cell junction, tight junction
{ECO:0000269|PubMed:16188940}. Membrane
{ECO:0000269|PubMed:22354168}; Multi-pass membrane protein
{ECO:0000305}. Cell membrane, sarcolemma
{ECO:0000269|PubMed:24066022}. Membrane, caveola
{ECO:0000269|PubMed:24066022}. Note=Its movement from the
cytoplasm to membrane is an early event occurring concurrently
with cell-cell contact. Detected at cell-cell contact but never
observed at the free surface of epithelial cells (By similarity).
Colocalizes in epithelial cells with OCLN and TJP1 in an apical-
lateral position within the z axis. Colocalizes with VAMP3 at the
cell-cell contact in cardiac and skeletal muscle.
{ECO:0000269|PubMed:16188940, ECO:0000269|PubMed:20057356}.
-!- TISSUE SPECIFICITY: Expressed in epithelial cells, skeletal
muscle, heart and intestinal smooth muscle (at protein level).
Expressed in fetal and adult heart and skeletal muscle.
{ECO:0000269|PubMed:10882522, ECO:0000269|PubMed:11839816,
ECO:0000269|PubMed:16188940, ECO:0000269|PubMed:18541910}.
-!- DEVELOPMENTAL STAGE: Expressed in the mesoderm of the cardiac
crescent at E9.5. Expressed in cardiac myocytes of the sinoatrial
compartment and some restricted areas of the dorsal part of the
ventricle chambers at E10.5 and E12.5. Expressed in branchial
arches, myotome and in a posterior domain in the limb at E10.5.
Expressed in the heart, mainly in the compact layer myocardium,
peridigital mesenchyme, the somites of the tail bud, the smooth
muscle cells of the trachea and the developing bronchial tree, the
smooth muscle cells lining the digestive tract, the dorsal root
ganglia and the pancreas anlage at E13.5 (at protein level).
Expressed in the sinoatrial compartment and some restricted areas
in the dorsal part of the ventricle at E9.5, E10.5 and E11.5. At
E12.5, expression was observed in the ventral half of the
ventricle where it was limited to the subepicardial compact layer.
{ECO:0000269|PubMed:10882522, ECO:0000269|PubMed:11839816}.
-!- DISRUPTION PHENOTYPE: Skeletal muscle regeneration appears to be
less efficient and delayed (PubMed:11839816). Knockout mice are
deficient to adapt heart rate to physiological stress, this
deficiency develops in older mice. They show severe sinus node
dysfunction with long pauses and intercurrent periods of normal
synus rhythm. The sinus node strucutre is abnormal with a loss of
pacemaker tissue from the inferior part of the sinus node and a
compact structure of the superior sinus node (PubMed:22354168).
They have inpaired functional recovery after ischemia/reperfusion
injury (PubMed:24066022). {ECO:0000269|PubMed:11839816,
ECO:0000269|PubMed:22354168, ECO:0000269|PubMed:24066022}.
-!- SIMILARITY: Belongs to the popeye family. {ECO:0000305}.
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EMBL; AF204174; AAG23407.1; -; mRNA.
EMBL; AF124510; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC132018; AAI32019.1; -; mRNA.
EMBL; BC132044; AAI32045.1; -; mRNA.
EMBL; AK046765; BAC32859.1; -; mRNA.
CCDS; CCDS23828.1; -.
RefSeq; NP_077247.1; NM_024285.2.
RefSeq; XP_006512799.1; XM_006512736.3.
RefSeq; XP_006512800.1; XM_006512737.2.
UniGene; Mm.332793; -.
ProteinModelPortal; Q9ES83; -.
SMR; Q9ES83; -.
DIP; DIP-46118N; -.
IntAct; Q9ES83; 3.
MINT; Q9ES83; -.
STRING; 10090.ENSMUSP00000093382; -.
iPTMnet; Q9ES83; -.
PhosphoSitePlus; Q9ES83; -.
MaxQB; Q9ES83; -.
PaxDb; Q9ES83; -.
PeptideAtlas; Q9ES83; -.
PRIDE; Q9ES83; -.
Ensembl; ENSMUST00000095715; ENSMUSP00000093382; ENSMUSG00000071317.
GeneID; 23828; -.
KEGG; mmu:23828; -.
UCSC; uc007ezz.1; mouse.
CTD; 11149; -.
MGI; MGI:1346013; Bves.
eggNOG; ENOG410IGHK; Eukaryota.
eggNOG; ENOG410ZTIT; LUCA.
GeneTree; ENSGT00390000002563; -.
HOGENOM; HOG000236292; -.
HOVERGEN; HBG053638; -.
InParanoid; Q9ES83; -.
KO; K21108; -.
OMA; TIGCTLY; -.
OrthoDB; EOG091G0B7Q; -.
PhylomeDB; Q9ES83; -.
TreeFam; TF326644; -.
PRO; PR:Q9ES83; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000071317; Expressed in 122 organ(s), highest expression level in heart left ventricle.
CleanEx; MM_BVES; -.
Genevisible; Q9ES83; MM.
GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
GO; GO:0005901; C:caveola; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0031253; C:cell projection membrane; IDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
GO; GO:0030552; F:cAMP binding; IDA:MGI.
GO; GO:0005198; F:structural molecule activity; ISS:UniProtKB.
GO; GO:0060973; P:cell migration involved in heart development; IMP:BHF-UCL.
GO; GO:0090136; P:epithelial cell-cell adhesion; ISS:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
GO; GO:0040017; P:positive regulation of locomotion; IDA:UniProtKB.
GO; GO:0001921; P:positive regulation of receptor recycling; IDA:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB.
GO; GO:2001135; P:regulation of endocytic recycling; IMP:BHF-UCL.
GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
GO; GO:0042391; P:regulation of membrane potential; IGI:MGI.
GO; GO:0002931; P:response to ischemia; IMP:UniProtKB.
GO; GO:0060931; P:sinoatrial node cell development; IMP:MGI.
GO; GO:0007519; P:skeletal muscle tissue development; ISS:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:UniProtKB.
GO; GO:0048278; P:vesicle docking; IMP:BHF-UCL.
GO; GO:0016192; P:vesicle-mediated transport; IDA:UniProtKB.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR006916; Popeye_prot.
InterPro; IPR014710; RmlC-like_jellyroll.
PANTHER; PTHR12101; PTHR12101; 1.
Pfam; PF04831; Popeye; 1.
SUPFAM; SSF51206; SSF51206; 1.
1: Evidence at protein level;
cAMP; cAMP-binding; Cell adhesion; Cell junction; Cell membrane;
Complete proteome; Developmental protein; Glycoprotein; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Tight junction; Transmembrane; Transmembrane helix.
CHAIN 1 358 Blood vessel epicardial substance.
/FTId=PRO_0000046792.
TOPO_DOM 1 48 Extracellular. {ECO:0000255}.
TRANSMEM 49 69 Helical. {ECO:0000255}.
TOPO_DOM 70 70 Cytoplasmic. {ECO:0000255}.
TRANSMEM 71 91 Helical. {ECO:0000255}.
TOPO_DOM 92 92 Extracellular. {ECO:0000255}.
TRANSMEM 93 113 Helical. {ECO:0000255}.
TOPO_DOM 114 358 Cytoplasmic. {ECO:0000255}.
REGION 93 115 Required for interaction with CAV3.
{ECO:0000269|PubMed:24066022}.
REGION 136 186 Required for interaction with KCNK2.
{ECO:0000250|UniProtKB:Q8NE79}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000250|UniProtKB:Q3BCU4}.
CARBOHYD 2 2 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 30 30 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 200 200 D->A: Almost abolishes cAMP-binding.
Interaction with KCNK2 is not inhibited
by cAMP. {ECO:0000269|PubMed:22354168}.
MUTAGEN 202 202 P->A: No effect on cAMP-binding.
{ECO:0000269|PubMed:22354168}.
MUTAGEN 203 203 E->A: Decreases cAMP-binding.
{ECO:0000269|PubMed:22354168}.
MUTAGEN 217 217 V->F: Decreases cAMP-binding.
{ECO:0000269|PubMed:22354168}.
SEQUENCE 358 AA; 41016 MW; B92F1942F1713027 CRC64;
MNSTESIPLA QSTVAGFTSE LESLTPVPSN ETTCENWREI HHLVFHVANV CFAVGLLIPT
TLHLHMILLR VMLSLGCTLY VVWATLYRCA LDVMIWNSVF LGINILHLSY LLYKKRPVKI
EKELGGVYHR LFEPLRVPPD LFRRLTGQFC MIQTLKRGQV YATEDKTSVD DRLSILLKGR
MKVSYRGHFL HNIYPCAFID SPEFRSTQMH KGEKFQVTIV ADDNCRFLCW SRERLTYFLE
SEPFLYEIFR YLIGKDITNK LYSLNDPTLN DKKVKKLEPQ MSLCTQISML EMRNSITSSS
DGEDGLHHFL RGSSSTASLP MSSPQQRASA KMKPIEEGVE DDDEVFVSPD ALKVHQLP


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