POPD1_RAT
ID POPD1_RAT Reviewed; 356 AA.
AC Q3BCU4;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Blood vessel epicardial substance;
DE AltName: Full=Popeye domain-containing protein 1;
DE Short=Popeye protein 1;
GN Name=Bves; Synonyms=Pop1, Popdc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Heart;
RX PubMed=17662479; DOI=10.1016/j.bbaexp.2007.06.001;
RA Parnes D., Jacoby V., Sharabi A., Schlesinger H., Brand T.,
RA Kessler-Icekson G.;
RT "The Popdc gene family in the rat: molecular cloning, characterization and
RT expression analysis in the heart and cultured cardiomyocytes.";
RL Biochim. Biophys. Acta 1769:586-592(2007).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND SER-318, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24066022; DOI=10.1371/journal.pone.0071100;
RA Alcalay Y., Hochhauser E., Kliminski V., Dick J., Zahalka M.A., Parnes D.,
RA Schlesinger H., Abassi Z., Shainberg A., Schindler R.F., Brand T.,
RA Kessler-Icekson G.;
RT "Popeye domain containing 1 (Popdc1/Bves) is a caveolae-associated protein
RT involved in ischemia tolerance.";
RL PLoS ONE 8:E71100-E71100(2013).
CC -!- FUNCTION: Cell adhesion molecule involved in the establishment and/or
CC maintenance of cell integrity. Involved in the formation and regulation
CC of the tight junction (TJ) paracellular permeability barrier in
CC epithelial cells. Plays a role in VAMP3-mediated vesicular transport
CC and recycling of different receptor molecules through its interaction
CC with VAMP3. Plays a role in the regulation of cell shape and movement
CC by modulating the Rho-family GTPase activity through its interaction
CC with ARHGEF25/GEFT. Induces primordial adhesive contact and aggregation
CC of epithelial cells in a Ca(2+)-independent manner. Important for
CC skeletal muscle and heart development. Also involved in striated muscle
CC regeneration and repair and in the regulation of cell spreading (By
CC similarity). 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. Is a caveolae-associated protein important for the
CC preservation of caveolae structural and functional integrity as well as
CC for heart protection against ischemia injury (By similarity).
CC {ECO:0000250|UniProtKB:Q5PQZ7, ECO:0000250|UniProtKB:Q8NE79,
CC ECO:0000250|UniProtKB:Q9ES83}.
CC -!- SUBUNIT: Homodimer. Homodimerization requires the C-terminus
CC cytoplasmic region (By similarity). Interacts (via the C-terminus
CC cytoplasmic tail) with TJP1. Interacts (via the C-terminus cytoplasmic
CC tail) with ARHGEF25/GEFT (via the DH domain). Interacts (via the C-
CC terminus cytoplasmic tail) with VAMP3. Interacts with KCNK2; the
CC interaction enhances KCNK2 surface expression and is inhibited by cAMP
CC (By similarity). Interacts with CAV3 (By similarity).
CC {ECO:0000250|UniProtKB:Q8NE79, ECO:0000250|UniProtKB:Q9DG23,
CC ECO:0000250|UniProtKB:Q9ES83}.
CC -!- SUBCELLULAR LOCATION: Lateral cell membrane
CC {ECO:0000250|UniProtKB:Q8NE79}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q8NE79}. Membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:24066022}. Membrane, caveola
CC {ECO:0000269|PubMed:24066022}. Note=Colocalizes with VAMP3 at the cell-
CC cell contact in cardiac and skeletal muscle (By similarity). Its
CC movement from the cytoplasm to membrane is an early event occurring
CC concurrently with cell-cell contact. Colocalizes in epithelial cells
CC with OCLN and TJP1 in an apical-lateral position within the z axis.
CC Detected at cell-cell contact but never observed at the free surface of
CC epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q9ES83}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in heart and skeletal muscle.
CC Weakly expressed in brain, spleen, liver, kidney and lung.
CC {ECO:0000269|PubMed:17662479, ECO:0000269|PubMed:24066022}.
CC -!- SIMILARITY: Belongs to the popeye family. {ECO:0000305}.
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DR EMBL; AY786529; AAX14396.2; -; mRNA.
DR RefSeq; NP_001071058.1; NM_001077590.1.
DR AlphaFoldDB; Q3BCU4; -.
DR SMR; Q3BCU4; -.
DR GlyGen; Q3BCU4; 2 sites.
DR iPTMnet; Q3BCU4; -.
DR PhosphoSitePlus; Q3BCU4; -.
DR PRIDE; Q3BCU4; -.
DR Ensembl; ENSRNOT00000066167; ENSRNOP00000091870; ENSRNOG00000043199.
DR GeneID; 365603; -.
DR KEGG; rno:365603; -.
DR UCSC; RGD:1561100; rat.
DR CTD; 11149; -.
DR RGD; 1561100; Bves.
DR GeneTree; ENSGT00390000002563; -.
DR InParanoid; Q3BCU4; -.
DR OrthoDB; 1369469at2759; -.
DR PhylomeDB; Q3BCU4; -.
DR PRO; PR:Q3BCU4; -.
DR Proteomes; UP000002494; Chromosome 20.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0031253; C:cell projection membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0030552; F:cAMP binding; ISO:RGD.
DR GO; GO:0005198; F:structural molecule activity; ISS:UniProtKB.
DR GO; GO:0060973; P:cell migration involved in heart development; ISO:RGD.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0040017; P:positive regulation of locomotion; ISS:UniProtKB.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:2001135; P:regulation of endocytic recycling; ISO:RGD.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
DR GO; GO:0060931; P:sinoatrial node cell development; ISO:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISS:UniProtKB.
DR GO; GO:0051146; P:striated muscle cell differentiation; IBA:GO_Central.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0048278; P:vesicle docking; ISO:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
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 adhesion; Cell junction; Cell membrane;
KW Developmental protein; Glycoprotein; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Tight junction; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..356
FT /note="Blood vessel epicardial substance"
FT /id="PRO_0000394477"
FT TOPO_DOM 1..48
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 93..115
FT /note="Required for interaction with CAV3"
FT /evidence="ECO:0000250|UniProtKB:Q9ES83"
FT REGION 136..186
FT /note="Required for interaction with KCNK2"
FT /evidence="ECO:0000250|UniProtKB:Q8NE79"
FT REGION 313..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 356 AA; 40860 MW; 3FC1347C9D510311 CRC64;
MNFTEPSPLA QSTVVGFLPE LESLTPVPSN ETSCENWREV HHLVFHAANV CFAVGLLIPT
TLHLHMILLR VMLSIGCTLY VVWATLYRCA LDMMIWNSVF LGINILHLSY LLYKKRPVKI
EKDLGGVYHR LFEPLRVPPD LFRRLTGQFC VIQTLKRGQV YATEDKTSVD DRLSILLKGR
MKVSYRGHFL HNIYPCAFID SPEFRSTQMH KGEKFQVTIV ADDNCRFLCW SRERLTYFLE
SEPFLYEIFR YLIGKDITNK LYSLNDPTLN DKKVKKLEPQ MSLSTQISML EMRNSITSSS
DIEDGLHHFL RGSSSTASLP MSSPQQRASP KMKPIEEGLE DDDEVFVPVS PAHQLP
