POPD1_PIG
ID POPD1_PIG Reviewed; 360 AA.
AC B8Q0B2; B8Q0B1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 62.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Liu B., Peng Y.;
RT "The porcine popeye domain containing genes: molecular cloning,
RT identification of alternative splicing, mapping and muscle-specific
RT expression analysis.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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. Interacts (via the C-terminus cytoplasmic tail)
CC with TJP1. Interacts (via the C-terminus cytoplasmic tail) with
CC ARHGEF25/GEFT (via the DH domain). Interacts (via the C-terminus
CC cytoplasmic tail) with VAMP3 (By similarity). Interacts with KCNK2; the
CC interaction enhances KCNK2 surface expression (By similarity).
CC Interacts with CAV3 (By similarity). {ECO:0000250|UniProtKB:Q8NE79,
CC ECO:0000250|UniProtKB:Q9DG23, ECO:0000250|UniProtKB:Q9ES83}.
CC -!- SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000250}. Cell
CC junction, tight junction {ECO:0000250}. Membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q9ES83}. Membrane, caveola
CC {ECO:0000250|UniProtKB:Q9ES83}. Note=Its movement from the cytoplasm to
CC membrane is an early event occurring concurrently with cell-cell
CC contact. Detected at cell-cell contact but never observed at the free
CC surface of epithelial cells. Colocalizes in epithelial cells with OCLN
CC and TJP1 in an apical-lateral position within the z axis. Colocalizes
CC with VAMP3 at the cell-cell contact in cardiac and skeletal muscle (By
CC similarity). {ECO:0000250|UniProtKB:Q9ES83}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B8Q0B2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B8Q0B2-2; Sequence=VSP_039260, VSP_039261;
CC -!- SIMILARITY: Belongs to the popeye family. {ECO:0000305}.
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DR EMBL; EU334860; ACB13183.1; -; mRNA.
DR EMBL; EU334861; ACB13184.1; -; mRNA.
DR RefSeq; NP_001335345.1; NM_001348416.1. [B8Q0B2-1]
DR AlphaFoldDB; B8Q0B2; -.
DR SMR; B8Q0B2; -.
DR STRING; 9823.ENSSSCP00000004711; -.
DR PaxDb; B8Q0B2; -.
DR Ensembl; ENSSSCT00065059824; ENSSSCP00065025953; ENSSSCG00065043727. [B8Q0B2-1]
DR GeneID; 100153106; -.
DR KEGG; ssc:100153106; -.
DR CTD; 11149; -.
DR eggNOG; ENOG502QRV2; Eukaryota.
DR InParanoid; B8Q0B2; -.
DR OrthoDB; 1369469at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0030552; F:cAMP binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; ISS:UniProtKB.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
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:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
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:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR006916; Popeye_prot.
DR PANTHER; PTHR12101; PTHR12101; 1.
DR Pfam; PF04831; Popeye; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; cAMP; cAMP-binding; Cell adhesion; Cell junction;
KW Cell membrane; Developmental protein; Glycoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Tight junction;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..360
FT /note="Blood vessel epicardial substance"
FT /id="PRO_0000394476"
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..360
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 325..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES83"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3BCU4"
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"
FT VAR_SEQ 321..327
FT /note="VPSPHQR -> WRDKMAE (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039260"
FT VAR_SEQ 328..360
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039261"
SQ SEQUENCE 360 AA; 41444 MW; 0DF08BD664CFEC8C CRC64;
MNYTESSPLA ESTAIGFTPE LGSITPVPSN ETTCENWREI HHLVFHVANV FFAIGLVLPT
TLHLHMILLR GMLTIGCTLY IVWATLYRCA LDIMIWNSVF LGINVLHLSY LLYKKRPVKI
EKELKGIYQR LFEPLRVPPD LFKRLTGQFC MIQTLKKGQA YAAEDKTSVD DRLSILLKGK
MKVSYRGHFL HNIYPCAFID SPEFRSTQMH KGEKFQVTII ADDNCRFLCW SRERLTYFLE
SEPFLYEVFR YLIGKDITNK LYSLNDPTLN DKTIKKLDHQ LSLCTQLSML EMRNSIVSTS
DSEDGLHQFL RGTSSVSSLY VPSPHQRASA KMKPIEEGVE DDDEVFEPET PNTFKVRQLP
