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

 POPD1_CHICK             Reviewed;         357 AA.
Q9DG23; Q9DG20; Q9DG21; Q9DG22; Q9PWC0;
15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
27-SEP-2017, entry version 77.
RecName: Full=Blood vessel epicardial substance;
AltName: Full=Popeye domain-containing protein 1;
Short=Popeye protein 1;
Name=BVES; Synonyms=POP1, POPDC1;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
TISSUE=Heart;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), NUCLEOTIDE SEQUENCE
[MRNA] OF 37-357 (ISOFORM 2), 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).
[3]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=15277466; DOI=10.1167/iovs.04-0013;
Ripley A.N., Chang M.S., Bader D.M.;
"Bves is expressed in the epithelial components of the retina, lens,
and cornea.";
Invest. Ophthalmol. Vis. Sci. 45:2475-2483(2004).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
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).
[5]
HOMODIMER, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-272 AND
LYS-273.
PubMed=18493308; DOI=10.1371/journal.pone.0002261;
Kawaguchi M., Hager H.A., Wada A., Koyama T., Chang M.S., Bader D.M.;
"Identification of a novel intracellular interaction domain essential
for Bves function.";
PLoS ONE 3:E2261-E2261(2008).
-!- 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. Induces primordial
adhesive contact and aggregation of epithelial cells in a Ca(2+)-
independent manner. Involved in epithelial movement during corneal
sheet formation and regeneration. May play a role in VAMP3-
mediated vesicular transport and recycling of receptor molecules.
May play a role in the regulation of cell shape and movement by
modulating the Rho-GTPase activity. May be involved in skeletal
muscle and heart development as well as in the maintenance of
heart function (By similarity). May also be involved in striated
muscle regeneration and in the regulation of cell spreading.
{ECO:0000250|UniProtKB:Q5PQZ7, ECO:0000250|UniProtKB:Q8NE79,
ECO:0000250|UniProtKB:Q9ES83, ECO:0000269|PubMed:15277466,
ECO:0000269|PubMed:16188940}.
-!- SUBUNIT: Homodimer. Homodimerization requires the C-terminus
cytoplasmic region. {ECO:0000269|PubMed:18493308}.
-!- SUBCELLULAR LOCATION: Lateral cell membrane
{ECO:0000269|PubMed:15277466}. Cell junction, tight junction
{ECO:0000269|PubMed:16188940}. Membrane
{ECO:0000269|PubMed:16188940}; Multi-pass membrane protein
{ECO:0000305}. Cell membrane, sarcolemma
{ECO:0000250|UniProtKB:Q9ES83}. Membrane, caveola
{ECO:0000250|UniProtKB:Q9ES83}. Note=Detected at points of cell-
cell contact in confluent epithelial sheets. Colocalizes with
components of the adherens and tight junctions.
{ECO:0000269|PubMed:15277466, ECO:0000269|PubMed:16188940,
ECO:0000269|PubMed:18493308}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=POP1A;
IsoId=Q9DG23-1; Sequence=Displayed;
Name=2; Synonyms=POP1B;
IsoId=Q9DG23-2; Sequence=VSP_039263, VSP_039267, VSP_039268;
Note=Incomplete sequence.;
Name=3; Synonyms=POP1C;
IsoId=Q9DG23-3; Sequence=VSP_039262, VSP_039265;
Name=4; Synonyms=POP1D;
IsoId=Q9DG23-4; Sequence=VSP_039264, VSP_039266;
-!- TISSUE SPECIFICITY: Expressed in the heart and skeletal muscle (at
protein level). Isoform 1 and isoform 4: expressed in heart,
muscle, brain, stomach, kidney, lung and spleen.
{ECO:0000269|PubMed:10208750, ECO:0000269|PubMed:10882522,
ECO:0000269|PubMed:15277466}.
-!- DEVELOPMENTAL STAGE: Expressed during heart development in the
proepicardial organ, migrating proepicardial strands, delaminated
mesenchymal cells and vascular smooth muscle. Expressed in
epithelial precursors of the cornea, lens and retina of the
developing eye (at protein level). Expressed in the left
ventricular segment of the tubular heart at stage 11. Expressed in
the myotome, notochord and ventral half of the neuronal tube.
{ECO:0000269|PubMed:10208750, ECO:0000269|PubMed:15277466}.
-!- SIMILARITY: Belongs to the popeye family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD51779.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF124511; AAD51779.1; ALT_INIT; mRNA.
EMBL; AF208398; AAG23410.1; -; mRNA.
EMBL; AF208399; AAG23411.1; -; mRNA.
EMBL; AF208400; AAG23412.1; -; mRNA.
EMBL; AF208401; AAG23413.1; -; mRNA.
RefSeq; NP_001001299.2; NM_001001299.2. [Q9DG23-1]
UniGene; Gga.3373; -.
SMR; Q9DG23; -.
STRING; 9031.ENSGALP00000024812; -.
PaxDb; Q9DG23; -.
PRIDE; Q9DG23; -.
Ensembl; ENSGALT00000037249; ENSGALP00000036453; ENSGALG00000015410. [Q9DG23-1]
GeneID; 408032; -.
KEGG; gga:408032; -.
CTD; 11149; -.
eggNOG; ENOG410IGHK; Eukaryota.
eggNOG; ENOG410ZTIT; LUCA.
GeneTree; ENSGT00390000002563; -.
HOGENOM; HOG000236292; -.
HOVERGEN; HBG053638; -.
InParanoid; Q9DG23; -.
KO; K21108; -.
OMA; TIGCTLY; -.
OrthoDB; EOG091G0B7Q; -.
PhylomeDB; Q9DG23; -.
PRO; PR:Q9DG23; -.
Proteomes; UP000000539; Chromosome 3.
Bgee; ENSGALG00000015410; -.
GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
GO; GO:0005901; C:caveola; ISS:UniProtKB.
GO; GO:0005623; C:cell; IDA:AgBase.
GO; GO:0071944; C:cell periphery; IDA:AgBase.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IMP:AgBase.
GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
GO; GO:0089717; C:spanning component of membrane; IDA:AgBase.
GO; GO:0044214; C:spanning component of plasma membrane; IMP:AgBase.
GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
GO; GO:0090136; P:epithelial cell-cell adhesion; IDA:UniProtKB.
GO; GO:0003201; P:epithelial to mesenchymal transition involved in coronary vasculature morphogenesis; IMP:AgBase.
GO; GO:0090132; P:epithelium migration; IMP:AgBase.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0040017; P:positive regulation of locomotion; ISS:UniProtKB.
GO; GO:0001921; P:positive regulation of receptor recycling; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:AgBase.
GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
GO; GO:0007519; P:skeletal muscle tissue development; ISS:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
GO; GO:0016192; P:vesicle-mediated transport; ISS: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;
Alternative splicing; cAMP; cAMP-binding; Cell adhesion;
Cell junction; Cell membrane; Complete proteome;
Developmental protein; Glycoprotein; Membrane; Nucleotide-binding;
Reference proteome; Tight junction; Transmembrane;
Transmembrane helix.
CHAIN 1 357 Blood vessel epicardial substance.
/FTId=PRO_0000394478.
TOPO_DOM 1 38 Extracellular. {ECO:0000255}.
TRANSMEM 39 59 Helical. {ECO:0000255}.
TOPO_DOM 60 62 Cytoplasmic. {ECO:0000255}.
TRANSMEM 63 83 Helical. {ECO:0000255}.
TOPO_DOM 84 89 Extracellular. {ECO:0000255}.
TRANSMEM 90 110 Helical. {ECO:0000255}.
TOPO_DOM 111 357 Cytoplasmic. {ECO:0000255}.
CARBOHYD 20 20 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 27 27 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 155 MDTTAISPLTPLGVIPDLKNATSVPFNETACENWKEIHHLV
FHVANICFAAGLVIPTTLNLHMIFLRGLLTVGCALFIIWAT
LYRCALDIMIWNSVFLVVNLLHFIYLVYKRRPIKIEKELSS
LYKRMFEPLHVPPELFQRLTGQFCNIQTLKTG -> MLPPM
VPGSSNSRIRVPW (in isoform 3).
{ECO:0000303|PubMed:10882522}.
/FTId=VSP_039262.
VAR_SEQ 1 44 MDTTAISPLTPLGVIPDLKNATSVPFNETACENWKEIHHLV
FHV -> NSRIRVPW (in isoform 2).
{ECO:0000303|PubMed:10882522}.
/FTId=VSP_039263.
VAR_SEQ 1 1 M -> MGENASFWESLIYAHPTCVTWKQEAEGSIYHLASIL
FVVGFMGGSGFSGLLYVFSLLGLGFLCSSVWAWLDVCAADI
FSWNFILFAICFVQFIYVTYQVRSVSFDKEFQELYSALFQP
LGISLTVYRKIVLCCDAEVITLEKEHCYAMQGKTPIDKLSL
LVSGRIRVTVDGEFLHYIFPLQFLDSPEWDSLRPTEEGIFQ
VTLTAETDCRYVAWRRKKLYLLFAKHRFISRLFSILIGSDI
AEKLYALNDRCTWGRGLGFFKM (in isoform 4).
{ECO:0000303|PubMed:10882522}.
/FTId=VSP_039264.
VAR_SEQ 317 357 RPGRTSPYLRTSAKMKPIEESVEDDVFEAPSAEKLELQRLP
-> LTGPAEPPPLIGSSIASARKLSTTVSRNLLAYLCLALL
PPDMGSQSSQVPRPSTVNIIQLSEEGFHLLALLDQAADTCW
KSPVLVCSLILPISSQLAFHLFQGKALCTGAGPLHRRHLNK
LALSEA (in isoform 3).
{ECO:0000303|PubMed:10882522}.
/FTId=VSP_039265.
VAR_SEQ 317 357 RPGRTSPYLRTSAKMKPIEESVEDDVFEAPSAEKLELQRLP
-> LTGPAEPPPLIGSSIASARKLSTTVSRNLLAYLCLALL
PPDMGSQSSEVPRPSTVKTSSSYLKKASIYLLFLIRQQIPA
VKSPVLVCSLIFTHKLSAGFSPVSRQSSMHWSWSFA (in
isoform 4).
{ECO:0000303|PubMed:10882522}.
/FTId=VSP_039266.
VAR_SEQ 318 324 PGRTSPY -> NNPTRVL (in isoform 2).
{ECO:0000303|PubMed:10882522}.
/FTId=VSP_039267.
VAR_SEQ 325 357 Missing (in isoform 2).
{ECO:0000303|PubMed:10882522}.
/FTId=VSP_039268.
MUTAGEN 272 272 K->A: Abolishes homodimerization and
cell-cell adhesion; when associated with
A-273. {ECO:0000269|PubMed:18493308}.
MUTAGEN 273 273 K->A: Abolishes homodimerization and
cell-cell adhesion; when associated with
A-272. {ECO:0000269|PubMed:18493308}.
CONFLICT 295 296 ST -> RS (in Ref. 1; AAD51779).
{ECO:0000305}.
SEQUENCE 357 AA; 40877 MW; 5CB9194C10924535 CRC64;
MDTTAISPLT PLGVIPDLKN ATSVPFNETA CENWKEIHHL VFHVANICFA AGLVIPTTLN
LHMIFLRGLL TVGCALFIIW ATLYRCALDI MIWNSVFLVV NLLHFIYLVY KRRPIKIEKE
LSSLYKRMFE PLHVPPELFQ RLTGQFCNIQ TLKTGQAYAA EDKTSVDDRL SILLKGKMKV
SYRGHFLHNI YPCAFIDSPE FRSTQMNRGE KFQVTIIADD NCKFLCWSRE RLTYFLETEP
FLYEIFKYLI GKDITNKLYS LNDPTLNDKA SKKIDRQPSL CSQLSVMQMR NSMASTSDSE
DGLQMFLRGT SSSSSLRPGR TSPYLRTSAK MKPIEESVED DVFEAPSAEK LELQRLP


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