POPD1_CHICK
ID POPD1_CHICK Reviewed; 357 AA.
AC Q9DG23; Q9DG20; Q9DG21; Q9DG22; Q9PWC0;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Heart;
RX PubMed=10208750; DOI=10.1006/dbio.1999.9246;
RA Reese D.E., Zavaljevski M., Streiff N.L., Bader D.;
RT "bves: a novel gene expressed during coronary blood vessel development.";
RL Dev. Biol. 209:159-171(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), NUCLEOTIDE SEQUENCE [MRNA]
RP OF 37-357 (ISOFORM 2), AND 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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15277466; DOI=10.1167/iovs.04-0013;
RA Ripley A.N., Chang M.S., Bader D.M.;
RT "Bves is expressed in the epithelial components of the retina, lens, and
RT cornea.";
RL Invest. Ophthalmol. Vis. Sci. 45:2475-2483(2004).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16188940; DOI=10.1242/jcs.02588;
RA Osler M.E., Chang M.S., Bader D.M.;
RT "Bves modulates epithelial integrity through an interaction at the tight
RT junction.";
RL J. Cell Sci. 118:4667-4678(2005).
RN [5]
RP HOMODIMER, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-272 AND LYS-273.
RX PubMed=18493308; DOI=10.1371/journal.pone.0002261;
RA Kawaguchi M., Hager H.A., Wada A., Koyama T., Chang M.S., Bader D.M.;
RT "Identification of a novel intracellular interaction domain essential for
RT Bves function.";
RL PLoS ONE 3:E2261-E2261(2008).
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. Induces primordial adhesive contact and aggregation
CC of epithelial cells in a Ca(2+)-independent manner. Involved in
CC epithelial movement during corneal sheet formation and regeneration.
CC May play a role in VAMP3-mediated vesicular transport and recycling of
CC receptor molecules. May play a role in the regulation of cell shape and
CC movement by modulating the Rho-GTPase activity. May be involved in
CC skeletal muscle and heart development as well as in the maintenance of
CC heart function (By similarity). May also be involved in striated muscle
CC regeneration and in the regulation of cell spreading.
CC {ECO:0000250|UniProtKB:Q5PQZ7, ECO:0000250|UniProtKB:Q8NE79,
CC ECO:0000250|UniProtKB:Q9ES83, ECO:0000269|PubMed:15277466,
CC ECO:0000269|PubMed:16188940}.
CC -!- SUBUNIT: Homodimer. Homodimerization requires the C-terminus
CC cytoplasmic region. {ECO:0000269|PubMed:18493308}.
CC -!- SUBCELLULAR LOCATION: Lateral cell membrane
CC {ECO:0000269|PubMed:15277466}. Cell junction, tight junction
CC {ECO:0000269|PubMed:16188940}. Membrane {ECO:0000269|PubMed:16188940};
CC Multi-pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q9ES83}. Membrane, caveola
CC {ECO:0000250|UniProtKB:Q9ES83}. Note=Detected at points of cell-cell
CC contact in confluent epithelial sheets. Colocalizes with components of
CC the adherens and tight junctions. {ECO:0000269|PubMed:15277466,
CC ECO:0000269|PubMed:16188940, ECO:0000269|PubMed:18493308}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=POP1A;
CC IsoId=Q9DG23-1; Sequence=Displayed;
CC Name=2; Synonyms=POP1B;
CC IsoId=Q9DG23-2; Sequence=VSP_039263, VSP_039267, VSP_039268;
CC Name=3; Synonyms=POP1C;
CC IsoId=Q9DG23-3; Sequence=VSP_039262, VSP_039265;
CC Name=4; Synonyms=POP1D;
CC IsoId=Q9DG23-4; Sequence=VSP_039264, VSP_039266;
CC -!- TISSUE SPECIFICITY: Expressed in the heart and skeletal muscle (at
CC protein level). Isoform 1 and isoform 4: expressed in heart, muscle,
CC brain, stomach, kidney, lung and spleen. {ECO:0000269|PubMed:10208750,
CC ECO:0000269|PubMed:10882522, ECO:0000269|PubMed:15277466}.
CC -!- DEVELOPMENTAL STAGE: Expressed during heart development in the
CC proepicardial organ, migrating proepicardial strands, delaminated
CC mesenchymal cells and vascular smooth muscle. Expressed in epithelial
CC precursors of the cornea, lens and retina of the developing eye (at
CC protein level). Expressed in the left ventricular segment of the
CC tubular heart at stage 11. Expressed in the myotome, notochord and
CC ventral half of the neuronal tube. {ECO:0000269|PubMed:10208750,
CC ECO:0000269|PubMed:15277466}.
CC -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the popeye family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD51779.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF124511; AAD51779.1; ALT_INIT; mRNA.
DR EMBL; AF208398; AAG23410.1; -; mRNA.
DR EMBL; AF208399; AAG23411.1; -; mRNA.
DR EMBL; AF208400; AAG23412.1; -; mRNA.
DR EMBL; AF208401; AAG23413.1; -; mRNA.
DR RefSeq; NP_001001299.2; NM_001001299.2. [Q9DG23-1]
DR AlphaFoldDB; Q9DG23; -.
DR SMR; Q9DG23; -.
DR STRING; 9031.ENSGALP00000036453; -.
DR PaxDb; Q9DG23; -.
DR GeneID; 408032; -.
DR KEGG; gga:408032; -.
DR CTD; 11149; -.
DR VEuPathDB; HostDB:geneid_408032; -.
DR eggNOG; ENOG502QRV2; Eukaryota.
DR HOGENOM; CLU_048494_0_0_1; -.
DR InParanoid; Q9DG23; -.
DR OrthoDB; 543991at2759; -.
DR PhylomeDB; Q9DG23; -.
DR PRO; PR:Q9DG23; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0071944; C:cell periphery; IDA:AgBase.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IMP:AgBase.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0089717; C:spanning component of membrane; IDA:AgBase.
DR GO; GO:0044214; C:spanning component of plasma membrane; IMP:AgBase.
DR GO; GO:0030552; F:cAMP binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0003201; P:epithelial to mesenchymal transition involved in coronary vasculature morphogenesis; IMP:AgBase.
DR GO; GO:0090132; P:epithelium migration; IMP:AgBase.
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:0051260; P:protein homooligomerization; IDA:AgBase.
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 1: Evidence at protein level;
KW Alternative splicing; cAMP; cAMP-binding; Cell adhesion; Cell junction;
KW Cell membrane; Developmental protein; Glycoprotein; Membrane;
KW Nucleotide-binding; Reference proteome; Tight junction; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..357
FT /note="Blood vessel epicardial substance"
FT /id="PRO_0000394478"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..89
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 309..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..155
FT /note="MDTTAISPLTPLGVIPDLKNATSVPFNETACENWKEIHHLVFHVANICFAAG
FT LVIPTTLNLHMIFLRGLLTVGCALFIIWATLYRCALDIMIWNSVFLVVNLLHFIYLVYK
FT RRPIKIEKELSSLYKRMFEPLHVPPELFQRLTGQFCNIQTLKTG -> MLPPMVPGSSN
FT SRIRVPW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10882522"
FT /id="VSP_039262"
FT VAR_SEQ 1..44
FT /note="MDTTAISPLTPLGVIPDLKNATSVPFNETACENWKEIHHLVFHV -> NSRI
FT RVPW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10882522"
FT /id="VSP_039263"
FT VAR_SEQ 1
FT /note="M -> MGENASFWESLIYAHPTCVTWKQEAEGSIYHLASILFVVGFMGGSGF
FT SGLLYVFSLLGLGFLCSSVWAWLDVCAADIFSWNFILFAICFVQFIYVTYQVRSVSFDK
FT EFQELYSALFQPLGISLTVYRKIVLCCDAEVITLEKEHCYAMQGKTPIDKLSLLVSGRI
FT RVTVDGEFLHYIFPLQFLDSPEWDSLRPTEEGIFQVTLTAETDCRYVAWRRKKLYLLFA
FT KHRFISRLFSILIGSDIAEKLYALNDRCTWGRGLGFFKM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10882522"
FT /id="VSP_039264"
FT VAR_SEQ 317..357
FT /note="RPGRTSPYLRTSAKMKPIEESVEDDVFEAPSAEKLELQRLP -> LTGPAEP
FT PPLIGSSIASARKLSTTVSRNLLAYLCLALLPPDMGSQSSQVPRPSTVNIIQLSEEGFH
FT LLALLDQAADTCWKSPVLVCSLILPISSQLAFHLFQGKALCTGAGPLHRRHLNKLALSE
FT A (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10882522"
FT /id="VSP_039265"
FT VAR_SEQ 317..357
FT /note="RPGRTSPYLRTSAKMKPIEESVEDDVFEAPSAEKLELQRLP -> LTGPAEP
FT PPLIGSSIASARKLSTTVSRNLLAYLCLALLPPDMGSQSSEVPRPSTVKTSSSYLKKAS
FT IYLLFLIRQQIPAVKSPVLVCSLIFTHKLSAGFSPVSRQSSMHWSWSFA (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:10882522"
FT /id="VSP_039266"
FT VAR_SEQ 318..324
FT /note="PGRTSPY -> NNPTRVL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10882522"
FT /id="VSP_039267"
FT VAR_SEQ 325..357
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10882522"
FT /id="VSP_039268"
FT MUTAGEN 272
FT /note="K->A: Abolishes homodimerization and cell-cell
FT adhesion; when associated with A-273."
FT /evidence="ECO:0000269|PubMed:18493308"
FT MUTAGEN 273
FT /note="K->A: Abolishes homodimerization and cell-cell
FT adhesion; when associated with A-272."
FT /evidence="ECO:0000269|PubMed:18493308"
FT CONFLICT 295..296
FT /note="ST -> RS (in Ref. 1; AAD51779)"
FT /evidence="ECO:0000305"
SQ 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
