POPD1_DANRE
ID POPD1_DANRE Reviewed; 352 AA.
AC Q5PQZ7; Q6JWV9;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Blood vessel epicardial substance;
DE Short=BVES;
DE AltName: Full=Popeye domain-containing protein 1;
DE Short=Popeye protein 1;
GN Name=bves; Synonyms=pop1, popdc1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Brand T., Meyer D., Yelon D.;
RT "Characterization of the popeye gene family in zebrafish.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-191, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26642364; DOI=10.1172/jci79562;
RA Schindler R.F., Scotton C., Zhang J., Passarelli C., Ortiz-Bonnin B.,
RA Simrick S., Schwerte T., Poon K.L., Fang M., Rinne S., Froese A.,
RA Nikolaev V.O., Grunert C., Mueller T., Tasca G., Sarathchandra P.,
RA Drago F., Dallapiccola B., Rapezzi C., Arbustini E., Di Raimo F.R.,
RA Neri M., Selvatici R., Gualandi F., Fattori F., Pietrangelo A., Li W.,
RA Jiang H., Xu X., Bertini E., Decher N., Wang J., Brand T., Ferlini A.;
RT "POPDC1S201F causes muscular dystrophy and arrhythmia by affecting protein
RT trafficking.";
RL J. Clin. Invest. 126:239-253(2016).
CC -!- FUNCTION: Cell adhesion molecule involved in the establishment and/or
CC maintenance of cell integrity. Involved in skeletal muscle and heart
CC development as well as in the maintenance of heart function
CC (PubMed:26642364). May play a role in vamp3-mediated vesicular
CC transport and recycling of receptor molecules. Involved in the
CC formation and regulation of the tight junction (TJ) paracellular
CC permeability barrier in epithelial cells. May induce primordial
CC adhesive contact and aggregation of epithelial cells in a Ca(2+)-
CC independent manner. May be involved in epithelial movement during
CC corneal sheet formation and regeneration. May play a role in the
CC regulation of cell shape and movement by modulating the Rho-GTPase
CC activity. May also be involved in striated muscle regeneration and in
CC the regulation of cell spreading (By similarity).
CC {ECO:0000250|UniProtKB:Q8NE79, ECO:0000250|UniProtKB:Q9ES83,
CC ECO:0000269|PubMed:26642364}.
CC -!- SUBCELLULAR LOCATION: Lateral cell membrane
CC {ECO:0000250|UniProtKB:Q8NE79}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q8NE79}. Membrane {ECO:0000269|PubMed:26642364};
CC Multi-pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:26642364}. 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9ES83}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5PQZ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5PQZ7-2; Sequence=VSP_039269;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:26642364}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC cardiac edema in 70% of the injected morphants. They show malformed
CC myotendinous junction and, in 80% of the morphants, skeletal muscle is
CC characterized by myofibrillar misalignment and fiber detachment.
CC {ECO:0000269|PubMed:26642364}.
CC -!- SIMILARITY: Belongs to the popeye family. {ECO:0000305}.
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DR EMBL; AY293117; AAQ57586.1; -; mRNA.
DR EMBL; AY293118; AAQ57587.1; -; mRNA.
DR EMBL; BC086956; AAH86956.1; -; mRNA.
DR RefSeq; NP_001001847.2; NM_001001847.2. [Q5PQZ7-2]
DR RefSeq; NP_001244091.1; NM_001257162.1. [Q5PQZ7-2]
DR RefSeq; NP_001244092.1; NM_001257163.1. [Q5PQZ7-1]
DR RefSeq; NP_001244093.1; NM_001257164.1. [Q5PQZ7-1]
DR AlphaFoldDB; Q5PQZ7; -.
DR SMR; Q5PQZ7; -.
DR STRING; 7955.ENSDARP00000075860; -.
DR PaxDb; Q5PQZ7; -.
DR PRIDE; Q5PQZ7; -.
DR Ensembl; ENSDART00000081418; ENSDARP00000075860; ENSDARG00000058548. [Q5PQZ7-1]
DR Ensembl; ENSDART00000081422; ENSDARP00000075863; ENSDARG00000058548. [Q5PQZ7-2]
DR Ensembl; ENSDART00000149404; ENSDARP00000123787; ENSDARG00000058548. [Q5PQZ7-2]
DR Ensembl; ENSDART00000184895; ENSDARP00000152394; ENSDARG00000058548. [Q5PQZ7-1]
DR GeneID; 415107; -.
DR KEGG; dre:415107; -.
DR CTD; 11149; -.
DR ZFIN; ZDB-GENE-040624-11; bves.
DR eggNOG; ENOG502QRV2; Eukaryota.
DR GeneTree; ENSGT00390000002563; -.
DR HOGENOM; CLU_048494_0_0_1; -.
DR InParanoid; Q5PQZ7; -.
DR OMA; TSCQEWE; -.
DR PhylomeDB; Q5PQZ7; -.
DR TreeFam; TF326644; -.
DR PRO; PR:Q5PQZ7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000058548; Expressed in heart and 29 other tissues.
DR ExpressionAtlas; Q5PQZ7; baseline.
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; IDA:UniProtKB.
DR GO; GO:0030552; F:cAMP binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; ISS:UniProtKB.
DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:ZFIN.
DR GO; GO:0045216; P:cell-cell junction organization; IMP:ZFIN.
DR GO; GO:0090504; P:epiboly; IMP:ZFIN.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0060429; P:epithelium development; IMP:ZFIN.
DR GO; GO:0061436; P:establishment of skin barrier; IMP:ZFIN.
DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:ZFIN.
DR GO; GO:0060047; P:heart contraction; IMP:ZFIN.
DR GO; GO:0007507; P:heart development; IMP: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:0060041; P:retina development in camera-type eye; IMP:ZFIN.
DR GO; GO:0010842; P:retina layer formation; IMP:ZFIN.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:UniProtKB.
DR GO; GO:0014866; P:skeletal myofibril assembly; IMP:ZFIN.
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 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 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..352
FT /note="Blood vessel epicardial substance"
FT /id="PRO_0000394479"
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
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 299..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 310..352
FT /note="QKNPLTKTSTTMKPIEEGLEDDVFESESPTTSQNVSKTTKKDI -> PVTSD
FT RA (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039269"
FT MUTAGEN 191
FT /note="S->F: Mutants display myofibrillar misalignment,
FT aberrant formation of the myotendinous junction, myofiber
FT detachment with various degrees of severity and a reduction
FT in heart rate and stroke volume. Membrane localization is
FT diminished in muscle."
FT /evidence="ECO:0000269|PubMed:26642364"
FT CONFLICT 221
FT /note="S -> T (in Ref. 1; AAQ57586/AAQ57587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 40340 MW; 8A594B7C5BCB3040 CRC64;
MSNTTSALPS SVPAVSLDPN ATLCQDWEQS HHLLFHLANL SLGLGFLIPT TLALHMIFLR
LLLMTGCSLF IAWATLYRCT LDVMVWNVVF LLVNFMHFFF LLYKRRPIKI DRELKSVYKR
MFEPLHVREA LFQRLTGQFC TIQTLKKGQV YAAEDKTSVD ERLSILLKGK MKVSYRGHFL
HNIYTNAFID SPEFRSTQMN RGERFQVTIA AEENCKLLCW SRERLTYFLE SESFLNEVFR
YLIGKDITNK LYSLNDPTLS DKAVKKMDRQ PSLCSQLSMM QMRNSMASTS DTDDVLNQIL
RGGSTGSSLQ KNPLTKTSTT MKPIEEGLED DVFESESPTT SQNVSKTTKK DI
