PPD1A_XENLA
ID PPD1A_XENLA Reviewed; 338 AA.
AC Q8JH92; Q6DFA7; Q8JHW3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Blood vessel epicardial substance-A;
DE Short=Xbves-A;
DE AltName: Full=Popeye domain-containing protein 1-A;
DE Short=Popeye protein 1-A;
DE Short=Xpop-1-A;
GN Name=bves-a; Synonyms=pop1-a, popdc1-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Heart;
RX PubMed=12049775; DOI=10.1016/s0925-4773(02)00085-0;
RA Hitz M.P., Pandur P., Brand T., Kuhl M.;
RT "Cardiac specific expression of Xenopus Popeye-1.";
RL Mech. Dev. 115:123-126(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Nesset A.L., Bader D.M.;
RT "Xenopus bves serves a novel function in the early embryo.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=16407138; DOI=10.1073/pnas.0506095103;
RA Ripley A.N., Osler M.E., Wright C.V., Bader D.;
RT "Xbves is a regulator of epithelial movement during early Xenopus laevis
RT development.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:614-619(2006).
RN [5]
RP FUNCTION.
RX PubMed=20057356; DOI=10.1038/emboj.2009.379;
RA Hager H.A., Roberts R.J., Cross E.E., Proux-Gillardeaux V., Bader D.M.;
RT "Identification of a novel Bves function: regulation of vesicular
RT transport.";
RL EMBO J. 29:532-545(2010).
CC -!- FUNCTION: Cell adhesion molecule involved in the establishment and/or
CC maintenance of cell integrity. Plays a role in vamp3-mediated vesicular
CC transport and recycling of different receptor molecules. May be
CC involved in the formation and regulation of the tight junction (TJ)
CC paracellular permeability barrier in epithelial cells. May induce
CC primordial adhesive contact and aggregation of epithelial cells in a
CC Ca(2+)-independent manner. May be involved in epithelial movement
CC during 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. {ECO:0000269|PubMed:16407138,
CC ECO:0000269|PubMed:20057356}.
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}. Note=Detected at points of cell-
CC cell contact in confluent epithelial sheets. Colocalizes with
CC components of the adherens and tight junctions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8JH92-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8JH92-2; Sequence=VSP_039270;
CC -!- TISSUE SPECIFICITY: Expressed in the heart.
CC {ECO:0000269|PubMed:12049775}.
CC -!- DEVELOPMENTAL STAGE: Expressed in epithelia cells during gastrulation
CC (at protein level). Expressed in oocyte, cleavage, gastrulation, and
CC neurulation stage embryos. Expression decreases by the end of
CC gastrulation at stage 12. Weakly expressed during neurula at stage 16.
CC Strongly expressed at stage 31 and remains at a robust level through
CC early tadpole stages. Expressed in heart, somites, cement gland and
CC eyes at stage 35. Expressed in the embryonic heart from stage 31
CC through 41 in the outer curvature of the ventricle and atrial regions.
CC {ECO:0000269|PubMed:12049775, ECO:0000269|PubMed:16407138}.
CC -!- SIMILARITY: Belongs to the popeye family. {ECO:0000305}.
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DR EMBL; AF461429; AAM54132.1; -; mRNA.
DR EMBL; AF527799; AAM90308.1; -; mRNA.
DR EMBL; BC076833; AAH76833.1; -; mRNA.
DR RefSeq; NP_001081141.1; NM_001087672.1. [Q8JH92-1]
DR AlphaFoldDB; Q8JH92; -.
DR SMR; Q8JH92; -.
DR DNASU; 394408; -.
DR GeneID; 394408; -.
DR KEGG; xla:394408; -.
DR CTD; 394408; -.
DR Xenbase; XB-GENE-6254222; bves.L.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 394408; Expressed in heart and 14 other tissues.
DR GO; GO:0005923; C:bicellular tight junction; 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:0005198; F:structural molecule activity; ISS:UniProtKB.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; ISS:UniProtKB.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0070587; P:regulation of cell-cell adhesion involved in gastrulation; IDA:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA: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; Cell adhesion; Cell junction; Cell membrane;
KW Developmental protein; Glycoprotein; Membrane; Reference proteome;
KW Tight junction; Transmembrane; Transmembrane helix.
FT CHAIN 1..338
FT /note="Blood vessel epicardial substance-A"
FT /id="PRO_0000394480"
FT TOPO_DOM 1..40
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 296..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..12
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12049775"
FT /id="VSP_039270"
FT CONFLICT 210
FT /note="R -> H (in Ref. 1; AAM54132)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="A -> S (in Ref. 3; AAH76833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 39025 MW; 16B221FFA421AEAB CRC64;
MTTESIFITT LPMDFNSQFD NITIGLNDNE TLCENWREIH HLVFHLANTC FAAGLVIPST
LNLHMLFLRG MLCLGCTFFI IWAVLFRCAL DIMIWNATFL SINFMHFVYL VYKKRPIKIK
KELKGIYHRM FEPLHVSPEL FNRLTGQFCE IKTLAKGQTY AVEDKTSVDD RLSILLKGIM
KVSYRGHFLH TISANAYIDS PEFRSTEMNR GETFQVTITA DDNCVFLCWS RERLTYFLES
EPFLYEIFKY LIGKDITTKL YSLNDPTLGK KRKLDTQPSL CSQLSVMEMR NSLASTNDNE
DGLQNFLRGT STTSSQRNKQ QEFYNAYGVG PLSHAVFC
