ID   PPD1B_XENLA             Reviewed;         338 AA.
AC   Q0IH22;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Blood vessel epicardial substance-B;
DE   AltName: Full=Popeye domain-containing protein 1-B;
DE            Short=Popeye protein 1-B;
DE            Short=Xpop-1-B;
GN   Name=bves-b; Synonyms=pop1-b, popdc1-b;
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 [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the popeye family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC123356; AAI23357.1; -; mRNA.
DR   RefSeq; NP_001090409.1; NM_001096940.1.
DR   AlphaFoldDB; Q0IH22; -.
DR   SMR; Q0IH22; -.
DR   DNASU; 779321; -.
DR   GeneID; 779321; -.
DR   KEGG; xla:779321; -.
DR   CTD; 779321; -.
DR   Xenbase; XB-GENE-865066; bves.S.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 779321; Expressed in heart and 12 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; 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: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   2: Evidence at transcript level;
KW   Cell adhesion; Cell junction; Cell membrane; Developmental protein;
KW   Glycoprotein; Membrane; Reference proteome; Tight junction; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..338
FT                   /note="Blood vessel epicardial substance-B"
FT                   /id="PRO_0000394481"
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   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"
SQ   SEQUENCE   338 AA;  38954 MW;  F7584B02397DAEB4 CRC64;
     MATESILITT LPMDFNSQMN NVTIGLNDNE TLCENWREIH HLVFHLANAC FAAGLVIPST
     LNLHMIFLRG MLCLGCTFFI IWAVLFRCAL DIMIWNATFL IINFMHFVYL VYKKRPIKVK
     NDLKDIYHRM FEPLHVSPEL FNRLTGQFCE MKTLAKGQTY AVEDKTSVDD RLSLLLMGIM
     KVSYRGHFLH TISANAYIDS PEFRSTEMNR GETFQVTITA DENCVFLCWS RERLTYFLES
     EPFLYEIFKY LIGKDITTKL YSLNDPTLGK KKKLDTQPSL CSQLSVMEMR NSLASTSDHE
     DGLQNFLRGT STTSSQRHNQ QEFYNAYGVG PLSHAVFC