APJB_DANRE
ID APJB_DANRE Reviewed; 359 AA.
AC A0T2N3; Q4V905;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Apelin receptor B;
DE AltName: Full=Angiotensin II receptor-like 1b;
DE AltName: Full=Angiotensin receptor-like 1b;
DE AltName: Full=G-protein coupled receptor APJ B;
DE AltName: Full=Protein grinch;
GN Name=aplnrb; Synonyms=agtrl1b, grn {ECO:0000303|PubMed:17336906};
GN ORFNames=zgc:114063;
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] {ECO:0000305, ECO:0000312|EMBL:ABK63803.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17336905; DOI=10.1016/j.devcel.2007.01.011;
RA Zeng X.-X.I., Wilm T.P., Sepich D.S., Solnica-Krezel L.;
RT "Apelin and its receptor control heart field formation during zebrafish
RT gastrulation.";
RL Dev. Cell 12:391-402(2007).
RN [2] {ECO:0000312|EMBL:AAH97125.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH97125.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF TRP-90.
RX PubMed=17336906; DOI=10.1016/j.devcel.2007.01.012;
RA Scott I.C., Masri B., D'Amico L.A., Jin S.-W., Jungblut B., Wehman A.M.,
RA Baier H., Audigier Y., Stainier D.Y.R.;
RT "The G protein-coupled receptor Agtrl1b regulates early development of
RT myocardial progenitors.";
RL Dev. Cell 12:403-413(2007).
RN [4] {ECO:0000305}
RP REVIEW.
RX PubMed=17336895; DOI=10.1016/j.devcel.2007.02.005;
RA Quertermous T.;
RT "Apelin and its G protein-coupled receptor regulate cardiac development as
RT well as cardiac function.";
RL Dev. Cell 12:319-320(2007).
RN [5]
RP FUNCTION, INTERACTION WITH APELA, MUTAGENESIS OF TRP-90, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24316148; DOI=10.1016/j.devcel.2013.11.002;
RA Chng S.C., Ho L., Tian J., Reversade B.;
RT "ELABELA: a hormone essential for heart development signals via the apelin
RT receptor.";
RL Dev. Cell 27:672-680(2013).
RN [6]
RP FUNCTION, INTERACTION WITH APELA, AND DISRUPTION PHENOTYPE.
RX PubMed=24407481; DOI=10.1126/science.1248636;
RA Pauli A., Norris M.L., Valen E., Chew G.L., Gagnon J.A., Zimmerman S.,
RA Mitchell A., Ma J., Dubrulle J., Reyon D., Tsai S.Q., Joung J.K.,
RA Saghatelian A., Schier A.F.;
RT "Toddler: an embryonic signal that promotes cell movement via apelin
RT receptors.";
RL Science 343:1248636-1248636(2014).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26017639; DOI=10.7554/elife.06726;
RA Helker C.S., Schuermann A., Pollmann C., Chng S.C., Kiefer F.,
RA Reversade B., Herzog W.;
RT "The hormonal peptide Elabela guides angioblasts to the midline during
RT vasculogenesis.";
RL Elife 4:0-0(2015).
CC -!- FUNCTION: Receptor for apelin receptor early endogenous ligand (apela)
CC and apelin (apln) hormones coupled to G proteins that inhibit adenylate
CC cyclase activity (PubMed:17336905, PubMed:17336906, PubMed:24316148,
CC PubMed:24407481). Plays a key role in early development such as
CC gastrulation, blood vessels formation and heart morphogenesis by acting
CC as a receptor for apela hormone, promoting endoderm and mesendoderm
CC cell migration and regulating the migration of cells fated to become
CC myocardial progenitors, respectively (PubMed:17336905, PubMed:17336906,
CC PubMed:24316148, PubMed:24407481, PubMed:26017639). Positively
CC regulates angioblast migration toward the embryonic midline, i.e. the
CC position of the future vessel formation, during vasculogenesis
CC (PubMed:26017639). May promote sinus venosus (SV)-derived endothelial
CC cells migration into the developing heart to promote coronary blood
CC vessel development (By similarity). Required for cardiovascular
CC development, particularly for intersomitic vein angiogenesis by acting
CC as a receptor for apln hormone (By similarity). Plays a role in various
CC processes in adults such as regulation of blood vessel formation, blood
CC pressure, heart contractility and heart failure (By similarity). Acts
CC redundantly with agtrl1a in heart development (PubMed:17336906).
CC {ECO:0000250|UniProtKB:P35414, ECO:0000250|UniProtKB:P79960,
CC ECO:0000250|UniProtKB:Q4VA82, ECO:0000250|UniProtKB:Q9WV08,
CC ECO:0000269|PubMed:17336905, ECO:0000269|PubMed:17336906,
CC ECO:0000269|PubMed:24316148, ECO:0000269|PubMed:24407481,
CC ECO:0000269|PubMed:26017639}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P79960};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P79960}.
CC Note=Internalized to the cytoplasm after exposure to apelin (apln).
CC After exposure to apelin receptor early endogenous ligand (apela),
CC internalized from the cell surface into an endosomal recycling
CC compartment, from where it is recycled to the cell membrane.
CC {ECO:0000250|UniProtKB:P35414, ECO:0000250|UniProtKB:P79960}.
CC -!- TISSUE SPECIFICITY: Mesendodermal expression at the blastoderm margin
CC appears by 4.5 hpf. At early gastrulation, expression is maintained
CC ventrolaterally while expression in dorsal cells and random deep cells
CC declines. During gastrulation and segmentation, expression is
CC maintained in adaxial, intermediate, and lateral plate mesoderm. During
CC late segmentation, expressed in several regions including the forming
CC heart. By 24 hpf, expressed in the dorsal aorta, caudal vein, and
CC intersomitic blood vessels. {ECO:0000269|PubMed:17336905}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein induces
CC embryonic lethality due to cardiac dysplasia with little to no blood
CC circulation around 6 days post-fertilization (dpf) (PubMed:24316148).
CC Mutant embryos show pericardial edema and accumulation of erythrocytes
CC in the intermediate cell mass (ICM) at 30 hours post-fertilization
CC (hpf) (PubMed:24316148). Display decreased angioblast migration to the
CC embryonic midline during late gastrulation (PubMed:24316148,
CC PubMed:24407481, PubMed:26017639). {ECO:0000269|PubMed:24316148,
CC ECO:0000269|PubMed:24407481, ECO:0000269|PubMed:26017639}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH97125.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EF079888; ABK63803.1; -; mRNA.
DR EMBL; BC097125; AAH97125.1; ALT_INIT; mRNA.
DR RefSeq; NP_001025368.2; NM_001030197.2.
DR AlphaFoldDB; A0T2N3; -.
DR SMR; A0T2N3; -.
DR STRING; 7955.ENSDARP00000108783; -.
DR PaxDb; A0T2N3; -.
DR Ensembl; ENSDART00000129643; ENSDARP00000108783; ENSDARG00000036670.
DR GeneID; 565492; -.
DR KEGG; dre:565492; -.
DR CTD; 565492; -.
DR ZFIN; ZDB-GENE-050913-90; aplnrb.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244888; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; A0T2N3; -.
DR OMA; FCLTCMS; -.
DR OrthoDB; 788659at2759; -.
DR PhylomeDB; A0T2N3; -.
DR TreeFam; TF330024; -.
DR Reactome; R-DRE-375276; Peptide ligand-binding receptors.
DR Reactome; R-DRE-418594; G alpha (i) signalling events.
DR PRO; PR:A0T2N3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 10.
DR Bgee; ENSDARG00000036670; Expressed in spleen and 38 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0060182; F:apelin receptor activity; IDA:ZFIN.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0035479; P:angioblast cell migration from lateral mesoderm to midline; IMP:ZFIN.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0001568; P:blood vessel development; IBA:GO_Central.
DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0060976; P:coronary vasculature development; ISS:UniProtKB.
DR GO; GO:0061371; P:determination of heart left/right asymmetry; IMP:ZFIN.
DR GO; GO:0071910; P:determination of liver left/right asymmetry; IMP:ZFIN.
DR GO; GO:0035987; P:endodermal cell differentiation; IGI:ZFIN.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IMP:ZFIN.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007369; P:gastrulation; IMP:ZFIN.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0008078; P:mesodermal cell migration; IMP:ZFIN.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:1904325; P:positive regulation of inhibitory G protein-coupled receptor phosphorylation; ISS:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:1900107; P:regulation of nodal signaling pathway; IGI:ZFIN.
DR GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
DR InterPro; IPR000248; ATII_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00241; ANGIOTENSINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Cell membrane; Developmental protein;
KW G-protein coupled receptor; Gastrulation; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="Apelin receptor B"
FT /id="PRO_0000312594"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..213
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 90
FT /note="W->L: In grns608; defective in early myocardial
FT specification."
FT /evidence="ECO:0000269|PubMed:17336906,
FT ECO:0000269|PubMed:24316148"
SQ SEQUENCE 359 AA; 40147 MW; 8D88B8A3EB169FCD CRC64;
MNAMDNMTAD YSPDYFDDAV NSSMCEYDEW EPSYSLIPVL YMLIFILGLT GNGVVIFTVW
RAQSKRRAAD VYIGNLALAD LTFVVTLPLW AVYTALGYHW PFGVALCKIS SYVVLLNMYA
SVFCLTCLSL DRYMAIVHSL TSTQLRTRGH MRASLTAIWL LSGVLAAPTL LFRTTVYDVE
TNRTSCAMDF NLVVSQPGQE TYWIAGLSIS STALGFLIPL LAMMVCYGFI GCTVTRHFNS
LRKEDQRKRR LLKIITTLVV VFAACWMPFH VVKTMDALSY LNLAPDSCTF LNLLLLAHPY
ATCLAYVNSC LNPLLYAFFD LRFRSQCLCL LNLKKALHAS PASSLSSQKT EAQSLATKV
