APJ_XENTR
ID APJ_XENTR Reviewed; 364 AA.
AC Q4VA82;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Apelin receptor;
DE AltName: Full=Angiotensin receptor-like 1;
DE AltName: Full=Angiotensin receptor-related protein;
DE AltName: Full=G-protein coupled receptor APJ;
GN Name=aplnr; Synonyms=agtrl1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH96504.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=F6 {ECO:0000312|EMBL:AAH96504.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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. 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. Promotes angioblast migration
CC toward the embryonic midline, i.e. the position of the future vessel
CC formation, during vasculogenesis. May promote sinus venosus (SV)-
CC derived endothelial cells migration into the developing heart to
CC promote coronary blood vessel development. Required for cardiovascular
CC development, particularly for intersomitic vein angiogenesis. Plays
CC also a role in various processes in adults such as regulation of blood
CC vessel formation, blood pressure, heart contractility, and heart
CC failure. Acts upstream of the i/o type of G-alpha proteins in the
CC differentiation of endothelium, erythroid cells, myeloid cells and
CC cardiomyocytes. {ECO:0000250|UniProtKB:P35414,
CC ECO:0000250|UniProtKB:P79960, ECO:0000250|UniProtKB:Q7SZP9,
CC ECO:0000250|UniProtKB:Q9WV08}.
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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; BC096504; AAH96504.1; -; mRNA.
DR RefSeq; NP_001027492.1; NM_001032321.1.
DR AlphaFoldDB; Q4VA82; -.
DR SMR; Q4VA82; -.
DR DNASU; 613084; -.
DR GeneID; 613084; -.
DR KEGG; xtr:613084; -.
DR CTD; 187; -.
DR Xenbase; XB-GENE-6456077; aplnr.
DR InParanoid; Q4VA82; -.
DR OrthoDB; 788659at2759; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
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; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0001568; P:blood vessel development; IBA:GO_Central.
DR GO; GO:0060976; P:coronary vasculature development; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
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:0001570; P:vasculogenesis; ISS:UniProtKB.
DR InterPro; IPR003904; Apelin_rcpt.
DR InterPro; IPR000248; ATII_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24228:SF31; PTHR24228:SF31; 1.
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 2: Evidence at transcript level;
KW Angiogenesis; Cell membrane; Developmental protein; Differentiation;
KW G-protein coupled receptor; Gastrulation; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..364
FT /note="Apelin receptor"
FT /id="PRO_0000311702"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..112
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 364 AA; 40917 MW; 623A1429999BA384 CRC64;
MATDEFSSST TPSYDYYDYT NESGLPPCDE TDWDLSYSLL PVFYMIVFVL GLSGNGVVIF
TVWKAKPKRR SADTYIGNLA LADLAFVVTL PLWATYTALG FHWPFGSALC KLSSYLVLLN
MFASVFCLTC LSFDRYLAIV HSLSSAKLRS RSSILVSLAV IWLFSGLLAL PSLILRDTRV
EGNNTICDLD FSGVSSKENE NFWIGGLSIL TTVPGFLLPL LLMTIFYCFI GGKVTMHFQN
LKKEEQKKKR LLKIIITLVV VFAICWLPFH ILKTIHFLDL MGFLELSCST QNIIVSLHPY
ATCLAYINSC LNPFLYAFFD LRFRSQCFFF FGFKKALQGH LSNTSSSLSA QTQKSEIHSL
ATKV
