APJ_RAT
ID APJ_RAT Reviewed; 377 AA.
AC Q9JHG3; Q9ESK2;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Apelin receptor;
DE AltName: Full=Angiotensin receptor-like 1;
DE AltName: Full=B78;
DE AltName: Full=G-protein coupled receptor APJ;
DE AltName: Full=GPCR34;
GN Name=Aplnr; Synonyms=Agtrl1, Apj;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10777510; DOI=10.1074/jbc.m908417199;
RA Hosoya M., Kawamata Y., Fukusumi S., Fujii R., Habata Y., Hinuma S.,
RA Kitada C., Honda S., Kurokawa T., Onda H., Nishimura O., Fujino M.;
RT "Molecular and functional characteristics of APJ: tissue distribution of
RT mRNA and interaction with the endogenous ligand apelin.";
RL J. Biol. Chem. 275:21061-21067(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Pituitary;
RX PubMed=11004481; DOI=10.1016/s0167-4781(00)00072-5;
RA O'Carroll A.-M., Selby T.L., Palkovits M., Lolait S.J.;
RT "Distribution of mRNA encoding B78/apj, the rat homologue of the human APJ
RT receptor, and its endogenous ligand apelin in brain and peripheral
RT tissues.";
RL Biochim. Biophys. Acta 1492:72-80(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=11146423; DOI=10.1159/000054609;
RA De Mota N., Lenkei Z., Llorens-Cortes C.;
RT "Cloning, pharmacological characterization and brain distribution of the
RT rat apelin receptor.";
RL Neuroendocrinology 72:400-407(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-300.
RC STRAIN=Sprague-Dawley;
RA Carroll S.L., Miller M.L., Benedict-Hamilton H.M.;
RT "Identification and characterization of novel G-protein coupled receptors
RT expressed in regenerating peripheral nerve.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=11359874; DOI=10.1046/j.1471-4159.2001.00320.x;
RA Reaux A., De Mota N., Skultetyova I., Lenkei Z., El Messari S., Gallatz K.,
RA Corvol P., Palkovits M., Llorens-Cortes C.;
RT "Physiological role of a novel neuropeptide, apelin, and its receptor in
RT the rat brain.";
RL J. Neurochem. 77:1085-1096(2001).
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:11359874). Plays a key role in early
CC development such as gastrulation, blood vessels formation and heart
CC morphogenesis by acting as a receptor for APELA hormone. May promote
CC angioblast migration toward the embryonic midline, i.e. the position of
CC the future vessel formation, during vasculogenesis. Promotes sinus
CC venosus (SV)-derived endothelial cells migration into the developing
CC heart to promote coronary blood vessel development. Also plays a role
CC in various processes in adults such as regulation of blood vessel
CC formation, blood pressure, heart contractility and heart failure (By
CC similarity). {ECO:0000250|UniProtKB:P35414,
CC ECO:0000250|UniProtKB:P79960, ECO:0000250|UniProtKB:Q7SZP9,
CC ECO:0000250|UniProtKB:Q9WV08, ECO:0000269|PubMed:11359874}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11359874};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P79960}. Note=After
CC exposure to apelin (APLN), internalized from the cell surface into an
CC endosomal recycling compartment, from where it is recycled to the cell
CC membrane (PubMed:11359874). After exposure to apelin receptor early
CC endogenous ligand (APELA), internalized from the cell surface into an
CC endosomal recycling compartment, from where it is recycled to the cell
CC membrane (By similarity). {ECO:0000250|UniProtKB:P35414,
CC ECO:0000269|PubMed:11359874}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in the lung,
CC lower in the heart, placenta, ovary, skeletal muscle, mammary gland,
CC kidney and several structures in the brain as the hypothalamus
CC (supraoptic and periventricular nuclei), pituitary, olfactory bulb and
CC pineal gland. {ECO:0000269|PubMed:11359874}.
CC -!- DEVELOPMENTAL STAGE: Higher expression in neonates than in adult.
CC {ECO:0000269|PubMed:11359874}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB033170; BAA95002.1; -; mRNA.
DR EMBL; AF184883; AAF80860.1; -; mRNA.
DR EMBL; BC072494; AAH72494.1; -; mRNA.
DR EMBL; AF090346; AAG24468.1; -; mRNA.
DR RefSeq; NP_112639.1; NM_031349.2.
DR AlphaFoldDB; Q9JHG3; -.
DR SMR; Q9JHG3; -.
DR STRING; 10116.ENSRNOP00000012379; -.
DR BindingDB; Q9JHG3; -.
DR ChEMBL; CHEMBL2398; -.
DR GuidetoPHARMACOLOGY; 36; -.
DR GlyGen; Q9JHG3; 2 sites.
DR PhosphoSitePlus; Q9JHG3; -.
DR PaxDb; Q9JHG3; -.
DR Ensembl; ENSRNOT00000012379; ENSRNOP00000012379; ENSRNOG00000009227.
DR GeneID; 83518; -.
DR KEGG; rno:83518; -.
DR UCSC; RGD:621645; rat.
DR CTD; 187; -.
DR RGD; 621645; Aplnr.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244888; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; Q9JHG3; -.
DR OMA; TVMLTCY; -.
DR OrthoDB; 788659at2759; -.
DR PhylomeDB; Q9JHG3; -.
DR TreeFam; TF330024; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:Q9JHG3; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000009227; Expressed in lung and 16 other tissues.
DR Genevisible; Q9JHG3; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA: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:0042277; F:peptide binding; TAS:RGD.
DR GO; GO:0007512; P:adult heart development; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0035904; P:aorta development; ISO:RGD.
DR GO; GO:0060183; P:apelin receptor signaling pathway; ISO:RGD.
DR GO; GO:0003171; P:atrioventricular valve development; ISO:RGD.
DR GO; GO:0001568; P:blood vessel development; IBA:GO_Central.
DR GO; GO:0060976; P:coronary vasculature development; ISS:UniProtKB.
DR GO; GO:0003272; P:endocardial cushion formation; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0001947; P:heart looping; ISO:RGD.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
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:0031065; P:positive regulation of histone deacetylation; ISO:RGD.
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:0050878; P:regulation of body fluid levels; IMP:RGD.
DR GO; GO:1903596; P:regulation of gap junction assembly; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0035886; P:vascular associated smooth muscle cell differentiation; ISO:RGD.
DR GO; GO:0001944; P:vasculature development; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
DR GO; GO:0060841; P:venous blood vessel development; ISO:RGD.
DR GO; GO:0060412; P:ventricular septum morphogenesis; ISO:RGD.
DR InterPro; IPR003904; Apelin_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; PR01416; APJRECEPTOR.
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;
KW G-protein coupled receptor; Gastrulation; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..377
FT /note="Apelin receptor"
FT /id="PRO_0000069176"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..53
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..106
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..265
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 335..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 117
FT /note="C -> W (in Ref. 5; AAG24468)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="A -> G (in Ref. 5; AAG24468)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="G -> R (in Ref. 5; AAG24468)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="L -> P (in Ref. 5; AAG24468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 42349 MW; C43F81EBC3855BB2 CRC64;
MEDDGYNYYG ADNQSECDYA DWTPSGALIP AIYILVFLLG TTGNGLVLWT VFWSSREKRR
SADIFIASLA VADLTFVVTL PLWATYTYRE FDWPFGTFSC KLSSYLIFVN MYASVFCLTG
LSFDRYLAIV RPVANARLRL RVSGAVATAV LWVLAALLAV PVMVFRSTDI PENSTKTQCY
MDYSMVATSN SEWAWEVGLG VSSTAVGFVV PFIIMLTCYF FIAQTIAGHF RKERIEGLRK
RRRLLSIIVV LVVTFALCWM PYHLVKTLYM LGNLLHWPCD FDSFLMNVFP YCTCISYVNS
CLNPFLYAFF DPRFRRACTS MLCCDQSGCK GSPHSSSAEK SASYSSGHSQ GPGPNMCKGG
EPMHEKSIPY SQETLVD
