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APJ_MOUSE
ID   APJ_MOUSE               Reviewed;         377 AA.
AC   Q9WV08; Q3TZS9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Apelin receptor;
DE   AltName: Full=Angiotensin receptor-like 1;
DE   AltName: Full=G-protein coupled receptor APJ;
DE   AltName: Full=MSR;
GN   Name=Aplnr; Synonyms=Agtrl1, Apj;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=10473142; DOI=10.1016/s0925-4773(99)00081-7;
RA   Devic E., Rizzoti K., Bodin S., Knibiehler B., Audigier Y.;
RT   "Amino acid sequence and embryonic expression of msr/apj, the mouse homolog
RT   of Xenopus X-msr and human APJ.";
RL   Mech. Dev. 84:199-203(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Lung, Pituitary, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=28854362; DOI=10.1016/j.celrep.2017.08.014;
RA   Freyer L., Hsu C.W., Nowotschin S., Pauli A., Ishida J., Kuba K.,
RA   Fukamizu A., Schier A.F., Hoodless P.A., Dickinson M.E.,
RA   Hadjantonakis A.K.;
RT   "Loss of Apela peptide in mice causes low penetrance embryonic lethality
RT   and defects in early mesodermal derivatives.";
RL   Cell Rep. 20:2116-2130(2017).
RN   [5]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=26611206; DOI=10.1007/s00395-015-0521-6;
RA   Perjes A., Kilpioe T., Ulvila J., Magga J., Alakoski T., Szabo Z.,
RA   Vainio L., Halmetoja E., Vuolteenaho O., Petaejae-Repo U., Szokodi I.,
RA   Kerkelae R.;
RT   "Characterization of apela, a novel endogenous ligand of apelin receptor,
RT   in the adult heart.";
RL   Basic Res. Cardiol. 111:2-2(2016).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28371822; DOI=10.1093/cvr/cvx061;
RA   Sato T., Sato C., Kadowaki A., Watanabe H., Ho L., Ishida J., Yamaguchi T.,
RA   Kimura A., Fukamizu A., Penninger J.M., Reversade B., Ito H., Imai Y.,
RA   Kuba K.;
RT   "ELABELA-APJ axis protects from pressure overload heart failure and
RT   angiotensin II-induced cardiac damage.";
RL   Cardiovasc. Res. 113:760-769(2017).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=28890073; DOI=10.1016/j.devcel.2017.08.008;
RA   Sharma B., Ho L., Ford G.H., Chen H.I., Goldstone A.B., Woo Y.J.,
RA   Quertermous T., Reversade B., Red-Horse K.;
RT   "Alternative progenitor cells compensate to rebuild the coronary
RT   vasculature in Elabela- and Apj-deficient hearts.";
RL   Dev. Cell 42:655-666(2017).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=28663440; DOI=10.1126/science.aam6607;
RA   Ho L., van Dijk M., Chye S.T.J., Messerschmidt D.M., Chng S.C., Ong S.,
RA   Yi L.K., Boussata S., Goh G.H., Afink G.B., Lim C.Y., Dunn N.R., Solter D.,
RA   Knowles B.B., Reversade B.;
RT   "ELABELA deficiency promotes preeclampsia and cardiovascular malformations
RT   in mice.";
RL   Science 357:707-713(2017).
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 (PubMed:28854362, PubMed:28890073,
CC       PubMed:28663440). May promote angioblast migration toward the embryonic
CC       midline, i.e. the position of the future vessel formation, during
CC       vasculogenesis (By similarity). Promotes sinus venosus (SV)-derived
CC       endothelial cells migration into the developing heart to promote
CC       coronary blood vessel development (PubMed:28890073). 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
CC       (PubMed:28371822). {ECO:0000250|UniProtKB:P79960,
CC       ECO:0000250|UniProtKB:Q7SZP9, ECO:0000269|PubMed:28371822,
CC       ECO:0000269|PubMed:28663440, ECO:0000269|PubMed:28854362,
CC       ECO:0000269|PubMed:28890073}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35414};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P79960}. Note=After
CC       exposure to apelin (APLN) or apelin receptor early endogenous ligand
CC       (APELA), 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:Q9JHG3}.
CC   -!- TISSUE SPECIFICITY: Expressed in coronary endothelial cells (at protein
CC       level) (PubMed:28890073). Expressed in the embryo, allantoic and
CC       endothelial precursor cells of the yolk sac at 8 days post-coitum (dpc)
CC       (PubMed:28663440). Expressed in the secondary heart field and somite at
CC       8.25 dpc (PubMed:28854362). Expressed in fetal allantoic endothelial
CC       cells at 9 dpc (PubMed:28663440). Expressed in the allantoid and the
CC       invading fetal vasculature of the placenta at 9.5 dpc
CC       (PubMed:28854362). Expressed in endothelial cells adjacent to
CC       syncytiotrophoblast cells at 10.5 dpc (PubMed:28663440). Expressed
CC       weakly in the embryonic heart at 11.5 dpc (PubMed:26611206). Expressed
CC       in the adult heart (PubMed:26611206). Expressed in endothelial cells
CC       and cardiomyocytes and weakly expressed in fibroblasts
CC       (PubMed:10473142, PubMed:26611206). {ECO:0000269|PubMed:10473142,
CC       ECO:0000269|PubMed:26611206, ECO:0000269|PubMed:28663440,
CC       ECO:0000269|PubMed:28854362, ECO:0000269|PubMed:28890073}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from embryonic 8 days post-coitum (dpc)
CC       throughout the subsequent stages of formation of the cardiovascular
CC       system (PubMed:10473142). {ECO:0000269|PubMed:10473142}.
CC   -!- INDUCTION: Up-regulated following myocardial infarction (MI) (at
CC       protein level) (PubMed:26611206). {ECO:0000269|PubMed:26611206}.
CC   -!- DISRUPTION PHENOTYPE: Mice lacking APLNR are not represented at
CC       Mendelian ratios. Mutant embryos exhibit incomplete penetrance of
CC       embryonic lethality (PubMed:28854362, PubMed:28663440). Mutant embryos
CC       display improper establishment of the fetal-maternal circulation, such
CC       as underdeveloped yolk sac vasculature, embryonic vascular
CC       malformations and impaired cardiac tube looping at 10.5 dpc
CC       (PubMed:28854362, PubMed:28663440). Mice heart of embryos show reduced
CC       coronary vessel growth at 13.5 dpc (PubMed:28890073). The heart of
CC       mutant adult mice induced by pressure overload display no improvement
CC       in cardiac dysfunction, hypertrophy and fibrosis in response to peptide
CC       hormone APELA treatment (PubMed:28371822). Conditional knockout in
CC       heart endothelial cells leads to delayed progression of vessel growth
CC       onto the heart and reduced branching of the developing coronary plexus
CC       in both the subepicardial and intramyocardial layers at 13.5 and 15.5
CC       dpc (PubMed:28890073). Conditional endothelial-specific knockout adult
CC       mice, despite severe embryonic coronary vessel defects recover normal
CC       cardiac functions; endocardial-derived coronary vessels expand to
CC       rescue defective sinus venosus development in a APELA-APLNR-independent
CC       manner (PubMed:28890073). Double knockout mice of APLNR and APELA genes
CC       exhibited the same penetrance and embryonic lethality as single APELA
CC       knockout mice (PubMed:28854362). {ECO:0000269|PubMed:28371822,
CC       ECO:0000269|PubMed:28663440, ECO:0000269|PubMed:28854362,
CC       ECO:0000269|PubMed:28890073}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AJ007612; CAB50696.1; -; mRNA.
DR   EMBL; AK075706; BAC35901.1; -; mRNA.
DR   EMBL; AK133580; BAE21731.1; -; mRNA.
DR   EMBL; AK157582; BAE34128.1; -; mRNA.
DR   EMBL; BC039224; AAH39224.1; -; mRNA.
DR   CCDS; CCDS16201.1; -.
DR   RefSeq; NP_035914.1; NM_011784.3.
DR   AlphaFoldDB; Q9WV08; -.
DR   SMR; Q9WV08; -.
DR   STRING; 10090.ENSMUSP00000053638; -.
DR   GlyGen; Q9WV08; 2 sites.
DR   iPTMnet; Q9WV08; -.
DR   PhosphoSitePlus; Q9WV08; -.
DR   SwissPalm; Q9WV08; -.
DR   MaxQB; Q9WV08; -.
DR   PaxDb; Q9WV08; -.
DR   PRIDE; Q9WV08; -.
DR   ProteomicsDB; 296374; -.
DR   Antibodypedia; 14066; 539 antibodies from 36 providers.
DR   DNASU; 23796; -.
DR   Ensembl; ENSMUST00000057019; ENSMUSP00000053638; ENSMUSG00000044338.
DR   GeneID; 23796; -.
DR   KEGG; mmu:23796; -.
DR   UCSC; uc008kkb.2; mouse.
DR   CTD; 187; -.
DR   MGI; MGI:1346086; Aplnr.
DR   VEuPathDB; HostDB:ENSMUSG00000044338; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244888; -.
DR   HOGENOM; CLU_009579_8_1_1; -.
DR   InParanoid; Q9WV08; -.
DR   OMA; TVMLTCY; -.
DR   OrthoDB; 788659at2759; -.
DR   PhylomeDB; Q9WV08; -.
DR   TreeFam; TF330024; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   BioGRID-ORCS; 23796; 2 hits in 73 CRISPR screens.
DR   PRO; PR:Q9WV08; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9WV08; protein.
DR   Bgee; ENSMUSG00000044338; Expressed in renal medulla interstitium and 211 other tissues.
DR   ExpressionAtlas; Q9WV08; baseline and differential.
DR   Genevisible; Q9WV08; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
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:0007512; P:adult heart development; IMP:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0035904; P:aorta development; IMP:BHF-UCL.
DR   GO; GO:0060183; P:apelin receptor signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0003171; P:atrioventricular valve development; IMP:BHF-UCL.
DR   GO; GO:0001568; P:blood vessel development; IBA:GO_Central.
DR   GO; GO:0060976; P:coronary vasculature development; IMP:UniProtKB.
DR   GO; GO:0003272; P:endocardial cushion formation; IMP:BHF-UCL.
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:0001947; P:heart looping; IMP:BHF-UCL.
DR   GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
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; IMP:UniProtKB.
DR   GO; GO:0031065; P:positive regulation of histone deacetylation; IMP:BHF-UCL.
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; ISO:MGI.
DR   GO; GO:1903596; P:regulation of gap junction assembly; IMP:BHF-UCL.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:BHF-UCL.
DR   GO; GO:0035886; P:vascular associated smooth muscle cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0001944; P:vasculature development; IMP:BHF-UCL.
DR   GO; GO:0001570; P:vasculogenesis; IMP:UniProtKB.
DR   GO; GO:0060841; P:venous blood vessel development; IMP:BHF-UCL.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
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   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..377
FT                   /note="Apelin receptor"
FT                   /id="PRO_0000069175"
FT   TOPO_DOM        1..24
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..49
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        50..64
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..89
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        90..98
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..123
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        124..142
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..164
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..198
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..269
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        270..282
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..306
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        307..377
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          334..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..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"
SQ   SEQUENCE   377 AA;  42266 MW;  AA443A7800A24E0B CRC64;
     MEDDGYNYYG ADNQSECDYA DWKPSGALIP AIYMLVFLLG TTGNGLVLWT VFRTSREKRR
     SADIFIASLA VADLTFVVTL PLWATYTYRE FDWPFGTFSC KLSSYLIFVN MYASVFCLTG
     LSFDRYLAIV RPVANARLRL RVSGAVATAV LWVLAALLAV PVMVFRSTDA SENGTKIQCY
     MDYSMVATSN SEWAWEVGLG VSSTAVGFVV PFTIMLTCYF FIAQTIAGHF RKERIEGLRK
     RRRLLSIIVV LVVTFALCWM PYHLVKTLYM LGSLLHWPCD FDIFLMNVFP YCTCISYVNS
     CLNPFLYAFF DPRFRQACTS MLCCDQSGCK GTPHSSSAEK SASYSSGHSQ GPGPNMGKGG
     EQMHEKSIPY SQETLVD
 
 
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