{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q8BQS5","secondaryAccessions":["Q8CA45","Q8CID6"],"uniProtkbId":"PAQR2_MOUSE","entryAudit":{"firstPublicDate":"2003-11-14","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2003-11-14","entryVersion":149,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Mus musculus","commonName":"Mouse","taxonId":10090,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12802337"}],"value":"Adiponectin receptor protein 2"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q86V24"}],"value":"Progestin and adipoQ receptor family member 2"}},{"fullName":{"value":"Progestin and adipoQ receptor family member II"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"MGI","id":"MGI:93830"}],"value":"Adipor2"},"synonyms":[{"value":"D6Ucla1e"},{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q86V24"}],"value":"Parq2"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12802337"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17068142"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17268472"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17327425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24742672"}],"value":"Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:17068142, PubMed:17268472, PubMed:17327425, PubMed:24742672). Required for normal body fat and glucose homeostasis (PubMed:17068142, PubMed:17268472, PubMed:17327425, PubMed:24742672). ADIPOQ-binding activates a signaling cascade that leads to increased PPARA activity, and ultimately to increased fatty acid oxidation and glucose uptake (PubMed:12802337, PubMed:17268472, PubMed:24742672). Has intermediate affinity for globular and full-length adiponectin (PubMed:12802337). Required for normal revascularization after chronic ischemia caused by severing of blood vessels (PubMed:24742672)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q86V24"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19661063"}],"value":"May form homooligomers and heterooligomers with ADIPOR1 (By similarity). Interacts with APPL2 (via BAR domain); ADIPOQ dissociates this interaction (PubMed:19661063)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q86V24"}],"value":"Localized to the cell membrane and intracellular organelles"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q86V24"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q86V24"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q8BQS5-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q8BQS5-2"],"sequenceIds":["VSP_008887","VSP_008888"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12802337"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17327425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24742672"}],"value":"Detected in liver and quadriceps muscle (at protein level) (PubMed:17327425). Highly expressed in liver (PubMed:12802337). Highly expressed in white adipose tissue, and at intermediate levels in brown adipose tissue (PubMed:24742672). Expressed at intermediate level in heart, kidney, lung and skeletal muscle. Weakly expressed in brain, spleen and testis"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q86V24"}],"value":"The N-terminus is cytoplasmic and the C-terminus is extracellular, contrary to what is observed for G protein-coupled receptors. Unlike G protein-coupled receptors, transmembrane helices are not kinked or tilted relative to the plane of the membrane"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17068142"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17268472"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17327425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24742672"}],"value":"Mutant mice are viable and fertile, and display increased glucose tolerance (PubMed:17068142, PubMed:17268472, PubMed:17327425, PubMed:24742672). On a high fat diet, they have lower fasting insulin levels than wild-type (PubMed:17327425, PubMed:24742672). Mutant mice have lower plasma cholesterol levels on a high fat diet, and possibly also on normal chow (PubMed:17068142, PubMed:17327425). The precise phenotype may depend on the experimental details and on genotype. Male and female mutant mice are somewhat leaner than wild-type on standard chow and do not display increased weight gain on a high fat diet (PubMed:17327425, PubMed:24742672). Mutant mice have normal body weight on standard chow, but decreased weight gain on a high-fat diet (PubMed:17068142). Female mutant mice display lower total body fat than wild-type on a high fat diet (PubMed:17327425). Both male and female mice have reduced levels of white and brown adipose tissue relative to wild-type (PubMed:17327425). Mutant male mice display decreased testis weight, atrophy of the seminiferous tubules and aspermia (PubMed:17327425). Both male and female mice display increased brain weight relative to wild-type (PubMed:17327425). Mutant mice have increased locomotor activity and increased energy expenditure on a high fat diet (PubMed:17327425). Mutant mice display impaired revascularization, limb retraction, atrophy and necrosis in response to limb ischemia caused by severing the femoral artery (PubMed:24742672). Hepatocytes from mice lacking both Adipor1 and Adipor2 show loss of adiponectin binding and lack of adiponectin-mediated activation of AMPK and Ppara (PubMed:17268472). Mice lacking both Adipor1 and Adipor2 display elevated glucose and insulin levels in blood plasma, indicative of glucose intolerance and insulin resistance (PubMed:17268472)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the ADIPOR family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":386,"modifier":"EXACT"}},"description":"Adiponectin receptor protein 2","featureId":"PRO_0000218830"},{"type":"Topological domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q86V24"}]},{"type":"Transmembrane","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"Helical; 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