PAQR1_MOUSE
ID PAQR1_MOUSE Reviewed; 375 AA.
AC Q91VH1; Q9CZA0;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Adiponectin receptor protein 1 {ECO:0000303|PubMed:12802337};
DE AltName: Full=Progestin and adipoQ receptor family member 1 {ECO:0000250|UniProtKB:Q96A54};
DE AltName: Full=Progestin and adipoQ receptor family member I;
GN Name=Adipor1 {ECO:0000312|MGI:MGI:1919924};
GN Synonyms=Parq1 {ECO:0000250|UniProtKB:Q86V24,
GN ECO:0000250|UniProtKB:Q96A54};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12802337; DOI=10.1038/nature01705;
RA Yamauchi T., Kamon J., Ito Y., Tsuchida A., Yokomizo T., Kita S.,
RA Sugiyama T., Miyagishi M., Hara K., Tsunoda M., Murakami K., Ohteki T.,
RA Uchida S., Takekawa S., Waki H., Tsuno N.H., Shibata Y., Terauchi Y.,
RA Froguel P., Tobe K., Koyasu S., Taira K., Kitamura T., Shimizu T.,
RA Nagai R., Kadowaki T.;
RT "Cloning of adiponectin receptors that mediate antidiabetic metabolic
RT effects.";
RL Nature 423:762-769(2003).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17327425; DOI=10.2337/db06-1432;
RA Bjursell M., Ahnmark A., Bohlooly-Y M., William-Olsson L., Rhedin M.,
RA Peng X.R., Ploj K., Gerdin A.K., Arnerup G., Elmgren A., Berg A.L.,
RA Oscarsson J., Linden D.;
RT "Opposing effects of adiponectin receptors 1 and 2 on energy metabolism.";
RL Diabetes 56:583-593(2007).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17268472; DOI=10.1038/nm1557;
RA Yamauchi T., Nio Y., Maki T., Kobayashi M., Takazawa T., Iwabu M.,
RA Okada-Iwabu M., Kawamoto S., Kubota N., Kubota T., Ito Y., Kamon J.,
RA Tsuchida A., Kumagai K., Kozono H., Hada Y., Ogata H., Tokuyama K.,
RA Tsunoda M., Ide T., Murakami K., Awazawa M., Takamoto I., Froguel P.,
RA Hara K., Tobe K., Nagai R., Ueki K., Kadowaki T.;
RT "Targeted disruption of AdipoR1 and AdipoR2 causes abrogation of
RT adiponectin binding and metabolic actions.";
RL Nat. Med. 13:332-339(2007).
RN [6]
RP INTERACTION WITH APPL2 AND APPL1.
RX PubMed=19661063; DOI=10.1074/jbc.m109.010355;
RA Wang C., Xin X., Xiang R., Ramos F.J., Liu M., Lee H.J., Chen H., Mao X.,
RA Kikani C.K., Liu F., Dong L.Q.;
RT "Yin-Yang regulation of adiponectin signaling by APPL isoforms in muscle
RT cells.";
RL J. Biol. Chem. 284:31608-31615(2009).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=24742672; DOI=10.1074/jbc.m114.548115;
RA Parker-Duffen J.L., Nakamura K., Silver M., Zuriaga M.A., MacLauchlan S.,
RA Aprahamian T.R., Walsh K.;
RT "Divergent roles for adiponectin receptor 1 (AdipoR1) and AdipoR2 in
RT mediating revascularization and metabolic dysfunction in vivo.";
RL J. Biol. Chem. 289:16200-16213(2014).
CC -!- FUNCTION: Receptor for ADIPOQ, an essential hormone secreted by
CC adipocytes that regulates glucose and lipid metabolism
CC (PubMed:17327425, PubMed:17268472, PubMed:24742672). Required for
CC normal glucose and fat homeostasis and for maintaining a normal body
CC weight (PubMed:17327425, PubMed:24742672). ADIPOQ-binding activates a
CC signaling cascade that leads to increased AMPK activity, and ultimately
CC to increased fatty acid oxidation, increased glucose uptake and
CC decreased gluconeogenesis (PubMed:12802337, PubMed:17327425,
CC PubMed:17268472, PubMed:24742672). Has high affinity for globular
CC adiponectin and low affinity for full-length adiponectin
CC (PubMed:12802337). {ECO:0000269|PubMed:12802337,
CC ECO:0000269|PubMed:17268472, ECO:0000269|PubMed:17327425,
CC ECO:0000269|PubMed:24742672}.
CC -!- SUBUNIT: May form homooligomers and heterooligomers with ADIPOR2 (By
CC similarity). Interacts with APPL2 (via BAR domain); hinders the
CC accessibility of APPL1 to ADIPOR1; negatively regulates adiponectin
CC signaling; ADIPOQ dissociates this interaction and facilitates the
CC recruitment of APPL1 to ADIPOR1 (PubMed:19661063). Interacts with
CC APPL1; ADIPOQ enhances this interaction; inhibites adiponectin-
CC stimulated binding of APPL2 to ADIPOR1 (PubMed:19661063).
CC {ECO:0000250|UniProtKB:Q96A54, ECO:0000269|PubMed:19661063}.
CC -!- INTERACTION:
CC Q91VH1; Q9UKG1: APPL1; Xeno; NbExp=3; IntAct=EBI-992398, EBI-741243;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17268472};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96A54}.
CC Note=Localized to the cell membrane and intracellular organelles.
CC {ECO:0000250|UniProtKB:Q96A54}.
CC -!- TISSUE SPECIFICITY: Detected in brain and quadriceps muscle (at protein
CC level) (PubMed:17327425). Widely expressed (PubMed:12802337). Expressed
CC in heart, kidney, liver, lung, skeletal muscle, white adipose tissue,
CC brown adipose tissue, aorta and spleen (PubMed:12802337,
CC PubMed:24742672). Weakly expressed in brain and testis
CC (PubMed:12802337). {ECO:0000269|PubMed:12802337,
CC ECO:0000269|PubMed:17268472, ECO:0000269|PubMed:17327425,
CC ECO:0000269|PubMed:24742672}.
CC -!- DOMAIN: The N-terminus is cytoplasmic and the C-terminus is
CC extracellular, contrary to what is observed for G-protein coupled
CC receptors. Unlike G-protein coupled receptors, transmembrane helices
CC are not kinked or tilted relative to the plane of the membrane.
CC {ECO:0000250|UniProtKB:Q96A54}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are viable and fertile, but display
CC defects in glucose and lipid homeostasis. The precise phenotype may
CC depend on experimental details and genetic background. Mutant mice have
CC normal body weight, but increased plasma glucose and insulin levels
CC (PubMed:17268472). Mutant male mice, but not female mice, display
CC increased body weight gain on standard chow, in spite of similar food
CC intake as wild-type (PubMed:17327425). Mutant mice display increased
CC body weight, both on standard chow and on high fat and high sucrose
CC diet (PubMed:24742672). Male mice have increased total body fat mass
CC after 15 weeks, and have increased weights of both white and brown
CC adipose tissue (PubMed:17327425, PubMed:24742672). Mutant mice have
CC impaired glucose tolerance (PubMed:24742672). Male mice have decreased
CC glucose tolerance, but no significant change in the insulin response
CC (PubMed:17327425). Female mice display increased fasting glucose
CC levels, but unchanged fasting insulin levels (PubMed:17327425). Male
CC and female mice display increased levels of liver triglycerides
CC relative to wild-type (PubMed:17327425, PubMed:24742672). Male mice
CC display decreased locomotor activity and decreased energy expenditure
CC relative to wild-type (PubMed:17327425). Mutant mice display normal
CC revascularization after chronic limb ischemia caused by severing of
CC blood vessels (PubMed:24742672). Hepatocytes from mice lacking both
CC Adipor1 and Adipor2 show loss of adiponectin binding and lack of
CC adiponectin-mediated activation of AMPK and Ppara (PubMed:17268472).
CC Mice lacking both Adipor1 and Adipor2 display elevated glucose and
CC insulin levels in blood plasma, indicative of glucose intolerance and
CC insulin resistance (PubMed:17268472). {ECO:0000269|PubMed:17268472,
CC ECO:0000269|PubMed:17327425, ECO:0000269|PubMed:24742672}.
CC -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB28509.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB28509.1; Type=Frameshift; Note=This frameshift abolishes the stop codon.; Evidence={ECO:0000305};
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DR EMBL; AK012847; BAB28509.1; ALT_SEQ; mRNA.
DR EMBL; BC014875; AAH14875.1; -; mRNA.
DR CCDS; CCDS15309.1; -.
DR RefSeq; NP_001292998.1; NM_001306069.1.
DR RefSeq; NP_082596.2; NM_028320.4.
DR AlphaFoldDB; Q91VH1; -.
DR SMR; Q91VH1; -.
DR IntAct; Q91VH1; 2.
DR STRING; 10090.ENSMUSP00000107856; -.
DR iPTMnet; Q91VH1; -.
DR PhosphoSitePlus; Q91VH1; -.
DR MaxQB; Q91VH1; -.
DR PaxDb; Q91VH1; -.
DR PRIDE; Q91VH1; -.
DR ProteomicsDB; 287884; -.
DR Antibodypedia; 34534; 420 antibodies from 37 providers.
DR Ensembl; ENSMUST00000027727; ENSMUSP00000027727; ENSMUSG00000026457.
DR Ensembl; ENSMUST00000112237; ENSMUSP00000107856; ENSMUSG00000026457.
DR GeneID; 72674; -.
DR KEGG; mmu:72674; -.
DR UCSC; uc007crx.1; mouse.
DR CTD; 51094; -.
DR MGI; MGI:1919924; Adipor1.
DR VEuPathDB; HostDB:ENSMUSG00000026457; -.
DR eggNOG; KOG0748; Eukaryota.
DR GeneTree; ENSGT00940000154563; -.
DR HOGENOM; CLU_023075_1_0_1; -.
DR InParanoid; Q91VH1; -.
DR OMA; DYCGIAM; -.
DR OrthoDB; 1524940at2759; -.
DR PhylomeDB; Q91VH1; -.
DR TreeFam; TF313640; -.
DR Reactome; R-MMU-163680; AMPK inhibits chREBP transcriptional activation activity.
DR BioGRID-ORCS; 72674; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Adipor1; mouse.
DR PRO; PR:Q91VH1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91VH1; protein.
DR Bgee; ENSMUSG00000026457; Expressed in blood and 266 other tissues.
DR ExpressionAtlas; Q91VH1; baseline and differential.
DR Genevisible; Q91VH1; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0097003; F:adipokinetic hormone receptor activity; ISS:UniProtKB.
DR GO; GO:0055100; F:adiponectin binding; IPI:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0033211; P:adiponectin-activated signaling pathway; IDA:MGI.
DR GO; GO:0019395; P:fatty acid oxidation; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0033210; P:leptin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; ISO:MGI.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IMP:UniProtKB.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP:UniProtKB.
DR InterPro; IPR004254; AdipoR/HlyIII-related.
DR PANTHER; PTHR20855; PTHR20855; 1.
DR Pfam; PF03006; HlyIII; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Fatty acid metabolism; Lipid metabolism; Membrane;
KW Metal-binding; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..375
FT /note="Adiponectin receptor protein 1"
FT /id="PRO_0000218828"
FT TOPO_DOM 1..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT TRANSMEM 137..157
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT TOPO_DOM 158..170
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT TRANSMEM 171..191
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT TOPO_DOM 192..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT TRANSMEM 204..224
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT TOPO_DOM 225..234
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT TRANSMEM 235..255
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT TOPO_DOM 256..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT TRANSMEM 265..285
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT TOPO_DOM 286..298
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT TRANSMEM 299..319
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT TOPO_DOM 320..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT TRANSMEM 338..358
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT TOPO_DOM 359..375
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96A54"
SQ SEQUENCE 375 AA; 42366 MW; 0E72F81B5E9938CE CRC64;
MSSHKGSAGA QGNGAPSGNR EADTVELAEL GPLLEEKGKR AASSPAKAEE DQACPVPQEE
EEEVRVLTLP LQAHHAMEKM EEFVYKVWEG RWRVIPYDVL PDWLKDNDYL LHGHRPPMPS
FRACFKSIFR IHTETGNIWT HLLGFVLFLF LGILTMLRPN MYFMAPLQEK VVFGMFFLGA
VLCLSFSWLF HTVYCHSEKV SRTFSKLDYS GIALLIMGSF VPWLYYSFYC SPQPRLIYLS
IVCVLGISAI IVAQWDRFAT PKHRQTRAGV FLGLGLSGVV PTMHFTIAEG FVKATTVGQM
GWFFLMAVMY ITGAGLYAAR IPERFFPGKF DIWFQSHQIF HVLVVAAAFV HFYGVSNLQE
FRYGLEGGCT DDSLL
