ID ADR1_HUMAN Reviewed; 375 AA. AC Q96A54; B3KMB0; Q53HS7; Q53YY6; Q9Y360; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=Adiponectin receptor protein 1; DE AltName: Full=Progestin and adipoQ receptor family member I; GN Name=ADIPOR1; Synonyms=PAQR1 {ECO:0000303|PubMed:16044242}, TESBP1A; GN ORFNames=CGI-45; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=16044242; DOI=10.1007/s00239-004-0375-2; RA Tang Y.T., Hu T., Arterburn M., Boyle B., Bright J.M., Emtage P.C., RA Funk W.D.; RT "PAQR proteins: a novel membrane receptor family defined by an ancient RT 7-transmembrane pass motif."; RL J. Mol. Evol. 61:372-380(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Sugihara T.; RT "Cloning and characterization of TESBP1A."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Adipose tissue; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Skin; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP TOPOLOGY. 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., RA Ohteki T., Uchida S., Takekawa S., Waki H., Tsuno N.H., Shibata Y., RA Terauchi Y., Froguel P., Tobe K., Koyasu S., Taira K., Kitamura T., RA Shimizu T., Nagai R., Kadowaki T.; RT "Cloning of adiponectin receptors that mediate antidiabetic metabolic RT effects."; RL Nature 423:762-769(2003). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 89-375 IN COMPLEX WITH ZINC, RP FUNCTION, TOPOLOGY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP 161-MET--LEU-167; HIS-191; ASP-208; 229-TYR--SER-231; RP 291-PHE--VAL-297; HIS-337 AND HIS-341. RX PubMed=25855295; DOI=10.1038/nature14301; RA Tanabe H., Fujii Y., Okada-Iwabu M., Iwabu M., Nakamura Y., Hosaka T., RA Motoyama K., Ikeda M., Wakiyama M., Terada T., Ohsawa N., Hato M., RA Ogasawara S., Hino T., Murata T., Iwata S., Hirata K., Kawano Y., RA Yamamoto M., Kimura-Someya T., Shirouzu M., Yamauchi T., Kadowaki T., RA Yokoyama S.; RT "Crystal structures of the human adiponectin receptors."; RL Nature 520:312-316(2015). CC -!- FUNCTION: Receptor for ADIPOQ, an essential hormone secreted by CC adipocytes that regulates glucose and lipid metabolism CC (PubMed:25855295, PubMed:12802337). Required for normal glucose CC and fat homeostasis and for maintaining a normal body weight. CC ADIPOQ-binding activates a signaling cascade that leads to CC increased AMPK activity, and ultimately to increased fatty acid CC oxidation, increased glucose uptake and decreased gluconeogenesis. CC Has high affinity for globular adiponectin and low affinity for CC full-length adiponectin (By similarity). CC {ECO:0000250|UniProtKB:Q91VH1, ECO:0000269|PubMed:12802337, CC ECO:0000269|PubMed:25855295}. CC -!- SUBUNIT: May form homooligomers and heterooligomers with ADIPOR2. CC {ECO:0000269|PubMed:12802337}. CC -!- INTERACTION: CC Self; NbExp=3; IntAct=EBI-1632076, EBI-1632076; CC Q9UKG1:APPL1; NbExp=6; IntAct=EBI-1632076, EBI-741243; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12802337, CC ECO:0000269|PubMed:25855295}; Multi-pass membrane protein CC {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:25855295}. CC Note=Localized to the cell membrane and intracellular organelles. CC {ECO:0000269|PubMed:12802337}. CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:16044242). Highly CC expressed in heart and skeletal muscle (PubMed:12802337). CC Expressed at intermediate level in brain, spleen, kidney, liver, CC placenta, lung and peripheral blood leukocytes (PubMed:12802337). CC Weakly expressed in colon, thymus and small intestine CC (PubMed:12802337). {ECO:0000269|PubMed:12802337, CC ECO:0000269|PubMed:16044242}. 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 CC helices are not kinked or tilted relative to the plane of the CC membrane. {ECO:0000269|PubMed:12802337}. CC -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD34040.1; Type=Frameshift; Positions=369; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/ADIPOR1ID44512ch1q32.html"; 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; AY424279; AAR08367.1; -; mRNA. DR EMBL; AF125179; AAQ13552.1; -; mRNA. DR EMBL; AF151803; AAD34040.1; ALT_FRAME; mRNA. DR EMBL; AK001484; BAG50922.1; -; mRNA. DR EMBL; AK222503; BAD96223.1; -; mRNA. DR EMBL; CH471067; EAW91450.1; -; Genomic_DNA. DR EMBL; BC001594; AAH01594.1; -; mRNA. DR EMBL; BC010743; AAH10743.1; -; mRNA. DR CCDS; CCDS1430.1; -. DR RefSeq; NP_001277482.1; NM_001290553.1. DR RefSeq; NP_001277486.1; NM_001290557.1. DR RefSeq; NP_001277558.1; NM_001290629.1. DR RefSeq; NP_057083.2; NM_015999.5. DR UniGene; Hs.5298; -. DR UniGene; Hs.713729; -. DR PDB; 3WXV; X-ray; 2.90 A; A=89-375. DR PDBsum; 3WXV; -. DR ProteinModelPortal; Q96A54; -. DR SMR; Q96A54; 89-373. DR BioGrid; 119283; 22. DR DIP; DIP-48622N; -. DR IntAct; Q96A54; 7. DR STRING; 9606.ENSP00000341785; -. DR GuidetoPHARMACOLOGY; 649; -. DR TCDB; 1.C.113.1.9; 1.c.113 the hly iii (hly iii) family. DR PhosphoSite; Q96A54; -. DR BioMuta; ADIPOR1; -. DR DMDM; 38372248; -. DR MaxQB; Q96A54; -. DR PaxDb; Q96A54; -. DR PRIDE; Q96A54; -. DR DNASU; 51094; -. DR Ensembl; ENST00000340990; ENSP00000341785; ENSG00000159346. DR GeneID; 51094; -. DR KEGG; hsa:51094; -. DR UCSC; uc001gyq.5; human. DR CTD; 51094; -. DR GeneCards; ADIPOR1; -. DR HGNC; HGNC:24040; ADIPOR1. DR MIM; 607945; gene. DR neXtProt; NX_Q96A54; -. DR PharmGKB; PA134861801; -. DR eggNOG; KOG0748; Eukaryota. DR eggNOG; COG1272; LUCA. DR GeneTree; ENSGT00530000062926; -. DR HOGENOM; HOG000197115; -. DR HOVERGEN; HBG013916; -. DR InParanoid; Q96A54; -. DR KO; K07297; -. DR OMA; EQACPVP; -. DR OrthoDB; EOG7BS49P; -. DR PhylomeDB; Q96A54; -. DR TreeFam; TF313640; -. DR ChiTaRS; ADIPOR1; human. DR GeneWiki; ADIPOR1; -. DR GenomeRNAi; 51094; -. DR NextBio; 53785; -. DR PRO; PR:Q96A54; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; Q96A54; -. DR CleanEx; HS_ADIPOR1; -. DR ExpressionAtlas; Q96A54; baseline and differential. DR Genevisible; Q96A54; HS. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0097003; F:adipokinetic hormone receptor activity; IDA:UniProtKB. DR GO; GO:0055100; F:adiponectin binding; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL. DR GO; GO:0004872; F:receptor activity; IBA:GO_Central. DR GO; GO:0033211; P:adiponectin-activated signaling pathway; IDA:UniProtKB. DR GO; GO:0019395; P:fatty acid oxidation; IDA:UniProtKB. DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:GOC. DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB. DR GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0033210; P:leptin-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl. DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl. DR GO; GO:0046427; P:positive regulation of JAK-STAT cascade; IEA:Ensembl. DR GO; GO:0010906; P:regulation of glucose metabolic process; ISS:UniProtKB. DR GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB. DR InterPro; IPR004254; AdipoR/HlyIII-related. DR PANTHER; PTHR20855; PTHR20855; 1. DR Pfam; PF03006; HlyIII; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Fatty acid metabolism; KW Lipid metabolism; Membrane; Metal-binding; Receptor; KW Reference proteome; Transmembrane; Transmembrane helix; Zinc. FT CHAIN 1 375 Adiponectin receptor protein 1. FT /FTId=PRO_0000218827. FT TOPO_DOM 1 136 Cytoplasmic. FT {ECO:0000269|PubMed:25855295}. FT TRANSMEM 137 157 Helical; Name=1. FT {ECO:0000269|PubMed:25855295}. FT TOPO_DOM 158 170 Extracellular. FT {ECO:0000269|PubMed:25855295}. FT TRANSMEM 171 191 Helical; Name=2. FT {ECO:0000269|PubMed:25855295}. FT TOPO_DOM 192 203 Cytoplasmic. FT {ECO:0000269|PubMed:25855295}. FT TRANSMEM 204 224 Helical; Name=3. FT {ECO:0000269|PubMed:25855295}. FT TOPO_DOM 225 234 Extracellular. FT {ECO:0000269|PubMed:25855295}. FT TRANSMEM 235 255 Helical; Name=4. FT {ECO:0000269|PubMed:25855295}. FT TOPO_DOM 256 264 Cytoplasmic. FT {ECO:0000269|PubMed:25855295}. FT TRANSMEM 265 285 Helical; Name=5. FT {ECO:0000269|PubMed:25855295}. FT TOPO_DOM 286 298 Extracellular. FT {ECO:0000269|PubMed:25855295}. FT TRANSMEM 299 319 Helical; Name=6. FT {ECO:0000269|PubMed:25855295}. FT TOPO_DOM 320 337 Cytoplasmic. FT {ECO:0000269|PubMed:25855295}. FT TRANSMEM 338 358 Helical; Name=7. FT {ECO:0000269|PubMed:25855295}. FT TOPO_DOM 359 375 Extracellular. FT {ECO:0000269|PubMed:25855295}. FT METAL 191 191 Zinc. {ECO:0000269|PubMed:25855295}. FT METAL 337 337 Zinc. {ECO:0000269|PubMed:25855295}. FT METAL 341 341 Zinc. {ECO:0000269|PubMed:25855295}. FT MUTAGEN 161 167 MYFMAPL->SGSSGGS: Decreases activation of FT AMPK in response to ADIPOQ binding; when FT associated with 229-G--G-231 and 291-S-- FT S-297. {ECO:0000269|PubMed:25855295}. FT MUTAGEN 191 191 H->A: Decreases activation of AMPK in FT response to ADIPOQ binding; when FT associated with A-208; A-337 and A-341. FT {ECO:0000269|PubMed:25855295}. FT MUTAGEN 208 208 D->A: Decreases activation of AMPK in FT response to ADIPOQ binding; when FT associated with A-191; A-337 and A-341. FT {ECO:0000269|PubMed:25855295}. FT MUTAGEN 229 231 YCS->GGG: Decreases activation of AMPK in FT response to ADIPOQ binding; when FT associated with 161-S--S-167 and 291-S-- FT S-297. {ECO:0000269|PubMed:25855295}. FT MUTAGEN 291 297 FVKATTV->SSSGGGS: Decreases activation of FT AMPK in response to ADIPOQ binding; when FT associated with 161-S--S-167 and 229-G-- FT G-231. {ECO:0000269|PubMed:25855295}. FT MUTAGEN 337 337 H->A: Decreases activation of AMPK in FT response to ADIPOQ binding; when FT associated with A-191; A-208 and A-341. FT {ECO:0000269|PubMed:25855295}. FT MUTAGEN 341 341 H->A: Decreases activation of AMPK in FT response to ADIPOQ binding; when FT associated with A-191; A-208 and A-337. FT {ECO:0000269|PubMed:25855295}. FT CONFLICT 183 183 C -> W (in Ref. 4; BAG50922). FT {ECO:0000305}. FT CONFLICT 340 340 F -> Y (in Ref. 5; BAD96223). FT {ECO:0000305}. FT HELIX 97 99 {ECO:0000244|PDB:3WXV}. FT HELIX 102 104 {ECO:0000244|PDB:3WXV}. FT HELIX 121 126 {ECO:0000244|PDB:3WXV}. FT HELIX 127 129 {ECO:0000244|PDB:3WXV}. FT HELIX 135 157 {ECO:0000244|PDB:3WXV}. FT HELIX 169 192 {ECO:0000244|PDB:3WXV}. FT HELIX 193 195 {ECO:0000244|PDB:3WXV}. FT HELIX 198 227 {ECO:0000244|PDB:3WXV}. FT TURN 228 230 {ECO:0000244|PDB:3WXV}. FT HELIX 232 252 {ECO:0000244|PDB:3WXV}. FT STRAND 257 260 {ECO:0000244|PDB:3WXV}. FT HELIX 261 263 {ECO:0000244|PDB:3WXV}. FT HELIX 264 275 {ECO:0000244|PDB:3WXV}. FT HELIX 276 278 {ECO:0000244|PDB:3WXV}. FT HELIX 279 288 {ECO:0000244|PDB:3WXV}. FT HELIX 291 295 {ECO:0000244|PDB:3WXV}. FT HELIX 305 319 {ECO:0000244|PDB:3WXV}. FT TURN 320 325 {ECO:0000244|PDB:3WXV}. FT STRAND 329 334 {ECO:0000244|PDB:3WXV}. FT HELIX 336 364 {ECO:0000244|PDB:3WXV}. SQ SEQUENCE 375 AA; 42616 MW; 1CC0300A7D178EB0 CRC64; MSSHKGSVVA QGNGAPASNR EADTVELAEL GPLLEEKGKR VIANPPKAEE EQTCPVPQEE 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 DDTLL //