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Protein

Adiponectin receptor protein 1

Gene

ADIPOR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:25855295, PubMed:12802337). Required for normal glucose and fat homeostasis and for maintaining a normal body weight. ADIPOQ-binding activates a signaling cascade that leads to increased AMPK activity, and ultimately to increased fatty acid oxidation, increased glucose uptake and decreased gluconeogenesis. Has high affinity for globular adiponectin and low affinity for full-length adiponectin (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi191 – 1911Zinc1 Publication
Metal bindingi337 – 3371Zinc1 Publication
Metal bindingi341 – 3411Zinc1 Publication

GO - Molecular functioni

  • adipokinetic hormone receptor activity Source: UniProtKB
  • adiponectin binding Source: UniProtKB
  • protein kinase binding Source: BHF-UCL
  • receptor activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Adiponectin receptor protein 1
Alternative name(s):
Progestin and adipoQ receptor family member I
Gene namesi
Name:ADIPOR1
Synonyms:PAQR11 Publication, TESBP1A
ORF Names:CGI-45
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:24040. ADIPOR1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 136136Cytoplasmic1 PublicationAdd
BLAST
Transmembranei137 – 15721Helical; Name=11 PublicationAdd
BLAST
Topological domaini158 – 17013Extracellular1 PublicationAdd
BLAST
Transmembranei171 – 19121Helical; Name=21 PublicationAdd
BLAST
Topological domaini192 – 20312Cytoplasmic1 PublicationAdd
BLAST
Transmembranei204 – 22421Helical; Name=31 PublicationAdd
BLAST
Topological domaini225 – 23410Extracellular1 Publication
Transmembranei235 – 25521Helical; Name=41 PublicationAdd
BLAST
Topological domaini256 – 2649Cytoplasmic1 Publication
Transmembranei265 – 28521Helical; Name=51 PublicationAdd
BLAST
Topological domaini286 – 29813Extracellular1 PublicationAdd
BLAST
Transmembranei299 – 31921Helical; Name=61 PublicationAdd
BLAST
Topological domaini320 – 33718Cytoplasmic1 PublicationAdd
BLAST
Transmembranei338 – 35821Helical; Name=71 PublicationAdd
BLAST
Topological domaini359 – 37517Extracellular1 PublicationAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • intrinsic component of plasma membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi161 – 1677MYFMAPL → SGSSGGS: Decreases activation of AMPK in response to ADIPOQ binding; when associated with 229-G--G-231 and 291-S--S-297. 1 Publication
Mutagenesisi191 – 1911H → A: Decreases activation of AMPK in response to ADIPOQ binding; when associated with A-208; A-337 and A-341. 1 Publication
Mutagenesisi208 – 2081D → A: Decreases activation of AMPK in response to ADIPOQ binding; when associated with A-191; A-337 and A-341. 1 Publication
Mutagenesisi229 – 2313YCS → GGG: Decreases activation of AMPK in response to ADIPOQ binding; when associated with 161-S--S-167 and 291-S--S-297. 1 Publication
Mutagenesisi291 – 2977FVKATTV → SSSGGGS: Decreases activation of AMPK in response to ADIPOQ binding; when associated with 161-S--S-167 and 229-G--G-231. 1 Publication
Mutagenesisi337 – 3371H → A: Decreases activation of AMPK in response to ADIPOQ binding; when associated with A-191; A-208 and A-341. 1 Publication
Mutagenesisi341 – 3411H → A: Decreases activation of AMPK in response to ADIPOQ binding; when associated with A-191; A-208 and A-337. 1 Publication

Organism-specific databases

PharmGKBiPA134861801.

Polymorphism and mutation databases

BioMutaiADIPOR1.
DMDMi38372248.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Adiponectin receptor protein 1PRO_0000218827Add
BLAST

Proteomic databases

MaxQBiQ96A54.
PaxDbiQ96A54.
PRIDEiQ96A54.

PTM databases

PhosphoSiteiQ96A54.

Expressioni

Tissue specificityi

Widely expressed (PubMed:16044242). Highly expressed in heart and skeletal muscle (PubMed:12802337). Expressed at intermediate level in brain, spleen, kidney, liver, placenta, lung and peripheral blood leukocytes (PubMed:12802337). Weakly expressed in colon, thymus and small intestine (PubMed:12802337).2 Publications

Gene expression databases

BgeeiQ96A54.
CleanExiHS_ADIPOR1.
ExpressionAtlasiQ96A54. baseline and differential.
GenevisibleiQ96A54. HS.

Interactioni

Subunit structurei

May form homooligomers and heterooligomers with ADIPOR2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1632076,EBI-1632076
APPL1Q9UKG16EBI-1632076,EBI-741243

Protein-protein interaction databases

BioGridi119283. 14 interactions.
DIPiDIP-48622N.
IntActiQ96A54. 7 interactions.
STRINGi9606.ENSP00000341785.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WXVX-ray2.90A89-375[»]
ProteinModelPortaliQ96A54.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the ADIPOR family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1272.
GeneTreeiENSGT00530000062926.
HOGENOMiHOG000197115.
HOVERGENiHBG013916.
InParanoidiQ96A54.
KOiK07297.
OMAiEQACPVP.
OrthoDBiEOG7BS49P.
PhylomeDBiQ96A54.
TreeFamiTF313640.

Family and domain databases

InterProiIPR004254. AdipoR/HlyIII-related.
[Graphical view]
PANTHERiPTHR20855. PTHR20855. 1 hit.
PfamiPF03006. HlyIII. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96A54-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSHKGSVVA QGNGAPASNR EADTVELAEL GPLLEEKGKR VIANPPKAEE
60 70 80 90 100
EQTCPVPQEE EEEVRVLTLP LQAHHAMEKM EEFVYKVWEG RWRVIPYDVL
110 120 130 140 150
PDWLKDNDYL LHGHRPPMPS FRACFKSIFR IHTETGNIWT HLLGFVLFLF
160 170 180 190 200
LGILTMLRPN MYFMAPLQEK VVFGMFFLGA VLCLSFSWLF HTVYCHSEKV
210 220 230 240 250
SRTFSKLDYS GIALLIMGSF VPWLYYSFYC SPQPRLIYLS IVCVLGISAI
260 270 280 290 300
IVAQWDRFAT PKHRQTRAGV FLGLGLSGVV PTMHFTIAEG FVKATTVGQM
310 320 330 340 350
GWFFLMAVMY ITGAGLYAAR IPERFFPGKF DIWFQSHQIF HVLVVAAAFV
360 370
HFYGVSNLQE FRYGLEGGCT DDTLL
Length:375
Mass (Da):42,616
Last modified:December 1, 2001 - v1
Checksum:i1CC0300A7D178EB0
GO

Sequence cautioni

The sequence AAD34040.1 differs from that shown. Reason: Frameshift at position 369. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti183 – 1831C → W in BAG50922 (PubMed:14702039).Curated
Sequence conflicti340 – 3401F → Y in BAD96223 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY424279 mRNA. Translation: AAR08367.1.
AF125179 mRNA. Translation: AAQ13552.1.
AF151803 mRNA. Translation: AAD34040.1. Frameshift.
AK001484 mRNA. Translation: BAG50922.1.
AK222503 mRNA. Translation: BAD96223.1.
CH471067 Genomic DNA. Translation: EAW91450.1.
BC001594 mRNA. Translation: AAH01594.1.
BC010743 mRNA. Translation: AAH10743.1.
CCDSiCCDS1430.1.
RefSeqiNP_001277482.1. NM_001290553.1.
NP_001277486.1. NM_001290557.1.
NP_001277558.1. NM_001290629.1.
NP_057083.2. NM_015999.5.
UniGeneiHs.5298.
Hs.713729.

Genome annotation databases

EnsembliENST00000340990; ENSP00000341785; ENSG00000159346.
GeneIDi51094.
KEGGihsa:51094.
UCSCiuc001gyq.5. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY424279 mRNA. Translation: AAR08367.1.
AF125179 mRNA. Translation: AAQ13552.1.
AF151803 mRNA. Translation: AAD34040.1. Frameshift.
AK001484 mRNA. Translation: BAG50922.1.
AK222503 mRNA. Translation: BAD96223.1.
CH471067 Genomic DNA. Translation: EAW91450.1.
BC001594 mRNA. Translation: AAH01594.1.
BC010743 mRNA. Translation: AAH10743.1.
CCDSiCCDS1430.1.
RefSeqiNP_001277482.1. NM_001290553.1.
NP_001277486.1. NM_001290557.1.
NP_001277558.1. NM_001290629.1.
NP_057083.2. NM_015999.5.
UniGeneiHs.5298.
Hs.713729.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WXVX-ray2.90A89-375[»]
ProteinModelPortaliQ96A54.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119283. 14 interactions.
DIPiDIP-48622N.
IntActiQ96A54. 7 interactions.
STRINGi9606.ENSP00000341785.

Chemistry

GuidetoPHARMACOLOGYi649.

PTM databases

PhosphoSiteiQ96A54.

Polymorphism and mutation databases

BioMutaiADIPOR1.
DMDMi38372248.

Proteomic databases

MaxQBiQ96A54.
PaxDbiQ96A54.
PRIDEiQ96A54.

Protocols and materials databases

DNASUi51094.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340990; ENSP00000341785; ENSG00000159346.
GeneIDi51094.
KEGGihsa:51094.
UCSCiuc001gyq.5. human.

Organism-specific databases

CTDi51094.
GeneCardsiGC01M202909.
HGNCiHGNC:24040. ADIPOR1.
MIMi607945. gene.
neXtProtiNX_Q96A54.
PharmGKBiPA134861801.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1272.
GeneTreeiENSGT00530000062926.
HOGENOMiHOG000197115.
HOVERGENiHBG013916.
InParanoidiQ96A54.
KOiK07297.
OMAiEQACPVP.
OrthoDBiEOG7BS49P.
PhylomeDBiQ96A54.
TreeFamiTF313640.

Miscellaneous databases

ChiTaRSiADIPOR1. human.
GeneWikiiADIPOR1.
GenomeRNAii51094.
NextBioi53785.
PROiQ96A54.
SOURCEiSearch...

Gene expression databases

BgeeiQ96A54.
CleanExiHS_ADIPOR1.
ExpressionAtlasiQ96A54. baseline and differential.
GenevisibleiQ96A54. HS.

Family and domain databases

InterProiIPR004254. AdipoR/HlyIII-related.
[Graphical view]
PANTHERiPTHR20855. PTHR20855. 1 hit.
PfamiPF03006. HlyIII. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PAQR proteins: a novel membrane receptor family defined by an ancient 7-transmembrane pass motif."
    Tang Y.T., Hu T., Arterburn M., Boyle B., Bright J.M., Emtage P.C., Funk W.D.
    J. Mol. Evol. 61:372-380(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Cloning and characterization of TESBP1A."
    Sugihara T.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Adipose tissue.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung and Skin.
  8. Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, TOPOLOGY.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 89-375 IN COMPLEX WITH ZINC, FUNCTION, TOPOLOGY, SUBCELLULAR LOCATION, MUTAGENESIS OF 161-MET--LEU-167; HIS-191; ASP-208; 229-TYR--SER-231; 291-PHE--VAL-297; HIS-337 AND HIS-341.

Entry informationi

Entry nameiADR1_HUMAN
AccessioniPrimary (citable) accession number: Q96A54
Secondary accession number(s): B3KMB0
, Q53HS7, Q53YY6, Q9Y360
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: December 1, 2001
Last modified: June 24, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.