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Q91VH1 (ADR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adiponectin receptor protein 1
Gene names
Name:Adipor1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for globular and full-length adiponectin (APM1), an essential hormone secreted by adipocytes that acts as an antidiabetic. Probably involved in metabolic pathways that regulate lipid metabolism such as fatty acid oxidation. Mediates increased AMPK, PPARA ligand activity, fatty acid oxidation and glucose uptake by adiponectin. Has some high-affinity receptor for globular adiponectin but low-affinity receptor for full-length adiponectin. Ref.3

Subunit structure

May form homomultimer and heteromultimers By similarity.

Subcellular location

Membrane; Multi-pass membrane protein By similarity. Note: Localized to the cell membrane and intracellular organelles By similarity.

Tissue specificity

Widely expressed. Expressed in heart, kidney, liver, lung, skeletal muscle and spleen. Weakly expressed in brain and testis. Ref.3

Sequence similarities

Belongs to the ADIPOR family.

Sequence caution

The sequence BAB28509.1 differs from that shown. Reason: Erroneous termination at position 353. Translated as Tyr.

The sequence BAB28509.1 differs from that shown. Reason: Frameshift at position 376. This frameshift abolishes the stop codon.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionReceptor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadiponectin-activated signaling pathway

Inferred from direct assay Ref.3. Source: MGI

fatty acid oxidation

Inferred from sequence or structural similarity Ref.3. Source: UniProtKB

hormone-mediated signaling pathway

Inferred from sequence or structural similarity Ref.3. Source: UniProtKB

leptin-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of JAK-STAT cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay Ref.3. Source: MGI

   Molecular_functionadiponectin binding

Inferred from physical interaction Ref.3. Source: MGI

hormone binding

Inferred from sequence or structural similarity Ref.3. Source: UniProtKB

identical protein binding

Inferred from direct assay Ref.3. Source: MGI

protein heterodimerization activity

Inferred from physical interaction Ref.3. Source: MGI

receptor activity

Inferred from direct assay Ref.3. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APPL1Q9UKG13EBI-992398,EBI-741243From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Adiponectin receptor protein 1
PRO_0000218828

Regions

Topological domain1 – 136136Cytoplasmic Potential
Transmembrane137 – 15721Helical; Name=1; Potential
Topological domain158 – 17013Extracellular Potential
Transmembrane171 – 19121Helical; Name=2; Potential
Topological domain192 – 20918Cytoplasmic Potential
Transmembrane210 – 23021Helical; Name=3; Potential
Topological domain231 – 2355Extracellular Potential
Transmembrane236 – 25621Helical; Name=4; Potential
Topological domain257 – 26711Cytoplasmic Potential
Transmembrane268 – 28821Helical; Name=5; Potential
Topological domain289 – 2968Extracellular Potential
Transmembrane297 – 31721Helical; Name=6; Potential
Topological domain318 – 33114Cytoplasmic Potential
Transmembrane332 – 35221Helical; Name=7; Potential
Topological domain353 – 37523Extracellular Potential

Sequences

Sequence LengthMass (Da)Tools
Q91VH1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 0E72F81B5E9938CE

FASTA37542,366
        10         20         30         40         50         60 
MSSHKGSAGA QGNGAPSGNR EADTVELAEL GPLLEEKGKR AASSPAKAEE DQACPVPQEE 

        70         80         90        100        110        120 
EEEVRVLTLP LQAHHAMEKM EEFVYKVWEG RWRVIPYDVL PDWLKDNDYL LHGHRPPMPS 

       130        140        150        160        170        180 
FRACFKSIFR IHTETGNIWT HLLGFVLFLF LGILTMLRPN MYFMAPLQEK VVFGMFFLGA 

       190        200        210        220        230        240 
VLCLSFSWLF HTVYCHSEKV SRTFSKLDYS GIALLIMGSF VPWLYYSFYC SPQPRLIYLS 

       250        260        270        280        290        300 
IVCVLGISAI IVAQWDRFAT PKHRQTRAGV FLGLGLSGVV PTMHFTIAEG FVKATTVGQM 

       310        320        330        340        350        360 
GWFFLMAVMY ITGAGLYAAR IPERFFPGKF DIWFQSHQIF HVLVVAAAFV HFYGVSNLQE 

       370 
FRYGLEGGCT DDSLL 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[2]"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: Mammary tumor.
[3]"Cloning of adiponectin receptors that mediate antidiabetic metabolic effects."
Yamauchi T., Kamon J., Ito Y., Tsuchida A., Yokomizo T., Kita S., Sugiyama T., Miyagishi M., Hara K., Tsunoda M., Murakami K., Ohteki T., Uchida S., Takekawa S., Waki H., Tsuno N.H., Shibata Y., Terauchi Y. expand/collapse author list , Froguel P., Tobe K., Koyasu S., Taira K., Kitamura T., Shimizu T., Nagai R., Kadowaki T.
Nature 423:762-769(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK012847 mRNA. Translation: BAB28509.1. Sequence problems.
BC014875 mRNA. Translation: AAH14875.1.
RefSeqNP_082596.2. NM_028320.3.
XP_006529951.1. XM_006529888.1.
UniGeneMm.259976.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ91VH1. 2 interactions.

Chemistry

GuidetoPHARMACOLOGY649.

PTM databases

PhosphoSiteQ91VH1.

Proteomic databases

PRIDEQ91VH1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027727; ENSMUSP00000027727; ENSMUSG00000026457.
ENSMUST00000112237; ENSMUSP00000107856; ENSMUSG00000026457.
GeneID72674.
KEGGmmu:72674.
UCSCuc007crx.1. mouse.

Organism-specific databases

CTD51094.
MGIMGI:1919924. Adipor1.

Phylogenomic databases

eggNOGCOG1272.
GeneTreeENSGT00530000062926.
HOGENOMHOG000197115.
HOVERGENHBG013916.
InParanoidQ91VH1.
KOK07297.
OMAAAFIHFY.
OrthoDBEOG7BS49P.
PhylomeDBQ91VH1.
TreeFamTF313640.

Gene expression databases

ArrayExpressQ91VH1.
BgeeQ91VH1.
CleanExMM_ADIPOR1.
GenevestigatorQ91VH1.

Family and domain databases

InterProIPR004254. HlyIII-related.
[Graphical view]
PANTHERPTHR20855. PTHR20855. 1 hit.
PfamPF03006. HlyIII. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSADIPOR1. mouse.
NextBio336721.
PROQ91VH1.
SOURCESearch...

Entry information

Entry nameADR1_MOUSE
AccessionPrimary (citable) accession number: Q91VH1
Secondary accession number(s): Q9CZA0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot