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Protein

Adiponectin receptor protein 1

Gene

Adipor1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. adiponectin binding Source: MGI
  2. hormone binding Source: UniProtKB
  3. identical protein binding Source: MGI
  4. protein heterodimerization activity Source: MGI
  5. protein kinase binding Source: MGI
  6. receptor activity Source: MGI

GO - Biological processi

  1. adiponectin-activated signaling pathway Source: MGI
  2. fatty acid oxidation Source: UniProtKB
  3. hormone-mediated signaling pathway Source: UniProtKB
  4. leptin-mediated signaling pathway Source: Ensembl
  5. negative regulation of cell growth Source: Ensembl
  6. positive regulation of insulin receptor signaling pathway Source: Ensembl
  7. positive regulation of JAK-STAT cascade Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Adiponectin receptor protein 1
Gene namesi
Name:Adipor1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1919924. Adipor1.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 136136CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei137 – 15721Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini158 – 17013ExtracellularSequence AnalysisAdd
BLAST
Transmembranei171 – 19121Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini192 – 20918CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei210 – 23021Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini231 – 2355ExtracellularSequence Analysis
Transmembranei236 – 25621Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini257 – 26711CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei268 – 28821Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini289 – 2968ExtracellularSequence Analysis
Transmembranei297 – 31721Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini318 – 33114CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei332 – 35221Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini353 – 37523ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. membrane Source: MGI
  3. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Adiponectin receptor protein 1PRO_0000218828Add
BLAST

Proteomic databases

MaxQBiQ91VH1.
PRIDEiQ91VH1.

PTM databases

PhosphoSiteiQ91VH1.

Expressioni

Tissue specificityi

Widely expressed. Expressed in heart, kidney, liver, lung, skeletal muscle and spleen. Weakly expressed in brain and testis.1 Publication

Gene expression databases

BgeeiQ91VH1.
CleanExiMM_ADIPOR1.
ExpressionAtlasiQ91VH1. baseline and differential.
GenevestigatoriQ91VH1.

Interactioni

Subunit structurei

May form homomultimer and heteromultimers.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
APPL1Q9UKG13EBI-992398,EBI-741243From a different organism.

Protein-protein interaction databases

IntActiQ91VH1. 2 interactions.

Family & Domainsi

Sequence similaritiesi

Belongs to the ADIPOR family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1272.
GeneTreeiENSGT00530000062926.
HOGENOMiHOG000197115.
HOVERGENiHBG013916.
InParanoidiQ91VH1.
KOiK07297.
OMAiEQACPVP.
OrthoDBiEOG7BS49P.
PhylomeDBiQ91VH1.
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.

Q91VH1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSHKGSAGA QGNGAPSGNR EADTVELAEL GPLLEEKGKR AASSPAKAEE
60 70 80 90 100
DQACPVPQEE 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 DDSLL
Length:375
Mass (Da):42,366
Last modified:December 1, 2001 - v1
Checksum:i0E72F81B5E9938CE
GO

Sequence cautioni

The sequence BAB28509.1 differs from that shown. Reason: Frameshift at position 376. This frameshift abolishes the stop codon.Curated
The sequence BAB28509.1 differs from that shown. Reason: Erroneous termination at position 353. Translated as Tyr.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012847 mRNA. Translation: BAB28509.1. Sequence problems.
BC014875 mRNA. Translation: AAH14875.1.
CCDSiCCDS15309.1.
RefSeqiNP_082596.2. NM_028320.3.
XP_006529951.1. XM_006529888.1.
UniGeneiMm.259976.

Genome annotation databases

EnsembliENSMUST00000027727; ENSMUSP00000027727; ENSMUSG00000026457.
ENSMUST00000112237; ENSMUSP00000107856; ENSMUSG00000026457.
GeneIDi72674.
KEGGimmu:72674.
UCSCiuc007crx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012847 mRNA. Translation: BAB28509.1. Sequence problems.
BC014875 mRNA. Translation: AAH14875.1.
CCDSiCCDS15309.1.
RefSeqiNP_082596.2. NM_028320.3.
XP_006529951.1. XM_006529888.1.
UniGeneiMm.259976.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91VH1. 2 interactions.

Chemistry

GuidetoPHARMACOLOGYi649.

PTM databases

PhosphoSiteiQ91VH1.

Proteomic databases

MaxQBiQ91VH1.
PRIDEiQ91VH1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027727; ENSMUSP00000027727; ENSMUSG00000026457.
ENSMUST00000112237; ENSMUSP00000107856; ENSMUSG00000026457.
GeneIDi72674.
KEGGimmu:72674.
UCSCiuc007crx.1. mouse.

Organism-specific databases

CTDi51094.
MGIiMGI:1919924. Adipor1.

Phylogenomic databases

eggNOGiCOG1272.
GeneTreeiENSGT00530000062926.
HOGENOMiHOG000197115.
HOVERGENiHBG013916.
InParanoidiQ91VH1.
KOiK07297.
OMAiEQACPVP.
OrthoDBiEOG7BS49P.
PhylomeDBiQ91VH1.
TreeFamiTF313640.

Miscellaneous databases

ChiTaRSiAdipor1. mouse.
NextBioi336721.
PROiQ91VH1.
SOURCEiSearch...

Gene expression databases

BgeeiQ91VH1.
CleanExiMM_ADIPOR1.
ExpressionAtlasiQ91VH1. baseline and differential.
GenevestigatoriQ91VH1.

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. "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.
    , 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(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  3. Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiADR1_MOUSE
AccessioniPrimary (citable) accession number: Q91VH1
Secondary accession number(s): Q9CZA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: December 1, 2001
Last modified: February 4, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.