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Protein

Retinoic acid receptor responder protein 2

Gene

Rarres2

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

Functioni

Adipocyte-secreted protein (adipokine) that regulates adipogenesis, metabolism and inflammation through activation of the chemokine-like receptor 1 (CMKLR1). Its other ligands include G protein-coupled receptor 1 (GPR1) and chemokine receptor-like 2 (CCRL2). Positively regulates adipocyte differentiation, modulates the expression of adipocyte genes involved in lipid and glucose metabolism and might play a role in angiogenesis, a process essential for the expansion of white adipose tissue. Also acts as a proinflammatory adipokine, causing an increase in secretion of proinflammatory and prodiabetic adipokines, which further impair adipose tissue metabolic function and have negative systemic effects including impaired insulin sensitivity, altered glucose and lipid metabolism, and a decrease in vascular function in other tissues. Can have both pro- and anti-inflammatory properties depending on the modality of enzymatic cleavage by different classes of proteases. Acts as a chemotactic factor for leukocyte populations expressing CMKLR1, particularly immature plasmacytoid dendritic cells, but also immature myeloid DCs, macrophages and natural killer cells. Exerts an anti-inflammatory role by preventing TNF/TNFA-induced VCAM1 expression and monocytes adhesion in vascular endothelial cells. The effect is mediated via inhibiting activation of NF-kappa-B and CRK/p38 through stimulation of AKT1/NOS3 signaling and nitric oxide production. Exhibits an antimicrobial function in the skin.2 Publications

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processChemotaxis, Differentiation, Inflammatory response

Enzyme and pathway databases

ReactomeiR-MMU-114608 Platelet degranulation

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoic acid receptor responder protein 2
Alternative name(s):
Chemerin
Gene namesi
Name:Rarres2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1918910 Rarres2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20By similarityAdd BLAST20
ChainiPRO_000002253021 – 156Retinoic acid receptor responder protein 2Add BLAST136
PropeptideiPRO_0000424871157 – 162By similarity6

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi79 ↔ 89By similarity
Disulfide bondi100 ↔ 119By similarity
Disulfide bondi103 ↔ 134Sequence analysis

Post-translational modificationi

Secreted in an inactive precursor form, prochemerin, which is proteolytically processed by a variety of extracellular proteases to generate forms with differing levels of bioactivity. For example, the removal of six amino acids results in chemerin-156, which exhibits the highest activity, while removal of seven amino acids results in chemerin-155 which has slightly less activity. Some proteases are able to cleave at more than one site and chemerin forms may be sequentially processed by different enzymes to modulate activity levels. The coordinated expression and activity of chemerin-modifying enzymes is essential for regulating its bioactivation, inactivation and, consequently, biological function. Cathepsin G cleaves seven C-terminal amino acids from prochemerin (chemerin-155), elastase is able to cleave six (chemerin-156), eight (chemerin-154) or eleven (chemerin-151), plasmin cleaves five amino acids (chemerin-157), and tryptase cleaves five (chemerin-157) or eight (chemerin-154). Multiple cleavages might be required to fully activate chemerin, with an initial tryptase cleavage resulting in chemerin with low activity (chemerin-157), and a second cleavage by carboxypeptidase N or B producing highly active chemerin (chemerin-156) (By similarity).By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ9DD06
PaxDbiQ9DD06
PeptideAtlasiQ9DD06
PRIDEiQ9DD06

PTM databases

PhosphoSitePlusiQ9DD06

Expressioni

Tissue specificityi

Expressed in the differentiated adipocytes (at protein level). Abundantly expressed in the liver, adipose tissue including visceral, epididymal, and brown adipose tissue.3 Publications

Inductioni

Strongly induced during adipocyte differentiation.1 Publication

Gene expression databases

BgeeiENSMUSG00000009281
ExpressionAtlasiQ9DD06 baseline and differential
GenevisibleiQ9DD06 MM

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9DD06, 1 interactor
MINTiQ9DD06
STRINGi10090.ENSMUSP00000009425

Structurei

3D structure databases

ProteinModelPortaliQ9DD06
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IY1C Eukaryota
ENOG410ZEJF LUCA
GeneTreeiENSGT00390000016226
HOGENOMiHOG000093205
HOVERGENiHBG000698
InParanoidiQ9DD06
KOiK10044
OrthoDBiEOG091G0OJ5
PhylomeDBiQ9DD06
TreeFamiTF330938

Family and domain databases

InterProiView protein in InterPro
IPR029562 Chemerin
PANTHERiPTHR15106 PTHR15106, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9DD06-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKCLLISLAL WLGTVGTRGT EPELSETQRR SLQVALEEFH KHPPVQLAFQ
60 70 80 90 100
EIGVDRAEEV LFSAGTFVRL EFKLQQTNCP KKDWKKPECT IKPNGRRRKC
110 120 130 140 150
LACIKMDPKG KILGRIVHCP ILKQGPQDPQ ELQCIKIAQA GEDPHGYFLP
160
GQFAFSRALR TK
Length:162
Mass (Da):18,350
Last modified:June 1, 2001 - v1
Checksum:i56FDE44B1BF167F3
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti3C → F in strain: FVB/N. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002298 mRNA Translation: BAB21997.1
BC038914 mRNA Translation: AAH38914.1
CCDSiCCDS20105.1
RefSeqiNP_001334097.1, NM_001347168.1
NP_082128.1, NM_027852.3
UniGeneiMm.28231

Genome annotation databases

EnsembliENSMUST00000204267; ENSMUSP00000144793; ENSMUSG00000009281
ENSMUST00000204930; ENSMUSP00000144799; ENSMUSG00000009281
GeneIDi71660
KEGGimmu:71660
UCSCiuc009but.1 mouse

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiRARR2_MOUSE
AccessioniPrimary (citable) accession number: Q9DD06
Secondary accession number(s): Q8CHU8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: June 1, 2001
Last modified: May 23, 2018
This is version 105 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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