RARRES2
entrez
5919
canonical
uniprot
Q99969
canonical
ensembl
ENSG00000106538
resolver
ensp
ENSP00000223271
resolver
ensp
ENSP00000418009
resolver
ensp
ENSP00000418483
resolver
ensp
ENSP00000533380
resolver
ensp
ENSP00000533381
resolver
ensp
ENSP00000533385
resolver
ensp
ENSP00000533386
resolver
ensp
ENSP00000533390
resolver
ensp
ENSP00000533391
resolver
ensp
ENSP00000533392
resolver
ensp
ENSP00000533395
resolver
ensp
ENSP00000533396
resolver
ensp
ENSP00000533398
resolver
ensp
ENSP00000533400
resolver
ensp
ENSP00000581650
resolver
ensp
ENSP00000634618
resolver
enst
ENST00000223271
resolver
enst
ENST00000466675
resolver
enst
ENST00000482669
resolver
enst
ENST00000863321
resolver
enst
ENST00000863322
resolver
enst
ENST00000863326
resolver
enst
ENST00000863327
resolver
enst
ENST00000863331
resolver
enst
ENST00000863332
resolver
enst
ENST00000863333
resolver
enst
ENST00000863336
resolver
enst
ENST00000863337
resolver
enst
ENST00000863339
resolver
enst
ENST00000863341
resolver
enst
ENST00000911591
resolver
enst
ENST00000964559
resolver
genesymbol
RARRES2
resolver
genesymbol_syn
TIG2
resolver
hgnc
HGNC:9868
resolver
uniprot
Q7LE02
resolver
uniprot_entry
RARR2_HUMAN
resolver
uniprot_sec
Q7LE02
resolver
amino_acid_sequence
MRRLLIPLALWLGAVGVGVAELTEAQRRGLQVALEEFHKHPPVQWAFQETSVESAVDTPFPAGIFVRLEFKLQQTSCRKRDWKKPECKVRPNGRKRKCLACIKLGSEDKVLGRLVHCPIETQVLREAEEHQETQCLRVQRAGEDPHSFYFPGQFAFSKALPRS
uniprot
proteins
function
FUNCTION: Adipocyte-secreted protein (adipokine) that regulates adipogenesis, metabolism and inflammation through activation of the chemokine-like receptor 1 (CMKLR1). Also acts as a ligand for CMKLR2. Can also bind to C-C chemokine receptor-like 2 (CCRL2), but with a lower affinity than it does to CMKLR1 or CMKLR2 (PubMed:27716822). 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 pro-inflammatory adipokine, causing an increase in secretion of pro-inflammatory 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. Its dual role in inflammation and metabolism might provide a link between chronic inflammation and obesity, as well as obesity-related disorders such as type 2 diabetes and cardiovascular disease. Exhibits an antimicrobial function in the skin. {ECO:0000269|PubMed:14675762, ECO:0000269|PubMed:17635925, ECO:0000269|PubMed:17767914, ECO:0000269|PubMed:18242188, ECO:0000269|PubMed:20237162, ECO:0000269|PubMed:22634313, ECO:0000269|PubMed:23527010, ECO:0000269|PubMed:27716822}.
uniprot
proteins
mass_dalton
18618
uniprot
proteins
post_translational_modification
PTM: 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-157, which exhibits the highest activity, while removal of seven amino acids results in chemerin-156 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-156), elastase is able to cleave six (chemerin-157), eight (chemerin-155) or eleven (chemerin-152), plasmin cleaves five amino acids (chemerin-158), and tryptase cleaves five (chemerin-158) or eight (chemerin-155). Multiple cleavages might be required to fully activate chemerin, with an initial tryptase cleavage resulting in chemerin with low activity (chemerin-158), and a second cleavage by carboxypeptidase N or B producing highly active chemerin (chemerin-157). {ECO:0000269|PubMed:14675762, ECO:0000269|PubMed:16096270}.
uniprot
proteins
pubmed
10072769
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14675762
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16096270
uniprot
proteins
pubmed
17635925
uniprot
proteins
pubmed
17767914
uniprot
proteins
pubmed
18242188
uniprot
proteins
pubmed
20011981
uniprot
proteins
pubmed
20237162
uniprot
proteins
pubmed
20817486
uniprot
proteins
pubmed
22119008
uniprot
proteins
pubmed
22610747
uniprot
proteins
pubmed
22634313
uniprot
proteins
pubmed
23216632
uniprot
proteins
pubmed
23527010
uniprot
proteins
pubmed
27716822
uniprot
proteins
pubmed
9204961
uniprot
proteins
sequence_length
163
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9DD06}.
uniprot
proteins