RARR2_HUMAN
ID RARR2_HUMAN Reviewed; 163 AA.
AC Q99969; Q7LE02;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Retinoic acid receptor responder protein 2;
DE AltName: Full=Chemerin;
DE AltName: Full=RAR-responsive protein TIG2;
DE AltName: Full=Tazarotene-induced gene 2 protein;
DE Flags: Precursor;
GN Name=RARRES2; Synonyms=TIG2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC TISSUE=Skin;
RX PubMed=9204961; DOI=10.1111/1523-1747.ep12276660;
RA Nagpal S., Patel S., Jacobe H., DiSepio D., Ghosn C., Malhotra M., Teng M.,
RA Duvic M., Chandraratna R.A.S.;
RT "Tazarotene-induced gene 2 (TIG2), a novel retinoid-responsive gene in
RT skin.";
RL J. Invest. Dermatol. 109:91-95(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Gastric adenocarcinoma;
RX PubMed=10072769; DOI=10.1016/s0378-1119(99)00004-9;
RA Yokoyama-Kobayashi M., Yamaguchi T., Sekine S., Kato S.;
RT "Selection of cDNAs encoding putative type II membrane proteins on the cell
RT surface from a human full-length cDNA bank.";
RL Gene 228:161-167(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 21-67, PROTEOLYTIC PROCESSING, AND FUNCTION AS LIGAND
RP FOR CMKLR1.
RX PubMed=14675762; DOI=10.1016/s0014-5793(03)01312-7;
RA Meder W., Wendland M., Busmann A., Kutzleb C., Spodsberg N., John H.,
RA Richter R., Schleuder D., Meyer M., Forssmann W.G.;
RT "Characterization of human circulating TIG2 as a ligand for the orphan
RT receptor ChemR23.";
RL FEBS Lett. 555:495-499(2003).
RN [9]
RP PROTEOLYTIC PROCESSING, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16096270; DOI=10.1074/jbc.m504868200;
RA Zabel B.A., Allen S.J., Kulig P., Allen J.A., Cichy J., Handel T.M.,
RA Butcher E.C.;
RT "Chemerin activation by serine proteases of the coagulation, fibrinolytic,
RT and inflammatory cascades.";
RL J. Biol. Chem. 280:34661-34666(2005).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17767914; DOI=10.1016/j.bbrc.2007.08.104;
RA Roh S.G., Song S.H., Choi K.C., Katoh K., Wittamer V., Parmentier M.,
RA Sasaki S.;
RT "Chemerin--a new adipokine that modulates adipogenesis via its own
RT receptor.";
RL Biochem. Biophys. Res. Commun. 362:1013-1018(2007).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17635925; DOI=10.1074/jbc.m700793200;
RA Goralski K.B., McCarthy T.C., Hanniman E.A., Zabel B.A., Butcher E.C.,
RA Parlee S.D., Muruganandan S., Sinal C.J.;
RT "Chemerin, a novel adipokine that regulates adipogenesis and adipocyte
RT metabolism.";
RL J. Biol. Chem. 282:28175-28188(2007).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18242188; DOI=10.1016/j.febslet.2008.01.023;
RA Takahashi M., Takahashi Y., Takahashi K., Zolotaryov F.N., Hong K.S.,
RA Kitazawa R., Iida K., Okimura Y., Kaji H., Kitazawa S., Kasuga M.,
RA Chihara K.;
RT "Chemerin enhances insulin signaling and potentiates insulin-stimulated
RT glucose uptake in 3T3-L1 adipocytes.";
RL FEBS Lett. 582:573-578(2008).
RN [13]
RP REVIEW ON PROTEOLYTIC PROCESSING.
RX PubMed=20011981; DOI=10.1093/abbs/gmp091;
RA Du X.Y., Leung L.L.;
RT "Proteolytic regulatory mechanism of chemerin bioactivity.";
RL Acta Biochim. Biophys. Sin. 41:973-979(2009).
RN [14]
RP FUNCTION.
RX PubMed=20237162; DOI=10.1210/jc.2010-0042;
RA Bozaoglu K., Curran J.E., Stocker C.J., Zaibi M.S., Segal D.,
RA Konstantopoulos N., Morrison S., Carless M., Dyer T.D., Cole S.A.,
RA Goring H.H., Moses E.K., Walder K., Cawthorne M.A., Blangero J.,
RA Jowett J.B.;
RT "Chemerin, a novel adipokine in the regulation of angiogenesis.";
RL J. Clin. Endocrinol. Metab. 95:2476-2485(2010).
RN [15]
RP REVIEW.
RX PubMed=20817486; DOI=10.1016/j.tem.2010.08.001;
RA Ernst M.C., Sinal C.J.;
RT "Chemerin: at the crossroads of inflammation and obesity.";
RL Trends Endocrinol. Metab. 21:660-667(2010).
RN [16]
RP REVIEW.
RX PubMed=22119008; DOI=10.1016/j.cytogfr.2011.11.004;
RA Bondue B., Wittamer V., Parmentier M.;
RT "Chemerin and its receptors in leukocyte trafficking, inflammation and
RT metabolism.";
RL Cytokine Growth Factor Rev. 22:331-338(2011).
RN [17]
RP FUNCTION.
RX PubMed=22634313; DOI=10.1016/j.bbrc.2012.05.103;
RA Yamawaki H., Kameshima S., Usui T., Okada M., Hara Y.;
RT "A novel adipocytokine, chemerin exerts anti-inflammatory roles in human
RT vascular endothelial cells.";
RL Biochem. Biophys. Res. Commun. 423:152-157(2012).
RN [18]
RP REVIEW.
RX PubMed=22610747; DOI=10.1007/s12020-012-9698-8;
RA Roman A.A., Parlee S.D., Sinal C.J.;
RT "Chemerin: a potential endocrine link between obesity and type 2
RT diabetes.";
RL Endocrine 42:243-251(2012).
RN [19]
RP REVIEW.
RX PubMed=23216632; DOI=10.1111/obr.12009;
RA Rourke J.L., Dranse H.J., Sinal C.J.;
RT "Towards an integrative approach to understanding the role of chemerin in
RT human health and disease.";
RL Obes. Rev. 14:245-262(2013).
RN [20]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23527010; DOI=10.1371/journal.pone.0058709;
RA Banas M., Zabieglo K., Kasetty G., Kapinska-Mrowiecka M., Borowczyk J.,
RA Drukala J., Murzyn K., Zabel B.A., Butcher E.C., Schroeder J.M.,
RA Schmidtchen A., Cichy J.;
RT "Chemerin is an antimicrobial agent in human epidermis.";
RL PLoS ONE 8:E58709-E58709(2013).
RN [21]
RP FUNCTION.
RX PubMed=27716822; DOI=10.1371/journal.pone.0164179;
RA De Henau O., Degroot G.N., Imbault V., Robert V., De Poorter C., Mcheik S.,
RA Gales C., Parmentier M., Springael J.Y.;
RT "Signaling properties of chemerin receptors CMKLR1, GPR1 and CCRL2.";
RL PLoS ONE 11:e0164179-e0164179(2016).
CC -!- FUNCTION: Adipocyte-secreted protein (adipokine) that regulates
CC adipogenesis, metabolism and inflammation through activation of the
CC chemokine-like receptor 1 (CMKLR1). Acts also as a ligand for CMKLR2.
CC Can also bind to C-C chemokine receptor-like 2 (CCRL2), but with a
CC lower affinity than it does to CMKLR1 or CMKLR2 (PubMed:27716822).
CC Positively regulates adipocyte differentiation, modulates the
CC expression of adipocyte genes involved in lipid and glucose metabolism
CC and might play a role in angiogenesis, a process essential for the
CC expansion of white adipose tissue. Also acts as a pro-inflammatory
CC adipokine, causing an increase in secretion of pro-inflammatory and
CC prodiabetic adipokines, which further impair adipose tissue metabolic
CC function and have negative systemic effects including impaired insulin
CC sensitivity, altered glucose and lipid metabolism, and a decrease in
CC vascular function in other tissues. Can have both pro- and anti-
CC inflammatory properties depending on the modality of enzymatic cleavage
CC by different classes of proteases. Acts as a chemotactic factor for
CC leukocyte populations expressing CMKLR1, particularly immature
CC plasmacytoid dendritic cells, but also immature myeloid DCs,
CC macrophages and natural killer cells. Exerts an anti-inflammatory role
CC by preventing TNF/TNFA-induced VCAM1 expression and monocytes adhesion
CC in vascular endothelial cells. The effect is mediated via inhibiting
CC activation of NF-kappa-B and CRK/p38 through stimulation of AKT1/NOS3
CC signaling and nitric oxide production. Its dual role in inflammation
CC and metabolism might provide a link between chronic inflammation and
CC obesity, as well as obesity-related disorders such as type 2 diabetes
CC and cardiovascular disease. Exhibits an antimicrobial function in the
CC skin. {ECO:0000269|PubMed:14675762, ECO:0000269|PubMed:17635925,
CC ECO:0000269|PubMed:17767914, ECO:0000269|PubMed:18242188,
CC ECO:0000269|PubMed:20237162, ECO:0000269|PubMed:22634313,
CC ECO:0000269|PubMed:23527010, ECO:0000269|PubMed:27716822}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9DD06}.
CC -!- TISSUE SPECIFICITY: Expressed at the highest levels in placenta, liver,
CC and white adipose tissue (WAT), and to a lesser extent in many other
CC tissues such as lung, brown adipose tissue, heart, ovary, kidney,
CC skeletal muscle and pancreas. Within WAT, expression is enriched in
CC adipocytes as compared to the stromal vascular fraction. Expression and
CC secretion increases dramatically with adipogenesis. Highly expressed in
CC skin (basal and suprabasal layers of the epidermis, hair follicles and
CC endothelial cells). Expression is elevated in numerous metabolic and
CC inflammatory diseases including psoriasis, obesity, type 2 diabetes,
CC metabolic syndrome and cardiovascular disease.
CC {ECO:0000269|PubMed:17635925, ECO:0000269|PubMed:17767914,
CC ECO:0000269|PubMed:23527010}.
CC -!- INDUCTION: Inhibited in psoriatic lesions. Activated by tazarotene in
CC skin rafts and in the epidermis of psoriatic lesions.
CC {ECO:0000269|PubMed:9204961}.
CC -!- PTM: Secreted in an inactive precursor form, prochemerin, which is
CC proteolytically processed by a variety of extracellular proteases to
CC generate forms with differing levels of bioactivity. For example, the
CC removal of six amino acids results in chemerin-157, which exhibits the
CC highest activity, while removal of seven amino acids results in
CC chemerin-156 which has slightly less activity. Some proteases are able
CC to cleave at more than one site and chemerin forms may be sequentially
CC processed by different enzymes to modulate activity levels. The
CC coordinated expression and activity of chemerin-modifying enzymes is
CC essential for regulating its bioactivation, inactivation and,
CC consequently, biological function. Cathepsin G cleaves seven C-terminal
CC amino acids from prochemerin (chemerin-156), elastase is able to cleave
CC six (chemerin-157), eight (chemerin-155) or eleven (chemerin-152),
CC plasmin cleaves five amino acids (chemerin-158), and tryptase cleaves
CC five (chemerin-158) or eight (chemerin-155). Multiple cleavages might
CC be required to fully activate chemerin, with an initial tryptase
CC cleavage resulting in chemerin with low activity (chemerin-158), and a
CC second cleavage by carboxypeptidase N or B producing highly active
CC chemerin (chemerin-157). {ECO:0000269|PubMed:14675762,
CC ECO:0000269|PubMed:16096270}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U77594; AAB47975.1; -; mRNA.
DR EMBL; AB015632; BAA76499.1; -; mRNA.
DR EMBL; AK312197; BAG35130.1; -; mRNA.
DR EMBL; CR541992; CAG46789.1; -; mRNA.
DR EMBL; CR542026; CAG46823.1; -; mRNA.
DR EMBL; AC005586; AAS00384.1; -; Genomic_DNA.
DR EMBL; CH471173; EAW54120.1; -; Genomic_DNA.
DR EMBL; CH471173; EAW54121.1; -; Genomic_DNA.
DR EMBL; BC000069; AAH00069.1; -; mRNA.
DR CCDS; CCDS5902.1; -.
DR RefSeq; NP_002880.1; NM_002889.3.
DR AlphaFoldDB; Q99969; -.
DR BMRB; Q99969; -.
DR SMR; Q99969; -.
DR BioGRID; 111854; 4.
DR STRING; 9606.ENSP00000418009; -.
DR iPTMnet; Q99969; -.
DR PhosphoSitePlus; Q99969; -.
DR BioMuta; RARRES2; -.
DR EPD; Q99969; -.
DR jPOST; Q99969; -.
DR MassIVE; Q99969; -.
DR MaxQB; Q99969; -.
DR PaxDb; Q99969; -.
DR PeptideAtlas; Q99969; -.
DR PRIDE; Q99969; -.
DR ProteomicsDB; 78557; -.
DR Antibodypedia; 32863; 365 antibodies from 23 providers.
DR DNASU; 5919; -.
DR Ensembl; ENST00000223271.8; ENSP00000223271.3; ENSG00000106538.10.
DR Ensembl; ENST00000466675.5; ENSP00000418009.1; ENSG00000106538.10.
DR Ensembl; ENST00000482669.1; ENSP00000418483.1; ENSG00000106538.10.
DR GeneID; 5919; -.
DR KEGG; hsa:5919; -.
DR MANE-Select; ENST00000223271.8; ENSP00000223271.3; NM_002889.4; NP_002880.1.
DR UCSC; uc003wha.4; human.
DR CTD; 5919; -.
DR DisGeNET; 5919; -.
DR GeneCards; RARRES2; -.
DR HGNC; HGNC:9868; RARRES2.
DR HPA; ENSG00000106538; Tissue enhanced (adrenal gland, liver, pancreas).
DR MIM; 601973; gene.
DR neXtProt; NX_Q99969; -.
DR OpenTargets; ENSG00000106538; -.
DR PharmGKB; PA34229; -.
DR VEuPathDB; HostDB:ENSG00000106538; -.
DR eggNOG; ENOG502SE7C; Eukaryota.
DR GeneTree; ENSGT00390000016226; -.
DR HOGENOM; CLU_138029_0_0_1; -.
DR InParanoid; Q99969; -.
DR OMA; WAFQKTS; -.
DR OrthoDB; 1596588at2759; -.
DR PhylomeDB; Q99969; -.
DR TreeFam; TF330938; -.
DR PathwayCommons; Q99969; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; Q99969; -.
DR BioGRID-ORCS; 5919; 69 hits in 1072 CRISPR screens.
DR ChiTaRS; RARRES2; human.
DR GeneWiki; Chemerin; -.
DR GenomeRNAi; 5919; -.
DR Pharos; Q99969; Tbio.
DR PRO; PR:Q99969; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q99969; protein.
DR Bgee; ENSG00000106538; Expressed in right adrenal gland cortex and 188 other tissues.
DR ExpressionAtlas; Q99969; baseline and differential.
DR Genevisible; Q99969; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0031089; C:platelet dense granule lumen; TAS:Reactome.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0019732; P:antifungal humoral response; IMP:UniProtKB.
DR GO; GO:0061760; P:antifungal innate immune response; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0048566; P:embryonic digestive tract development; IMP:DFLAT.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IMP:DFLAT.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0050994; P:regulation of lipid catabolic process; ISS:UniProtKB.
DR GO; GO:0001523; P:retinoid metabolic process; IDA:UniProtKB.
DR InterPro; IPR029562; Chemerin.
DR InterPro; IPR046350; Cystatin_sf.
DR PANTHER; PTHR15106; PTHR15106; 1.
DR SUPFAM; SSF54403; SSF54403; 1.
PE 1: Evidence at protein level;
KW Chemotaxis; Differentiation; Direct protein sequencing; Disulfide bond;
KW Inflammatory response; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:14675762"
FT CHAIN 21..157
FT /note="Retinoic acid receptor responder protein 2"
FT /id="PRO_0000022529"
FT PROPEP 158..163
FT /id="PRO_0000424870"
FT DISULFID 77..87
FT /evidence="ECO:0000250"
FT DISULFID 98..117
FT /evidence="ECO:0000250"
FT DISULFID 101..135
FT /evidence="ECO:0000255"
SQ SEQUENCE 163 AA; 18618 MW; A96EB7D0999EC3DB CRC64;
MRRLLIPLAL WLGAVGVGVA ELTEAQRRGL QVALEEFHKH PPVQWAFQET SVESAVDTPF
PAGIFVRLEF KLQQTSCRKR DWKKPECKVR PNGRKRKCLA CIKLGSEDKV LGRLVHCPIE
TQVLREAEEH QETQCLRVQR AGEDPHSFYF PGQFAFSKAL PRS
