ID   METRL_RAT               Reviewed;         311 AA.
AC   Q5RJL6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Meteorin-like protein;
DE   AltName: Full=Subfatin;
DE   Flags: Precursor;
GN   Name=Metrnl;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
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   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=24393292; DOI=10.1111/cns.12219;
RA   Li Z.Y., Zheng S.L., Wang P., Xu T.Y., Guan Y.F., Zhang Y.J., Miao C.Y.;
RT   "Subfatin is a novel adipokine and unlike Meteorin in adipose and brain
RT   expression.";
RL   CNS Neurosci. Ther. 20:344-354(2014).
CC   -!- FUNCTION: Hormone induced following exercise or cold exposure that
CC       promotes energy expenditure. Induced either in the skeletal muscle
CC       after exercise or in adipose tissue following cold exposure and is
CC       present in the circulation. Able to stimulate energy expenditure
CC       associated with the browning of the white fat depots and improves
CC       glucose tolerance. Does not promote an increase in a thermogenic gene
CC       program via direct action on adipocytes, but acts by stimulating
CC       several immune cell subtypes to enter the adipose tissue and activate
CC       their prothermogenic actions. Stimulates an eosinophil-dependent
CC       increase in IL4 expression and promotes alternative activation of
CC       adipose tissue macrophages, which are required for the increased
CC       expression of the thermogenic and anti-inflammatory gene programs in
CC       fat. Required for some cold-induced thermogenic responses, suggesting a
CC       role in metabolic adaptations to cold temperatures (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in adipose tissue.
CC       {ECO:0000269|PubMed:24393292}.
CC   -!- SIMILARITY: Belongs to the meteorin family. {ECO:0000305}.
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DR   EMBL; BC086590; AAH86590.1; -; mRNA.
DR   RefSeq; NP_001014126.1; NM_001014104.1.
DR   AlphaFoldDB; Q5RJL6; -.
DR   STRING; 10116.ENSRNOP00000066593; -.
DR   GlyGen; Q5RJL6; 1 site.
DR   PaxDb; Q5RJL6; -.
DR   Ensembl; ENSRNOT00000072190; ENSRNOP00000066593; ENSRNOG00000046202.
DR   GeneID; 316842; -.
DR   KEGG; rno:316842; -.
DR   CTD; 284207; -.
DR   RGD; 1359271; Metrnl.
DR   eggNOG; ENOG502QUQB; Eukaryota.
DR   GeneTree; ENSGT00390000001390; -.
DR   InParanoid; Q5RJL6; -.
DR   OMA; GAVEWMY; -.
DR   OrthoDB; 1364884at2759; -.
DR   PhylomeDB; Q5RJL6; -.
DR   PRO; PR:Q5RJL6; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000046202; Expressed in esophagus and 19 other tissues.
DR   ExpressionAtlas; Q5RJL6; baseline and differential.
DR   Genevisible; Q5RJL6; RN.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; ISS:UniProtKB.
DR   GO; GO:0050873; P:brown fat cell differentiation; ISS:UniProtKB.
DR   GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR   GO; GO:0045444; P:fat cell differentiation; ISS:CAFA.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB.
DR   GO; GO:0009409; P:response to cold; ISS:UniProtKB.
DR   GO; GO:0014850; P:response to muscle activity; ISS:UniProtKB.
DR   InterPro; IPR039224; Meteorin-like.
DR   PANTHER; PTHR28593:SF1; PTHR28593:SF1; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..45
FT                   /evidence="ECO:0000255"
FT   CHAIN           46..311
FT                   /note="Meteorin-like protein"
FT                   /id="PRO_0000289106"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        52..75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        107..143
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        188..260
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        191..284
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        201..306
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   311 AA;  34468 MW;  870AF0034061391E CRC64;
     MRGVVWAARR RAGQQWPRSP GPGPGPPPPP PLLLLLLLLL GGASAQYSSD LCSWKGSGLT
     REAHSKEVEQ VYLRCSAGSV EWMYPTGALI VNLRPNTFSP AQNLTVCIKP FRDSSGANIY
     LEKTGELRLL VRDVRGEPGQ VQCFSLEQGG LFVEATPQQD ISRRTTGFQY ELMSGQRGLD
     LHVLSAPCRP CSDTEVLLAI CTSDFVVRGF IEDVTHVPEQ QVSVIHLRVS RLHRQKSRVF
     QPAPEDSGHW LGHVTTLLQC GVRPGHGEFL FTGHVHFGEA QLGCAPRFSD FQKMYRKAEE
     RGINPCEINM E