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Growth/differentiation factor 15 (GDF-15) (Macrophage inhibitory cytokine 1) (MIC-1) (NSAID-activated gene 1 protein) (NAG-1) (NSAID-regulated gene 1 protein) (NRG-1) (Placental TGF-beta) (Placental bone morphogenetic protein) (Prostate differentiation factor)

 GDF15_HUMAN             Reviewed;         308 AA.
Q99988; O14629; P78360; Q9BWA0; Q9NRT0;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 3.
23-MAY-2018, entry version 158.
RecName: Full=Growth/differentiation factor 15 {ECO:0000305};
Short=GDF-15 {ECO:0000305};
AltName: Full=Macrophage inhibitory cytokine 1 {ECO:0000305};
Short=MIC-1 {ECO:0000303|PubMed:28846099};
AltName: Full=NSAID-activated gene 1 protein;
Short=NAG-1;
AltName: Full=NSAID-regulated gene 1 protein;
Short=NRG-1;
AltName: Full=Placental TGF-beta;
AltName: Full=Placental bone morphogenetic protein;
AltName: Full=Prostate differentiation factor;
Flags: Precursor;
Name=GDF15 {ECO:0000312|HGNC:HGNC:30142};
Synonyms=MIC1 {ECO:0000303|PubMed:28846099}, PDF, PLAB, PTGFB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-202.
TISSUE=Placenta;
PubMed=9375789; DOI=10.1016/S0167-4781(97)00122-X;
Hromas R., Hufford M., Sutton J., Xu D., Li Y., Lu L.;
"PLAB, a novel placental bone morphogenetic protein.";
Biochim. Biophys. Acta 1354:40-44(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-9 AND THR-48, AND TISSUE
SPECIFICITY.
TISSUE=Fibrosarcoma;
PubMed=9348093; DOI=10.1093/oxfordjournals.jbchem.a021798;
Yokoyama-Kobayashi M., Saeki M., Sekine S., Kato S.;
"Human cDNA encoding a novel TGF-beta superfamily protein highly
expressed in placenta.";
J. Biochem. 122:622-626(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LEU-9 AND THR-48.
PubMed=9326641; DOI=10.1073/pnas.94.21.11514;
Bootcov M.R., Bauskin A.R., Valenzuela S.M., Moore A.G., Bansal M.,
He X.Y., Zhang H.P., Donnellan M., Mahler S., Pryor K., Walsh B.J.,
Nicholson R.C., Fairlie W.D., Por S.B., Robbins J.M., Breit S.N.;
"MIC-1, a novel macrophage inhibitory cytokine, is a divergent member
of the TGF-beta superfamily.";
Proc. Natl. Acad. Sci. U.S.A. 94:11514-11519(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-9.
TISSUE=Placenta;
PubMed=9593718; DOI=10.1074/jbc.273.22.13760;
Paralkar V.M., Vail A.L., Grasser W.A., Brown T.A., Xu H.,
Vukicevic S., Ke H.Z., Qi H., Owen T.A., Thompson D.D.;
"Cloning and characterization of a novel member of the transforming
growth factor-beta/bone morphogenetic protein family.";
J. Biol. Chem. 273:13760-13767(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-9 AND THR-48.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-308.
PubMed=9426002; DOI=10.1016/S0378-1119(97)00485-X;
Lawton L.N., de Fatima Bonaldo M., Jelenc P.C., Qiu L., Baumes S.A.,
Marcelino R.A., de Jesus G.M., Wellington S., Knowles J.A.,
Warburton D., Brown S., Soares M.B.;
"Identification of a novel member of the TGF-beta superfamily highly
expressed in human placenta.";
Gene 203:17-26(1997).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 264-308.
PubMed=11259636;
Baek S.J., Kim K.S., Nixon J.B., Wilson L.C., Eling T.E.;
"Cyclooxygenase inhibitors regulate the expression of a TGF-beta
superfamily member that has proapoptotic and antitumorigenic
activities.";
Mol. Pharmacol. 59:901-908(2001).
[12]
FUNCTION.
PubMed=23468844; DOI=10.1371/journal.pone.0055174;
Tsai V.W., Macia L., Johnen H., Kuffner T., Manadhar R.,
Joergensen S.B., Lee-Ng K.K., Zhang H.P., Wu L., Marquis C.P.,
Jiang L., Husaini Y., Lin S., Herzog H., Brown D.A., Sainsbury A.,
Breit S.N.;
"TGF-b superfamily cytokine MIC-1/GDF15 is a physiological appetite
and body weight regulator.";
PLoS ONE 8:E55174-E55174(2013).
[13]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INVOLVEMENT IN DISEASE.
PubMed=28572090; DOI=10.15252/emmm.201707604;
Wang T., Liu J., McDonald C., Lupino K., Zhai X., Wilkins B.J.,
Hakonarson H., Pei L.;
"GDF15 is a heart-derived hormone that regulates body growth.";
EMBO Mol. Med. 9:1150-1164(2017).
[14]
FUNCTION, INTERACTION WITH GFRAL, AND MUTAGENESIS OF TRP-225 AND
ILE-285.
PubMed=28846097; DOI=10.1038/nm.4392;
Mullican S.E., Lin-Schmidt X., Chin C.N., Chavez J.A., Furman J.L.,
Armstrong A.A., Beck S.C., South V.J., Dinh T.Q., Cash-Mason T.D.,
Cavanaugh C.R., Nelson S., Huang C., Hunter M.J., Rangwala S.M.;
"GFRAL is the receptor for GDF15 and the ligand promotes weight loss
in mice and nonhuman primates.";
Nat. Med. 23:1150-1157(2017).
[15]
FUNCTION, INTERACTION WITH GFRAL, AND MUTAGENESIS OF VAL-283.
PubMed=28846099; DOI=10.1038/nm.4394;
Yang L., Chang C.C., Sun Z., Madsen D., Zhu H., Padkjaer S.B., Wu X.,
Huang T., Hultman K., Paulsen S.J., Wang J., Bugge A., Frantzen J.B.,
Noergaard P., Jeppesen J.F., Yang Z., Secher A., Chen H., Li X.,
John L.M., Shan B., He Z., Gao X., Su J., Hansen K.T., Yang W.,
Joergensen S.B.;
"GFRAL is the receptor for GDF15 and is required for the anti-obesity
effects of the ligand.";
Nat. Med. 23:1158-1166(2017).
[16]
FUNCTION, AND INTERACTION WITH GFRAL.
PubMed=28846098; DOI=10.1038/nm.4393;
Emmerson P.J., Wang F., Du Y., Liu Q., Pickard R.T., Gonciarz M.D.,
Coskun T., Hamang M.J., Sindelar D.K., Ballman K.K., Foltz L.A.,
Muppidi A., Alsina-Fernandez J., Barnard G.C., Tang J.X., Liu X.,
Mao X., Siegel R., Sloan J.H., Mitchell P.J., Zhang B.B., Gimeno R.E.,
Shan B., Wu X.;
"The metabolic effects of GDF15 are mediated by the orphan receptor
GFRAL.";
Nat. Med. 23:1215-1219(2017).
[17] {ECO:0000244|PDB:5VZ3, ECO:0000244|PDB:5VZ4}
X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 197-308 IN COMPLEX WITH
GFRAL, INTERACTION WITH GFRAL, FUNCTION, AND MUTAGENESIS OF VAL-283
AND ILE-285.
PubMed=28953886; DOI=10.1038/nature24042;
Hsu J.Y., Crawley S., Chen M., Ayupova D.A., Lindhout D.A., Higbee J.,
Kutach A., Joo W., Gao Z., Fu D., To C., Mondal K., Li B.,
Kekatpure A., Wang M., Laird T., Horner G., Chan J., McEntee M.,
Lopez M., Lakshminarasimhan D., White A., Wang S.P., Yao J., Yie J.,
Matern H., Solloway M., Haldankar R., Parsons T., Tang J., Shen W.D.,
Alice Chen Y., Tian H., Allan B.B.;
"Non-homeostatic body weight regulation through a brainstem-restricted
receptor for GDF15.";
Nature 550:255-259(2017).
[18]
ERRATUM.
PubMed=29144449; DOI=10.1038/nature24481;
Hsu J.Y., Crawley S., Chen M., Ayupova D.A., Lindhout D.A., Higbee J.,
Kutach A., Joo W., Gao Z., Fu D., To C., Mondal K., Li B.,
Kekatpure A., Wang M., Laird T., Horner G., Chan J., McEntee M.,
Lopez M., Lakshminarasimhan D., White A., Wang S.P., Yao J., Yie J.,
Matern H., Solloway M., Haldankar R., Parsons T., Tang J., Shen W.D.,
Alice Chen Y., Tian H., Allan B.B.;
"Non-homeostatic body weight regulation through a brainstem-restricted
receptor for GDF15.";
Nature 551:398-398(2017).
[19] {ECO:0000244|PDB:5VT2}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 197-308, FUNCTION, SUBUNIT,
INDUCTION BY OBESITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=29046435; DOI=10.1126/scitranslmed.aan8732;
Xiong Y., Walker K., Min X., Hale C., Tran T., Komorowski R., Yang J.,
Davda J., Nuanmanee N., Kemp D., Wang X., Liu H., Miller S., Lee K.J.,
Wang Z., Veniant M.M.;
"Long-acting MIC-1/GDF15 molecules to treat obesity: Evidence from
mice to monkeys.";
Sci. Transl. Med. 9:0-0(2017).
-!- FUNCTION: Regulates food intake, energy expenditure and body
weight in response to metabolic and toxin-induced stresses
(PubMed:28953886, PubMed:28846097, PubMed:28846098,
PubMed:28846099, PubMed:23468844, PubMed:29046435). Binds to its
receptor, GFRAL, and activates GFRAL-expressing neurons localized
in the area postrema and nucleus tractus solitarius of the
brainstem (PubMed:28953886, PubMed:28846097, PubMed:28846098,
PubMed:28846099). It then triggers the activation of neurons
localized within the parabrachial nucleus and central amygdala,
which contitutes part of the 'emergency circuit' that shapes
feeding responses to stressful conditions (PubMed:28953886). On
hepatocytes, inhibits growth hormone signaling (By similarity).
{ECO:0000250|UniProtKB:Q9Z0J7, ECO:0000269|PubMed:23468844,
ECO:0000269|PubMed:28846097, ECO:0000269|PubMed:28846098,
ECO:0000269|PubMed:28846099, ECO:0000269|PubMed:28953886,
ECO:0000269|PubMed:29046435}.
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:29046435). Interacts
with GFRAL; ligand of GFRAL which mediates GDF15 internalization
and cellular signaling through interaction with RET
(PubMed:28953886, PubMed:28846097, PubMed:28846098,
PubMed:28846099). {ECO:0000269|PubMed:28846097,
ECO:0000269|PubMed:28846098, ECO:0000269|PubMed:28846099,
ECO:0000269|PubMed:28953886, ECO:0000269|PubMed:29046435}.
-!- INTERACTION:
Q99750:MDFI; NbExp=6; IntAct=EBI-2116863, EBI-724076;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28572090,
ECO:0000269|PubMed:29046435}.
-!- TISSUE SPECIFICITY: Highly expressed in placenta, with lower
levels in prostate and colon and some expression in kidney
(PubMed:9348093). Detected in plasma (at protein level)
(PubMed:28572090, PubMed:29046435). {ECO:0000269|PubMed:28572090,
ECO:0000269|PubMed:29046435, ECO:0000269|PubMed:9348093}.
-!- INDUCTION: Expression is up-regulated by obesity.
{ECO:0000269|PubMed:29046435}.
-!- DISEASE: Note=Plasma levels are increased in children with
concomitant heart disease and failure to thrive but not in
children with heart disease and normal body weight.
{ECO:0000269|PubMed:28572090}.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/GDF15ID40701ch19p13.html";
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EMBL; U88323; AAB88913.1; -; mRNA.
EMBL; AB000584; BAA19151.1; -; mRNA.
EMBL; AF019770; AAB88673.1; -; mRNA.
EMBL; AF003934; AAC24456.1; -; mRNA.
EMBL; AK291530; BAF84219.1; -; mRNA.
EMBL; BT019465; AAV38272.1; -; mRNA.
EMBL; AC008397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471106; EAW84694.1; -; Genomic_DNA.
EMBL; BC000529; AAH00529.1; -; mRNA.
EMBL; BC008962; AAH08962.1; -; mRNA.
EMBL; AF008303; AAC39537.1; -; Genomic_DNA.
EMBL; AF173860; AAF89834.1; -; mRNA.
CCDS; CCDS12376.1; -.
PIR; JC5697; JC5697.
RefSeq; NP_004855.2; NM_004864.3.
UniGene; Hs.616962; -.
PDB; 5VT2; X-ray; 2.30 A; A/B=197-308.
PDB; 5VZ3; X-ray; 1.97 A; A=197-308.
PDB; 5VZ4; X-ray; 2.20 A; A=197-308.
PDBsum; 5VT2; -.
PDBsum; 5VZ3; -.
PDBsum; 5VZ4; -.
ProteinModelPortal; Q99988; -.
SMR; Q99988; -.
BioGrid; 114895; 13.
IntAct; Q99988; 13.
STRING; 9606.ENSP00000252809; -.
ChEMBL; CHEMBL3120039; -.
iPTMnet; Q99988; -.
PhosphoSitePlus; Q99988; -.
BioMuta; GDF15; -.
DMDM; 313104195; -.
EPD; Q99988; -.
MaxQB; Q99988; -.
PaxDb; Q99988; -.
PeptideAtlas; Q99988; -.
PRIDE; Q99988; -.
Ensembl; ENST00000252809; ENSP00000252809; ENSG00000130513.
GeneID; 9518; -.
KEGG; hsa:9518; -.
UCSC; uc002niv.2; human.
CTD; 9518; -.
DisGeNET; 9518; -.
EuPathDB; HostDB:ENSG00000130513.6; -.
GeneCards; GDF15; -.
H-InvDB; HIX0014912; -.
HGNC; HGNC:30142; GDF15.
HPA; CAB062554; -.
HPA; HPA011191; -.
MIM; 605312; gene.
neXtProt; NX_Q99988; -.
OpenTargets; ENSG00000130513; -.
PharmGKB; PA134866647; -.
eggNOG; KOG3900; Eukaryota.
eggNOG; ENOG410XT8Z; LUCA.
GeneTree; ENSGT00910000143982; -.
HOGENOM; HOG000143379; -.
HOVERGEN; HBG051718; -.
InParanoid; Q99988; -.
KO; K05504; -.
OMA; LGWADWV; -.
OrthoDB; EOG091G0IUS; -.
PhylomeDB; Q99988; -.
TreeFam; TF351787; -.
SIGNOR; Q99988; -.
ChiTaRS; GDF15; human.
GeneWiki; GDF15; -.
GenomeRNAi; 9518; -.
PMAP-CutDB; Q9BWA0; -.
PRO; PR:Q99988; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000130513; -.
CleanEx; HS_GDF15; -.
ExpressionAtlas; Q99988; baseline and differential.
Genevisible; Q99988; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:ProtInc.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IBA:GO_Central.
GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
GO; GO:0048468; P:cell development; IBA:GO_Central.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:1901741; P:positive regulation of myoblast fusion; IEA:Ensembl.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0060395; P:SMAD protein signal transduction; IDA:UniProtKB.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:ProtInc.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR001839; TGF-b_C.
InterPro; IPR015615; TGF-beta-rel.
PANTHER; PTHR11848; PTHR11848; 1.
Pfam; PF00019; TGF_beta; 1.
SMART; SM00204; TGFB; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS51362; TGF_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues; Complete proteome;
Cytokine; Disulfide bond; Glycoprotein; Growth factor; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 29 {ECO:0000255}.
PROPEP 30 194 {ECO:0000255}.
/FTId=PRO_0000033992.
CHAIN 195 308 Growth/differentiation factor 15.
/FTId=PRO_0000033993.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 203 210 {ECO:0000244|PDB:5VT2,
ECO:0000244|PDB:5VZ3,
ECO:0000244|PDB:5VZ4,
ECO:0000269|PubMed:28953886,
ECO:0000269|PubMed:29046435}.
DISULFID 211 274 {ECO:0000244|PDB:5VT2,
ECO:0000244|PDB:5VZ3,
ECO:0000244|PDB:5VZ4,
ECO:0000269|PubMed:28953886,
ECO:0000269|PubMed:29046435}.
DISULFID 240 305 {ECO:0000244|PDB:5VT2,
ECO:0000244|PDB:5VZ3,
ECO:0000244|PDB:5VZ4,
ECO:0000269|PubMed:28953886,
ECO:0000269|PubMed:29046435}.
DISULFID 244 307 {ECO:0000244|PDB:5VT2,
ECO:0000244|PDB:5VZ3,
ECO:0000244|PDB:5VZ4,
ECO:0000269|PubMed:28953886,
ECO:0000269|PubMed:29046435}.
DISULFID 273 273 Interchain. {ECO:0000244|PDB:5VT2,
ECO:0000269|PubMed:29046435}.
VARIANT 9 9 V -> L (in dbSNP:rs1059519).
{ECO:0000269|PubMed:9326641,
ECO:0000269|PubMed:9348093,
ECO:0000269|PubMed:9593718,
ECO:0000269|Ref.5}.
/FTId=VAR_047646.
VARIANT 48 48 S -> T (in dbSNP:rs1059369).
{ECO:0000269|PubMed:9326641,
ECO:0000269|PubMed:9348093,
ECO:0000269|Ref.5}.
/FTId=VAR_010386.
VARIANT 202 202 H -> D (in dbSNP:rs1058587).
{ECO:0000269|PubMed:9375789}.
/FTId=VAR_047647.
MUTAGEN 225 225 W->A: No effect on interaction with
GFRAL. Attenuates GDF15-mediated food-
intake inhibition.
{ECO:0000269|PubMed:28846097}.
MUTAGEN 283 283 V->A: Reduces cellular signaling mediated
by GFRAL and RET.
{ECO:0000269|PubMed:28953886}.
MUTAGEN 283 283 V->R: Abolishes interaction with GFRAL.
Abolishes RET phosphorylation and
cellular signaling mediated by GFRAL and
RET. {ECO:0000269|PubMed:28846099}.
MUTAGEN 285 285 I->A: Reduces cellular signaling mediated
by GFRAL and RET. Abolishes interaction
with GFRAL and GDF15-mediated food-intake
inhibition. {ECO:0000269|PubMed:28846097,
ECO:0000269|PubMed:28953886}.
CONFLICT 269 269 V -> E (in Ref. 1; AAB88913).
{ECO:0000305}.
CONFLICT 288 288 T -> A (in Ref. 10; AAF89834).
{ECO:0000305}.
STRAND 204 219 {ECO:0000244|PDB:5VZ3}.
TURN 220 224 {ECO:0000244|PDB:5VZ3}.
TURN 226 228 {ECO:0000244|PDB:5VZ3}.
STRAND 229 231 {ECO:0000244|PDB:5VZ3}.
STRAND 233 243 {ECO:0000244|PDB:5VZ3}.
STRAND 248 250 {ECO:0000244|PDB:5VZ3}.
HELIX 253 264 {ECO:0000244|PDB:5VZ3}.
TURN 266 268 {ECO:0000244|PDB:5VZ3}.
STRAND 273 287 {ECO:0000244|PDB:5VZ3}.
STRAND 289 308 {ECO:0000244|PDB:5VZ3}.
SEQUENCE 308 AA; 34140 MW; 2FF3959021B95238 CRC64;
MPGQELRTVN GSQMLLVLLV LSWLPHGGAL SLAEASRASF PGPSELHSED SRFRELRKRY
EDLLTRLRAN QSWEDSNTDL VPAPAVRILT PEVRLGSGGH LHLRISRAAL PEGLPEASRL
HRALFRLSPT ASRSWDVTRP LRRQLSLARP QAPALHLRLS PPPSQSDQLL AESSSARPQL
ELHLRPQAAR GRRRARARNG DHCPLGPGRC CRLHTVRASL EDLGWADWVL SPREVQVTMC
IGACPSQFRA ANMHAQIKTS LHRLKPDTVP APCCVPASYN PMVLIQKTDT GVSLQTYDDL
LAKDCHCI


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