ID I3NCG8_ICTTR Unreviewed; 184 AA.
AC I3NCG8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Gremlin {ECO:0000256|PIRNR:PIRNR037254};
GN Name=GREM1 {ECO:0000313|Ensembl:ENSSTOP00000022065.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000022065.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000022065.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|PIRNR:PIRNR037254}.
CC -!- SIMILARITY: Belongs to the DAN family. {ECO:0000256|ARBA:ARBA00007872,
CC ECO:0000256|PIRNR:PIRNR037254}.
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DR EMBL; AGTP01091567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005337192.1; XM_005337135.1.
DR AlphaFoldDB; I3NCG8; -.
DR STRING; 43179.ENSSTOP00000022065; -.
DR Ensembl; ENSSTOT00000010058.1; ENSSTOP00000022065.1; ENSSTOG00000010068.1.
DR GeneID; 101973472; -.
DR CTD; 26585; -.
DR eggNOG; ENOG502QQ5X; Eukaryota.
DR GeneTree; ENSGT00940000154209; -.
DR HOGENOM; CLU_101024_0_0_1; -.
DR InParanoid; I3NCG8; -.
DR OMA; TIHEDGC; -.
DR OrthoDB; 5347549at2759; -.
DR TreeFam; TF106445; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
DR GO; GO:0036122; F:BMP binding; IEA:Ensembl.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IEA:Ensembl.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IEA:Ensembl.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; IEA:Ensembl.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0007267; P:cell-cell signaling; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0048263; P:determination of dorsal identity; IEA:Ensembl.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
DR GO; GO:0003337; P:mesenchymal to epithelial transition involved in metanephros morphogenesis; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:1900158; P:negative regulation of bone mineralization involved in bone maturation; IEA:Ensembl.
DR GO; GO:0046851; P:negative regulation of bone remodeling; IEA:Ensembl.
DR GO; GO:1900155; P:negative regulation of bone trabecula formation; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; IEA:Ensembl.
DR GO; GO:0090291; P:negative regulation of osteoclast proliferation; IEA:Ensembl.
DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; IEA:Ensembl.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0060676; P:ureteric bud formation; IEA:Ensembl.
DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 1.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR004133; DAN.
DR InterPro; IPR017159; Gremlin-1/2.
DR PANTHER; PTHR15283; GREMLIN 1; 1.
DR PANTHER; PTHR15283:SF3; GREMLIN-1; 1.
DR Pfam; PF03045; DAN; 1.
DR PIRSF; PIRSF037254; Gremlin_precursor; 1.
DR SMART; SM00041; CT; 1.
PE 3: Inferred from homology;
KW Cytokine {ECO:0000256|ARBA:ARBA00022514, ECO:0000256|PIRNR:PIRNR037254};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR037254-1};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR037254};
KW Signal {ECO:0000256|PIRNR:PIRNR037254}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|PIRNR:PIRNR037254"
FT CHAIN 25..184
FT /note="Gremlin"
FT /evidence="ECO:0000256|PIRNR:PIRNR037254"
FT /id="PRO_5005153532"
FT DOMAIN 96..183
FT /note="CTCK"
FT /evidence="ECO:0000259|SMART:SM00041"
FT REGION 23..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 94..144
FT /evidence="ECO:0000256|PIRSR:PIRSR037254-1"
FT DISULFID 108..158
FT /evidence="ECO:0000256|PIRSR:PIRSR037254-1"
FT DISULFID 118..176
FT /evidence="ECO:0000256|PIRSR:PIRSR037254-1"
FT DISULFID 122..178
FT /evidence="ECO:0000256|PIRSR:PIRSR037254-1"
SQ SEQUENCE 184 AA; 20715 MW; 436D90998F572B20 CRC64;
MSRTAYTVGA LLLLLGTLMP AAEGKKKGSQ GAIPPPDKAQ HNDSEQTQSP QQPGSRNRGR
GQGRGTAMPG EEVLESSQEA LHVTERKYLK RDWCKTQPLK QTIHEEGCNS RTIINRFCYG
QCNSFYIPRH IRKEEGSFQS CSFCKPKKFT TMMVTLNCPE LQPPTKKKRV TRVKQCRCIS
IDLD
//
