ID   GREM1_MACMU             Reviewed;         184 AA.
AC   Q8WNY1;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Gremlin-1;
DE   Flags: Precursor;
GN   Name=GREM1;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Christenson L.K., Duffy D.M.;
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cytokine that may play an important role during
CC       carcinogenesis and metanephric kidney organogenesis, as a BMP
CC       antagonist required for early limb outgrowth and patterning in
CC       maintaining the FGF4-SHH feedback loop. Down-regulates the BMP4
CC       signaling in a dose-dependent manner (By similarity). Antagonist of
CC       BMP2; inhibits BMP2-mediated differentiation of osteoblasts (in vitro)
CC       (By similarity). Acts as inhibitor of monocyte chemotaxis. Can inhibit
CC       the growth or viability of normal cells but not transformed cells when
CC       is overexpressed (By similarity). {ECO:0000250|UniProtKB:O35793,
CC       ECO:0000250|UniProtKB:O60565, ECO:0000250|UniProtKB:O70326}.
CC   -!- SUBUNIT: Homodimer; can also form homooligomers. Interacts with BMP2;
CC       can form higher oligomers with BMP2 (By similarity). Interacts with
CC       SLIT1 and SLIT2 in a glycosylation-dependent manner (By similarity).
CC       {ECO:0000250|UniProtKB:O35793, ECO:0000250|UniProtKB:O60565}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DAN family. {ECO:0000305}.
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DR   EMBL; AF439783; AAL32022.1; -; mRNA.
DR   RefSeq; NP_001028020.1; NM_001032848.1.
DR   AlphaFoldDB; Q8WNY1; -.
DR   SMR; Q8WNY1; -.
DR   STRING; 9544.ENSMMUP00000002409; -.
DR   GeneID; 574176; -.
DR   KEGG; mcc:574176; -.
DR   CTD; 26585; -.
DR   eggNOG; ENOG502QQ5X; Eukaryota.
DR   HOGENOM; CLU_101024_0_0_1; -.
DR   InParanoid; Q8WNY1; -.
DR   OMA; MPRTRCA; -.
DR   OrthoDB; 1270652at2759; -.
DR   TreeFam; TF106445; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0036122; F:BMP binding; ISS:UniProtKB.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0048018; F:receptor ligand activity; IBA:GO_Central.
DR   GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0038098; P:sequestering of BMP from receptor via BMP binding; IBA:GO_Central.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR006207; Cys_knot_C.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR004133; DAN.
DR   InterPro; IPR017159; Gremlin-1/2.
DR   Pfam; PF03045; DAN; 1.
DR   PIRSF; PIRSF037254; Gremlin_precursor; 1.
DR   SMART; SM00041; CT; 1.
PE   2: Evidence at transcript level;
KW   Cytokine; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..184
FT                   /note="Gremlin-1"
FT                   /id="PRO_0000006715"
FT   DOMAIN          94..184
FT                   /note="CTCK"
FT   REGION          24..77
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   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        94..144
FT                   /evidence="ECO:0000250|UniProtKB:O60565"
FT   DISULFID        108..158
FT                   /evidence="ECO:0000250|UniProtKB:O60565"
FT   DISULFID        118..176
FT                   /evidence="ECO:0000250|UniProtKB:O60565"
FT   DISULFID        122..178
FT                   /evidence="ECO:0000250|UniProtKB:O60565"
SQ   SEQUENCE   184 AA;  20697 MW;  4B588598DE12C47E CRC64;
     MSRTAYTVGA LLLLLGTLLP AAEGKKKGSQ GAIPPPDKAQ HNDSEQTQSP QQPGSRNRGR
     GQGRGTAMPG EEVLESSQEA LHVTERKYLK RDWCKTQPLK QTIHEEGCNS RTIINRFCYG
     QCNSFYIPRH IRKEEGSFQS CSFCKPKKFT TMMVTLNCPE LQPPTKKKRV TRVKQCRCIS
     IDLD