ID   NOGG_XENLA              Reviewed;         222 AA.
AC   P49011;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Noggin;
DE   Flags: Precursor;
GN   Name=nog;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1339313; DOI=10.1016/0092-8674(92)90316-5;
RA   Smith W.C., Harland R.M.;
RT   "Expression cloning of noggin, a new dorsalizing factor localized to the
RT   Spemann organizer in Xenopus embryos.";
RL   Cell 70:829-840(1992).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=8429909; DOI=10.1038/361547a0;
RA   Smith W.C., Knecht A.K., Wu M., Harland R.M.;
RT   "Secreted noggin protein mimics the Spemann organizer in dorsalizing
RT   Xenopus mesoderm.";
RL   Nature 361:547-549(1993).
RN   [3]
RP   FUNCTION.
RX   PubMed=8752214; DOI=10.1016/s0092-8674(00)80133-6;
RA   Zimmerman L.B., De Jesus-Escobar J.M., Harland R.M.;
RT   "The Spemann organizer signal noggin binds and inactivates bone
RT   morphogenetic protein 4.";
RL   Cell 86:599-606(1996).
CC   -!- FUNCTION: Patterns the embryo by interrupting bone morphogenetic
CC       proteins (BMP) signaling. Binds BMP-4 and BMP-2 with high affinity. Can
CC       abolish BMP-4 activity by blocking binding to cognate cell-surface
CC       receptors. Capable of inducing dorsal development in embryos. Causes
CC       dorsal mesodermal differentiation of animal cap ectoderm when
CC       coexpressed with xWNT-8 and nuclear, sequence-specific DNA-binding
CC       protein xBRA. None of these molecules causes dorsal mesoderm formation
CC       when expressed alone. {ECO:0000269|PubMed:8752214}.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expression starts at late blastula stages in the dorsal marginal zone
CC       and persists throughout gastrulation in the prechordal plat and the
CC       presumptive notochord, both derivatives of the Spemann organizer. At
CC       later stages expression is initiated at several new sites, including
CC       the roof plate of the neural tube and skeletogenic cells in the
CC       branchial arches.
CC   -!- INDUCTION: By activin.
CC   -!- SIMILARITY: Belongs to the noggin family. {ECO:0000305}.
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DR   EMBL; M98807; AAA49916.1; -; mRNA.
DR   PIR; A43343; A43343.
DR   RefSeq; NP_001079113.1; NM_001085644.1.
DR   AlphaFoldDB; P49011; -.
DR   SMR; P49011; -.
DR   GeneID; 373646; -.
DR   KEGG; xla:373646; -.
DR   CTD; 373646; -.
DR   Xenbase; XB-GENE-864891; nog.L.
DR   OMA; FCPVVYA; -.
DR   OrthoDB; 1391421at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 373646; Expressed in gastrula and 16 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007517; P:muscle organ development; IPI:UniProtKB.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:CACAO.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; IEA:InterPro.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR008717; Noggin.
DR   PANTHER; PTHR10494; PTHR10494; 1.
DR   PIRSF; PIRSF008129; Noggin; 1.
DR   SUPFAM; SSF57501; SSF57501; 1.
PE   1: Evidence at protein level;
KW   Chondrogenesis; Developmental protein; Differentiation; Disulfide bond;
KW   Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..222
FT                   /note="Noggin"
FT                   /id="PRO_0000019821"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        145..182
FT                   /evidence="ECO:0000250"
FT   DISULFID        168..218
FT                   /evidence="ECO:0000250"
FT   DISULFID        174..220
FT                   /evidence="ECO:0000250"
FT   DISULFID        197..205
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   222 AA;  25799 MW;  99A11096CD21A8C3 CRC64;
     MDHSQCLVTI YALMVFLGLR IDQGGCQHYL HIRPAPSENL PLVDLIEHPD PIYDPKEKDL
     NETLLRTLMV GHFDPNFMAT ILPEERLGVE DLGELDLLLR QKPSGAMPAE IKGLEFYEGL
     QSKKHRLSKK LRRKLQMWLW SQTFCPVLYT WNDLGTRFWP RYVKVGSCYS KRSCSVPEGM
     VCKAAKSMHL TILRWRCQRR VQQKCAWITI QYPVISECKC SC