GDF10_XENLA
ID GDF10_XENLA Reviewed; 443 AA.
AC Q7T2X6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Growth/differentiation factor 10;
DE Short=GDF-10;
DE AltName: Full=Bone morphogenetic protein 3B;
DE Short=BMP-3B;
DE Short=xBMP-3B;
DE Flags: Precursor;
GN Name=gdf10; Synonyms=bmp3b;
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], FUNCTION, INTERACTION WITH ADMP; BMP2; DERRIERE
RP AND NODAL, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12885561; DOI=10.1016/s0012-1606(03)00223-9;
RA Hino J., Nishimatsu S., Nagai T., Matsuo H., Kangawa K., Nohno T.;
RT "Coordination of BMP-3b and cerberus is required for head formation of
RT Xenopus embryos.";
RL Dev. Biol. 260:138-157(2003).
CC -!- FUNCTION: Dorsalizing factor. Antagonizes mesoderm formation by nodal-
CC like proteins and ventralizing BMPs. Cooperates with cer1 to promote
CC embryonic head formation. {ECO:0000269|PubMed:12885561}.
CC -!- SUBUNIT: Homodimer. Can form heterodimers with admp, bmp2-I and/or
CC bmp2-II, derriere and nodal/nr-1.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12885561}.
CC -!- DEVELOPMENTAL STAGE: Tends to mark the dorsal ectodermal and mesodermal
CC cells. Initially expressed in the dorsal-lateral ectoderm, and
CC subsequently extends through the entire neural plate at the neurula
CC stage. Also expressed in the prechordal plate. Prechordal plate
CC mesoderm specifies anterior neuroectoderm and pharyngeal endoderm,
CC which are progenitors for the formation of head structures. At the
CC hatching stage, enriched from the dorsal mesenchyme to the olfactory
CC pit and optic cup. {ECO:0000269|PubMed:12885561}.
CC -!- DOMAIN: The region required for head formation is located in the
CC propeptide, which itself interferes with proteolytic processing of the
CC precursor. The mature region has the same activity as that of BMP3.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; AB059564; BAC77408.1; -; mRNA.
DR RefSeq; NP_001082633.1; NM_001089164.1.
DR AlphaFoldDB; Q7T2X6; -.
DR SMR; Q7T2X6; -.
DR GeneID; 398614; -.
DR KEGG; xla:398614; -.
DR CTD; 398614; -.
DR Xenbase; XB-GENE-5998699; gdf10.L.
DR OMA; YRKEDLW; -.
DR OrthoDB; 1002140at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 398614; Expressed in zone of skin and 7 other tissues.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0016015; F:morphogen activity; IEA:UniProtKB-KW.
DR GO; GO:0038100; F:nodal binding; IPI:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProtKB-KW.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:InterPro.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR017197; BMP3/BMP3B.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR PIRSF; PIRSF037403; BMP3/GDF10; 1.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Cytokine; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Growth factor; Morphogen;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..333
FT /evidence="ECO:0000255"
FT /id="PRO_0000033850"
FT CHAIN 334..443
FT /note="Growth/differentiation factor 10"
FT /id="PRO_0000033851"
FT REGION 99..202
FT /note="Induces head formation"
FT REGION 236..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 341..408
FT /evidence="ECO:0000250"
FT DISULFID 370..440
FT /evidence="ECO:0000250"
FT DISULFID 374..442
FT /evidence="ECO:0000250"
FT DISULFID 407
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 443 AA; 50657 MW; 32B5545845CA0ADF CRC64;
MQFSLVMSYY CLACFLVMFA LGRAIKAHTS KLPPEGVGTI RLQSDPLSLH MAKLYEKYSR
EGSRLQDGNT VRSFRAQPDS QFGSPLYRFN LSSLQQTEEV LAATLHFAPV KGSRSSRDSY
CKRSKKSSCR LLLPTQHQKI SLVFKSVIQN KTLGSEKWNT TNIFHKRAAW HVKDITNIIK
DAQHERDLFI SMEISFGEKF ATVFENNPSE LPYILVFADD RAISDPNSIA LTLQRYDPFQ
PNGGNSKQAP NTFPESRVKR DTSDLASSHD NELPDIKYMR YSKEDLWEST YKSLKHKSPR
KEKKKKGQEN EETLPKSPVL HFDERTMKKA RRRQWDEPRV CSRRYLKVDF ADIGWSEWII
SPKSFDAYYC SGACEFPMAK VVRPSNHATI QSIVKAVGII PGVPEPCCTP DMMNSLSVLF
LDEGRNMVLK VYPNMSVESC SCR
