ID   DECA_TRICA              Reviewed;         372 AA.
AC   Q26974;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Protein decapentaplegic;
DE   Flags: Precursor;
GN   Name=dpp;
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Sanchez-Salazar J., Pletcher M.T., Bennett R.L., Brown S.J.,
RA   Dandamudi T.J., Denell R.E., Doctor J.S.;
RT   "The Tribolium decapentaplegic gene is similar in sequence, structure, and
RT   expression to the Drosophila dpp gene.";
RL   Dev. Genes Evol. 206:237-246(1996).
CC   -!- FUNCTION: Acts as an extracellular morphogen to establish at least two
CC       cellular response thresholds within the dorsal half of the drosophila
CC       embryo. Required for the proper development of the embryonic dorsal
CC       hypoderm, for viability of larvae and for cell viability of the
CC       epithelial cells in the imaginal disks. Acts together with scw (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer or heterodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR   EMBL; U63132; AAB38392.1; -; Genomic_DNA.
DR   RefSeq; NP_001034540.1; NM_001039451.1.
DR   RefSeq; XP_008192737.1; XM_008194515.2.
DR   RefSeq; XP_008192738.1; XM_008194516.2.
DR   RefSeq; XP_008192739.1; XM_008194517.2.
DR   RefSeq; XP_015834296.1; XM_015978810.1.
DR   RefSeq; XP_015834297.1; XM_015978811.1.
DR   AlphaFoldDB; Q26974; -.
DR   SMR; Q26974; -.
DR   STRING; 7070.TC008466-PA; -.
DR   EnsemblMetazoa; TC008466_001; TC008466_001; TC008466.
DR   GeneID; 654513; -.
DR   KEGG; tca:654513; -.
DR   CTD; 33432; -.
DR   eggNOG; KOG3900; Eukaryota.
DR   HOGENOM; CLU_020515_4_1_1; -.
DR   OMA; HEEHMEQ; -.
DR   OrthoDB; 962484at2759; -.
DR   PhylomeDB; Q26974; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0010033; P:response to organic substance; IEA:UniProt.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR001839; TGF-b_C.
DR   InterPro; IPR001111; TGF-b_propeptide.
DR   InterPro; IPR015615; TGF-beta-rel.
DR   InterPro; IPR017948; TGFb_CS.
DR   PANTHER; PTHR11848; PTHR11848; 1.
DR   Pfam; PF00019; TGF_beta; 1.
DR   Pfam; PF00688; TGFb_propeptide; 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   3: Inferred from homology;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Growth factor; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033670"
FT   CHAIN           ?..372
FT                   /note="Protein decapentaplegic"
FT                   /id="PRO_0000033671"
FT   REGION          237..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        271..337
FT                   /evidence="ECO:0000250"
FT   DISULFID        300..369
FT                   /evidence="ECO:0000250"
FT   DISULFID        304..371
FT                   /evidence="ECO:0000250"
FT   DISULFID        336
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   372 AA;  42435 MW;  C9991AB75D2E3173 CRC64;
     MRLNMLIYLI VACCWGKSLS IPQQILNEFK STLLPLFGLK EQPKIEGKVQ VPEALKKIYN
     IQNNFEYDTA SLPLPGLYTK SANTIRSFTH VESPIDEKFV HPHRFRLKFN ISSIPRHEKL
     TAAEIKLTRE TAKNTSHPFQ RVLVHDILQP GVKGLHGPIT RVIDSKVVDS RKNTTVSIDV
     FPAVARWMQD PKTNHGILIV VYSIGAKKSP PEKHLRLRRD TAPPQWYQHQ PLLFTYTDDG
     KNQQRTGTEL TKMRPKRQSS RRHRKNLKDP CRRRQMYVDF GSVGWNDWIV APLGYDAYYC
     GGECEYPIPD HMNTTNHAIV QSLVNSMKPK EVPGPCCVPT QLGQMSMLYL GSDGSVILKN
     YKEMVVVGCG CR