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DECA_DROPS
ID   DECA_DROPS              Reviewed;         616 AA.
AC   P91699; Q29KY8; Q56RP3;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 3.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Protein decapentaplegic;
DE            Short=Protein DPP-C;
DE   Flags: Precursor;
GN   Name=dpp; ORFNames=GA22099;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9071585; DOI=10.1093/genetics/145.2.297;
RA   Newfeld S.J., Padgett R.W., Findley S.D., Richter B.G., Sanicola M.,
RA   de Cuevas M., Gelbart W.M.;
RT   "Molecular evolution at the decapentaplegic locus in Drosophila.";
RL   Genetics 145:297-309(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-333.
RX   PubMed=15545653; DOI=10.1534/genetics.104.033068;
RA   Bartolome C., Maside X., Yi S., Grant A.L., Charlesworth B.;
RT   "Patterns of selection on synonymous and nonsynonymous variants in
RT   Drosophila miranda.";
RL   Genetics 169:1495-1507(2005).
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: Heterodimers of scw/dpp are the active subunit, dpp/dpp
CC       homodimers elicit a basal response and scw/scw homodimers alone are
CC       ineffective in specifying a dorsal pattern. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Is internalized by receptor-
CC       mediated endocytosis. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in the imaginal discs associated with
CC       establishment of the proximal-distal axis of the appendages, and midgut
CC       mesoderm.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL33036.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; U63856; AAC47553.1; -; Genomic_DNA.
DR   EMBL; CH379061; EAL33036.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY754464; AAX13039.1; -; Genomic_DNA.
DR   AlphaFoldDB; P91699; -.
DR   SMR; P91699; -.
DR   STRING; 7237.FBpp0287762; -.
DR   PRIDE; P91699; -.
DR   eggNOG; KOG3900; Eukaryota.
DR   InParanoid; P91699; -.
DR   Proteomes; UP000001819; Genome assembly.
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   2: Evidence at transcript level;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Growth factor; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..474
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000033666"
FT   CHAIN           475..616
FT                   /note="Protein decapentaplegic"
FT                   /id="PRO_0000033667"
FT   REGION          80..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        360
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        557
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        515..581
FT                   /evidence="ECO:0000250"
FT   DISULFID        544..613
FT                   /evidence="ECO:0000250"
FT   DISULFID        548..615
FT                   /evidence="ECO:0000250"
FT   DISULFID        580
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        45
FT                   /note="A -> AAAA (in Ref. 3; AAX13039)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54
FT                   /note="T -> TAT (in Ref. 1; AAC47553 and 3; AAX13039)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95..96
FT                   /note="Missing (in Ref. 3; AAX13039)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="Q -> QQQQ (in Ref. 1; AAC47553)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        179
FT                   /note="T -> A (in Ref. 1; AAC47553)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   616 AA;  68512 MW;  413349FE288F48B8 CRC64;
     MRAWILLLAV LATSQPIVQV ASTEDTSISQ RFIAAIAPTR TEPSAASAAA AAATATATAT
     ATTALAKAFN PFNELLYKSS DSDSDNNNNN YKNRNNNNNN LNKGPRNNKN KGNKHSKSDA
     NRQFNEVHKP RTDQLENSKN KPKQLVNKTN KMAVKDQKHH QPQQQQQQHH KPATTTALTS
     TESHQSPIET IFVDDPALAL EEEVASINVP ANAGAIIEEQ EPSTYSKKEL IKDKLKPDPS
     TLVEIENSLL SLFNMKRPPK IDRSKIIIPE AMKKLYAEIM GHELDSVNIP RPGLLTKSAN
     TVRSFTHKDS KIDDRFPHHH RFRLHFDVKS IPAEEKLKAA ELQLTRDALA QAAVASTSAN
     RTRYQVLVYD ITRVGVRGQR EPSYLLLDTK TVRLNSTDTV SLDVQPAVDR WLATPQKNYG
     LLVEVRTMRS LKPAPHHHVR LRRSADEAHE QWQHKQPLLF AYTDDGRHKA RSIRDVSGGG
     GGGGGAGEGG KGNGGGRNRR HQRRPARRKN HEETCRRHSL YVDFADVGWD DWIVAPPGYD
     AYYCHGKCPF PLADHFNSTN HAVVQTLVNN LNPGKVPKAC CVPTQLDSVA MLYLNDQSTV
     VLKNYQEMTV VGCGCR
 
 
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