位置:首页 > 蛋白库 > SRYD_DROME
SRYD_DROME
ID   SRYD_DROME              Reviewed;         433 AA.
AC   P07664; Q9VAB3;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 192.
DE   RecName: Full=Serendipity locus protein delta;
GN   Name=Sry-delta; Synonyms=Sry-d; ORFNames=CG17958;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=Oregon-R;
RX   PubMed=3935797; DOI=10.1016/0022-2836(85)90265-7;
RA   Vincent A., Colot H.V., Rosbash M.;
RT   "Sequence and structure of the serendipity locus of Drosophila
RT   melanogaster. A densely transcribed region including a blastoderm-specific
RT   gene.";
RL   J. Mol. Biol. 186:149-166(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 339-433, AND DEVELOPMENTAL STAGE.
RX   PubMed=6329730; DOI=10.1002/j.1460-2075.1984.tb01920.x;
RA   Vincent A., O'Connell P., Gray M.R., Rosbash M.;
RT   "Drosophila maternal and embryo mRNAs transcribed from a single
RT   transcription unit use alternate combinations of exons.";
RL   EMBO J. 3:1003-1013(1984).
RN   [6]
RP   DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=2081456; DOI=10.1242/dev.110.1.141;
RA   Payre F., Noselli S., Lefrere V., Vincent A.;
RT   "The closely related Drosophila sry beta and sry delta zinc finger proteins
RT   show differential embryonic expression and distinct patterns of binding
RT   sites on polytene chromosomes.";
RL   Development 110:141-149(1990).
RN   [7]
RP   NUCLEAR LOCALIZATION SIGNAL.
RX   PubMed=1849091; DOI=10.1016/0014-5793(91)80229-v;
RA   Noselli S., Vincent A.;
RT   "A Drosophila nuclear localisation signal included in an 18 amino acid
RT   fragment from the serendipity delta zinc finger protein.";
RL   FEBS Lett. 280:167-170(1991).
RN   [8]
RP   DNA-BINDING SPECIFICITY.
RX   PubMed=1868833; DOI=10.1002/j.1460-2075.1991.tb07793.x;
RA   Payre F., Vincent A.;
RT   "Genomic targets of the serendipity beta and delta zinc finger proteins and
RT   their respective DNA recognition sites.";
RL   EMBO J. 10:2533-2541(1991).
RN   [9]
RP   FUNCTION, DNA-BINDING, AND HOMODIMERIZATION.
RX   PubMed=9154812; DOI=10.1128/mcb.17.6.3137;
RA   Payre F., Buono P., Vanzo N., Vincent A.;
RT   "Two types of zinc fingers are required for dimerization of the serendipity
RT   delta transcriptional activator.";
RL   Mol. Cell. Biol. 17:3137-3145(1997).
RN   [10]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=9858707; DOI=10.1016/s0925-4773(98)00159-2;
RA   Ruez C., Payre F., Vincent A.;
RT   "Transcriptional control of Drosophila bicoid by Serendipity delta:
RT   cooperative binding sites, promoter context, and co-evolution.";
RL   Mech. Dev. 78:125-134(1998).
CC   -!- FUNCTION: Transcriptional activator that controls bicoid gene
CC       expression during oogenesis. Found in transcriptionally active cells.
CC       Binds to specific sites on polytene chromosomes of third instar larvae.
CC       Binds to the consensus DNA sequence 5'-YTAGAGATGGRAA-3'.
CC       {ECO:0000269|PubMed:9154812, ECO:0000269|PubMed:9858707}.
CC   -!- SUBUNIT: Binds DNA as a homodimer. N-terminal regions of the protein
CC       are required, in addition to the zinc fingers, for the specificity of
CC       chromatin-binding.
CC   -!- INTERACTION:
CC       P07664; Q7JN06: BEAF-32; NbExp=4; IntAct=EBI-498092, EBI-134484;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2081456}.
CC   -!- TISSUE SPECIFICITY: Predominantly localized to the sub- and
CC       supraesophagal ganglia and the ventral nerve cord in the embryo, after
CC       dorsal closure. {ECO:0000269|PubMed:2081456}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Found
CC       in ovaries and abundant in early embryos. Also found in variable
CC       amounts at every stage of the life cycle. {ECO:0000269|PubMed:2081456,
CC       ECO:0000269|PubMed:3935797, ECO:0000269|PubMed:6329730}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X03121; CAA26898.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF57000.1; -; Genomic_DNA.
DR   EMBL; AY069691; AAL39836.1; -; mRNA.
DR   EMBL; X00555; CAA25221.1; -; Genomic_DNA.
DR   PIR; C23351; C23351.
DR   RefSeq; NP_524581.1; NM_079842.3.
DR   PDB; 7POH; X-ray; 2.85 A; A/B=1-90.
DR   PDBsum; 7POH; -.
DR   AlphaFoldDB; P07664; -.
DR   SMR; P07664; -.
DR   BioGRID; 68428; 10.
DR   IntAct; P07664; 8.
DR   STRING; 7227.FBpp0084924; -.
DR   PaxDb; P07664; -.
DR   DNASU; 43572; -.
DR   EnsemblMetazoa; FBtr0085558; FBpp0084924; FBgn0003512.
DR   GeneID; 43572; -.
DR   KEGG; dme:Dmel_CG17958; -.
DR   CTD; 43572; -.
DR   FlyBase; FBgn0003512; Sry-delta.
DR   VEuPathDB; VectorBase:FBgn0003512; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000164700; -.
DR   HOGENOM; CLU_776751_0_0_1; -.
DR   InParanoid; P07664; -.
DR   OMA; HINEDHS; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; P07664; -.
DR   BioGRID-ORCS; 43572; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 43572; -.
DR   PRO; PR:P07664; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0003512; Expressed in ovary and 11 other tissues.
DR   Genevisible; P07664; DM.
DR   GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005705; C:polytene chromosome interband; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0008595; P:anterior/posterior axis specification, embryo; IMP:FlyBase.
DR   GO; GO:0045450; P:bicoid mRNA localization; IMP:UniProtKB.
DR   GO; GO:0048477; P:oogenesis; IGI:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0019953; P:sexual reproduction; IEP:FlyBase.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Developmental protein; DNA-binding; Metal-binding;
KW   Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..433
FT                   /note="Serendipity locus protein delta"
FT                   /id="PRO_0000047050"
FT   ZN_FING         194..217
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         223..245
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         251..273
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         279..301
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         308..330
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         337..359
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         405..428
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          141..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           187..193
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:1849091"
FT   COMPBIAS        145..162
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        62
FT                   /note="Missing (in Ref. 1; CAA26898)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272
FT                   /note="M -> S (in Ref. 1; CAA26898)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        393
FT                   /note="V -> F (in Ref. 1 and 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        413
FT                   /note="N -> T (in Ref. 1 and 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        431..433
FT                   /note="VLK -> S (in Ref. 1 and 5)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..4
FT                   /evidence="ECO:0007829|PDB:7POH"
FT   TURN            31..33
FT                   /evidence="ECO:0007829|PDB:7POH"
FT   HELIX           37..47
FT                   /evidence="ECO:0007829|PDB:7POH"
FT   HELIX           62..90
FT                   /evidence="ECO:0007829|PDB:7POH"
SQ   SEQUENCE   433 AA;  50028 MW;  9F89FB7696ECF3F7 CRC64;
     MDTCFFCGAV DLSDTGSSSS MRYETLSAKV PSSQKTVSLV LTHLANCIQT QLDLKPGARL
     CPRCFQELSD YDTIMVNLMT TQKRLTTQLK GALKSEFEVP ESGEDILVEE VEIPQSDVET
     DADAEADALF VELVKDQEES DTEIKREFVD EEEEEDDDDD DEFICEDVDV GDSEALYGKS
     SDGEDRPTKK RVKQECTTCG KVYNSWYQLQ KHISEEHSKQ PNHICPICGV IRRDEEYLEL
     HMNLHEGKTE KQCRYCPKSF SRPVNTLRHM RMHWDKKKYQ CEKCGLRFSQ DNLLYNHRLR
     HEAEENPIIC SICNVSFKSR KTFNHHTLIH KENRPRHYCS VCPKSFTERY TLKMHMKTHE
     GDVVYGVREE APADEQQVVE ELHVDVDESE AAVTVIMSDN DENSGFCLIC NTNFENKKEL
     EHHLQFDHDV VLK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024