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FTZ_DROME
ID   FTZ_DROME               Reviewed;         410 AA.
AC   P02835; O96929; Q4V6Y3; Q9V3W3;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 213.
DE   RecName: Full=Segmentation protein fushi tarazu;
GN   Name=ftz; ORFNames=CG2047;
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 FUNCTION.
RX   PubMed=6330566; DOI=10.1038/310025a0;
RA   Laughon A., Scott M.P.;
RT   "Sequence of a Drosophila segmentation gene: protein structure homology
RT   with DNA-binding proteins.";
RL   Nature 310:25-31(1984).
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;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Berkeley;
RA   Celniker S.E., Pfeiffer B., Knafels J., Martin C.H., Mayeda C.A.,
RA   Palazzolo M.J.;
RT   "Complete sequence of the Antennapedia complex of Drosophila.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 207-218, AND MUTAGENESIS.
RX   PubMed=2276626; DOI=10.1101/gad.4.11.1936;
RA   Kellerman K.A., Mattson D.M., Duncan I.;
RT   "Mutations affecting the stability of the fushi tarazu protein of
RT   Drosophila.";
RL   Genes Dev. 4:1936-1950(1990).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 247-320.
RX   PubMed=6327065; DOI=10.1016/0092-8674(84)90370-2;
RA   McGinnis W., Garber R.L., Wirz J., Kuroiwa A., Gehring W.J.;
RT   "A homologous protein-coding sequence in Drosophila homeotic genes and its
RT   conservation in other metazoans.";
RL   Cell 37:403-408(1984).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-320.
RX   PubMed=6330741; DOI=10.1073/pnas.81.13.4115;
RA   Scott M.P., Weiner A.J.;
RT   "Structural relationships among genes that control development: sequence
RT   homology between the Antennapedia, Ultrabithorax, and fushi tarazu loci of
RT   Drosophila.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:4115-4119(1984).
RN   [9]
RP   FUNCTION.
RX   PubMed=2892267; DOI=10.1126/science.2892267;
RA   Doe C.Q., Hiromi Y., Gehring W.J., Goodman C.S.;
RT   "Expression and function of the segmentation gene fushi tarazu during
RT   Drosophila neurogenesis.";
RL   Science 239:170-175(1988).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=3049237; DOI=10.1101/gad.2.8.1021;
RA   Krause H.M., Klemenz R., Gehring W.J.;
RT   "Expression, modification, and localization of the fushi tarazu protein in
RT   Drosophila embryos.";
RL   Genes Dev. 2:1021-1036(1988).
RN   [11]
RP   PHOSPHORYLATION.
RX   PubMed=2743978; DOI=10.1002/j.1460-2075.1989.tb03492.x;
RA   Krause H.M., Gehring W.J.;
RT   "Stage-specific phosphorylation of the fushi tarazu protein during
RT   Drosophila development.";
RL   EMBO J. 8:1197-1204(1989).
RN   [12]
RP   STRUCTURE BY NMR OF HOMEOBOX.
RX   PubMed=7909851; DOI=10.1006/jmbi.1994.1296;
RA   Qian Y.Q., Furukubo-Tokunaga K., Resendez-Perez D., Mueller M.,
RA   Gehring W.J., Wuethrich K.;
RT   "Nuclear magnetic resonance solution structure of the fushi tarazu
RT   homeodomain from Drosophila and comparison with the Antennapedia
RT   homeodomain.";
RL   J. Mol. Biol. 238:333-345(1994).
CC   -!- FUNCTION: May play a role in determining neuronal identity, may be
CC       directly involved in specifying identity of individual neurons.
CC       Required during embryogenesis for the process of body segmentation.
CC       Homeotic protein, required in alternating segment primordia, it
CC       specifies the correct number of segments. {ECO:0000269|PubMed:2892267,
CC       ECO:0000269|PubMed:3049237, ECO:0000269|PubMed:6330566}.
CC   -!- INTERACTION:
CC       P02835; P33244: ftz-f1; NbExp=3; IntAct=EBI-125786, EBI-160447;
CC       P02835; P23758: Poxn; NbExp=3; IntAct=EBI-125786, EBI-105329;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC       ECO:0000269|PubMed:3049237}.
CC   -!- TISSUE SPECIFICITY: Expressed early in development in a striped pattern
CC       at the blastoderm stage. Later expressed in a specific subset of
CC       neuronal precursor cells, neurons and glia in the developing CNS.
CC       Between 5 and 6 hours of development, found in the midline precursor-2
CC       cells in a segmentally repeating pattern. Expression in many other
CC       neuronal precursors follows and reaches a second peak of abundance at 9
CC       hours of development. Expressed in the hindgut between 11-15 hours of
CC       development.
CC   -!- DEVELOPMENTAL STAGE: Expressed during embryonic development.
CC       {ECO:0000269|PubMed:3049237}.
CC   -!- PTM: Phosphorylated at as many as 16 sites.
CC       {ECO:0000269|PubMed:2743978}.
CC   -!- MISCELLANEOUS: 'Fushi tarazu' means 'segment deficient' in Japanese.
CC       Flies lacking ftz exhibit embryos with half the usual number of body
CC       segments.
CC   -!- SIMILARITY: Belongs to the Antp homeobox family. {ECO:0000305}.
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DR   EMBL; X00854; CAA25408.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF54081.1; -; Genomic_DNA.
DR   EMBL; BT022173; AAY51567.1; -; mRNA.
DR   EMBL; AE001572; AAD19794.1; -; Genomic_DNA.
DR   EMBL; X78905; CAA55518.1; -; Genomic_DNA.
DR   EMBL; K01947; AAA28372.1; -; Genomic_DNA.
DR   PIR; A93334; WJFFFT.
DR   RefSeq; NP_477498.1; NM_058150.3.
DR   PDB; 1FTZ; NMR; -; A=253-321.
DR   PDB; 2XHS; X-ray; 2.80 A; B=107-115.
DR   PDBsum; 1FTZ; -.
DR   PDBsum; 2XHS; -.
DR   AlphaFoldDB; P02835; -.
DR   SMR; P02835; -.
DR   BioGRID; 66032; 29.
DR   DIP; DIP-18500N; -.
DR   IntAct; P02835; 14.
DR   STRING; 7227.FBpp0081139; -.
DR   iPTMnet; P02835; -.
DR   PaxDb; P02835; -.
DR   DNASU; 40834; -.
DR   EnsemblMetazoa; FBtr0081625; FBpp0081139; FBgn0001077.
DR   GeneID; 40834; -.
DR   KEGG; dme:Dmel_CG2047; -.
DR   CTD; 40834; -.
DR   FlyBase; FBgn0001077; ftz.
DR   VEuPathDB; VectorBase:FBgn0001077; -.
DR   eggNOG; KOG0489; Eukaryota.
DR   GeneTree; ENSGT00940000175004; -.
DR   HOGENOM; CLU_589608_0_0_1; -.
DR   InParanoid; P02835; -.
DR   OMA; CKDSKRT; -.
DR   OrthoDB; 858478at2759; -.
DR   PhylomeDB; P02835; -.
DR   SignaLink; P02835; -.
DR   BioGRID-ORCS; 40834; 0 hits in 1 CRISPR screen.
DR   EvolutionaryTrace; P02835; -.
DR   GenomeRNAi; 40834; -.
DR   PRO; PR:P02835; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0001077; Expressed in parasegment (Drosophila) and 23 other tissues.
DR   Genevisible; P02835; DM.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IDA:FlyBase.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IBA:GO_Central.
DR   GO; GO:0001708; P:cell fate specification; TAS:FlyBase.
DR   GO; GO:0007417; P:central nervous system development; TAS:FlyBase.
DR   GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
DR   GO; GO:0007506; P:gonadal mesoderm development; IMP:FlyBase.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR   GO; GO:0007366; P:periodic partitioning by pair rule gene; TAS: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:0006355; P:regulation of transcription, DNA-templated; IMP:FlyBase.
DR   GO; GO:0035282; P:segmentation; IMP:FlyBase.
DR   CDD; cd00086; homeodomain; 1.
DR   IDEAL; IID50242; -.
DR   InterPro; IPR005567; FTZ_N.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR020479; Homeobox_metazoa.
DR   Pfam; PF03867; FTZ; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   PRINTS; PR00024; HOMEOBOX.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Developmental protein; DNA-binding; Homeobox; Nucleus;
KW   Pair-rule protein; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..410
FT                   /note="Segmentation protein fushi tarazu"
FT                   /id="PRO_0000049062"
FT   DNA_BIND        254..313
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          71..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..207
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         208
FT                   /note="P->L: In allele Ual2; half-life is increased."
FT                   /evidence="ECO:0000269|PubMed:2276626"
FT   MUTAGEN         212
FT                   /note="P->L: In allele Ual1; half-life is increased."
FT                   /evidence="ECO:0000269|PubMed:2276626"
FT   MUTAGEN         212
FT                   /note="P->S: In allele Ual3; half-life is increased."
FT                   /evidence="ECO:0000269|PubMed:2276626"
FT   CONFLICT        47
FT                   /note="Y -> YHSY (in Ref. 1; CAA25408)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="S -> T (in Ref. 1; CAA25408)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        247..249
FT                   /note="LAS -> MLT (in Ref. 7; AAA28372)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        395
FT                   /note="H -> Q (in Ref. 1; CAA25408)"
FT                   /evidence="ECO:0000305"
FT   HELIX           108..113
FT                   /evidence="ECO:0007829|PDB:2XHS"
FT   HELIX           263..273
FT                   /evidence="ECO:0007829|PDB:1FTZ"
FT   HELIX           281..290
FT                   /evidence="ECO:0007829|PDB:1FTZ"
FT   HELIX           295..305
FT                   /evidence="ECO:0007829|PDB:1FTZ"
FT   HELIX           315..317
FT                   /evidence="ECO:0007829|PDB:1FTZ"
SQ   SEQUENCE   410 AA;  46479 MW;  517154F3DAF8262F CRC64;
     MATTNSQSHY SYADNMNMYN MYHPHSLPPT YYDNSGSNAY YQNTSNYQGY YPQESYSESC
     YYYNNQEQVT TQTVPPVQPT TPPPKATKRK AEDDAASIIA AVEERPSTLR ALLTNPVKKL
     KYTPDYFYTT VEQVKKAPAV STKVTASPAP SYDQEYVTVP TPSASEDVDY LDVYSPQSQT
     QKLKNGDFAT PPPTTPTSLP PLEGISTPPQ SPGEKSSSAV SQEINHRIVT APNGAGDFNW
     SHIEETLASD CKDSKRTRQT YTRYQTLELE KEFHFNRYIT RRRRIDIANA LSLSERQIKI
     WFQNRRMKSK KDRTLDSSPE HCGAGYTAML PPLEATSTAT TGAPSVPVPM YHHHQTTAAY
     PAYSHSHSHG YGLLNDYPQQ QTHQQYDAYP QQYQHQCSYQ QHPQDLYHLS
 
 
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