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TIPT_DROME
ID   TIPT_DROME              Reviewed;        1024 AA.
AC   Q9U3V5; Q95SG6; Q9V9P4;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   24-OCT-2003, sequence version 2.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Protein tiptop;
GN   Name=tio; ORFNames=CG12630;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15936749; DOI=10.1016/j.ydbio.2005.05.005;
RA   Laugier E., Yang Z., Fasano L., Kerridge S., Vola C.;
RT   "A critical role of teashirt for patterning the ventral epidermis is masked
RT   by ectopic expression of tiptop, a paralog of teashirt in Drosophila.";
RL   Dev. Biol. 283:446-458(2005).
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] OF 1-18.
RC   STRAIN=Berkeley; TISSUE=Head;
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).
CC   -!- FUNCTION: Tiptop (tio) and teashirt (tsh) have, on the whole, common
CC       activities. Tio and tsh repress each other's expression and tsh has a
CC       crucial role for trunk patterning that is in part masked by ectopic
CC       expression of tiptop. Both genes share a common activity required for
CC       the activation of Ser and svb and the maintenance of en and wg.
CC       {ECO:0000269|PubMed:15936749}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expression in the Malpighian tubules (MTs) and
CC       stomatogastric nervous system starts at embryonic stage 10. At stage
CC       11, expression in the head domain is initiated in the clypeolabrum in
CC       two bilaterally symmetric clusters of cells. At stage 12, expression
CC       appears in the central nervous system (CNS) of the trunk and the
CC       epidermis. The staining in the hindgut is maintained throughout
CC       embryogenesis. At stage 13, expression is present in elongating MTs.
CC       The anterior staining is detected in cells that invaginate into the
CC       stomodeum and by stage 15 onwards, in cells close to the pharynx. Also
CC       expressed in cells of the brain, the second constriction of the gut,
CC       the trunk epidermis, the anterior segments of the CNS (the three
CC       thoracic and the first two abdominal segments) and in the MTs. From
CC       stage 12 onwards, tsh and tio are colocalized in some cells.
CC       {ECO:0000269|PubMed:15936749}.
CC   -!- MISCELLANEOUS: The tsh tio gene pair seems to have arisen from a recent
CC       duplication event: tsh has the dominant role compared to tio.
CC   -!- SIMILARITY: Belongs to the teashirt C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF23183.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAL28355.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR   EMBL; AF219383; AAF23183.1; ALT_INIT; mRNA.
DR   EMBL; AE014134; AAF57242.3; -; Genomic_DNA.
DR   EMBL; AY060807; AAL28355.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001260679.1; NM_001273750.1.
DR   RefSeq; NP_524733.2; NM_079994.4.
DR   AlphaFoldDB; Q9U3V5; -.
DR   BioGRID; 68936; 11.
DR   IntAct; Q9U3V5; 9.
DR   STRING; 7227.FBpp0088404; -.
DR   PaxDb; Q9U3V5; -.
DR   EnsemblMetazoa; FBtr0089377; FBpp0088404; FBgn0028979.
DR   EnsemblMetazoa; FBtr0335391; FBpp0307374; FBgn0028979.
DR   GeneID; 44272; -.
DR   KEGG; dme:Dmel_CG12630; -.
DR   UCSC; CG12630-RA; d. melanogaster.
DR   CTD; 44272; -.
DR   FlyBase; FBgn0028979; tio.
DR   VEuPathDB; VectorBase:FBgn0028979; -.
DR   eggNOG; ENOG502QV71; Eukaryota.
DR   GeneTree; ENSGT00950000183051; -.
DR   HOGENOM; CLU_007777_0_0_1; -.
DR   InParanoid; Q9U3V5; -.
DR   OMA; GHCFNNN; -.
DR   OrthoDB; 967773at2759; -.
DR   PhylomeDB; Q9U3V5; -.
DR   BioGRID-ORCS; 44272; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; neb; fly.
DR   GenomeRNAi; 44272; -.
DR   PRO; PR:Q9U3V5; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0028979; Expressed in testis and 11 other tissues.
DR   ExpressionAtlas; Q9U3V5; baseline and differential.
DR   Genevisible; Q9U3V5; DM.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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:0048749; P:compound eye development; IMP:FlyBase.
DR   GO; GO:0048730; P:epidermis morphogenesis; IMP:FlyBase.
DR   GO; GO:0061330; P:Malpighian tubule stellate cell differentiation; IGI:FlyBase.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007380; P:specification of segmental identity, head; IMP:FlyBase.
DR   InterPro; IPR027008; Teashirt_fam.
DR   InterPro; IPR026807; Tio/Tsh.
DR   InterPro; IPR041661; ZN622/Rei1/Reh1_Znf-C2H2.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR12487; PTHR12487; 1.
DR   PANTHER; PTHR12487:SF7; PTHR12487:SF7; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   Pfam; PF12756; zf-C2H2_2; 2.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   2: Evidence at transcript level;
KW   Activator; Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..1024
FT                   /note="Protein tiptop"
FT                   /id="PRO_0000047068"
FT   ZN_FING         317..341
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         426..450
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         499..523
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         926..949
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          20..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          786..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          954..1004
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..175
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..489
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..741
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..759
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        798..818
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..988
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1024 AA;  108364 MW;  93888A08467C4F5C CRC64;
     MMLHEAVMLE IYRQALSASE LTSPRCQSRD SNTSAGAGAG MADVRCPSNE SHCSANDRLT
     PAATPTLTPT EATISPNSVG LPLTATLPPA AAVALLPPQS AAMAAYLAAA QQNHLLLTNP
     LAAAASLVQH ATQQAVVEGE VESPALDFSR KRPKSHGDDD QEEDQEQDQE QEQEQEPDHD
     VQCDNGPLDL SVSTGKRQES VSPPARKIPR SISADYKSPL PPGSWMPPIN PYLAAVAAKT
     GGLGYSKLAP SEASKALEKM TEMSRLETSP TAARSLGATS SVGAGVPAGA SSNSGGRHSA
     WQSHWLNKGA DTAKDVFKCV WCKQSFSTLA NLTAHMKETQ HCGVQIPSPL PTGGVGTPSA
     PPPTRLATSA SNSACSSSSS STSSSSNSSK SELNMLIKET MPLPRKLVRG QDVWLGKGAE
     QTRQILKCMW CGQSFRSLAE MTSHMQETQH YTNIISQEQI ISWKSGDERE RPTNTGVPST
     STAAPSSPSC TAPSVSAVLT CKVCDQAFGS LKELSTHMAQ KSHYKESPAP SASPPAAGTG
     NPKRGRQNRN EKRKKSLPVR KLLELERSGS NSSLDSALKP LRDFAAATKI TCEKCGSKIE
     TALFVEHIRK CLGESIPIPP RRSNAGVDRL PSPSLGLGAE KPPSVLNALE QLIEKSFESR
     TSRTMTHGGY SEAGTPLGAS ILKRLGIEDS SDYTKPLMDA QAMHLLRSSF ASRDRSASES
     SSASRVESSY TPDRQQATPH KSPDTPAPPP PPPPTIKAEP LEAEPLVGCD REGCSPRQQI
     QVKKEFSMEA CRESPRSVSK SPAPQTERSP PDNGSLLALN SMFDQLSGVE NSGNNNSGHC
     FNNNNSCSSV SAQKPKAHPL AALQKLCETT DPPSTGLRSA SSAGSSTASA TLPSANGNDL
     VAFSWACNEA VLSASNGGSA GDSSIIKCSY CDTPFASKGA YRHHLSKVHF VKDAGEDSPR
     LKSPAVQSPR SMPLASPRRS ASRSPATGSQ QPPPSPTISP YDESPQSKFL KYTELAKQLS
     SKNA
 
 
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