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CAZ_DROME
ID   CAZ_DROME               Reviewed;         399 AA.
AC   Q27294; Q24445; Q8T3M2; Q9VXI4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=RNA-binding protein cabeza;
DE   AltName: Full=P19;
DE   AltName: Full=Sarcoma-associated RNA-binding fly homolog;
GN   Name=caz; Synonyms=SARFH; ORFNames=CG3606;
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, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP   STAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=Canton-S;
RX   PubMed=7623847; DOI=10.1128/mcb.15.8.4562;
RA   Immanuel D., Zinszner H., Ron D.;
RT   "Association of SARFH (sarcoma-associated RNA-binding fly homolog) with
RT   regions of chromatin transcribed by RNA polymerase II.";
RL   Mol. Cell. Biol. 15:4562-4571(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Canton-S; TISSUE=Pupae;
RX   PubMed=7708500; DOI=10.1093/nar/23.5.835;
RA   Stolow D.T., Haynes S.R.;
RT   "Cabeza, a Drosophila gene encoding a novel RNA binding protein, shares
RT   homology with EWS and TLS, two genes involved in human sarcoma formation.";
RL   Nucleic Acids Res. 23:835-843(1995).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 39-399.
RC   STRAIN=Oregon-R; TISSUE=Pupae;
RA   Haynes S.R.;
RL   Submitted (APR-1988) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-91.
RC   STRAIN=Berkeley; TISSUE=Ovary;
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   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 212-261.
RC   STRAIN=Oregon-R;
RX   PubMed=3031652; DOI=10.1073/pnas.84.7.1819;
RA   Haynes S.R., Rebbert M.L., Mozer B.A., Forquignon F., Dawid I.B.;
RT   "Pen repeat sequences are GGN clusters and encode a glycine-rich domain in
RT   a Drosophila cDNA homologous to the rat helix destabilizing protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:1819-1823(1987).
CC   -!- FUNCTION: May participate in a function common to the expression of
CC       most genes transcribed by RNA polymerase II.
CC       {ECO:0000269|PubMed:7623847}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7623847}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Enriched in the brain and central
CC       nervous system during embryogenesis. Enriched in the adult head.
CC       Embryos contain both isoforms A and B, whereas later in development
CC       (heads and torsos) only isoform B is detected.
CC       {ECO:0000269|PubMed:7623847, ECO:0000269|PubMed:7708500}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the developing embryo from the
CC       earliest stages of cellularization and is subsequently found in many
CC       cell types. {ECO:0000269|PubMed:7623847}.
CC   -!- MISCELLANEOUS: 'Cabeza' means 'head' in Spanish.
CC   -!- SIMILARITY: Belongs to the RRM TET family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM11116.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR   EMBL; U13178; AAA86955.1; -; mRNA.
DR   EMBL; L37083; AAC41563.1; -; mRNA.
DR   EMBL; AE014298; AAN09389.1; -; Genomic_DNA.
DR   EMBL; BT004875; AAO45231.1; -; mRNA.
DR   EMBL; M15765; AAA70425.1; -; mRNA.
DR   EMBL; AY094763; AAM11116.1; ALT_SEQ; mRNA.
DR   PIR; S54729; S54729.
DR   RefSeq; NP_523365.2; NM_078641.4.
DR   AlphaFoldDB; Q27294; -.
DR   SMR; Q27294; -.
DR   BioGRID; 58928; 15.
DR   IntAct; Q27294; 18.
DR   STRING; 7227.FBpp0073996; -.
DR   PaxDb; Q27294; -.
DR   PRIDE; Q27294; -.
DR   DNASU; 32587; -.
DR   EnsemblMetazoa; FBtr0074217; FBpp0073996; FBgn0285954.
DR   GeneID; 32587; -.
DR   KEGG; dme:Dmel_CG3606; -.
DR   CTD; 32587; -.
DR   FlyBase; FBgn0285954; caz.
DR   VEuPathDB; VectorBase:FBgn0285954; -.
DR   eggNOG; KOG1995; Eukaryota.
DR   GeneTree; ENSGT00940000169684; -.
DR   InParanoid; Q27294; -.
DR   OMA; DSYNKGP; -.
DR   OrthoDB; 1539664at2759; -.
DR   PhylomeDB; Q27294; -.
DR   Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-DME-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-DME-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-DME-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-DME-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   SignaLink; Q27294; -.
DR   BioGRID-ORCS; 32587; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; caz; fly.
DR   GenomeRNAi; 32587; -.
DR   PRO; PR:Q27294; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0285954; Expressed in eye disc (Drosophila) and 22 other tissues.
DR   ExpressionAtlas; Q27294; baseline and differential.
DR   Genevisible; Q27294; DM.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR   GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0005669; C:transcription factor TFIID complex; ISS:FlyBase.
DR   GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR   GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR   GO; GO:0008345; P:larval locomotory behavior; IMP:FlyBase.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
DR   GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR   GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISS:FlyBase.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR034870; TET_fam.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   PANTHER; PTHR23238; PTHR23238; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00641; zf-RanBP; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   SUPFAM; SSF90209; SSF90209; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Nucleus; Reference proteome; RNA-binding; Zinc; Zinc-finger.
FT   CHAIN           1..399
FT                   /note="RNA-binding protein cabeza"
FT                   /id="PRO_0000081498"
FT   DOMAIN          120..206
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   ZN_FING         275..304
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        39..41
FT                   /note="PNY -> LFI (in Ref. 6; AAA70425)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        92
FT                   /note="H -> P (in Ref. 1; AAA86955, 2; AAC41563 and 6;
FT                   AAA70425)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        109
FT                   /note="Missing (in Ref. 1; AAA86955, 2; AAC41563 and 6;
FT                   AAA70425)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        253
FT                   /note="G -> GGNGGGG (in Ref. 1; AAA86955, 2; AAC41563 and
FT                   6; AAA70425)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        278
FT                   /note="D -> E (in Ref. 6; AAA70425)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        384..393
FT                   /note="DGGPMRNDGG -> MVDQEKRWS (in Ref. 6; AAA70425)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   399 AA;  38839 MW;  3001FC96BDD6FDCA CRC64;
     MERGGYGGGS GQGYNNFAVP PPNYQQMPNK TGNYNEPPPN YGKQGGGYDS GSGHRGSGGS
     GNGGGGGGSW NDRGGNSYGN GGASKDSYNK GHGGYSGGGG GGGGGGGGGS GGNDMITQED
     TIFVSGMDPS TTEQDIETHF GAIGIIKKDK RTMKPKIWLY KNKETGASKG EATVTYDDTN
     AAQSAIEWFD GRDFNGNAIK VSLAQRQNNW NKGGGGGGGG GGRGGFGGRR GGGGGGGGGG
     GGGGRFDRGG GGGGGRYDRG GGGGGGGGGG NVQPRDGDWK CNSCNNTNFA WRNECNRCKT
     PKGDDEGSSG GGGGGGYGGG GGGGGYDRGN DRGSGGGGYH NRDRGGNSQG GGGGGGGGGG
     YSRFNDNNGG GRGGRGGGGG NRRDGGPMRN DGGMRSRPY
 
 
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