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ZC3H3_DROME
ID   ZC3H3_DROME             Reviewed;         597 AA.
AC   Q9VSK8;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Zinc finger CCCH domain-containing protein 3 {ECO:0000250|UniProtKB:Q8IXZ2};
DE   AltName: Full=dZC3H3 {ECO:0000303|PubMed:19364924};
GN   Name=ZC3H3 {ECO:0000312|FlyBase:FBgn0035900};
GN   ORFNames=CG6694 {ECO:0000312|FlyBase:FBgn0035900};
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 {ECO:0000312|Proteomes:UP000000803};
RN   [1] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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   [2] {ECO:0000312|EMBL:AAQ22530.1}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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   [3] {ECO:0000312|EMBL:AAQ22530.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAQ22530.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAQ22530.1};
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH SBR; PABP2 AND SWM, SUBCELLULAR LOCATION, AND
RP   DOMAIN.
RX   PubMed=19364924; DOI=10.1083/jcb.200811072;
RA   Hurt J.A., Obar R.A., Zhai B., Farny N.G., Gygi S.P., Silver P.A.;
RT   "A conserved CCCH-type zinc finger protein regulates mRNA nuclear
RT   adenylation and export.";
RL   J. Cell Biol. 185:265-277(2009).
CC   -!- FUNCTION: Required for the export of polyadenylated mRNAs from the
CC       nucleu; binds to polyadenylated mRNA, and is involved in the regulation
CC       of mRNA polyadenylation. {ECO:0000269|PubMed:19364924}.
CC   -!- SUBUNIT: Interacts with Pabp2, sbr and swm.
CC       {ECO:0000269|PubMed:19364924}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19364924}.
CC   -!- DOMAIN: The C-terminal region is required for nuclear mRNA export.
CC       {ECO:0000269|PubMed:19364924}.
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DR   EMBL; AE014296; AAF50410.2; -; Genomic_DNA.
DR   EMBL; BT010061; AAQ22530.1; -; mRNA.
DR   RefSeq; NP_648230.1; NM_139973.3.
DR   AlphaFoldDB; Q9VSK8; -.
DR   IntAct; Q9VSK8; 2.
DR   STRING; 7227.FBpp0076380; -.
DR   PaxDb; Q9VSK8; -.
DR   PRIDE; Q9VSK8; -.
DR   DNASU; 38968; -.
DR   EnsemblMetazoa; FBtr0076656; FBpp0076380; FBgn0035900.
DR   GeneID; 38968; -.
DR   KEGG; dme:Dmel_CG6694; -.
DR   UCSC; CG6694-RA; d. melanogaster.
DR   CTD; 23144; -.
DR   FlyBase; FBgn0035900; ZC3H3.
DR   VEuPathDB; VectorBase:FBgn0035900; -.
DR   eggNOG; KOG1492; Eukaryota.
DR   GeneTree; ENSGT00940000161068; -.
DR   HOGENOM; CLU_453625_0_0_1; -.
DR   InParanoid; Q9VSK8; -.
DR   OMA; CPYLHKK; -.
DR   OrthoDB; 941054at2759; -.
DR   PhylomeDB; Q9VSK8; -.
DR   BioGRID-ORCS; 38968; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 38968; -.
DR   PRO; PR:Q9VSK8; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0035900; Expressed in eye disc (Drosophila) and 21 other tissues.
DR   Genevisible; Q9VSK8; DM.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0051168; P:nuclear export; IMP:FlyBase.
DR   GO; GO:0010793; P:regulation of mRNA export from nucleus; IMP:UniProtKB.
DR   GO; GO:1900363; P:regulation of mRNA polyadenylation; IMP:UniProtKB.
DR   InterPro; IPR000571; Znf_CCCH.
DR   SMART; SM00356; ZnF_C3H1; 3.
DR   PROSITE; PS50103; ZF_C3H1; 3.
PE   1: Evidence at protein level;
KW   Metal-binding; mRNA processing; mRNA transport; Nucleus;
KW   Reference proteome; Repeat; RNA-binding; Transport; Zinc; Zinc-finger.
FT   CHAIN           1..597
FT                   /note="Zinc finger CCCH domain-containing protein 3"
FT                   /id="PRO_0000434014"
FT   ZN_FING         397..423
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         424..450
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         451..478
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          515..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..536
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..574
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   597 AA;  66322 MW;  A2D190600601BC22 CRC64;
     MLPHISADEA QPSMSRKVYI NPNFQLQGQT AHQLPFQVPF QAFQAPLQPQ PAIHINPHFL
     NRQRAMYDQY QREQQEQLMM QQVSASHYRL DPTIHLLATP PPPPAKIISK VSTCLVRKPS
     VVASGPAVKL AASVPVPTVS SLVQPPLVSI SKRKIVRQGA LKAAPAVAAL HPPPPAKRTR
     YKLVRSISLT CTPLVKKRRP LREFVGQYAL RRTNEAQPNR KLSSKPQALK LGVNKSLSMV
     SIHGVMYKKI SKNKITKLDA SSSARVAKSE SPRTLQRTLS GRTLFVSGNK FILDPSGCRL
     TRVSTSSTGA TQSSVNRSIL RRIDIGGLTY VASPKALNVF VRTSNHVSRA HLITAKQRSL
     TLLNKSLVKT NVPCAIFQKL GKCVAHSRGK CRKLHDKRQV AICVSFLRGE CTKPKCLLSH
     NVTLEKMPVC RYYLRGVCVR EDCPYLHKKL SSKTEICIDF VRGYCPLAAE CNKRHEFSCP
     ELERKGKCEL PRCVFCKKSP SKRLAKVKSR PKLGSKPVAF TDTAKESSTA DELPTSSRYF
     GSHKEPAEAI LTRDDVEQKK PEAEDEDQKE AGAPCPRRRP QLGTLPSFIP LGGEEKL
 
 
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