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SRYC_DROME
ID   SRYC_DROME              Reviewed;         869 AA.
AC   P15619; Q9VAT4;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 187.
DE   RecName: Full=Serendipity locus protein H-1;
DE   AltName: Full=Protein pourquoi-pas;
DE   AltName: Full=Protein wings-down;
GN   Name=wdn; Synonyms=pqp, sry h-1, Sry-c; ORFNames=CG1454;
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], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Canton-S;
RX   PubMed=3141791; DOI=10.1128/mcb.8.10.4459-4468.1988;
RA   Vincent A., Kejzlarova-Lepesant J., Segalat L., Yanicostas C.,
RA   Lepesant J.-A.;
RT   "sry h-1, a new Drosophila melanogaster multifingered protein gene showing
RT   maternal and zygotic expression.";
RL   Mol. Cell. Biol. 8:4459-4468(1988).
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   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=1592256; DOI=10.1101/gad.6.6.1019;
RA   Segalat L., Perichon R., Bouly J.-P., Lepesant J.-A.;
RT   "The Drosophila pourquoi-pas?/wings-down zinc finger protein: oocyte
RT   nucleus localization and embryonic requirement.";
RL   Genes Dev. 6:1019-1029(1992).
CC   -!- FUNCTION: May belong to a complex set of multifingered proteins which
CC       play an important role in gene activation or regulation at early
CC       embryonic stages through a maximal accumulation of their transcripts
CC       (or protein product) in the mature oocyte.
CC       {ECO:0000269|PubMed:3141791}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1592256}.
CC   -!- TISSUE SPECIFICITY: Distribution varies between nurse cells and the
CC       oocyte during oogenesis. Weakly expressed in follicle and border cells.
CC       {ECO:0000269|PubMed:1592256}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expressed from stage 1 of oogenesis. Expressed at a low level in the
CC       embryo from the tenth nuclear division to the end of cellularization in
CC       all cell nuclei except those of pole cells. Also weakly expressed in
CC       the embryo after germ-band retraction, and in larvae (at protein
CC       level). {ECO:0000269|PubMed:1592256, ECO:0000269|PubMed:3141791}.
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DR   EMBL; M23391; AAA28487.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF56815.1; -; Genomic_DNA.
DR   EMBL; AY058690; AAL13919.1; -; mRNA.
DR   PIR; A30817; A30817.
DR   RefSeq; NP_476900.1; NM_057552.4.
DR   AlphaFoldDB; P15619; -.
DR   SMR; P15619; -.
DR   BioGRID; 68274; 16.
DR   IntAct; P15619; 12.
DR   STRING; 7227.FBpp0084725; -.
DR   PaxDb; P15619; -.
DR   EnsemblMetazoa; FBtr0085356; FBpp0084725; FBgn0005642.
DR   GeneID; 43398; -.
DR   KEGG; dme:Dmel_CG1454; -.
DR   CTD; 43398; -.
DR   FlyBase; FBgn0005642; wdn.
DR   VEuPathDB; VectorBase:FBgn0005642; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000168270; -.
DR   HOGENOM; CLU_014494_0_0_1; -.
DR   InParanoid; P15619; -.
DR   OMA; FNVTFLR; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; P15619; -.
DR   BioGRID-ORCS; 43398; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 43398; -.
DR   PRO; PR:P15619; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0005642; Expressed in egg cell and 40 other tissues.
DR   Genevisible; P15619; DM.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF57667; SSF57667; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   1: Evidence at protein level;
KW   Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..869
FT                   /note="Serendipity locus protein H-1"
FT                   /id="PRO_0000047051"
FT   ZN_FING         269..293
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         299..321
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         331..352
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         358..380
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         386..408
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         414..436
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         442..464
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         470..493
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        120
FT                   /note="V -> L (in Ref. 1; AAA28487)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        247..252
FT                   /note="AASMPP -> RLACR (in Ref. 1; AAA28487)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        706
FT                   /note="T -> N (in Ref. 1; AAA28487)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        750
FT                   /note="P -> A (in Ref. 1; AAA28487)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   869 AA;  95314 MW;  550D0871C6664E70 CRC64;
     MEGGKGEGKR MKEEAPSKKL PPKIYGGDAG TPTKAAHDEI LSSLLRINNF DSISSIKDES
     LDIDLSACVT ISSASLVNGN SLSSTDFWRV LDESAQNNTE LNLSSDVCRD DLAATSSSTV
     PSTLTSDNHS SSEFSVTFLR PEPPNAFTNS PFKKTSSSGT STPVKLSPEQ LHQQHQLQMP
     QSQLLQRKPK LPAATAVRLK VFKEEPPEEK HPPEQVVTKV EVCESELLPP SFTIFQQAKS
     AESVADAASM PPPAASETKP LEVDPAPLHK CLDCNGLLLE TPDEVAKHEA AAHRLRLTYR
     CSECQREFEL LAGLKKHLKT HRTEGRKDTW KKCPDCGKCL KLGSMWMHRK IHSDNKKYQC
     DICGQKFVQK INLTHHARIH SSEKPYECPE CQKRFQERSH LQRHQKYHAQ TRSYRCEKCG
     KMYKTERCLK VHNLVHLEQR PFACTVCDKS FISNSKLKQH SNIHTGMRPF KCNYCPRDFT
     NFPNWLKHTR RRHKVDHKTG EHLENIPSYC SKKSTTNKAQ KAAAAAAAAA AASSAVNPNE
     LSASSELKAK ANLTSTAAPA PAKQARKKKQ PQQATLAALG ITLPAGTALQ QVHPVPLAQQ
     HQQELTTVLV PLAPPAPKQT KAKRERKQLA PKQLQQKPQL LQQGQPQQSS LEPIPAVPQI
     KKEPVQTQGP FLDLHGLSLT SAEELIMEQA LEMEECGLYD APNANTEMGT SDNAISDSAA
     ALHFQIKNEL PDELLPDDDF LPCKPSDRLP CPSLESSPFS SPASMELTAV SCASSVAIST
     NALPVRSGNY YLPAFTLNAH GKLSSTGNGV QSVTTSLAQT PSVSMVNVPL LVRSNQMLPS
     VDTLLFTNQT GGSRFFAGKS ATAATPHLT
 
 
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