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SWM_DROME
ID   SWM_DROME               Reviewed;        1062 AA.
AC   Q9VIV2; B1NLF3; B1NLF4;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Zinc finger protein swm {ECO:0000305};
DE   AltName: Full=Protein second mitotic wave missing {ECO:0000312|EMBL:ABV58368.1};
GN   Name=swm {ECO:0000312|FlyBase:FBgn0002044};
GN   ORFNames=CG10084 {ECO:0000312|FlyBase:FBgn0002044};
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|EMBL:ABV58368.1, ECO:0000312|EMBL:ABV58369.1, ECO:0000312|EMBL:ABV58370.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-921.
RX   PubMed=18245841; DOI=10.1534/genetics.107.081638;
RA   Casso D.J., Liu S., Iwaki D.D., Ogden S.K., Kornberg T.B.;
RT   "A screen for modifiers of hedgehog signaling in Drosophila melanogaster
RT   identifies swm and mts.";
RL   Genetics 178:1399-1413(2008).
RN   [2] {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   [3] {ECO:0000312|Proteomes:UP000000803}
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   [4] {ECO:0000312|EMBL:AAM11384.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAM11384.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAM11384.1};
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] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21203496; DOI=10.1371/journal.pgen.1001254;
RA   Yamamoto-Hino M., Kanie Y., Awano W., Aoki-Kinoshita K.F., Yano H.,
RA   Nishihara S., Okano H., Ueda R., Kanie O., Goto S.;
RT   "Identification of genes required for neural-specific glycosylation using
RT   functional genomics.";
RL   PLoS Genet. 6:E1001254-E1001254(2010).
CC   -!- FUNCTION: Negatively regulates Hedgehog (hh) protein signal in wing
CC       development (PubMed:18245841). Regulates neural-specific glycosylation
CC       by binding to FucTA mRNA and facilitating its nuclear export in neural
CC       cells (PubMed:21203496). {ECO:0000269|PubMed:18245841,
CC       ECO:0000269|PubMed:21203496}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18245841}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in precellular embryo along the ventral
CC       midline and, in germ-band retraction embryos, in segmental stripes.
CC       Expressed in third instar larvae in imaginal disks, salivary gland,
CC       optic lobe, fat body, wreath cells and gastric caecae of the gut.
CC       {ECO:0000269|PubMed:18245841}.
CC   -!- DISRUPTION PHENOTYPE: Recessive lethal (PubMed:18245841). Heteroallelic
CC       larvae are severely developmentally delayed and most have wing disks
CC       smaller than wild-type (PubMed:18245841). Heteroallelic adult flies
CC       show defects in wing hair orientation (PubMed:18245841). Defective
CC       alpha-1,3-fucosylation (PubMed:21203496). RNAi-mediated knockdown in
CC       the eye results in reduced FucTA protein levels (PubMed:21203496).
CC       {ECO:0000269|PubMed:18245841, ECO:0000269|PubMed:21203496}.
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DR   EMBL; EF601876; ABV58368.1; -; mRNA.
DR   EMBL; EF601877; ABV58369.1; -; Genomic_DNA.
DR   EMBL; EF601878; ABV58370.1; -; Genomic_DNA.
DR   EMBL; AE014134; AAF53812.1; -; Genomic_DNA.
DR   EMBL; AE014134; AAN11045.1; -; Genomic_DNA.
DR   EMBL; AY095056; AAM11384.1; -; mRNA.
DR   RefSeq; NP_609976.1; NM_136132.5.
DR   RefSeq; NP_724201.1; NM_165304.2.
DR   AlphaFoldDB; Q9VIV2; -.
DR   SMR; Q9VIV2; -.
DR   IntAct; Q9VIV2; 5.
DR   STRING; 7227.FBpp0303743; -.
DR   DNASU; 35235; -.
DR   EnsemblMetazoa; FBtr0081244; FBpp0080785; FBgn0002044.
DR   EnsemblMetazoa; FBtr0081245; FBpp0080786; FBgn0002044.
DR   GeneID; 35235; -.
DR   KEGG; dme:Dmel_CG10084; -.
DR   UCSC; CG10084-RA; d. melanogaster.
DR   CTD; 35235; -.
DR   FlyBase; FBgn0002044; swm.
DR   VEuPathDB; VectorBase:FBgn0002044; -.
DR   eggNOG; KOG2135; Eukaryota.
DR   GeneTree; ENSGT00510000046929; -.
DR   HOGENOM; CLU_006190_1_0_1; -.
DR   InParanoid; Q9VIV2; -.
DR   OMA; HADQDQL; -.
DR   PhylomeDB; Q9VIV2; -.
DR   BioGRID-ORCS; 35235; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; swm; fly.
DR   GenomeRNAi; 35235; -.
DR   PRO; PR:Q9VIV2; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0002044; Expressed in cleaving embryo and 31 other tissues.
DR   ExpressionAtlas; Q9VIV2; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IDA:FlyBase.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IMP:FlyBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
DR   GO; GO:0046833; P:positive regulation of RNA export from nucleus; IMP:FlyBase.
DR   CDD; cd12258; RRM2_RBM26_like; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR002483; PWI_dom.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR039511; RBM26-like_RRM2.
DR   InterPro; IPR045137; RBM26/27.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR14398; PTHR14398; 2.
DR   Pfam; PF01480; PWI; 1.
DR   SUPFAM; SSF54928; SSF54928; 2.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Developmental protein; Metal-binding; mRNA transport; Nucleus;
KW   Reference proteome; RNA-binding; Transport; Zinc; Zinc-finger.
FT   CHAIN           1..1062
FT                   /note="Zinc finger protein swm"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000438659"
FT   DOMAIN          7..75
FT                   /note="PWI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00627"
FT   DOMAIN          561..635
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   ZN_FING         363..391
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          119..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          666..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          716..741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          822..847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..920
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1004..1062
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..327
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..441
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        823..841
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1020..1037
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         921
FT                   /note="D->N: In swmF15; recessive lethal and induces
FT                   reduced fucosylation levels."
FT                   /evidence="ECO:0000269|PubMed:18245841,
FT                   ECO:0000269|PubMed:21203496"
FT   CONFLICT        402
FT                   /note="S -> A (in Ref. 1; ABV58369/ABV58370)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1062 AA;  115717 MW;  8A80CF12C504380D CRC64;
     MILENSDKLK DWLSVVLEPL CDADSSALAR YVIALLKKDK SDKDLKRIMI EQLDVFLSEE
     TTRFVERLFD AIASEEYLTV PAAPLITASS ASTAELTVDQ ELALVIDGPQ DDIEAVLVAD
     SPPPPPKDNV IKPDSNQVKL EQASQDAREA EALAFISQEA GIAMHVPTDA KPAFDHKTKD
     SHNQQSASNY QHHHVRSASP PGRSSGVSGS GGGGPGGAGL AAGYADKENQ PRDSRRRRAS
     LRSRSRSRSR SNERAFRRSR SRDRRVNERE KTQRQFRNKS PPGSQTDNRH HGRRNFDRRR
     IGGNADDRPR FGNNKSRRSH SRSMSPERNA RRNQNSPDRV QTAQANLIPA PVAPPAPVEH
     PASHPRQRCR DFDEKGYCVR GETCPWDHGV NPVVFEGINN TSLMMSMREY NPDAPEIWAR
     SGGPPPGAGQ GPVPPPTQPG QTTINPFSGN VRPTTLMSGS GPSPMGVPNP ADYARNPGAP
     PQAAMMPFPF NPTAVTTPLQ RQLIPIPVVD GAPTGGVAEV GKRRFELEDT VAIADVPTKR
     KVPINSRLGP RVNPNMQQHN SSLELRKVPR GLNTIAHLNN HFAKFGKIVN IQVSYEGDPE
     AAIVTFSTHA EANVAYRSTE AVLNNRFIKV FWHNDSSGAD VGQMNQMGGG GGGGGRKNAS
     QYHLHNVPAV PTPNADGAKI SNANPLTEAG AGNIGTPATE QANTAAPASM RLKLNTTTAG
     GSAGGAAGAG APGSGRPLNP AANAASIRKK QEEQQKAVHQ LANGLRKRKQ ELLQSYMKQM
     KTALELVERM DQQDPQRAPT LQTIKVLQMT IDKLRKEIKA DQDQLQAQMQ QQQQQQQPPV
     KKTKEQQKKE LLDMELELIA QQQEGNDTTA IQKRLEELQR NLGVGSAANN KSTHYAPASG
     APGGGAGRKR PNLPEGPTRV DRRPKAIVVT GFAAEEADFV LGHFKNFGEI SKHDVDREIP
     QLILSYATRL NAEQAVLRGK MYKDKRLQIS WAPVVTPAPA PMAAPVEKSA APGDMSVSLE
     NPKQLIQSVS ESESLLGSDT LPELRLEDEE EDEESEDRSW RR
 
 
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