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COIL_DROME
ID   COIL_DROME              Reviewed;         634 AA.
AC   A1Z7A8; A1Z7A9; Q8MSN4; Q95SB3;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Coilin {ECO:0000312|FlyBase:FBgn0033265};
GN   Name=coil {ECO:0000312|FlyBase:FBgn0033265};
GN   ORFNames=CG8710 {ECO:0000312|FlyBase:FBgn0033265};
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|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   [3] {ECO:0000312|EMBL:AAL28426.1, ECO:0000312|EMBL:AAM50550.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4] {ECO:0000312|EMBL:ACJ13185.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=19158395; DOI=10.1091/mbc.e08-05-0525;
RA   Liu J.L., Wu Z., Nizami Z., Deryusheva S., Rajendra T.K., Beumer K.J.,
RA   Gao H., Matera A.G., Carroll D., Gall J.G.;
RT   "Coilin is essential for Cajal body organization in Drosophila
RT   melanogaster.";
RL   Mol. Biol. Cell 20:1661-1670(2009).
RN   [6] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19846657; DOI=10.1091/mbc.e09-09-0777;
RA   Deryusheva S., Gall J.G.;
RT   "Small Cajal body-specific RNAs of Drosophila function in the absence of
RT   Cajal bodies.";
RL   Mol. Biol. Cell 20:5250-5259(2009).
RN   [7] {ECO:0000305}
RP   SUBCELLULAR LOCATION.
RX   PubMed=23885126; DOI=10.1091/mbc.e13-03-0118;
RA   Natalizio A.H., Matera A.G.;
RT   "Identification and characterization of Drosophila Snurportin reveals a
RT   role for the import receptor Moleskin/Importin7 in snRNP biogenesis.";
RL   Mol. Biol. Cell 24:2932-2942(2013).
CC   -!- FUNCTION: Component of nuclear coiled bodies, also known as Cajal
CC       bodies or CBs, which are involved in the modification and assembly of
CC       nucleoplasmic snRNPs (PubMed:19846657). Required for Cajal body
CC       formation (PubMed:19158395, PubMed:19846657).
CC       {ECO:0000269|PubMed:19158395, ECO:0000269|PubMed:19846657}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19158395}. Nucleus,
CC       nucleoplasm {ECO:0000269|PubMed:19158395}. Nucleus, Cajal body
CC       {ECO:0000269|PubMed:19158395, ECO:0000269|PubMed:23885126}. Chromosome,
CC       centromere {ECO:0000269|PubMed:19158395}. Cytoplasm, cytoskeleton,
CC       spindle {ECO:0000269|PubMed:19158395}. Note=Detected in the CBs of
CC       cells from a number of different larval and adult tissues. In stage 8-9
CC       oocytes detected only in the single CB of the germinal vesicle. Also
CC       detected in the histone locus bodies (HLBs) of late stage nurse cells,
CC       and low expression in the HLBs of large polytene or polyploid nuclei
CC       within the salivary glands, fat bodies and Malpighian tubule cells. In
CC       germline stem cells and cystocytes (where CBs are not evident),
CC       expressed throughout the nucleoplasm. During interphase localized to
CC       foci scattered throughout the nucleoplasm. During metaphase (in meiotic
CC       and mitotic cells) these foci localize to the centromere regions on the
CC       metaphase plate. At anaphase, no longer detected as foci and is instead
CC       detected throughout the spindle. When the nucleus reforms, it localizes
CC       to multiple nuclear foci and throughout the nucleoplasm.
CC       {ECO:0000269|PubMed:19158395}.
CC   -!- SUBCELLULAR LOCATION: [Isoform C]: Cytoplasm
CC       {ECO:0000269|PubMed:19158395}. Note=Very low expression and not
CC       detected at the protein level. Relatively higher levels of expression
CC       in the cytoplasm of follicle cells that have no expression of Isoform D
CC       in their CBs. {ECO:0000269|PubMed:19158395}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=D {ECO:0000312|FlyBase:FBgn0033265}; Synonyms=long
CC       {ECO:0000303|PubMed:19158395};
CC         IsoId=A1Z7A8-1; Sequence=Displayed;
CC       Name=C {ECO:0000312|FlyBase:FBgn0033265}; Synonyms=short
CC       {ECO:0000303|PubMed:19158395};
CC         IsoId=A1Z7A8-2; Sequence=VSP_058383;
CC   -!- TISSUE SPECIFICITY: In egg chambers expressed in the follicle cells,
CC       nurse cells and oocyte. Expressed in the larval brain, salivary glands,
CC       fat bodies and in the somatic hub cells at the tip of the testis.
CC       Expressed in the spermatogonia and spermatocytes, and in the adult
CC       ejaculatory duct (at protein level). Expressed in the adult Malpighian
CC       tubules. {ECO:0000269|PubMed:19158395}.
CC   -!- DISRUPTION PHENOTYPE: Viable and fertile with no obvious phenotype
CC       (PubMed:19158395). Loss of Cajal bodies (CBs) in the nurse cells,
CC       spermatocytes, ejaculatory ducts (PubMed:19158395). Loss of CBs in the
CC       adult Malpighian tubule cells (PubMed:19158395, PubMed:19846657).
CC       Histone locus bodies (HLBs) in the same cell types are present and not
CC       affected (PubMed:19158395). In stage 8-9 oocytes, the single CB present
CC       in the germinal vesicle is unaffected (PubMed:19158395).
CC       {ECO:0000269|PubMed:19158395, ECO:0000269|PubMed:19846657}.
CC   -!- SIMILARITY: Belongs to the coilin family. {ECO:0000305}.
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DR   EMBL; AE013599; AAX52725.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAX52726.1; -; Genomic_DNA.
DR   EMBL; AY060878; AAL28426.1; -; mRNA.
DR   EMBL; AY118690; AAM50550.1; -; mRNA.
DR   EMBL; BT050478; ACJ13185.1; -; mRNA.
DR   RefSeq; NP_001014505.1; NM_001014505.2. [A1Z7A8-1]
DR   RefSeq; NP_001014506.1; NM_001014506.3.
DR   AlphaFoldDB; A1Z7A8; -.
DR   IntAct; A1Z7A8; 4.
DR   STRING; 7227.FBpp0100132; -.
DR   PaxDb; A1Z7A8; -.
DR   DNASU; 35785; -.
DR   EnsemblMetazoa; FBtr0100668; FBpp0100132; FBgn0033265. [A1Z7A8-1]
DR   GeneID; 35785; -.
DR   KEGG; dme:Dmel_CG8710; -.
DR   UCSC; CG8710-RC; d. melanogaster.
DR   UCSC; CG8710-RD; d. melanogaster. [A1Z7A8-1]
DR   CTD; 8161; -.
DR   FlyBase; FBgn0033265; coil.
DR   VEuPathDB; VectorBase:FBgn0033265; -.
DR   eggNOG; ENOG502SF1H; Eukaryota.
DR   HOGENOM; CLU_039345_0_0_1; -.
DR   InParanoid; A1Z7A8; -.
DR   OMA; IKDVQDH; -.
DR   PhylomeDB; A1Z7A8; -.
DR   SignaLink; A1Z7A8; -.
DR   BioGRID-ORCS; 35785; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 35785; -.
DR   PRO; PR:A1Z7A8; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0033265; Expressed in embryonic/larval hemocyte (Drosophila) and 29 other tissues.
DR   ExpressionAtlas; A1Z7A8; baseline and differential.
DR   Genevisible; A1Z7A9; DM.
DR   GO; GO:0015030; C:Cajal body; IDA:FlyBase.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035363; C:histone locus body; IDA:FlyBase.
DR   GO; GO:0016604; C:nuclear body; IDA:FlyBase.
DR   GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0030576; P:Cajal body organization; IMP:FlyBase.
DR   InterPro; IPR031722; Coilin_N.
DR   Pfam; PF15862; Coilin_N; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..634
FT                   /note="Coilin"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000436526"
FT   REGION          87..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..206
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..146
FT                   /note="Missing (in isoform C)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058383"
FT   CONFLICT        389
FT                   /note="R -> T (in Ref. 3; AAM50550/AAL28426)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   634 AA;  70558 MW;  04F744A6EFB618CD CRC64;
     MQHSSMKVDL SNFFKDERRN SLVFIDAAWN NIKDLQDHIQ NLFSLKDISL LTSDGCYLPP
     RESIKVLNSA EGLKAFRFAS HDSDTFVSPA PVKSSKKRKN RSVEEQVHLT ASTPLRPSKR
     SKNQNNSEWI NIAENPSRVR KKELLDMAPG PSVQSKLLTN KGTPKAPETQ TEVSNMSANI
     ETENKESAPQ IKNKSKNKKP TKSPEASDQV ENEPAPKSIS RCTLKEGKMS ESKNQETSPD
     ILSEKSGVVT KENETREEQQ DKTHLESNKI PDKLSQLKAG DQIEKSPGIA ASLLSISFRS
     PLLEMPFNVP RIFQFPTKKQ QIEILEYKKL KPISPRFLLQ KGAKSDDTAK QFPSNGKDST
     LKPKSYEILH DEELPDVKDK KNVSEGIKRA VAPLCEDIIE TSTTLPGAIG AVESAYLDNS
     TEAETTLPSE AEATNPLELT ESFLQNNTSM EKTPKVEKIL PDDGSASPIK NNVDSKDVKT
     VTVPIFEEQL VSDSDDDVML VDDSNIDVSY GDSDIEPIPV VENRQSLDII RDLLRTATPL
     NSLPSRGDTV IFKLLKIKGN ANSGTTEFVA GRCTYVNRRT KIVTVETITY PPEIGRMLRQ
     YYMSGLDESS EDVRTLSIHL KDMLEAKIIV ATID
 
 
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