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C2D1_DROME
ID   C2D1_DROME              Reviewed;         816 AA.
AC   Q9VKJ9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Coiled-coil and C2 domain-containing protein 1-like;
DE   AltName: Full=Lethal giant disks protein;
GN   Name=l(2)gd1; Synonyms=lgd; ORFNames=CG4713;
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 [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   [2]
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   [3]
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   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=12648493; DOI=10.1016/s0012-1606(02)00052-0;
RA   Klein T.;
RT   "The tumour suppressor gene l(2)giant discs is required to restrict the
RT   activity of Notch to the dorsoventral boundary during Drosophila wing
RT   development.";
RL   Dev. Biol. 255:313-333(2003).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=17088062; DOI=10.1016/j.cub.2006.09.031;
RA   Childress J.L., Acar M., Tao C., Halder G.;
RT   "Lethal giant discs, a novel C2-domain protein, restricts notch activation
RT   during endocytosis.";
RL   Curr. Biol. 16:2228-2233(2006).
CC   -!- FUNCTION: Negative regulator of the Notch signaling pathway, acting to
CC       restrict the activity of Notch to the dorsoventral (D/V) boundary of
CC       the wing imaginal disk. Also causes negative regulation of Notch during
CC       vein, eye, and bristle development. Acts by targeting Notch for
CC       endosomal degradation or recycling. {ECO:0000269|PubMed:12648493,
CC       ECO:0000269|PubMed:17088062}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17088062}.
CC   -!- TISSUE SPECIFICITY: Expressed in wing and eye imaginal disks.
CC       {ECO:0000269|PubMed:12648493, ECO:0000269|PubMed:17088062}.
CC   -!- DISRUPTION PHENOTYPE: Flies exhibit problems in vein, eye, and bristle
CC       development. {ECO:0000269|PubMed:12648493}.
CC   -!- SIMILARITY: Belongs to the CC2D1 family. {ECO:0000305}.
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DR   EMBL; AE014134; AAF53069.1; -; Genomic_DNA.
DR   EMBL; AY058523; AAL13752.1; -; mRNA.
DR   RefSeq; NP_609488.1; NM_135644.4.
DR   PDB; 5VNY; X-ray; 1.10 A; A=359-423.
DR   PDB; 5VO5; X-ray; 2.00 A; A=359-423.
DR   PDB; 6EI6; X-ray; 2.46 A; A/B=550-816.
DR   PDBsum; 5VNY; -.
DR   PDBsum; 5VO5; -.
DR   PDBsum; 6EI6; -.
DR   AlphaFoldDB; Q9VKJ9; -.
DR   SMR; Q9VKJ9; -.
DR   BioGRID; 60605; 16.
DR   IntAct; Q9VKJ9; 12.
DR   STRING; 7227.FBpp0297275; -.
DR   PaxDb; Q9VKJ9; -.
DR   DNASU; 34543; -.
DR   EnsemblMetazoa; FBtr0080197; FBpp0079786; FBgn0261983.
DR   GeneID; 34543; -.
DR   KEGG; dme:Dmel_CG4713; -.
DR   FlyBase; FBgn0261983; l(2)gd1.
DR   VEuPathDB; VectorBase:FBgn0261983; -.
DR   eggNOG; KOG3837; Eukaryota.
DR   GeneTree; ENSGT00390000009595; -.
DR   InParanoid; Q9VKJ9; -.
DR   OMA; NLAKQHY; -.
DR   PhylomeDB; Q9VKJ9; -.
DR   Reactome; R-DME-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   BioGRID-ORCS; 34543; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 34543; -.
DR   PRO; PR:Q9VKJ9; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0261983; Expressed in embryonic/larval hemocyte (Drosophila) and 25 other tissues.
DR   ExpressionAtlas; Q9VKJ9; baseline and differential.
DR   Genevisible; Q9VKJ9; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0098592; C:cytoplasmic side of apical plasma membrane; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0005543; F:phospholipid binding; IDA:FlyBase.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR   GO; GO:0016197; P:endosomal transport; IMP:FlyBase.
DR   GO; GO:0048132; P:female germ-line stem cell asymmetric division; IMP:FlyBase.
DR   GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
DR   GO; GO:0006886; P:intracellular protein transport; IMP:FlyBase.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
DR   GO; GO:0045746; P:negative regulation of Notch signaling pathway; IMP:FlyBase.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
DR   GO; GO:0045035; P:sensory organ precursor cell division; IMP:FlyBase.
DR   GO; GO:0007472; P:wing disc morphogenesis; IMP:FlyBase.
DR   CDD; cd08690; C2_Freud-1; 1.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037772; C2_Freud.
DR   InterPro; IPR039725; CC2D1A/B.
DR   InterPro; IPR006608; DM14.
DR   PANTHER; PTHR13076; PTHR13076; 1.
DR   Pfam; PF00168; C2; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00685; DM14; 4.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   PROSITE; PS50004; C2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Cytoplasm; Notch signaling pathway;
KW   Reference proteome.
FT   CHAIN           1..816
FT                   /note="Coiled-coil and C2 domain-containing protein 1-like"
FT                   /id="PRO_0000288430"
FT   DOMAIN          637..776
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          1..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          354..385
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..45
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..98
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..253
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..447
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           361..380
FT                   /evidence="ECO:0007829|PDB:5VNY"
FT   TURN            381..383
FT                   /evidence="ECO:0007829|PDB:5VNY"
FT   HELIX           385..406
FT                   /evidence="ECO:0007829|PDB:5VNY"
FT   HELIX           413..415
FT                   /evidence="ECO:0007829|PDB:5VNY"
FT   HELIX           580..608
FT                   /evidence="ECO:0007829|PDB:6EI6"
FT   HELIX           612..637
FT                   /evidence="ECO:0007829|PDB:6EI6"
FT   STRAND          645..648
FT                   /evidence="ECO:0007829|PDB:6EI6"
FT   HELIX           654..656
FT                   /evidence="ECO:0007829|PDB:6EI6"
FT   STRAND          665..674
FT                   /evidence="ECO:0007829|PDB:6EI6"
FT   STRAND          686..691
FT                   /evidence="ECO:0007829|PDB:6EI6"
FT   STRAND          695..697
FT                   /evidence="ECO:0007829|PDB:6EI6"
FT   STRAND          701..703
FT                   /evidence="ECO:0007829|PDB:6EI6"
FT   STRAND          717..722
FT                   /evidence="ECO:0007829|PDB:6EI6"
FT   HELIX           728..736
FT                   /evidence="ECO:0007829|PDB:6EI6"
FT   STRAND          738..745
FT                   /evidence="ECO:0007829|PDB:6EI6"
FT   STRAND          754..763
FT                   /evidence="ECO:0007829|PDB:6EI6"
FT   HELIX           764..767
FT                   /evidence="ECO:0007829|PDB:6EI6"
FT   STRAND          770..797
FT                   /evidence="ECO:0007829|PDB:6EI6"
FT   HELIX           801..809
FT                   /evidence="ECO:0007829|PDB:6EI6"
FT   STRAND          811..814
FT                   /evidence="ECO:0007829|PDB:6EI6"
SQ   SEQUENCE   816 AA;  89038 MW;  CD757E267DA491E5 CRC64;
     MFSRKKPEPA KRRQHDLSQF GLTEIPDDFD PSAGYGEDDG GDSDLEAELA AITGGEGAKP
     KPKPKAKLLP ASDLDKMIAD SLRDVSDDDD DDNLESDPDL LGELSGIGGL EEAEEEEPVA
     QPPAASEEPV QTFLPTTTVD TLSIIKQRLE MYKQAEANAK TAGDSGKARR FGRGLKTLKD
     LHRQAAAGKS INVDDIPPEV SVKPIGGQAP PVPAEESPAP STPASPPPVP SRAAPDPPTP
     GTPVEPTTSV APTSPPNPLV TQMRSRQTDY KAAALQSKRS GDISTALQFL KVVKQFDVVI
     KMCEDGQEVD LSDMPPPPAE FLEFLKKMQE EAAAEAVAEP TAAPEPTPVA PAPVLAAATN
     MLEALQQRLE KYQSVEAAAK AENNSGKARR FGRIVKQYED AIKLYKAGKP VPYDELPVPP
     GFGPLPTADA APVAPTPSLP TSPTSPPPTA STSAGGTPSS SSATTPTAPR KAPSPPKPKE
     LTTRTSGNQQ KNNIAEQQMK LLLERQKEFK LAAIEAKKAG EIDQAKEYLK IFKGFDSLLN
     AASSGLPVDL STLPVPPSQR DNLEASFAIV SAEECDPTDD ICEIGVRMEE QLAKQLMMCK
     NTRDHHKAMG DVAGMNRFEN LALTVQKDLD LVRYSKRKNE PLPKFHYEKR SFNIVHCNTD
     LTDSELEIVV VRGISYNVAN PKDVDTYVRV EFPLLNDESF KTKTNVIRDT SSPDYDERFK
     VDIQRTNRQF QRIFKRHGVK FEIYSRGGFL RSDTLIGTVN VKLQPLETKC EIHDTYDLMD
     GRKQVGGKLE VKIRVRNPIL TKQMEHITEK WLVLDA
 
 
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