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COPB2_DROME
ID   COPB2_DROME             Reviewed;         914 AA.
AC   O62621; Q3KN33; Q8MRM3; Q9VJZ0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-JAN-2003, sequence version 2.
DT   03-AUG-2022, entry version 183.
DE   RecName: Full=Coatomer subunit beta';
DE   AltName: Full=Beta'-coat protein;
DE            Short=Beta'-COP;
GN   Name=beta'COP {ECO:0000312|FlyBase:FBgn0025724};
GN   ORFNames=CG6699 {ECO:0000312|FlyBase:FBgn0025724};
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 / MRNA].
RC   TISSUE=Embryo;
RA   Merdes G., Heid H.W., Mechler B.M.;
RT   "Cloning and characterization of the Drosophila coatomer subunit beta'.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
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=Head;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 613-914.
RC   STRAIN=Berkeley; TISSUE=Head;
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).
CC   -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to
CC       dilysine motifs and reversibly associates with Golgi non-clathrin-
CC       coated vesicles, which further mediate biosynthetic protein transport
CC       from the ER, via the Golgi up to the trans Golgi network. Coatomer
CC       complex is required for budding from Golgi membranes, and is essential
CC       for the retrograde Golgi-to-ER transport of dilysine-tagged proteins
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on
CC       the cytoplasmic side of the Golgi, as well as on the vesicles/buds
CC       originating from it. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat COPB2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM50181.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ006523; CAA07084.1; -; mRNA.
DR   EMBL; AJ006524; CAA07085.1; -; Genomic_DNA.
DR   EMBL; AE014134; AAF53294.2; -; Genomic_DNA.
DR   EMBL; BT023906; ABA81840.1; -; mRNA.
DR   EMBL; AY119527; AAM50181.1; ALT_INIT; mRNA.
DR   RefSeq; NP_524836.2; NM_080097.4.
DR   AlphaFoldDB; O62621; -.
DR   SMR; O62621; -.
DR   BioGRID; 69859; 15.
DR   DIP; DIP-22262N; -.
DR   IntAct; O62621; 3.
DR   STRING; 7227.FBpp0080048; -.
DR   PaxDb; O62621; -.
DR   PRIDE; O62621; -.
DR   DNASU; 45757; -.
DR   EnsemblMetazoa; FBtr0080469; FBpp0080048; FBgn0025724.
DR   GeneID; 45757; -.
DR   KEGG; dme:Dmel_CG6699; -.
DR   CTD; 45757; -.
DR   FlyBase; FBgn0025724; beta'COP.
DR   VEuPathDB; VectorBase:FBgn0025724; -.
DR   eggNOG; KOG0276; Eukaryota.
DR   GeneTree; ENSGT00900000141083; -.
DR   HOGENOM; CLU_005507_1_0_1; -.
DR   InParanoid; O62621; -.
DR   OMA; NVFWNES; -.
DR   OrthoDB; 139008at2759; -.
DR   PhylomeDB; O62621; -.
DR   Reactome; R-DME-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   SignaLink; O62621; -.
DR   BioGRID-ORCS; 45757; 1 hit in 1 CRISPR screen.
DR   ChiTaRS; beta'COP; fly.
DR   GenomeRNAi; 45757; -.
DR   PRO; PR:O62621; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0025724; Expressed in spermathecum and 25 other tissues.
DR   Genevisible; O62621; DM.
DR   GO; GO:0030126; C:COPI vesicle coat; IDA:FlyBase.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005795; C:Golgi stack; IDA:FlyBase.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0010883; P:regulation of lipid storage; IDA:FlyBase.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISS:FlyBase.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR006692; Coatomer_WD-assoc_reg.
DR   InterPro; IPR016453; COPB2.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF04053; Coatomer_WDAD; 1.
DR   Pfam; PF00400; WD40; 4.
DR   PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Protein transport; Reference proteome; Repeat; Transport;
KW   WD repeat.
FT   CHAIN           1..914
FT                   /note="Coatomer subunit beta'"
FT                   /id="PRO_0000050916"
FT   REPEAT          13..54
FT                   /note="WD 1"
FT   REPEAT          55..94
FT                   /note="WD 2"
FT   REPEAT          97..136
FT                   /note="WD 3"
FT   REPEAT          140..180
FT                   /note="WD 4"
FT   REPEAT          183..224
FT                   /note="WD 5"
FT   REPEAT          227..266
FT                   /note="WD 6"
FT   REPEAT          352..390
FT                   /note="WD 7"
FT   CONFLICT        254
FT                   /note="R -> C (in Ref. 1; CAA07084/CAA07085)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        343..345
FT                   /note="LPV -> CPF (in Ref. 1; CAA07084/CAA07085)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   914 AA;  102713 MW;  15E862E1944F5C4B CRC64;
     MPLKLDIKRR LTSRSDRVKC VDLHPAEPWM LCALYNGHVH IMNYENQQMV KDFEVCDVPV
     RSARFVARKN WILTGSDDMQ IRVFNYNTLE KVHSFEAHSD YLRCIAVHPT QPLVLTSSDD
     MLIKLWNWEK MWACQRVFEG HTHYVMQIVF NPKDNNTFAS ASLDRTVKVW QLGSNFANFT
     LEGHEKGVNC VDYYHGGDKP YLISGADDRL VKIWDYQNKT CVQTLEGHAQ NISAVCFHPE
     LPIVLTGSED GTVRIWHSGT YRLETCLNYG FERVWTISSM RGTNNVALGY DEGSIIIKVG
     REEPAMSMDV VGSKIIWAKH SEMQQVNLKT IADGTEIKDG ERLPVATKDM GACEIYPQTI
     AHNPNGRFVV VCGDGEYIIY TSMALRNKAF GSAQEFVWAL ESNEYAIREN NGTVRLFRNF
     KERKSFTPEY GAESIYGGYY FGVKTSSGLA FYDWETLQLV RRIEVQPKNV FWNESGSLVC
     LATDDSYFVL GVDTAQVANA VETKEGLEDD GVESAFNVLG EVSECVKTGL WVGDCFIYTN
     SVNRINYYVG GEIVTVSHLD RTMYLLGYVP KDNRIYLGDK ELNVISFCLQ LSVLEYQTAV
     MRRDFERADV VLPTIPKEHR TRVAHFLEKQ GFKSQALQVS TDADHKFDLA LQIGDLEIAL
     KLARESENSQ KWSQLADVAS SKNNMSLVKE CMQKANDLSG LLLLSTASGD AQLLEVVGAA
     GSAQGHHNLA FLSAFLRSDV ERCLEILIET NRLPEAAFFA RTYLPSQMSR IVELWREKLG
     KVNEKAGQSL ADPAQYTNLF PGLGDALRVE QHLQEERARK APARLAANLP LNSERHPLQE
     LFAAEQGAAG QHLEEKVKPA YVPAQAVVSS SQVAEPTSAA DDDDDLDLEI DGITLDDNID
     TTDVNLDDDF LSDD
 
 
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