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COPB_DROME
ID   COPB_DROME              Reviewed;         964 AA.
AC   P45437; Q9VWV7; Q9Y116;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Coatomer subunit beta;
DE   AltName: Full=Beta-coat protein;
DE            Short=Beta-COP;
GN   Name=betaCOP {ECO:0000312|FlyBase:FBgn0008635};
GN   ORFNames=CG6223 {ECO:0000312|FlyBase:FBgn0008635};
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 [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=8127899; DOI=10.1073/pnas.91.5.1878;
RA   Ripoche J., Link B., Yucel J.K., Tokuyasu K., Malhotra V.;
RT   "Location of Golgi membranes with reference to dividing nuclei in syncytial
RT   Drosophila embryos.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:1878-1882(1994).
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;
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.
RX   PubMed=10953008; DOI=10.1083/jcb.150.4.849;
RA   Lecuit T., Wieschaus E.;
RT   "Polarized insertion of new membrane from a cytoplasmic reservoir during
RT   cleavage of the Drosophila embryo.";
RL   J. Cell Biol. 150:849-860(2000).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11533661; DOI=10.1038/ncb0901-816;
RA   Goto S., Taniguchi M., Muraoka M., Toyoda H., Sado Y., Kawakita M.,
RA   Hayashi S.;
RT   "UDP-sugar transporter implicated in glycosylation and processing of
RT   Notch.";
RL   Nat. Cell Biol. 3:816-822(2001).
RN   [7]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16169286; DOI=10.1016/j.modgep.2005.06.001;
RA   Grieder N.C., Kloter U., Gehring W.J.;
RT   "Expression of COPI components during development of Drosophila
RT   melanogaster.";
RL   Gene Expr. Patterns 6:11-21(2005).
RN   [8]
RP   FUNCTION.
RX   PubMed=16452979; DOI=10.1038/nature04377;
RA   Bard F., Casano L., Mallabiabarrena A., Wallace E., Saito K., Kitayama H.,
RA   Guizzunti G., Hu Y., Wendler F., Dasgupta R., Perrimon N., Malhotra V.;
RT   "Functional genomics reveals genes involved in protein secretion and Golgi
RT   organization.";
RL   Nature 439:604-607(2006).
RN   [9]
RP   FUNCTION.
RX   PubMed=19067489; DOI=10.1371/journal.pbio.0060292;
RA   Beller M., Sztalryd C., Southall N., Bell M., Jackle H., Auld D.S.,
RA   Oliver B.;
RT   "COPI complex is a regulator of lipid homeostasis.";
RL   PLoS Biol. 6:E292-E292(2008).
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       Required for limiting lipid storage in lipid droplets.
CC       {ECO:0000269|PubMed:16452979, ECO:0000269|PubMed:19067489}.
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. Golgi apparatus membrane; Peripheral
CC       membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated
CC       vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is
CC       cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as
CC       well as on the vesicles/buds originating from it (By similarity).
CC       Present within the clusters of tubulo-vesicular structures of Golgi
CC       membrane and cis-Golgi membranes. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: During oogenesis and spermatogenesis, expressed in
CC       ovariole, germarium, testis tip and testis.
CC       {ECO:0000269|PubMed:16169286}.
CC   -!- DEVELOPMENTAL STAGE: Before the first zygotic nuclear division, seen in
CC       membrane structures confined in the embryonic cortex. This cortical
CC       distribution is maintained through stage 6. In cycles 10 and 11, the
CC       presence in the Golgi membranes between hexagonally arranged nuclei is
CC       readily observed in tangential optical sections through the embryonic
CC       surface. In stage 14, present in a thin vitelloplasmic layer below the
CC       plane that represents the basal borders of the cells separating the
CC       cellularized cortex from the rest of the embryo, and also within cells.
CC       Within the cells, appear to be more abundant in the cytoplasmic region
CC       between the nucleus and the embryonic surface. In early embryos, a
CC       large proportion appears randomly diffused, but in the later stages of
CC       embryogenesis, a larger proportion is associated with the membranes. In
CC       early embryos, expressed in the ovary. During embryogenesis, up-
CC       regulated in regions 2 and 3 of the germarium in meiotic cysts and in
CC       follicle cells. Expressed in testis tip starting in early meiotic
CC       spermatocytes. Also detected in paragonia. During embryogenesis,
CC       appears to be expressed ubiquitously at low levels and markedly up-
CC       regulated in the cells of the presumptive proventriculus and the
CC       salivary glands starting at stage 10. {ECO:0000269|PubMed:16169286,
CC       ECO:0000269|PubMed:8127899}.
CC   -!- MISCELLANEOUS: Brefeldin A induces dissociation from the Golgi of
CC       betaCOP and presumably the other coatomer subunits. {ECO:0000250}.
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DR   EMBL; L31852; AAA21090.1; -; mRNA.
DR   EMBL; AE014298; AAF48830.2; -; Genomic_DNA.
DR   EMBL; AF145656; AAD38631.1; -; mRNA.
DR   RefSeq; NP_523400.1; NM_078676.4.
DR   AlphaFoldDB; P45437; -.
DR   SMR; P45437; -.
DR   BioGRID; 59137; 35.
DR   DIP; DIP-23112N; -.
DR   IntAct; P45437; 7.
DR   STRING; 7227.FBpp0074348; -.
DR   PaxDb; P45437; -.
DR   PRIDE; P45437; -.
DR   DNASU; 32820; -.
DR   EnsemblMetazoa; FBtr0074576; FBpp0074348; FBgn0008635.
DR   GeneID; 32820; -.
DR   KEGG; dme:Dmel_CG6223; -.
DR   CTD; 32820; -.
DR   FlyBase; FBgn0008635; betaCOP.
DR   VEuPathDB; VectorBase:FBgn0008635; -.
DR   eggNOG; KOG1058; Eukaryota.
DR   GeneTree; ENSGT00390000005270; -.
DR   HOGENOM; CLU_006949_0_0_1; -.
DR   InParanoid; P45437; -.
DR   OMA; QCGFMAA; -.
DR   OrthoDB; 195812at2759; -.
DR   PhylomeDB; P45437; -.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   Reactome; R-DME-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   SignaLink; P45437; -.
DR   BioGRID-ORCS; 32820; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; betaCOP; fly.
DR   GenomeRNAi; 32820; -.
DR   PRO; PR:P45437; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0008635; Expressed in spermathecum and 33 other tissues.
DR   Genevisible; P45437; DM.
DR   GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
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; IEA:InterPro.
DR   GO; GO:0046597; P:negative regulation of viral entry into host cell; HMP:FlyBase.
DR   GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
DR   GO; GO:0010883; P:regulation of lipid storage; IDA:FlyBase.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR011710; Coatomer_bsu_C.
DR   InterPro; IPR016460; COPB1.
DR   InterPro; IPR029446; COPB1_appendage_platform_dom.
DR   PANTHER; PTHR10635; PTHR10635; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF07718; Coatamer_beta_C; 1.
DR   Pfam; PF14806; Coatomer_b_Cpla; 1.
DR   PIRSF; PIRSF005727; Coatomer_beta_subunit; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Protein transport; Reference proteome; Repeat; Transport.
FT   CHAIN           1..964
FT                   /note="Coatomer subunit beta"
FT                   /id="PRO_0000193837"
FT   REPEAT          129..166
FT                   /note="HEAT 1"
FT   REPEAT          238..275
FT                   /note="HEAT 2"
FT   REPEAT          314..351
FT                   /note="HEAT 3"
FT   REPEAT          393..430
FT                   /note="HEAT 4"
FT   REPEAT          466..506
FT                   /note="HEAT 5"
FT   REGION          490..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..530
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        68
FT                   /note="Q -> E (in Ref. 1; AAA21090)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        168
FT                   /note="V -> A (in Ref. 1; AAA21090)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        239..240
FT                   /note="ER -> DG (in Ref. 1; AAA21090)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        325
FT                   /note="R -> P (in Ref. 1; AAA21090)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        507..515
FT                   /note="AGGNAAGSA -> EAAMQLDR (in Ref. 1; AAA21090)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        543
FT                   /note="A -> P (in Ref. 1; AAA21090)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        938..943
FT                   /note="IRAKSQ -> LRQES (in Ref. 1; AAA21090)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   964 AA;  107407 MW;  08AB7F17F04F361D CRC64;
     MTSQVPCYTI INSPDLEVTN EMQLKRDLEK GDTNVKIETL KRVIKLLLNG ERYPGLIMTI
     IRFVLPVQNH TIKKLLLIFW EIVPKTSADG KLLQEMILVC DAYRKDLQHP NEFLRGSTLR
     FLCKLKEPEL LEPLMPAIRA CLDHRHSYVR RNAVLAIFTI YKNFDWLVPD GPELIASFLD
     TQQDMSCKRN AFLMLLHADQ ERALNYLASC IDQVHTFGDI LQLVIVELIY KVCHANPAER
     SRFIRCIYNL LNSSSNAVRY ESAGTLITLS LAPTAIKAAA SCYIELVVKE SDNNVKLIVL
     DRLVAMKEHE GMEKVMQDLV MDVLRVLAAP DIEVRRKTLA LALDLVYSRN IGEMVLVLKK
     EVAKTHNVEH EDTGKYRQLL VRTLHTCSIK FPDVAANVIP VLVEFLSDTN ELAAADVLIF
     IREAIQKFPA LRALIIEHLI EAFPQIKSSK IHRAAVWILG EYVEGSQILE VIAVIQQTLG
     EVPMVEAEQR RLAGDQTEEQ KQQQGSAGGN AAGSAAEGSG SGNASNKVTS DGTYATQSAY
     SLAPVAKAEK RPPLRQYLMD GDFFIGAALS ATLTKLALRY AELETEARAQ NRLTTQVMLI
     MSSILHLGKS GFPSKPITND DTDRIFVCLR TLSERTPEAI SVFTLYCREA LGKMLDAQHD
     EDQRMLKEKQ KATAKVQPDD PVLFAQLSNG RDNQLGENVF ESSLNQALAG SKNAQLSDVA
     SPNSKLNKVT QLTGFSDPVY AEAYVNVNQY DIVLDVLIVN QTNDTLQNCT LELATLGDLK
     LVERPHPVVL APHDFCNIKA NVKVSSTENG IIFGNIVYET ALNTNVVVLN TIHIDIMDYI
     IPASCTDTEF RQMWQDFEWE NKVTVNTSFT DLHEYLKHLL KSTNMKCLTP EKALSGQCGF
     MAANMYAKSI FGENALANLS IEKPVDDPDS KVTGHIRIRA KSQGMALSLG DKISSSQKQS
     VQAA
 
 
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