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