COPB_DROPS
ID COPB_DROPS Reviewed; 965 AA.
AC Q29G21;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Coatomer subunit beta {ECO:0000250|UniProtKB:P45437};
DE AltName: Full=Beta-coat protein {ECO:0000250|UniProtKB:P45437};
DE Short=Beta-COP {ECO:0000250|UniProtKB:P45437};
GN Name=betaCOP {ECO:0000250|UniProtKB:P45437}; ORFNames=GA19453;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EAL31408.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P45437}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC {ECO:0000250|UniProtKB:A0JN39}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P45437}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:P45437}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P45437}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P45437}. Cytoplasmic vesicle, COPI-coated
CC vesicle membrane {ECO:0000250|UniProtKB:P45437}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P45437}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P45437}. Note=The coatomer is cytoplasmic or
CC polymerized on the cytoplasmic side of the Golgi, as well as on the
CC vesicles/buds originating from it. Present within the clusters of
CC tubulo-vesicular structures of Golgi membrane and cis-Golgi membranes.
CC {ECO:0000250|UniProtKB:P45437}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH379065; EAL31408.2; -; Genomic_DNA.
DR RefSeq; XP_001354355.2; XM_001354319.3.
DR AlphaFoldDB; Q29G21; -.
DR SMR; Q29G21; -.
DR STRING; 7237.FBpp0272222; -.
DR EnsemblMetazoa; FBtr0273784; FBpp0272222; FBgn0079449.
DR GeneID; 4814235; -.
DR KEGG; dpo:Dpse_GA19453; -.
DR eggNOG; KOG1058; Eukaryota.
DR HOGENOM; CLU_006949_0_0_1; -.
DR InParanoid; Q29G21; -.
DR OMA; QCGFMAA; -.
DR ChiTaRS; betaCOP; fly.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0079449; Expressed in female reproductive system and 3 other tissues.
DR GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
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; IEA:EnsemblMetazoa.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0010883; P:regulation of lipid storage; IEA:EnsemblMetazoa.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..965
FT /note="Coatomer subunit beta"
FT /id="PRO_0000408945"
FT REPEAT 128..165
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 237..273
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 274..311
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 313..350
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 392..429
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REGION 488..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 965 AA; 107693 MW; 42E8E8B091AE38F7 CRC64;
MSQVPCYTII NSPDLEVPNE MQLKQDLEKG DTNHKIETLK KVIKLLLNGE RYPGLIMTII
RFVLPVQDHT IKKLLLIFWE IVPKTSGDGK LLQEMILVCD AYRKDLQHPN EFLRGSTLRF
LCKLKEPELL EPLMPAIRAC LDHRHSYVRR NAVLAIFTIY KNFDWLVPDG PELIANFLDT
QQDMSCKRNA FLMLLHADQE RALNYLASCI DQVHSFGDIL QLVIVELIYK VCHANPAERS
RFIRCIYNLL NSSSNAVRYE SAGTLITLSL APTAIKAAAS CYIELIVKES DNNVKLIVLD
RLIAMKENEN MEKVMQDLVM DVLRVLAAPD IEVRRKALAL AMDLVYSRNI GEMVLVLKKE
VAKTHNVEHE DTGKYRQLLV RTLHTCSIKF PDVAATVIPV LVEFLSDTNE LAAADVLIFI
REAIQKFPAL SGLIIEHLIE AFPQIKSSKI HRAAVWILGE YVEGPQIIEV IDAIQQTLGD
VPMVEAEQRR LSGDPTEEQS QQQGSATGGV SGDGSSSTTT STSNAINKVT SDGTYATQSA
YSLAPVAKVE KRPPLRQYLM DGDFFIGAAL SATLTKLALR YVELQPDSSA QNRLTTRVML
IMSSILHLGK SGFPSKPITN DDTDRIFICL RTLSERTPEA VSVFMHYCRE ALGKMLDAQH
DEDQRVLKEK QRATAKVQPD DPVLFAQLSN GRDNQLGENV FESSLNQALA GTKTAQLSDI
SSPNNKLNKV TQLTGFSDPV YAEAYVNVNQ YDIVLDVLIV NQTNDTLQNC TLELATLGDL
KLVERPHPVV LAPHDFCNIK ANVKVSSTEN GIIFGNIVYD TALNTNVVVL NTIHIDIMDY
IIPASCTDTE FRQMWQDFEW ENKVTVNTSF TDLHEYLRHL LKSTNMKCLT PEKALSGQCG
FMAANMYAKS IFGENALANL SIEKPVDDPD SKVTGHIRIR AKSQGMALSL GDKISSSQKQ
SVQAA
