COPB2_CAEEL
ID COPB2_CAEEL Reviewed; 1000 AA.
AC Q20168;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Probable coatomer subunit beta';
DE AltName: Full=Beta'-coat protein;
DE Short=Beta'-COP;
GN Name=copb-2; ORFNames=F38E11.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP CONCEPTUAL TRANSLATION.
RA Gaitatzes C.;
RL Unpublished observations (JUN-1998).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=10588660; DOI=10.1091/mbc.10.12.4311;
RA Grant B., Hirsh D.;
RT "Receptor-mediated endocytosis in the Caenorhabditis elegans oocyte.";
RL Mol. Biol. Cell 10:4311-4326(1999).
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 -!- DISRUPTION PHENOTYPE: Embryonic death and abnormal oocytes.
CC {ECO:0000269|PubMed:10588660}.
CC -!- SIMILARITY: Belongs to the WD repeat COPB2 family. {ECO:0000305}.
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DR EMBL; Z68342; CAA92776.1; -; Genomic_DNA.
DR PIR; T21970; T21970.
DR RefSeq; NP_501671.1; NM_069270.5.
DR AlphaFoldDB; Q20168; -.
DR SMR; Q20168; -.
DR BioGRID; 42885; 23.
DR IntAct; Q20168; 6.
DR STRING; 6239.F38E11.5; -.
DR iPTMnet; Q20168; -.
DR EPD; Q20168; -.
DR PaxDb; Q20168; -.
DR PeptideAtlas; Q20168; -.
DR EnsemblMetazoa; F38E11.5.1; F38E11.5.1; WBGene00009542.
DR GeneID; 177779; -.
DR KEGG; cel:CELE_F38E11.5; -.
DR UCSC; F38E11.5; c. elegans.
DR CTD; 177779; -.
DR WormBase; F38E11.5; CE18673; WBGene00009542; copb-2.
DR eggNOG; KOG0276; Eukaryota.
DR GeneTree; ENSGT00900000141083; -.
DR HOGENOM; CLU_005507_0_0_1; -.
DR InParanoid; Q20168; -.
DR OMA; PAISMDV; -.
DR OrthoDB; 139008at2759; -.
DR PhylomeDB; Q20168; -.
DR Reactome; R-CEL-6807878; COPI-mediated anterograde transport.
DR Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q20168; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00009542; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
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; IMP:WormBase.
DR GO; GO:0048599; P:oocyte development; IMP:WormBase.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
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; 5.
DR PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Repeat; Transport;
KW WD repeat.
FT CHAIN 1..1000
FT /note="Probable coatomer subunit beta'"
FT /id="PRO_0000050915"
FT REPEAT 13..52
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 351..391
FT /note="WD 7"
FT REGION 863..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..895
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..914
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..1000
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1000 AA; 111107 MW; 152E17D986E0B0C9 CRC64;
MPLRLDVKRK LLARSDRVKC VDLHPVETWL LAALYNGNVH IWNYETQTLV KSFEVCDVPV
RAAKFVPRKS WVVTGSDDMH IRVFNYNTLE RVHQFEAHSD YLRSLVVHPT LPYVISSSDD
MLVKMWDWDN KWAMKQSFEG HTHYVMQIAI NPKDNNTFAT ASLDKTVKVW QFGSNVPNFT
LEGHEKGVNC VDYYHGGEKP YIISGADDHL VKIWDYQNKT CVQTLDGHAQ NVSSVCFHPE
LPLIITGSED STVRLWHANT YRLETTLNYG LERVWCIQAQ KGANTIAIGY DEGSVTLKLG
REEPAVSMDS SGKILWAKHS EIQQANLKTI STEESEAIQD GERLPLSVKD LGSSEIYPQT
LAHSSNGRFV VACGDGEYIV YTAMALRNKD FGQGLEFVWA VDPNMFAVRE SATNVKIKKN
FKDHKSIRSD MVLEGISGGP LLALRSNNSL CFFDWESAVL VRRIEITSKS IYWSDNGEMV
AICGDDSFYV LKYSAEAVAN ATEVTEDGIE DAFEVIGEQA EAVKTGFWIG DCFIFTTALN
RINYYVGGEI VTIAHVDRPL YLLGYMAKES RVYAVDKDLN VISYKLLLSV LEYQTAVMRR
DFDTADKVLT TIPKEQRTRV AHFLEKQGFK KQALAVSQDP DHKFDLSVAL GDLKTAYDLA
LQSDSEEKWK ALSNAATLKS ELLLAGECLG RARDFGGLML LATCAGSAPL LQKLADDSAA
AESHNISFLS SLLLGDIDAC LDKLISTGRL PEAAFLARTH APSRVSSILE LWKAKASGHS
EKSSRKIGES LADPVKYENL FPGFTQSLKA ESFVREISKI PVPASVRVPS AATRNIQEEL
DEAVASGAVS FTDDGQAVLK NAPRQTETQL KAPPPPSVAR QPSPVRQPSP IREPSPIREP
EPEEEEEQEE FDDDQQEVHV PANQESADAH GTSKTPDVVL ETSRPDIVPP RGSAAPDLVS
ASSQQSAQDF QDDTQWSDED FGDAENGDLN MDDLNLDEED
