ID COPB2_DICDI Reviewed; 1005 AA.
AC Q54YD8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 133.
DE RecName: Full=Coatomer subunit beta';
DE AltName: Full=Beta'-coat protein;
DE Short=Beta'-COP;
GN Name=copb2; ORFNames=DDB_G0278285;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(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 (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 ---------------------------------------------------------------------------
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; AAFI02000023; EAL68315.1; -; Genomic_DNA.
DR RefSeq; XP_642264.1; XM_637172.1.
DR AlphaFoldDB; Q54YD8; -.
DR SMR; Q54YD8; -.
DR STRING; 44689.Q54YD8; -.
DR PaxDb; 44689-DDB0233798; -.
DR EnsemblProtists; EAL68315; EAL68315; DDB_G0278285.
DR GeneID; 8621473; -.
DR KEGG; ddi:DDB_G0278285; -.
DR dictyBase; DDB_G0278285; copB2.
DR eggNOG; KOG0276; Eukaryota.
DR HOGENOM; CLU_005507_1_0_1; -.
DR InParanoid; Q54YD8; -.
DR OMA; NVFWNES; -.
DR PhylomeDB; Q54YD8; -.
DR Reactome; R-DDI-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DDI-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q54YD8; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0030126; C:COPI vesicle coat; ISS:dictyBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR CDD; cd22947; Coatomer_WDAD_beta-like; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.25.40.470; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19876; COATOMER; 1.
DR PANTHER; PTHR19876:SF2; COATOMER SUBUNIT BETA; 1.
DR Pfam; PF04053; Coatomer_WDAD; 1.
DR Pfam; PF00400; WD40; 6.
DR PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome; Repeat;
KW Transport; WD repeat.
FT CHAIN 1..1005
FT /note="Coatomer subunit beta'"
FT /id="PRO_0000330864"
FT REPEAT 13..54
FT /note="WD 1"
FT REPEAT 56..95
FT /note="WD 2"
FT REPEAT 98..137
FT /note="WD 3"
FT REPEAT 141..181
FT /note="WD 4"
FT REPEAT 184..225
FT /note="WD 5"
FT REPEAT 228..267
FT /note="WD 6"
FT REPEAT 349..389
FT /note="WD 7"
FT REPEAT 391..426
FT /note="WD 8"
FT REGION 908..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 829..853
FT /evidence="ECO:0000255"
FT COMPBIAS 974..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1005 AA; 113222 MW; 0758B8E35000054F CRC64;
MPLRLDIKKK LSTRSDRVKS VDIHPTEPWI LASLYDGNVY IWNYETQNMV KSFEVSPNNP
VRTARFIAKK QWIVTGSDDT YIRVYNYNTM EKIKSFEAHA DYIRCIIVHP TLPYILSSSD
DMFIKLWDYE KGWSNTQVFE GHSHYVMSIA WNPKDTNQFA TASLDKTVKV WSINSPHPHF
TLEGHEKGIN SVEYFSGGEK PYLISGADDK LVKIWDYQSK TCVQTLEGHS NNVSVVCYHP
ELPLILSGSE DGTVKLWHSS TYRLERTLNY GMGFVWSMNF LRGSNFIGLG YDDGTVVLKI
GKNKPPVSMD QGGKVIYAKH NEIRISNISS TLEQEVQDGE KLSLQSKDLG NCEVFPQSLQ
HNSNGRFVSV CGDGEFIIYT ALAWRNKSFG NALEFVWAED SGQYAVREST SRIKIFKNFK
ETHSFKPSFS AEGIFGGSLL GVKSNDTLCF YSWDSADIIR RIEKTSPKNI FWSENGDYLA
IVTDKSTFIL RYYKDTVQKY IESGQPIGEL GIENAFDVVH EIEDTIGTGL WVGDCFIYIN
RSSKLNYCVG TEVVTISHLE KHMYLLKYLP QSGRLYLSDK NLNIVSYKLH ISVISYQTSI
LRGDLEGAER ILPKIPQDQR NSIAHFLESQ GYKEKALEVS TDLDHRFELA IQLENLDVAH
EIALKSDSET KFKHLGDLAL SIGEIKLAEN CLKKAEDLPG LLLLYTSTGD IEGMKMLAKL
SEEKGQTNIS FICNLLLPNS LLNCLNTLCA SGDYSEAAFM ARTYLPSMVP DMVEKWKESL
KSTSSKASDA LSNPIDFPNL FPQYDLSIKA EKYFESLRSQ PKSSFDYLKN ATAQSLSKKQ
RNLLEEIESV SQQDYDKVLS QLQHFSLHSG ISDITTTTTN TNNNTNNTNN NNTASLLDDL
DFTSTTTTTT TTTNTNTTQK VASPLSSPSP IRKNDSIASP QKQQQQQQDI NITAPPLIDP
SPVDHDLVLE PTPIINTVSP TKTSPTADLS FLDNIPVDHD EEDEF
//
