COPB2_RAT
ID COPB2_RAT Reviewed; 905 AA.
AC O35142;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Coatomer subunit beta';
DE AltName: Full=Beta'-coat protein;
DE Short=Beta'-COP;
DE AltName: Full=p102;
GN Name=Copb2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=9360998; DOI=10.1074/jbc.272.46.29200;
RA Csukai M., Chen C.-H., de Matteis M.A., Mochly-Rosen D.;
RT "The coatomer protein beta'-COP, a selective binding protein (RACK) for
RT protein kinase Cepsilon.";
RL J. Biol. Chem. 272:29200-29206(1997).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=17360540; DOI=10.1073/pnas.0611360104;
RA Moelleken J., Malsam J., Betts M.J., Movafeghi A., Reckmann I.,
RA Meissner I., Hellwig A., Russell R.B., Sollner T., Brugger B.,
RA Wieland F.T.;
RT "Differential localization of coatomer complex isoforms within the Golgi
RT apparatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4425-4430(2007).
RN [3]
RP INTERACTION WITH SCYL1.
RX PubMed=18556652; DOI=10.1074/jbc.m801869200;
RA Burman J.L., Bourbonniere L., Philie J., Stroh T., Dejgaard S.Y.,
RA Presley J.F., McPherson P.S.;
RT "Scyl1, mutated in a recessive form of spinocerebellar neurodegeneration,
RT regulates COPI-mediated retrograde traffic.";
RL J. Biol. Chem. 283:22774-22786(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 In mammals, the coatomer can only be recruited by membranes associated
CC to ADP-ribosylation factors (ARFs), which are small GTP-binding
CC proteins; the complex also influences the Golgi structural integrity,
CC as well as the processing, activity, and endocytic recycling of LDL
CC receptors (By similarity). {ECO:0000250}.
CC -!- FUNCTION: This coatomer complex protein, essential for Golgi budding
CC and vesicular trafficking, is a selective binding protein (RACK) for
CC protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-
CC dependent manner.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits. Probably interacts with
CC PEX11A. Interacts with JAGN1 (By similarity). Interacts with SCYL1.
CC {ECO:0000250|UniProtKB:P35606, ECO:0000269|PubMed:18556652}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus
CC membrane {ECO:0000269|PubMed:17360540}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17360540}; Cytoplasmic side
CC {ECO:0000269|PubMed:17360540}. Cytoplasmic vesicle, COPI-coated vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. 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 (By similarity). Shows only a slight
CC preference for the cis-Golgi apparatus (<55%), compared with the trans-
CC Golgi (>45%). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat COPB2 family. {ECO:0000305}.
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DR EMBL; AF002705; AAB88018.1; -; mRNA.
DR RefSeq; NP_068533.1; NM_021765.1.
DR AlphaFoldDB; O35142; -.
DR SMR; O35142; -.
DR BioGRID; 248811; 4.
DR IntAct; O35142; 3.
DR STRING; 10116.ENSRNOP00000066994; -.
DR iPTMnet; O35142; -.
DR PhosphoSitePlus; O35142; -.
DR jPOST; O35142; -.
DR PaxDb; O35142; -.
DR PRIDE; O35142; -.
DR GeneID; 60384; -.
DR KEGG; rno:60384; -.
DR CTD; 9276; -.
DR RGD; 628746; Copb2.
DR eggNOG; KOG0276; Eukaryota.
DR InParanoid; O35142; -.
DR OrthoDB; 139008at2759; -.
DR PhylomeDB; O35142; -.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:O35142; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030126; C:COPI vesicle coat; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:RGD.
DR GO; GO:0005080; F:protein kinase C binding; IPI:RGD.
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; ISO:RGD.
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 GO; GO:1901998; P:toxin transport; ISO:RGD.
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; 4.
DR PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..905
FT /note="Coatomer subunit beta'"
FT /id="PRO_0000050914"
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 350..388
FT /note="WD 7"
FT REPEAT 390..425
FT /note="WD 8"
FT REPEAT 746..783
FT /note="WD 9"
FT REGION 837..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 867..891
FT /evidence="ECO:0000255"
FT COMPBIAS 844..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..905
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 627
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35606"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35606"
SQ SEQUENCE 905 AA; 102551 MW; 1529F14FCCA19B65 CRC64;
MPLRLDIKRK LTAMSDRVKS VDLHPTEPWM LASLYNGSVC VWNHETQTLV KTFEVCDLPV
RAAKFVARKN WVVTGADDMQ IRVFNYNTLE RVHMFEAHSD YIRCIAVHPT QPFILTSSDD
MLIKLWDWDK KWSCSQVFEG HTHYVMQIVI NPKDNNQFAS ASLDRTIKVW QLGSSSPNFT
LEGHEKGVNC IDYYSGGDKP YLISGADDRL VKIWDYQNKT CVQTPEGHAQ NVSCATFHPE
LPIIITGSED GTVRIWHSST YRLESTLNYG MERVWCVASL RGSNNVALGY DEGSIIVKLG
REEPAMSMDA NGKIIWAKHS EVQQANLKAM GDTEIKDGER LPLAVKDMGS CEIYPQTIQH
NPNGRFVVVC GDGEYIIYTA MALRNKSFGS AQEFAWAHDS SEYAIRESNS VVKIFKNFKE
KKSFKPDFGA ESIYGGFLLG VRSVNGLAFY DWENTELIRR IEIQPKHIFW SDSGELVCIA
TEESFFILKY LSEKVLAAQE THEGVTEDGI EDAFEVLGEI QEIVKTGLWV GDCFIYTSSV
NRLNYYVGGE IVTIAHLDRT MYLLGYIPKD NRLYLGDKEL NIVSYSLLVS VLEYQTAVMR
RDFSMADKVL PTIPKEQRTR VAHFLEKQGF KQQALTVSTD PEHRFELALQ LGELKIAYQL
AVEAESEQKW KQLAELAISK CQFSLAQECL HHAQDYGGLL LLATASGNAS MVNKLAEGAE
RDGKNNVAFM SYFLQGKLDA CLELLIRTGR LPEAAFLART YLPSQVSRVV KLWRENLSKV
NQKAAESLAD PTEYENLFPG LKEAFVVEEW VKETHADLWP AKQYPLVTPN EERNVMEEAK
RFQPSRATAQ QEPDGKPASS PVIMASQTTH KEEKSFQELE DDLDTMELED IDTTDINLDE
DILDD
