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Coatomer subunit beta' (Beta'-coat protein) (Beta'-COP) (p102)

 COPB2_RAT               Reviewed;         905 AA.
O35142;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 124.
RecName: Full=Coatomer subunit beta';
AltName: Full=Beta'-coat protein;
Short=Beta'-COP;
AltName: Full=p102;
Name=Copb2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Heart;
PubMed=9360998; DOI=10.1074/jbc.272.46.29200;
Csukai M., Chen C.-H., de Matteis M.A., Mochly-Rosen D.;
"The coatomer protein beta'-COP, a selective binding protein (RACK)
for protein kinase Cepsilon.";
J. Biol. Chem. 272:29200-29206(1997).
[2]
SUBCELLULAR LOCATION.
PubMed=17360540; DOI=10.1073/pnas.0611360104;
Moelleken J., Malsam J., Betts M.J., Movafeghi A., Reckmann I.,
Meissner I., Hellwig A., Russell R.B., Sollner T., Brugger B.,
Wieland F.T.;
"Differential localization of coatomer complex isoforms within the
Golgi apparatus.";
Proc. Natl. Acad. Sci. U.S.A. 104:4425-4430(2007).
[3]
INTERACTION WITH SCYL1.
PubMed=18556652; DOI=10.1074/jbc.M801869200;
Burman J.L., Bourbonniere L., Philie J., Stroh T., Dejgaard S.Y.,
Presley J.F., McPherson P.S.;
"Scyl1, mutated in a recessive form of spinocerebellar
neurodegeneration, regulates COPI-mediated retrograde traffic.";
J. Biol. Chem. 283:22774-22786(2008).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: The coatomer is a cytosolic protein complex that binds
to dilysine motifs and reversibly associates with Golgi non-
clathrin-coated vesicles, which further mediate biosynthetic
protein transport from the ER, via the Golgi up to the trans Golgi
network. Coatomer complex is required for budding from Golgi
membranes, and is essential for the retrograde Golgi-to-ER
transport of dilysine-tagged proteins. In mammals, the coatomer
can only be recruited by membranes associated to ADP-ribosylation
factors (ARFs), which are small GTP-binding proteins; the complex
also influences the Golgi structural integrity, as well as the
processing, activity, and endocytic recycling of LDL receptors (By
similarity). {ECO:0000250}.
-!- FUNCTION: This coatomer complex protein, essential for Golgi
budding and vesicular trafficking, is a selective binding protein
(RACK) for protein kinase C, epsilon type. It binds to Golgi
membranes in a GTP-dependent manner.
-!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
beta, beta', gamma, delta, epsilon and zeta subunits. Probably
interacts with PEX11A. Interacts with JAGN1 (By similarity).
Interacts with SCYL1. {ECO:0000250|UniProtKB:P35606,
ECO:0000269|PubMed:18556652}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi
apparatus membrane {ECO:0000269|PubMed:17360540}; Peripheral
membrane protein {ECO:0000269|PubMed:17360540}; Cytoplasmic side
{ECO:0000269|PubMed:17360540}. Cytoplasmic vesicle, COPI-coated
vesicle membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer
is cytoplasmic or polymerized on the cytoplasmic side of the
Golgi, as well as on the vesicles/buds originating from it (By
similarity). Shows only a slight preference for the cis-Golgi
apparatus (<55%), compared with the trans-Golgi (>45%).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the WD repeat COPB2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF002705; AAB88018.1; -; mRNA.
RefSeq; NP_068533.1; NM_021765.1.
UniGene; Rn.37178; -.
ProteinModelPortal; O35142; -.
SMR; O35142; -.
BioGrid; 248811; 3.
IntAct; O35142; 3.
STRING; 10116.ENSRNOP00000066994; -.
iPTMnet; O35142; -.
PhosphoSitePlus; O35142; -.
PaxDb; O35142; -.
PRIDE; O35142; -.
GeneID; 60384; -.
KEGG; rno:60384; -.
CTD; 9276; -.
RGD; 628746; Copb2.
eggNOG; KOG0276; Eukaryota.
eggNOG; ENOG410XNNY; LUCA.
HOVERGEN; HBG051076; -.
InParanoid; O35142; -.
KO; K17302; -.
PhylomeDB; O35142; -.
PRO; PR:O35142; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0000139; C:Golgi membrane; IDA:RGD.
GO; GO:0005080; F:protein kinase C binding; IPI:RGD.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IBA:GO_Central.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR006692; Coatomer_WD-assoc_reg.
InterPro; IPR016453; COPB2.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF04053; Coatomer_WDAD; 1.
Pfam; PF00400; WD40; 4.
PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 3.
PROSITE; PS50082; WD_REPEATS_2; 5.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus; Membrane;
Phosphoprotein; Protein transport; Reference proteome; Repeat;
Transport; WD repeat.
CHAIN 1 905 Coatomer subunit beta'.
/FTId=PRO_0000050914.
REPEAT 13 52 WD 1.
REPEAT 55 94 WD 2.
REPEAT 97 136 WD 3.
REPEAT 140 180 WD 4.
REPEAT 183 224 WD 5.
REPEAT 227 266 WD 6.
REPEAT 350 388 WD 7.
REPEAT 390 425 WD 8.
REPEAT 746 783 WD 9.
COILED 867 891 {ECO:0000255}.
MOD_RES 627 627 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35606}.
MOD_RES 859 859 Phosphoserine.
{ECO:0000250|UniProtKB:P35606}.
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


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