COPB2_MOUSE
ID COPB2_MOUSE Reviewed; 905 AA.
AC O55029; Q3U5Z9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Coatomer subunit beta';
DE AltName: Full=Beta'-coat protein;
DE Short=Beta'-COP;
DE AltName: Full=p102;
GN Name=Copb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 456-905.
RC TISSUE=Testis;
RA Tarsounas M., Moens P.B., Pearlman R.E.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-254.
RX PubMed=29036432; DOI=10.1093/hmg/ddx362;
RA DiStasio A., Driver A., Sund K., Donlin M., Muraleedharan R.M., Pooya S.,
RA Kline-Fath B., Kaufman K.M., Prows C.A., Schorry E., Dasgupta B.,
RA Stottmann R.W.;
RT "Copb2 is essential for embryogenesis and hypomorphic mutations cause human
RT microcephaly.";
RL Hum. Mol. Genet. 26:4836-4848(2017).
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 SCYL1. Interacts with JAGN1 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P35606}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17360540}.
CC Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle,
CC COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is
CC cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as
CC well as on the vesicles/buds originating from it. Shows only a slight
CC preference for the cis-Golgi apparatus, compared with the trans-Golgi.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: The knockout of the gene results in early
CC embryonic lethality with no viable embryos recovered at 12.5 dpc.
CC {ECO:0000269|PubMed:29036432}.
CC -!- SIMILARITY: Belongs to the WD repeat COPB2 family. {ECO:0000305}.
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DR EMBL; AK088064; BAC40125.1; -; mRNA.
DR EMBL; AK153352; BAE31926.1; -; mRNA.
DR EMBL; AF043120; AAB97760.1; -; mRNA.
DR EMBL; BC006675; AAH06675.1; -; mRNA.
DR CCDS; CCDS40734.1; -.
DR RefSeq; NP_056642.1; NM_015827.2.
DR PDB; 5A1U; EM; 13.00 A; D=1-905.
DR PDB; 5A1V; EM; 21.00 A; D/L/U=1-905.
DR PDB; 5A1W; EM; 18.00 A; D=1-905.
DR PDB; 5A1X; EM; 23.00 A; D/L=1-905.
DR PDB; 5A1Y; EM; 21.00 A; D/L=1-905.
DR PDB; 5NZR; EM; 9.20 A; C=1-905.
DR PDB; 5NZS; EM; 10.10 A; C=1-905.
DR PDB; 5NZT; EM; 17.00 A; C/H=1-905.
DR PDB; 5NZU; EM; 15.00 A; C=1-905.
DR PDB; 5NZV; EM; 17.30 A; C/J=1-905.
DR PDBsum; 5A1U; -.
DR PDBsum; 5A1V; -.
DR PDBsum; 5A1W; -.
DR PDBsum; 5A1X; -.
DR PDBsum; 5A1Y; -.
DR PDBsum; 5NZR; -.
DR PDBsum; 5NZS; -.
DR PDBsum; 5NZT; -.
DR PDBsum; 5NZU; -.
DR PDBsum; 5NZV; -.
DR AlphaFoldDB; O55029; -.
DR SMR; O55029; -.
DR BioGRID; 206128; 27.
DR CORUM; O55029; -.
DR IntAct; O55029; 4.
DR MINT; O55029; -.
DR STRING; 10090.ENSMUSP00000035033; -.
DR iPTMnet; O55029; -.
DR PhosphoSitePlus; O55029; -.
DR SwissPalm; O55029; -.
DR EPD; O55029; -.
DR jPOST; O55029; -.
DR MaxQB; O55029; -.
DR PaxDb; O55029; -.
DR PeptideAtlas; O55029; -.
DR PRIDE; O55029; -.
DR ProteomicsDB; 284083; -.
DR Antibodypedia; 33460; 126 antibodies from 25 providers.
DR DNASU; 50797; -.
DR Ensembl; ENSMUST00000035033; ENSMUSP00000035033; ENSMUSG00000032458.
DR GeneID; 50797; -.
DR KEGG; mmu:50797; -.
DR UCSC; uc009rdm.1; mouse.
DR CTD; 9276; -.
DR MGI; MGI:1354962; Copb2.
DR VEuPathDB; HostDB:ENSMUSG00000032458; -.
DR eggNOG; KOG0276; Eukaryota.
DR GeneTree; ENSGT00900000141083; -.
DR HOGENOM; CLU_005507_1_0_1; -.
DR InParanoid; O55029; -.
DR OMA; NVFWNES; -.
DR OrthoDB; 139008at2759; -.
DR PhylomeDB; O55029; -.
DR TreeFam; TF300688; -.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 50797; 25 hits in 72 CRISPR screens.
DR ChiTaRS; Copb2; mouse.
DR PRO; PR:O55029; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O55029; protein.
DR Bgee; ENSMUSG00000032458; Expressed in ascending aorta and 281 other tissues.
DR Genevisible; O55029; MM.
DR GO; GO:0030126; C:COPI vesicle coat; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
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:MGI.
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; IMP:MGI.
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 3D-structure; 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_0000050913"
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..873
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 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"
FT MUTAGEN 254
FT /note="R->C: No effect on protein abundance. Mice
FT homozygous for that mutation do not display any
FT developmental abnormality."
FT /evidence="ECO:0000269|PubMed:29036432"
FT CONFLICT 684
FT /note="S -> H (in Ref. 3; AAB97760)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="F -> L (in Ref. 3; AAB97760)"
FT /evidence="ECO:0000305"
FT CONFLICT 839
FT /note="A -> P (in Ref. 3; AAB97760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 905 AA; 102449 MW; 5845082CAB10FD12 CRC64;
MPLRLDIKRK LTARSDRVKS VDLHPTEPWM LASLYNGSVC VWNHETQTLV KTFEVCDLPV
RAAKFVARKN WVVTGADDMQ IRVFNYNTLE RVHMFEAHSD YIRCIAVHPT QPFILTSSDD
MLIKLWDWDK KWSCSQVFEG HTHYVMQIVI NPKDNNQFAS ASLDRTIKVW QLGSSSPNFT
LEGHEKGVNC IDYYSGGDKP YLISGADDRL VKIWDYQNKT CVQTLEGHAQ NVSCASFHPE
LPIIITGSED GTVRIWHSST YRLESTLNYG MERVWCVASL RGSNNVALGY DEGSIIVKLG
REEPAMSMDA NGKIIWAKHS EVQQANLKAM GDTEIKDGER LPLAVKDMGS CEIYPQTIQH
NPNGRFVVVC GDGEYIIYTA MALRNKSFGS AQEFAWAHDS SEYAIRESNS IVKIFKNFKE
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
GFQPSRPTAQ QEPDGKPASS PVIMASQTTH KEEKSLLELE VDLDNLELED IDTTDINLDE
DILDD
