COPB2_BOVIN
ID COPB2_BOVIN Reviewed; 906 AA.
AC P35605; A4IFE1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Coatomer subunit beta';
DE AltName: Full=Beta'-coat protein;
DE Short=Beta'-COP;
DE AltName: Full=p102;
GN Name=COPB2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8334999; DOI=10.1002/j.1460-2075.1993.tb05945.x;
RA Stenbeck G., Harter C., Brecht A., Herrmann D., Lottspeich F., Orci L.,
RA Wieland F.T.;
RT "Beta'-COP, a novel subunit of coatomer.";
RL EMBO J. 12:2841-2845(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH PEX11A.
RX PubMed=9548716; DOI=10.1083/jcb.141.2.373;
RA Passreiter M., Anton M., Lay D., Frank R., Harter C., Wieland F.T.,
RA Gorgas K., Just W.W.;
RT "Peroxisome biogenesis: involvement of ARF and coatomer.";
RL J. Cell Biol. 141:373-383(1998).
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 (By similarity). {ECO:0000250}.
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 -!- INTERACTION:
CC P35605; Q27954: COPA; NbExp=2; IntAct=EBI-620411, EBI-620400;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated
CC 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 -!- SIMILARITY: Belongs to the WD repeat COPB2 family. {ECO:0000305}.
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DR EMBL; X72756; CAA51285.1; -; mRNA.
DR EMBL; BC134537; AAI34538.1; -; mRNA.
DR PIR; S35312; S35312.
DR RefSeq; NP_776706.2; NM_174281.3.
DR AlphaFoldDB; P35605; -.
DR SMR; P35605; -.
DR BioGRID; 159022; 1.
DR IntAct; P35605; 1.
DR MINT; P35605; -.
DR STRING; 9913.ENSBTAP00000019767; -.
DR PaxDb; P35605; -.
DR PeptideAtlas; P35605; -.
DR PRIDE; P35605; -.
DR Ensembl; ENSBTAT00000085263; ENSBTAP00000068170; ENSBTAG00000014843.
DR GeneID; 281706; -.
DR KEGG; bta:281706; -.
DR CTD; 9276; -.
DR VEuPathDB; HostDB:ENSBTAG00000014843; -.
DR VGNC; VGNC:27594; COPB2.
DR eggNOG; KOG0276; Eukaryota.
DR GeneTree; ENSGT00900000141083; -.
DR InParanoid; P35605; -.
DR OMA; NVFWNES; -.
DR OrthoDB; 139008at2759; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000014843; Expressed in saliva-secreting gland and 108 other tissues.
DR ExpressionAtlas; P35605; baseline and differential.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:AgBase.
DR GO; GO:0000139; C:Golgi membrane; ISS:AgBase.
DR GO; GO:0005080; F:protein kinase C binding; ISS:AgBase.
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; ISS:AgBase.
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; IEA:Ensembl.
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 Direct protein sequencing; ER-Golgi transport; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport;
KW WD repeat.
FT CHAIN 1..906
FT /note="Coatomer subunit beta'"
FT /id="PRO_0000050911"
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..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 866..891
FT /evidence="ECO:0000255"
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 MOD_RES 861
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35606"
FT CONFLICT 682
FT /note="Q -> P (in Ref. 1; CAA51285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 906 AA; 102393 MW; E34526000E424E88 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 GDAEIKDGER LPLAVKDMGS CEIYPQTIQH
NPNGRFVVVC GDGEYIIYTA MALRNKSFGS AQEFAWAHDS SEYAIRESNS VVKIFKNFKE
KKSFKPDFGA ESIYGGFLLG VRSVNGLAFY DWENTELIRR IEIQPKHIFW SDSGELVCIA
TEESFFILKY LSEKVLAAQE THEGVTEDGI EDGFEVLGEI QEIVKTGLWV GDCFIYTSSV
NRLNYYVGGE IVTIAHLDRT MYLLGYIPKD NRLYLGDKEL NIVSYSLLVS VLEYQTAVMR
RDFSMADKVL PTIPKEQRTR VAHFLEKQGF KQQALTVSTD PEHRFELALQ LGELKIAYQL
AVEAESEQKW KQLAELAISK CQFGLAQECL HHAQDYGGLL LLATASGNAS MVNKLAEGAE
RDGKNNVAFM SYFLQGKLDA CLELLIRTGR LPEAAFLART YLPSQVSRVV KLWRENLSKV
NQKAAESLAD PTEYENLFPG LKEAFVVEEW VKETHADLWP AKQYPLVTPN EERNVMEEAK
GFQPSRSAAQ QELDGKPASP TPVIVTSQTA NKEEKSLLEL EVDLDNLEIE DIDTTDINLD
EDILDD
