COPB_RAT
ID COPB_RAT Reviewed; 953 AA.
AC P23514;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Coatomer subunit beta;
DE AltName: Full=Beta-coat protein;
DE Short=Beta-COP;
GN Name=Copb1; Synonyms=Copb;
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], PROTEIN SEQUENCE OF 108-117; 262-276; 328-337;
RP 496-527; 568-575; 768-786 AND 853-967, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=1840503; DOI=10.1016/0092-8674(91)90248-w;
RA Duden R., Griffiths G., Frank R., Argos P., Kreis T.E.;
RT "Beta-COP, a 110 kd protein associated with non-clathrin-coated vesicles
RT and the Golgi complex, shows homology to beta-adaptin.";
RL Cell 64:649-665(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1957170; DOI=10.1126/science.1957170;
RA Donaldson J.G., Kahn R.A., Lippincott-Schwartz J., Klausner R.D.;
RT "Binding of ARF and beta-COP to Golgi membranes: possible regulation by a
RT trimeric G protein.";
RL Science 254:1197-1199(1991).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=8458872; DOI=10.1083/jcb.121.1.49;
RA Oprins A., Duden R., Kreis T.E., Geuze H.J., Slot J.W.;
RT "Beta-COP localizes mainly to the cis-Golgi side in exocrine pancreas.";
RL J. Cell Biol. 121:49-59(1993).
RN [5]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=8376457; DOI=10.1083/jcb.122.6.1155;
RA Peter F., Plutner H., Zhu H., Kreis T.E., Balch W.E.;
RT "Beta-COP is essential for transport of protein from the endoplasmic
RT reticulum to the Golgi in vitro.";
RL J. Cell Biol. 122:1155-1167(1993).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=9165027; DOI=10.1210/endo.138.6.5166;
RA Mastick C.C., Falick A.L.;
RT "Association of N-ethylmaleimide sensitive fusion (NSF) protein and soluble
RT NSF attachment proteins-alpha and -gamma with glucose transporter-4-
RT containing vesicles in primary rat adipocytes.";
RL Endocrinology 138:2391-2397(1997).
RN [7]
RP INTERACTION WITH PRKCE.
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=10402461; DOI=10.1083/jcb.146.1.71;
RA Claude A., Zhao B.-P., Kuziemsky C.E., Dahan S., Berger S.J., Yan J.-P.,
RA Armold A.D., Sullivan E.M., Melancon P.;
RT "GBF1. A novel Golgi-associated bfa-resistant guanine nucleotide exchange
RT factor that displays specificity for ADP-ribosylation factor 5.";
RL J. Cell Biol. 146:71-84(1999).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=10359600; DOI=10.1091/mbc.10.6.1837;
RA Tisdale E.J.;
RT "A Rab2 mutant with impaired GTPase activity stimulates vesicle formation
RT from pre-Golgi intermediates.";
RL Mol. Biol. Cell 10:1837-1849(1999).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=12486083; DOI=10.1177/002215540205001205;
RA Tamaki H., Yamashina S.;
RT "Structural integrity of the Golgi stack is essential for normal secretory
RT functions of rat parotid acinar cells: effects of brefeldin A and okadaic
RT acid.";
RL J. Histochem. Cytochem. 50:1611-1623(2002).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=15749703; DOI=10.1074/jbc.m501833200;
RA Le-Niculescu H., Niesman I., Fischer T., DeVries L., Farquhar M.G.;
RT "Identification and characterization of GIV, a novel Galpha i/s-interacting
RT protein found on COPI, endoplasmic reticulum-Golgi transport vesicles.";
RL J. Biol. Chem. 280:22012-22020(2005).
RN [12]
RP FUNCTION.
RX PubMed=17698811; DOI=10.1073/pnas.0703805104;
RA Bi J., Tsai N.P., Lu H.Y., Loh H.H., Wei L.N.;
RT "Copb1-facilitated axonal transport and translation of kappa opioid-
RT receptor mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13810-13815(2007).
RN [13]
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 [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20056612; DOI=10.1074/jbc.m109.047084;
RA Chen X., Simon E.S., Xiang Y., Kachman M., Andrews P.C., Wang Y.;
RT "Quantitative proteomics analysis of cell cycle-regulated Golgi disassembly
RT and reassembly.";
RL J. Biol. Chem. 285:7197-7207(2010).
RN [15]
RP INTERACTION WITH STX17.
RX PubMed=21545355; DOI=10.1042/bc20110006;
RA Muppirala M., Gupta V., Swarup G.;
RT "Syntaxin 17 cycles between the ER and ERGIC and is required to maintain
RT the architecture of ERGIC and Golgi.";
RL Biol. Cell 103:333-350(2011).
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. Involved in the Golgi disassembly and reassembly processes
CC during cell cycle. Involved in autophagy by playing a role in early
CC endosome function. Plays a role in organellar compartmentalization of
CC secretory compartments including endoplasmic reticulum (ER)-Golgi
CC intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and
CC recycling endosomes, and in biosynthetic transport of CAV1. Plays a
CC functional role in facilitating the transport of kappa-type opioid
CC receptor mRNAs into axons and enhances translation of these proteins in
CC the axonal compartment of dorsal root ganglion (DRG) cells. Required
CC for limiting lipid storage in lipid droplets. Involved in lipid
CC homeostasis by regulating the presence of perilipin family members
CC PLIN2 and PLIN3 at the lipid droplet surface and promoting the
CC association of adipocyte triglyceride lipase (PNPLA2) with the lipid
CC droplet surface to mediate lipolysis. {ECO:0000269|PubMed:17698811,
CC ECO:0000269|PubMed:1957170, ECO:0000269|PubMed:20056612,
CC ECO:0000269|PubMed:8376457}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits. Interacts with SCYL1.
CC Interacts with CAPN8 (By similarity). Interacts with COPG1 (By
CC similarity). Interacts with ARF1 (myristoylated); this interaction is
CC required for binding of COPB1 to Golgi membranes (By similarity).
CC Interacts (via trunk domain) with ARF1 (via switch I region); the
CC interaction is direct (By similarity). Interacts with KCNK2 (via N-
CC terminus); this interaction increases the channel-mediated whole cell
CC currents and promotes plasma membrane expression of KCNK2 (By
CC similarity). Interacts with PRKCE. Interacts with STX17. Interacts with
CC TMEM115 (By similarity). Interacts with TMEM41B (By similarity).
CC {ECO:0000250|UniProtKB:P53618, ECO:0000250|UniProtKB:Q9JIF7,
CC ECO:0000269|PubMed:18556652, ECO:0000269|PubMed:21545355,
CC ECO:0000269|PubMed:8376457, ECO:0000269|PubMed:9360998}.
CC -!- INTERACTION:
CC P23514; P53619: ARCN1; Xeno; NbExp=3; IntAct=EBI-620488, EBI-620432;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8376457,
CC ECO:0000269|PubMed:8458872}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:10359600, ECO:0000269|PubMed:10402461,
CC ECO:0000269|PubMed:12486083, ECO:0000269|PubMed:1957170,
CC ECO:0000269|PubMed:20056612, ECO:0000269|PubMed:8376457,
CC ECO:0000269|PubMed:8458872}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P53618}; Cytoplasmic side {ECO:0000305}.
CC Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000269|PubMed:10359600, ECO:0000269|PubMed:15749703,
CC ECO:0000269|PubMed:8458872}; Peripheral membrane protein; Cytoplasmic
CC side {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P53618}.
CC Endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000250|UniProtKB:Q9JIF7}. Microsome membrane
CC {ECO:0000269|PubMed:9165027}. 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 (PubMed:8458872). Proteolytic
CC cleavage by CAPN8 triggers translocation from Golgi to cytoplasm (By
CC similarity). Found in perinuclear vesicular-tubular clusters (VTCs) and
CC in the Golgi region where associated with vesicles, buds and rims of
CC the Golgi stack (PubMed:8458872). Occasionally present at the trans-
CC side of Golgi, but mainly present at the cis-Golgi side in transitional
CC areas (TA), on so-called peripheral elements (PE) consisting of tubules
CC and vesicles located between the cup-shaped transitional elements (TE)
CC of the rough endoplasmic reticulum (RER) and the cis-most Golgi
CC cisternae (PubMed:8458872). Present in cytoplasm, not associated with
CC visible coats or membranes, with a minor fraction present on small
CC clusters of tubules and vesicles (PubMed:8458872). Some association
CC with high-density and low-density microsomes and mitochondria/nuclei
CC fraction (PubMed:9165027). Very little found in plasma membrane
CC fraction (PubMed:9165027). {ECO:0000250|UniProtKB:Q9JIF7,
CC ECO:0000269|PubMed:8458872, ECO:0000269|PubMed:9165027}.
CC -!- PTM: Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Brefeldin A induces dissociation from the Golgi of the
CC beta-COP and presumably the other coatomer subunits.
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; X57228; CAA40505.1; -; mRNA.
DR EMBL; BC061882; AAH61882.1; -; mRNA.
DR PIR; S13520; S13520.
DR RefSeq; NP_542959.1; NM_080781.2.
DR RefSeq; XP_008757882.1; XM_008759660.1.
DR RefSeq; XP_008757883.1; XM_008759661.2.
DR AlphaFoldDB; P23514; -.
DR SMR; P23514; -.
DR BioGRID; 250261; 5.
DR IntAct; P23514; 7.
DR STRING; 10116.ENSRNOP00000016292; -.
DR jPOST; P23514; -.
DR PaxDb; P23514; -.
DR PRIDE; P23514; -.
DR Ensembl; ENSRNOT00000083293; ENSRNOP00000072797; ENSRNOG00000057623.
DR GeneID; 114023; -.
DR KEGG; rno:114023; -.
DR UCSC; RGD:620861; rat.
DR CTD; 1315; -.
DR RGD; 620861; Copb1.
DR eggNOG; KOG1058; Eukaryota.
DR GeneTree; ENSGT00390000005270; -.
DR HOGENOM; CLU_006949_0_0_1; -.
DR InParanoid; P23514; -.
DR OMA; QCGFMAA; -.
DR OrthoDB; 195812at2759; -.
DR PhylomeDB; P23514; -.
DR TreeFam; TF105737; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:P23514; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000057623; Expressed in jejunum and 20 other tissues.
DR Genevisible; P23514; RN.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
DR GO; GO:0030137; C:COPI-coated vesicle; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005798; C:Golgi-associated vesicle; IDA:RGD.
DR GO; GO:0005886; C:plasma 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; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; TAS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR011710; Coatomer_bsu_C.
DR InterPro; IPR016460; COPB1.
DR InterPro; IPR029446; COPB1_appendage_platform_dom.
DR PANTHER; PTHR10635; PTHR10635; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF07718; Coatamer_beta_C; 1.
DR Pfam; PF14806; Coatomer_b_Cpla; 1.
DR PIRSF; PIRSF005727; Coatomer_beta_subunit; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Membrane; Microsome; Protein transport;
KW Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P53618"
FT CHAIN 2..953
FT /note="Coatomer subunit beta"
FT /id="PRO_0000193835"
FT REPEAT 96..131
FT /note="HEAT 1"
FT REPEAT 132..168
FT /note="HEAT 2"
FT REPEAT 240..276
FT /note="HEAT 3"
FT REPEAT 277..314
FT /note="HEAT 4"
FT REPEAT 316..353
FT /note="HEAT 5"
FT REPEAT 396..433
FT /note="HEAT 6"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P53618"
FT MOD_RES 494
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIF7"
SQ SEQUENCE 953 AA; 107011 MW; FB44C55D13A9B101 CRC64;
MTAAENVCYT LINVPMDSEP PSEISLKNDL EKGDVKSKTE ALKKVIIMIL NGEKLPGLLM
TIIRFVLPLQ DHTIKKLLLV FWEIVPKTTP DGRLLHEMIL VCDAYRKDLQ HPNEFIRGST
LRFLCKLKEA ELLEPLMPAI RACLEHRHSY VRRNAVLAIY TIYRNFENLI PDAPELIHDF
LVNEKDASCK RNAFMMLIHA DQDRALDYLS TCIDQVQTFG DILQLVIVEL IYKVCHANPS
ERARFIRCIY NLLQSSSPAV KYEAAGTLVT LSSAPTAIKA AAQCYIDLII KESDNNVKLI
VLDRLVELKE HPAHERVLQD LVMDILRVLS TPDLEVRKKT LQLALDLVSS RNVEELVIVL
KKEVIKTNNV SEHEDTDKYR QLLVRTLHSC SVRFPDMAAN VIPVLMEFLS DSNEAAAADV
LEFVREAIQR FDNLRMLIVE KMLEVFHAIK SVKIYRGALW ILGEYCSTKE DIQSVMTEVR
RSLGEIPIVE SEIKKEAGEL KPEEEITVGP VQKLVTEMGT YATQSALSSS RPTKKEEDRP
PLRGFLLDGD FFVAASLATT LTKIALRYVA LVQEKKKQNS FVAEAMLLMA TILHLGKSSL
PKKPITDDDV DRISLCLKVL SECSPLMNDI FNKECRQSLS QMLSAKLEEE KLSQKKESEK
RNVTVQPDDP ISFMQLTAKN EMNCKEDQFQ LSLLAAMGNT QRKEAADPLA SKLNKVTQLT
GFSDPVYAEA YVHVNQYDIV LDVLVVNQTS DTLQNCTLEL ATLGDLKLVE KPSPLTLAPH
DFANIKANVK VASTENGIIF GNIVYDVSGA ASDRNCVVLS DIHIDIMDYI QPATCTDAEF
RQMWAEFEWE NKVTVNTNVT DLNDYLQHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI
FGEDALANVS IEKPVHQGPD AAVTGHIRIR AKSQGMALSL GDKINLSQKK TSL
