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

 COPB_RAT                Reviewed;         953 AA.
P23514;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 1.
23-MAY-2018, entry version 143.
RecName: Full=Coatomer subunit beta;
AltName: Full=Beta-coat protein;
Short=Beta-COP;
Name=Copb1; Synonyms=Copb;
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], PROTEIN SEQUENCE OF 108-117; 262-276;
328-337; 496-527; 568-575; 768-786 AND 853-967, AND SUBCELLULAR
LOCATION.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=1840503; DOI=10.1016/0092-8674(91)90248-W;
Duden R., Griffiths G., Frank R., Argos P., Kreis T.E.;
"Beta-COP, a 110 kd protein associated with non-clathrin-coated
vesicles and the Golgi complex, shows homology to beta-adaptin.";
Cell 64:649-665(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=1957170; DOI=10.1126/science.1957170;
Donaldson J.G., Kahn R.A., Lippincott-Schwartz J., Klausner R.D.;
"Binding of ARF and beta-COP to Golgi membranes: possible regulation
by a trimeric G protein.";
Science 254:1197-1199(1991).
[4]
SUBCELLULAR LOCATION.
PubMed=8458872; DOI=10.1083/jcb.121.1.49;
Oprins A., Duden R., Kreis T.E., Geuze H.J., Slot J.W.;
"Beta-COP localizes mainly to the cis-Golgi side in exocrine
pancreas.";
J. Cell Biol. 121:49-59(1993).
[5]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=8376457; DOI=10.1083/jcb.122.6.1155;
Peter F., Plutner H., Zhu H., Kreis T.E., Balch W.E.;
"Beta-COP is essential for transport of protein from the endoplasmic
reticulum to the Golgi in vitro.";
J. Cell Biol. 122:1155-1167(1993).
[6]
SUBCELLULAR LOCATION.
PubMed=9165027; DOI=10.1210/endo.138.6.5166;
Mastick C.C., Falick A.L.;
"Association of N-ethylmaleimide sensitive fusion (NSF) protein and
soluble NSF attachment proteins-alpha and -gamma with glucose
transporter-4-containing vesicles in primary rat adipocytes.";
Endocrinology 138:2391-2397(1997).
[7]
INTERACTION WITH PRKCE.
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).
[8]
SUBCELLULAR LOCATION.
PubMed=10402461; DOI=10.1083/jcb.146.1.71;
Claude A., Zhao B.-P., Kuziemsky C.E., Dahan S., Berger S.J.,
Yan J.-P., Armold A.D., Sullivan E.M., Melancon P.;
"GBF1. A novel Golgi-associated bfa-resistant guanine nucleotide
exchange factor that displays specificity for ADP-ribosylation factor
5.";
J. Cell Biol. 146:71-84(1999).
[9]
SUBCELLULAR LOCATION.
PubMed=10359600; DOI=10.1091/mbc.10.6.1837;
Tisdale E.J.;
"A Rab2 mutant with impaired GTPase activity stimulates vesicle
formation from pre-Golgi intermediates.";
Mol. Biol. Cell 10:1837-1849(1999).
[10]
SUBCELLULAR LOCATION.
PubMed=12486083; DOI=10.1177/002215540205001205;
Tamaki H., Yamashina S.;
"Structural integrity of the Golgi stack is essential for normal
secretory functions of rat parotid acinar cells: effects of brefeldin
A and okadaic acid.";
J. Histochem. Cytochem. 50:1611-1623(2002).
[11]
SUBCELLULAR LOCATION.
PubMed=15749703; DOI=10.1074/jbc.M501833200;
Le-Niculescu H., Niesman I., Fischer T., DeVries L., Farquhar M.G.;
"Identification and characterization of GIV, a novel Galpha i/s-
interacting protein found on COPI, endoplasmic reticulum-Golgi
transport vesicles.";
J. Biol. Chem. 280:22012-22020(2005).
[12]
FUNCTION.
PubMed=17698811; DOI=10.1073/pnas.0703805104;
Bi J., Tsai N.P., Lu H.Y., Loh H.H., Wei L.N.;
"Copb1-facilitated axonal transport and translation of kappa opioid-
receptor mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 104:13810-13815(2007).
[13]
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).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=20056612; DOI=10.1074/jbc.M109.047084;
Chen X., Simon E.S., Xiang Y., Kachman M., Andrews P.C., Wang Y.;
"Quantitative proteomics analysis of cell cycle-regulated Golgi
disassembly and reassembly.";
J. Biol. Chem. 285:7197-7207(2010).
[15]
INTERACTION WITH STX17.
PubMed=21545355; DOI=10.1042/BC20110006;
Muppirala M., Gupta V., Swarup G.;
"Syntaxin 17 cycles between the ER and ERGIC and is required to
maintain the architecture of ERGIC and Golgi.";
Biol. Cell 103:333-350(2011).
-!- 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.
Involved in the Golgi disassembly and reassembly processes during
cell cycle. Involved in autophagy by playing a role in early
endosome function. Plays a role in organellar compartmentalization
of secretory compartments including endoplasmic reticulum (ER)-
Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network
(TGN) and recycling endosomes, and in biosynthetic transport of
CAV1. Plays a functional role in facilitating the transport of
kappa-type opioid receptor mRNAs into axons and enhances
translation of these proteins in the axonal compartment of dorsal
root ganglion (DRG) cells. Required for limiting lipid storage in
lipid droplets. Involved in lipid homeostasis by regulating the
presence of perilipin family members PLIN2 and PLIN3 at the lipid
droplet surface and promoting the association of adipocyte
triglyceride lipase (PNPLA2) with the lipid droplet surface to
mediate lipolysis. {ECO:0000269|PubMed:17698811,
ECO:0000269|PubMed:1957170, ECO:0000269|PubMed:20056612,
ECO:0000269|PubMed:8376457}.
-!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
beta, beta', gamma, delta, epsilon and zeta subunits. Interacts
with SCYL1. Interacts with CAPN8 (By similarity). Interacts with
COPG1 (By similarity). Interacts with ARF1 (myristoylated); this
interaction is required for binding of COPB1 to Golgi membranes
(By similarity). Interacts (via trunk domain) with ARF1 (via
switch I region); the interaction is direct (By similarity).
Interacts with KCNK2 (via N-terminus); this interaction increases
the channel-mediated whole cell currents and promotes plasma
membrane expression of KCNK2 (By similarity). Interacts with
PRKCE. Interacts with STX17. Interacts with TMEM115 (By
similarity). {ECO:0000250, ECO:0000269|PubMed:18556652,
ECO:0000269|PubMed:21545355, ECO:0000269|PubMed:8376457,
ECO:0000269|PubMed:9360998}.
-!- INTERACTION:
P53619:ARCN1 (xeno); NbExp=3; IntAct=EBI-620488, EBI-620432;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8376457,
ECO:0000269|PubMed:8458872}. Golgi apparatus membrane
{ECO:0000269|PubMed:10359600, ECO:0000269|PubMed:10402461,
ECO:0000269|PubMed:12486083, ECO:0000269|PubMed:1957170,
ECO:0000269|PubMed:20056612, ECO:0000269|PubMed:8376457,
ECO:0000269|PubMed:8458872}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P53618}; Cytoplasmic side {ECO:0000305}.
Cytoplasmic vesicle, COPI-coated vesicle membrane
{ECO:0000269|PubMed:10359600, ECO:0000269|PubMed:15749703,
ECO:0000269|PubMed:8458872}; Peripheral membrane protein;
Cytoplasmic side {ECO:0000305}. Cell membrane
{ECO:0000250|UniProtKB:P53618}. Endoplasmic reticulum-Golgi
intermediate compartment {ECO:0000250|UniProtKB:Q9JIF7}. Microsome
membrane {ECO:0000269|PubMed:9165027}. Note=The coatomer is
cytoplasmic or polymerized on the cytoplasmic side of the Golgi,
as well as on the vesicles/buds originating from it
(PubMed:8458872). Proteolytic cleavage by CAPN8 triggers
translocation from Golgi to cytoplasm (By similarity). Found in
perinuclear vesicular-tubular clusters (VTCs) and in the Golgi
region where associated with vesicles, buds and rims of the Golgi
stack (PubMed:8458872). Occasionally present at the trans-side of
Golgi, but mainly present at the cis-Golgi side in transitional
areas (TA), on so-called peripheral elements (PE) consisting of
tubules and vesicles located between the cup-shaped transitional
elements (TE) of the rough endoplasmic reticulum (RER) and the
cis-most Golgi cisternae (PubMed:8458872). Present in cytoplasm,
not associated with visible coats or membranes, with a minor
fraction present on small clusters of tubules and vesicles
(PubMed:8458872). Some association with high-density and low-
density microsomes and mitochondria/nuclei fraction
(PubMed:9165027). Very little found in plasma membrane fraction
(PubMed:9165027). {ECO:0000250|UniProtKB:Q9JIF7,
ECO:0000269|PubMed:8458872, ECO:0000269|PubMed:9165027}.
-!- PTM: Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8.
{ECO:0000250}.
-!- MISCELLANEOUS: Brefeldin A induces dissociation from the Golgi of
the beta-COP and presumably the other coatomer subunits.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; X57228; CAA40505.1; -; mRNA.
EMBL; BC061882; AAH61882.1; -; mRNA.
PIR; S13520; S13520.
RefSeq; NP_542959.1; NM_080781.2.
RefSeq; XP_008757882.1; XM_008759660.1.
RefSeq; XP_008757883.1; XM_008759661.2.
UniGene; Rn.4327; -.
ProteinModelPortal; P23514; -.
BioGrid; 250261; 3.
IntAct; P23514; 5.
STRING; 10116.ENSRNOP00000016292; -.
PaxDb; P23514; -.
PRIDE; P23514; -.
Ensembl; ENSRNOT00000083293; ENSRNOP00000072797; ENSRNOG00000057623.
GeneID; 114023; -.
KEGG; rno:114023; -.
UCSC; RGD:620861; rat.
CTD; 1315; -.
RGD; 620861; Copb1.
eggNOG; KOG1058; Eukaryota.
eggNOG; COG5096; LUCA.
GeneTree; ENSGT00390000005270; -.
HOGENOM; HOG000207417; -.
HOVERGEN; HBG005380; -.
InParanoid; P23514; -.
KO; K17301; -.
OMA; QCGFMAA; -.
OrthoDB; EOG091G03TX; -.
PhylomeDB; P23514; -.
TreeFam; TF105737; -.
Reactome; R-RNO-6798695; Neutrophil degranulation.
Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
PRO; PR:P23514; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000057623; -.
Genevisible; P23514; RN.
GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005798; C:Golgi-associated vesicle; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IDA:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:UniProtKB.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
InterPro; IPR011710; Coatomer_bsu_C.
InterPro; IPR016460; COPB1.
InterPro; IPR029446; COPB1_appendage_platform_dom.
PANTHER; PTHR10635; PTHR10635; 1.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF07718; Coatamer_beta_C; 1.
Pfam; PF14806; Coatomer_b_Cpla; 1.
PIRSF; PIRSF005727; Coatomer_beta_subunit; 1.
SUPFAM; SSF48371; SSF48371; 2.
1: Evidence at protein level;
Acetylation; Cell membrane; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Direct protein sequencing; Endoplasmic reticulum;
ER-Golgi transport; Golgi apparatus; Membrane; Microsome;
Protein transport; Reference proteome; Repeat; Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P53618}.
CHAIN 2 953 Coatomer subunit beta.
/FTId=PRO_0000193835.
REPEAT 96 131 HEAT 1.
REPEAT 132 168 HEAT 2.
REPEAT 240 276 HEAT 3.
REPEAT 277 314 HEAT 4.
REPEAT 316 353 HEAT 5.
REPEAT 396 433 HEAT 6.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000250|UniProtKB:P53618}.
MOD_RES 494 494 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9JIF7}.
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


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