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

 COPB_BOVIN              Reviewed;         953 AA.
A0JN39;
17-APR-2007, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 1.
10-OCT-2018, entry version 92.
RecName: Full=Coatomer subunit beta;
AltName: Full=Beta-coat protein;
Short=Beta-COP;
Name=COPB1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Thalamus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[2]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=1898986; DOI=10.1038/349248a0;
Waters M.G., Serafini T., Rothman J.E.;
"'Coatomer': a cytosolic protein complex containing subunits of non-
clathrin-coated Golgi transport vesicles.";
Nature 349:248-251(1991).
[3]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=1631136; DOI=10.1073/pnas.89.14.6408;
Donaldson J.G., Cassel D., Kahn R.A., Klausner R.D.;
"ADP-ribosylation factor, a small GTP-binding protein, is required for
binding of the coatomer protein beta-COP to Golgi membranes.";
Proc. Natl. Acad. Sci. U.S.A. 89:6408-6412(1992).
[4]
INTERACTION WITH ARF1, AND SUBCELLULAR LOCATION.
PubMed=8505331;
Palmer D.J., Helms J.B., Beckers C.J., Orci L., Rothman J.E.;
"Binding of coatomer to Golgi membranes requires ADP-ribosylation
factor.";
J. Biol. Chem. 268:12083-12089(1993).
-!- 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. Plays a functional role in facilitating the transport
of kappa-type opioid receptor mRNAs into axons and enhances
translation of these proteins. 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 surface
triglyceride lipase (PNPLA2) with the lipid droplet to mediate
lipolysis. 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. {ECO:0000269|PubMed:1631136}.
-!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
beta, beta', gamma, delta, epsilon and zeta subunits. Interacts
with ARF1 (myristoylated); this interaction is required for
binding of COPB1 to Golgi membranes. Interacts with CAPN8 and
PRKCE (By similarity). Interacts with SCYL1 (By similarity).
Interacts with COPG1 (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 STX17 (By similarity). Interacts with TMEM115 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:1898986}. Golgi apparatus membrane
{ECO:0000269|PubMed:1631136, ECO:0000269|PubMed:8505331};
Peripheral membrane protein; Cytoplasmic side. Cytoplasmic
vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Cell membrane {ECO:0000250}. Endoplasmic reticulum-Golgi
intermediate compartment {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 (Ref.1).
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 (By similarity).
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
(By similarity). Present in cytoplasm, not associated with visible
coats or membranes, with a minor fraction present on small
clusters of tubules and vesicles (By similarity). Some association
with high-density and low-density microsomes and
mitochondria/nuclei fraction (By similarity). Very little found in
plasma membrane fraction (By similarity). {ECO:0000250}.
-!- 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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EMBL; BC126502; AAI26503.1; -; mRNA.
RefSeq; NP_001071475.1; NM_001078007.1.
RefSeq; XP_015330164.1; XM_015474678.1.
UniGene; Bt.22486; -.
BioGrid; 192108; 1.
STRING; 9913.ENSBTAP00000008616; -.
PaxDb; A0JN39; -.
PeptideAtlas; A0JN39; -.
PRIDE; A0JN39; -.
Ensembl; ENSBTAT00000008616; ENSBTAP00000008616; ENSBTAG00000006556.
GeneID; 535533; -.
KEGG; bta:535533; -.
CTD; 1315; -.
VGNC; VGNC:27593; COPB1.
eggNOG; KOG1058; Eukaryota.
eggNOG; COG5096; LUCA.
GeneTree; ENSGT00390000005270; -.
HOGENOM; HOG000207417; -.
HOVERGEN; HBG005380; -.
InParanoid; A0JN39; -.
KO; K17301; -.
OMA; QCGFMAA; -.
OrthoDB; EOG091G03TX; -.
TreeFam; TF105737; -.
Reactome; R-BTA-6798695; Neutrophil degranulation.
Reactome; R-BTA-6807878; COPI-mediated anterograde transport.
Reactome; R-BTA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
Proteomes; UP000009136; Chromosome 15.
Bgee; ENSBTAG00000006556; Expressed in 10 organ(s), highest expression level in spleen.
GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IBA:GO_Central.
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; ER-Golgi transport; Golgi apparatus; Membrane;
Protein transport; Reference proteome; Repeat; Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P53618}.
CHAIN 2 953 Coatomer subunit beta.
/FTId=PRO_0000283808.
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; 107127 MW; 60DDC06C7A2B56FD CRC64;
MTAAENVCYT LINVPMDSEP PSEISLKNDL EKGDVKSKTE ALKKVIIMIL NGEKLPGLLM
TIIRFVLPLQ DHTIKKLLLV FWEIVPKTTP DGRLLHEMIL VCDAYRKDLQ HPNEFIRGST
LRFLCKLKEA ELLEPLMPAI RACLEHRHSY VRRNAVLAIY TIYRNFEHLI PDAPELIHDF
LVNEKDASCK RNAFMMLIHA DQDRALDYLS TCIDQVQTFG DILQLVIVEL IYKVCHANPS
ERARFIRCIY NLLQSSSPAV KYEAAGTLVT LSSAPTAIKA AAQCYIDLII KESDNNVKLI
VLDRLIELKE HPAHERVLQD LVMDILRVLS TPDLEVRKKT LQLALDLVSS RNVEELVIVL
KKEVIKTNNV SEHEDTDKYR QLLVRTLHSC SVRFPDMAAN VIPVLMEFLS DSNEAAAADV
LEFVREAIQR FDNLRMLIVE KMLEVFHAIK SVKIYRGALW ILGEYCSTKD DIQSVMTEVR
RSLGEIPIVE SEIKKEAGEL KPEEEITVGP VQKLVTEMGT YATQSALSSS RPTKKEEERP
PLRGFLLDGD FFVAASLATT LTKIALRYVA LVQEKKKQNS FVAEAMLLMA TILHLGKSSL
PKKPITDDDV DRISLCLKVL SECSPLMNDI FNKECRQSLS HMLSAKLEEE KLSQKKESEK
RNVTVQPDDP ISFMQLTAKN EMNCKEDQFQ LSLLAAMGNT QRKEAADPLA SKLNKVTQLT
GFSDPVYAEA YVHVNQYDIV LDVLVVNQTS DTLQNCTLEL ATLGDLKLVE KPSPLTLAPH
DFANIKANVK VASTENGIIF GNIVYDVSGA ASDRNCVVLS DIHIDIMDYI QPATCTDAEF
RQMWAEFEWE NKVTVNTNIV DLNDYLQHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI
FGEDALANVS IEKPIQQGPE APVTGHIRIR AKSQGMALSL GDKINLSQKK NSI


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