COPB_BOVIN
ID COPB_BOVIN Reviewed; 953 AA.
AC A0JN39;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Coatomer subunit beta;
DE AltName: Full=Beta-coat protein;
DE Short=Beta-COP;
GN Name=COPB1;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=1898986; DOI=10.1038/349248a0;
RA Waters M.G., Serafini T., Rothman J.E.;
RT "'Coatomer': a cytosolic protein complex containing subunits of non-
RT clathrin-coated Golgi transport vesicles.";
RL Nature 349:248-251(1991).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1631136; DOI=10.1073/pnas.89.14.6408;
RA Donaldson J.G., Cassel D., Kahn R.A., Klausner R.D.;
RT "ADP-ribosylation factor, a small GTP-binding protein, is required for
RT binding of the coatomer protein beta-COP to Golgi membranes.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6408-6412(1992).
RN [4]
RP INTERACTION WITH ARF1, AND SUBCELLULAR LOCATION.
RX PubMed=8505331; DOI=10.1016/s0021-9258(19)50311-8;
RA Palmer D.J., Helms J.B., Beckers C.J., Orci L., Rothman J.E.;
RT "Binding of coatomer to Golgi membranes requires ADP-ribosylation factor.";
RL J. Biol. Chem. 268:12083-12089(1993).
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. Plays a functional role in facilitating the
CC transport of kappa-type opioid receptor mRNAs into axons and enhances
CC translation of these proteins. Required for limiting lipid storage in
CC lipid droplets. Involved in lipid homeostasis by regulating the
CC presence of perilipin family members PLIN2 and PLIN3 at the lipid
CC droplet surface and promoting the association of adipocyte surface
CC triglyceride lipase (PNPLA2) with the lipid droplet to mediate
CC lipolysis. Involved in autophagy by playing a role in early endosome
CC function. Plays a role in organellar compartmentalization of secretory
CC compartments including endoplasmic reticulum (ER)-Golgi intermediate
CC compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling
CC endosomes, and in biosynthetic transport of CAV1.
CC {ECO:0000269|PubMed:1631136}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits. Interacts with ARF1
CC (myristoylated); this interaction is required for binding of COPB1 to
CC Golgi membranes. Interacts with CAPN8 and PRKCE (By similarity).
CC Interacts with SCYL1 (By similarity). Interacts with COPG1 (By
CC similarity). Interacts (via trunk domain) with ARF1 (via switch I
CC region); the interaction is direct (By similarity). Interacts with
CC KCNK2 (via N-terminus); this interaction increases the channel-mediated
CC whole cell currents and promotes plasma membrane expression of KCNK2
CC (By similarity). Interacts with STX17 (By similarity). Interacts with
CC TMEM115 (By similarity). Interacts with TMEM41B (By similarity).
CC {ECO:0000250|UniProtKB:P23514, ECO:0000250|UniProtKB:P53618,
CC ECO:0000250|UniProtKB:Q9JIF7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1898986}.
CC Golgi apparatus membrane {ECO:0000269|PubMed:1631136,
CC ECO:0000269|PubMed:8505331}; Peripheral membrane protein; Cytoplasmic
CC side. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cell membrane {ECO:0000250}. Endoplasmic reticulum-Golgi
CC intermediate compartment {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 (Ref.1). 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 (By similarity). Occasionally present at the trans-side
CC 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 (By similarity). Present in cytoplasm, not associated with
CC visible coats or membranes, with a minor fraction present on small
CC clusters of tubules and vesicles (By similarity). Some association with
CC high-density and low-density microsomes and mitochondria/nuclei
CC fraction (By similarity). Very little found in plasma membrane fraction
CC (By similarity). {ECO:0000250}.
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.
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DR EMBL; BC126502; AAI26503.1; -; mRNA.
DR RefSeq; NP_001071475.1; NM_001078007.1.
DR RefSeq; XP_015330164.1; XM_015474678.1.
DR AlphaFoldDB; A0JN39; -.
DR SMR; A0JN39; -.
DR BioGRID; 192108; 1.
DR STRING; 9913.ENSBTAP00000008616; -.
DR PaxDb; A0JN39; -.
DR PeptideAtlas; A0JN39; -.
DR PRIDE; A0JN39; -.
DR Ensembl; ENSBTAT00000008616; ENSBTAP00000008616; ENSBTAG00000006556.
DR GeneID; 535533; -.
DR KEGG; bta:535533; -.
DR CTD; 1315; -.
DR VEuPathDB; HostDB:ENSBTAG00000006556; -.
DR VGNC; VGNC:27593; COPB1.
DR eggNOG; KOG1058; Eukaryota.
DR GeneTree; ENSGT00390000005270; -.
DR HOGENOM; CLU_006949_0_0_1; -.
DR InParanoid; A0JN39; -.
DR OMA; QCGFMAA; -.
DR OrthoDB; 195812at2759; -.
DR TreeFam; TF105737; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000006556; Expressed in saliva-secreting gland and 107 other tissues.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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 ER-Golgi transport; Golgi apparatus; Membrane; 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_0000283808"
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; 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
