COPB_PONAB
ID COPB_PONAB Reviewed; 953 AA.
AC Q5R922;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Coatomer subunit beta;
DE AltName: Full=Beta-coat protein;
DE Short=Beta-COP;
GN Name=COPB1; Synonyms=COPB;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Plays a functional role in facilitating the transport of
CC kappa-type opioid receptor mRNAs into axons and enhances translation of
CC these proteins. Required for limiting lipid storage in lipid droplets.
CC Involved in lipid homeostasis by regulating the presence of perilipin
CC family members PLIN2 and PLIN3 at the lipid droplet surface and
CC promoting the association of adipocyte surface triglyceride lipase
CC (PNPLA2) with the lipid droplet to mediate lipolysis. Involved in the
CC Golgi disassembly and reassembly processes during cell cycle. Involved
CC in autophagy by playing a role in early endosome function. Plays a role
CC in organellar compartmentalization of secretory compartments including
CC endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC),
CC Golgi, trans-Golgi network (TGN) and recycling endosomes, and in
CC biosynthetic transport of CAV1. Promotes degradation of Nef cellular
CC targets CD4 and MHC class I antigens by facilitating their trafficking
CC to degradative compartments (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits. Interacts (via C-
CC terminus) with HIV-1 Nef; the interaction is direct. Interacts with
CC CAPN8 and PRKCE. Interacts with SCYL1. Interacts with COPG1. Interacts
CC with ARF1 (myristoylated); this interaction is required for binding of
CC COPB1 to Golgi membranes. Interacts (via trunk domain) with ARF1 (via
CC switch I region); the interaction is direct. Interacts with KCNK2 (via
CC N-terminus); this interaction increases the channel-mediated whole cell
CC currents and promotes plasma membrane expression of KCNK2. Interacts
CC with anthrax lethal factor (LF); this interaction may facilitate
CC endosomal vesicle membrane translocation of LF and its release from the
CC lumen of endosomal vesicles to external milieu. Interacts with STX17.
CC Interacts with TMEM115 (By similarity). Interacts with TMEM41B (By
CC similarity). {ECO:0000250|UniProtKB:P23514,
CC ECO:0000250|UniProtKB:P53618, ECO:0000250|UniProtKB:Q9JIF7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cell membrane {ECO:0000250}. Endoplasmic reticulum-
CC Golgi 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. Proteolytic cleavage
CC by CAPN8 triggers translocation from Golgi to cytoplasm. Found in
CC perinuclear vesicular-tubular clusters (VTCs) and in the Golgi region
CC where associated with vesicles, buds and rims of the Golgi stack.
CC Occasionally present at the trans- side of Golgi, but mainly present at
CC the cis-Golgi side in transitional areas (TA), on so-called peripheral
CC elements (PE) consisting of tubules and vesicles located between the
CC cup-shaped transitional elements (TE) of the rough endoplasmic
CC reticulum (RER) and the cis-most Golgi cisternae. Present in cytoplasm,
CC not associated with visible coats or membranes, with a minor fraction
CC present on small clusters of tubules and vesicles. Some association
CC with high-density and low-density microsomes and mitochondria/nuclei
CC fraction. Very little found in plasma membrane fraction. {ECO:0000250}.
CC -!- MISCELLANEOUS: Brefeldin A induces dissociation from the Golgi of the
CC beta-COP and presumably the other coatomer subunits. {ECO:0000250}.
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DR EMBL; CR859574; CAH91738.1; -; mRNA.
DR AlphaFoldDB; Q5R922; -.
DR SMR; Q5R922; -.
DR STRING; 9601.ENSPPYP00000003980; -.
DR eggNOG; KOG1058; Eukaryota.
DR InParanoid; Q5R922; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
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:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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_0000347229"
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; 107157 MW; AC6B2865032165B9 CRC64;
MTAAENVCYT LINVPMDSEP PSEISLKNDL EKGDVKSKTE ALKKVIIMIL NGEKLPGLLM
TIIRFVLPLQ DHTIKKLLLV FWEIVPKTTP DGRLLHEMIL VCDAYRKDLQ HPNEFIRGST
LRFLCKLKEA ELLEPLMPAI RACLEHRHSY VRRNAVLAIY TIYRNFEHLI PDAPELIHDF
LVDEKDASCK RNAFMMLIHA DQDRALDYLS TCIDQVQTFG DILQLVIVEL IYKACHANPS
ERARFIRCIY NLLQSSSPAV KYEAAGTLVT LSSAPTAIKA AAQCYIDLII KESDNNVKLI
VLDRLIELKE HPAHERVLQD LVMDILRVLS TPDLEVRKKT LQLALDLVSS RNVEELVIVL
KKEVIKTNNV SEHEDTDKYR QLLVRTLHSC SVRFPDMAAN VIPVLMEFLS DNNEAAAADV
LEFVREAIQR FDNLRMLIVE KMLEVFHAIK SVKIYRGALW ILGEYCSTKE DIQSVMTEIR
RSLGEIPIVE SEIKKEAGEL KPEEEITVGP VQKLVTEMGT YATQSALSSS RPTKKEEDRP
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 NKVTVNTNMI DLNDYLRHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI
FGEDALANVS IEKPIHQGPD AAVTGHIRIR AKSQGMALSL GDKINLSQKK TSI
