COPB_PIG
ID COPB_PIG Reviewed; 953 AA.
AC D2SW95;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Coatomer subunit beta {ECO:0000250|UniProtKB:A0JN39};
DE AltName: Full=Beta-coat protein {ECO:0000250|UniProtKB:A0JN39};
DE Short=Beta-COP {ECO:0000250|UniProtKB:A0JN39};
GN Name=COPB1 {ECO:0000250|UniProtKB:A0JN39};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ACZ15983.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=19830590; DOI=10.1007/s11033-009-9882-y;
RA Qiu H., Xu X., Fan B., Rothschild M.F., Martin Y., Liu B.;
RT "Investigation of LDHA and COPB1 as candidate genes for muscle development
RT in the MYOD1 region of pig chromosome 2.";
RL Mol. Biol. Rep. 37:629-636(2010).
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 (By similarity).
CC {ECO:0000250|UniProtKB:A0JN39, ECO:0000250|UniProtKB:P23514,
CC ECO:0000250|UniProtKB:P53618, ECO:0000250|UniProtKB:Q9JIF7}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits. Interacts with CAPN8
CC and PRKCE. Interacts with SCYL1. Interacts with COPG1. Interacts with
CC ARF1 (myristoylated); this interaction is required for binding of COPB1
CC to Golgi membranes. Interacts (via trunk domain) with ARF1 (via switch
CC I region); the interaction is direct. Interacts with KCNK2 (via N-
CC terminus); this interaction increases the channel-mediated whole cell
CC currents and promotes plasma membrane expression of KCNK2. Interacts
CC with STX17. Interacts with TMEM115 (By similarity). Interacts with
CC TMEM41B (By similarity). {ECO:0000250|UniProtKB:P23514,
CC ECO:0000250|UniProtKB:P53618, ECO:0000250|UniProtKB:Q9JIF7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0JN39,
CC ECO:0000250|UniProtKB:P23514, ECO:0000250|UniProtKB:P53618,
CC ECO:0000250|UniProtKB:Q9JIF7}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:A0JN39, ECO:0000250|UniProtKB:P23514,
CC ECO:0000250|UniProtKB:P53618, ECO:0000250|UniProtKB:Q9JIF7}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:A0JN39,
CC ECO:0000250|UniProtKB:P23514, ECO:0000250|UniProtKB:P53618,
CC ECO:0000250|UniProtKB:Q9JIF7}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:A0JN39, ECO:0000250|UniProtKB:P23514,
CC ECO:0000250|UniProtKB:P53618, ECO:0000250|UniProtKB:Q9JIF7}.
CC Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000250|UniProtKB:A0JN39, ECO:0000250|UniProtKB:P23514,
CC ECO:0000250|UniProtKB:P53618, ECO:0000250|UniProtKB:Q9JIF7}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:A0JN39,
CC ECO:0000250|UniProtKB:P23514, ECO:0000250|UniProtKB:P53618,
CC ECO:0000250|UniProtKB:Q9JIF7}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:A0JN39, ECO:0000250|UniProtKB:P23514,
CC ECO:0000250|UniProtKB:P53618, ECO:0000250|UniProtKB:Q9JIF7}. Cell
CC membrane {ECO:0000250|UniProtKB:A0JN39, ECO:0000250|UniProtKB:P23514,
CC ECO:0000250|UniProtKB:P53618, ECO:0000250|UniProtKB:Q9JIF7}.
CC Endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000250|UniProtKB:A0JN39, ECO:0000250|UniProtKB:P23514,
CC ECO:0000250|UniProtKB:P53618, ECO:0000250|UniProtKB:Q9JIF7}. Note=The
CC coatomer is cytoplasmic or polymerized on the cytoplasmic side of the
CC Golgi, as well as on the vesicles/buds originating from it. Proteolytic
CC cleavage by CAPN8 triggers translocation from Golgi to cytoplasm. Found
CC in perinuclear vesicular-tubular clusters (VTCs) and in the Golgi
CC region where associated with vesicles, buds and rims of the Golgi
CC stack. Occassionally present at the trans- side of Golgi, but mainly
CC present at the cis-Golgi side in transitional areas (TA), on so-called
CC peripheral elements (PE) consisting of tubules and vesicles located
CC between the cup-shaped transitional elements (TE) of the rough
CC endoplasmic reticulum (RER) and the cis-most Golgi cisternae. Present
CC in cytoplasm, not associated with visible coats or membranes, with a
CC minor fraction present on small clusters of tubules and vesicles. Some
CC association with high-density and low-density microsomes and
CC mitochondria/nuclei fraction. Very little found in plasma membrane
CC fraction. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: High expression in the lung, kidney, skeletal
CC muscle and small intestine, and lower level of expression in heart,
CC liver, spleen, stomach and fat. {ECO:0000269|PubMed:19830590}.
CC -!- MISCELLANEOUS: Brefeldin A induces dissociation from the Golgi of the
CC beta-COP and presumably the other coatomer subunits.
CC {ECO:0000250|UniProtKB:P53618}.
CC -!- MISCELLANEOUS: Important candidate gene for meat quality and growth
CC traits in animal breeding. May also be useful for the research of
CC muscle development mechanisms. {ECO:0000269|PubMed:19830590}.
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DR EMBL; FJ865397; ACZ15983.1; -; mRNA.
DR RefSeq; NP_001165837.1; NM_001172366.1.
DR AlphaFoldDB; D2SW95; -.
DR SMR; D2SW95; -.
DR STRING; 9823.ENSSSCP00000014234; -.
DR PaxDb; D2SW95; -.
DR PeptideAtlas; D2SW95; -.
DR PRIDE; D2SW95; -.
DR GeneID; 100337660; -.
DR KEGG; ssc:100337660; -.
DR CTD; 1315; -.
DR eggNOG; KOG1058; Eukaryota.
DR InParanoid; D2SW95; -.
DR OrthoDB; 195812at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
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 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_0000408943"
FT REPEAT 96..131
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 132..168
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 240..276
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 277..314
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 316..353
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 396..433
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
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; 107123 MW; 66C0CCAC4E407AE7 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 ILGEYCSTKE DIQSVMTEVR
RSLGEIPIVE SEIKKEAGEL KPEEEITVGP VQKLVTKMGT YATQSALSSS RPTKKEEERP
PLRGFLLDGD FFVAASLATT LTKIALRYVA LVQEKKRQNS FVAEAMLLMA TILHLGKSSP
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 NKVTVNTNII DLNDYLQHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI
FGEDALANVS IEKPIQQGPE APVTGHIRIR AKGQGMALSL GDKINLSQKK TSI
