COPB_MOUSE
ID COPB_MOUSE Reviewed; 953 AA.
AC Q9JIF7; Q3T9Y4; Q3TT72; Q3U8G9; Q3UE02;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Coatomer subunit beta;
DE AltName: Full=Beta-coat protein;
DE Short=Beta-COP;
GN Name=Copb1; Synonyms=Copb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=11441537; DOI=10.1023/a:1018845607777;
RA Li W., Elliott R.W., Novak E.K., Swank R.T.;
RT "cDNA sequence and mapping of the mouse Copb gene encoding the beta subunit
RT of the COPI coatomer complex.";
RL Somat. Cell Mol. Genet. 25:177-183(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Pituitary, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=7593324; DOI=10.1242/jcs.108.8.2839;
RA Griffiths G., Pepperkok R., Locker J.K., Kreis T.E.;
RT "Immunocytochemical localization of beta-COP to the ER-Golgi boundary and
RT the TGN.";
RL J. Cell Sci. 108:2839-2856(1995).
RN [6]
RP INTERACTION WITH CAPN8, SUBCELLULAR LOCATION, PTM, AND TISSUE SPECIFICITY.
RX PubMed=16476741; DOI=10.1074/jbc.m509244200;
RA Hata S., Koyama S., Kawahara H., Doi N., Maeda T., Toyama-Sorimachi N.,
RA Abe K., Suzuki K., Sorimachi H.;
RT "Stomach-specific calpain, nCL-2, localizes in mucus cells and proteolyzes
RT the beta-subunit of coatomer complex, beta-COP.";
RL J. Biol. Chem. 281:11214-11224(2006).
RN [7]
RP FUNCTION.
RX PubMed=17698811; DOI=10.1073/pnas.0703805104;
RA Bi J., Tsai N.P., Lu H.Y., Loh H.H., Wei L.N.;
RT "Copb1-facilitated axonal transport and translation of kappa opioid-
RT receptor mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13810-13815(2007).
RN [8]
RP FUNCTION.
RX PubMed=19067489; DOI=10.1371/journal.pbio.0060292;
RA Beller M., Sztalryd C., Southall N., Bell M., Jackle H., Auld D.S.,
RA Oliver B.;
RT "COPI complex is a regulator of lipid homeostasis.";
RL PLoS Biol. 6:E292-E292(2008).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=19587158; DOI=10.1177/0022034509338452;
RA Takatalo M.S., Tummers M., Thesleff I., Roennholm R.;
RT "Novel Golgi protein, GoPro49, is a specific dental follicle marker.";
RL J. Dent. Res. 88:534-538(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-494, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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. Involved in autophagy by playing a role in early
CC endosome function. Plays a role in organellar compartmentalization of
CC secretory compartments including endoplasmic reticulum (ER)-Golgi
CC intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and
CC recycling endosomes, and in biosynthetic transport of CAV1 (By
CC similarity). Plays a functional role in facilitating the transport of
CC kappa-type opioid receptor mRNAs into axons and enhances translation of
CC these proteins in cortical neurons. Required for limiting lipid storage
CC in 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 triglyceride
CC lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis.
CC {ECO:0000250, ECO:0000269|PubMed:17698811,
CC ECO:0000269|PubMed:19067489}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits (By similarity).
CC Interacts with CAPN8. Interacts with SCYL1 and PRKCE (By similarity).
CC Interacts with COPG1 (By similarity). Interacts with ARF1
CC (myristoylated); this interaction is required for binding of COPB1 to
CC Golgi membranes (By similarity). Interacts (via trunk domain) with ARF1
CC (via switch I region); the interaction is direct (By similarity).
CC Interacts with KCNK2 (via N-terminus); this interaction increases the
CC channel-mediated whole cell currents and promotes plasma membrane
CC expression of KCNK2 (By similarity). Interacts with STX17 (By
CC similarity). Interacts with TMEM115 (By similarity). Interacts with
CC TMEM41B (By similarity). {ECO:0000250|UniProtKB:P23514,
CC ECO:0000250|UniProtKB:P53618}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23514}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:16476741,
CC ECO:0000269|PubMed:19587158, ECO:0000269|PubMed:7593324}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:P53618}; Cytoplasmic side
CC {ECO:0000305}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000269|PubMed:7593324}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane
CC {ECO:0000250|UniProtKB:P53618}. Endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000269|PubMed:7593324}. 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 (By
CC similarity). Proteolytic cleavage by CAPN8 triggers translocation from
CC Golgi to cytoplasm (PubMed:16476741). Found in perinuclear vesicular-
CC tubular clusters (VTCs) and in the Golgi region where associated with
CC vesicles, buds and rims of the Golgi stack (By similarity).
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 (By similarity).
CC Present in cytoplasm, not associated with visible coats or membranes,
CC with a minor fraction present on small clusters of tubules and vesicles
CC (By similarity). Some association with high-density and low-density
CC microsomes and mitochondria/nuclei fraction (By similarity). Very
CC little found in plasma membrane fraction (By similarity).
CC {ECO:0000250|UniProtKB:P23514, ECO:0000269|PubMed:16476741}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the upper one-third of
CC the oxyntic mucosa and in most regions of the pyloric mucosa
CC (PubMed:16476741). Ubiquitously expressed including platelet, liver,
CC heart, spleen, lung and kidney (PubMed:11441537).
CC {ECO:0000269|PubMed:11441537, ECO:0000269|PubMed:16476741}.
CC -!- PTM: Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8.
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; AF231925; AAF76856.1; -; mRNA.
DR EMBL; AK149828; BAE29109.1; -; mRNA.
DR EMBL; AK152222; BAE31049.1; -; mRNA.
DR EMBL; AK161544; BAE36453.1; -; mRNA.
DR EMBL; AK172214; BAE42886.1; -; mRNA.
DR EMBL; CH466531; EDL17060.1; -; Genomic_DNA.
DR EMBL; BC030837; AAH30837.1; -; mRNA.
DR CCDS; CCDS21759.1; -.
DR RefSeq; NP_203534.1; NM_033370.3.
DR PDB; 5A1U; EM; 13.00 A; G=1-953.
DR PDB; 5A1V; EM; 21.00 A; G/O/X=1-953.
DR PDB; 5A1W; EM; 18.00 A; G=1-953.
DR PDB; 5A1X; EM; 23.00 A; G/O=1-953.
DR PDB; 5A1Y; EM; 21.00 A; G/O=1-953.
DR PDB; 5NZR; EM; 9.20 A; B=1-953.
DR PDB; 5NZS; EM; 10.10 A; B=1-953.
DR PDB; 5NZT; EM; 17.00 A; B/N=1-953.
DR PDB; 5NZU; EM; 15.00 A; B=1-953.
DR PDB; 5NZV; EM; 17.30 A; B/I=1-953.
DR PDBsum; 5A1U; -.
DR PDBsum; 5A1V; -.
DR PDBsum; 5A1W; -.
DR PDBsum; 5A1X; -.
DR PDBsum; 5A1Y; -.
DR PDBsum; 5NZR; -.
DR PDBsum; 5NZS; -.
DR PDBsum; 5NZT; -.
DR PDBsum; 5NZU; -.
DR PDBsum; 5NZV; -.
DR AlphaFoldDB; Q9JIF7; -.
DR SMR; Q9JIF7; -.
DR BioGRID; 213992; 25.
DR CORUM; Q9JIF7; -.
DR DIP; DIP-42642N; -.
DR IntAct; Q9JIF7; 6.
DR MINT; Q9JIF7; -.
DR STRING; 10090.ENSMUSP00000033012; -.
DR iPTMnet; Q9JIF7; -.
DR PhosphoSitePlus; Q9JIF7; -.
DR SwissPalm; Q9JIF7; -.
DR EPD; Q9JIF7; -.
DR jPOST; Q9JIF7; -.
DR MaxQB; Q9JIF7; -.
DR PaxDb; Q9JIF7; -.
DR PeptideAtlas; Q9JIF7; -.
DR PRIDE; Q9JIF7; -.
DR ProteomicsDB; 284084; -.
DR Antibodypedia; 3231; 244 antibodies from 32 providers.
DR DNASU; 70349; -.
DR Ensembl; ENSMUST00000033012; ENSMUSP00000033012; ENSMUSG00000030754.
DR GeneID; 70349; -.
DR KEGG; mmu:70349; -.
DR UCSC; uc009jhx.1; mouse.
DR CTD; 1315; -.
DR MGI; MGI:1917599; Copb1.
DR VEuPathDB; HostDB:ENSMUSG00000030754; -.
DR eggNOG; KOG1058; Eukaryota.
DR GeneTree; ENSGT00390000005270; -.
DR HOGENOM; CLU_006949_0_0_1; -.
DR InParanoid; Q9JIF7; -.
DR OMA; QCGFMAA; -.
DR OrthoDB; 195812at2759; -.
DR PhylomeDB; Q9JIF7; -.
DR TreeFam; TF105737; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 70349; 25 hits in 77 CRISPR screens.
DR ChiTaRS; Copb1; mouse.
DR PRO; PR:Q9JIF7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JIF7; protein.
DR Bgee; ENSMUSG00000030754; Expressed in ureter smooth muscle and 274 other tissues.
DR Genevisible; Q9JIF7; MM.
DR GO; GO:0030126; C:COPI vesicle coat; ISO:MGI.
DR GO; GO:0030137; C:COPI-coated vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005798; C:Golgi-associated vesicle; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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; ISO:MGI.
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 3D-structure; 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_0000193834"
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:0007744|PubMed:23806337"
FT CONFLICT 757
FT /note="T -> I (in Ref. 2; BAE29109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 953 AA; 107066 MW; 4CD5407AD87ACB4B 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
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 NKVTVNTNMT DLNDYLQHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI
FGEDALANVS IEKPVHQGPD AAVTGHIRIR AKSQGMALSL GDKINLSQKK TSL
