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   14-OCT-2015, entry version 121.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; 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
RT   subunit 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH CAPN8, SUBCELLULAR LOCATION, PTM, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=16476741; DOI=10.1074/jbc.M509244200;
RA   Hata S., Koyama S., Kawahara H., Doi N., Maeda T.,
RA   Toyama-Sorimachi N., Abe K., Suzuki K., Sorimachi H.;
RT   "Stomach-specific calpain, nCL-2, localizes in mucus cells and
RT   proteolyzes the beta-subunit of coatomer complex, beta-COP.";
RL   J. Biol. Chem. 281:11214-11224(2006).
RN   [6]
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   [7]
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   [8]
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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-494, AND IDENTIFICATION BY
RP   MASS 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.,
RA   Zhang Y., 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
CC       to dilysine motifs and reversibly associates with Golgi non-
CC       clathrin-coated vesicles, which further mediate biosynthetic
CC       protein transport from the ER, via the Golgi up to the trans Golgi
CC       network. Coatomer complex is required for budding from Golgi
CC       membranes, and is essential for the retrograde Golgi-to-ER
CC       transport of dilysine-tagged proteins. In mammals, the coatomer
CC       can only be recruited by membranes associated to ADP-ribosylation
CC       factors (ARFs), which are small GTP-binding proteins; the complex
CC       also influences the Golgi structural integrity, as well as the
CC       processing, activity, and endocytic recycling of LDL receptors.
CC       Involved in the Golgi disassembly and reassembly processes during
CC       cell cycle. Involved in autophagy by playing a role in early
CC       endosome function. Plays a role in organellar compartmentalization
CC       of secretory compartments including endoplasmic reticulum (ER)-
CC       Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network
CC       (TGN) and recycling endosomes, and in biosynthetic transport of
CC       CAV1 (By similarity). Plays a functional role in facilitating the
CC       transport of kappa-type opioid receptor mRNAs into axons and
CC       enhances translation of these proteins in cortical neurons.
CC       Required for limiting lipid storage in lipid droplets. Involved in
CC       lipid homeostasis by regulating the presence of perilipin family
CC       members PLIN2 and PLIN3 at the lipid droplet surface and promoting
CC       the association of adipocyte triglyceride lipase (PNPLA2) with the
CC       lipid droplet surface to mediate lipolysis. {ECO:0000250,
CC       ECO:0000269|PubMed:17698811, ECO:0000269|PubMed:19067489}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
CC       beta, beta', gamma, delta, epsilon and zeta subunits (By
CC       similarity). Interacts with CAPN8. Interacts with SCYL1 and PRKCE
CC       (By similarity). Interacts with COPG1 (By similarity). Interacts
CC       with ARF1 (myristoylated); this interaction is required for
CC       binding of COPB1 to Golgi membranes (By similarity). Interacts
CC       (via trunk domain) with ARF1 (via switch I region); the
CC       interaction is direct (By similarity). Interacts with KCNK2 (via
CC       N-terminus); this interaction increases the channel-mediated whole
CC       cell currents and promotes plasma membrane expression of KCNK2 (By
CC       similarity). Interacts with STX17 (By similarity). Interacts with
CC       TMEM115 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated
CC       vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
CC       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,
CC       as well as on the vesicles/buds originating from it (By
CC       similarity). Proteolytic cleavage by CAPN8 triggers translocation
CC       from Golgi to cytoplasm. Found in perinuclear vesicular-tubular
CC       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
CC       present at the cis- Golgi side in transitional areas (TA), on so-
CC       called peripheral elements (PE) consisting of tubules and vesicles
CC       located between the cup-shaped transitional elements (TE) of the
CC       rough endoplasmic reticulum (RER) and the cis-most Golgi cisternae
CC       (By similarity). Present in cytoplasm, not associated with visible
CC       coats or membranes, with a minor fraction present on small
CC       clusters of tubules and vesicles (By similarity). Some association
CC       with high-density and low-density microsomes and
CC       mitochondria/nuclei fraction (By similarity). Very little found in
CC       plasma membrane fraction (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the upper one-third
CC       of the oxyntic mucosa and in most regions of the pyloric mucosa
CC       (PubMed:16476741). Ubiquitiously expressed including platelet,
CC       liver, 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
CC       the beta-COP and presumably the other coatomer subunits.
CC   -!- SIMILARITY: Contains 6 HEAT repeats. {ECO:0000305}.
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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   UniGene; Mm.277024; -.
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   PDBsum; 5A1U; -.
DR   PDBsum; 5A1V; -.
DR   PDBsum; 5A1W; -.
DR   PDBsum; 5A1X; -.
DR   PDBsum; 5A1Y; -.
DR   ProteinModelPortal; Q9JIF7; -.
DR   BioGrid; 213992; 3.
DR   DIP; DIP-42642N; -.
DR   IntAct; Q9JIF7; 9.
DR   MINT; MINT-1489518; -.
DR   STRING; 10090.ENSMUSP00000033012; -.
DR   PhosphoSite; Q9JIF7; -.
DR   MaxQB; Q9JIF7; -.
DR   PaxDb; Q9JIF7; -.
DR   PRIDE; Q9JIF7; -.
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   eggNOG; COG5096; -.
DR   GeneTree; ENSGT00390000005270; -.
DR   HOGENOM; HOG000207417; -.
DR   HOVERGEN; HBG005380; -.
DR   InParanoid; Q9JIF7; -.
DR   KO; K17301; -.
DR   OMA; WSDFEWE; -.
DR   OrthoDB; EOG7ZWD12; -.
DR   PhylomeDB; Q9JIF7; -.
DR   TreeFam; TF105737; -.
DR   Reactome; R-MMU-199997; COPI Mediated Transport.
DR   ChiTaRS; Copb1; mouse.
DR   NextBio; 331414; -.
DR   PRO; PR:Q9JIF7; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; Q9JIF7; -.
DR   CleanEx; MM_COPB1; -.
DR   Genevisible; Q9JIF7; MM.
DR   GO; GO:0030126; C:COPI vesicle coat; IEA:Ensembl.
DR   GO; GO:0030137; C:COPI-coated vesicle; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; 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:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0016020; C:membrane; 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:0006891; P:intra-Golgi vesicle-mediated transport; IEA:Ensembl.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   Gene3D; 1.25.10.10; -; 3.
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; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell membrane; Complete proteome;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Protein transport; Reference proteome; Repeat; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P53618}.
FT   CHAIN         2    953       Coatomer subunit beta.
FT                                /FTId=PRO_0000193834.
FT   REPEAT       96    131       HEAT 1.
FT   REPEAT      132    168       HEAT 2.
FT   REPEAT      240    276       HEAT 3.
FT   REPEAT      277    314       HEAT 4.
FT   REPEAT      316    353       HEAT 5.
FT   REPEAT      396    433       HEAT 6.
FT   MOD_RES       2      2       N-acetylthreonine.
FT                                {ECO:0000250|UniProtKB:P53618}.
FT   MOD_RES     494    494       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   CONFLICT    757    757       T -> I (in Ref. 2; BAE29109).
FT                                {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
//