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Protein

Coatomer subunit beta

Gene

Copb1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1. Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins in the axonal compartment of dorsal root ganglion (DRG) cells. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis.4 Publications

GO - Molecular functioni

GO - Biological processi

  • intracellular protein transport Source: InterPro
  • intra-Golgi vesicle-mediated transport Source: UniProtKB
  • retrograde vesicle-mediated transport, Golgi to ER Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-199997. COPI Mediated Transport.
R-RNO-6807878. COPI-mediated anterograde transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Coatomer subunit beta
Alternative name(s):
Beta-coat protein
Short name:
Beta-COP
Gene namesi
Name:Copb1
Synonyms:Copb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi620861. Copb1.

Subcellular locationi

GO - Cellular componenti

  • COPI vesicle coat Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB-KW
  • endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
  • Golgi apparatus Source: MGI
  • Golgi-associated vesicle Source: RGD
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 953952Coatomer subunit betaPRO_0000193835Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei494 – 4941N6-acetyllysineBy similarity

Post-translational modificationi

Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8.By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP23514.
PRIDEiP23514.

Expressioni

Gene expression databases

GenevisibleiP23514. RN.

Interactioni

Subunit structurei

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts with SCYL1. Interacts with CAPN8 (By similarity). Interacts with COPG1 (By similarity). Interacts with ARF1 (myristoylated); this interaction is required for binding of COPB1 to Golgi membranes (By similarity). Interacts (via trunk domain) with ARF1 (via switch I region); the interaction is direct (By similarity). Interacts with KCNK2 (via N-terminus); this interaction increases the channel-mediated whole cell currents and promotes plasma membrane expression of KCNK2 (By similarity). Interacts with PRKCE. Interacts with STX17. Interacts with TMEM115 (By similarity).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARCN1P536193EBI-620488,EBI-620432From a different organism.

Protein-protein interaction databases

BioGridi250261. 1 interaction.
IntActiP23514. 3 interactions.
MINTiMINT-4563577.
STRINGi10116.ENSRNOP00000016292.

Structurei

3D structure databases

ProteinModelPortaliP23514.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati96 – 13136HEAT 1Add
BLAST
Repeati132 – 16837HEAT 2Add
BLAST
Repeati240 – 27637HEAT 3Add
BLAST
Repeati277 – 31438HEAT 4Add
BLAST
Repeati316 – 35338HEAT 5Add
BLAST
Repeati396 – 43338HEAT 6Add
BLAST

Sequence similaritiesi

Contains 6 HEAT repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1058. Eukaryota.
COG5096. LUCA.
GeneTreeiENSGT00390000005270.
HOGENOMiHOG000207417.
HOVERGENiHBG005380.
InParanoidiP23514.
KOiK17301.
OMAiWSDFEWE.
OrthoDBiEOG7ZWD12.
PhylomeDBiP23514.
TreeFamiTF105737.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR011710. Coatomer_bsu_C.
IPR016460. COPB1.
IPR029446. COPB1_appendage_platform_dom.
[Graphical view]
PANTHERiPTHR10635. PTHR10635. 1 hit.
PfamiPF01602. Adaptin_N. 1 hit.
PF07718. Coatamer_beta_C. 1 hit.
PF14806. Coatomer_b_Cpla. 1 hit.
[Graphical view]
PIRSFiPIRSF005727. Coatomer_beta_subunit. 1 hit.
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23514-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAAENVCYT LINVPMDSEP PSEISLKNDL EKGDVKSKTE ALKKVIIMIL
60 70 80 90 100
NGEKLPGLLM TIIRFVLPLQ DHTIKKLLLV FWEIVPKTTP DGRLLHEMIL
110 120 130 140 150
VCDAYRKDLQ HPNEFIRGST LRFLCKLKEA ELLEPLMPAI RACLEHRHSY
160 170 180 190 200
VRRNAVLAIY TIYRNFENLI PDAPELIHDF LVNEKDASCK RNAFMMLIHA
210 220 230 240 250
DQDRALDYLS TCIDQVQTFG DILQLVIVEL IYKVCHANPS ERARFIRCIY
260 270 280 290 300
NLLQSSSPAV KYEAAGTLVT LSSAPTAIKA AAQCYIDLII KESDNNVKLI
310 320 330 340 350
VLDRLVELKE HPAHERVLQD LVMDILRVLS TPDLEVRKKT LQLALDLVSS
360 370 380 390 400
RNVEELVIVL KKEVIKTNNV SEHEDTDKYR QLLVRTLHSC SVRFPDMAAN
410 420 430 440 450
VIPVLMEFLS DSNEAAAADV LEFVREAIQR FDNLRMLIVE KMLEVFHAIK
460 470 480 490 500
SVKIYRGALW ILGEYCSTKE DIQSVMTEVR RSLGEIPIVE SEIKKEAGEL
510 520 530 540 550
KPEEEITVGP VQKLVTEMGT YATQSALSSS RPTKKEEDRP PLRGFLLDGD
560 570 580 590 600
FFVAASLATT LTKIALRYVA LVQEKKKQNS FVAEAMLLMA TILHLGKSSL
610 620 630 640 650
PKKPITDDDV DRISLCLKVL SECSPLMNDI FNKECRQSLS QMLSAKLEEE
660 670 680 690 700
KLSQKKESEK RNVTVQPDDP ISFMQLTAKN EMNCKEDQFQ LSLLAAMGNT
710 720 730 740 750
QRKEAADPLA SKLNKVTQLT GFSDPVYAEA YVHVNQYDIV LDVLVVNQTS
760 770 780 790 800
DTLQNCTLEL ATLGDLKLVE KPSPLTLAPH DFANIKANVK VASTENGIIF
810 820 830 840 850
GNIVYDVSGA ASDRNCVVLS DIHIDIMDYI QPATCTDAEF RQMWAEFEWE
860 870 880 890 900
NKVTVNTNVT DLNDYLQHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI
910 920 930 940 950
FGEDALANVS IEKPVHQGPD AAVTGHIRIR AKSQGMALSL GDKINLSQKK

TSL
Length:953
Mass (Da):107,011
Last modified:November 1, 1991 - v1
Checksum:iFB44C55D13A9B101
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57228 mRNA. Translation: CAA40505.1.
BC061882 mRNA. Translation: AAH61882.1.
PIRiS13520.
RefSeqiNP_542959.1. NM_080781.2.
XP_008757882.1. XM_008759660.1.
XP_008757883.1. XM_008759661.1.
UniGeneiRn.4327.

Genome annotation databases

EnsembliENSRNOT00000083293; ENSRNOP00000072797; ENSRNOG00000057623.
GeneIDi114023.
KEGGirno:114023.
UCSCiRGD:620861. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57228 mRNA. Translation: CAA40505.1.
BC061882 mRNA. Translation: AAH61882.1.
PIRiS13520.
RefSeqiNP_542959.1. NM_080781.2.
XP_008757882.1. XM_008759660.1.
XP_008757883.1. XM_008759661.1.
UniGeneiRn.4327.

3D structure databases

ProteinModelPortaliP23514.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250261. 1 interaction.
IntActiP23514. 3 interactions.
MINTiMINT-4563577.
STRINGi10116.ENSRNOP00000016292.

Proteomic databases

PaxDbiP23514.
PRIDEiP23514.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000083293; ENSRNOP00000072797; ENSRNOG00000057623.
GeneIDi114023.
KEGGirno:114023.
UCSCiRGD:620861. rat.

Organism-specific databases

CTDi1315.
RGDi620861. Copb1.

Phylogenomic databases

eggNOGiKOG1058. Eukaryota.
COG5096. LUCA.
GeneTreeiENSGT00390000005270.
HOGENOMiHOG000207417.
HOVERGENiHBG005380.
InParanoidiP23514.
KOiK17301.
OMAiWSDFEWE.
OrthoDBiEOG7ZWD12.
PhylomeDBiP23514.
TreeFamiTF105737.

Enzyme and pathway databases

ReactomeiR-RNO-199997. COPI Mediated Transport.
R-RNO-6807878. COPI-mediated anterograde transport.

Miscellaneous databases

NextBioi618175.
PROiP23514.

Gene expression databases

GenevisibleiP23514. RN.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR011710. Coatomer_bsu_C.
IPR016460. COPB1.
IPR029446. COPB1_appendage_platform_dom.
[Graphical view]
PANTHERiPTHR10635. PTHR10635. 1 hit.
PfamiPF01602. Adaptin_N. 1 hit.
PF07718. Coatamer_beta_C. 1 hit.
PF14806. Coatomer_b_Cpla. 1 hit.
[Graphical view]
PIRSFiPIRSF005727. Coatomer_beta_subunit. 1 hit.
SUPFAMiSSF48371. SSF48371. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Beta-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to beta-adaptin."
    Duden R., Griffiths G., Frank R., Argos P., Kreis T.E.
    Cell 64:649-665(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 108-117; 262-276; 328-337; 496-527; 568-575; 768-786 AND 853-967, SUBCELLULAR LOCATION.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. "Binding of ARF and beta-COP to Golgi membranes: possible regulation by a trimeric G protein."
    Donaldson J.G., Kahn R.A., Lippincott-Schwartz J., Klausner R.D.
    Science 254:1197-1199(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  4. "Beta-COP localizes mainly to the cis-Golgi side in exocrine pancreas."
    Oprins A., Duden R., Kreis T.E., Geuze H.J., Slot J.W.
    J. Cell Biol. 121:49-59(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Beta-COP is essential for transport of protein from the endoplasmic reticulum to the Golgi in vitro."
    Peter F., Plutner H., Zhu H., Kreis T.E., Balch W.E.
    J. Cell Biol. 122:1155-1167(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  6. "Association of N-ethylmaleimide sensitive fusion (NSF) protein and soluble NSF attachment proteins-alpha and -gamma with glucose transporter-4-containing vesicles in primary rat adipocytes."
    Mastick C.C., Falick A.L.
    Endocrinology 138:2391-2397(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "The coatomer protein beta'-COP, a selective binding protein (RACK) for protein kinase Cepsilon."
    Csukai M., Chen C.-H., de Matteis M.A., Mochly-Rosen D.
    J. Biol. Chem. 272:29200-29206(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKCE.
  8. "GBF1. A novel Golgi-associated bfa-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5."
    Claude A., Zhao B.-P., Kuziemsky C.E., Dahan S., Berger S.J., Yan J.-P., Armold A.D., Sullivan E.M., Melancon P.
    J. Cell Biol. 146:71-84(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "A Rab2 mutant with impaired GTPase activity stimulates vesicle formation from pre-Golgi intermediates."
    Tisdale E.J.
    Mol. Biol. Cell 10:1837-1849(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Structural integrity of the Golgi stack is essential for normal secretory functions of rat parotid acinar cells: effects of brefeldin A and okadaic acid."
    Tamaki H., Yamashina S.
    J. Histochem. Cytochem. 50:1611-1623(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Identification and characterization of GIV, a novel Galpha i/s-interacting protein found on COPI, endoplasmic reticulum-Golgi transport vesicles."
    Le-Niculescu H., Niesman I., Fischer T., DeVries L., Farquhar M.G.
    J. Biol. Chem. 280:22012-22020(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "Copb1-facilitated axonal transport and translation of kappa opioid-receptor mRNA."
    Bi J., Tsai N.P., Lu H.Y., Loh H.H., Wei L.N.
    Proc. Natl. Acad. Sci. U.S.A. 104:13810-13815(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Scyl1, mutated in a recessive form of spinocerebellar neurodegeneration, regulates COPI-mediated retrograde traffic."
    Burman J.L., Bourbonniere L., Philie J., Stroh T., Dejgaard S.Y., Presley J.F., McPherson P.S.
    J. Biol. Chem. 283:22774-22786(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCYL1.
  14. "Quantitative proteomics analysis of cell cycle-regulated Golgi disassembly and reassembly."
    Chen X., Simon E.S., Xiang Y., Kachman M., Andrews P.C., Wang Y.
    J. Biol. Chem. 285:7197-7207(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  15. "Syntaxin 17 cycles between the ER and ERGIC and is required to maintain the architecture of ERGIC and Golgi."
    Muppirala M., Gupta V., Swarup G.
    Biol. Cell 103:333-350(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STX17.

Entry informationi

Entry nameiCOPB_RAT
AccessioniPrimary (citable) accession number: P23514
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: February 17, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Brefeldin A induces dissociation from the Golgi of the beta-COP and presumably the other coatomer subunits.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.