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Protein

Coatomer subunit beta

Gene

SEC26

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 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. Required for mitochondrial morphology.2 Publications

GO - Molecular functioni

GO - Biological processi

  • ER to Golgi vesicle-mediated transport Source: SGD
  • intracellular protein transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29813-MONOMER.
ReactomeiR-SCE-6807878. COPI-mediated anterograde transport.
R-SCE-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

Names & Taxonomyi

Protein namesi
Recommended name:
Coatomer subunit beta
Alternative name(s):
Beta-coat protein
Short name:
Beta-COP
Gene namesi
Name:SEC26
Ordered Locus Names:YDR238C
ORF Names:YD8419.05C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR238C.
SGDiS000002646. SEC26.

Subcellular locationi

GO - Cellular componenti

  • coated vesicle Source: SGD
  • COPI vesicle coat Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Causes a block in ER to Golgi transport. Exhibits exaggerated ER structures displaying interconnected networks of ER cisternae. Cells arrest at all stages of the vegetative cycle.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi334 – 3363DLD → NAN: Loses ability to recognize arginine (R)-based ER localization signals in proteins. Recognition of C-terminal di-lysine signals present in proteins is unimpaired. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 973973Coatomer subunit betaPRO_0000193839Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei181 – 1811PhosphoserineCombined sources
Modified residuei540 – 5401PhosphoserineCombined sources

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP41810.
PeptideAtlasiP41810.

PTM databases

iPTMnetiP41810.

Interactioni

Subunit structurei

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. The complex interacts with ARF1 and PAB1.1 Publication

Protein-protein interaction databases

BioGridi32289. 107 interactions.
DIPiDIP-6467N.
IntActiP41810. 32 interactions.
MINTiMINT-429001.

Structurei

3D structure databases

ProteinModelPortaliP41810.
SMRiP41810. Positions 27-468, 741-966.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati98 – 13336HEAT 1Add
BLAST
Repeati134 – 17037HEAT 2Add
BLAST
Repeati279 – 31739HEAT 3Add
BLAST
Repeati318 – 35437HEAT 4Add
BLAST

Sequence similaritiesi

Contains 4 HEAT repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00390000005270.
HOGENOMiHOG000207417.
InParanoidiP41810.
KOiK17301.
OMAiRTLHQCS.
OrthoDBiEOG78M09D.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
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.
SMARTiSM00185. ARM. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequencei

Sequence statusi: Complete.

P41810-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSLSSQPAY TLVFDPSPSM ETYSSTDFQK ALEKGSDEQK IDTMKSILVT
60 70 80 90 100
MLEGNPMPEL LMHIIRFVMP SKNKELKKLL YFYWEIVPKL AEDGKLRHEM
110 120 130 140 150
ILVCNAIQHD LQHPNEYIRG NTLRFLTKLR EAELLEQMVP SVLACLEYRH
160 170 180 190 200
AYVRKYAILA VFSIFKVSEH LLPDAKEIIN SFIVAETDPI CKRNAFIGLA
210 220 230 240 250
ELDRENALHY LENNIADIEN LDPLLQAVFV QFIRQDANRT PALKAQYIEL
260 270 280 290 300
LMELLSTTTS DEVIFETALA LTVLSANPNV LVPAVNKLID LAVKVSDNNI
310 320 330 340 350
KLIVLDRIQD INANNVGALE ELTLDILRVL NAEDLDVRSK ALDISMDLAT
360 370 380 390 400
SRNAEDVVQL LKKELQTTVN NPDQDKAMQY RQLLIKTIRT VAVNFVEMAA
410 420 430 440 450
SVVSLLLDFI GDLNSVAASG IIAFIKEVIE KYPQLRANIL ENMVQTLDKV
460 470 480 490 500
RSAKAYRGAL WIMGEYAEGE SEIQHCWKHI RNSVGEVPIL QSEIKKLTQN
510 520 530 540 550
QEHTEENEVD ATAKPTGPVI LPDGTYATES AFDVKTSQKS VTDEERDSRP
560 570 580 590 600
PIRRFVLSGD FYTAAILANT IIKLVLKFEN VSKNKTVINA LKAEALLILV
610 620 630 640 650
SIVRVGQSSL VEKKIDEDSL ERVMTSISIL LDEVNPEEKK EEVKLLEVAF
660 670 680 690 700
LDTTKSSFKR QIEIAKKNKH KRALKDSCKN IEPIDTPISF RQFAGVDSTN
710 720 730 740 750
VQKDSIEEDL QLAMKGDAIH ATSSSSISKL KKIVPLCGFS DPVYAEACIT
760 770 780 790 800
NNQFDVVLDV LLVNQTKETL KNLHVQFATL GDLKIIDTPQ KTNVIPHGFH
810 820 830 840 850
KFTVTVKVSS ADTGVIFGNI IYDGAHGEDA RYVILNDVHV DIMDYIKPAT
860 870 880 890 900
ADDEHFRTMW NAFEWENKIS VKSQLPTLHA YLRELVKGTN MGILTPSESL
910 920 930 940 950
GEDDCRFLSC NLYAKSSFGE DALANLCIEK DSKTNDVIGY VRIRSKGQGL
960 970
ALSLGDRVAL IAKKTNKLAL THV
Length:973
Mass (Da):109,019
Last modified:November 1, 1997 - v2
Checksum:i885420DB026BCFA3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti412 – 4121D → E in AAA61710 (PubMed:7929113).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11236 Genomic DNA. Translation: AAA61710.1.
Z49701 Genomic DNA. Translation: CAA89724.1.
BK006938 Genomic DNA. Translation: DAA12079.1.
PIRiS54534.
RefSeqiNP_010524.3. NM_001180546.3.

Genome annotation databases

EnsemblFungiiYDR238C; YDR238C; YDR238C.
GeneIDi851824.
KEGGisce:YDR238C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11236 Genomic DNA. Translation: AAA61710.1.
Z49701 Genomic DNA. Translation: CAA89724.1.
BK006938 Genomic DNA. Translation: DAA12079.1.
PIRiS54534.
RefSeqiNP_010524.3. NM_001180546.3.

3D structure databases

ProteinModelPortaliP41810.
SMRiP41810. Positions 27-468, 741-966.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32289. 107 interactions.
DIPiDIP-6467N.
IntActiP41810. 32 interactions.
MINTiMINT-429001.

PTM databases

iPTMnetiP41810.

Proteomic databases

MaxQBiP41810.
PeptideAtlasiP41810.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR238C; YDR238C; YDR238C.
GeneIDi851824.
KEGGisce:YDR238C.

Organism-specific databases

EuPathDBiFungiDB:YDR238C.
SGDiS000002646. SEC26.

Phylogenomic databases

GeneTreeiENSGT00390000005270.
HOGENOMiHOG000207417.
InParanoidiP41810.
KOiK17301.
OMAiRTLHQCS.
OrthoDBiEOG78M09D.

Enzyme and pathway databases

BioCyciYEAST:G3O-29813-MONOMER.
ReactomeiR-SCE-6807878. COPI-mediated anterograde transport.
R-SCE-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

Miscellaneous databases

PROiP41810.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
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.
SMARTiSM00185. ARM. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast beta- and beta'-coat proteins (COP). Two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein traffic."
    Duden R., Hosobuchi M., Hamamoto S., Winey M., Byers B., Schekman R.
    J. Biol. Chem. 269:24486-24495(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 353-362; 496-514; 645-655 AND 934-942, FUNCTION, PTM, DISRUPTION PHENOTYPE.
    Strain: RSY255.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Arf1p provides an unexpected link between COPI vesicles and mRNA in Saccharomyces cerevisiae."
    Trautwein M., Dengjel J., Schirle M., Spang A.
    Mol. Biol. Cell 15:5021-5037(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae."
    Altmann K., Westermann B.
    Mol. Biol. Cell 16:5410-5417(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Novel cargo-binding site in the beta and delta subunits of coatomer."
    Michelsen K., Schmid V., Metz J., Heusser K., Liebel U., Schwede T., Spang A., Schwappach B.
    J. Cell Biol. 179:209-217(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 334-ASP--ASP-336.
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-540, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCOPB_YEAST
AccessioniPrimary (citable) accession number: P41810
Secondary accession number(s): D6VSL9, Q03779
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 26000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.