P15303 · SEC23_YEAST
- ProteinProtein transport protein SEC23
- GeneSEC23
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids768 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC23 interacts with BET3 in order to target TRAPPI complex to COPII involved in internalization of plasma membrane proteins like the maltose transporter.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | COPII vesicle coat | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum exit site | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | Golgi membrane | |
Molecular Function | GTPase activator activity | |
Molecular Function | zinc ion binding | |
Biological Process | COPII-coated vesicle cargo loading | |
Biological Process | intracellular protein transport | |
Biological Process | macroautophagy | |
Biological Process | positive regulation of ER to Golgi vesicle-mediated transport | |
Biological Process | positive regulation of protein exit from endoplasmic reticulum | |
Biological Process | regulation of COPII vesicle coating | |
Biological Process | reticulophagy |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProtein transport protein SEC23
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP15303
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle, COPII-coated vesicle membrane ; Peripheral membrane protein
Endoplasmic reticulum membrane ; Peripheral membrane protein
Golgi apparatus membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000205145 | 1-768 | Protein transport protein SEC23 | |||
Sequence: MDFETNEDINGVRFTWNVFPSTRSDANSNVVPVGCLYTPLKEYDELNVAPYNPVVCSGPHCKSILNPYCVIDPRNSSWSCPICNSRNHLPPQYTNLSQENMPLELQSTTIEYITNKPVTVPPIFFFVVDLTSETENLDSLKESIITSLSLLPPNALIGLITYGNVVQLHDLSSETIDRCNVFRGDREYQLEALTEMLTGQKPTGPGGAASHLPNAMNKVTPFSLNRFFLPLEQVEFKLNQLLENLSPDQWSVPAGHRPLRATGSALNIASLLLQGCYKNIPARIILFASGPGTVAPGLIVNSELKDPLRSHHDIDSDHAQHYKKACKFYNQIAQRVAANGHTVDIFAGCYDQIGMSEMKQLTDSTGGVLLLTDAFSTAIFKQSYLRLFAKDEEGYLKMAFNGNMAVKTSKDLKVQGLIGHASAVKKTDANNISESEIGIGATSTWKMASLSPYHSYAIFFEIANTAANSNPMMSAPGSADRPHLAYTQFITTYQHSSGTNRIRVTTVANQLLPFGTPAIAASFDQEAAAVLMARIAVHKAETDDGADVIRWLDRTLIKLCQKYADYNKDDPQSFRLAPNFSLYPQFTYYLRRSQFLSVFNNSPDETAFYRHIFTREDTTNSLIMIQPTLTSFSMEDDPQPVLLDSISVKPNTILLLDTFFFILIYHGEQIAQWRKAGYQDDPQYADFKALLEEPKLEAAELLVDRFPLPRFIDTEAGGSQARFLLSKLNPSDNYQDMARGGSTIVLTDDVSLQNFMTHLQQVAVSGQA |
Post-translational modification
Ubiquitinated. Ubiquitination is required for the formation of the SEC23/24 complex. Deubiquitinated by the UBP3/BRE5 complex.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
The COPII coat is composed of at least 7 proteins: the SEC23/24 complex, the SEC13/31 complex, SFB2, SFB3 and the protein SAR1. Forms two other heterodimeric complexes with SFB3 and PDR17. Interacts with BET1, BET3, BOS1, EMP24, GRH1, SEC16, SEC22 and SYS1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P15303 | GRH1 Q04410 | 5 | EBI-16584, EBI-32083 | |
BINARY | P15303 | HRR25 P29295 | 5 | EBI-16584, EBI-8536 | |
BINARY | P15303 | SAR1 P20606 | 3 | EBI-16584, EBI-16472 | |
BINARY | P15303 | SEC16 P48415 | 6 | EBI-16584, EBI-16551 | |
BINARY | P15303 | SEC24 P40482 | 6 | EBI-16584, EBI-16592 | |
BINARY | P15303 | SEC31 P38968 | 3 | EBI-16584, EBI-20524 | |
BINARY | P15303 | SFB2 P53953 | 5 | EBI-16584, EBI-17006 | |
BINARY | P15303 | SFB3 P38810 | 3 | EBI-16584, EBI-17012 | |
BINARY | P15303 | TRS33 Q99394 | 3 | EBI-16584, EBI-19480 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Sequence similarities
Belongs to the SEC23/SEC24 family. SEC23 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length768
- Mass (Da)85,385
- Last updated1990-04-01 v1
- Checksum69811913848265FB
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X15474 EMBL· GenBank· DDBJ | CAA33501.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U25842 EMBL· GenBank· DDBJ | AAB68114.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006949 EMBL· GenBank· DDBJ | DAA11597.1 EMBL· GenBank· DDBJ | Genomic DNA |