P38968 · SEC31_YEAST
- ProteinProtein transport protein SEC31
- GeneSEC31
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1273 (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.
Miscellaneous
Present with 1840 molecules/cell in log phase SD medium.
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 | mating projection tip | |
Molecular Function | structural molecule activity | |
Biological Process | COPII-coated vesicle budding | |
Biological Process | COPII-coated vesicle cargo loading | |
Biological Process | endoplasmic reticulum organization | |
Biological Process | positive regulation of ER to Golgi vesicle-mediated transport | |
Biological Process | positive regulation of protein exit from endoplasmic reticulum | |
Biological Process | protein transport |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein transport protein SEC31
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP38968
- 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
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000051436 | 1-1273 | Protein transport protein SEC31 | |||
Sequence: MVKLAEFSRTATFAWSHDKIPLLVSGTVSGTVDANFSTDSSLELWSLLAADSEKPIASLQVDSKFNDLDWSHNNKIIAGALDNGSLELYSTNEANNAINSMARFSNHSSSVKTVKFNAKQDNVLASGGNNGEIFIWDMNKCTESPSNYTPLTPGQSMSSVDEVISLAWNQSLAHVFASAGSSNFASIWDLKAKKEVIHLSYTSPNSGIKQQLSVVEWHPKNSTRVATATGSDNDPSILIWDLRNANTPLQTLNQGHQKGILSLDWCHQDEHLLLSSGRDNTVLLWNPESAEQLSQFPARGNWCFKTKFAPEAPDLFACASFDNKIEVQTLQNLTNTLDEQETETKQQESETDFWNNVSREESKEKPTVFHLQAPTWYGEPSPAAHWAFGGKLVQITPDGKGVSITNPKISGLESNTTLSEALKTKDFKPLINQRLVKVIDDVNEEDWNLLEKLSMDGTEEFLKEALAFDNDESDAQDDANNEKEDDGEEFFQQIETNFQPEGDFSLSGNIEQTISKNLVSGNIKSAVKNSLENDLLMEAMVIALDSNNERLKESVKNAYFAKYGSKSSLSRILYSISKREVDDLVENLDVSQWKFISKAIQNLYPNDIAQRNEMLIKLGDRLKENGHRQDSLTLYLAAGSLDKVASIWLSEFPDLEDKLKKDNKTIYEAHSECLTEFIERFTVFSNFINGSSTINNEQLIAKFLEFINLTTSTGNFELATEFLNSLPSDNEEVKTEKARVLIASGKSLPAQNPATATTSKAKYTNAKTNKNVPVLPTPGMPSTTSIPSMQAPFYGMTPGASANALPPKPYVPATTTSAPVHTEGKYAPPSQPSMASPFVNKTNSSTRLNSFAPPPNPYATATVPATNVSTTSIPQNTFAPIQPGMPIMGDYNAQSSSIPSQPPINAVSGQTPHLNRKANDGWNDLPLKVKEKPSRAKAVSVAPPNILSTPTPLNGIPANAASTMPPPPLSRAPSSVSMVSPPPLHKNSRVPSLVATSESPRASISNPYAPPQSSQQFPIGTISTANQTSNTAQVASSNPYAPPPQQRVATPLSGGVPPAPLPKASNPYAPTATTQPNGSSYPPTGPYTNNHTMTSPPPVFNKPPTGPPPISMKKRSNKLASIEQNPSQGATYPPTLSSSASPLQPSQPPTLASQVNTSAENVSHEIPADQQPIVDFLKEELARVTPLTPKEYSKQLKDCDKRLKILFYHLEKQDLLTQPTIDCLHDLVALMKEKKYKEAMVIHANIATNHAQEGGNWLTGVKRLIGIAEATLN | ||||||
Modified residue | 349 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 836 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 974 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 977 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 980 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 988 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 992 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 999 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1050 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1053 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
The COPII coat is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. SEC13 and SEC31 make a 2:2 tetramer that forms the edge element of the COPII outer coat. The tetramer self-assembles in multiple copies to form the complete polyhedral cage. Interacts (via WD 8) with SEC13. Interacts with EMP24, ERV25, SEC16 and SHR3.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P38968 | SEC13 Q04491 | 7 | EBI-20524, EBI-16529 | |
BINARY | P38968 | SEC16 P48415 | 3 | EBI-20524, EBI-16551 | |
BINARY | P38968 | SEC23 P15303 | 3 | EBI-20524, EBI-16584 | |
BINARY | P38968 | SEC24 P40482 | 4 | EBI-20524, EBI-16592 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 6-46 | WD 1 | ||||
Sequence: EFSRTATFAWSHDKIPLLVSGTVSGTVDANFSTDSSLELWS | ||||||
Repeat | 60-99 | WD 2 | ||||
Sequence: QVDSKFNDLDWSHNNKIIAGALDNGSLELYSTNEANNAIN | ||||||
Repeat | 106-146 | WD 3 | ||||
Sequence: NHSSSVKTVKFNAKQDNVLASGGNNGEIFIWDMNKCTESPS | ||||||
Repeat | 158-198 | WD 4 | ||||
Sequence: SSVDEVISLAWNQSLAHVFASAGSSNFASIWDLKAKKEVIH | ||||||
Repeat | 207-250 | WD 5 | ||||
Sequence: GIKQQLSVVEWHPKNSTRVATATGSDNDPSILIWDLRNANTPLQ | ||||||
Repeat | 255-295 | WD 6 | ||||
Sequence: GHQKGILSLDWCHQDEHLLLSSGRDNTVLLWNPESAEQLSQ | ||||||
Repeat | 298-338 | WD 7 | ||||
Sequence: ARGNWCFKTKFAPEAPDLFACASFDNKIEVQTLQNLTNTLD | ||||||
Repeat | 385-405 | WD 8; interaction with SEC13 | ||||
Sequence: HWAFGGKLVQITPDGKGVSIT | ||||||
Region | 815-835 | Disordered | ||||
Sequence: TTSAPVHTEGKYAPPSQPSMA | ||||||
Region | 933-1162 | Disordered | ||||
Sequence: PSRAKAVSVAPPNILSTPTPLNGIPANAASTMPPPPLSRAPSSVSMVSPPPLHKNSRVPSLVATSESPRASISNPYAPPQSSQQFPIGTISTANQTSNTAQVASSNPYAPPPQQRVATPLSGGVPPAPLPKASNPYAPTATTQPNGSSYPPTGPYTNNHTMTSPPPVFNKPPTGPPPISMKKRSNKLASIEQNPSQGATYPPTLSSSASPLQPSQPPTLASQVNTSAENV | ||||||
Compositional bias | 944-958 | Polar residues | ||||
Sequence: PNILSTPTPLNGIPA | ||||||
Compositional bias | 990-1043 | Polar residues | ||||
Sequence: VPSLVATSESPRASISNPYAPPQSSQQFPIGTISTANQTSNTAQVASSNPYAPP | ||||||
Compositional bias | 1067-1096 | Polar residues | ||||
Sequence: PYAPTATTQPNGSSYPPTGPYTNNHTMTSP | ||||||
Compositional bias | 1117-1162 | Polar residues | ||||
Sequence: NKLASIEQNPSQGATYPPTLSSSASPLQPSQPPTLASQVNTSAENV |
Sequence similarities
Belongs to the WD repeat SEC31 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,273
- Mass (Da)138,717
- Last updated2011-07-27 v3
- Checksum87F192E4B10E7571
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 317 | in Ref. 1; AAA50367 | ||||
Sequence: A → T | ||||||
Sequence conflict | 367 | in Ref. 2; CAA58252 and 3; CAA98772 | ||||
Sequence: T → S | ||||||
Sequence conflict | 691 | in Ref. 1; AAA50367 | ||||
Sequence: S → N | ||||||
Sequence conflict | 754 | in Ref. 1; AAA50367 | ||||
Sequence: A → V | ||||||
Sequence conflict | 877 | in Ref. 1; AAA50367 | ||||
Sequence: T → A | ||||||
Compositional bias | 944-958 | Polar residues | ||||
Sequence: PNILSTPTPLNGIPA | ||||||
Compositional bias | 990-1043 | Polar residues | ||||
Sequence: VPSLVATSESPRASISNPYAPPQSSQQFPIGTISTANQTSNTAQVASSNPYAPP | ||||||
Compositional bias | 1067-1096 | Polar residues | ||||
Sequence: PYAPTATTQPNGSSYPPTGPYTNNHTMTSP | ||||||
Compositional bias | 1117-1162 | Polar residues | ||||
Sequence: NKLASIEQNPSQGATYPPTLSSSASPLQPSQPPTLASQVNTSAENV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U15219 EMBL· GenBank· DDBJ | AAA50367.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X83276 EMBL· GenBank· DDBJ | CAA58252.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z74243 EMBL· GenBank· DDBJ | CAA98772.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006938 EMBL· GenBank· DDBJ | DAA11668.2 EMBL· GenBank· DDBJ | Genomic DNA |