Q9UBV8 · PEF1_HUMAN
- ProteinPeflin
- GenePEF1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids284 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Calcium-binding protein that acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium. Together with PDCD6, acts as a calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in endoplasmic reticulum (ER)-Golgi transport by regulating the size of COPII coats (PubMed:27716508).
In response to cytosolic calcium increase, the heterodimer formed with PDCD6 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification (PubMed:27716508).
Its role in the heterodimer formed with PDCD6 is however unclear: some evidence shows that PEF1 and PDCD6 work together and promote association between PDCD6 and SEC31 in presence of calcium (PubMed:27716508).
Other reports show that PEF1 dissociates from PDCD6 in presence of calcium, and may act as a negative regulator of PDCD6 (PubMed:11278427).
Also acts as a negative regulator of ER-Golgi transport; possibly by inhibiting interaction between PDCD6 and SEC31 (By similarity).
In response to cytosolic calcium increase, the heterodimer formed with PDCD6 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification (PubMed:27716508).
Its role in the heterodimer formed with PDCD6 is however unclear: some evidence shows that PEF1 and PDCD6 work together and promote association between PDCD6 and SEC31 in presence of calcium (PubMed:27716508).
Other reports show that PEF1 dissociates from PDCD6 in presence of calcium, and may act as a negative regulator of PDCD6 (PubMed:11278427).
Also acts as a negative regulator of ER-Golgi transport; possibly by inhibiting interaction between PDCD6 and SEC31 (By similarity).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 127 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 129 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 131 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 133 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 138 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 194 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 196 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 198 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 200 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 205 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | COPII vesicle coat | |
Cellular Component | Cul3-RING ubiquitin ligase complex | |
Cellular Component | cytoplasm | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular exosome | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent protein binding | |
Molecular Function | identical protein binding | |
Molecular Function | protein dimerization activity | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | RNA binding | |
Molecular Function | ubiquitin-like ligase-substrate adaptor activity | |
Biological Process | COPII vesicle coating | |
Biological Process | endoplasmic reticulum to Golgi vesicle-mediated transport | |
Biological Process | neural crest cell development | |
Biological Process | neural crest formation | |
Biological Process | positive regulation of protein monoubiquitination | |
Biological Process | response to calcium ion |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeflin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UBV8
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Peripheral membrane protein
Cytoplasmic vesicle, COPII-coated vesicle membrane ; Peripheral membrane protein
Note: Membrane-associated in the presence of Ca2+ (PubMed:11278427).
Localizes to endoplasmic reticulum exit site (ERES) (By similarity).
Localizes to endoplasmic reticulum exit site (ERES) (By similarity).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 137 | Decreased ubiquitination by the BCR(KLHL12) E3 ubiquitin ligase complex. | ||||
Sequence: K → R | ||||||
Mutagenesis | 165 | Does not affect ubiquitination by the BCR(KLHL12) E3 ubiquitin ligase complex. | ||||
Sequence: K → R | ||||||
Mutagenesis | 167 | Does not affect ubiquitination by the BCR(KLHL12) E3 ubiquitin ligase complex. | ||||
Sequence: K → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 323 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000247045 | 1-284 | Peflin | |||
Sequence: MASYPYRQGCPGAAGQAPGAPPGSYYPGPPNSGGQYGSGLPPGGGYGGPAPGGPYGPPAGGGPYGHPNPGMFPSGTPGGPYGGAAPGGPYGQPPPSSYGAQQPGLYGQGGAPPNVDPEAYSWFQSVDSDHSGYISMKELKQALVNCNWSSFNDETCLMMINMFDKTKSGRIDVYGFSALWKFIQQWKNLFQQYDRDRSGSISYTELQQALSQMGYNLSPQFTQLLVSRYCPRSANPAMQLDRFIQVCTQLQVLTEAFREKDTAVQGNIRLSFEDFVTMTASRML | ||||||
Cross-link | 137 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Ubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Interaction
Subunit
Heterodimer; heterodimerizes (via the EF-hand 5) with PDCD6 (PubMed:11278427, PubMed:11883899, PubMed:27716508).
Dissociates from PDCD6 in presence of calcium (PubMed:11278427).
Dissociates from PDCD6 in presence of calcium (PubMed:11278427).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, repeat, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-111 | Disordered | ||||
Sequence: MASYPYRQGCPGAAGQAPGAPPGSYYPGPPNSGGQYGSGLPPGGGYGGPAPGGPYGPPAGGGPYGHPNPGMFPSGTPGGPYGGAAPGGPYGQPPPSSYGAQQPGLYGQGGA | ||||||
Repeat | 21-29 | 1 | ||||
Sequence: PPGSYYPGP | ||||||
Region | 21-109 | 9 X 9 AA approximate tandem repeat of [AP]-P-G-G-P-Y-G-G-P-P | ||||
Sequence: PPGSYYPGPPNSGGQYGSGLPPGGGYGGPAPGGPYGPPAGGGPYGHPNPGMFPSGTPGGPYGGAAPGGPYGQPPPSSYGAQQPGLYGQG | ||||||
Repeat | 31-39 | 2 | ||||
Sequence: NSGGQYGSG | ||||||
Repeat | 41-49 | 3 | ||||
Sequence: PPGGGYGGP | ||||||
Compositional bias | 47-64 | Pro residues | ||||
Sequence: GGPAPGGPYGPPAGGGPY | ||||||
Repeat | 50-58 | 4 | ||||
Sequence: APGGPYGPP | ||||||
Repeat | 59-67 | 5 | ||||
Sequence: AGGGPYGHP | ||||||
Repeat | 76-84 | 6 | ||||
Sequence: TPGGPYGGA | ||||||
Repeat | 85-92 | 7 | ||||
Sequence: APGGPYGQ | ||||||
Repeat | 93-100 | 8 | ||||
Sequence: PPPSSYGA | ||||||
Repeat | 101-109 | 9 | ||||
Sequence: QQPGLYGQG | ||||||
Domain | 114-149 | EF-hand 1 | ||||
Sequence: NVDPEAYSWFQSVDSDHSGYISMKELKQALVNCNWS | ||||||
Domain | 155-183 | EF-hand 2 | ||||
Sequence: TCLMMINMFDKTKSGRIDVYGFSALWKFI | ||||||
Domain | 181-216 | EF-hand 3 | ||||
Sequence: KFIQQWKNLFQQYDRDRSGSISYTELQQALSQMGYN | ||||||
Region | 204-284 | Required for interaction with PDCD6 | ||||
Sequence: TELQQALSQMGYNLSPQFTQLLVSRYCPRSANPAMQLDRFIQVCTQLQVLTEAFREKDTAVQGNIRLSFEDFVTMTASRML | ||||||
Domain | 217-253 | EF-hand 4 | ||||
Sequence: LSPQFTQLLVSRYCPRSANPAMQLDRFIQVCTQLQVL | ||||||
Domain | 254-283 | EF-hand 5 | ||||
Sequence: TEAFREKDTAVQGNIRLSFEDFVTMTASRM |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length284
- Mass (Da)30,381
- Last updated2000-05-01 v1
- Checksum2E9AA5750CB7A68A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 47-64 | Pro residues | ||||
Sequence: GGPAPGGPYGPPAGGGPY |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB026628 EMBL· GenBank· DDBJ | BAA85163.1 EMBL· GenBank· DDBJ | mRNA | ||
AB018357 EMBL· GenBank· DDBJ | BAA84922.1 EMBL· GenBank· DDBJ | mRNA | ||
AY359011 EMBL· GenBank· DDBJ | AAQ89370.1 EMBL· GenBank· DDBJ | mRNA | ||
AK001420 EMBL· GenBank· DDBJ | BAA91680.1 EMBL· GenBank· DDBJ | mRNA | ||
CR542139 EMBL· GenBank· DDBJ | CAG46936.1 EMBL· GenBank· DDBJ | mRNA | ||
BC002773 EMBL· GenBank· DDBJ | AAH02773.1 EMBL· GenBank· DDBJ | mRNA | ||
BC012561 EMBL· GenBank· DDBJ | AAH12561.1 EMBL· GenBank· DDBJ | mRNA |