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IID50124
UniprotP62743
ProteinAP-2 complex subunit sigma
GeneAp2s1
OrganismMus musculus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
142
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-142 Hetero pentamer : IID50129Complex,P63010
 Evidence X-RAY 2xa7 S Reference
       Region 2xa7 S 1-142 order
Seq 1-142 Hetero tetramer : IID50129Complex,P63010
 Evidence X-RAY 2xa7 S Reference
       Region 2xa7 S 1-142 order
Seq 1-142 Hetero pentamer : IID50122Complex,P01730,P17427
 Evidence X-RAY 2jkt I Reference
       Region 2jkt I 1-142 order
 Evidence X-RAY 2jkt S Reference
       Region 2jkt S 1-142 order
 Evidence X-RAY 2jkr I Reference
       Region 2jkr I 1-142 order
 Evidence X-RAY 2jkr S Reference
       Region 2jkr S 1-142 order
Seq 1-142 Hetero tetramer : IID50122Complex,IID50129Complex,P63010
 Evidence X-RAY 2vgl S Reference
       Region 2vgl S 1-142 order
 Evidence X-RAY 4uqi S Reference
       Region 4uqi S 1-142 order
Seqphosphorylation
    140-140 Phosphoserine
 
Prediction
NeProc
Order 1-142
AlphaFold
Order 1-142
Pfam Hmmer
PF01217 1-142 7.4e-97
Function
Function in SwissProt
Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via Transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif. May also play a role in extracellular calcium homeostasis (By similarity).