Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor superfamily

SCOP classification

• Root: SCOP hierarchy in SUPERFAMILY [ 0] (11)
• Class: All beta proteins [ 48724] (165)
• Fold: Common fold of diphtheria toxin/transcription factors/cytochrome f [ 49379] (10)
  • sandwich; 9 strands in 2 sheet; greek-key; subclass of immunoglobin-like fold
• Superfamily: Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor [ 49447]
• Families: Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor [ 49448]

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Superfamily statistics

	Genomes (264)	UniProt 15.0	PDB chains (SCOP 1.73)
Domains	1,825	883	7
Proteins	1,825	883	7

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Functional annotation

• General category: Processes_IC
• Detailed category: Transport

Function annotation of SCOP domain superfamilies

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InterPro annotation

• Cross references: IPR008968 SSF49447 Protein matches
• Abstract:

  This entry represents the C-terminal domain of the mu subunit from various clathrin adaptors (AP1, AP2 and AP3) [11583591]. The C-teminal domain has an immunoglobulin-like beta-sandwich fold consisting of 9 strands in 2 sheets with a Greek key topology, similar to that found in cytochrome f and certain transcription factors [11583591]. The mu subunit regulates the coupling of clathrin lattices with particular membrane proteins by self-phosphorylation via a mechanism that is still unclear [1761056]. The mu subunit possesses a highly conserved N-terminal domain of around 230 amino acids, which may be the region of interaction with other AP proteins; a linker region of between 10 and 42 amino acids; and a less well-conserved C-terminal domain of around 190 amino acids, which may be the site of specific interaction with the protein being transported in the vesicle [1761056].

  More information about these proteins can be found at Protein of the Month: Clathrin.

InterPro database

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