CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004683
UniProt Accession
Genbank Protein ID
 X53773 
Genbank Nucleotide ID
Protein Name
 AP-2 complex subunit alpha-2 
Protein Synonyms/Alias
 100 kDa coated vesicle protein C; Adapter-related protein complex 2 alpha-2 subunit; Adaptor protein complex AP-2 subunit alpha-2; Alpha-adaptin C; Alpha2-adaptin; Clathrin assembly protein complex 2 alpha-C large chain; Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit 
Gene Name
 Ap2a2 
Gene Synonyms/Alias
 Adtab 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
855QEVQNIFKAKHPMDTubiquitination[1]
Reference
 [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113
Functional Description
 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 subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C- terminal appendage domain as a scaffolding platform for endocytic accessory proteins. 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 (By similarity). 
Sequence Annotation
 REGION 5 80 Lipid-binding.
 BINDING 43 43 Phosphatidylinositol lipid headgroup (By
 BINDING 53 53 Phosphatidylinositol lipid headgroup (By
 BINDING 57 57 Phosphatidylinositol lipid headgroup (By
 BINDING 58 58 Phosphatidylinositol lipid headgroup (By
 BINDING 61 61 Phosphatidylinositol lipid headgroup (By
 MOD_RES 807 807 Phosphotyrosine (By similarity).  
Keyword
 3D-structure; Cell membrane; Coated pit; Complete proteome; Direct protein sequencing; Endocytosis; Lipid-binding; Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 938 AA 
Protein Sequence
MPAVSKGEGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC 60
KLLFIFLLGH DIDFGHMEAV NLLSSNRYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL 120
ASRNPTFMGL ALHCIANVGS REMAEAFAGE IPKILVAGDT MDSVKQSAAL CLLRLYRTSP 180
DLVPMGDWTS RVVHLLNDQH LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA 240
STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PDPAVRGRLT ECLETILNKA QEPPKSKKVQ 300
HSNAKNAVLF EAISLIIHHD SEPNLLVRAC NQLGQFLQHR ETNLRYLALE SMCTLASSEF 360
SHEAVKTHIE TVINALKTER DVSVRQRAVD LLYAMCDRSN AQQIVAEMLS YLETADYSIR 420
EEIVLKVAIL AEKYAVDYTW YVDTILNLIR IAGDYVSEEV WYRVIQIVIN RDDVQGYAAK 480
TVFEALQAPA CHENLVKVGG YILGEFGNLI AGDPRSSPLI QFNLLHSKFH LCSVPTRALL 540
LSTYIKFVNL FPEVKATIQD VLRSDSQLKN ADVELQQRAV EYLRLSTVAS TDILATVLEE 600
MPPFPERESS ILAKLKKKKG PSTVTDLEET KRERSIDVNG GPEPVPASTS AASTPSPSAD 660
LLGLGAVPPA PTGPPPSSGG GLLVDVFSDS ASAVAPLAPG SEDNFARFVC KNNGVLFENQ 720
LLQIGLKSEF RQNLGRMFIF YGNKTSTQFL NFTPTLICAD DLQTNLNLQT KPVDPTVDGG 780
AQVQQVINIE CISDFTEAPV LNIQFRYGGT FQNVSVKLPI TLNKFFQPTE MASQDFFQRW 840
KQLSNPQQEV QNIFKAKHPM DTEITKAKII GFGSALLEEV DPNPANFVGA GIIHTKTTQI 900
GCLLRLEPNL QAQMYRLTLR TSKDTVSQRL CELLSEQF 938 
Gene Ontology
 GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
 GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
 GO:0008565; F:protein transporter activity; IEA:InterPro.
 GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
 GO:0006886; P:intracellular protein transport; IEA:InterPro. 
Interpro
 IPR017104; AP2_complex_asu.
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR002553; Clathrin/coatomer_adapt-like_N.
 IPR013038; Clathrin_a-adaptin_app_Ig-like.
 IPR003164; Clathrin_a-adaptin_app_sub_C.
 IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
 IPR015873; Clathrin_a/coatomer_app_sub_C.
 IPR009028; Coatomer/calthrin_app_sub_C.
 IPR013041; Coatomer/clathrin_app_Ig-like. 
Pfam
 PF01602; Adaptin_N
 PF02296; Alpha_adaptin_C
 PF02883; Alpha_adaptinC2 
SMART
 SM00809; Alpha_adaptinC2 
PROSITE
  
PRINTS