Overview
| Uniprot ID | O94973 |
| Protein Name | AP-2 complex subunit alpha-2 |
| Gene Name | AP2A2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 6 |
**MPAVSKGDGMRGL |
| 619 |
LAKLKKKKGPSTVTD |
Function
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. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497). 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)
Protein Sequence
10
MPAVSKGDGM
20
RGLAVFISDI
30
RNCKSKEAEI
40
KRINKELANI
50
RSKFKGDKAL
60
DGYSKKKYVC
70
KLLFIFLLGH
80
DIDFGHMEAV
90
NLLSSNRYTE
100
KQIGYLFISV
110
LVNSNSELIR
120
LINNAIKNDL
130
ASRNPTFMGL
140
ALHCIASVGS
150
REMAEAFAGE
160
IPKVLVAGDT
170
MDSVKQSAAL
180
CLLRLYRTSP
190
DLVPMGDWTS
200
RVVHLLNDQH
210
LGVVTAATSL
220
ITTLAQKNPE
230
EFKTSVSLAV
240
SRLSRIVTSA
250
STDLQDYTYY
260
FVPAPWLSVK
270
LLRLLQCYPP
280
PDPAVRGRLT
290
ECLETILNKA
300
QEPPKSKKVQ
310
HSNAKNAVLF
320
EAISLIIHHD
330
SEPNLLVRAC
340
NQLGQFLQHR
350
ETNLRYLALE
360
SMCTLASSEF
370
SHEAVKTHIE
380
TVINALKTER
390
DVSVRQRAVD
400
LLYAMCDRSN
410
APQIVAEMLS
420
YLETADYSIR
430
EEIVLKVAIL
440
AEKYAVDYTW
450
YVDTILNLIR
460
IAGDYVSEEV
470
WYRVIQIVIN
480
RDDVQGYAAK
490
TVFEALQAPA
500
CHENLVKVGG
510
YILGEFGNLI
520
AGDPRSSPLI
530
QFHLLHSKFH
540
LCSVPTRALL
550
LSTYIKFVNL
560
FPEVKPTIQD
570
VLRSDSQLRN
580
ADVELQQRAV
590
EYLRLSTVAS
600
TDILATVLEE
610
MPPFPERESS
620
ILAKLKKKKG
630
PSTVTDLEDT
640
KRDRSVDVNG
650
GPEPAPASTS
660
AVSTPSPSAD
670
LLGLGAAPPA
680
PAGPPPSSGG
690
SGLLVDVFSD
700
SASVVAPLAP
710
GSEDNFARFV
720
CKNNGVLFEN
730
QLLQIGLKSE
740
FRQNLGRMFI
750
FYGNKTSTQF
760
LNFTPTLICS
770
DDLQPNLNLQ
780
TKPVDPTVEG
790
GAQVQQVVNI
800
ECVSDFTEAP
810
VLNIQFRYGG
820
TFQNVSVQLP
830
ITLNKFFQPT
840
EMASQDFFQR
850
WKQLSNPQQE
860
VQNIFKAKHP
870
MDTEVTKAKI
880
IGFGSALLEE
890
VDPNPANFVG
900
AGIIHTKTTQ
910
IGCLLRLEPN
920
LQAQMYRLTL
930
RTSKEAVSQR
LCELLSAQF
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0030122 |
AP-2 adaptor complex |
| Cellular Component |
GO:0045334 |
clathrin-coated endocytic vesicle |
| Cellular Component |
GO:0030669 |
clathrin-coated endocytic vesicle membrane |
| Cellular Component |
GO:0009898 |
cytoplasmic side of plasma membrane |
| Cellular Component |
GO:0031410 |
cytoplasmic vesicle |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0030666 |
endocytic vesicle membrane |
| Cellular Component |
GO:0036020 |
endolysosome membrane |
| Cellular Component |
GO:0101003 |
ficolin-1-rich granule membrane |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Cellular Component |
GO:0098794 |
postsynapse |
| Cellular Component |
GO:0098793 |
presynapse |
| Cellular Component |
GO:0030667 |
secretory granule membrane |
| Molecular Function |
GO:0035615 |
clathrin adaptor activity |
| Molecular Function |
GO:0097718 |
disordered domain specific binding |
| Molecular Function |
GO:0008289 |
lipid binding |
| Molecular Function |
GO:0019901 |
protein kinase binding |
| Biological Process |
GO:0072583 |
clathrin-dependent endocytosis |
| Biological Process |
GO:0006886 |
intracellular protein transport |
| Biological Process |
GO:0098884 |
postsynaptic neurotransmitter receptor internalization |
| Biological Process |
GO:0048488 |
synaptic vesicle endocytosis |
| Biological Process |
GO:0016192 |
vesicle-mediated transport |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.