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Overview

Uniprot IDH0VIB5
Protein NameAP-2 complex subunit alpha
Gene NameAP2A2
OrganismCavia porcellus

Kla Sites from experimental identification

Position Flanking peptide
48 RSKFKGDKALDGYSK
6 **MPAVSKGDGMRGL

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. 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

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 ALHCIANVGS 150 REMAEAFAGE 160 IPKILVAGDT 170 MDSVKQSAAL 180 CLLRLYRASP 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 SHEAVKTHID 380 TVINALKTER 390 DVSVRQRAVD 400 LLYAMCDRSN 410 AQQIVAEMLS 420 YLETADYSIR 430 EEIVLKVAIL 440 AEKYAVDYTW 450 YVDTILNLIR 460 IAGDYVSEEV 470 WYRVIQIVIN 480 RDDVQGYAAK 490 TVFEALQAPA 500 CHENLVKVGG 510 YILGEFGNLI 520 AGDPRSSPLI 530 QFNLLHSKFH 540 LCSVPTRALL 550 LSTYIKFVNL 560 FPEVKATIQD 570 VLRGDSQLRN 580 ADVELQQRAV 590 EYLRLSTVAS 600 TDILATVLEE 610 MPPFPERESS 620 ILAKLKKKKG 630 PSTVTDLEEA 640 KRERSVDVNG 650 GPEPAPASTS 660 AVSTPSPSAD 670 LLGLGAAPPA 680 PTGPPSSAGG 690 LLVDVFSDSA 700 SAIAPLAPGS 710 EDNFARFVCK 720 NNGVLFENQL 730 LQIGLKSEFR 740 QNLGRMFIFY 750 GNKTSTQFLN 760 FTPTLICADD 770 LQANLNLQTK 780 PVDPTVDGGA 790 QVQQVVNIEC 800 VSDFTEAPVL 810 NIQFRYGGTF 820 QNVSVKLPIT 830 LNKFFQPTEM 840 VSQDFFQRWK 850 QLSNPQQEVQ 860 NIFKAKHPMD 870 TEITKAKIIG 880 FGSALLEEVD 890 PNPANFVGAG 900 IIHTKTTQIG 910 CLLRLEPNLQ 920 AQMYRLTLRT 930 SKDTVSQRLC DLLSEQF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0030122 AP-2 adaptor complex
Cellular Component GO:0098793 presynapse
Molecular Function GO:0035615 clathrin adaptor activity
Molecular Function GO:0097718 disordered domain specific 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:0048488 synaptic vesicle endocytosis

Reference

[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.