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Overview

Uniprot IDA0A286XJ44
Protein NameAP-2 complex subunit alpha
Gene NameAP2A1
OrganismCavia porcellus

Kla Sites from experimental identification

Position Flanking peptide
177 LCLLRLYKASPDLVP

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 NLLSSNKYTE 100 KQIGYLFISV 110 LVNSNSELIR 120 LINNAIKNDL 130 ASRNPTSMCL 140 ALHCIANVGS 150 REMGEAFAAD 160 IPRILVAGDS 170 MDSVKQSAAL 180 CLLRLYKASP 190 DLVPMGEWTA 200 RVVHLLNDQH 210 MGVVTAAVSL 220 ITCLCKKNPD 230 DFKTCISLAV 240 SRLSRIVSSA 250 STDLQDYTYY 260 FVPAPWLSVK 270 LLRLLQCYPP 280 PEDAAVKGRL 290 VECLETVLNK 300 AQEPPKSKKV 310 QHSNAKNAIL 320 FETISLIIHY 330 DSEPNLLVRA 340 CNQLGQFLQH 350 RETNLRYLAL 360 ESMCTLASSE 370 FSHEAVKTHI 380 DTVINALKTE 390 RDVSVRQRAA 400 DLLYAMCDRS 410 NAKQIVSEML 420 RYLETADYAI 430 REEIVLKVAI 440 LAEKYAVDYS 450 WYVDTILNLI 460 RIAGDYVSEE 470 VWYRVLQIVT 480 NRDDVQGYAA 490 KTVFEALQAP 500 ACHENMVKVG 510 GYILGEFGNL 520 IAGDPRSSPP 530 VQFSLLHSKF 540 HLCSVATRAL 550 LLSTYIKFIN 560 LFPETKATIQ 570 GVLRAGSQLR 580 NADVELQQRA 590 VEYLTLSSVA 600 STDVLATVLE 610 EMPPFPERES 620 SILAKLKRKK 630 GPGAASGLDD 640 GRRDASNNDI 650 NGGVEPTAST 660 LSTPSPSADL 670 LGLRAAPPPA 680 TAPAPASAGN 690 LLVDVFSDSP 700 AAQPSLGPTP 710 EEAFLSPGPE 720 DIGPPIPEAD 730 ELLNKFVCKN 740 NGVLFENQLL 750 QIGVKSEFRQ 760 NLGRMYLFYG 770 NKTSMQFQNF 780 APTVVHPGDL 790 QTQLAVQTKR 800 VATQVDGGAQ 810 VQQVLNIECL 820 RDFLTPPLLL 830 VRFRYGGAPQ 840 SLTLKLPVTI 850 NKFFQPTEMA 860 AQDFFQRWKQ 870 LSLPLQEAQK 880 IFKANHPMDA 890 EVTKAKLLGF 900 GSALLDNVDP 910 NPENFVGAGI 920 IQTKALQVGC 930 LLRLEPNAQA 940 QMYRLTLRTS 950 KEPVSRHLCE LLAQQF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0030122 AP-2 adaptor complex
Molecular Function GO:0035615 clathrin adaptor activity
Molecular Function GO:0019901 protein kinase binding
Biological Process GO:0072583 clathrin-dependent endocytosis
Biological Process GO:0006886 intracellular protein transport

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.