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Protein

AP-2 complex subunit alpha-2

Gene

Ap2a2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei43Phosphatidylinositol lipid headgroupBy similarity1
Binding sitei53Phosphatidylinositol lipid headgroupBy similarity1
Binding sitei57Phosphatidylinositol lipid headgroupBy similarity1
Binding sitei58Phosphatidylinositol lipid headgroupBy similarity1
Binding sitei61Phosphatidylinositol lipid headgroupBy similarity1

GO - Molecular functioni

  • lipid binding Source: UniProtKB-KW
  • protein complex binding Source: RGD
  • protein transporter activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-RNO-177504. Retrograde neurotrophin signalling.

Names & Taxonomyi

Protein namesi
Recommended name:
AP-2 complex subunit alpha-2
Alternative name(s):
100 kDa coated vesicle protein C
Adaptor protein complex AP-2 subunit alpha-2
Adaptor-related protein complex 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 namesi
Name:Ap2a2
Synonyms:Adtab
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71015. Ap2a2.

Subcellular locationi

  • Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Membranecoated pit By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

  • Note: AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001937342 – 938AP-2 complex subunit alpha-2Add BLAST937

Proteomic databases

PaxDbiP18484.
PeptideAtlasiP18484.
PRIDEiP18484.

Expressioni

Tissue specificityi

Widely expressed.

Interactioni

Subunit structurei

Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1). Binds EPN1, EPS15, AMPH, SNAP91 and BIN1. Interacts with HIP1. Interacts with DGKD isoform 2 (By similarity). Interacts with DENND1A, DENND1B and DENND1C (By similarity). Interacts with FCHO1 and DAB2 (By similarity). Interacts with ATAT1; this interaction is required for efficient alpha-tubulin acetylation by ATAT1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Syt1P217075EBI-539360,EBI-458098

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

DIPiDIP-29765N.
IntActiP18484. 6 interactors.
MINTiMINT-93156.
STRINGi10116.ENSRNOP00000060992.

Structurei

Secondary structure

1938
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 22Combined sources12
Helixi26 – 45Combined sources20
Beta strandi46 – 48Combined sources3
Helixi52 – 68Combined sources17
Helixi76 – 81Combined sources6
Helixi82 – 84Combined sources3
Helixi88 – 100Combined sources13
Helixi106 – 121Combined sources16
Helixi125 – 138Combined sources14
Helixi141 – 147Combined sources7
Helixi150 – 156Combined sources7
Beta strandi158 – 160Combined sources3
Helixi162 – 178Combined sources17
Helixi180 – 182Combined sources3
Helixi189 – 195Combined sources7
Helixi201 – 217Combined sources17
Helixi219 – 222Combined sources4
Helixi225 – 238Combined sources14
Beta strandi241 – 243Combined sources3
Helixi245 – 247Combined sources3
Beta strandi252 – 254Combined sources3
Helixi255 – 264Combined sources10
Helixi265 – 267Combined sources3
Beta strandi268 – 270Combined sources3
Helixi273 – 291Combined sources19
Helixi299 – 319Combined sources21
Helixi323 – 336Combined sources14
Helixi342 – 355Combined sources14
Turni359 – 361Combined sources3
Helixi362 – 366Combined sources5
Helixi369 – 376Combined sources8
Helixi382 – 395Combined sources14
Helixi398 – 414Combined sources17
Helixi417 – 434Combined sources18
Helixi439 – 452Combined sources14
Helixi453 – 455Combined sources3
Helixi459 – 468Combined sources10
Helixi469 – 471Combined sources3
Helixi472 – 474Combined sources3
Helixi475 – 486Combined sources12
Beta strandi488 – 490Combined sources3
Helixi493 – 506Combined sources14
Helixi508 – 511Combined sources4
Helixi518 – 529Combined sources12
Helixi534 – 550Combined sources17
Helixi552 – 554Combined sources3
Helixi555 – 562Combined sources8
Helixi565 – 568Combined sources4
Helixi573 – 587Combined sources15
Turni592 – 597Combined sources6
Beta strandi598 – 600Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VGLX-ray2.59A1-620[»]
2XA7X-ray3.10A1-621[»]
4NEEX-ray2.88A/B/G/J1-395[»]
4UQIX-ray2.79A1-620[»]
ProteinModelPortaliP18484.
SMRiP18484.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18484.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni5 – 80Lipid-bindingAdd BLAST76

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1077. Eukaryota.
ENOG410XNQE. LUCA.
HOVERGENiHBG050518.
InParanoidiP18484.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.60.40.1030. 1 hit.
3.30.310.30. 1 hit.
InterProiIPR017104. 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.
[Graphical view]
PfamiPF01602. Adaptin_N. 1 hit.
PF02296. Alpha_adaptin_C. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
[Graphical view]
PIRSFiPIRSF037091. AP2_complex_alpha. 1 hit.
SMARTiSM00809. Alpha_adaptinC2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18484-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAVSKGEGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL
60 70 80 90 100
DGYSKKKYVC KLLFIFLLGH DIDFGHMEAV NLLSSNRYTE KQIGYLFISV
110 120 130 140 150
LVNSNSELIR LINNAIKNDL ASRNPTFMGL ALHCIANVGS REMAEAFAGE
160 170 180 190 200
IPKILVAGDT MDSVKQSAAL CLLRLYRTSP DLVPMGDWTS RVVHLLNDQH
210 220 230 240 250
LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA STDLQDYTYY
260 270 280 290 300
FVPAPWLSVK LLRLLQCYPP PDPAVRGRLT ECLETILNKA QEPPKSKKVQ
310 320 330 340 350
HSNAKNAVLF EAISLIIHHD SEPNLLVRAC NQLGQFLQHR ETNLRYLALE
360 370 380 390 400
SMCTLASSEF SHEAVKTHIE TVINALKTER DVSVRQRAVD LLYAMCDRSN
410 420 430 440 450
AQQIVAEMLS YLETADYSIR EEIVLKVAIL AEKYAVDYTW YVDTILNLIR
460 470 480 490 500
IAGDYVSEEV WYRVIQIVIN RDDVQGYAAK TVFEALQAPA CHENLVKVGG
510 520 530 540 550
YILGEFGNLI AGDPRSSPLI QFNLLHSKFH LCSVPTRALL LSTYIKFVNL
560 570 580 590 600
FPEVKATIQD VLRSDSQLKN ADVELQQRAV EYLRLSTVAS TDILATVLEE
610 620 630 640 650
MPPFPERESS ILAKLKKKKG PSTVTDLEET KRERSIDVNG GPEPVPASTS
660 670 680 690 700
AASTPSPSAD LLGLGAVPPA PTGPPPSSGG GLLVDVFSDS ASAVAPLAPG
710 720 730 740 750
SEDNFARFVC KNNGVLFENQ LLQIGLKSEF RQNLGRMFIF YGNKTSTQFL
760 770 780 790 800
NFTPTLICAD DLQTNLNLQT KPVDPTVDGG AQVQQVINIE CISDFTEAPV
810 820 830 840 850
LNIQFRYGGT FQNVSVKLPI TLNKFFQPTE MASQDFFQRW KQLSNPQQEV
860 870 880 890 900
QNIFKAKHPM DTEITKAKII GFGSALLEEV DPNPANFVGA GIIHTKTTQI
910 920 930
GCLLRLEPNL QAQMYRLTLR TSKDTVSQRL CELLSEQF
Length:938
Mass (Da):104,045
Last modified:January 23, 2007 - v3
Checksum:i406428A9BFFB1E53
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53773 mRNA. Translation: CAA37791.1.
PIRiS11276.
UniGeneiRn.34928.

Genome annotation databases

UCSCiRGD:71015. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53773 mRNA. Translation: CAA37791.1.
PIRiS11276.
UniGeneiRn.34928.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VGLX-ray2.59A1-620[»]
2XA7X-ray3.10A1-621[»]
4NEEX-ray2.88A/B/G/J1-395[»]
4UQIX-ray2.79A1-620[»]
ProteinModelPortaliP18484.
SMRiP18484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29765N.
IntActiP18484. 6 interactors.
MINTiMINT-93156.
STRINGi10116.ENSRNOP00000060992.

Proteomic databases

PaxDbiP18484.
PeptideAtlasiP18484.
PRIDEiP18484.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:71015. rat.

Organism-specific databases

RGDi71015. Ap2a2.

Phylogenomic databases

eggNOGiKOG1077. Eukaryota.
ENOG410XNQE. LUCA.
HOVERGENiHBG050518.
InParanoidiP18484.

Enzyme and pathway databases

ReactomeiR-RNO-177504. Retrograde neurotrophin signalling.

Miscellaneous databases

EvolutionaryTraceiP18484.
PROiP18484.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.60.40.1030. 1 hit.
3.30.310.30. 1 hit.
InterProiIPR017104. 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.
[Graphical view]
PfamiPF01602. Adaptin_N. 1 hit.
PF02296. Alpha_adaptin_C. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
[Graphical view]
PIRSFiPIRSF037091. AP2_complex_alpha. 1 hit.
SMARTiSM00809. Alpha_adaptinC2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAP2A2_RAT
AccessioniPrimary (citable) accession number: P18484
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.