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Protein

AP-2 complex subunit alpha-2

Gene

Ap2a2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei43Phosphatidylinositol lipid headgroup1
Binding sitei53Phosphatidylinositol lipid headgroup1
Binding sitei57Phosphatidylinositol lipid headgroup1
Binding sitei58Phosphatidylinositol lipid headgroup1
Binding sitei61Phosphatidylinositol lipid headgroup1

GO - Molecular functioni

GO - Biological processi

  • clathrin-dependent endocytosis Source: InterPro
  • intracellular protein transport Source: MGI
  • regulation of hematopoietic stem cell differentiation Source: BHF-UCL
  • vesicle-mediated transport Source: MGI

Keywordsi

Biological processEndocytosis, Protein transport, Transport
LigandLipid-binding

Enzyme and pathway databases

ReactomeiR-MMU-177504 Retrograde neurotrophin signalling
R-MMU-2132295 MHC class II antigen presentation
R-MMU-416993 Trafficking of GluR2-containing AMPA receptors
R-MMU-437239 Recycling pathway of L1
R-MMU-5099900 WNT5A-dependent internalization of FZD4
R-MMU-5140745 WNT5A-dependent internalization of FZD2, FZD5 and ROR2
R-MMU-6798695 Neutrophil degranulation
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis
R-MMU-8866427 VLDLR internalisation and degradation
R-MMU-8964038 LDL clearance

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:101920 Ap2a2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Coated pit, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi21R → E: Reduces interaction with CD4 endocytosis signal motif; when associated with AP2S1 S-15. 1 Publication1
Mutagenesisi31K → Q: Reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi32R → Q: Reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi35K → Q: Reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi45K → Q: Reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi55K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-56 and Q-57. 1 Publication1
Mutagenesisi56K → E: Strongly reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi56K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-57. 1 Publication1
Mutagenesisi57K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-56. 1 Publication1
Mutagenesisi61K → Q: Reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi727K → A: No effect on DENND1A-,DENND1B- nor DENND1C-binding. 1
Mutagenesisi782Q → A: Reduces DENND1A- and DENND1C-binding. 1 Publication1
Mutagenesisi837F → A: Reduces SNAP91, AMPH and BIN1 binding. Abolishes AMPH and SNAP91 binding; when associated with A-916. Abolishes EPN1 and EPS15 binding; when associated with A-905. 2 Publications1
Mutagenesisi840W → A: Abolishes AMPH, BIN1, EPS15, EPN1, auxilin and SNAP91 binding. Abolishes interaction with DGKD. 2 Publications1
Mutagenesisi849E → A: No effect. 1 Publication1
Mutagenesisi905R → A: Strongly reduces AMPH, SNAP91, auxilin and BIN1 binding. Abolishes EPN1 and EPS15 binding; when associated with A-837. 2 Publications1
Mutagenesisi907E → A: Strongly reduces AMPH, SNAP91 and BIN1 binding. Slightly reduces EPS15 and auxilin binding. 1 Publication1
Mutagenesisi916R → A: Strongly reduces AMPH and SNAP91 binding. Abolishes DENND1B-binding; no effect on DENND1A-, nor DENND1C-binding. Abolishes AMPH and SNAP91 binding; when associated with A-837. 2 Publications1
Mutagenesisi920R → A: Abolishes AMPH and BIN1 binding. Reduces EPS15, SNAP91 and auxilin binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001937331 – 938AP-2 complex subunit alpha-2Add BLAST938

Proteomic databases

EPDiP17427
MaxQBiP17427
PaxDbiP17427
PeptideAtlasiP17427
PRIDEiP17427

PTM databases

iPTMnetiP17427
PhosphoSitePlusiP17427
SwissPalmiP17427

Miscellaneous databases

PMAP-CutDBiP17427

Expressioni

Gene expression databases

BgeeiENSMUSG00000002957 Expressed in 295 organ(s), highest expression level in embryo
CleanExiMM_AP2A2
ExpressionAtlasiP17427 baseline and differential
GenevisibleiP17427 MM

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 (By similarity). Interacts with DGKD isoform 2. Interacts with DENND1A, DENND1B and DENND1C. Interacts with FCHO1 and DAB2. Interacts with ATAT1; this interaction is required for efficient alpha-tubulin acetylation by ATAT1. Interacts with KIAA1107 (PubMed:29262337).By similarity12 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198130, 17 interactors
CORUMiP17427
DIPiDIP-32160N
IntActiP17427, 24 interactors
MINTiP17427
STRINGi10090.ENSMUSP00000003038

Structurei

Secondary structure

1938
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP17427
SMRiP17427
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17427

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1077 Eukaryota
ENOG410XNQE LUCA
GeneTreeiENSGT00550000074757
HOVERGENiHBG050518
InParanoidiP17427
KOiK11824
OMAiFMNLALH
OrthoDBiEOG091G01JZ
TreeFamiTF300308

Family and domain databases

Gene3Di1.25.10.10, 1 hit
3.30.310.10, 1 hit
InterProiView protein in InterPro
IPR017104 AP2_complex_asu
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR002553 Clathrin/coatomer_adapt-like_N
IPR003164 Clathrin_a-adaptin_app_sub_C
IPR008152 Clathrin_a/b/g-adaptin_app_Ig
IPR013041 Clathrin_app_Ig-like_sf
IPR009028 Coatomer/calthrin_app_sub_C
IPR012295 TBP_dom_sf
PfamiView protein in Pfam
PF01602 Adaptin_N, 1 hit
PF02296 Alpha_adaptin_C, 1 hit
PF02883 Alpha_adaptinC2, 1 hit
PIRSFiPIRSF037091 AP2_complex_alpha, 1 hit
SMARTiView protein in SMART
SM00809 Alpha_adaptinC2, 1 hit
SUPFAMiSSF48371 SSF48371, 1 hit
SSF49348 SSF49348, 1 hit
SSF55711 SSF55711, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P17427-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPAVSKGDGM 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 AQVQQVVNIE 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):104,017
Last modified:July 27, 2011 - v2
Checksum:i183FE8DFE199DBCA
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0J9YUA7A0A0J9YUA7_MOUSE
AP-2 complex subunit alpha-2
Ap2a2
131Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti858 – 859HP → LE in AAH10597 (PubMed:15489334).Curated2
Sequence conflicti889 – 890GA → VL in CAA33097 (PubMed:2564002).Curated2
Sequence conflicti889 – 890GA → VL in AAB62703 (PubMed:9618202).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14972 mRNA Translation: CAA33097.1
AK088500 mRNA Translation: BAC40392.1
AC158224 Genomic DNA No translation available.
AC102524 Genomic DNA No translation available.
BC010597 mRNA Translation: AAH10597.1
AF006990 mRNA Translation: AAB62703.1
CCDSiCCDS40188.1
PIRiB30111
S12471
RefSeqiNP_031485.3, NM_007459.3
UniGeneiMm.253090

Genome annotation databases

EnsembliENSMUST00000003038; ENSMUSP00000003038; ENSMUSG00000002957
GeneIDi11772
KEGGimmu:11772
UCSCiuc009kls.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14972 mRNA Translation: CAA33097.1
AK088500 mRNA Translation: BAC40392.1
AC158224 Genomic DNA No translation available.
AC102524 Genomic DNA No translation available.
BC010597 mRNA Translation: AAH10597.1
AF006990 mRNA Translation: AAB62703.1
CCDSiCCDS40188.1
PIRiB30111
S12471
RefSeqiNP_031485.3, NM_007459.3
UniGeneiMm.253090

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B9KX-ray1.90A701-938[»]
1KY6X-ray2.00A701-938[»]
1KY7X-ray2.15A701-938[»]
1KYDX-ray2.00A701-938[»]
1KYFX-ray1.22A701-938[»]
1KYUX-ray1.80A701-938[»]
1QTPX-ray1.60A701-938[»]
1QTSX-ray1.40A701-938[»]
1W80X-ray1.90A695-938[»]
2JKRX-ray2.98A/L1-620[»]
2JKTX-ray3.40A/L1-620[»]
2VJ0X-ray1.60A695-938[»]
3HS8X-ray1.90A702-938[»]
ProteinModelPortaliP17427
SMRiP17427
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198130, 17 interactors
CORUMiP17427
DIPiDIP-32160N
IntActiP17427, 24 interactors
MINTiP17427
STRINGi10090.ENSMUSP00000003038

PTM databases

iPTMnetiP17427
PhosphoSitePlusiP17427
SwissPalmiP17427

Proteomic databases

EPDiP17427
MaxQBiP17427
PaxDbiP17427
PeptideAtlasiP17427
PRIDEiP17427

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003038; ENSMUSP00000003038; ENSMUSG00000002957
GeneIDi11772
KEGGimmu:11772
UCSCiuc009kls.2 mouse

Organism-specific databases

CTDi161
MGIiMGI:101920 Ap2a2

Phylogenomic databases

eggNOGiKOG1077 Eukaryota
ENOG410XNQE LUCA
GeneTreeiENSGT00550000074757
HOVERGENiHBG050518
InParanoidiP17427
KOiK11824
OMAiFMNLALH
OrthoDBiEOG091G01JZ
TreeFamiTF300308

Enzyme and pathway databases

ReactomeiR-MMU-177504 Retrograde neurotrophin signalling
R-MMU-2132295 MHC class II antigen presentation
R-MMU-416993 Trafficking of GluR2-containing AMPA receptors
R-MMU-437239 Recycling pathway of L1
R-MMU-5099900 WNT5A-dependent internalization of FZD4
R-MMU-5140745 WNT5A-dependent internalization of FZD2, FZD5 and ROR2
R-MMU-6798695 Neutrophil degranulation
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis
R-MMU-8866427 VLDLR internalisation and degradation
R-MMU-8964038 LDL clearance

Miscellaneous databases

ChiTaRSiAp2a2 mouse
EvolutionaryTraceiP17427
PMAP-CutDBiP17427
PROiPR:P17427
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000002957 Expressed in 295 organ(s), highest expression level in embryo
CleanExiMM_AP2A2
ExpressionAtlasiP17427 baseline and differential
GenevisibleiP17427 MM

Family and domain databases

Gene3Di1.25.10.10, 1 hit
3.30.310.10, 1 hit
InterProiView protein in InterPro
IPR017104 AP2_complex_asu
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR002553 Clathrin/coatomer_adapt-like_N
IPR003164 Clathrin_a-adaptin_app_sub_C
IPR008152 Clathrin_a/b/g-adaptin_app_Ig
IPR013041 Clathrin_app_Ig-like_sf
IPR009028 Coatomer/calthrin_app_sub_C
IPR012295 TBP_dom_sf
PfamiView protein in Pfam
PF01602 Adaptin_N, 1 hit
PF02296 Alpha_adaptin_C, 1 hit
PF02883 Alpha_adaptinC2, 1 hit
PIRSFiPIRSF037091 AP2_complex_alpha, 1 hit
SMARTiView protein in SMART
SM00809 Alpha_adaptinC2, 1 hit
SUPFAMiSSF48371 SSF48371, 1 hit
SSF49348 SSF49348, 1 hit
SSF55711 SSF55711, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiAP2A2_MOUSE
AccessioniPrimary (citable) accession number: P17427
Secondary accession number(s): Q8C2J5, Q921V0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: July 27, 2011
Last modified: September 12, 2018
This is version 187 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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