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P17426 (AP2A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AP-2 complex subunit alpha-1
Alternative name(s):
100 kDa coated vesicle protein A
Adapter-related protein complex 2 subunit alpha-1
Adaptor protein complex AP-2 subunit alpha-1
Alpha-adaptin A
Alpha1-adaptin
Clathrin assembly protein complex 2 alpha-A large chain
Plasma membrane adaptor HA2/AP2 adaptin alpha A subunit
Gene names
Name:Ap2a1
Synonyms:Adtaa, Clapa1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length977 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity. Ref.5 Ref.6

Subunit structure

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). Interacts with HIP1 and RAB11FIP2 By similarity. Interacts with SLC12A5. Interacts with clathrin. Interacts with SLC12A5. Interacts with clathrin. Interacts with SGIP1. Ref.3 Ref.7 Ref.9

Subcellular location

Cell membrane By similarity. Membranecoated pit; Peripheral membrane protein; 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.

Tissue specificity

Isoform A is expressed only in neuronal tissue and skeletal muscle. Isoform B is widely expressed.

Sequence similarities

Belongs to the adaptor complexes large subunit family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Grin2bQ010972EBI-775189,EBI-400125

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P17426-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: P17426-2)

The sequence of this isoform differs from the canonical sequence as follows:
     706-727: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 977977AP-2 complex subunit alpha-1
PRO_0000193731

Amino acid modifications

Modified residue6261Phosphoserine By similarity
Modified residue6521Phosphoserine By similarity
Modified residue6531Phosphothreonine By similarity
Modified residue6551Phosphoserine By similarity

Natural variations

Alternative sequence706 – 72722Missing in isoform B.
VSP_000162

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: F4ED87D3F9EF230A

FASTA977107,664
        10         20         30         40         50         60 
MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC 

        70         80         90        100        110        120 
KLLFIFLLGH DIDFGHMEAV NLLSSNKYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL 

       130        140        150        160        170        180 
ASRNPTFMCL ALHCIANVGS REMGEAFAAD IPRILVAGDS MDSVKQSAAL CLLRLYKASP 

       190        200        210        220        230        240 
DLVPMGEWTA RVVHLLNDQH MGVVTAAVSL ITCLCKKNPD DFKTCISLAV SRLSRIVSSA 

       250        260        270        280        290        300 
STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PEDAAVKGRL VECLETVLNK AQEPPKSKKV 

       310        320        330        340        350        360 
QHSNAKNAIL FETISLIIHY DSEPNLLVRA CNQLGQFLQH RETNLRYLAL ESMCTLASSE 

       370        380        390        400        410        420 
FSHEAVKTHI DTVINALKTE RDVSVRQRAA DLLYAMCDRS NAKQIVSEML RYLETADYAI 

       430        440        450        460        470        480 
REEIVLKVAI LAEKYAVDYS WYVDTILNLI RIAGDYVSEE VWYRVLQIVT NRDDVQGYAA 

       490        500        510        520        530        540 
KTVFEALQAP ACHENMVKVG GYILGEFGNL IAGDPRSSPP VQFSLLHSKF HLCSVATRAL 

       550        560        570        580        590        600 
LLSTYIKFIN LFPETKATIQ GVLRAGSQLR NADVELQQRA VEYLTLSSVA STDVLATVLE 

       610        620        630        640        650        660 
EMPPFPERES SILAKLKRKK GPGAASALDD SRRDTSSNDI NGGVEPTPST VSTPSPSADL 

       670        680        690        700        710        720 
LGLRAAPPPA APPAPVGGNL LVDVFSDGPT AQPSLGPTPE EAFLSELEPP APESPMALLA 

       730        740        750        760        770        780 
DPAPAADPGP EDIGPPIPEA DELLNKFVCK NSGVLFENQL LQIGVKSEFR QNLGRMYLFY 

       790        800        810        820        830        840 
GNKTSVQFQN FLPTVVHPGD LQTQLAVQTK RVAAQVDGGA QVQQVLNIEC LRDFLTPPLL 

       850        860        870        880        890        900 
SVRFRYGGTA QSLTLKLPVT INKFFQPTEM AAQDFFQRWK QLSLPLQEAQ KIFKANHPMD 

       910        920        930        940        950        960 
AEVTKAKLLG FGSALLDNVD PNPENFVGAG IIQTKALQVG CLLRLEPNAQ AQMYRLTLRT 

       970 
SKEPVSRHLC ELLAQQF 

« Hide

Isoform B [UniParc].

Checksum: D6EB4672359D66B9
Show »

FASTA955105,480

References

« Hide 'large scale' references
[1]"Cloning of cDNAs encoding two related 100-kD coated vesicle proteins (alpha-adaptins)."
Robinson M.S.
J. Cell Biol. 108:833-842(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Tissue: Retina.
[3]"The alpha chain of the AP-2 adaptor is a clathrin binding subunit."
Goodman O.B. Jr., Keen J.H.
J. Biol. Chem. 270:23768-23773(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLATHRIN.
[4]"Expression and localization of alpha-adaptin isoforms."
Ball C.L., Hunt S.P., Robinson M.S.
J. Cell Sci. 108:2865-2875(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF ISOFORMS A AND B.
[5]"Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network."
Nakatsu F., Ohno H.
Cell Struct. Funct. 28:419-429(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[6]"Adaptors for clathrin coats: structure and function."
Owen D.J., Collins B.M., Evans P.R.
Annu. Rev. Cell Dev. Biol. 20:153-191(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[7]"SGIP1alpha is an endocytic protein that directly interacts with phospholipids and Eps15."
Uezu A., Horiuchi A., Kanda K., Kikuchi N., Umeda K., Tsujita K., Suetsugu S., Araki N., Yamamoto H., Takenawa T., Nakanishi H.
J. Biol. Chem. 282:26481-26489(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SGIP1.
[8]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"Identification of a novel di-leucine motif mediating K(+)/Cl(-) cotransporter KCC2 constitutive endocytosis."
Zhao B., Wong A.Y.C., Murshid A., Bowie D., Presley J.F., Bedford F.K.
Cell. Signal. 20:1769-1779(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLC12A5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14971 mRNA. Translation: CAA33096.1.
BC031433 mRNA. Translation: AAH31433.1.
CCDSCCDS52238.1. [P17426-2]
CCDS52239.1. [P17426-1]
PIRA30111.
RefSeqNP_001070732.1. NM_001077264.1. [P17426-2]
NP_031484.1. NM_007458.2. [P17426-1]
UniGeneMm.6877.

3D structure databases

ProteinModelPortalP17426.
SMRP17426. Positions 3-621, 746-977.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198129. 5 interactions.
IntActP17426. 12 interactions.
MINTMINT-1865011.
STRING10090.ENSMUSP00000082519.

PTM databases

PhosphoSiteP17426.

Proteomic databases

MaxQBP17426.
PaxDbP17426.
PRIDEP17426.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000085399; ENSMUSP00000082519; ENSMUSG00000060279. [P17426-1]
ENSMUST00000107857; ENSMUSP00000103489; ENSMUSG00000060279. [P17426-2]
ENSMUST00000166972; ENSMUSP00000127842; ENSMUSG00000060279. [P17426-1]
ENSMUST00000167930; ENSMUSP00000127497; ENSMUSG00000060279. [P17426-2]
GeneID11771.
KEGGmmu:11771.
UCSCuc009grv.1. mouse. [P17426-1]
uc009grw.1. mouse. [P17426-2]

Organism-specific databases

CTD160.
MGIMGI:101921. Ap2a1.

Phylogenomic databases

eggNOGNOG303101.
GeneTreeENSGT00550000074757.
HOGENOMHOG000170596.
HOVERGENHBG050518.
InParanoidP17426.
KOK11824.
OMANYVGAGI.
OrthoDBEOG7GQXV2.
PhylomeDBP17426.
TreeFamTF300308.

Gene expression databases

ArrayExpressP17426.
BgeeP17426.
CleanExMM_AP2A1.
GenevestigatorP17426.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
2.60.40.1030. 1 hit.
3.30.310.30. 1 hit.
InterProIPR017104. 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]
PfamPF01602. Adaptin_N. 1 hit.
PF02296. Alpha_adaptin_C. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
[Graphical view]
PIRSFPIRSF037091. AP2_complex_alpha. 1 hit.
SMARTSM00809. Alpha_adaptinC2. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.
ProtoNetSearch...

Other

ChiTaRSAP2A1. mouse.
NextBio279549.
PMAP-CutDBP17426.
PROP17426.
SOURCESearch...

Entry information

Entry nameAP2A1_MOUSE
AccessionPrimary (citable) accession number: P17426
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: July 9, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot