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P62743 (AP2S1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AP-2 complex subunit sigma
Alternative name(s):
Adapter-related protein complex 2 subunit sigma
Adaptor protein complex AP-2 subunit sigma
Clathrin assembly protein 2 sigma small chain
Clathrin coat assembly protein AP17
Clathrin coat-associated protein AP17
Plasma membrane adaptor AP-2 17 kDa protein
Sigma-adaptin 3b
Sigma2-adaptin
Gene names
Name:Ap2s1
Synonyms:Ap17, Claps2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length142 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 and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif. May also play a role in extracellular calcium homeostasis By similarity. Ref.2 Ref.3

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).

Subcellular location

Cell membrane. Membranecoated pit; Peripheral membrane protein; Cytoplasmic side. 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.

Sequence similarities

Belongs to the adaptor complexes small subunit family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 142142AP-2 complex subunit sigma
PRO_0000193805

Amino acid modifications

Modified residue1401Phosphoserine By similarity

Experimental info

Mutagenesis151R → S: Reduces interaction with CD4 endocytosis signal motif; when associated with AP2A2 E-21. Ref.5
Mutagenesis621Y → S: Abolishes interaction with CD4 endocytosis signal motif. Ref.5
Mutagenesis631A → W: Abolishes interaction with CD4 endocytosis signal motif. Ref.5
Mutagenesis651L → S: Slightly reduces interaction with CD4 endocytosis signal motif. Ref.5
Mutagenesis881V → D: Abolishes interaction with CD4 endocytosis signal motif. Ref.5
Mutagenesis921N → W: Abolishes interaction with CD4 endocytosis signal motif. Ref.5
Mutagenesis981V → F: Reduces interaction with CD4 endocytosis signal motif. Ref.5
Mutagenesis981V → S: Abolishes interaction with CD4 endocytosis signal motif. Ref.5
Mutagenesis1001E → Y: Abolishes interaction with CD4 endocytosis signal motif. Ref.5
Mutagenesis1031L → S: Abolishes interaction with CD4 endocytosis signal motif. Ref.5

Secondary structure

......................... 142
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62743 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: CA3FD868C65AEDF6

FASTA14217,018
        10         20         30         40         50         60 
MIRFILIQNR AGKTRLAKWY MQFDDDEKQK LIEEVHAVVT VRDAKHTNFV EFRNFKIIYR 

        70         80         90        100        110        120 
RYAGLYFCIC VDVNDNNLAY LEAIHNFVEV LNEYFHNVCE LDLVFNFYKV YTVVDEMFLA 

       130        140 
GEIRETSQTK VLKQLLMLQS LE 

« Hide

References

[1]Marra M., Hillier L., Allen M., Bowles M., Dietrich N., Dubuque T., Geisel S., Kucaba T., Lacy M., Le M., Martin J., Morris M., Schellenberg K., Steptoe M., Tan F., Underwood K., Moore B., Theising B. expand/collapse author list , Wylie T., Lennon G., Soares B., Wilson R., Waterston R.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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.
[3]"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.
[4]"Molecular architecture and functional model of the endocytic AP2 complex."
Collins B.M., McCoy A.J., Kent H.M., Evans P.R., Owen D.J.
Cell 109:523-535(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) IN COMPLEX WITH AP2B1; AP2M1; AP2A2 AND AN INOSITOL POLYPHOSPHATE HEADGROUP.
[5]"A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex."
Kelly B.T., McCoy A.J., Spaete K., Miller S.E., Evans P.R., Hoening S., Owen D.J.
Nature 456:976-979(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.98 ANGSTROMS) IN COMPLEX WITH AP2A2; AP2B1; AP2M1 AND CD4 INTERNALIZATION SIGNAL, MUTAGENESIS OF ARG-15; TYR-62; ALA-63; LEU-65; VAL-88; ASN-92; VAL-98; GLU-100 AND LEU-103.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AA277150 mRNA. No translation available.
CCDSCCDS52042.1.
RefSeqNP_941015.2. NM_198613.2.
UniGeneMm.333597.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JKRX-ray2.98I/S1-142[»]
2JKTX-ray3.40I/S1-142[»]
2VGLX-ray2.59S1-142[»]
2XA7X-ray3.10S1-142[»]
ProteinModelPortalP62743.
SMRP62743. Positions 1-142.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid231318. 1 interaction.
DIPDIP-37505N.
IntActP62743. 2 interactions.
MINTMINT-1869996.

Chemistry

BindingDBP62743.

PTM databases

PhosphoSiteP62743.

Proteomic databases

MaxQBP62743.
PaxDbP62743.
PRIDEP62743.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000086112; ENSMUSP00000083281; ENSMUSG00000008036.
GeneID232910.
KEGGmmu:232910.
UCSCuc012faj.1. mouse.

Organism-specific databases

CTD1175.
MGIMGI:2141861. Ap2s1.

Phylogenomic databases

eggNOGCOG5030.
HOGENOMHOG000185227.
HOVERGENHBG050517.
InParanoidP62743.
KOK11827.
OMASFFDNVC.
OrthoDBEOG7S7SGC.
PhylomeDBP62743.
TreeFamTF300139.

Gene expression databases

ArrayExpressP62743.
BgeeP62743.
GenevestigatorP62743.

Family and domain databases

InterProIPR016635. AP_complex_ssu.
IPR022775. AP_mu_sigma_su.
IPR027156. APS2.
IPR000804. Clathrin_sm-chain_CS.
IPR011012. Longin-like_dom.
[Graphical view]
PANTHERPTHR11753. PTHR11753. 1 hit.
PTHR11753:SF6. PTHR11753:SF6. 1 hit.
PfamPF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
PIRSFPIRSF015588. AP_complex_sigma. 1 hit.
SUPFAMSSF64356. SSF64356. 1 hit.
PROSITEPS00989. CLAT_ADAPTOR_S. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP62743.
NextBio381325.
PROP62743.
SOURCESearch...

Entry information

Entry nameAP2S1_MOUSE
AccessionPrimary (citable) accession number: P62743
Secondary accession number(s): P70626, P97626, Q00380
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 93 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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