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Protein

AP-2 complex subunit sigma

Gene

Ap2s1

Organism
Mus musculus (Mouse)
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 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).By similarity

GO - Molecular functioni

  1. protein transporter activity Source: InterPro

GO - Biological processi

  1. endocytosis Source: UniProtKB-KW
  2. intracellular protein transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_299462. WNT5A-dependent internalization of FZD4.
REACT_304279. Retrograde neurotrophin signalling.
REACT_316383. MHC class II antigen presentation.
REACT_322343. Trafficking of GluR2-containing AMPA receptors.
REACT_350802. EGFR downregulation.
REACT_353475. Recycling pathway of L1.

Names & Taxonomyi

Protein namesi
Recommended name:
AP-2 complex subunit sigma
Alternative name(s):
Adaptor protein complex AP-2 subunit sigma
Adaptor-related protein complex 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 namesi
Name:Ap2s1
Synonyms:Ap17, Claps2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2141861. Ap2s1.

Subcellular locationi

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

GO - Cellular componenti

  1. AP-2 adaptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151R → S: Reduces interaction with CD4 endocytosis signal motif; when associated with AP2A2 E-21. 1 Publication
Mutagenesisi62 – 621Y → S: Abolishes interaction with CD4 endocytosis signal motif. 1 Publication
Mutagenesisi63 – 631A → W: Abolishes interaction with CD4 endocytosis signal motif. 1 Publication
Mutagenesisi65 – 651L → S: Slightly reduces interaction with CD4 endocytosis signal motif. 1 Publication
Mutagenesisi88 – 881V → D: Abolishes interaction with CD4 endocytosis signal motif. 1 Publication
Mutagenesisi92 – 921N → W: Abolishes interaction with CD4 endocytosis signal motif. 1 Publication
Mutagenesisi98 – 981V → F: Reduces interaction with CD4 endocytosis signal motif. 1 Publication
Mutagenesisi98 – 981V → S: Abolishes interaction with CD4 endocytosis signal motif. 1 Publication
Mutagenesisi100 – 1001E → Y: Abolishes interaction with CD4 endocytosis signal motif. 1 Publication
Mutagenesisi103 – 1031L → S: Abolishes interaction with CD4 endocytosis signal motif. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 142142AP-2 complex subunit sigmaPRO_0000193805Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei140 – 1401PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP62743.
PaxDbiP62743.
PRIDEiP62743.

PTM databases

PhosphoSiteiP62743.

Expressioni

Gene expression databases

BgeeiP62743.
ExpressionAtlasiP62743. baseline and differential.
GenevestigatoriP62743.

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).2 Publications

Protein-protein interaction databases

BioGridi231318. 1 interaction.
DIPiDIP-37505N.
IntActiP62743. 2 interactions.
MINTiMINT-1869996.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Beta strandi14 – 196Combined sources
Helixi25 – 4016Combined sources
Beta strandi44 – 463Combined sources
Beta strandi48 – 525Combined sources
Beta strandi55 – 628Combined sources
Beta strandi65 – 717Combined sources
Beta strandi73 – 753Combined sources
Helixi77 – 9418Combined sources
Helixi100 – 1056Combined sources
Helixi107 – 11711Combined sources
Helixi128 – 14013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JKRX-ray2.98I/S1-142[»]
2JKTX-ray3.40I/S1-142[»]
2VGLX-ray2.59S1-142[»]
2XA7X-ray3.10S1-142[»]
4UQIX-ray2.79S1-142[»]
SMRiP62743. Positions 1-142.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62743.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5030.
HOGENOMiHOG000185227.
HOVERGENiHBG050517.
InParanoidiP62743.
KOiK11827.
OMAiSFFDNVC.
OrthoDBiEOG7S7SGC.
PhylomeDBiP62743.
TreeFamiTF300139.

Family and domain databases

InterProiIPR016635. AP_complex_ssu.
IPR022775. AP_mu_sigma_su.
IPR027156. APS2.
IPR000804. Clathrin_sm-chain_CS.
IPR011012. Longin-like_dom.
[Graphical view]
PANTHERiPTHR11753. PTHR11753. 1 hit.
PTHR11753:SF6. PTHR11753:SF6. 1 hit.
PfamiPF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
PIRSFiPIRSF015588. AP_complex_sigma. 1 hit.
SUPFAMiSSF64356. SSF64356. 1 hit.
PROSITEiPS00989. CLAT_ADAPTOR_S. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P62743-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRFILIQNR AGKTRLAKWY MQFDDDEKQK LIEEVHAVVT VRDAKHTNFV
60 70 80 90 100
EFRNFKIIYR RYAGLYFCIC VDVNDNNLAY LEAIHNFVEV LNEYFHNVCE
110 120 130 140
LDLVFNFYKV YTVVDEMFLA GEIRETSQTK VLKQLLMLQS LE
Length:142
Mass (Da):17,018
Last modified:August 15, 2004 - v1
Checksum:iCA3FD868C65AEDF6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AA277150 mRNA. No translation available.
CCDSiCCDS52042.1.
RefSeqiNP_941015.2. NM_198613.2.
UniGeneiMm.333597.

Genome annotation databases

EnsembliENSMUST00000086112; ENSMUSP00000083281; ENSMUSG00000008036.
GeneIDi232910.
KEGGimmu:232910.
UCSCiuc012faj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AA277150 mRNA. No translation available.
CCDSiCCDS52042.1.
RefSeqiNP_941015.2. NM_198613.2.
UniGeneiMm.333597.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JKRX-ray2.98I/S1-142[»]
2JKTX-ray3.40I/S1-142[»]
2VGLX-ray2.59S1-142[»]
2XA7X-ray3.10S1-142[»]
4UQIX-ray2.79S1-142[»]
SMRiP62743. Positions 1-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231318. 1 interaction.
DIPiDIP-37505N.
IntActiP62743. 2 interactions.
MINTiMINT-1869996.

Chemistry

BindingDBiP62743.

PTM databases

PhosphoSiteiP62743.

Proteomic databases

MaxQBiP62743.
PaxDbiP62743.
PRIDEiP62743.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000086112; ENSMUSP00000083281; ENSMUSG00000008036.
GeneIDi232910.
KEGGimmu:232910.
UCSCiuc012faj.1. mouse.

Organism-specific databases

CTDi1175.
MGIiMGI:2141861. Ap2s1.

Phylogenomic databases

eggNOGiCOG5030.
HOGENOMiHOG000185227.
HOVERGENiHBG050517.
InParanoidiP62743.
KOiK11827.
OMAiSFFDNVC.
OrthoDBiEOG7S7SGC.
PhylomeDBiP62743.
TreeFamiTF300139.

Enzyme and pathway databases

ReactomeiREACT_299462. WNT5A-dependent internalization of FZD4.
REACT_304279. Retrograde neurotrophin signalling.
REACT_316383. MHC class II antigen presentation.
REACT_322343. Trafficking of GluR2-containing AMPA receptors.
REACT_350802. EGFR downregulation.
REACT_353475. Recycling pathway of L1.

Miscellaneous databases

EvolutionaryTraceiP62743.
NextBioi381325.
PROiP62743.
SOURCEiSearch...

Gene expression databases

BgeeiP62743.
ExpressionAtlasiP62743. baseline and differential.
GenevestigatoriP62743.

Family and domain databases

InterProiIPR016635. AP_complex_ssu.
IPR022775. AP_mu_sigma_su.
IPR027156. APS2.
IPR000804. Clathrin_sm-chain_CS.
IPR011012. Longin-like_dom.
[Graphical view]
PANTHERiPTHR11753. PTHR11753. 1 hit.
PTHR11753:SF6. PTHR11753:SF6. 1 hit.
PfamiPF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
PIRSFiPIRSF015588. AP_complex_sigma. 1 hit.
SUPFAMiSSF64356. SSF64356. 1 hit.
PROSITEiPS00989. CLAT_ADAPTOR_S. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. 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(2002) [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(2003) [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(2001) [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(2007) [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.

Entry informationi

Entry nameiAP2S1_MOUSE
AccessioniPrimary (citable) accession number: P62743
Secondary accession number(s): P70626, P97626, Q00380
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2004
Last sequence update: August 15, 2004
Last modified: March 31, 2015
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.