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Protein

AP-2 complex subunit sigma

Gene

Ap2s1

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 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 similarity2 Publications

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processEndocytosis, Protein transport, Transport

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-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 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2141861 Ap2s1

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
Mutagenesisi15R → S: Reduces interaction with CD4 endocytosis signal motif; when associated with AP2A2 E-21. 1 Publication1
Mutagenesisi62Y → S: Abolishes interaction with CD4 endocytosis signal motif. 1 Publication1
Mutagenesisi63A → W: Abolishes interaction with CD4 endocytosis signal motif. 1 Publication1
Mutagenesisi65L → S: Slightly reduces interaction with CD4 endocytosis signal motif. 1 Publication1
Mutagenesisi88V → D: Abolishes interaction with CD4 endocytosis signal motif. 1 Publication1
Mutagenesisi92N → W: Abolishes interaction with CD4 endocytosis signal motif. 1 Publication1
Mutagenesisi98V → F: Reduces interaction with CD4 endocytosis signal motif. 1 Publication1
Mutagenesisi98V → S: Abolishes interaction with CD4 endocytosis signal motif. 1 Publication1
Mutagenesisi100E → Y: Abolishes interaction with CD4 endocytosis signal motif. 1 Publication1
Mutagenesisi103L → S: Abolishes interaction with CD4 endocytosis signal motif. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001938051 – 142AP-2 complex subunit sigmaAdd BLAST142

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei140PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP62743
PaxDbiP62743
PeptideAtlasiP62743
PRIDEiP62743

PTM databases

iPTMnetiP62743
PhosphoSitePlusiP62743

Expressioni

Gene expression databases

BgeeiENSMUSG00000008036
ExpressionAtlasiP62743 baseline and differential
GenevisibleiP62743 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).2 Publications

Protein-protein interaction databases

BioGridi231318, 1 interactor
CORUMiP62743
DIPiDIP-37505N
IntActiP62743, 4 interactors
STRINGi10090.ENSMUSP00000083281

Structurei

Secondary structure

1142
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 9Combined sources8
Beta strandi14 – 19Combined sources6
Helixi25 – 40Combined sources16
Beta strandi44 – 46Combined sources3
Beta strandi48 – 52Combined sources5
Beta strandi55 – 62Combined sources8
Beta strandi65 – 71Combined sources7
Beta strandi73 – 75Combined sources3
Helixi77 – 94Combined sources18
Helixi100 – 105Combined sources6
Helixi107 – 117Combined sources11
Helixi128 – 140Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP62743
SMRiP62743
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62743

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0935 Eukaryota
COG5030 LUCA
GeneTreeiENSGT00530000062839
HOGENOMiHOG000185227
HOVERGENiHBG050517
InParanoidiP62743
KOiK11827
OMAiSFFDNVC
OrthoDBiEOG091G0QZV
PhylomeDBiP62743
TreeFamiTF300139

Family and domain databases

InterProiView protein in InterPro
IPR016635 AP_complex_ssu
IPR022775 AP_mu_sigma_su
IPR027156 APS2
IPR000804 Clathrin_sm-chain_CS
IPR011012 Longin-like_dom_sf
PANTHERiPTHR11753 PTHR11753, 1 hit
PTHR11753:SF6 PTHR11753:SF6, 1 hit
PfamiView protein in Pfam
PF01217 Clat_adaptor_s, 1 hit
PIRSFiPIRSF015588 AP_complex_sigma, 1 hit
SUPFAMiSSF64356 SSF64356, 1 hit
PROSITEiView protein in PROSITE
PS00989 CLAT_ADAPTOR_S, 1 hit

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 16, 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

Similar proteinsi

Entry informationi

Entry nameiAP2S1_MOUSE
AccessioniPrimary (citable) accession number: P62743
Secondary accession number(s): P70626, P97626, Q00380
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: February 28, 2018
This is version 125 of the entry and version 1 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

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