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Q99K10

- NLGN1_MOUSE

UniProt

Q99K10 - NLGN1_MOUSE

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Protein

Neuroligin-1

Gene

Nlgn1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses.3 Publications

GO - Molecular functioni

  1. neurexin family protein binding Source: UniProtKB
  2. protein dimerization activity Source: BHF-UCL
  3. receptor activity Source: RefGenome

GO - Biological processi

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor clustering Source: BHF-UCL
  2. calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules Source: UniProtKB
  3. cytoskeletal matrix organization at active zone Source: BHF-UCL
  4. establishment of protein localization Source: BHF-UCL
  5. heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: BHF-UCL
  6. nervous system development Source: UniProtKB
  7. neurexin clustering Source: BHF-UCL
  8. neuron cell-cell adhesion Source: BHF-UCL
  9. N-methyl-D-aspartate receptor clustering Source: BHF-UCL
  10. positive regulation of dendritic spine development Source: BHF-UCL
  11. positive regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
  12. positive regulation of filopodium assembly Source: BHF-UCL
  13. positive regulation of ruffle assembly Source: Ensembl
  14. positive regulation of synapse assembly Source: BHF-UCL
  15. positive regulation of synaptic transmission, GABAergic Source: BHF-UCL
  16. positive regulation of synaptic transmission, glutamatergic Source: BHF-UCL
  17. positive regulation of synaptic vesicle endocytosis Source: BHF-UCL
  18. positive regulation of synaptic vesicle exocytosis Source: BHF-UCL
  19. postsynaptic density protein 95 clustering Source: BHF-UCL
  20. postsynaptic membrane assembly Source: BHF-UCL
  21. presynaptic membrane assembly Source: BHF-UCL
  22. protein heterotetramerization Source: Ensembl
  23. protein homooligomerization Source: BHF-UCL
  24. protein localization to synapse Source: BHF-UCL
  25. protein targeting Source: Ensembl
  26. receptor localization to synapse Source: BHF-UCL
  27. regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: BHF-UCL
  28. regulation of neuron differentiation Source: UniProtKB
  29. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: BHF-UCL
  30. regulation of respiratory gaseous exchange by neurological system process Source: MGI
  31. regulation of synaptic transmission Source: MGI
  32. synapse assembly Source: UniProtKB
  33. synapse organization Source: MGI
  34. synaptic vesicle clustering Source: BHF-UCL
  35. synaptic vesicle targeting Source: UniProtKB
  36. terminal button organization Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Protein family/group databases

MEROPSiS09.994.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuroligin-1
Gene namesi
Name:Nlgn1
Synonyms:Kiaa1070
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:2179435. Nlgn1.

Subcellular locationi

Cell membrane By similarity; Single-pass type I membrane protein By similarity. Cell junctionsynapse By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity
Note: Enriched in synaptic plasma membranes and clustered in synaptic clefts and postsynaptic densities. Detected at dendritic spines. Colocalized with DLG4/PSD-95 and GRIN1/NMDAR1 (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini46 – 697652ExtracellularSequence AnalysisAdd
BLAST
Transmembranei698 – 71821HelicalSequence AnalysisAdd
BLAST
Topological domaini719 – 843125CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell surface Source: BHF-UCL
  3. dendrite Source: BHF-UCL
  4. excitatory synapse Source: BHF-UCL
  5. external side of plasma membrane Source: MGI
  6. filopodium tip Source: BHF-UCL
  7. integral component of plasma membrane Source: UniProtKB
  8. N-methyl-D-aspartate selective glutamate receptor complex Source: Ensembl
  9. postsynaptic membrane Source: UniProtKB-KW
  10. synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

No obvious phenotype, but mice present subtle behavorial changes with some deficits in spatial learning and memory. In addition, mice have reduced brain volume. Mice lacking both NLGN1 and NLGN2, or NLGN1 and NLGN3, are viable, but have impaired breathing, drastically reduced reproduction rates and striking deficits in raising their offspring. Mice lacking NLGN1, NLGN2 and NLGN3 are born at the expected Mendelian rate, but die shortly after birth due to respiratory failure. They do not show a significant change in the number of synapses, but synapse function is strongly impaired.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4545Sequence AnalysisAdd
BLAST
Chaini46 – 843798Neuroligin-1PRO_0000008641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi109 – 1091N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi117 ↔ 1531 Publication
Glycosylationi303 – 3031N-linked (GlcNAc...) (complex)By similarity
Disulfide bondi342 ↔ 3531 Publication
Glycosylationi343 – 3431N-linked (GlcNAc...) (complex)By similarity
Disulfide bondi512 ↔ 5461 Publication
Glycosylationi547 – 5471N-linked (GlcNAc...)1 Publication
Glycosylationi683 – 6831O-linked (GalNAc...)By similarity
Glycosylationi686 – 6861O-linked (GalNAc...)By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ99K10.
PaxDbiQ99K10.
PRIDEiQ99K10.

PTM databases

PhosphoSiteiQ99K10.

Expressioni

Tissue specificityi

Brain and arteries (at protein level). Expressed in olfactory bulb. Detected in brain.4 Publications

Gene expression databases

BgeeiQ99K10.
CleanExiMM_NLGN1.
ExpressionAtlasiQ99K10. baseline and differential.
GenevestigatoriQ99K10.

Interactioni

Subunit structurei

Interacts with NRXN1, NRXN2 and NRXN3. Interacts (via its C-terminus) with DLG4/PSD-95 (via PDZ domain 3). Interacts with AIP1, GOPC and PDZRN3 (By similarity). Interacts with NLGN3.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PTPRTO145222EBI-775037,EBI-728180From a different organism.

Protein-protein interaction databases

DIPiDIP-32027N.
IntActiQ99K10. 2 interactions.
MINTiMINT-5104301.
STRINGi10090.ENSMUSP00000074565.

Structurei

Secondary structure

1
843
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi54 – 574Combined sources
Beta strandi60 – 634Combined sources
Beta strandi65 – 673Combined sources
Beta strandi77 – 848Combined sources
Helixi91 – 933Combined sources
Beta strandi105 – 1095Combined sources
Beta strandi122 – 1243Combined sources
Turni128 – 1303Combined sources
Helixi133 – 1375Combined sources
Helixi139 – 1457Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi155 – 1606Combined sources
Beta strandi193 – 1986Combined sources
Beta strandi202 – 2065Combined sources
Helixi209 – 2113Combined sources
Helixi215 – 2217Combined sources
Beta strandi224 – 2285Combined sources
Helixi233 – 2375Combined sources
Beta strandi241 – 2455Combined sources
Helixi249 – 26416Combined sources
Helixi266 – 2683Combined sources
Beta strandi270 – 28011Combined sources
Helixi282 – 2909Combined sources
Beta strandi310 – 3167Combined sources
Beta strandi319 – 3213Combined sources
Beta strandi324 – 3274Combined sources
Helixi329 – 33911Combined sources
Helixi347 – 35610Combined sources
Helixi359 – 3635Combined sources
Beta strandi375 – 3773Combined sources
Beta strandi382 – 3854Combined sources
Helixi389 – 3957Combined sources
Beta strandi402 – 4087Combined sources
Turni409 – 4124Combined sources
Helixi413 – 4164Combined sources
Helixi417 – 4193Combined sources
Beta strandi422 – 4243Combined sources
Helixi428 – 44316Combined sources
Helixi451 – 4599Combined sources
Helixi469 – 48416Combined sources
Helixi486 – 49813Combined sources
Beta strandi503 – 5086Combined sources
Turni525 – 5284Combined sources
Helixi529 – 5324Combined sources
Turni536 – 5383Combined sources
Beta strandi542 – 5443Combined sources
Helixi550 – 56920Combined sources
Beta strandi572 – 5765Combined sources
Turni600 – 6023Combined sources
Beta strandi604 – 6118Combined sources
Beta strandi613 – 6175Combined sources
Helixi620 – 6278Combined sources
Helixi630 – 6334Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3B3QX-ray2.40A/B46-635[»]
ProteinModelPortaliQ99K10.
SMRiQ99K10. Positions 52-631.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99K10.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2272.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000231424.
HOVERGENiHBG008839.
InParanoidiQ99K10.
KOiK07378.
OMAiKFVELIV.
PhylomeDBiQ99K10.
TreeFamiTF326187.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR000460. Neuroligin.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR01090. NEUROLIGIN.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99K10-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MALPRCMWPN YVWRAMMACV VHRGSGAPLT LCLLGCLLQT FHVLSQKLDD
60 70 80 90 100
VDPLVTTNFG KIRGIKKELN NEILGPVIQF LGVPYAAPPT GEHRFQPPEP
110 120 130 140 150
PSPWSDIRNA TQFAPVCPQN IIDGRLPEVM LPVWFTNNLD VVSSYVQDQS
160 170 180 190 200
EDCLYLNIYV PTEDGPLTKK HTDDLGDNDG AEDEDIRDSG GPKPVMVYIH
210 220 230 240 250
GGSYMEGTGN LYDGSVLASY GNVIVITVNY RLGVLGFLST GDQAAKGNYG
260 270 280 290 300
LLDLIQALRW TSENIGFFGG DPLRITVFGS GAGGSCVNLL TLSHYSEGNR
310 320 330 340 350
WSNSTKGLFQ RAIAQSGTAL SSWAVSFQPA KYARILATKV GCNVSDTVEL
360 370 380 390 400
VECLQKKPYK ELVDQDVQPA RYHIAFGPVI DGDVIPDDPQ ILMEQGEFLN
410 420 430 440 450
YDIMLGVNQG EGLKFVENIV DSDDGVSASD FDFAVSNFVD NLYGYPEGKD
460 470 480 490 500
VLRETIKFMY TDWADRHNPE TRRKTLLALF TDHQWVAPAV ATADLHSNFG
510 520 530 540 550
SPTYFYAFYH HCQTDQVPAW ADAAHGDEVP YVLGIPMIGP TELFPCNFSK
560 570 580 590 600
NDVMLSAVVM TYWTNFAKTG DPNQPVPQDT KFIHTKPNRF EEVAWTRYSQ
610 620 630 640 650
KDQLYLHIGL KPRVKEHYRA NKVNLWLELV PHLHNLNDIS QYTSTTTKVP
660 670 680 690 700
STDITLRPTR KNSTPVTSAF PTAKQDDPKQ QPSPFSVDQR DYSTELSVTI
710 720 730 740 750
AVGASLLFLN ILAFAALYYK KDKRRHDVHR RCSPQRTTTN DLTHAPEEEI
760 770 780 790 800
MSLQMKHTDL DHECESIHPH EVVLRTACPP DYTLAMRRSP DDIPLMTPNT
810 820 830 840
ITMIPNTIPG IQPLHTFNTF TGGQNNTLPH PHPHPHSHST TRV

Note: No experimental confirmation available.

Length:843
Mass (Da):94,149
Last modified:May 23, 2003 - v2
Checksum:i69E50709CF7D2E1F
GO
Isoform 2 (identifier: Q99K10-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     165-184: Missing.
     236-269: GFLSTGDQAAKGNYGLLDLIQALRWTSENIGFFG → EKETIKETISVALQALRTKGGGFIPKQATYKRCE
     270-843: Missing.

Note: No experimental confirmation available.

Show »
Length:249
Mass (Da):27,602
Checksum:i1D87ADF1EAFF2F0B
GO

Sequence cautioni

The sequence BAC65715.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei165 – 18420Missing in isoform 2. 1 PublicationVSP_007528Add
BLAST
Alternative sequencei236 – 26934GFLST…IGFFG → EKETIKETISVALQALRTKG GGFIPKQATYKRCE in isoform 2. 1 PublicationVSP_007529Add
BLAST
Alternative sequencei270 – 843574Missing in isoform 2. 1 PublicationVSP_007530Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122433 mRNA. Translation: BAC65715.1. Different initiation.
BC005523 mRNA. Translation: AAH05523.1.
CCDSiCCDS17268.1. [Q99K10-1]
RefSeqiNP_619607.2. NM_138666.3. [Q99K10-1]
UniGeneiMm.316080.

Genome annotation databases

EnsembliENSMUST00000075054; ENSMUSP00000074565; ENSMUSG00000063887. [Q99K10-1]
GeneIDi192167.
KEGGimmu:192167.
UCSCiuc008otc.1. mouse. [Q99K10-1]
uc008otd.1. mouse. [Q99K10-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122433 mRNA. Translation: BAC65715.1 . Different initiation.
BC005523 mRNA. Translation: AAH05523.1 .
CCDSi CCDS17268.1. [Q99K10-1 ]
RefSeqi NP_619607.2. NM_138666.3. [Q99K10-1 ]
UniGenei Mm.316080.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3B3Q X-ray 2.40 A/B 46-635 [» ]
ProteinModelPortali Q99K10.
SMRi Q99K10. Positions 52-631.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-32027N.
IntActi Q99K10. 2 interactions.
MINTi MINT-5104301.
STRINGi 10090.ENSMUSP00000074565.

Protein family/group databases

MEROPSi S09.994.

PTM databases

PhosphoSitei Q99K10.

Proteomic databases

MaxQBi Q99K10.
PaxDbi Q99K10.
PRIDEi Q99K10.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000075054 ; ENSMUSP00000074565 ; ENSMUSG00000063887 . [Q99K10-1 ]
GeneIDi 192167.
KEGGi mmu:192167.
UCSCi uc008otc.1. mouse. [Q99K10-1 ]
uc008otd.1. mouse. [Q99K10-2 ]

Organism-specific databases

CTDi 22871.
MGIi MGI:2179435. Nlgn1.
Rougei Search...

Phylogenomic databases

eggNOGi COG2272.
GeneTreei ENSGT00760000118946.
HOGENOMi HOG000231424.
HOVERGENi HBG008839.
InParanoidi Q99K10.
KOi K07378.
OMAi KFVELIV.
PhylomeDBi Q99K10.
TreeFami TF326187.

Miscellaneous databases

EvolutionaryTracei Q99K10.
NextBioi 371168.
PROi Q99K10.
SOURCEi Search...

Gene expression databases

Bgeei Q99K10.
CleanExi MM_NLGN1.
ExpressionAtlasi Q99K10. baseline and differential.
Genevestigatori Q99K10.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR000460. Neuroligin.
[Graphical view ]
Pfami PF00135. COesterase. 1 hit.
[Graphical view ]
PRINTSi PR01090. NEUROLIGIN.
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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 2).
  3. "Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons."
    Scheiffele P., Fan J., Choih J., Fetter R., Serafini T.
    Cell 101:657-669(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Neuroligin 3 is a vertebrate gliotactin expressed in the olfactory ensheathing glia, a growth-promoting class of macroglia."
    Gilbert M., Smith J., Roskams A.J., Auld V.J.
    Glia 34:151-164(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins."
    Graf E.R., Zhang X., Jin S.X., Linhoff M.W., Craig A.M.
    Cell 119:1013-1026(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
  7. "Neuroligin-3 is a neuronal adhesion protein at GABAergic and glutamatergic synapses."
    Budreck E.C., Scheiffele P.
    Eur. J. Neurosci. 26:1738-1748(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NLGN3.
  8. Cited for: TISSUE SPECIFICITY.
  9. "The synaptic proteins neurexins and neuroligins are widely expressed in the vascular system and contribute to its functions."
    Bottos A., Destro E., Rissone A., Graziano S., Cordara G., Assenzio B., Cera M.R., Mascia L., Bussolino F., Arese M.
    Proc. Natl. Acad. Sci. U.S.A. 106:20782-20787(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  10. "Neuroligin-1 deletion results in impaired spatial memory and increased repetitive behavior."
    Blundell J., Blaiss C.A., Etherton M.R., Espinosa F., Tabuchi K., Walz C., Bolliger M.F., Sudhof T.C., Powell C.M.
    J. Neurosci. 30:2115-2129(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  11. "Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions."
    Chen X., Liu H., Shim A.H., Focia P.J., He X.
    Nat. Struct. Mol. Biol. 15:50-56(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 39-635 IN COMPLEX WITH HUMAN NRX1B, DISULFIDE BONDS, GLYCOSYLATION AT ASN-109 AND ASN-547.

Entry informationi

Entry nameiNLGN1_MOUSE
AccessioniPrimary (citable) accession number: Q99K10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: November 26, 2014
This is version 119 of the entry and version 2 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