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I3LM39

- CGAS_PIG

UniProt

I3LM39 - CGAS_PIG

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Protein
Cyclic GMP-AMP synthase
Gene
MB21D1
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (cGAMP) from ATP and GTP. Catalysis involves both the formation of a 2',5' phosphodiester linkage at the GpA step and the formation of a 3',5' phosphodiester linkage at the ApG step, producing c[G(2',5')pA(3',5')p]. Has antiviral activity by acting as a key cytosolic DNA sensor, the presence of double-stranded DNA (dsDNA) in the cytoplasm being a danger signal that triggers the immune responses. Binds cytosolic DNA directly, leading to activation and synthesis of cGAMP, a second messenger that binds to and activates TMEM173/STING, thereby triggering type-I interferon production.1 Publication

Catalytic activityi

ATP + GTP = 2 diphosphate + cyclic 3',5'-AMP-GMP.1 Publication

Cofactori

Binds 1 Mg2+ per subunit.1 Publication

Enzyme regulationi

The enzyme activity is strongly increased by double-stranded DNA, but not by single-stranded DNA or RNA.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei186 – 1861GTP
Binding sitei188 – 1881ATP
Metal bindingi200 – 2001Magnesium; catalytic
Metal bindingi202 – 2021Magnesium; catalytic
Metal bindingi294 – 2941Magnesium; catalytic
Binding sitei294 – 2941GTP
Binding sitei358 – 3581ATP
Metal bindingi365 – 3651Zinc
Metal bindingi371 – 3711Zinc
Metal bindingi372 – 3721Zinc
Metal bindingi379 – 3791Zinc
Binding sitei389 – 3891ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi351 – 3588GTP
Nucleotide bindingi410 – 4145ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. GTP binding Source: UniProtKB-KW
  4. cyclic-GMP-AMP synthase activity Source: Ensembl
  5. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. activation of innate immune response Source: Ensembl
  2. cellular response to exogenous dsRNA Source: Ensembl
  3. cyclic nucleotide biosynthetic process Source: Ensembl
  4. defense response to virus Source: UniProtKB-KW
  5. innate immune response Source: UniProtKB-KW
  6. positive regulation of defense response to virus by host Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, DNA-binding, GTP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_222145. STING mediated induction of host immune responses.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclic GMP-AMP synthase (EC:2.7.7.86)
Short name:
cGAMP synthase
Short name:
cGAS
Alternative name(s):
Mab-21 domain-containing protein 1
Gene namesi
Name:MB21D1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Chromosome 1

Subcellular locationi

Cytoplasmcytosol By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi200 – 2001E → Q: Abolishes enzyme activity and stimulation of interferon production; when associated with N-202. 1 Publication
Mutagenesisi202 – 2021D → N: Abolishes enzyme activity and stimulation of interferon production; when associated with Q-200. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Cyclic GMP-AMP synthase
PRO_0000423063Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei7 – 71N6-acetyllysine By similarity
Modified residuei389 – 3891N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi139 – 1479
Helixi150 – 17324
Turni177 – 1804
Beta strandi182 – 1843
Turni188 – 1925
Beta strandi200 – 2089
Beta strandi213 – 2175
Beta strandi221 – 2277
Helixi238 – 2403
Helixi248 – 26215
Beta strandi269 – 2713
Beta strandi281 – 2855
Beta strandi287 – 2893
Beta strandi291 – 30111
Helixi307 – 3093
Turni316 – 3194
Helixi321 – 3288
Beta strandi332 – 3354
Beta strandi339 – 3446
Helixi346 – 3483
Beta strandi350 – 3534
Helixi355 – 3639
Beta strandi366 – 3683
Turni369 – 3724
Helixi381 – 39818
Turni399 – 4013
Turni404 – 4074
Helixi410 – 42314
Helixi427 – 4293
Helixi432 – 4343
Helixi435 – 45218
Turni468 – 4703
Helixi473 – 48816
Helixi492 – 4943

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JLXX-ray2.00A135-495[»]
4JLZX-ray2.27A/B135-495[»]
4KB6X-ray3.08A135-495[»]

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni147 – 19044DNA-binding
Add
BLAST
Regioni359 – 38224DNA-binding
Add
BLAST

Sequence similaritiesi

Belongs to the mab-21 family.

Phylogenomic databases

GeneTreeiENSGT00710000106842.
OMAiPQDSQWD.
OrthoDBiEOG7S21ZG.
TreeFamiTF331255.

Family and domain databases

InterProiIPR024810. Mab-21_dom.
[Graphical view]
PfamiPF03281. Mab-21. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

I3LM39-1 [UniParc]FASTAAdd to Basket

« Hide

MAARRGKSTR TASEVGAAGP RASARSVNGA PTVPEAARPG ARRNGPSRAS    50
GCRREKSGPD PREKPQVRTR TARAEDQAEG PSAPSERVEP PSAQGASLLR 100
AGSCRAREAR SARELRPQAG ATELAAPARM EAPPGAWKLQ TVLEKVRLSR 150
HEISEAAEVV NWVVEHLLRR LQGGESEFKG VALLRTGSYY ERVKISAPNE 200
FDVMFKLEVP RIQLEEYCNS GAHYFVKFKR NPGGNPLEQF LEKEILSASK 250
MLSKFRKIIK EEIKNIEGVT VERKRRGSPA VTLLISKPKE ISVDIILALE 300
SKSSWPASTQ KGLPISQWLG AKVKNNLKRQ PFYLVPKHAK EGSGFQEETW 350
RLSFSHIEKD ILKNHGQSKT CCEIDGVKCC RKECLKLMKY LLEQLKKKFG 400
NRRELAKFCS YHVKTAFFHV CTQDPHDNQW HLKNLECCFD NCVAYFLQCL 450
KTEQLANYFI PGVNLFSRDL IDKPSKEFLS KQIEYERNNG FPVFW 495
Length:495
Mass (Da):55,809
Last modified:July 11, 2012 - v1
Checksum:i13E76296D97E176B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FP102323 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENSSSCT00000030573; ENSSSCP00000025159; ENSSSCG00000021383.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FP102323 Genomic DNA. No translation available.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4JLX X-ray 2.00 A 135-495 [» ]
4JLZ X-ray 2.27 A/B 135-495 [» ]
4KB6 X-ray 3.08 A 135-495 [» ]
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSSSCT00000030573 ; ENSSSCP00000025159 ; ENSSSCG00000021383 .

Phylogenomic databases

GeneTreei ENSGT00710000106842.
OMAi PQDSQWD.
OrthoDBi EOG7S21ZG.
TreeFami TF331255.

Enzyme and pathway databases

Reactomei REACT_222145. STING mediated induction of host immune responses.

Family and domain databases

InterProi IPR024810. Mab-21_dom.
[Graphical view ]
Pfami PF03281. Mab-21. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Porcine genome sequencing project
    Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 135-495 IN COMPLEXES WITH MAGNESIUM IONS, ZINC IONS; ATP; GTP; UTP AND DNA, COFACTOR, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, DNA-BINDING, MUTAGENESIS OF GLU-200 AND ASP-202.

Entry informationi

Entry nameiCGAS_PIG
AccessioniPrimary (citable) accession number: I3LM39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2013
Last sequence update: July 11, 2012
Last modified: September 3, 2014
This is version 13 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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