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DescriptionRecName: Full=Stimulator of interferon genes protein; Short=STING; AltName: Full=Transmembrane protein 173;
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MyHits synonymsSTING_XENTR , A8E5V9 , 66F389EB83EC7199
match map segment
ipfam:TMEM173  
Legends: 1, BINDING c-di-GMP. {ECO:0000250|UniProtKB:Q86WV6}; 2, TRANSMEM Helical. {ECO:0000255}; 3, REGION c-di-GMP binding. {ECO:0000250|UniProtKB:Q86WV6}.
ID   STING_XENTR             Reviewed;         329 AA.
AC   A8E5V9;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   10-MAY-2017, entry version 53.
DE   RecName: Full=Stimulator of interferon genes protein;
DE            Short=STING;
DE   AltName: Full=Transmembrane protein 173;
GN   Name=tmem173; Synonyms=sting;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=26300263; DOI=10.1016/j.molcel.2015.07.022;
RA   Kranzusch P.J., Wilson S.C., Lee A.S., Berger J.M., Doudna J.A.,
RA   Vance R.E.;
RT   "Ancient origin of cGAS-STING reveals mechanism of universal 2',3'
RT   cGAMP signaling.";
RL   Mol. Cell 59:891-903(2015).
CC   -!- FUNCTION: Facilitator of innate immune signaling that acts as a
CC       sensor of cytosolic DNA from bacteria and viruses and promotes the
CC       production of type I interferon (IFN-alpha and IFN-beta). Innate
CC       immune response is triggered in response to non-CpG double-
CC       stranded DNA from viruses and bacteria delivered to the cytoplasm.
CC       Acts by recognizing and binding cyclic di-GMP (c-di-GMP), a second
CC       messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a
CC       messenger produced in response to DNA virus in the cytosol: upon
CC       binding of c-di-GMP or cGAMP, autoinhibition is alleviated and
CC       TMEM173/STING is able to activate both NF-kappa-B and IRF3
CC       transcription pathways to induce expression of type I interferon
CC       and exert a potent anti-viral state (By similarity). Can bind 2'-
CC       3' linked cGAMP but not 3'-3' linked cGAMP (PubMed:26300263).
CC       {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:26300263}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q86WV6}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3};
CC       Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer
CC       membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the TMEM173 family. {ECO:0000305}.
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DR   EMBL; BC153736; AAI53737.1; -; mRNA.
DR   RefSeq; NP_001106445.2; NM_001112974.1.
DR   UniGene; Str.62876; -.
DR   SMR; A8E5V9; -.
DR   STRING; 8364.ENSXETP00000055434; -.
DR   PaxDb; A8E5V9; -.
DR   GeneID; 100127621; -.
DR   KEGG; xtr:100127621; -.
DR   CTD; 340061; -.
DR   Xenbase; XB-GENE-5880492; tmem173.
DR   eggNOG; ENOG410IH2R; Eukaryota.
DR   eggNOG; ENOG4111M85; LUCA.
DR   HOGENOM; HOG000076316; -.
DR   HOVERGEN; HBG094065; -.
DR   InParanoid; A8E5V9; -.
DR   KO; K12654; -.
DR   Proteomes; UP000008143; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0035438; F:cyclic-di-GMP binding; ISS:UniProtKB.
DR   GO; GO:0061507; F:cyclic-GMP-AMP binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0002218; P:activation of innate immune response; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR   GO; GO:0032608; P:interferon-beta production; ISS:UniProtKB.
DR   GO; GO:0032481; P:positive regulation of type I interferon production; IEA:InterPro.
DR   CDD; cd12146; STING_C; 1.
DR   InterPro; IPR029158; STING.
DR   InterPro; IPR033952; STING_C.
DR   Pfam; PF15009; TMEM173; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Cell membrane; Complete proteome; Endoplasmic reticulum;
KW   Immunity; Innate immunity; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    329       Stimulator of interferon genes protein.
FT                                /FTId=PRO_0000355181.
FT   TRANSMEM      5     27       Helical. {ECO:0000255}.
FT   TRANSMEM     68     88       Helical. {ECO:0000255}.
FT   TRANSMEM     98    118       Helical. {ECO:0000255}.
FT   REGION      135    325       c-di-GMP-binding domain (CBD).
FT                                {ECO:0000250|UniProtKB:Q86WV6}.
FT   REGION      144    149       c-di-GMP binding.
FT                                {ECO:0000250|UniProtKB:Q86WV6}.
FT   REGION      220    223       c-di-GMP binding.
FT                                {ECO:0000250|UniProtKB:Q86WV6}.
FT   BINDING     245    245       c-di-GMP. {ECO:0000250|UniProtKB:Q86WV6}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        29    322       ipfam:TMEM173 [T]
SQ   SEQUENCE   329 AA;  37815 MW;  66F389EB83EC7199 CRC64;
     MACVLAIGSI LFVWILGKGK YSGAQLIYRM ATNFAISQGC CLVTCACELT EEIKHLHTRY
     NGHYWRALKA SFNLSCAAFV TAILCYVFYE PKLMASLPLT IDITLTLLSW LFCWILGIQG
     PTPATISEIT EIKQLNVAHG LAWSYYVGYL QFVLPALKES IQKFNEENHN LLKFPETCRL
     HILIPLSCRL YGDLKDVDEN ITFLKEIPPL YIDRAGIKGR VFKNNVYRIL DEDGRPYNCI
     VEYATPLASL LKMTDIPSAA FSADDRLQQT KLFYRTLKDI LENAHELQNT YRLIVYEDFP
     ETKDHSRHLL SQEILKHIRQ QHSEEYSML
//