ID STING_CHICK Reviewed; 380 AA.
AC E1C7U0;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 30-NOV-2016, entry version 37.
DE RecName: Full=Stimulator of interferon genes protein;
DE Short=STING;
DE AltName: Full=Transmembrane protein 173;
GN Name=TMEM173; Synonyms=STING;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC Phasianidae; Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C.,
RA Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E.,
RA Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W.,
RA Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C.,
RA Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E.,
RA Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J.,
RA Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M.,
RA Paton B., Smith J., Morrice D., Daniels L., Tempest H.G.,
RA Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V.,
RA Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J.,
RA van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J.,
RA Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H.,
RA Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S.,
RA Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J.,
RA Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H.,
RA Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C.,
RA Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C.,
RA Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P.,
RA King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S.,
RA Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S.,
RA Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S.,
RA Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z.,
RA Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J.,
RA Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z.,
RA Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J.,
RA Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G.,
RA Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D.,
RA Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G.,
RA Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A.,
RA Mardis E.R., Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide
RT unique perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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).
CC {ECO:0000250|UniProtKB:Q86WV6}.
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}.
DR EMBL; AADN02063745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02063746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR UniGene; Gga.34881; -.
DR UniGene; Gga.55678; -.
DR STRING; 9031.ENSGALP00000001248; -.
DR PaxDb; E1C7U0; -.
DR eggNOG; ENOG410IH2R; Eukaryota.
DR eggNOG; ENOG4111M85; LUCA.
DR InParanoid; E1C7U0; -.
DR PhylomeDB; E1C7U0; -.
DR TreeFam; TF324444; -.
DR Proteomes; UP000000539; Unplaced.
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; ISS: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 3: Inferred from homology;
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 1 380 Stimulator of interferon genes protein.
FT /FTId=PRO_0000404588.
FT TRANSMEM 30 50 Helical. {ECO:0000255}.
FT TRANSMEM 87 107 Helical. {ECO:0000255}.
FT TRANSMEM 124 144 Helical. {ECO:0000255}.
FT REGION 158 346 c-di-GMP-binding domain (CBD).
FT {ECO:0000250|UniProtKB:Q86WV6}.
FT REGION 167 172 c-di-GMP binding.
FT {ECO:0000250|UniProtKB:Q86WV6}.
FT REGION 243 246 c-di-GMP binding.
FT {ECO:0000250|UniProtKB:Q86WV6}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 51 343 ipfam:TMEM173 [T]
SQ SEQUENCE 380 AA; 42672 MW; C1BF18AA30046713 CRC64;
MPQDPSTRSS PARLLIPEPR AGRARHAACV LLAVCFVVLF LSGEPLAPII RSVCTQLAAL
QLGVLLKGCC CLAEEIFHLH SRHHGSLWQV LCSCFPPRWY LALLLVGGSA YLDPPEDNGH
SPRLALTLSC LCQLLVLALG LQKLSAVEVS ELTESSKKNV AHGLAWSYYI GYLKVVLPRL
KECMEELSRT NPMLRAHRDT WKLHILVPLG CDIWDDLEKA DSNIQYLADL PETILTRAGI
KRRVYKHSLY VIRDKDNKLR ALRAGSLRPP LQTLCAMSQD DCAAFSREQR LEQARLFYRS
LRDILGSSKE CAGLYRLIAY EEPAEPESHF LSGLILWHLQ QQQREEYMVQ EELPLGTSSV
ELSLQVSSSD LPQPLRSDCP
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