ID ENTC3_STAAU Reviewed; 266 AA. AC P0A0L5; P23313; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 03-MAY-2023, entry version 88. DE RecName: Full=Enterotoxin type C-3; DE AltName: Full=SEC3; DE Flags: Precursor; GN Name=entC3; OS Staphylococcus aureus. OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=1280; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2325627; DOI=10.1007/bf00260504; RA Hovde C.J., Hackett S.P., Bohach G.A.; RT "Nucleotide sequence of the staphylococcal enterotoxin C3 gene: sequence RT comparison of all three type C staphylococcal enterotoxins."; RL Mol. Gen. Genet. 220:329-333(1990). RN [2] RP FUNCTION, AND INTERACTION WITH HOST MHC CLASS II HLA-DRA; HLA-DRB1 AND RP T-CELL RECEPTOR/TCR BETA VARIABLE CHAIN. RX PubMed=10229190; DOI=10.1016/s1074-7613(00)80047-3; RA Andersen P.S., Lavoie P.M., Sekaly R.P., Churchill H., Kranz D.M., RA Schlievert P.M., Karjalainen K., Mariuzza R.A.; RT "Role of the T cell receptor alpha chain in stabilizing TCR-superantigen- RT MHC class II complexes."; RL Immunity 10:473-483(1999). RN [3] RP FUNCTION. RX PubMed=28849041; DOI=10.3892/mmr.2017.7199; RA Xie Y., Wang M., Dong Z., Song H., Li L., Yang M., Li P., Tian J., RA Zhang K., Xia X., Zhang T., Tang A.; RT "In vitro effects of Staphylococcus aureus enterotoxin C3 on T cell RT activation, proliferation and cytokine production."; RL Mol. Med. Report. 16:4744-4750(2017). RN [4] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF COMPLEX WITH HOST TCR, AND RP DISULFIDE BOND. RX PubMed=8906797; DOI=10.1038/384188a0; RA Fields B.A., Malchiodi E.L., Li H., Ysern X., Stauffacher C.V., RA Schlievert P.M., Karjalainen K., Mariuzza R.A.; RT "Crystal structure of a T-cell receptor beta-chain complexed with a RT superantigen."; RL Nature 384:188-192(1996). RN [5] {ECO:0007744|PDB:1JWM, ECO:0007744|PDB:1JWS, ECO:0007744|PDB:1JWU} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 28-266, INTERACTION WITH HOST MHC RP CLASS II SUBUNITS HLA-DRA AND HLA-DRB1, AND DISULFIDE BOND. RX PubMed=12962633; DOI=10.1016/s0969-2126(03)00187-4; RA Sundberg E.J., Andersen P.S., Schlievert P.M., Karjalainen K., RA Mariuzza R.A.; RT "Structural, energetic, and functional analysis of a protein-protein RT interface at distinct stages of affinity maturation."; RL Structure 11:1151-1161(2003). RN [6] {ECO:0007744|PDB:3BVM, ECO:0007744|PDB:3BVZ, ECO:0007744|PDB:3BYT, ECO:0007744|PDB:3BYY, ECO:0007744|PDB:3BZD} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 28-266 IN COMPLEX WITH ZINC. RA Cho S., Swaminathan C.P., Kerzic M.C., Guan R., Yang J., Kieke M.C., RA Andersen P.S., Krantz D.M., Mariuzza R.A., Eric S.J.; RT "Manipulating the coupled folding and binding process drives affinity RT maturation in a protein-protein complex."; RL Submitted (JAN-2008) to the PDB data bank. RN [7] {ECO:0007744|PDB:3BVG} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 28-266 IN COMPLEX WITH ZINC, AND RP INTERACTION WITH HOST T-CELL RECEPTOR/TCR BETA VARIABLE/TRBV8-2. RX PubMed=20836565; DOI=10.1021/bi1008968; RA Cho S., Swaminathan C.P., Bonsor D.A., Kerzic M.C., Guan R., Yang J., RA Kieke M.C., Andersen P.S., Kranz D.M., Mariuzza R.A., Sundberg E.J.; RT "Assessing energetic contributions to binding from a disordered region in a RT protein-protein interaction."; RL Biochemistry 49:9256-9268(2010). CC -!- FUNCTION: Staphylococcal enterotoxin that activates the host immune CC system by binding as unprocessed molecules to major histocompatibility CC (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, CC this ternary complex activates a large number of T-lymphocytes CC initiating a systemic release of pro-inflammatory cytokines CC (PubMed:10229190, PubMed:28849041). Causes also the intoxication CC staphylococcal food poisoning syndrome (By similarity). CC {ECO:0000250|UniProtKB:P34071, ECO:0000269|PubMed:10229190, CC ECO:0000269|PubMed:28849041}. CC -!- SUBUNIT: Interacts with MHC class II molecules composed of alpha/HLA- CC DRA and beta/HLA-DRB1 chains (PubMed:10229190). Interacts with host T- CC cell receptor/TCR beta variable chain TRBV8-2 (PubMed:10229190, CC PubMed:20836565). {ECO:0000269|PubMed:10229190, CC ECO:0000269|PubMed:20836565}. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X51661; CAA35972.1; -; Genomic_DNA. DR PIR; S11885; S11885. DR RefSeq; WP_000278088.1; NZ_WJTW01000001.1. DR PDB; 1JCK; X-ray; 3.50 A; B/D=28-266. DR PDB; 1JWM; X-ray; 2.70 A; D=28-266. DR PDB; 1JWS; X-ray; 2.60 A; D=28-266. DR PDB; 1JWU; X-ray; 2.30 A; D=28-266. DR PDB; 1KLG; X-ray; 2.40 A; D=28-266. DR PDB; 1KLU; X-ray; 1.93 A; D=28-266. DR PDB; 1SJE; X-ray; 2.45 A; D=28-266. DR PDB; 1SJH; X-ray; 2.25 A; D=28-266. DR PDB; 1T5X; X-ray; 2.50 A; D=28-266. DR PDB; 2AQ1; X-ray; 2.10 A; B/D/F/H=28-266. DR PDB; 2AQ2; X-ray; 1.80 A; B=28-266. DR PDB; 2AQ3; X-ray; 2.30 A; B/D/F/H=28-266. DR PDB; 2IPK; X-ray; 2.30 A; D=28-266. DR PDB; 3BVG; X-ray; 2.00 A; A=28-266. DR PDB; 3BVM; X-ray; 2.00 A; A=28-266. DR PDB; 3BVZ; X-ray; 2.30 A; A=28-266. DR PDB; 3BYT; X-ray; 2.30 A; B/D/F/H=28-266. DR PDB; 3BYY; X-ray; 2.20 A; B=28-266. DR PDB; 3BZD; X-ray; 2.30 A; B=28-266. DR PDBsum; 1JCK; -. DR PDBsum; 1JWM; -. DR PDBsum; 1JWS; -. DR PDBsum; 1JWU; -. DR PDBsum; 1KLG; -. DR PDBsum; 1KLU; -. DR PDBsum; 1SJE; -. DR PDBsum; 1SJH; -. DR PDBsum; 1T5X; -. DR PDBsum; 2AQ1; -. DR PDBsum; 2AQ2; -. DR PDBsum; 2AQ3; -. DR PDBsum; 2IPK; -. DR PDBsum; 3BVG; -. DR PDBsum; 3BVM; -. DR PDBsum; 3BVZ; -. DR PDBsum; 3BYT; -. DR PDBsum; 3BYY; -. DR PDBsum; 3BZD; -. DR AlphaFoldDB; P0A0L5; -. DR SMR; P0A0L5; -. DR Allergome; 2141; Sta a SEC. DR OMA; KFTGLME; -. DR EvolutionaryTrace; P0A0L5; -. DR PRO; PR:P0A0L5; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.110; -; 1. DR Gene3D; 3.10.20.120; -; 1. DR InterPro; IPR008992; Enterotoxin. DR InterPro; IPR006126; Staph/Strept_toxin_CS. DR InterPro; IPR006173; Staph_tox_OB. DR InterPro; IPR016091; SuperAg_toxin_C. DR InterPro; IPR013307; Superantigen_bac. DR InterPro; IPR006123; Toxin_b-grasp_Staph/Strep. DR InterPro; IPR006177; Toxin_bac. DR Pfam; PF02876; Stap_Strp_tox_C; 1. DR Pfam; PF01123; Stap_Strp_toxin; 1. DR PRINTS; PR00279; BACTRLTOXIN. DR PRINTS; PR01898; SAGSUPRFAMLY. DR SUPFAM; SSF50203; Bacterial enterotoxins; 1. DR SUPFAM; SSF54334; Superantigen toxins, C-terminal domain; 1. DR PROSITE; PS00277; STAPH_STREP_TOXIN_1; 1. DR PROSITE; PS00278; STAPH_STREP_TOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Enterotoxin; Metal-binding; Secreted; Signal; KW Superantigen; Toxin; Virulence; Zinc. FT SIGNAL 1..27 FT CHAIN 28..266 FT /note="Enterotoxin type C-3" FT /id="PRO_0000035611" FT BINDING 36 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:20836565, ECO:0000269|Ref.6, FT ECO:0007744|PDB:3BVG, ECO:0007744|PDB:3BVM, FT ECO:0007744|PDB:3BVZ" FT BINDING 110 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:20836565, ECO:0000269|Ref.6, FT ECO:0007744|PDB:3BVG, ECO:0007744|PDB:3BVM, FT ECO:0007744|PDB:3BVZ" FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:20836565, ECO:0000269|Ref.6, FT ECO:0007744|PDB:3BVG, ECO:0007744|PDB:3BVM, FT ECO:0007744|PDB:3BVZ" FT BINDING 149 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:20836565, ECO:0000269|Ref.6, FT ECO:0007744|PDB:3BVG, ECO:0007744|PDB:3BVM, FT ECO:0007744|PDB:3BVZ" FT DISULFID 120..137 FT /evidence="ECO:0000269|PubMed:12962633, FT ECO:0000269|PubMed:20836565, ECO:0000269|PubMed:8906797, FT ECO:0000269|Ref.6, ECO:0007744|PDB:1JCK, FT ECO:0007744|PDB:1JWM, ECO:0007744|PDB:1JWS, FT ECO:0007744|PDB:1JWU, ECO:0007744|PDB:3BVG, FT ECO:0007744|PDB:3BVM, ECO:0007744|PDB:3BVZ, FT ECO:0007744|PDB:3BYT, ECO:0007744|PDB:3BYY, FT ECO:0007744|PDB:3BZD" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:2AQ2" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:2AQ2" FT HELIX 49..52 FT /evidence="ECO:0007829|PDB:2AQ2" FT TURN 53..55 FT /evidence="ECO:0007829|PDB:2AQ2" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:2AQ2" FT STRAND 69..72 FT /evidence="ECO:0007829|PDB:3BZD" FT STRAND 75..78 FT /evidence="ECO:0007829|PDB:2AQ2" FT STRAND 83..94 FT /evidence="ECO:0007829|PDB:2AQ2" FT HELIX 98..104 FT /evidence="ECO:0007829|PDB:2AQ2" FT STRAND 109..113 FT /evidence="ECO:0007829|PDB:2AQ2" FT STRAND 122..124 FT /evidence="ECO:0007829|PDB:2AQ2" FT STRAND 134..139 FT /evidence="ECO:0007829|PDB:2AQ2" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:2AQ2" FT TURN 146..148 FT /evidence="ECO:0007829|PDB:3BZD" FT TURN 151..153 FT /evidence="ECO:0007829|PDB:1KLU" FT STRAND 156..164 FT /evidence="ECO:0007829|PDB:2AQ2" FT STRAND 167..182 FT /evidence="ECO:0007829|PDB:2AQ2" FT HELIX 183..198 FT /evidence="ECO:0007829|PDB:2AQ2" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:1JWU" FT STRAND 207..216 FT /evidence="ECO:0007829|PDB:2AQ2" FT TURN 218..220 FT /evidence="ECO:0007829|PDB:3BZD" FT STRAND 222..226 FT /evidence="ECO:0007829|PDB:2AQ2" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:2AQ2" FT HELIX 237..241 FT /evidence="ECO:0007829|PDB:2AQ2" FT HELIX 242..246 FT /evidence="ECO:0007829|PDB:2AQ2" FT STRAND 249..251 FT /evidence="ECO:0007829|PDB:2AQ2" FT TURN 252..254 FT /evidence="ECO:0007829|PDB:2AQ2" FT STRAND 256..263 FT /evidence="ECO:0007829|PDB:2AQ2" SQ SEQUENCE 266 AA; 30671 MW; 5ED8A32D11FFCA59 CRC64; MYKRLFISRV ILIFALILVI STPNVLAESQ PDPMPDDLHK SSEFTGTMGN MKYLYDDHYV SATKVKSVDK FLAHDLIYNI SDKKLKNYDK VKTELLNEDL AKKYKDEVVD VYGSNYYVNC YFSSKDNVGK VTGGKTCMYG GITKHEGNHF DNGNLQNVLV RVYENKRNTI SFEVQTDKKS VTAQELDIKA RNFLINKKNL YEFNSSPYET GYIKFIENNG NTFWYDMMPA PGDKFDQSKY LMMYNDNKTV DSKSVKIEVH LTTKNG //