ID Q9DJY8_9ENTO PRELIMINARY; PRT; 233 AA. AC Q9DJY8; DT 01-MAR-2001 (TrEMBLrel. 16, Created) DT 01-MAR-2001 (TrEMBLrel. 16, Last sequence update) DT 01-MAR-2004 (TrEMBLrel. 26, Last annotation update) DE Polyprotein (Fragment). OS Human coxsackievirus A20. OC Viruses; ssRNA positive-strand viruses, no DNA stage; Picornaviridae; OC Enterovirus. OX NCBI_TaxID=42782; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=21064585; PubMed=11125161; RA Caro V., Guillot S., Delpeyroux F., Crainic R.; RT "Molecular strategy for 'serotyping' of human enteroviruses."; RL J. Gen. Virol. 82:79-91(2001). CC -!- FUNCTION: P2A and P3C polypeptides are cysteine proteases that CC cleave at certain Gln-|-Gly and Tyr-|-Gly sites in the polyprotein CC (By similarity). CC -!- FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as CC a proteolytic factor in a variety of other processes including CC embryonic development, tissue remodeling, tumor invasion, and CC inflammation; in ovulation it weakens the walls of the Graafian CC follicle. It activates the urokinase-type plasminogen activator, CC collagenases and several complement zymogens, such as C1 and C5. CC It cleaves fibrin, fibronectin, thrombospondin, laminin and von CC Willebrand factor (By similarity). CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- CATALYTIC ACTIVITY: Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; CC higher selectivity than trypsin. Converts fibrin into soluble CC products. CC -!- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the CC poliovirus polyprotein. In other picornavirus reactions Glu may be CC substituted for Gln, and Ser or Thr for Gly. CC -!- CATALYTIC ACTIVITY: Selective cleavage of Tyr-|-Gly bond in the CC picornavirus polyprotein. CC -!- SUBUNIT: The virus capsid is composed of 60 icosahedral units, CC each of which is composed of one copy each of proteins VP1, VP2, CC VP3, and VP4 (By similarity). 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; AJ279184; CAC08133.1; -. DR HSSP; P03300; 2PLV. DR MEROPS; C03.020; -. DR GO; GO:0019028; C:viral capsid; IEA. DR GO; GO:0008233; F:peptidase activity; IEA. DR GO; GO:0005198; F:structural molecule activity; IEA. DR InterPro; IPR000081; Peptidase_C3. DR InterPro; IPR011565; Peptidase_C3_2. DR InterPro; IPR001676; Rhv. DR Pfam; PF00947; Pico_P2A; 1. DR Pfam; PF00073; Rhv; 1. DR ProDom; PD001306; Peptidase_C3_2; 1. KW Capsid protein; Core protein; Fibrinolysis; Hydrolase; Polyprotein; KW Protease; RNA replication; RNA-directed RNA polymerase; KW Thiol protease; Tissue remodeling; Transferase. FT NON_TER 1 1 FT CHAIN <1 107 VP1 protein. FT CHAIN 108 >233 2A protein. FT NON_TER 233 233 SQ SEQUENCE 233 AA; 25697 MW; D1058CA9CDDFB6ED CRC64; IPYVGIANAY SNFYDGCATV PIEGETTDPC AAYYGATSIN DFGILAVRVV NEHNPVQVSS KIRVYMKPKH VRVWCPRPPR AVPYFGPGVD YKGDALTPLS TKSLTTYGFG HQNKAVYTAG YKICNYHLAT QEDLSNAVNV MWNRDLLVTE SKAQGTDSIA RCTCNAGVYY CESRRKYYPV SFIGPTFQYM EANDYYPARY QSHMLIGYGF ASPGDCGGIL RCQHGVIGII TAG //