VSPCA_AGKCO
ID VSPCA_AGKCO Reviewed; 231 AA.
AC P09872;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein C activator;
DE EC=3.4.21.-;
DE AltName: Full=ACC-C;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
OS Agkistrodon contortrix contortrix (Southern copperhead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX NCBI_TaxID=8713;
RN [1]
RP PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-21; ASN-78 AND ASN-129.
RC TISSUE=Venom;
RX PubMed=2653426; DOI=10.1021/bi00428a039;
RA McMullen B.A., Fujikawa K., Kisiel W.;
RT "Primary structure of a protein C activator from Agkistrodon contortrix
RT contortrix venom.";
RL Biochemistry 28:674-679(1989).
RN [2]
RP PROTEIN SEQUENCE OF 1-63, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=3624272; DOI=10.1016/s0021-9258(18)45249-0;
RA Kisiel W., Kondo S., Smith K.J., McMullen B.A., Smith L.F.;
RT "Characterization of a protein C activator from Agkistrodon contortrix
RT contortrix venom.";
RL J. Biol. Chem. 262:12607-12613(1987).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS), ACTIVE SITE, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-21; ASN-78 AND ASN-129.
RX PubMed=16162508; DOI=10.1074/jbc.m508502200;
RA Murakami M.T., Arni R.K.;
RT "Thrombomodulin-independent activation of protein C and specificity of
RT hemostatically active snake venom serine proteinases: crystal structures of
RT native and inhibited Agkistrodon contortrix contortrix protein C
RT activator.";
RL J. Biol. Chem. 280:39309-39315(2005).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=11910194; DOI=10.1159/000048072;
RA Gempeler-Messina P.M., Volz K., Buhler B., Muller C.;
RT "Protein C activators from snake venoms and their diagnostic use.";
RL Haemostasis 31:266-272(2001).
CC -!- FUNCTION: Snake venom serine protease that selectively cleaves the
CC heavy chain of protein C (PROC). This activation is thrombomodulin-
CC independent. {ECO:0000269|PubMed:3624272}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- BIOTECHNOLOGY: Is used in diagnostic practice for the determination of
CC disorders in the PC pathway. Functional assays are either clotting
CC assays or based on determinations using chromogenic assays. Sold under
CC the name Protac by Pentapharm. {ECO:0000269|PubMed:11910194}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR PIR; A60468; A60468.
DR PDB; 2AIP; X-ray; 1.65 A; A=1-231.
DR PDB; 2AIQ; X-ray; 1.54 A; A=1-231.
DR PDBsum; 2AIP; -.
DR PDBsum; 2AIQ; -.
DR AlphaFoldDB; P09872; -.
DR SMR; P09872; -.
DR MEROPS; S01.466; -.
DR iPTMnet; P09872; -.
DR EvolutionaryTrace; P09872; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation cascade inhibiting toxin;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Protease; Secreted; Serine protease;
KW Toxin.
FT CHAIN 1..231
FT /note="Protein C activator"
FT /id="PRO_0000088726"
FT DOMAIN 1..222
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 40
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:16162508"
FT ACT_SITE 85
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:16162508"
FT ACT_SITE 177
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:16162508"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16162508,
FT ECO:0000269|PubMed:2653426"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16162508,
FT ECO:0000269|PubMed:2653426"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16162508,
FT ECO:0000269|PubMed:2653426"
FT DISULFID 7..138
FT /evidence="ECO:0000269|PubMed:16162508,
FT ECO:0007744|PDB:2AIP, ECO:0007744|PDB:2AIQ"
FT DISULFID 25..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:16162508, ECO:0007744|PDB:2AIP,
FT ECO:0007744|PDB:2AIQ"
FT DISULFID 73..229
FT /evidence="ECO:0000269|PubMed:16162508,
FT ECO:0007744|PDB:2AIP, ECO:0007744|PDB:2AIQ"
FT DISULFID 117..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:16162508, ECO:0007744|PDB:2AIP,
FT ECO:0007744|PDB:2AIQ"
FT DISULFID 149..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:16162508, ECO:0007744|PDB:2AIP,
FT ECO:0007744|PDB:2AIQ"
FT DISULFID 173..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:16162508, ECO:0007744|PDB:2AIP,
FT ECO:0007744|PDB:2AIQ"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:2AIQ"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:2AIQ"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:2AIQ"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2AIQ"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:2AIQ"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2AIQ"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:2AIQ"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2AIQ"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:2AIQ"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:2AIQ"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:2AIQ"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:2AIQ"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:2AIQ"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:2AIQ"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:2AIQ"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:2AIQ"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:2AIQ"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:2AIQ"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:2AIQ"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:2AIQ"
SQ SEQUENCE 231 AA; 25106 MW; DC3D7CBE601EC52B CRC64;
VIGGDECNIN EHRFLALVYA NGSLCGGTLI NQEWVLTARH CDRGNMRIYL GMHNLKVLNK
DALRRFPKEK YFCLNTRNDT IWDKDIMLIR LNRPVRNSAH IAPLSLPSNP PSVGSVCRIM
GWGTITSPNA TLPDVPHCAN INILDYAVCQ AAYKGLAATT LCAGILEGGK DTCKGDSGGP
LICNGQFQGI LSVGGNPCAQ PRKPGIYTKV FDYTDWIQSI ISGNTDATCP P
