ID   SL117_ECHCA             Reviewed;          30 AA.
AC   Q9PRP8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Snaclec carinactivase-1 regulatory subunit 17 kDa chain;
DE            Short=CA-1 17 kDa subunit;
DE   AltName: Full=CA-1 25 kDa subunit chain 2;
DE   Flags: Fragment;
OS   Echis carinatus (Saw-scaled viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX   NCBI_TaxID=40353;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=8617803; DOI=10.1074/jbc.271.9.5200;
RA   Yamada D., Sekiya F., Morita T.;
RT   "Isolation and characterization of carinactivase, a novel prothrombin
RT   activator in Echis carinatus venom with a unique catalytic mechanism.";
RL   J. Biol. Chem. 271:5200-5207(1996).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=10336237; DOI=10.1016/s0049-3848(98)00212-6;
RA   Yamada D., Morita T.;
RT   "CA-1 method, a novel assay for quantification of normal prothrombin using
RT   a Ca2+ -dependent prothrombin activator, carinactivase-1.";
RL   Thromb. Res. 94:221-226(1999).
CC   -!- FUNCTION: Calcium-dependent prothrombin activator. This protein may
CC       activate prothrombin via recognition by the regulatory subunit of the
CC       calcium ion bound conformation of its gamma-carboxyglutamic acid (GLA)
CC       domain, and the subsequent conversion of prothrombin to active thrombin
CC       is catalyzed by the catalytic subunit. {ECO:0000269|PubMed:8617803}.
CC   -!- SUBUNIT: Heterodimer of a metalloproteinase subunit and a regulatory
CC       subunit comprising two polypeptides disulfide-linked (14 kDa and 17 kDa
CC       chains). {ECO:0000269|PubMed:8617803}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- BIOTECHNOLOGY: Used for quantification of normal prothrombin (CA-1
CC       method). {ECO:0000269|PubMed:10336237}.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   AlphaFoldDB; Q9PRP8; -.
DR   SMR; Q9PRP8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   SUPFAM; SSF56436; SSF56436; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade activating toxin; Calcium;
KW   Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Hemostasis impairing toxin; Prothrombin activator; Secreted; Toxin.
FT   CHAIN           1..>30
FT                   /note="Snaclec carinactivase-1 regulatory subunit 17 kDa
FT                   chain"
FT                   /id="PRO_0000326261"
FT   DOMAIN          1..>30
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        2..13
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   NON_TER         30
SQ   SEQUENCE   30 AA;  3582 MW;  21C190F0EBC0D8FE CRC64;
     DCLPGWSSHE GHCYKVFNQE MYWADAEKFC