ID M9T1P5_CYLRU Unreviewed; 329 AA.
AC M9T1P5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Veficolin-Cyl-1 {ECO:0000313|EMBL:AGI97189.1};
OS Cylindrophis ruffus (Red-tailed pipe snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Henophidia; Cylindrophiidae; Cylindrophis.
OX NCBI_TaxID=186578 {ECO:0000313|EMBL:AGI97189.1};
RN [1] {ECO:0000313|EMBL:AGI97189.1}
RP NUCLEOTIDE SEQUENCE.
RA Fry B.G., Undheim E.A.B., Ali S.A., Debono J., Scheib H., Ruder T.,
RA Jackson T.N.W., Morgenstern D., Cadwallader L., Whitehead D., Nabuurs R.,
RA van der Weerd L., Vidal N., Roelants K., Hendrikx I., Pineda Gonzalez S.,
RA Jones A., King G.F., Antunes A., Sunagar K.;
RT "Squeezers and leaf-cutters: differential diversification and degeneration
RT of the venom system in toxicoferan reptiles.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Initiates complement activation and/or interferes in platelet
CC aggregation and/or blood coagulation. {ECO:0000256|ARBA:ARBA00003654}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the ficolin lectin family. Veficolin subfamily.
CC {ECO:0000256|ARBA:ARBA00006932}.
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DR EMBL; JX467168; AGI97189.1; -; mRNA.
DR AlphaFoldDB; M9T1P5; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR020837; Fibrinogen_CS.
DR NCBIfam; NF040941; GGGWT_bact; 1.
DR PANTHER; PTHR19143; FIBRINOGEN/TENASCIN/ANGIOPOEITIN; 1.
DR PANTHER; PTHR19143:SF449; FICOLIN (COLLAGEN_FIBRINOGEN DOMAIN CONTAINING) 3 (HAKATA ANTIGEN); 1.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 2: Evidence at transcript level;
KW Complement system impairing toxin {ECO:0000256|ARBA:ARBA00023220};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hemostasis impairing toxin {ECO:0000256|ARBA:ARBA00023240};
KW Signal {ECO:0000256|SAM:SignalP}; Toxin {ECO:0000256|ARBA:ARBA00022656}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..329
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004102498"
FT DOMAIN 112..329
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT REGION 56..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 329 AA; 36344 MW; 4F18E4A4E178517A CRC64;
MRPWAGFHLI FLVALCVERE VLGQDTEANC CAQLKGLTQC GGDKIILQGQ AGIPGIPGVP
GTNGSPGLKG DLGPQGPPGE RGSAGMTGKA GPKGDKGDKG DACSLDNVAN CQQKGTEARN
CKDLLERGET LSGWHTIYPT KGNPMMVFCD METDGGGWLV FQRRRDGSVD FYRDWESYKK
GFGSFESEFW LGNDKIHLLT SNETQQLWID LEDFNSSRTF AKYSSFRIAN ENQKYRLMVG
SYLDGNMGDS FSGHNNQAFS TKDRDNDIYD GNCAVSFKGA WWYSKCHSSN LNGLYHKGEH
TSYADGINWS AGKGQYYSYK YADMKIRPQ
//
