ID   FCNV1_VARKO             Reviewed;         221 AA.
AC   E2IYB3;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Veficolin-1;
DE   Flags: Precursor; Fragment;
OS   Varanus komodoensis (Komodo dragon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Anguimorpha; Paleoanguimorpha; Varanoidea; Varanidae; Varanus.
OX   NCBI_TaxID=61221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=20631207; DOI=10.1074/mcp.m110.001370;
RA   Fry B.G., Winter K., Norman J.A., Roelants K., Nabuurs R.J., van Osch M.J.,
RA   Teeuwisse W.M., van der Weerd L., McNaughtan J.E., Kwok H.F., Scheib H.,
RA   Greisman L., Kochva E., Miller L.J., Gao F., Karas J., Scanlon D., Lin F.,
RA   Kuruppu S., Shaw C., Wong L., Hodgson W.C.;
RT   "Functional and structural diversification of the Anguimorpha lizard venom
RT   system.";
RL   Mol. Cell. Proteomics 9:2369-2390(2010).
CC   -!- FUNCTION: Initiates complement activation and/or interferes in platelet
CC       aggregation and/or blood coagulation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the mandibular venom duct.
CC   -!- SIMILARITY: Belongs to the ficolin lectin family. Veficolin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; HM641898; ADK46899.1; -; mRNA.
DR   AlphaFoldDB; E2IYB3; -.
DR   SMR; E2IYB3; -.
DR   Proteomes; UP000694545; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.215.10; -; 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   Pfam; PF01391; Collagen; 1.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   SMART; SM00186; FBG; 1.
DR   SUPFAM; SSF56496; SSF56496; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE   2: Evidence at transcript level;
KW   Complement system impairing toxin; Disulfide bond;
KW   Hemostasis impairing toxin; Reference proteome; Secreted; Signal; Toxin.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..>221
FT                   /note="Veficolin-1"
FT                   /id="PRO_0000414109"
FT   DOMAIN          50..104
FT                   /note="Collagen-like"
FT   DOMAIN          111..>221
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   REGION          54..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        120..148
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   NON_TER         221
SQ   SEQUENCE   221 AA;  23486 MW;  FDC93F097A45771F CRC64;
     MTAWLDFPLA LSPLVVVSMK GGSFGQGSEA NGSPQLTGLS ECGADRIFLQ GQAGIPGIPG
     VPGTNGLPGA KGDLGPQGPP GERGSTGIPG KAGPKGDKGD QGEACSLASC QQQEAGAKDC
     KELLDRGETL TGWYMIYPTT GRGMRAYCDM ETDGGGWLVF QRRLDGSVDF YRDWEAYKKG
     FGRQVSEFWL GNDKIHLLTS SGIQQLRIDV EDFNNSKTFA K