ID   FCNV2_CERRY             Reviewed;         347 AA.
AC   D8VNS8;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Ryncolin-2;
DE   Flags: Precursor;
OS   Cerberus rynchops (Dog-faced water snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Homalopsidae; Cerberus.
OX   NCBI_TaxID=46267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   HYDROXYLATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=20158271; DOI=10.1021/pr901044x;
RA   Ompraba G., Chapeaurouge A., Doley R., Devi K.R., Padmanaban P.,
RA   Venkatraman C., Velmurugan D., Lin Q., Kini R.M.;
RT   "Identification of a novel family of snake venom proteins Veficolins from
RT   Cerberus rynchops using a venom gland transcriptomics and proteomics
RT   approach.";
RL   J. Proteome Res. 9:1882-1893(2010).
CC   -!- FUNCTION: Initiates complement activation and/or interferes in platelet
CC       aggregation and/or blood coagulation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- PTM: Hydroxylated, possibly at Pro-74 and Pro-94.
CC       {ECO:0000269|PubMed:20158271}.
CC   -!- SIMILARITY: Belongs to the ficolin lectin family. Veficolin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; GU065324; ADJ51063.1; -; mRNA.
DR   AlphaFoldDB; D8VNS8; -.
DR   SMR; D8VNS8; -.
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; -; 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   Pfam; PF01391; Collagen; 1.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   SMART; SM00186; FBG; 1.
DR   SUPFAM; SSF56496; SSF56496; 1.
DR   PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE   1: Evidence at protein level;
KW   Complement system impairing toxin; Disulfide bond;
KW   Hemostasis impairing toxin; Hydroxylation; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..347
FT                   /note="Ryncolin-2"
FT                   /id="PRO_0000414919"
FT   DOMAIN          57..114
FT                   /note="Collagen-like"
FT   DOMAIN          121..341
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   REGION          49..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        132..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        284..297
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ   SEQUENCE   347 AA;  38681 MW;  2C6AB9DC2FB759C1 CRC64;
     MKPWAAFHLI FLVASSLEGE VSNYGTRGAQ DTEPTCRTEH QCTRDKIILQ SQPGIPGIPG
     VPGINGSEGL KGDPGPQGLP GETGFDGIPG VAGPKGDKGD QGDKGDKGDK GDKGDACILD
     DCPPTDVEVR NCQDLLEHGE ILNGWYTIYP TKENPMVVFC DMETDGGGWL VFQRRQDGSV
     DFYLDWESYK KGFGKQESEF WLGNDKIHLL TSSGTQQLRI DLEDFEGSRT FAKYSSFSIG
     DENEKYRLIV GSYLDGSMND SFRIHNGHSF STKDRDNDTN KGNCAMMYKG AWWYFHCHHA
     NLNGLYYKGK HANYADGINW RSGKGYYYSY KYADMKIRPQ QSETTVS