ID   FCNV1_CERRY             Reviewed;         345 AA.
AC   D8VNS7;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Ryncolin-1;
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-80. {ECO:0000269|PubMed:20158271}.
CC   -!- SIMILARITY: Belongs to the ficolin lectin family. Veficolin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; GU065323; ADJ51062.1; -; mRNA.
DR   AlphaFoldDB; D8VNS7; -.
DR   SMR; D8VNS7; -.
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..345
FT                   /note="Ryncolin-1"
FT                   /id="PRO_0000414918"
FT   DOMAIN          57..114
FT                   /note="Collagen-like"
FT   DOMAIN          121..339
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   REGION          48..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        130..158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        282..295
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ   SEQUENCE   345 AA;  38464 MW;  9D9EE0CE720CA805 CRC64;
     MKPWAAFHLI FLVASSLEGE VSNYGTGGTQ DTEPTCRTEH QCTRDKIILQ SQPGIPGIPG
     VPGTNGSEGL KGDPGPQGPP GIRGPDGIRG EAGPKGDKGD QGDKGDKGDK GDKGEDCNLD
     GCLPTEVRNC QDLLEHGEIL NGWYTIYPTK ENPMVVFCDM ETDGGGWLVF QRRQDGSVDF
     YLDWESYKKG FGKQESEFWL GNDKIHLLTS SGTQQLRIDL EDFEGSRTFA KYSSFSIGDE
     NEKYRLIVGS YLDGSMNDSF RIHNGHSFST KDRDNDTNKG NCAMMYKGAW WYFHCHHANL
     NGLYYKGKHA NYADGINWRS GKGYYYSYKY ADMKIRPQQS ETTVS