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 26-FEB-2020, entry version 29. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GU065323; ADJ51062.1; -; mRNA. DR SMR; D8VNS7; -. DR PRIDE; 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 Gene3D; 4.10.530.10; -; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR036056; Fibrinogen-like_C. DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1. DR InterPro; IPR014715; Fibrinogen_a/b/g_C_2. 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 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 //