ID   FCNV4_CERRY             Reviewed;         345 AA.
AC   D8VNT0;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Ryncolin-4;
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; GU065326; ADJ51065.1; -; mRNA.
DR   AlphaFoldDB; D8VNT0; -.
DR   SMR; D8VNT0; -.
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-4"
FT                   /id="PRO_0000414921"
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;  38323 MW;  BC8A77D69A97A253 CRC64;
     MKPWAAFHLI FLVASSLEGE VSNYGTRGAQ DTEPTCRTEH QCTRDKIILQ SQPGIPGIPG
     VPGTNGSEGL KGDPGPQGPP GIRGPDGIRG EAGPKGDKGD QGDKGDKGDK GDKGEDCNLD
     DCLPTEVRNC QDLLERGETL NGWYKIYPTE EVSMLVFCDM STDGGGWLVF QRRQDGSVNF
     YREWESYKKG FGRQGSEFWL GNDKIHLLTN SGTQQLRIDL ADFENIHTFA TYSSFSIGNE
     TEKYKLTLGS HLDGNMGDSL TLQNGRSFST KDRDNDVSHI HCAVNFKGAW WYRKCHESNL
     NGLYHKGKHA TYANGINWLT GKGYHYSYKY ADMKIRPQKS ETTVS