ID A0A2G8JT06_STIJA Unreviewed; 472 AA.
AC A0A2G8JT06;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Putative ficolin-2-like {ECO:0000313|EMBL:PIK38849.1};
GN ORFNames=BSL78_24315 {ECO:0000313|EMBL:PIK38849.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK38849.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK38849.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK38849.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK38849.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIK38849.1}.
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DR EMBL; MRZV01001307; PIK38849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8JT06; -.
DR STRING; 307972.A0A2G8JT06; -.
DR Proteomes; UP000230750; Unassembled WGS sequence.
DR CDD; cd19941; TIL; 1.
DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 3.
DR Gene3D; 2.10.25.10; Laminin; 2.
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 InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR NCBIfam; NF040941; GGGWT_bact; 2.
DR PANTHER; PTHR19143; FIBRINOGEN/TENASCIN/ANGIOPOEITIN; 1.
DR Pfam; PF00147; Fibrinogen_C; 2.
DR Pfam; PF01826; TIL; 1.
DR SMART; SM00186; FBG; 2.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 2.
DR SUPFAM; SSF57567; Serine protease inhibitors; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 3.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000230750}.
FT DOMAIN 34..170
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 298..346
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 347..472
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
SQ SEQUENCE 472 AA; 53793 MW; 60ECF8966BEF47B1 CRC64;
MSYTFLGRYF TAEAGTSDAA NSEDGPSSSA FFFYQQSTYP RDCKEVQEQC SSHNSTGVFM
IKPDGYLEPF EVYCDGTDTS GGWTVIQRRI DGSIDFGRDW DSYKTGFGFL SREFWLGNEK
LSFLTNQKKY QLVIDMTTSN GSLIRVSYDH FRISDAFSYF KLVNLGLYSG ETDVVTLCPT
NMVYTNCSTA CQRTCEAPGI CQDDVCTEVE ACVCRDGYFL LGSDCVPREQ CGCYESEGQT
IVPEGEFNVN PRCTRKGVCT DGQISWDETY ACSPNAVCDV RNDIRRCYCT GGYRGDGEVC
ERPPKDCQEI YEDGTSDNGI YRIEPTGWTG EAFEVYCNMT DGGGWTRYEI RIDLVNKEGA
PYYAKFDFFR INDESDNYRL SGVGTYSGTA DQRSNPDGYA LTYHRNYQFS TKDETMMLYS
GNCATYYLGA WWYNNCYYSN LNGRYGHSYF YWYYLPGSDN YLQFVEMKIR PV
//