ID W8BTX1_CERCA Unreviewed; 340 AA.
AC W8BTX1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=(Mediterranean fruit fly) hypothetical protein {ECO:0000313|EMBL:CAD6998842.1};
DE SubName: Full=Fibrinogen C domain-containing protein 1 {ECO:0000313|EMBL:JAC04801.1};
GN Name=FBCD1 {ECO:0000313|EMBL:JAC04801.1};
GN ORFNames=CCAP1982_LOCUS7391 {ECO:0000313|EMBL:CAD6998842.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAC04801.1};
RN [1] {ECO:0000313|EMBL:JAC04801.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAC04801.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
RN [3] {ECO:0000313|EMBL:CAD6998842.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EGII {ECO:0000313|EMBL:CAD6998842.1};
RA Whitehead M.;
RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
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; CAJHJT010000012; CAD6998842.1; -; Genomic_DNA.
DR EMBL; GAMC01001755; JAC04801.1; -; mRNA.
DR AlphaFoldDB; W8BTX1; -.
DR Proteomes; UP000606786; Unassembled WGS sequence.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
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 PANTHER; PTHR19143:SF327; FI21813P1-RELATED; 1.
DR PANTHER; PTHR19143; FIBRINOGEN/TENASCIN/ANGIOPOEITIN; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000606786};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..340
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033708399"
FT DOMAIN 112..338
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
SQ SEQUENCE 340 AA; 38962 MW; 09D4947ECFF284A3 CRC64;
MAYLAVITLL TLSALCLHIA TCLPQNQLSS SGNVSPFITY LCDDDLLKTT SNKMDLLNLK
FENHNLRLQS DFNAMREQLL REIKTNLELM ELKAKNVCTE QCKSNEVIPP PPPLLKAAST
CAEAMLKPNG EYAPSGVYEL YLPEYLPQPF SVYCLQDTDG GGPWTIIQRR QNNDTDFYRG
WYEYVNGFGD LESNFWLGLD KIYALTQSHM YNLWFQLENF QNEKRYAKYE SFAIDGASGK
YALSVLGEFS GTAGDSFTPH RGEKFTTKDS DNDQWGENCA KQYTGAWWYQ KCHASNLNGL
YYGGEFPKDQ YAKGVVWHSW LGHYYSLKYV HMAMRPRKLL
//