ID   FBCD1_XENTR             Reviewed;         457 AA.
AC   Q0P4P2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Fibrinogen C domain-containing protein 1;
GN   Name=fibcd1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acetyl group-binding receptor which shows a calcium-dependent
CC       binding to acetylated structures such as chitin, some N-acetylated
CC       carbohydrates, and amino acids. {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer; disulfide-linked. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
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DR   EMBL; BC121964; AAI21965.1; -; mRNA.
DR   RefSeq; NP_001072519.1; NM_001079051.1.
DR   AlphaFoldDB; Q0P4P2; -.
DR   SMR; Q0P4P2; -.
DR   STRING; 8364.ENSXETP00000011091; -.
DR   PaxDb; Q0P4P2; -.
DR   DNASU; 779974; -.
DR   GeneID; 779974; -.
DR   KEGG; xtr:779974; -.
DR   CTD; 84929; -.
DR   Xenbase; XB-GENE-483361; fibcd1.
DR   eggNOG; KOG2579; Eukaryota.
DR   InParanoid; Q0P4P2; -.
DR   OrthoDB; 523014at2759; -.
DR   Proteomes; UP000008143; Chromosome 8.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000001469; Expressed in brain and 1 other tissue.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   CDD; cd00087; FReD; 1.
DR   Gene3D; 3.90.215.10; -; 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   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   2: Evidence at transcript level;
KW   Calcium; Chitin-binding; Disulfide bond; Glycoprotein; Membrane;
KW   Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..457
FT                   /note="Fibrinogen C domain-containing protein 1"
FT                   /id="PRO_0000294320"
FT   TOPO_DOM        1..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..457
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          231..454
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         389
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         391
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            401
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250"
FT   SITE            411
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250"
FT   SITE            427
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250"
FT   SITE            428
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        240..269
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        397..410
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ   SEQUENCE   457 AA;  50966 MW;  16F2E2C0BB45651C CRC64;
     MGSDRWKNIG GAPQMEDSVQ DKSQRKGCGY ILCTVLLSVA VLLAVTVTGA VLFMNHYHAP
     STEPPPVITT NMEDPNALVT IERADSSHIN IFIDPNCPDP FPRLEGLQSA LLSALADHDS
     EQKVAGGKER ALLTSLSDQV AQMVSQVARQ RADWENVKKV QNGLGAEIGA LKNEQGRLIK
     LLSEGQSHVA QLGSSVSEVL ETVQRELGSG RPRVKADLQR APSRSSRPRG CANGSKPRDC
     YDIYMSGQQE DGVYSVFPIH YPSGFQVFCD MTTDGGGWTV FQRREDGSVN FFQGWEQYRD
     GFGKLTGEHW LGLQRIHLLT MQTHYQLRID LEDFENATAY ALYNTFGVGL FSVNPEEDGY
     PITISDYTGT AGDSLGKHSG MKFTTKDMDN DHSENNCASF YHGAWWYRNC HTSNLNGQYL
     RGHHASYADG IEWSSWTGWQ YSLKFTEMKI RPQREEN