ID   FBCDA_XENLA             Reviewed;         457 AA.
AC   Q6AX44;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Fibrinogen C domain-containing protein 1-A;
GN   Name=fibcd1-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) 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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
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DR   EMBL; BC079767; AAH79767.1; -; mRNA.
DR   RefSeq; NP_001087425.1; NM_001093956.1.
DR   AlphaFoldDB; Q6AX44; -.
DR   SMR; Q6AX44; -.
DR   DNASU; 447249; -.
DR   GeneID; 447249; -.
DR   KEGG; xla:447249; -.
DR   CTD; 447249; -.
DR   Xenbase; XB-GENE-864972; fibcd1.L.
DR   OrthoDB; 523014at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 447249; Expressed in brain and 7 other tissues.
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   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-A"
FT                   /id="PRO_0000294318"
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          216..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;  51009 MW;  2977C7AE0B50F67C CRC64;
     MGSDRWKNIG GTPQMEDSAQ EKTQRKGCGY ILCTVLLSVA VLLAVTVTGA VLFMNHYHAP
     STEPPPVITT NMEDPNALVT IERADSSHIN IFIDPNCPDP FPRLDGLQSA LLSALADHDS
     EQKVAGGKER VLLTSLSDQV AQMVSQVARQ RADWEIVKKV QNGLGAEIGA LKNEQGRLIK
     LLSEGQSHVV QLGSSVSEVL ETVQRELGSG RPRLKADLQR APSRNSRPRG CANGSKPRDC
     YDIYMSGQQE DGVYSVFPIH YPSGFQVFCD MTTDGGGWTV FQRREDGSVN FFQGWEQYRD
     GFGKLTGEHW LGLQRIHLLT MQTHYQLRID LEDFENATAY ALYNTFGVGL FSVNPEEDGY
     PITVSDYTGT AGDSLGKHSG MKFTTKDMDN DHSENNCASF YHGAWWYRNC HTSNLNGQYL
     TGHHASYADG IEWSSWTGWQ YSLKFTEMKI RPQREEN