ID   FBCDB_XENLA             Reviewed;         457 AA.
AC   Q5XK91;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Fibrinogen C domain-containing protein 1-B;
GN   Name=fibcd1-b;
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=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-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:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
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DR   EMBL; BC083021; AAH83021.1; -; mRNA.
DR   RefSeq; NP_001088141.1; NM_001094672.1.
DR   RefSeq; XP_018087538.1; XM_018232049.1.
DR   RefSeq; XP_018087539.1; XM_018232050.1.
DR   RefSeq; XP_018087540.1; XM_018232051.1.
DR   RefSeq; XP_018087541.1; XM_018232052.1.
DR   RefSeq; XP_018087542.1; XM_018232053.1.
DR   AlphaFoldDB; Q5XK91; -.
DR   SMR; Q5XK91; -.
DR   GeneID; 494847; -.
DR   KEGG; xla:494847; -.
DR   CTD; 494847; -.
DR   Xenbase; XB-GENE-6255067; fibcd1.S.
DR   OMA; PQRMSCG; -.
DR   OrthoDB; 523014at2759; -.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 494847; Expressed in camera-type eye and 13 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-B"
FT                   /id="PRO_0000294319"
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..21
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;  51037 MW;  926D5DB33703BBE1 CRC64;
     MGSDRWKNIR GTPQMEDSVQ EKSQRKGCGY ILCTVLLSVA VLLAVTVTGA VLFMNQYHAP
     STEPPPVITT NMEDPNALVT IERADSSHIN IFIDPNCPDT FPRLEGLQST MLSALADHDS
     EQKMAGGKER ALLTSLSDQV AQMVSQVARQ RADWENVKKV QNGLGTEIGA LKNEQGRLIK
     LLSEGQSHVA QLGSSVSEVL ETVQRELGSG RPRLKADLQR APSRSARPRG CANGSKPRDC
     YDIYMSGQQE DGVYSVFPIH YPSGFQVFCD MTTDGGGWTV FQRREDGSVN FFQGWEQYRD
     GFGKLTGEHW LGLQGIHLLT MQAHYQLRID LEDFDNATAY AVYNTFGVGL FSVNPEEDGY
     PITVSDYTGT AGDSLGKHSG MKFTTKDLDN DHSENNCATF YHGAWWYRNC HTSNLNGQYL
     RGHHASYADG IEWSSWTGWQ YSLKFTEMKI RPQREEN