ID   FBCD1_MACFA             Reviewed;         431 AA.
AC   Q95LU3;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Fibrinogen C domain-containing protein 1;
GN   Name=FIBCD1; ORFNames=QtsA-17952;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA   Terao K., Sugano S., Hashimoto K.;
RT   "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT   the human genome sequence.";
RL   BMC Genomics 3:36-36(2002).
CC   -!- FUNCTION: Acetyl group-binding receptor which shows a high-affinity and
CC       calcium-dependent binding to acetylated structures such as chitin, some
CC       N-acetylated carbohydrates, and amino acids, but not to their non-
CC       acetylated counterparts. Can facilitate the endocytosis of acetylated
CC       components (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
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DR   EMBL; AB071099; BAB64493.1; -; mRNA.
DR   RefSeq; NP_001274638.1; NM_001287709.1.
DR   RefSeq; XP_015291592.1; XM_015436106.1.
DR   AlphaFoldDB; Q95LU3; -.
DR   SMR; Q95LU3; -.
DR   STRING; 9541.XP_005580678.1; -.
DR   GeneID; 102115035; -.
DR   CTD; 84929; -.
DR   eggNOG; KOG2579; Eukaryota.
DR   OrthoDB; 523014at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0008061; F:chitin binding; ISS:UniProtKB.
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..431
FT                   /note="Fibrinogen C domain-containing protein 1"
FT                   /id="PRO_0000294316"
FT   TOPO_DOM        1..3
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..24
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..431
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          205..428
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   BINDING         363
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         365
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            375
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250"
FT   SITE            385
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250"
FT   SITE            401
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250"
FT   SITE            402
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        214..243
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        371..384
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ   SEQUENCE   431 AA;  47323 MW;  2F3F28338B111F45 CRC64;
     MLCTVLLALA VLLAVAVTGA VLFLNHTHTP GTAPPPVVST GAAGANSALV TVERADSSRL
     SILIDPRCPD LADSFARLES AQASVLEALT EHQAQPRLVG DQEQELLDTL ADQLPRLLTR
     ASELQTECMG LRKGHGTLGQ GLSALQSEQG RLIQLLSESQ GHMAHLVNSV GDVLDALQRD
     RGLGRPRAKA DLQRAPARGA RPRGCATGSR PRDCLDVLLS GQQDDGIYSV FPTHYPAGFQ
     VYCDMRTDGG GWTVFQRRED GSVNFFRGWD AYRDGFGRLT GEHWLGLKRI HALTTQTAYE
     LHVDLEDFDN GTAYARYGSF GVGLFSVDPE EDGYPLTVAD YSGTAGDSLL KHSGMRFTTK
     DRDSDHSENN CAAFYRGAWW YRNCHTSNLN GQYLRGAHTS YADGVEWSSW TGWQYSLKFS
     EMKIRPVRED R