FCN1_RAT
ID FCN1_RAT Reviewed; 335 AA.
AC Q9WTS8;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Ficolin-1;
DE AltName: Full=Collagen/fibrinogen domain-containing protein 1;
DE AltName: Full=Ficolin-A;
DE AltName: Full=Ficolin-alpha;
DE AltName: Full=M-ficolin;
DE Flags: Precursor;
GN Name=Fcn1; Synonyms=Fcna;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Yoshida Y., Tachikawa H., Fujimori Y., Miura Y., Yagasaki K., Fujimoto D.,
RA Harumiya S.;
RT "Molecular cloning and characterization of rat ficolin-A.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Extracellular lectin functioning as a pattern-recognition
CC receptor in innate immunity. Binds the sugar moieties of pathogen-
CC associated molecular patterns (PAMPs) displayed on microbes and
CC activates the lectin pathway of the complement system. May also
CC activate monocytes through a G protein-coupled receptor, FFAR2,
CC inducing the secretion of interleukin-8/IL-8. Binds preferentially to
CC 9-O-acetylated 2-6-linked sialic acid derivatives and to various
CC glycans containing sialic acid engaged in a 2-3 linkage (By
CC similarity). {ECO:0000250|UniProtKB:O00602}.
CC -!- SUBUNIT: Homotrimer. Interacts with elastin/ELN. Interacts (via
CC Fibrinogen C-terminal domain) with FFAR2. Interacts with CRP; may
CC regulate monocyte activation by FCN1. {ECO:0000250|UniProtKB:O00602}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O00602}. Cell
CC membrane {ECO:0000250|UniProtKB:O00602}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O00602}; Extracellular side
CC {ECO:0000250|UniProtKB:O00602}. Note=Found on the monocyte and
CC granulocyte surface. {ECO:0000250|UniProtKB:O00602}.
CC -!- DOMAIN: The fibrinogen C-terminal domain mediates calcium-dependent
CC binding to carbohydrates and tethering to the cell surface in monocytes
CC and granulocytes. The domain undergoes a conformational switch at pH
CC under 6.2, and looses its carbohydrate-binding ability.
CC {ECO:0000250|UniProtKB:O00602}.
CC -!- SIMILARITY: Belongs to the ficolin lectin family. {ECO:0000305}.
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DR EMBL; AB026057; BAA76940.2; -; mRNA.
DR AlphaFoldDB; Q9WTS8; -.
DR SMR; Q9WTS8; -.
DR STRING; 10116.ENSRNOP00000023022; -.
DR GlyGen; Q9WTS8; 1 site.
DR PaxDb; Q9WTS8; -.
DR PRIDE; Q9WTS8; -.
DR UCSC; RGD:621221; rat.
DR RGD; 621221; Fcn1.
DR eggNOG; KOG2579; Eukaryota.
DR InParanoid; Q9WTS8; -.
DR PhylomeDB; Q9WTS8; -.
DR Reactome; R-RNO-166662; Lectin pathway of complement activation.
DR Reactome; R-RNO-166663; Initial triggering of complement.
DR Reactome; R-RNO-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q9WTS8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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:0031232; C:extrinsic component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:RGD.
DR GO; GO:0003823; F:antigen binding; ISO:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0097367; F:carbohydrate derivative binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038187; F:pattern recognition receptor activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006956; P:complement activation; ISO:RGD.
DR GO; GO:0001867; P:complement activation, lectin pathway; ISO:RGD.
DR GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1902679; P:negative regulation of RNA biosynthetic process; ISO:RGD.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:RGD.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:1903028; P:positive regulation of opsonization; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0043654; P:recognition of apoptotic cell; ISO:RGD.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR008160; Collagen.
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; PF01391; Collagen; 1.
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; Cell membrane; Collagen; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Lectin; Membrane; Metal-binding; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..335
FT /note="Ficolin-1"
FT /id="PRO_0000009138"
FT DOMAIN 50..88
FT /note="Collagen-like"
FT DOMAIN 117..335
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 47..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..162
FT /note="A domain; contributes to trimerization"
FT /evidence="ECO:0000250"
FT REGION 163..251
FT /note="B domain; contributes to trimerization"
FT /evidence="ECO:0000250"
FT REGION 326..335
FT /note="P domain"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT BINDING 291..293
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT SITE 309
FT /note="Mediates specificity for sialic acids"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 119..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 126..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 279..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ SEQUENCE 335 AA; 36627 MW; 1A7FC9568E76ED5D CRC64;
MWWPMLWAFP VLLCLCSSQA LGQESGACPD VKIVGLGAQD KVAVIQSCPS FPGPPGPKGE
PGSPAGRGER GLQGSPGKMG PPGSKGEPGT MGPPGVKGEK GERGTASPLG QKELGDALCR
RGPRSCKDLL TRGIFLTGWY TIYLPDCRPL TVLCDMDVDG GGWTVFQRRV DGSINFYRDW
DSYKRGFGNL GTEFWLGNDY LHLLTANGNQ ELRVDLREFQ GQTSFAKYSS FQVSGEQEKY
KLTLGQFLEG TAGDSLTKHN NMAFSTHDQD NDTNGGKNCA ALFHGAWWYH DCHQSNLNGR
YLPGSHESYA DGINWLSGRG HRYSYKVAEM KIRAS
