FCN1_MOUSE
ID FCN1_MOUSE Reviewed; 334 AA.
AC O70165;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 165.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=9535745; DOI=10.1006/bbrc.1998.8344;
RA Fujimori Y., Harumiya S., Fukumoto Y., Miura Y., Yagasaki K., Tachikawa H.,
RA Fujimoto D.;
RT "Molecular cloning and characterization of mouse ficolin-A.";
RL Biochem. Biophys. Res. Commun. 244:796-800(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 18-32.
RX PubMed=17669269; DOI=10.5483/bmbrep.2007.40.4.532;
RA Kwon S., Kim M.-S., Kim D., Lee K.-W., Choi S.Y., Park J., Kim Y.H.,
RA Lee Y., Kwon H.-J.;
RT "Identification of a functionally relevant signal peptide of mouse ficolin
RT A.";
RL J. Biochem. Mol. Biol. 40:532-538(2007).
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}.
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 -!- TISSUE SPECIFICITY: Highly expressed in liver and spleen.
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; AB007813; BAA25126.1; -; mRNA.
DR EMBL; BC019180; AAH19180.1; -; mRNA.
DR CCDS; CCDS15785.1; -.
DR PIR; JC5980; JC5980.
DR RefSeq; NP_032021.1; NM_007995.3.
DR RefSeq; XP_006497736.1; XM_006497673.3.
DR RefSeq; XP_011237318.1; XM_011239016.2.
DR AlphaFoldDB; O70165; -.
DR SMR; O70165; -.
DR BioGRID; 199622; 2.
DR STRING; 10090.ENSMUSP00000028307; -.
DR GlyGen; O70165; 1 site.
DR iPTMnet; O70165; -.
DR PhosphoSitePlus; O70165; -.
DR CPTAC; non-CPTAC-3577; -.
DR PaxDb; O70165; -.
DR PeptideAtlas; O70165; -.
DR PRIDE; O70165; -.
DR ProteomicsDB; 270976; -.
DR DNASU; 14133; -.
DR Ensembl; ENSMUST00000028307; ENSMUSP00000028307; ENSMUSG00000026938.
DR GeneID; 14133; -.
DR KEGG; mmu:14133; -.
DR UCSC; uc008isz.1; mouse.
DR CTD; 14133; -.
DR MGI; MGI:1340905; Fcna.
DR VEuPathDB; HostDB:ENSMUSG00000026938; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000157531; -.
DR HOGENOM; CLU_038628_3_3_1; -.
DR InParanoid; O70165; -.
DR OMA; NIEINCA; -.
DR OrthoDB; 1035379at2759; -.
DR PhylomeDB; O70165; -.
DR TreeFam; TF329953; -.
DR Reactome; R-MMU-166662; Lectin pathway of complement activation.
DR Reactome; R-MMU-166663; Initial triggering of complement.
DR Reactome; R-MMU-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 14133; 2 hits in 71 CRISPR screens.
DR PRO; PR:O70165; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O70165; protein.
DR Bgee; ENSMUSG00000026938; Expressed in spleen and 112 other tissues.
DR ExpressionAtlas; O70165; baseline and differential.
DR Genevisible; O70165; MM.
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:MGI.
DR GO; GO:0003823; F:antigen binding; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0097367; F:carbohydrate derivative binding; IBA:GO_Central.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:2001065; F:mannan binding; ISO:MGI.
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:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0033691; F:sialic acid binding; ISO:MGI.
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:0001867; P:complement activation, lectin pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Calcium; Cell membrane; Collagen; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunity; Innate immunity; Lectin; Membrane;
KW Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:17669269"
FT CHAIN 18..334
FT /note="Ficolin-1"
FT /id="PRO_0000009137"
FT DOMAIN 50..88
FT /note="Collagen-like"
FT DOMAIN 117..334
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 47..117
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 325..334
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 290..292
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT SITE 308
FT /note="Mediates specificity for sialic acids"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT CARBOHYD 261
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 278..291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ SEQUENCE 334 AA; 36298 MW; 9D30C05036AA04B1 CRC64;
MQWPTLWAFS GLLCLCPSQA LGQERGACPD VKVVGLGAQD KVVVIQSCPG FPGPPGPKGE
PGSPAGRGER GFQGSPGKMG PAGSKGEPGT MGPPGVKGEK GDTGAAPSLG EKELGDTLCQ
RGPRSCKDLL TRGIFLTGWY TIHLPDCRPL TVLCDMDVDG GGWTVFQRRV DGSIDFFRDW
DSYKRGFGNL GTEFWLGNDY LHLLTANGNQ ELRVDLQDFQ GKGSYAKYSS FQVSEEQEKY
KLTLGQFLEG TAGDSLTKHN NMSFTTHDQD NDANSMNCAA LFHGAWWYHN CHQSNLNGRY
LSGSHESYAD GINWGTGQGH HYSYKVAEMK IRAS
