FCN2_MOUSE
ID FCN2_MOUSE Reviewed; 314 AA.
AC O70497; Q3KNL6;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ficolin-2;
DE AltName: Full=Collagen/fibrinogen domain-containing protein 2;
DE AltName: Full=Ficolin-B;
DE AltName: Full=Ficolin-beta;
DE AltName: Full=L-ficolin;
DE Flags: Precursor;
GN Name=Fcn2; Synonyms=Fcnb;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-308.
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=9851834; DOI=10.1006/abbi.1998.0957;
RA Ohashi T., Erickson H.P.;
RT "Oligomeric structure and tissue distribution of ficolins from mouse, pig
RT and human.";
RL Arch. Biochem. Biophys. 360:223-232(1998).
CC -!- FUNCTION: May function in innate immunity through activation of the
CC lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin
CC (By similarity). {ECO:0000250|UniProtKB:Q15485}.
CC -!- SUBUNIT: Homotrimer. Interacts with elastin. Interacts with MASP1 and
CC MASP2. {ECO:0000250|UniProtKB:Q15485}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: The fibrinogen-like domain (FBG) contains calcium-binding sites
CC that may be involved in carbohydrate binding.
CC {ECO:0000250|UniProtKB:Q15485}.
CC -!- SIMILARITY: Belongs to the ficolin lectin family. {ECO:0000305}.
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DR EMBL; BC107220; AAI07221.1; -; mRNA.
DR EMBL; BC107221; AAI07222.1; -; mRNA.
DR EMBL; AF063217; AAC98781.1; -; mRNA.
DR CCDS; CCDS15832.1; -.
DR RefSeq; NP_034320.1; NM_010190.1.
DR AlphaFoldDB; O70497; -.
DR SMR; O70497; -.
DR STRING; 10090.ENSMUSP00000028179; -.
DR GlyGen; O70497; 1 site.
DR CPTAC; non-CPTAC-4035; -.
DR MaxQB; O70497; -.
DR PaxDb; O70497; -.
DR PRIDE; O70497; -.
DR ProteomicsDB; 272977; -.
DR Antibodypedia; 602; 401 antibodies from 31 providers.
DR Ensembl; ENSMUST00000028179; ENSMUSP00000028179; ENSMUSG00000026835.
DR GeneID; 14134; -.
DR KEGG; mmu:14134; -.
DR UCSC; uc008ixv.1; mouse.
DR CTD; 14134; -.
DR MGI; MGI:1341158; Fcnb.
DR VEuPathDB; HostDB:ENSMUSG00000026835; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000157531; -.
DR HOGENOM; CLU_038628_3_3_1; -.
DR InParanoid; O70497; -.
DR OMA; HKSYANG; -.
DR OrthoDB; 1035379at2759; -.
DR PhylomeDB; O70497; -.
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; 14134; 0 hits in 72 CRISPR screens.
DR PRO; PR:O70497; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O70497; protein.
DR Bgee; ENSMUSG00000026835; Expressed in granulocyte and 21 other tissues.
DR ExpressionAtlas; O70497; baseline and differential.
DR Genevisible; O70497; 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; ISO:MGI.
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; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0033691; F:sialic acid binding; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001867; P:complement activation, lectin pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IEA:Ensembl.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:1903028; P:positive regulation of opsonization; IEA:Ensembl.
DR GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:Ensembl.
DR GO; GO:0043654; P:recognition of apoptotic cell; IEA:Ensembl.
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; Collagen; Complement activation lectin pathway; Disulfide bond;
KW Glycoprotein; Immunity; Innate immunity; Lectin; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..314
FT /note="Ficolin-2"
FT /id="PRO_0000009140"
FT DOMAIN 40..96
FT /note="Collagen-like"
FT DOMAIN 97..314
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 49..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..127
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT DISULFID 106..134
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT DISULFID 258..271
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT CONFLICT 130
FT /note="L -> M (in Ref. 2; AAC98781)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 33984 MW; 6C1467BF0BE96E67 CRC64;
MALGSAALFV LTLTVHAAGT CPELKVLDLE GYKQLTILQG CPGLPGAAGP KGEAGAKGDR
GESGLPGIPG KEGPTGPKGN QGEKGIRGEK GDSGPSQSCA TGPRTCKELL TQGHFLTGWY
TIYLPDCRPL TVLCDMDTDG GGWTVFQRRL DGSVDFFRDW TSYKRGFGSQ LGEFWLGNDN
IHALTTQGTS ELRVDLSDFE GKHDFAKYSS FQIQGEAEKY KLILGNFLGG GAGDSLTPHN
NRLFSTKDQD NDGSTSSCAM GYHGAWWYSQ CHTSNLNGLY LRGPHKSYAN GVNWKSWRGY
NYSCKVSEMK VRLI
