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   27-MAR-2024, entry version 165.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyCosmos; O70497; 1 site, No reported glycans.
DR   GlyGen; O70497; 1 site.
DR   CPTAC; non-CPTAC-4035; -.
DR   MaxQB; O70497; -.
DR   PaxDb; 10090-ENSMUSP00000028179; -.
DR   ProteomicsDB; 272977; -.
DR   Antibodypedia; 602; 419 antibodies from 31 providers.
DR   Ensembl; ENSMUST00000028179.15; ENSMUSP00000028179.9; ENSMUSG00000026835.16.
DR   GeneID; 14134; -.
DR   KEGG; mmu:14134; -.
DR   UCSC; uc008ixv.1; mouse.
DR   AGR; MGI:1341158; -.
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; GNCAKQY; -.
DR   OrthoDB; 3134470at2759; -.
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 77 CRISPR screens.
DR   PRO; PR:O70497; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; O70497; Protein.
DR   Bgee; ENSMUSG00000026835; Expressed in granulocyte and 21 other cell types or tissues.
DR   ExpressionAtlas; O70497; baseline and differential.
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:0005886; C: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; Gamma Fibrinogen, chain A, domain 1; 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   NCBIfam; NF040941; GGGWT_bact; 1.
DR   PANTHER; PTHR19143; FIBRINOGEN/TENASCIN/ANGIOPOEITIN; 1.
DR   PANTHER; PTHR19143:SF448; FICOLIN-2; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   SMART; SM00186; FBG; 1.
DR   SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR   PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   Genevisible; O70497; MM.
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
//