ID   FCN2_BOVIN              Reviewed;         329 AA.
AC   Q5I2E5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Bone marrow;
RA   Keirstead N.D., Brooks A.S., Lillie B.N.M., Caswell J.L., Hayes M.A.;
RT   "Comparison of porcine and bovine ficolins expressed by neutrophils.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
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; AY860499; AAW52550.1; -; mRNA.
DR   RefSeq; NP_001010996.1; NM_001010996.1.
DR   AlphaFoldDB; Q5I2E5; -.
DR   SMR; Q5I2E5; -.
DR   PRIDE; Q5I2E5; -.
DR   Ensembl; ENSBTAT00000084171; ENSBTAP00000071732; ENSBTAG00000048155.
DR   GeneID; 497016; -.
DR   KEGG; bta:497016; -.
DR   CTD; 2219; -.
DR   VEuPathDB; HostDB:ENSBTAG00000048155; -.
DR   GeneTree; ENSGT00940000157531; -.
DR   HOGENOM; CLU_038628_3_3_1; -.
DR   InParanoid; Q5I2E5; -.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000048155; Expressed in monocyte and 92 other tissues.
DR   ExpressionAtlas; Q5I2E5; 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:0003823; F:antigen binding; IBA:GO_Central.
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:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0001867; P:complement activation, lectin pathway; IBA:GO_Central.
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..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..329
FT                   /note="Ficolin-2"
FT                   /id="PRO_5000094837"
FT   DOMAIN          52..111
FT                   /note="Collagen-like"
FT   DOMAIN          112..329
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   REGION          64..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         265
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O00602"
FT   BINDING         267
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O00602"
FT   BINDING         269
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O00602"
FT   BINDING         271
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O00602"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        114..142
FT                   /evidence="ECO:0000250|UniProtKB:O00602"
FT   DISULFID        121..149
FT                   /evidence="ECO:0000250|UniProtKB:O00602"
FT   DISULFID        273..286
FT                   /evidence="ECO:0000250|UniProtKB:O00602"
SQ   SEQUENCE   329 AA;  35339 MW;  F8A2BA6FD65E3F16 CRC64;
     MELGGAAGAL GPSGPLLVCL CFGTLAAQAA DTCPEVKLVG LEGSDKLSIL RGCPGLPGAP
     GLKGETGAAG LKGERGLPGV PGKAGPAGPK GSTGAQGEKG ARGEKGESGQ LHSCATGPRT
     CTELLTRGHF LSGWHTIYLP DCRPLTVLCD MDTDGGGWTV FQRRKDGSVD FFRTWTAYKQ
     GFGSQLGEFW LGNDNIHALT AQGTSELRVD LMDFEGNHRF AKYQSFRMAD EAEKYKLVLG
     AFVEGNAGDS LTDHGNHFFS TKDRDNDESP SNCAAQFQGA WWYHSCHSSN LNGRYLRGPH
     TSYANGINWK SWGRYNYSYK VSEMKLRLT