ID FCN2_PIG Reviewed; 323 AA. AC Q29041; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 105. 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 Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND TISSUE SPECIFICITY. RC TISSUE=Uterus; RX PubMed=7686157; DOI=10.1016/s0021-9258(19)85267-5; RA Ichijo H., Hellman U., Wernstedt C., Gonez L.J., Claesson-Welsh L., RA Heldin C.H., Miyazono K.; RT "Molecular cloning and characterization of ficolin, a multimeric protein RT with fibrinogen- and collagen-like domains."; RL J. Biol. Chem. 268:14505-14513(1993). 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 -!- TISSUE SPECIFICITY: Mainly expressed in skeletal muscle. CC {ECO:0000269|PubMed:7686157}. 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; L12344; AAA92455.1; -; mRNA. DR PIR; A47172; A47172. DR RefSeq; NP_999033.1; NM_213868.1. DR AlphaFoldDB; Q29041; -. DR SMR; Q29041; -. DR GlyCosmos; Q29041; 3 sites, No reported glycans. DR PaxDb; 9823-ENSSSCP00000019414; -. DR PeptideAtlas; Q29041; -. DR GeneID; 396881; -. DR KEGG; ssc:396881; -. DR CTD; 2220; -. DR eggNOG; KOG2579; Eukaryota. DR InParanoid; Q29041; -. DR OrthoDB; 3134470at2759; -. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; 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: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; 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. PE 1: Evidence at protein 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..26 FT /evidence="ECO:0000255" FT CHAIN 27..323 FT /note="Ficolin-2" FT /id="PRO_0000269571" FT DOMAIN 52..102 FT /note="Collagen-like" FT DOMAIN 106..323 FT /note="Fibrinogen C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739" FT REGION 55..107 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 86..100 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 259 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:O00602" FT BINDING 261 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:O00602" FT BINDING 265 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:O00602" FT CARBOHYD 249 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 302 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 310 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 108..136 FT /evidence="ECO:0000250|UniProtKB:O00602" FT DISULFID 115..143 FT /evidence="ECO:0000250|UniProtKB:O00602" FT DISULFID 267..280 FT /evidence="ECO:0000250|UniProtKB:O00602" SQ SEQUENCE 323 AA; 34682 MW; 849BF031D77E16B7 CRC64; MDTRGVAAAM RPLVLLVAFL CTAAPALDTC PEVKVVGLEG SDKLSILRGC PGLPGAAGPK GEAGASGPKG GQGPPGAPGE PGPPGPKGDR GEKGEPGPKG ESWETEQCLT GPRTCKELLT RGHILSGWHT IYLPDCQPLT VLCDMDTDGG GWTVFQRRSD GSVDFYRDWA AYKRGFGSQL GEFWLGNDHI HALTAQGTNE LRVDLVDFEG NHQFAKYRSF QVADEAEKYM LVLGAFVEGN AGDSLTSHNN SLFTTKDQDN DQYASNCAVL YQGAWWYNSC HVSNLNGRYL GGSHGSFANG VNWSSGKGYN YSYKVSEMKF RAT //