FCN1_PIG
ID FCN1_PIG Reviewed; 326 AA.
AC Q29042;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Ficolin-1;
DE AltName: Full=Ficolin-A;
DE AltName: Full=Ficolin-alpha;
DE Flags: Precursor;
GN Name=FCN1;
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: 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|UniProtKB:O00602}.
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: Most abundantly expressed in placenta and lung.
CC {ECO:0000269|PubMed:7686157}.
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}.
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; L12345; AAC69641.1; -; mRNA.
DR PIR; B47172; B47172.
DR RefSeq; NP_999325.1; NM_214160.2.
DR AlphaFoldDB; Q29042; -.
DR SMR; Q29042; -.
DR STRING; 9823.ENSSSCP00000023182; -.
DR PaxDb; Q29042; -.
DR PeptideAtlas; Q29042; -.
DR GeneID; 397316; -.
DR KEGG; ssc:397316; -.
DR CTD; 2219; -.
DR eggNOG; KOG2579; Eukaryota.
DR InParanoid; Q29042; -.
DR OrthoDB; 1035379at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Calcium; Cell membrane; Collagen; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Lectin; Membrane; Metal-binding; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000250"
FT CHAIN 30..326
FT /note="Ficolin-1"
FT /id="PRO_0000269570"
FT DOMAIN 55..93
FT /note="Collagen-like"
FT DOMAIN 109..326
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 61..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..154
FT /note="A domain; contributes to trimerization"
FT /evidence="ECO:0000250"
FT REGION 155..243
FT /note="B domain; contributes to trimerization"
FT /evidence="ECO:0000250"
FT REGION 317..326
FT /note="P domain"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT BINDING 282..284
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT SITE 300
FT /note="Mediates specificity for sialic acids"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT SITE 312
FT /note="Mediates specificity for sialic acids"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 118..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 270..283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ SEQUENCE 326 AA; 35246 MW; 170A5E9EA1E8F310 CRC64;
MELSRVAVAL GPTGQLLLFL SFQTLAAQAA DTCPEVKVVG LEGSDKLSIL RGCPGLPGAA
GPKGEAGANG PKGERGSPGV VGKAGPAGPK GDRGEKGARG EKGEPGQLQS CATGPRTCKE
LLTRGHFLSG WHTIYLPDCQ PLTVLCDMDT DGGGWTVFQR RSDGSVDFYR DWAAYKRGFG
SQLGEFWLGN DHIHALTAQG TSELRVDLVD FEGNHQFAKY RSFQVAGEAE KYKLVLGGFL
EGNAGDSLSS HRDQFFSTKD QDNDNHSGNC AEQYHGAWWY NACHSSNLNG RYLRGLHTSY
ANGVNWRSGR GYNYSYQVSE MKVRLT
