FCN2_RAT
ID FCN2_RAT Reviewed; 319 AA.
AC P57756;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Tachikawa H., Fujimori Y., Yoshida Y., Harumiya S., Takahashi N.,
RA Fujimoto D.;
RT "Molecular cloning of rat ficolin B.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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).
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; AB036792; BAB20440.1; -; mRNA.
DR EMBL; BC088123; AAH88123.1; -; mRNA.
DR RefSeq; NP_446086.1; NM_053634.1.
DR AlphaFoldDB; P57756; -.
DR SMR; P57756; -.
DR STRING; 10116.ENSRNOP00000012494; -.
DR GlyGen; P57756; 1 site.
DR PaxDb; P57756; -.
DR Ensembl; ENSRNOT00000012494; ENSRNOP00000012494; ENSRNOG00000009342.
DR GeneID; 114091; -.
DR KEGG; rno:114091; -.
DR UCSC; RGD:621222; rat.
DR CTD; 14134; -.
DR RGD; 621222; Fcnb.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000157531; -.
DR HOGENOM; CLU_038628_3_3_1; -.
DR InParanoid; P57756; -.
DR OMA; HKSYANG; -.
DR OrthoDB; 1035379at2759; -.
DR PhylomeDB; P57756; -.
DR TreeFam; TF329953; -.
DR Reactome; R-RNO-166662; Lectin pathway of complement activation.
DR Reactome; R-RNO-166663; Initial triggering of complement.
DR Reactome; R-RNO-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P57756; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000009342; Expressed in spleen and 16 other tissues.
DR Genevisible; P57756; RN.
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:RGD.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038187; F:pattern recognition receptor activity; ISO:RGD.
DR GO; GO:0033691; F:sialic acid binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; ISO:RGD.
DR GO; GO:0001867; P:complement activation, lectin pathway; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:RGD.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:RGD.
DR GO; GO:1903028; P:positive regulation of opsonization; ISO:RGD.
DR GO; GO:0034394; P:protein localization to cell surface; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0043654; P:recognition of apoptotic cell; ISO:RGD.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..319
FT /note="Ficolin-2"
FT /id="PRO_0000009141"
FT DOMAIN 45..101
FT /note="Collagen-like"
FT DOMAIN 102..319
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 53..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT BINDING 257
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 CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..132
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT DISULFID 111..139
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT DISULFID 263..276
FT /evidence="ECO:0000250|UniProtKB:O00602"
SQ SEQUENCE 319 AA; 34684 MW; 0A11670A6B541B16 CRC64;
MVLGSAALFV LSLCVTELTL HAADTCPEVK VLDLEGSNKL TILQGCPGLP GALGPKGEAG
AKGDRGESGL PGHPGKAGPT GPKGDRGEKG VRGEKGDTGP SQSCATGPRT CKELLTRGYF
LTGWYTIYLP DCRPLTVLCD MDTDGGGWTV FQRRIDGTVD FFRDWTSYKQ GFGSQLGEFW
LGNDNIHALT TQGTNELRVD LADFDGNHDF AKYSSFQIQG EAEKYKLILG NFLGGGAGDS
LTSQNNMLFS TKDQDNDQGS SNCAVRYHGA WWYSDCHTSN LNGLYLRGLH KSYANGVNWK
SWKGYNYSYK VSEMKVRLI
