FCN2_HUMAN
ID FCN2_HUMAN Reviewed; 313 AA.
AC Q15485; A6NFG7; A8K478; Q6IS69; Q7M4P4; Q9UC57;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Ficolin-2;
DE AltName: Full=37 kDa elastin-binding protein;
DE AltName: Full=Collagen/fibrinogen domain-containing protein 2;
DE AltName: Full=EBP-37;
DE AltName: Full=Ficolin-B;
DE AltName: Full=Ficolin-beta;
DE AltName: Full=Hucolin;
DE AltName: Full=L-ficolin;
DE AltName: Full=Serum lectin p35;
DE Flags: Precursor;
GN Name=FCN2; Synonyms=FCNL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8884275; DOI=10.1006/geno.1996.0497;
RA Endo Y., Sato Y., Matsushita M., Fujita T.;
RT "Cloning and characterization of the human lectin P35 gene and its related
RT gene.";
RL Genomics 36:515-521(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8576206; DOI=10.1074/jbc.271.5.2448;
RA Matsushita M., Endo Y., Taira S., Sato Y., Fujita T., Ichikawa N.,
RA Nakata M., Mizuochi T.;
RT "A novel human serum lectin with collagen- and fibrinogen-like domains that
RT functions as an opsonin.";
RL J. Biol. Chem. 271:2448-2454(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tan J., Ong R., Hibberd M.L., Seielstad M.;
RT "Genetic variation in immune response genes.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TYR-113.
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [8]
RP PROTEIN SEQUENCE OF 26-50 (ISOFORM 1).
RC TISSUE=Plasma;
RX PubMed=7498469; DOI=10.1016/0014-5793(95)01205-s;
RA Edgar P.F.;
RT "Hucolin, a new corticosteroid-binding protein from human plasma with
RT structural similarities to ficolins, transforming growth factor-beta 1-
RT binding proteins.";
RL FEBS Lett. 375:159-161(1995).
RN [9]
RP PROTEIN SEQUENCE OF 65-99; 191-198 AND 218-228 (ISOFORM 1), SUBUNIT, AND
RP HYDROXYLATION AT PRO-77; PRO-80 AND PRO-86.
RC TISSUE=Plasma;
RX PubMed=8586615; DOI=10.1093/oxfordjournals.jbchem.a124802;
RA Harumiya S., Omori A., Sugiura T., Fukumoto Y., Tachikawa H., Fujimoto D.;
RT "EBP-37, a new elastin-binding protein in human plasma: structural
RT similarity to ficolins, transforming growth factor-beta 1-binding
RT proteins.";
RL J. Biochem. 117:1029-1035(1995).
RN [10]
RP FUNCTION, AND INTERACTION WITH MASP1 AND MASP2.
RX PubMed=10679061; DOI=10.4049/jimmunol.164.5.2281;
RA Matsushita M., Endo Y., Fujita T.;
RT "Complement-activating complex of ficolin and mannose-binding lectin-
RT associated serine protease.";
RL J. Immunol. 164:2281-2284(2000).
RN [11]
RP INTERACTION WITH CR1.
RX PubMed=23460739; DOI=10.4049/jimmunol.1202451;
RA Jacquet M., Lacroix M., Ancelet S., Gout E., Gaboriaud C., Thielens N.M.,
RA Rossi V.;
RT "Deciphering complement receptor type 1 interactions with recognition
RT proteins of the lectin complement pathway.";
RL J. Immunol. 190:3721-3731(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 97-313 IN COMPLEXES WITH CALCIUM
RP AND FUCOSE, FUNCTION, SUBUNIT, DOMAIN, DISULFIDE BOND, AND GLYCOSYLATION AT
RP ASN-240.
RX PubMed=17215869; DOI=10.1038/sj.emboj.7601500;
RA Garlatti V., Belloy N., Martin L., Lacroix M., Matsushita M., Endo Y.,
RA Fujita T., Fontecilla-Camps J.C., Arlaud G.J., Thielens N.M., Gaboriaud C.;
RT "Structural insights into the innate immune recognition specificities of
RT L- and H-ficolins.";
RL EMBO J. 26:623-633(2007).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-80.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May function in innate immunity through activation of the
CC lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin.
CC Enhances phagocytosis of S.typhimurium by neutrophils, suggesting an
CC opsonic effect via the collagen region. {ECO:0000269|PubMed:10679061,
CC ECO:0000269|PubMed:17215869}.
CC -!- SUBUNIT: Homotrimer (PubMed:17215869). Interacts with elastin.
CC Interacts with MASP1 and MASP2. Interacts with CR1.
CC {ECO:0000269|PubMed:10679061, ECO:0000269|PubMed:17215869,
CC ECO:0000269|PubMed:23460739, ECO:0000269|PubMed:8586615}.
CC -!- INTERACTION:
CC Q15485; P17927: CR1; NbExp=7; IntAct=EBI-7468784, EBI-2807625;
CC Q15485; O75636: FCN3; NbExp=12; IntAct=EBI-7468784, EBI-11786958;
CC Q15485; Q07954: LRP1; NbExp=2; IntAct=EBI-7468784, EBI-1046087;
CC Q15485; P48740-2: MASP1; NbExp=2; IntAct=EBI-7468784, EBI-26435098;
CC Q15485; P26022: PTX3; NbExp=7; IntAct=EBI-7468784, EBI-11574553;
CC Q15485; PRO_0000000214 [P9WQP3]: fbpA; Xeno; NbExp=2; IntAct=EBI-7468784, EBI-26878164;
CC Q15485; P9WQP1: fbpB; Xeno; NbExp=3; IntAct=EBI-7468784, EBI-26878221;
CC PRO_0000009139; PRO_0000009139 [Q15485]: FCN2; NbExp=2; IntAct=EBI-26568205, EBI-26568205;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15485-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15485-2; Sequence=VSP_030027;
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- DOMAIN: The fibrinogen-like domain (FBG) contains calcium-binding sites
CC that may be involved in carbohydrate binding.
CC {ECO:0000269|PubMed:17215869}.
CC -!- SIMILARITY: Belongs to the ficolin lectin family. {ECO:0000305}.
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DR EMBL; D63160; BAA09636.1; -; Genomic_DNA.
DR EMBL; D49353; BAA08352.1; -; mRNA.
DR EMBL; DQ217935; ABB01005.1; -; Genomic_DNA.
DR EMBL; AK290843; BAF83532.1; -; mRNA.
DR EMBL; AL603650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88133.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88135.1; -; Genomic_DNA.
DR EMBL; BC069572; AAH69572.1; -; mRNA.
DR EMBL; BC069825; AAH69825.1; -; mRNA.
DR CCDS; CCDS6983.1; -. [Q15485-1]
DR PIR; PH0263; PH0263.
DR PIR; S68005; S68005.
DR RefSeq; NP_004099.2; NM_004108.2. [Q15485-1]
DR RefSeq; NP_056652.1; NM_015837.2. [Q15485-2]
DR PDB; 2J0G; X-ray; 2.85 A; A/B/C/D/E/F=97-313.
DR PDB; 2J0H; X-ray; 2.85 A; A/B/C/D/E/F=97-313.
DR PDB; 2J0Y; X-ray; 2.35 A; A/B/C/D/E/F=97-313.
DR PDB; 2J1G; X-ray; 1.95 A; A/B/C/D/E/F=97-313.
DR PDB; 2J2P; X-ray; 2.80 A; A/B/C/D/E/F=97-313.
DR PDB; 2J3F; X-ray; 2.80 A; A/B/C/D/E/F=95-313.
DR PDB; 2J3G; X-ray; 2.50 A; A/B/C/D/E/F=97-313.
DR PDB; 2J3O; X-ray; 2.65 A; A/B/C/D/E/F=95-313.
DR PDB; 2J3U; X-ray; 2.15 A; A/B/C/D/E/F=97-313.
DR PDB; 2J61; X-ray; 2.70 A; A/B=97-313.
DR PDB; 4NYT; X-ray; 2.25 A; A/B/C=97-313.
DR PDB; 4R9J; X-ray; 2.10 A; A/B/G=97-313.
DR PDB; 4R9T; X-ray; 2.25 A; A/B/C=97-313.
DR PDBsum; 2J0G; -.
DR PDBsum; 2J0H; -.
DR PDBsum; 2J0Y; -.
DR PDBsum; 2J1G; -.
DR PDBsum; 2J2P; -.
DR PDBsum; 2J3F; -.
DR PDBsum; 2J3G; -.
DR PDBsum; 2J3O; -.
DR PDBsum; 2J3U; -.
DR PDBsum; 2J61; -.
DR PDBsum; 4NYT; -.
DR PDBsum; 4R9J; -.
DR PDBsum; 4R9T; -.
DR AlphaFoldDB; Q15485; -.
DR SMR; Q15485; -.
DR BioGRID; 108514; 3.
DR ComplexPortal; CPX-6178; FCN2-MASP1 lectin-protease complex.
DR ComplexPortal; CPX-6238; FCN2-MASP2 lectin-protease complex.
DR IntAct; Q15485; 20.
DR MINT; Q15485; -.
DR STRING; 9606.ENSP00000291744; -.
DR UniLectin; Q15485; -.
DR GlyGen; Q15485; 2 sites.
DR iPTMnet; Q15485; -.
DR BioMuta; FCN2; -.
DR DMDM; 166214934; -.
DR jPOST; Q15485; -.
DR MassIVE; Q15485; -.
DR MaxQB; Q15485; -.
DR PaxDb; Q15485; -.
DR PeptideAtlas; Q15485; -.
DR PRIDE; Q15485; -.
DR ProteomicsDB; 60608; -. [Q15485-1]
DR ProteomicsDB; 60609; -. [Q15485-2]
DR Antibodypedia; 32017; 244 antibodies from 21 providers.
DR DNASU; 2220; -.
DR Ensembl; ENST00000291744.11; ENSP00000291744.6; ENSG00000160339.16. [Q15485-1]
DR Ensembl; ENST00000350339.3; ENSP00000291741.5; ENSG00000160339.16. [Q15485-2]
DR GeneID; 2220; -.
DR KEGG; hsa:2220; -.
DR MANE-Select; ENST00000291744.11; ENSP00000291744.6; NM_004108.3; NP_004099.2.
DR UCSC; uc004cfg.1; human. [Q15485-1]
DR CTD; 2220; -.
DR DisGeNET; 2220; -.
DR GeneCards; FCN2; -.
DR HGNC; HGNC:3624; FCN2.
DR HPA; ENSG00000160339; Tissue enriched (liver).
DR MIM; 601624; gene.
DR neXtProt; NX_Q15485; -.
DR OpenTargets; ENSG00000160339; -.
DR PharmGKB; PA28070; -.
DR VEuPathDB; HostDB:ENSG00000160339; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000164320; -.
DR HOGENOM; CLU_038628_3_3_1; -.
DR InParanoid; Q15485; -.
DR OMA; TANCAVQ; -.
DR OrthoDB; 1035379at2759; -.
DR PhylomeDB; Q15485; -.
DR TreeFam; TF329953; -.
DR PathwayCommons; Q15485; -.
DR Reactome; R-HSA-166662; Lectin pathway of complement activation.
DR Reactome; R-HSA-166663; Initial triggering of complement.
DR Reactome; R-HSA-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface.
DR SignaLink; Q15485; -.
DR SIGNOR; Q15485; -.
DR BioGRID-ORCS; 2220; 13 hits in 1058 CRISPR screens.
DR EvolutionaryTrace; Q15485; -.
DR GeneWiki; FCN2; -.
DR GenomeRNAi; 2220; -.
DR Pharos; Q15485; Tbio.
DR PRO; PR:Q15485; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q15485; protein.
DR Bgee; ENSG00000160339; Expressed in right lobe of liver and 92 other tissues.
DR Genevisible; Q15485; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
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:0009897; C:external side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IDA:ComplexPortal.
DR GO; GO:0003823; F:antigen binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0097367; F:carbohydrate derivative binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:2001065; F:mannan binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043394; F:proteoglycan binding; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0001867; P:complement activation, lectin pathway; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0008228; P:opsonization; IDA:UniProtKB.
DR GO; GO:1903028; P:positive regulation of opsonization; IDA:ComplexPortal.
DR GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
DR GO; GO:0043654; P:recognition of apoptotic cell; IDA:UniProtKB.
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 3D-structure; Alternative splicing; Calcium; Collagen;
KW Complement activation lectin pathway; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydroxylation; Immunity; Innate immunity;
KW Lectin; Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..313
FT /note="Ficolin-2"
FT /id="PRO_0000009139"
FT DOMAIN 51..92
FT /note="Collagen-like"
FT DOMAIN 96..313
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 51..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 241..242
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:17215869"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17215869,
FT ECO:0007744|PDB:2J1G"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17215869,
FT ECO:0007744|PDB:2J1G"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17215869,
FT ECO:0007744|PDB:2J1G"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17215869,
FT ECO:0007744|PDB:2J1G"
FT MOD_RES 77
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8586615"
FT MOD_RES 80
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8586615"
FT MOD_RES 86
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8586615"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:17215869"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 98..126
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT DISULFID 105..133
FT /evidence="ECO:0000269|PubMed:17215869,
FT ECO:0007744|PDB:2J1G"
FT DISULFID 257..270
FT /evidence="ECO:0000269|PubMed:17215869,
FT ECO:0007744|PDB:2J1G"
FT VAR_SEQ 34..71
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_030027"
FT VARIANT 80
FT /note="P -> L (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036342"
FT VARIANT 113
FT /note="H -> Y (in dbSNP:rs17549179)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_049072"
FT VARIANT 117
FT /note="G -> S (in dbSNP:rs12684476)"
FT /id="VAR_049073"
FT VARIANT 236
FT /note="T -> M (in dbSNP:rs17549193)"
FT /id="VAR_049074"
FT VARIANT 258
FT /note="A -> S (in dbSNP:rs7851696)"
FT /id="VAR_049075"
FT CONFLICT 61
FT /note="P -> D (in Ref. 1; BAA08352 and 2; ABB01005)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="C -> A (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:2J1G"
FT HELIX 105..110
FT /evidence="ECO:0007829|PDB:2J1G"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:2J1G"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2J3U"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:2J1G"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2J3U"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:2J1G"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:2J1G"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2J1G"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:2J1G"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2J1G"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:2J1G"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:2J3F"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:2J1G"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:4NYT"
FT TURN 215..219
FT /evidence="ECO:0007829|PDB:2J1G"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:4R9J"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2J1G"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:4R9J"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2J3F"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:4R9J"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:2J1G"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:2J61"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:2J1G"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4R9J"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:2J1G"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:2J1G"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:2J1G"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:2J3O"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:2J1G"
SQ SEQUENCE 313 AA; 34001 MW; D363029846CCB3C9 CRC64;
MELDRAVGVL GAATLLLSFL GMAWALQAAD TCPEVKMVGL EGSDKLTILR GCPGLPGAPG
PKGEAGTNGK RGERGPPGPP GKAGPPGPNG APGEPQPCLT GPRTCKDLLD RGHFLSGWHT
IYLPDCRPLT VLCDMDTDGG GWTVFQRRVD GSVDFYRDWA TYKQGFGSRL GEFWLGNDNI
HALTAQGTSE LRVDLVDFED NYQFAKYRSF KVADEAEKYN LVLGAFVEGS AGDSLTFHNN
QSFSTKDQDN DLNTGNCAVM FQGAWWYKNC HVSNLNGRYL RGTHGSFANG INWKSGKGYN
YSYKVSEMKV RPA
