FCN1_HUMAN
ID FCN1_HUMAN Reviewed; 326 AA.
AC O00602; Q5VYV5; Q92596;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Ficolin-1;
DE AltName: Full=Collagen/fibrinogen domain-containing protein 1;
DE AltName: Full=Ficolin-A;
DE AltName: Full=Ficolin-alpha;
DE AltName: Full=M-ficolin;
DE Flags: Precursor;
GN Name=FCN1; Synonyms=FCNM;
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 [MRNA].
RC TISSUE=Uterus;
RX PubMed=8573080; DOI=10.1042/bj3130473;
RA Lu J., Tay P.N., Kon O.L., Reid K.B.;
RT "Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes
RT as the major site of synthesis and assignment of the gene to chromosome
RT 9.";
RL Biochem. J. 313:473-478(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-326.
RC TISSUE=Uterus;
RX PubMed=8947836; DOI=10.1093/oxfordjournals.jbchem.a021474;
RA Harumiya S., Takeda K., Sugiura T., Fukumoto Y., Tachikawa H., Miyazono K.,
RA Fujimoto D., Ichijo H.;
RT "Characterization of ficolins as novel elastin-binding proteins and
RT molecular cloning of human ficolin-1.";
RL J. Biochem. 120:745-751(1996).
RN [7]
RP PROTEIN SEQUENCE OF 30-44.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CRP AND FFAR2.
RX PubMed=21037097; DOI=10.4049/jimmunol.1001225;
RA Zhang J., Yang L., Ang Z., Yoong S.L., Tran T.T., Anand G.S., Tan N.S.,
RA Ho B., Ding J.L.;
RT "Secreted M-ficolin anchors onto monocyte transmembrane G protein-coupled
RT receptor 43 and cross talks with plasma C-reactive protein to mediate
RT immune signaling and regulate host defense.";
RL J. Immunol. 185:6899-6910(2010).
RN [9]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=20400674; DOI=10.1189/jlb.1209802;
RA Honore C., Rorvig S., Hummelshoj T., Skjoedt M.O., Borregaard N.,
RA Garred P.;
RT "Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid
RT by the fibrinogen-like domain.";
RL J. Leukoc. Biol. 88:145-158(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 115-326 IN COMPLEX WITH CALCIUM,
RP SUBUNIT, DISULFIDE BONDS, CALCIUM-BINDING SITES, PH-DEPENDENCY, AND DOMAIN.
RX PubMed=17148457; DOI=10.1074/jbc.m608627200;
RA Tanio M., Kondo S., Sugio S., Kohno T.;
RT "Trivalent recognition unit of innate immunity system: crystal structure of
RT trimeric human M-ficolin fibrinogen-like domain.";
RL J. Biol. Chem. 282:3889-3895(2007).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 109-326 IN COMPLEX WITH CALCIUM
RP AND CARBOHYDRATE, SUBUNIT, DISULFIDE BONDS, CALCIUM-BINDING SITES,
RP PH-DEPENDENCY, AND DOMAIN.
RX PubMed=17897951; DOI=10.1074/jbc.m705741200;
RA Garlatti V., Martin L., Gout E., Reiser J.B., Fujita T., Arlaud G.J.,
RA Thielens N.M., Gaboriaud C.;
RT "Structural basis for innate immune sensing by M-ficolin and its control by
RT a pH-dependent conformational switch.";
RL J. Biol. Chem. 282:35814-35820(2007).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.21 ANGSTROMS) OF 110-326 IN COMPLEX WITH CALCIUM,
RP DISULFIDE BONDS, FUNCTION, SUBUNIT, SUBSTRATE SPECIFICITY, CALCIUM-BINDING
RP SITES, AND MUTAGENESIS OF GLY-250; ALA-285 AND TYR-300.
RX PubMed=20032467; DOI=10.1074/jbc.m109.065854;
RA Gout E., Garlatti V., Smith D.F., Lacroix M., Dumestre-Perard C.,
RA Lunardi T., Martin L., Cesbron J.Y., Arlaud G.J., Gaboriaud C.,
RA Thielens N.M.;
RT "Carbohydrate recognition properties of human ficolins: glycan array
RT screening reveals the sialic acid binding specificity of M-ficolin.";
RL J. Biol. Chem. 285:6612-6622(2010).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-175.
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: 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 (PubMed:21037097). Binds
CC preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and
CC to various glycans containing sialic acid engaged in a 2-3 linkage.
CC {ECO:0000269|PubMed:20032467, ECO:0000269|PubMed:21037097}.
CC -!- SUBUNIT: Homotrimer (PubMed:17897951). Interacts with elastin/ELN.
CC Interacts (via Fibrinogen C-terminal domain) with FFAR2. Interacts with
CC CRP; may regulate monocyte activation by FCN1.
CC {ECO:0000269|PubMed:17148457, ECO:0000269|PubMed:17897951,
CC ECO:0000269|PubMed:20032467, ECO:0000269|PubMed:21037097}.
CC -!- INTERACTION:
CC O00602; P02741: CRP; NbExp=4; IntAct=EBI-5282479, EBI-1395983;
CC O00602; P26022: PTX3; NbExp=3; IntAct=EBI-5282479, EBI-11574553;
CC O00602; Q2TS39: CRP-1; Xeno; NbExp=3; IntAct=EBI-5282479, EBI-7468648;
CC PRO_0000009136; O15552: FFAR2; NbExp=7; IntAct=EBI-11784425, EBI-2833872;
CC PRO_0000009136; P26022: PTX3; NbExp=7; IntAct=EBI-11784425, EBI-11574553;
CC PRO_0000009136; P02769: ALB; Xeno; NbExp=2; IntAct=EBI-11784425, EBI-2296927;
CC PRO_0000009136; PRO_0000000214 [P9WQP3]: fbpA; Xeno; NbExp=2; IntAct=EBI-11784425, EBI-26878164;
CC PRO_0000009136; P9WQP1: fbpB; Xeno; NbExp=3; IntAct=EBI-11784425, EBI-26878221;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20400674,
CC ECO:0000269|PubMed:21037097}. Cell membrane
CC {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}; Peripheral
CC membrane protein {ECO:0000269|PubMed:20400674,
CC ECO:0000269|PubMed:21037097}; Extracellular side
CC {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}. Note=Found
CC on the monocyte and granulocyte surface (PubMed:20400674).
CC -!- TISSUE SPECIFICITY: Peripheral blood leukocytes, monocytes and
CC granulocytes. Also detected in spleen, lung, and thymus, may be due to
CC the presence of tissue macrophages or trapped blood in these tissues.
CC Not detected on lymphocytes. {ECO:0000269|PubMed:20400674}.
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:0000269|PubMed:17148457, ECO:0000269|PubMed:17897951}.
CC -!- SIMILARITY: Belongs to the ficolin lectin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA12120.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S80990; AAB50706.1; -; mRNA.
DR EMBL; AK314867; BAG37382.1; -; mRNA.
DR EMBL; AL353611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88137.1; -; Genomic_DNA.
DR EMBL; BC020635; AAH20635.1; -; mRNA.
DR EMBL; D83920; BAA12120.1; ALT_INIT; mRNA.
DR CCDS; CCDS6985.1; -.
DR PIR; S61517; S61517.
DR RefSeq; NP_001994.2; NM_002003.4.
DR PDB; 2D39; X-ray; 1.90 A; A/B/C=115-326.
DR PDB; 2JHH; X-ray; 1.70 A; C/F=109-326.
DR PDB; 2JHI; X-ray; 1.80 A; F=109-326.
DR PDB; 2JHK; X-ray; 1.75 A; F=109-326.
DR PDB; 2JHL; X-ray; 1.75 A; F=109-326.
DR PDB; 2JHM; X-ray; 1.52 A; F=109-326.
DR PDB; 2WNP; X-ray; 1.21 A; F=110-326.
DR PDBsum; 2D39; -.
DR PDBsum; 2JHH; -.
DR PDBsum; 2JHI; -.
DR PDBsum; 2JHK; -.
DR PDBsum; 2JHL; -.
DR PDBsum; 2JHM; -.
DR PDBsum; 2WNP; -.
DR AlphaFoldDB; O00602; -.
DR BMRB; O00602; -.
DR SMR; O00602; -.
DR BioGRID; 108513; 36.
DR ComplexPortal; CPX-6172; FCN1-MASP1 lectin-protease complex.
DR ComplexPortal; CPX-6237; FCN1-MASP2 lectin-protease complex.
DR IntAct; O00602; 54.
DR MINT; O00602; -.
DR STRING; 9606.ENSP00000360871; -.
DR UniLectin; O00602; -.
DR GlyGen; O00602; 1 site.
DR PhosphoSitePlus; O00602; -.
DR BioMuta; FCN1; -.
DR EPD; O00602; -.
DR jPOST; O00602; -.
DR MassIVE; O00602; -.
DR PaxDb; O00602; -.
DR PeptideAtlas; O00602; -.
DR PRIDE; O00602; -.
DR ProteomicsDB; 47994; -.
DR Antibodypedia; 602; 401 antibodies from 31 providers.
DR DNASU; 2219; -.
DR Ensembl; ENST00000371806.4; ENSP00000360871.3; ENSG00000085265.12.
DR GeneID; 2219; -.
DR KEGG; hsa:2219; -.
DR MANE-Select; ENST00000371806.4; ENSP00000360871.3; NM_002003.5; NP_001994.2.
DR UCSC; uc004cfi.4; human.
DR CTD; 2219; -.
DR DisGeNET; 2219; -.
DR GeneCards; FCN1; -.
DR HGNC; HGNC:3623; FCN1.
DR HPA; ENSG00000085265; Group enriched (bone marrow, lung, lymphoid tissue).
DR MIM; 601252; gene.
DR neXtProt; NX_O00602; -.
DR OpenTargets; ENSG00000085265; -.
DR PharmGKB; PA28069; -.
DR VEuPathDB; HostDB:ENSG00000085265; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000157531; -.
DR HOGENOM; CLU_038628_3_3_1; -.
DR InParanoid; O00602; -.
DR OMA; HKSYANG; -.
DR OrthoDB; 1035379at2759; -.
DR PhylomeDB; O00602; -.
DR TreeFam; TF329953; -.
DR PathwayCommons; O00602; -.
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 Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; O00602; -.
DR BioGRID-ORCS; 2219; 9 hits in 1066 CRISPR screens.
DR EvolutionaryTrace; O00602; -.
DR GeneWiki; FCN1; -.
DR GenomeRNAi; 2219; -.
DR Pharos; O00602; Tbio.
DR PRO; PR:O00602; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O00602; protein.
DR Bgee; ENSG00000085265; Expressed in monocyte and 113 other tissues.
DR ExpressionAtlas; O00602; baseline and differential.
DR Genevisible; O00602; HS.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IDA:ComplexPortal.
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:0001664; F:G protein-coupled receptor binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038187; F:pattern recognition receptor activity; IMP:UniProtKB.
DR GO; GO:0033691; F:sialic acid 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; IMP:UniProtKB.
DR GO; GO:0001867; P:complement activation, lectin pathway; IDA:ComplexPortal.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:UniProtKB.
DR GO; GO:1903028; P:positive regulation of opsonization; IDA:ComplexPortal.
DR GO; GO:0034394; P:protein localization to cell surface; IDA:UniProtKB.
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; Calcium; Cell membrane; Collagen; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunity; Innate immunity; Lectin; Membrane;
KW Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 30..326
FT /note="Ficolin-1"
FT /id="PRO_0000009136"
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 72..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..154
FT /note="A domain; contributes to trimerization"
FT REGION 155..243
FT /note="B domain; contributes to trimerization"
FT REGION 317..326
FT /note="P domain"
FT /evidence="ECO:0000303|PubMed:17148457"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17148457,
FT ECO:0000269|PubMed:17897951, ECO:0000269|PubMed:20032467,
FT ECO:0007744|PDB:2D39, ECO:0007744|PDB:2WNP"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17148457,
FT ECO:0000269|PubMed:17897951, ECO:0000269|PubMed:20032467,
FT ECO:0007744|PDB:2D39, ECO:0007744|PDB:2WNP"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17148457,
FT ECO:0000269|PubMed:17897951, ECO:0000269|PubMed:20032467,
FT ECO:0007744|PDB:2D39, ECO:0007744|PDB:2WNP"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17148457,
FT ECO:0000269|PubMed:17897951, ECO:0000269|PubMed:20032467,
FT ECO:0007744|PDB:2D39, ECO:0007744|PDB:2WNP"
FT BINDING 282..284
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:17897951"
FT SITE 300
FT /note="Mediates specificity for sialic acids"
FT /evidence="ECO:0000305|PubMed:17897951,
FT ECO:0000305|PubMed:20032467"
FT SITE 312
FT /note="Mediates specificity for sialic acids"
FT /evidence="ECO:0000305|PubMed:17897951"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..139
FT /evidence="ECO:0000269|PubMed:17897951,
FT ECO:0000269|PubMed:20032467, ECO:0007744|PDB:2WNP"
FT DISULFID 118..146
FT /evidence="ECO:0000269|PubMed:17148457,
FT ECO:0000269|PubMed:17897951, ECO:0000269|PubMed:20032467,
FT ECO:0007744|PDB:2WNP"
FT DISULFID 270..283
FT /evidence="ECO:0000269|PubMed:17148457,
FT ECO:0000269|PubMed:17897951, ECO:0000269|PubMed:20032467,
FT ECO:0007744|PDB:2WNP"
FT VARIANT 93
FT /note="R -> Q (in dbSNP:rs56345770)"
FT /id="VAR_061172"
FT VARIANT 126
FT /note="Y -> H (in dbSNP:rs771359747)"
FT /id="VAR_024450"
FT VARIANT 175
FT /note="Y -> C (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036341"
FT MUTAGEN 250
FT /note="G->F: Inhibits binding to the 9-O-acetylated sialic
FT acid derivatives."
FT /evidence="ECO:0000269|PubMed:20032467"
FT MUTAGEN 285
FT /note="A->V: Inhibits binding to the 9-O-acetylated sialic
FT acid derivatives."
FT /evidence="ECO:0000269|PubMed:20032467"
FT MUTAGEN 300
FT /note="Y->F: Abolishes interaction with all sialic acid-
FT containing glycans."
FT /evidence="ECO:0000269|PubMed:20032467"
FT CONFLICT 133
FT /note="T -> N (in Ref. 1; AAB50706)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="N -> S (in Ref. 1; AAB50706)"
FT /evidence="ECO:0000305"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:2WNP"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:2WNP"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:2WNP"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:2WNP"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2WNP"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:2WNP"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:2WNP"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2D39"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:2WNP"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:2WNP"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:2WNP"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:2WNP"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:2WNP"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2WNP"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2WNP"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:2WNP"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:2WNP"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:2WNP"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:2WNP"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:2WNP"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:2WNP"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:2WNP"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:2WNP"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:2JHK"
FT STRAND 317..325
FT /evidence="ECO:0007829|PDB:2WNP"
SQ SEQUENCE 326 AA; 35078 MW; 184D24B371B251AB CRC64;
MELSGATMAR GLAVLLVLFL HIKNLPAQAA DTCPEVKVVG LEGSDKLTIL RGCPGLPGAP
GPKGEAGVIG ERGERGLPGA PGKAGPVGPK GDRGEKGMRG EKGDAGQSQS CATGPRNCKD
LLDRGYFLSG WHTIYLPDCR PLTVLCDMDT DGGGWTVFQR RMDGSVDFYR DWAAYKQGFG
SQLGEFWLGN DNIHALTAQG SSELRVDLVD FEGNHQFAKY KSFKVADEAE KYKLVLGAFV
GGSAGNSLTG HNNNFFSTKD QDNDVSSSNC AEKFQGAWWY ADCHASNLNG LYLMGPHESY
ANGINWSAAK GYKYSYKVSE MKVRPA
