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Protein

Ficolin-1

Gene

FCN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Extracellular lectin functioning as a pattern-recognition receptor in innate immunity. Binds the sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes and activates the lectin pathway of the complement system. May also activate monocytes through a G protein-coupled receptor, FFAR2, inducing the secretion of interleukin-8/IL-8 (PubMed:21037097). Binds preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi262CalciumCombined sources3 Publications1
Metal bindingi264CalciumCombined sources3 Publications1
Metal bindingi266Calcium; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi268Calcium; via carbonyl oxygenCombined sources3 Publications1
Sitei300Mediates specificity for sialic acids2 Publications1
Sitei312Mediates specificity for sialic acids1 Publication1

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB-KW
  • G-protein coupled receptor binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • serine-type endopeptidase activity Source: Reactome
  • sialic acid binding Source: UniProtKB
  • signaling pattern recognition receptor activity Source: UniProtKB

GO - Biological processi

  • cell surface pattern recognition receptor signaling pathway Source: UniProtKB
  • complement activation Source: Reactome
  • complement activation, lectin pathway Source: Reactome
  • G-protein coupled receptor signaling pathway Source: UniProtKB
  • negative regulation of viral entry into host cell Source: UniProtKB
  • positive regulation of interleukin-8 secretion Source: UniProtKB
  • protein localization to cell surface Source: UniProtKB
  • recognition of apoptotic cell Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Immunity, Innate immunity

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000085265-MONOMER.
ReactomeiR-HSA-166662. Lectin pathway of complement activation.
R-HSA-166663. Initial triggering of complement.
R-HSA-2855086. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
R-HSA-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Ficolin-1
Alternative name(s):
Collagen/fibrinogen domain-containing protein 1
Ficolin-A
Ficolin-alpha
M-ficolin
Gene namesi
Name:FCN1
Synonyms:FCNM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:3623. FCN1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi250G → F: Inhibits binding to the 9-O-acetylated sialic acid derivatives. 1 Publication1
Mutagenesisi285A → V: Inhibits binding to the 9-O-acetylated sialic acid derivatives. 1 Publication1
Mutagenesisi300Y → F: Abolishes interaction with all sialic acid-containing glycans. 1 Publication1

Organism-specific databases

DisGeNETi2219.
OpenTargetsiENSG00000085265.
PharmGKBiPA28069.

Polymorphism and mutation databases

BioMutaiFCN1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 291 PublicationAdd BLAST29
ChainiPRO_000000913630 – 326Ficolin-1Add BLAST297

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi111 ↔ 139Combined sources2 Publications
Disulfide bondi118 ↔ 146Combined sources3 Publications
Disulfide bondi270 ↔ 283Combined sources3 Publications
Glycosylationi305N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiO00602.
PaxDbiO00602.
PeptideAtlasiO00602.
PRIDEiO00602.

PTM databases

PhosphoSitePlusiO00602.

Expressioni

Tissue specificityi

Peripheral blood leukocytes, monocytes and granulocytes. Also detected in spleen, lung, and thymus, may be due to the presence of tissue macrophages or trapped blood in these tissues. Not detected on lymphocytes.1 Publication

Gene expression databases

BgeeiENSG00000085265.
CleanExiHS_FCN1.
ExpressionAtlasiO00602. baseline and differential.
GenevisibleiO00602. HS.

Organism-specific databases

HPAiCAB016760.
HPA000685.
HPA001295.

Interactioni

Subunit structurei

Homotrimer (PubMed:17897951). Interacts with elastin/ELN. Interacts (via Fibrinogen C-terminal domain) with FFAR2. Interacts with CRP; may regulate monocyte activation by FCN1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CRP-1Q2TS393EBI-5282479,EBI-7468648From a different organism.
PTX3P260223EBI-5282479,EBI-11574553

GO - Molecular functioni

  • G-protein coupled receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108513. 16 interactors.
IntActiO00602. 2 interactors.
MINTiMINT-5223276.
STRINGi9606.ENSP00000360871.

Structurei

Secondary structure

1326
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni111 – 113Combined sources3
Helixi118 – 123Combined sources6
Beta strandi130 – 135Combined sources6
Beta strandi141 – 147Combined sources7
Helixi150 – 152Combined sources3
Beta strandi155 – 164Combined sources10
Helixi172 – 177Combined sources6
Beta strandi179 – 181Combined sources3
Helixi190 – 198Combined sources9
Beta strandi202 – 209Combined sources8
Beta strandi215 – 221Combined sources7
Beta strandi223 – 225Combined sources3
Helixi228 – 230Combined sources3
Beta strandi234 – 236Combined sources3
Beta strandi239 – 241Combined sources3
Helixi249 – 251Combined sources3
Beta strandi264 – 268Combined sources5
Helixi270 – 273Combined sources4
Beta strandi281 – 283Combined sources3
Beta strandi285 – 287Combined sources3
Beta strandi298 – 301Combined sources4
Beta strandi303 – 306Combined sources4
Turni307 – 309Combined sources3
Beta strandi312 – 315Combined sources4
Beta strandi317 – 325Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2D39X-ray1.90A/B/C115-326[»]
2JHHX-ray1.70C/F109-326[»]
2JHIX-ray1.80F109-326[»]
2JHKX-ray1.75F109-326[»]
2JHLX-ray1.75F109-326[»]
2JHMX-ray1.52F109-326[»]
2WNPX-ray1.21F110-326[»]
ProteinModelPortaliO00602.
SMRiO00602.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00602.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 93Collagen-likeAdd BLAST39
Domaini109 – 326Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST218

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni115 – 154A domain; contributes to trimerizationAdd BLAST40
Regioni155 – 243B domain; contributes to trimerizationAdd BLAST89
Regioni282 – 284Carbohydrate-binding1 Publication3
Regioni317 – 326P domain1 Publication10

Domaini

The fibrinogen C-terminal domain mediates calcium-dependent binding to carbohydrates and tethering to the cell surface in monocytes and granulocytes. The domain undergoes a conformational switch at pH under 6.2, and looses its carbohydrate-binding ability.2 Publications

Sequence similaritiesi

Belongs to the ficolin lectin family.Curated
Contains 1 collagen-like domain.Curated
Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00830000128240.
HOGENOMiHOG000037127.
HOVERGENiHBG001644.
InParanoidiO00602.
KOiK10104.
OMAiWYADCHA.
PhylomeDBiO00602.
TreeFamiTF329953.

Family and domain databases

CDDicd00087. FReD. 1 hit.
Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR008160. Collagen.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR020837. Fibrinogen_CS.
[Graphical view]
PfamiPF01391. Collagen. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O00602-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELSGATMAR GLAVLLVLFL HIKNLPAQAA DTCPEVKVVG LEGSDKLTIL
60 70 80 90 100
RGCPGLPGAP GPKGEAGVIG ERGERGLPGA PGKAGPVGPK GDRGEKGMRG
110 120 130 140 150
EKGDAGQSQS CATGPRNCKD LLDRGYFLSG WHTIYLPDCR PLTVLCDMDT
160 170 180 190 200
DGGGWTVFQR RMDGSVDFYR DWAAYKQGFG SQLGEFWLGN DNIHALTAQG
210 220 230 240 250
SSELRVDLVD FEGNHQFAKY KSFKVADEAE KYKLVLGAFV GGSAGNSLTG
260 270 280 290 300
HNNNFFSTKD QDNDVSSSNC AEKFQGAWWY ADCHASNLNG LYLMGPHESY
310 320
ANGINWSAAK GYKYSYKVSE MKVRPA
Length:326
Mass (Da):35,078
Last modified:May 2, 2002 - v2
Checksum:i184D24B371B251AB
GO

Sequence cautioni

The sequence BAA12120 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti133T → N in AAB50706 (PubMed:8573080).Curated1
Sequence conflicti287N → S in AAB50706 (PubMed:8573080).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06117293R → Q.Corresponds to variant rs56345770dbSNPEnsembl.1
Natural variantiVAR_024450126Y → H.Corresponds to variant rs17549179dbSNPEnsembl.1
Natural variantiVAR_036341175Y → C in a colorectal cancer sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S80990 mRNA. Translation: AAB50706.1.
AK314867 mRNA. Translation: BAG37382.1.
AL353611 Genomic DNA. Translation: CAH73911.1.
CH471090 Genomic DNA. Translation: EAW88137.1.
BC020635 mRNA. Translation: AAH20635.1.
D83920 mRNA. Translation: BAA12120.1. Different initiation.
CCDSiCCDS6985.1.
PIRiS61517.
RefSeqiNP_001994.2. NM_002003.4.
UniGeneiHs.440898.
Hs.638586.

Genome annotation databases

EnsembliENST00000371806; ENSP00000360871; ENSG00000085265.
GeneIDi2219.
KEGGihsa:2219.
UCSCiuc004cfi.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S80990 mRNA. Translation: AAB50706.1.
AK314867 mRNA. Translation: BAG37382.1.
AL353611 Genomic DNA. Translation: CAH73911.1.
CH471090 Genomic DNA. Translation: EAW88137.1.
BC020635 mRNA. Translation: AAH20635.1.
D83920 mRNA. Translation: BAA12120.1. Different initiation.
CCDSiCCDS6985.1.
PIRiS61517.
RefSeqiNP_001994.2. NM_002003.4.
UniGeneiHs.440898.
Hs.638586.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2D39X-ray1.90A/B/C115-326[»]
2JHHX-ray1.70C/F109-326[»]
2JHIX-ray1.80F109-326[»]
2JHKX-ray1.75F109-326[»]
2JHLX-ray1.75F109-326[»]
2JHMX-ray1.52F109-326[»]
2WNPX-ray1.21F110-326[»]
ProteinModelPortaliO00602.
SMRiO00602.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108513. 16 interactors.
IntActiO00602. 2 interactors.
MINTiMINT-5223276.
STRINGi9606.ENSP00000360871.

PTM databases

PhosphoSitePlusiO00602.

Polymorphism and mutation databases

BioMutaiFCN1.

Proteomic databases

EPDiO00602.
PaxDbiO00602.
PeptideAtlasiO00602.
PRIDEiO00602.

Protocols and materials databases

DNASUi2219.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371806; ENSP00000360871; ENSG00000085265.
GeneIDi2219.
KEGGihsa:2219.
UCSCiuc004cfi.4. human.

Organism-specific databases

CTDi2219.
DisGeNETi2219.
GeneCardsiFCN1.
HGNCiHGNC:3623. FCN1.
HPAiCAB016760.
HPA000685.
HPA001295.
MIMi601252. gene.
neXtProtiNX_O00602.
OpenTargetsiENSG00000085265.
PharmGKBiPA28069.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00830000128240.
HOGENOMiHOG000037127.
HOVERGENiHBG001644.
InParanoidiO00602.
KOiK10104.
OMAiWYADCHA.
PhylomeDBiO00602.
TreeFamiTF329953.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000085265-MONOMER.
ReactomeiR-HSA-166662. Lectin pathway of complement activation.
R-HSA-166663. Initial triggering of complement.
R-HSA-2855086. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiO00602.
GeneWikiiFCN1.
GenomeRNAii2219.
PROiO00602.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000085265.
CleanExiHS_FCN1.
ExpressionAtlasiO00602. baseline and differential.
GenevisibleiO00602. HS.

Family and domain databases

CDDicd00087. FReD. 1 hit.
Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR008160. Collagen.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR020837. Fibrinogen_CS.
[Graphical view]
PfamiPF01391. Collagen. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFCN1_HUMAN
AccessioniPrimary (citable) accession number: O00602
Secondary accession number(s): Q5VYV5, Q92596
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 2, 2002
Last modified: November 30, 2016
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.