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Protein

Ficolin-1

Gene

Fcn1

Organism
Mus musculus (Mouse)
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. 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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi270CalciumBy similarity1
Metal bindingi272CalciumBy similarity1
Sitei308Mediates specificity for sialic acidsBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Immunity, Innate immunity

Keywords - Ligandi

Calcium, Lectin, Metal-binding

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:Fcna
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1340905. Fcna.

Subcellular locationi

  • Secreted By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity; Extracellular side By similarity

  • Note: Found on the monocyte and granulocyte surface.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 171 PublicationAdd BLAST17
ChainiPRO_000000913718 – 334Ficolin-1Add BLAST317

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi119 ↔ 147PROSITE-ProRule annotation
Disulfide bondi126 ↔ 154PROSITE-ProRule annotation
Glycosylationi261N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi278 ↔ 291PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO70165.
PeptideAtlasiO70165.
PRIDEiO70165.

PTM databases

iPTMnetiO70165.
PhosphoSitePlusiO70165.

Expressioni

Tissue specificityi

Highly expressed in liver and spleen.

Gene expression databases

BgeeiENSMUSG00000026938.
CleanExiMM_FCNA.
ExpressionAtlasiO70165. baseline and differential.
GenevisibleiO70165. MM.

Interactioni

Subunit structurei

Homotrimer. Interacts with elastin/ELN. Interacts (via Fibrinogen C-terminal domain) with FFAR2. Interacts with CRP; may regulate monocyte activation by FCN1.By similarity

Protein-protein interaction databases

BioGridi199622. 1 interactor.
STRINGi10090.ENSMUSP00000028307.

Structurei

3D structure databases

ProteinModelPortaliO70165.
SMRiO70165.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini50 – 88Collagen-likeAdd BLAST39
Domaini117 – 334Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST218

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni123 – 162A domain; contributes to trimerizationBy similarityAdd BLAST40
Regioni163 – 251B domain; contributes to trimerizationBy similarityAdd BLAST89
Regioni290 – 292Carbohydrate-bindingBy similarity3
Regioni325 – 334P domainBy similarity10

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.By similarity

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.
InParanoidiO70165.
KOiK10104.
OMAiEMKIRAS.
OrthoDBiEOG091G03M1.
PhylomeDBiO70165.
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.

O70165-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQWPTLWAFS GLLCLCPSQA LGQERGACPD VKVVGLGAQD KVVVIQSCPG
60 70 80 90 100
FPGPPGPKGE PGSPAGRGER GFQGSPGKMG PAGSKGEPGT MGPPGVKGEK
110 120 130 140 150
GDTGAAPSLG EKELGDTLCQ RGPRSCKDLL TRGIFLTGWY TIHLPDCRPL
160 170 180 190 200
TVLCDMDVDG GGWTVFQRRV DGSIDFFRDW DSYKRGFGNL GTEFWLGNDY
210 220 230 240 250
LHLLTANGNQ ELRVDLQDFQ GKGSYAKYSS FQVSEEQEKY KLTLGQFLEG
260 270 280 290 300
TAGDSLTKHN NMSFTTHDQD NDANSMNCAA LFHGAWWYHN CHQSNLNGRY
310 320 330
LSGSHESYAD GINWGTGQGH HYSYKVAEMK IRAS
Length:334
Mass (Da):36,298
Last modified:August 1, 1998 - v1
Checksum:i9D30C05036AA04B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007813 mRNA. Translation: BAA25126.1.
BC019180 mRNA. Translation: AAH19180.1.
CCDSiCCDS15785.1.
PIRiJC5980.
RefSeqiNP_032021.1. NM_007995.3.
XP_006497736.1. XM_006497673.3.
XP_011237318.1. XM_011239016.2.
UniGeneiMm.10510.

Genome annotation databases

EnsembliENSMUST00000028307; ENSMUSP00000028307; ENSMUSG00000026938.
GeneIDi14133.
KEGGimmu:14133.
UCSCiuc008isz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007813 mRNA. Translation: BAA25126.1.
BC019180 mRNA. Translation: AAH19180.1.
CCDSiCCDS15785.1.
PIRiJC5980.
RefSeqiNP_032021.1. NM_007995.3.
XP_006497736.1. XM_006497673.3.
XP_011237318.1. XM_011239016.2.
UniGeneiMm.10510.

3D structure databases

ProteinModelPortaliO70165.
SMRiO70165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199622. 1 interactor.
STRINGi10090.ENSMUSP00000028307.

PTM databases

iPTMnetiO70165.
PhosphoSitePlusiO70165.

Proteomic databases

PaxDbiO70165.
PeptideAtlasiO70165.
PRIDEiO70165.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028307; ENSMUSP00000028307; ENSMUSG00000026938.
GeneIDi14133.
KEGGimmu:14133.
UCSCiuc008isz.1. mouse.

Organism-specific databases

CTDi14133.
MGIiMGI:1340905. Fcna.

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00830000128240.
HOGENOMiHOG000037127.
HOVERGENiHBG001644.
InParanoidiO70165.
KOiK10104.
OMAiEMKIRAS.
OrthoDBiEOG091G03M1.
PhylomeDBiO70165.
TreeFamiTF329953.

Miscellaneous databases

PROiO70165.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026938.
CleanExiMM_FCNA.
ExpressionAtlasiO70165. baseline and differential.
GenevisibleiO70165. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: O70165
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: August 1, 1998
Last modified: November 30, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.