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Q29042 (FCN1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ficolin-1
Alternative name(s):
Ficolin-A
Ficolin-alpha
Gene names
Name:FCN1
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Complement-activating lectin and pattern recognition receptor. Binds GlcNAc. 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.

Subunit structure

Homotrimer By similarity. Interacts with elastin. Ref.1

Subcellular location

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

Tissue specificity

Most abundantly expressed in placenta and lung. Ref.1

Domain

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 similarities

Belongs to the ficolin lectin family.

Contains 1 collagen-like domain.

Contains 1 fibrinogen C-terminal domain.

Ontologies

Keywords
   Biological processImmunity
Innate immunity
   Cellular componentSecreted
   DomainCollagen
Repeat
Signal
   LigandCalcium
Lectin
Metal-binding
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processinnate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcollagen

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 By similarity
Chain30 – 326297Ficolin-1
PRO_0000269570

Regions

Domain55 – 9339Collagen-like
Domain109 – 326218Fibrinogen C-terminal
Region115 – 15440A domain; contributes to trimerization By similarity
Region155 – 24389B domain; contributes to trimerization By similarity
Region282 – 2843Carbohydrate-binding By similarity
Region317 – 32610P domain By similarity

Sites

Metal binding2621Calcium By similarity
Metal binding2641Calcium By similarity
Site3001Mediates specificity for sialic acids By similarity
Site3121Mediates specificity for sialic acids By similarity

Amino acid modifications

Glycosylation2651N-linked (GlcNAc...) Potential
Glycosylation3131N-linked (GlcNAc...) Potential
Disulfide bond111 ↔ 139 By similarity
Disulfide bond118 ↔ 146 By similarity
Disulfide bond270 ↔ 283 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q29042 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 170A5E9EA1E8F310

FASTA32635,246
        10         20         30         40         50         60 
MELSRVAVAL GPTGQLLLFL SFQTLAAQAA DTCPEVKVVG LEGSDKLSIL RGCPGLPGAA 

        70         80         90        100        110        120 
GPKGEAGANG PKGERGSPGV VGKAGPAGPK GDRGEKGARG EKGEPGQLQS CATGPRTCKE 

       130        140        150        160        170        180 
LLTRGHFLSG WHTIYLPDCQ PLTVLCDMDT DGGGWTVFQR RSDGSVDFYR DWAAYKRGFG 

       190        200        210        220        230        240 
SQLGEFWLGN DHIHALTAQG TSELRVDLVD FEGNHQFAKY RSFQVAGEAE KYKLVLGGFL 

       250        260        270        280        290        300 
EGNAGDSLSS HRDQFFSTKD QDNDNHSGNC AEQYHGAWWY NACHSSNLNG RYLRGLHTSY 

       310        320 
ANGVNWRSGR GYNYSYQVSE MKVRLT 

« Hide

References

[1]"Molecular cloning and characterization of ficolin, a multimeric protein with fibrinogen- and collagen-like domains."
Ichijo H., Hellman U., Wernstedt C., Gonez L.J., Claesson-Welsh L., Heldin C.H., Miyazono K.
J. Biol. Chem. 268:14505-14513(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, TISSUE SPECIFICITY.
Tissue: Uterus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L12345 mRNA. Translation: AAC69641.1.
PIRB47172.
RefSeqNP_999325.1. NM_214160.2.
UniGeneSsc.16008.

3D structure databases

ProteinModelPortalQ29042.
SMRQ29042. Positions 111-324.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397316.
KEGGssc:397316.

Organism-specific databases

CTD2219.

Phylogenomic databases

HOVERGENHBG001644.
KOK10104.

Family and domain databases

Gene3D3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProIPR008160. 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]
PfamPF01391. Collagen. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMSSF56496. SSF56496. 1 hit.
PROSITEPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFCN1_PIG
AccessionPrimary (citable) accession number: Q29042
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families