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Q29042

- FCN1_PIG

UniProt

Q29042 - FCN1_PIG

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Protein

Ficolin-1

Gene
FCN1
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi262 – 2621Calcium By similarity
Metal bindingi264 – 2641Calcium By similarity
Sitei300 – 3001Mediates specificity for sialic acids By similarity
Sitei312 – 3121Mediates specificity for sialic acids By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. innate immune response Source: UniProtKB-KW
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):
Ficolin-A
Ficolin-alpha
Gene namesi
Name:FCN1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

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

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929 By similarityAdd
BLAST
Chaini30 – 326297Ficolin-1PRO_0000269570Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi111 ↔ 139 By similarity
Disulfide bondi118 ↔ 146 By similarity
Glycosylationi265 – 2651N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi270 ↔ 283 By similarity
Glycosylationi313 – 3131N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Most abundantly expressed in placenta and lung.1 Publication

Interactioni

Subunit structurei

Homotrimer By similarity. Interacts with elastin.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ29042.
SMRiQ29042. Positions 111-324.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 9339Collagen-likeAdd
BLAST
Domaini109 – 326218Fibrinogen C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni115 – 15440A domain; contributes to trimerization By similarityAdd
BLAST
Regioni155 – 24389B domain; contributes to trimerization By similarityAdd
BLAST
Regioni282 – 2843Carbohydrate-binding By similarity
Regioni317 – 32610P domain By similarity

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.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

HOVERGENiHBG001644.
KOiK10104.

Family and domain databases

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.

Q29042-1 [UniParc]FASTAAdd to Basket

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MELSRVAVAL GPTGQLLLFL SFQTLAAQAA DTCPEVKVVG LEGSDKLSIL    50
RGCPGLPGAA GPKGEAGANG PKGERGSPGV VGKAGPAGPK GDRGEKGARG 100
EKGEPGQLQS CATGPRTCKE LLTRGHFLSG WHTIYLPDCQ PLTVLCDMDT 150
DGGGWTVFQR RSDGSVDFYR DWAAYKRGFG SQLGEFWLGN DHIHALTAQG 200
TSELRVDLVD FEGNHQFAKY RSFQVAGEAE KYKLVLGGFL EGNAGDSLSS 250
HRDQFFSTKD QDNDNHSGNC AEQYHGAWWY NACHSSNLNG RYLRGLHTSY 300
ANGVNWRSGR GYNYSYQVSE MKVRLT 326
Length:326
Mass (Da):35,246
Last modified:November 1, 1996 - v1
Checksum:i170A5E9EA1E8F310
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L12345 mRNA. Translation: AAC69641.1.
PIRiB47172.
RefSeqiNP_999325.1. NM_214160.2.
UniGeneiSsc.16008.

Genome annotation databases

GeneIDi397316.
KEGGissc:397316.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L12345 mRNA. Translation: AAC69641.1 .
PIRi B47172.
RefSeqi NP_999325.1. NM_214160.2.
UniGenei Ssc.16008.

3D structure databases

ProteinModelPortali Q29042.
SMRi Q29042. Positions 111-324.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 397316.
KEGGi ssc:397316.

Organism-specific databases

CTDi 2219.

Phylogenomic databases

HOVERGENi HBG001644.
KOi K10104.

Family and domain databases

Gene3Di 3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProi IPR008160. 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 ]
Pfami PF01391. Collagen. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view ]
SMARTi SM00186. FBG. 1 hit.
[Graphical view ]
SUPFAMi SSF56496. SSF56496. 1 hit.
PROSITEi PS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiFCN1_PIG
AccessioniPrimary (citable) accession number: Q29042
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 67 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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