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Protein

Ficolin-3

Gene

FCN3

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

Functioni

May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin. Has affinity with GalNAc, GlcNAc, D-fucose, as mono/oligosaccharide and lipopolysaccharides from S.typhimurium and S.minnesota.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi237 – 2371CalciumCombined sources1 Publication
Metal bindingi239 – 2391CalciumCombined sources1 Publication
Metal bindingi241 – 2411Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi243 – 2431Calcium; via carbonyl oxygenCombined sources1 Publication

GO - Molecular functioni

  • antigen binding Source: UniProtKB
  • carbohydrate binding Source: ProtInc
  • metal ion binding Source: UniProtKB-KW
  • serine-type endopeptidase activity Source: Reactome

GO - Biological processi

  • complement activation Source: UniProtKB
  • complement activation, lectin pathway Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • negative regulation of RNA biosynthetic process Source: UniProtKB
  • negative regulation of viral entry into host cell Source: UniProtKB
  • recognition of apoptotic cell Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Complement activation lectin pathway, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Enzyme and pathway databases

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.

Names & Taxonomyi

Protein namesi
Recommended name:
Ficolin-3
Alternative name(s):
Collagen/fibrinogen domain-containing lectin 3 p35
Collagen/fibrinogen domain-containing protein 3
Hakata antigen
Gene namesi
Name:FCN3
Synonyms:FCNH, HAKA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3625. FCN3.

Subcellular locationi

  • Secreted

  • Note: Found in blood plasma, bronchus, alveolus and bile duct.

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • collagen trimer Source: UniProtKB-KW
  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Ficolin 3 deficiency (FCN3D)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by immunodeficiency, recurrent infections, brain abscesses and recurrent warts on the fingers. Affected individuals have normal levels of lymphocytes, normal T-cell responses, and normal antibodies, but a selective deficient antibody response to pneumococcal polysaccharide vaccine.
See also OMIM:613860

Organism-specific databases

MalaCardsiFCN3.
MIMi613860. phenotype.
Orphaneti331190. Immunodeficiency due to ficolin3 deficiency.
PharmGKBiPA28071.

Polymorphism and mutation databases

BioMutaiFCN3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 299276Ficolin-3PRO_0000009142Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501Hydroxyproline1 Publication
Modified residuei53 – 531Hydroxyproline1 Publication
Modified residuei59 – 591Hydroxyproline1 Publication
Modified residuei65 – 651Hydroxyproline1 Publication
Modified residuei68 – 681Hydroxyproline1 Publication
Modified residuei77 – 771Hydroxyproline1 Publication
Disulfide bondi86 ↔ 110Combined sources1 Publication
Disulfide bondi93 ↔ 121Combined sources1 Publication
Glycosylationi189 – 1891N-linked (GlcNAc...) (complex)3 Publications
Disulfide bondi245 ↔ 258Combined sources1 Publication

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiO75636.
PeptideAtlasiO75636.
PRIDEiO75636.

PTM databases

iPTMnetiO75636.

Expressioni

Tissue specificityi

Liver and lung. In liver it is produced by bile duct epithelial cells and hepatocytes. In lung it is produced by both ciliated bronchial epithelial cells and type II alveolar epithelial cells.1 Publication

Gene expression databases

BgeeiO75636.
CleanExiHS_FCN3.
ExpressionAtlasiO75636. baseline and differential.
GenevisibleiO75636. HS.

Organism-specific databases

HPAiCAB025945.

Interactioni

Subunit structurei

Homotrimer (PubMed:17215869). May form an octadecamer consisting of an elementary trimer unit. Does not interact with fibronectin, elastin or zymosan. Interacts with MASP1 and MASP2.2 Publications

Protein-protein interaction databases

BioGridi114117. 1 interaction.
STRINGi9606.ENSP00000270879.

Structurei

Secondary structure

1
299
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi93 – 986Combined sources
Beta strandi103 – 1108Combined sources
Beta strandi116 – 1227Combined sources
Helixi125 – 1273Combined sources
Beta strandi130 – 13910Combined sources
Helixi147 – 1526Combined sources
Beta strandi154 – 1563Combined sources
Helixi165 – 1728Combined sources
Beta strandi173 – 1753Combined sources
Beta strandi178 – 1847Combined sources
Beta strandi190 – 1967Combined sources
Beta strandi198 – 2003Combined sources
Helixi203 – 2053Combined sources
Beta strandi209 – 2113Combined sources
Beta strandi214 – 2163Combined sources
Helixi224 – 2263Combined sources
Beta strandi239 – 2435Combined sources
Helixi245 – 2495Combined sources
Beta strandi256 – 2583Combined sources
Beta strandi269 – 2713Combined sources
Turni282 – 2854Combined sources
Beta strandi292 – 2998Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LA5model-A1-299[»]
2J5ZX-ray1.73A/B/C79-299[»]
2J60X-ray1.80A/B/C79-299[»]
2J64X-ray2.20A/B/C89-299[»]
ProteinModelPortaliO75636.
SMRiO75636. Positions 42-68, 86-299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75636.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 8033Collagen-likeAdd
BLAST
Domaini84 – 299216Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni258 – 2592Carbohydrate binding1 Publication

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.
InParanoidiO75636.
KOiK10104.
OMAiSSYKAGF.
OrthoDBiEOG7X9G60.
PhylomeDBiO75636.
TreeFamiTF351983.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR014716. 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]
PfamiPF00147. 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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75636-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDLLWILPSL WLLLLGGPAC LKTQEHPSCP GPRELEASKV VLLPSCPGAP
60 70 80 90 100
GSPGEKGAPG PQGPPGPPGK MGPKGEPGDP VNLLRCQEGP RNCRELLSQG
110 120 130 140 150
ATLSGWYHLC LPEGRALPVF CDMDTEGGGW LVFQRRQDGS VDFFRSWSSY
160 170 180 190 200
RAGFGNQESE FWLGNENLHQ LTLQGNWELR VELEDFNGNR TFAHYATFRL
210 220 230 240 250
LGEVDHYQLA LGKFSEGTAG DSLSLHSGRP FTTYDADHDS SNSNCAVIVH
260 270 280 290
GAWWYASCYR SNLNGRYAVS EAAAHKYGID WASGRGVGHP YRRVRMMLR
Length:299
Mass (Da):32,903
Last modified:March 7, 2006 - v2
Checksum:i5CB8A7D3668FA364
GO
Isoform 2 (identifier: O75636-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     79-89: Missing.

Show »
Length:288
Mass (Da):31,678
Checksum:i5027676AFCA39752
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2711E → D in BAA32277 (PubMed:9694814).Curated
Sequence conflicti271 – 2711E → D in AAH20731 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei79 – 8911Missing in isoform 2. 2 PublicationsVSP_001541Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88587 mRNA. Translation: BAA32277.1.
AK075140 mRNA. Translation: BAC11429.1.
CR456808 mRNA. Translation: CAG33089.1.
AY756173 Genomic DNA. Translation: AAU85296.1.
FO393419 Genomic DNA. No translation available.
BC020731 mRNA. Translation: AAH20731.1.
CCDSiCCDS300.1. [O75636-1]
CCDS301.1. [O75636-2]
RefSeqiNP_003656.2. NM_003665.2. [O75636-1]
NP_775628.1. NM_173452.1. [O75636-2]
UniGeneiHs.333383.

Genome annotation databases

EnsembliENST00000270879; ENSP00000270879; ENSG00000142748. [O75636-1]
ENST00000354982; ENSP00000347077; ENSG00000142748. [O75636-2]
GeneIDi8547.
KEGGihsa:8547.
UCSCiuc001boa.4. human. [O75636-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88587 mRNA. Translation: BAA32277.1.
AK075140 mRNA. Translation: BAC11429.1.
CR456808 mRNA. Translation: CAG33089.1.
AY756173 Genomic DNA. Translation: AAU85296.1.
FO393419 Genomic DNA. No translation available.
BC020731 mRNA. Translation: AAH20731.1.
CCDSiCCDS300.1. [O75636-1]
CCDS301.1. [O75636-2]
RefSeqiNP_003656.2. NM_003665.2. [O75636-1]
NP_775628.1. NM_173452.1. [O75636-2]
UniGeneiHs.333383.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LA5model-A1-299[»]
2J5ZX-ray1.73A/B/C79-299[»]
2J60X-ray1.80A/B/C79-299[»]
2J64X-ray2.20A/B/C89-299[»]
ProteinModelPortaliO75636.
SMRiO75636. Positions 42-68, 86-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114117. 1 interaction.
STRINGi9606.ENSP00000270879.

PTM databases

iPTMnetiO75636.

Polymorphism and mutation databases

BioMutaiFCN3.

Proteomic databases

PaxDbiO75636.
PeptideAtlasiO75636.
PRIDEiO75636.

Protocols and materials databases

DNASUi8547.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000270879; ENSP00000270879; ENSG00000142748. [O75636-1]
ENST00000354982; ENSP00000347077; ENSG00000142748. [O75636-2]
GeneIDi8547.
KEGGihsa:8547.
UCSCiuc001boa.4. human. [O75636-1]

Organism-specific databases

CTDi8547.
GeneCardsiFCN3.
HGNCiHGNC:3625. FCN3.
HPAiCAB025945.
MalaCardsiFCN3.
MIMi604973. gene.
613860. phenotype.
neXtProtiNX_O75636.
Orphaneti331190. Immunodeficiency due to ficolin3 deficiency.
PharmGKBiPA28071.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00830000128240.
HOGENOMiHOG000037127.
HOVERGENiHBG001644.
InParanoidiO75636.
KOiK10104.
OMAiSSYKAGF.
OrthoDBiEOG7X9G60.
PhylomeDBiO75636.
TreeFamiTF351983.

Enzyme and pathway databases

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.

Miscellaneous databases

ChiTaRSiFCN3. human.
EvolutionaryTraceiO75636.
GeneWikiiFCN3.
GenomeRNAii8547.
PROiO75636.
SOURCEiSearch...

Gene expression databases

BgeeiO75636.
CleanExiHS_FCN3.
ExpressionAtlasiO75636. baseline and differential.
GenevisibleiO75636. HS.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR014716. 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]
PfamiPF00147. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the Hakata antigen, a member of the ficolin/opsonin p35 lectin family."
    Sugimoto R., Yae Y., Akaiwa M., Kitajima S., Shibata Y., Sato H., Hirata J., Okochi K., Izuhara K., Hamasaki N.
    J. Biol. Chem. 273:20721-20727(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, HYDROXYLATION AT PRO-50; PRO-53; PRO-59; PRO-65; PRO-68 AND PRO-77.
    Tissue: Lung.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. SeattleSNPs variation discovery resource
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Lung.
  7. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-38.
  8. "Hakata antigen, a new member of the ficolin/opsonin p35 family, is a novel human lectin secreted into bronchus/alveolus and bile."
    Akaiwa M., Yae Y., Sugimoto R., Suzuki S.O., Iwaki T., Izuhara K., Hamasaki N.
    J. Histochem. Cytochem. 47:777-786(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "Activation of the lectin complement pathway by H-ficolin (Hakata antigen)."
    Matsushita M., Kuraya M., Hamasaki N., Tsujimura M., Shiraki H., Fujita T.
    J. Immunol. 168:3502-3506(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MASP1 AND MASP2.
  10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-189.
    Tissue: Plasma.
  11. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-189.
    Tissue: Liver.
  12. Cited for: GLYCOSYLATION AT ASN-189.
  13. "Immunodeficiency associated with FCN3 mutation and ficolin-3 deficiency."
    Munthe-Fog L., Hummelshoj T., Honore C., Madsen H.O., Permin H., Garred P.
    N. Engl. J. Med. 360:2637-2644(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN FCN3D.
  14. "In silico designed structure of ficolin precursor."
    Mallena S.C., Yadugiri K.
    Submitted (NOV-2002) to the PDB data bank
    Cited for: 3D-STRUCTURE MODELING.
  15. "Structural insights into the innate immune recognition specificities of L- and H-ficolins."
    Garlatti V., Belloy N., Martin L., Lacroix M., Matsushita M., Endo Y., Fujita T., Fontecilla-Camps J.C., Arlaud G.J., Thielens N.M., Gaboriaud C.
    EMBO J. 26:623-633(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 79-299 IN COMPLEX WITH CALCIUM AND GALACTOSE, DISULFIDE BONDS, SUBUNIT, FUNCTION.

Entry informationi

Entry nameiFCN3_HUMAN
AccessioniPrimary (citable) accession number: O75636
Secondary accession number(s): Q6IBJ5, Q8WW86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: March 7, 2006
Last modified: July 6, 2016
This is version 171 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.