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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi262 – 2621Calcium
Metal bindingi264 – 2641Calcium
Metal bindingi266 – 2661Calcium; via carbonyl oxygen
Metal bindingi268 – 2681Calcium; via carbonyl oxygen
Sitei300 – 3001Mediates specificity for sialic acids
Sitei312 – 3121Mediates specificity for sialic acids

GO - Molecular functioni

  1. antigen binding Source: ProtInc
  2. calcium ion binding Source: ProtInc
  3. carbohydrate binding Source: ProtInc
  4. G-protein coupled receptor binding Source: UniProtKB
  5. signaling pattern recognition receptor activity Source: UniProtKB

GO - Biological processi

  1. cell surface pattern recognition receptor signaling pathway Source: UniProtKB
  2. complement activation Source: Reactome
  3. complement activation, lectin pathway Source: Reactome
  4. G-protein coupled receptor signaling pathway Source: UniProtKB
  5. innate immune response Source: Reactome
  6. opsonization Source: ProtInc
  7. positive regulation of interleukin-8 secretion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Immunity, Innate immunity

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_163810. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
REACT_7964. Lectin pathway of complement activation.
REACT_8024. Initial triggering of complement.

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
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:3623. FCN1.

Subcellular locationi

Secreted. Cell membrane; Peripheral membrane protein; Extracellular side
Note: Found on the monocyte and granulocyte surface.

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. extracellular region Source: Reactome
  3. extrinsic component of external side of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi250 – 2501G → F: Inhibits binding to the 9-O-acetylated sialic acid derivatives. 1 Publication
Mutagenesisi285 – 2851A → V: Inhibits binding to the 9-O-acetylated sialic acid derivatives. 1 Publication
Mutagenesisi300 – 3001Y → F: Abolishes interaction with all sialic acid-containing glycans. 1 Publication

Organism-specific databases

PharmGKBiPA28069.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 PublicationAdd
BLAST
Chaini30 – 326297Ficolin-1PRO_0000009136Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi111 ↔ 139
Disulfide bondi118 ↔ 146
Disulfide bondi270 ↔ 283
Glycosylationi305 – 3051N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO00602.
PeptideAtlasiO00602.
PRIDEiO00602.

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

BgeeiO00602.
CleanExiHS_FCN1.
ExpressionAtlasiO00602. baseline and differential.
GenevestigatoriO00602.

Organism-specific databases

HPAiCAB016760.
HPA000685.
HPA001295.

Interactioni

Subunit structurei

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

Binary interactionsi

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

Protein-protein interaction databases

BioGridi108513. 15 interactions.
IntActiO00602. 1 interaction.
MINTiMINT-5223276.
STRINGi9606.ENSP00000360871.

Structurei

Secondary structure

1
326
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni111 – 1133Combined sources
Helixi118 – 1236Combined sources
Beta strandi130 – 1356Combined sources
Beta strandi141 – 1477Combined sources
Helixi150 – 1523Combined sources
Beta strandi155 – 16410Combined sources
Helixi172 – 1776Combined sources
Beta strandi179 – 1813Combined sources
Helixi190 – 1989Combined sources
Beta strandi202 – 2098Combined sources
Beta strandi215 – 2217Combined sources
Beta strandi223 – 2253Combined sources
Helixi228 – 2303Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi239 – 2413Combined sources
Helixi249 – 2513Combined sources
Beta strandi264 – 2685Combined sources
Helixi270 – 2734Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi285 – 2873Combined sources
Beta strandi298 – 3014Combined sources
Beta strandi303 – 3064Combined sources
Turni307 – 3093Combined sources
Beta strandi312 – 3154Combined sources
Beta strandi317 – 3259Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 110-326.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00602.

Family & Domainsi

Domains and Repeats

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

Region

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

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.

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

eggNOGiNOG249945.
GeneTreeiENSGT00770000120463.
HOGENOMiHOG000037127.
HOVERGENiHBG001644.
InParanoidiO00602.
KOiK10104.
OMAiNFFSTKD.
OrthoDBiEOG7X9G60.
PhylomeDBiO00602.
TreeFamiTF329953.

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.

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 BAA12120.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331T → N in AAB50706. (PubMed:8573080)Curated
Sequence conflicti287 – 2871N → S in AAB50706. (PubMed:8573080)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 931R → Q.
Corresponds to variant rs56345770 [ dbSNP | Ensembl ].
VAR_061172
Natural varianti126 – 1261Y → H.
Corresponds to variant rs17549179 [ dbSNP | Ensembl ].
VAR_024450
Natural varianti175 – 1751Y → C in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036341

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_002003.3.
UniGeneiHs.440898.

Genome annotation databases

EnsembliENST00000371806; ENSP00000360871; ENSG00000085265.
GeneIDi2219.
KEGGihsa:2219.
UCSCiuc004cfi.3. 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_002003.3.
UniGeneiHs.440898.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 110-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108513. 15 interactions.
IntActiO00602. 1 interaction.
MINTiMINT-5223276.
STRINGi9606.ENSP00000360871.

Proteomic databases

PaxDbiO00602.
PeptideAtlasiO00602.
PRIDEiO00602.

Protocols and materials databases

DNASUi2219.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371806; ENSP00000360871; ENSG00000085265.
GeneIDi2219.
KEGGihsa:2219.
UCSCiuc004cfi.3. human.

Organism-specific databases

CTDi2219.
GeneCardsiGC09M137801.
HGNCiHGNC:3623. FCN1.
HPAiCAB016760.
HPA000685.
HPA001295.
MIMi601252. gene.
neXtProtiNX_O00602.
PharmGKBiPA28069.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG249945.
GeneTreeiENSGT00770000120463.
HOGENOMiHOG000037127.
HOVERGENiHBG001644.
InParanoidiO00602.
KOiK10104.
OMAiNFFSTKD.
OrthoDBiEOG7X9G60.
PhylomeDBiO00602.
TreeFamiTF329953.

Enzyme and pathway databases

ReactomeiREACT_163810. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
REACT_7964. Lectin pathway of complement activation.
REACT_8024. Initial triggering of complement.

Miscellaneous databases

EvolutionaryTraceiO00602.
GeneWikiiFCN1.
GenomeRNAii2219.
NextBioi9001.
PROiO00602.
SOURCEiSearch...

Gene expression databases

BgeeiO00602.
CleanExiHS_FCN1.
ExpressionAtlasiO00602. baseline and differential.
GenevestigatoriO00602.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9."
    Lu J., Tay P.N., Kon O.L., Reid K.B.
    Biochem. J. 313:473-478(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Uterus.
  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].
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Lung.
  6. "Characterization of ficolins as novel elastin-binding proteins and molecular cloning of human ficolin-1."
    Harumiya S., Takeda K., Sugiura T., Fukumoto Y., Tachikawa H., Miyazono K., Fujimoto D., Ichijo H.
    J. Biochem. 120:745-751(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-326.
    Tissue: Uterus.
  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 30-44.
  8. "Secreted M-ficolin anchors onto monocyte transmembrane G protein-coupled receptor 43 and cross talks with plasma C-reactive protein to mediate immune signaling and regulate host defense."
    Zhang J., Yang L., Ang Z., Yoong S.L., Tran T.T., Anand G.S., Tan N.S., Ho B., Ding J.L.
    J. Immunol. 185:6899-6910(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CRP AND FFAR2.
  9. "Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain."
    Honore C., Rorvig S., Hummelshoj T., Skjoedt M.O., Borregaard N., Garred P.
    J. Leukoc. Biol. 88:145-158(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  10. "Trivalent recognition unit of innate immunity system: crystal structure of trimeric human M-ficolin fibrinogen-like domain."
    Tanio M., Kondo S., Sugio S., Kohno T.
    J. Biol. Chem. 282:3889-3895(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 115-326, SUBUNIT, DISULFIDE BONDS, CALCIUM-BINDING SITES, PH-DEPENDENCY.
  11. "Structural basis for innate immune sensing by M-ficolin and its control by a pH-dependent conformational switch."
    Garlatti V., Martin L., Gout E., Reiser J.B., Fujita T., Arlaud G.J., Thielens N.M., Gaboriaud C.
    J. Biol. Chem. 282:35814-35820(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 109-326 IN COMPLEX WITH CARBOHYDRATE, DISULFIDE BONDS, CALCIUM-BINDING SITES, PH-DEPENDENCY.
  12. "Carbohydrate recognition properties of human ficolins: glycan array screening reveals the sialic acid binding specificity of M-ficolin."
    Gout E., Garlatti V., Smith D.F., Lacroix M., Dumestre-Perard C., Lunardi T., Martin L., Cesbron J.Y., Arlaud G.J., Gaboriaud C., Thielens N.M.
    J. Biol. Chem. 285:6612-6622(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.21 ANGSTROMS) OF 110-326, DISULFIDE BONDS, FUNCTION, SUBUNIT, SUBSTRATE SPECIFICITY, CALCIUM-BINDING SITES, MUTAGENESIS OF GLY-250; ALA-285 AND TYR-300.
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-175.

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: February 4, 2015
This is version 137 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

External Data

Dasty 3

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 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.