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O00602 (FCN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ficolin-1
Alternative name(s):
Collagen/fibrinogen domain-containing protein 1
Ficolin-A
Ficolin-alpha
M-ficolin
Gene names
Name:FCN1
Synonyms:FCNM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.11

Subunit structure

Homotrimer. Interacts with elastin. Ref.9 Ref.11

Subcellular location

Secreted. Note: Found on the monocyte and granulocyte surface. Ref.8

Tissue specificity

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. Ref.8

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.

Sequence similarities

Belongs to the ficolin lectin family.

Contains 1 collagen-like domain.

Contains 1 fibrinogen C-terminal domain.

Sequence caution

The sequence BAA12120.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CRP-1Q2TS393EBI-5282479,EBI-7468648From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Ref.7
Chain30 – 326297Ficolin-1
PRO_0000009136

Regions

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

Sites

Metal binding2621Calcium
Metal binding2641Calcium
Metal binding2661Calcium; via carbonyl oxygen
Metal binding2681Calcium; via carbonyl oxygen
Site3001Mediates specificity for sialic acids
Site3121Mediates specificity for sialic acids

Amino acid modifications

Glycosylation3051N-linked (GlcNAc...) Potential
Disulfide bond111 ↔ 139 Ref.9 Ref.10 Ref.11
Disulfide bond118 ↔ 146 Ref.9 Ref.10 Ref.11
Disulfide bond270 ↔ 283 Ref.9 Ref.10 Ref.11

Natural variations

Natural variant931R → Q.
Corresponds to variant rs56345770 [ dbSNP | Ensembl ].
VAR_061172
Natural variant1261Y → H.
Corresponds to variant rs17549179 [ dbSNP | Ensembl ].
VAR_024450
Natural variant1751Y → C in a colorectal cancer sample; somatic mutation. Ref.12
VAR_036341

Experimental info

Mutagenesis2501G → F: Inhibits binding to the 9-O-acetylated sialic acid derivatives. Ref.11
Mutagenesis2851A → V: Inhibits binding to the 9-O-acetylated sialic acid derivatives. Ref.11
Mutagenesis3001Y → F: Abolishes interaction with all sialic acid-containing glycans. Ref.11
Sequence conflict1331T → N in AAB50706. Ref.1
Sequence conflict2871N → S in AAB50706. Ref.1

Secondary structure

.................................................. 326
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O00602 [UniParc].

Last modified May 2, 2002. Version 2.
Checksum: 184D24B371B251AB

FASTA32635,078
        10         20         30         40         50         60 
MELSGATMAR GLAVLLVLFL HIKNLPAQAA DTCPEVKVVG LEGSDKLTIL RGCPGLPGAP 

        70         80         90        100        110        120 
GPKGEAGVIG ERGERGLPGA PGKAGPVGPK GDRGEKGMRG EKGDAGQSQS CATGPRNCKD 

       130        140        150        160        170        180 
LLDRGYFLSG WHTIYLPDCR PLTVLCDMDT DGGGWTVFQR RMDGSVDFYR DWAAYKQGFG 

       190        200        210        220        230        240 
SQLGEFWLGN DNIHALTAQG SSELRVDLVD FEGNHQFAKY KSFKVADEAE KYKLVLGAFV 

       250        260        270        280        290        300 
GGSAGNSLTG HNNNFFSTKD QDNDVSSSNC AEKFQGAWWY ADCHASNLNG LYLMGPHESY 

       310        320 
ANGINWSAAK GYKYSYKVSE MKVRPA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-175.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6985.1.
PIRS61517.
RefSeqNP_001994.2. NM_002003.3.
UniGeneHs.440898.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalO00602.
SMRO00602. Positions 110-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108513. 2 interactions.
IntActO00602. 1 interaction.
MINTMINT-5223276.
STRING9606.ENSP00000360871.

Proteomic databases

PaxDbO00602.
PeptideAtlasO00602.
PRIDEO00602.

Protocols and materials databases

DNASU2219.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371806; ENSP00000360871; ENSG00000085265.
GeneID2219.
KEGGhsa:2219.
UCSCuc004cfi.3. human.

Organism-specific databases

CTD2219.
GeneCardsGC09M137801.
HGNCHGNC:3623. FCN1.
HPACAB016760.
HPA000685.
HPA001295.
MIM601252. gene.
neXtProtNX_O00602.
PharmGKBPA28069.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249945.
HOGENOMHOG000037127.
HOVERGENHBG001644.
KOK10104.
OMANFFSTKD.
OrthoDBEOG7X9G60.
PhylomeDBO00602.
TreeFamTF329953.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressO00602.
BgeeO00602.
CleanExHS_FCN1.
GenevestigatorO00602.

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...

Other

EvolutionaryTraceO00602.
GeneWikiFCN1.
GenomeRNAi2219.
NextBio9001.
PROO00602.
SOURCESearch...

Entry information

Entry nameFCN1_HUMAN
AccessionPrimary (citable) accession number: O00602
Secondary accession number(s): Q5VYV5, Q92596
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 2, 2002
Last modified: July 9, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM