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O00602

- FCN1_HUMAN

UniProt

O00602 - FCN1_HUMAN

Protein

Ficolin-1

Gene

FCN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (02 May 2002)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    6. 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

    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

    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

    ArrayExpressiO00602.
    BgeeiO00602.
    CleanExiHS_FCN1.
    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. 2 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 – 1133
    Helixi118 – 1236
    Beta strandi130 – 1356
    Beta strandi141 – 1477
    Helixi150 – 1523
    Beta strandi155 – 16410
    Helixi172 – 1776
    Beta strandi179 – 1813
    Helixi190 – 1989
    Beta strandi202 – 2098
    Beta strandi215 – 2217
    Beta strandi223 – 2253
    Helixi228 – 2303
    Beta strandi234 – 2363
    Beta strandi239 – 2413
    Helixi249 – 2513
    Beta strandi264 – 2685
    Helixi270 – 2734
    Beta strandi281 – 2833
    Beta strandi285 – 2873
    Beta strandi298 – 3014
    Beta strandi303 – 3064
    Turni307 – 3093
    Beta strandi312 – 3154
    Beta strandi317 – 3259

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000037127.
    HOVERGENiHBG001644.
    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

    MELSGATMAR GLAVLLVLFL HIKNLPAQAA DTCPEVKVVG LEGSDKLTIL    50
    RGCPGLPGAP GPKGEAGVIG ERGERGLPGA PGKAGPVGPK GDRGEKGMRG 100
    EKGDAGQSQS CATGPRNCKD LLDRGYFLSG WHTIYLPDCR PLTVLCDMDT 150
    DGGGWTVFQR RMDGSVDFYR DWAAYKQGFG SQLGEFWLGN DNIHALTAQG 200
    SSELRVDLVD FEGNHQFAKY KSFKVADEAE KYKLVLGAFV GGSAGNSLTG 250
    HNNNFFSTKD QDNDVSSSNC AEKFQGAWWY ADCHASNLNG LYLMGPHESY 300
    ANGINWSAAK GYKYSYKVSE MKVRPA 326
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS6985.1.
    PIRi S61517.
    RefSeqi NP_001994.2. NM_002003.3.
    UniGenei Hs.440898.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D39 X-ray 1.90 A/B/C 115-326 [» ]
    2JHH X-ray 1.70 C/F 109-326 [» ]
    2JHI X-ray 1.80 F 109-326 [» ]
    2JHK X-ray 1.75 F 109-326 [» ]
    2JHL X-ray 1.75 F 109-326 [» ]
    2JHM X-ray 1.52 F 109-326 [» ]
    2WNP X-ray 1.21 F 110-326 [» ]
    ProteinModelPortali O00602.
    SMRi O00602. Positions 110-326.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108513. 2 interactions.
    IntActi O00602. 1 interaction.
    MINTi MINT-5223276.
    STRINGi 9606.ENSP00000360871.

    Proteomic databases

    PaxDbi O00602.
    PeptideAtlasi O00602.
    PRIDEi O00602.

    Protocols and materials databases

    DNASUi 2219.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371806 ; ENSP00000360871 ; ENSG00000085265 .
    GeneIDi 2219.
    KEGGi hsa:2219.
    UCSCi uc004cfi.3. human.

    Organism-specific databases

    CTDi 2219.
    GeneCardsi GC09M137801.
    HGNCi HGNC:3623. FCN1.
    HPAi CAB016760.
    HPA000685.
    HPA001295.
    MIMi 601252. gene.
    neXtProti NX_O00602.
    PharmGKBi PA28069.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249945.
    HOGENOMi HOG000037127.
    HOVERGENi HBG001644.
    KOi K10104.
    OMAi NFFSTKD.
    OrthoDBi EOG7X9G60.
    PhylomeDBi O00602.
    TreeFami TF329953.

    Enzyme and pathway databases

    Reactomei REACT_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

    EvolutionaryTracei O00602.
    GeneWikii FCN1.
    GenomeRNAii 2219.
    NextBioi 9001.
    PROi O00602.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00602.
    Bgeei O00602.
    CleanExi HS_FCN1.
    Genevestigatori O00602.

    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. "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: October 1, 2014
    This is version 133 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