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Ficolin-3 (Collagen/fibrinogen domain-containing lectin 3 p35) (Collagen/fibrinogen domain-containing protein 3) (Hakata antigen)

 FCN3_HUMAN              Reviewed;         299 AA.
O75636; Q6IBJ5; Q8WW86;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 2.
28-FEB-2018, entry version 182.
RecName: Full=Ficolin-3;
AltName: Full=Collagen/fibrinogen domain-containing lectin 3 p35;
AltName: Full=Collagen/fibrinogen domain-containing protein 3;
AltName: Full=Hakata antigen;
Flags: Precursor;
Name=FCN3; Synonyms=FCNH, HAKA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
HYDROXYLATION AT PRO-50; PRO-53; PRO-59; PRO-65; PRO-68 AND PRO-77.
TISSUE=Lung;
PubMed=9694814; DOI=10.1074/jbc.273.33.20721;
Sugimoto R., Yae Y., Akaiwa M., Kitajima S., Shibata Y., Sato H.,
Hirata J., Okochi K., Izuhara K., Hamasaki N.;
"Cloning and characterization of the Hakata antigen, a member of the
ficolin/opsonin p35 lectin family.";
J. Biol. Chem. 273:20721-20727(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 24-38.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[8]
TISSUE SPECIFICITY.
PubMed=10330454; DOI=10.1177/002215549904700607;
Akaiwa M., Yae Y., Sugimoto R., Suzuki S.O., Iwaki T., Izuhara K.,
Hamasaki N.;
"Hakata antigen, a new member of the ficolin/opsonin p35 family, is a
novel human lectin secreted into bronchus/alveolus and bile.";
J. Histochem. Cytochem. 47:777-786(1999).
[9]
FUNCTION, AND INTERACTION WITH MASP1 AND MASP2.
PubMed=11907111; DOI=10.4049/jimmunol.168.7.3502;
Matsushita M., Kuraya M., Hamasaki N., Tsujimura M., Shiraki H.,
Fujita T.;
"Activation of the lectin complement pathway by H-ficolin (Hakata
antigen).";
J. Immunol. 168:3502-3506(2002).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-189.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-189.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[12]
GLYCOSYLATION AT ASN-189.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[13]
INVOLVEMENT IN FCN3D.
PubMed=19535802; DOI=10.1056/NEJMoa0900381;
Munthe-Fog L., Hummelshoj T., Honore C., Madsen H.O., Permin H.,
Garred P.;
"Immunodeficiency associated with FCN3 mutation and ficolin-3
deficiency.";
N. Engl. J. Med. 360:2637-2644(2009).
[14]
3D-STRUCTURE MODELING.
Mallena S.C., Yadugiri K.;
"In silico designed structure of ficolin precursor.";
Submitted (NOV-2002) to the PDB data bank.
[15]
X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 79-299 IN COMPLEX WITH
CALCIUM AND GALACTOSE, DISULFIDE BONDS, SUBUNIT, AND FUNCTION.
PubMed=17215869; DOI=10.1038/sj.emboj.7601500;
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.;
"Structural insights into the innate immune recognition specificities
of L- and H-ficolins.";
EMBO J. 26:623-633(2007).
-!- FUNCTION: 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. {ECO:0000269|PubMed:11907111,
ECO:0000269|PubMed:17215869}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:11907111, ECO:0000269|PubMed:17215869}.
-!- SUBCELLULAR LOCATION: Secreted. Note=Found in blood plasma,
bronchus, alveolus and bile duct.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O75636-1; Sequence=Displayed;
Name=2;
IsoId=O75636-2; Sequence=VSP_001541;
-!- TISSUE SPECIFICITY: 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. {ECO:0000269|PubMed:10330454}.
-!- PTM: The N-terminus is blocked.
-!- DISEASE: Ficolin 3 deficiency (FCN3D) [MIM:613860]: A 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.
{ECO:0000269|PubMed:19535802}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ficolin lectin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/fcn3/";
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EMBL; D88587; BAA32277.1; -; mRNA.
EMBL; AK075140; BAC11429.1; -; mRNA.
EMBL; CR456808; CAG33089.1; -; mRNA.
EMBL; AY756173; AAU85296.1; -; Genomic_DNA.
EMBL; FO393419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC020731; AAH20731.1; -; mRNA.
CCDS; CCDS300.1; -. [O75636-1]
CCDS; CCDS301.1; -. [O75636-2]
RefSeq; NP_003656.2; NM_003665.3. [O75636-1]
RefSeq; NP_775628.1; NM_173452.2. [O75636-2]
UniGene; Hs.333383; -.
PDB; 1LA5; Model; -; A=1-299.
PDB; 2J5Z; X-ray; 1.73 A; A/B/C=79-299.
PDB; 2J60; X-ray; 1.80 A; A/B/C=79-299.
PDB; 2J64; X-ray; 2.20 A; A/B/C=79-299.
PDBsum; 1LA5; -.
PDBsum; 2J5Z; -.
PDBsum; 2J60; -.
PDBsum; 2J64; -.
ProteinModelPortal; O75636; -.
SMR; O75636; -.
BioGrid; 114117; 1.
IntAct; O75636; 1.
STRING; 9606.ENSP00000270879; -.
iPTMnet; O75636; -.
PhosphoSitePlus; O75636; -.
BioMuta; FCN3; -.
PaxDb; O75636; -.
PeptideAtlas; O75636; -.
PRIDE; O75636; -.
DNASU; 8547; -.
Ensembl; ENST00000270879; ENSP00000270879; ENSG00000142748. [O75636-1]
Ensembl; ENST00000354982; ENSP00000347077; ENSG00000142748. [O75636-2]
GeneID; 8547; -.
KEGG; hsa:8547; -.
UCSC; uc001boa.4; human. [O75636-1]
CTD; 8547; -.
DisGeNET; 8547; -.
EuPathDB; HostDB:ENSG00000142748.12; -.
GeneCards; FCN3; -.
HGNC; HGNC:3625; FCN3.
HPA; CAB025945; -.
MalaCards; FCN3; -.
MIM; 604973; gene.
MIM; 613860; phenotype.
neXtProt; NX_O75636; -.
OpenTargets; ENSG00000142748; -.
Orphanet; 331190; Immunodeficiency due to ficolin3 deficiency.
PharmGKB; PA28071; -.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
GeneTree; ENSGT00830000128240; -.
HOGENOM; HOG000037127; -.
HOVERGEN; HBG001644; -.
InParanoid; O75636; -.
KO; K10104; -.
OMA; SSYKAGF; -.
OrthoDB; EOG091G03M1; -.
PhylomeDB; O75636; -.
TreeFam; TF351983; -.
Reactome; R-HSA-166662; Lectin pathway of complement activation.
Reactome; R-HSA-166663; Initial triggering of complement.
Reactome; R-HSA-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface.
ChiTaRS; FCN3; human.
EvolutionaryTrace; O75636; -.
GeneWiki; FCN3; -.
GenomeRNAi; 8547; -.
PRO; PR:O75636; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000142748; -.
CleanEx; HS_FCN3; -.
ExpressionAtlas; O75636; baseline and differential.
Genevisible; O75636; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0003823; F:antigen binding; IDA:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0006956; P:complement activation; IDA:UniProtKB.
GO; GO:0001867; P:complement activation, lectin pathway; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:1902679; P:negative regulation of RNA biosynthetic process; IDA:UniProtKB.
GO; GO:0046597; P:negative regulation of viral entry into host cell; IMP:UniProtKB.
GO; GO:0043654; P:recognition of apoptotic cell; IDA:UniProtKB.
CDD; cd00087; FReD; 1.
Gene3D; 3.90.215.10; -; 1.
Gene3D; 4.10.530.10; -; 1.
InterPro; IPR036056; Fibrinogen-like_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
InterPro; IPR014715; Fibrinogen_a/b/g_C_2.
InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
InterPro; IPR020837; Fibrinogen_CS.
Pfam; PF00147; Fibrinogen_C; 1.
SMART; SM00186; FBG; 1.
SUPFAM; SSF56496; SSF56496; 1.
PROSITE; PS00514; FIBRINOGEN_C_1; 1.
PROSITE; PS51406; FIBRINOGEN_C_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Collagen;
Complement activation lectin pathway; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Hydroxylation; Immunity; Innate immunity; Lectin; Metal-binding;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 23 {ECO:0000269|PubMed:15340161}.
CHAIN 24 299 Ficolin-3.
/FTId=PRO_0000009142.
DOMAIN 48 80 Collagen-like.
DOMAIN 84 299 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
REGION 258 259 Carbohydrate binding.
{ECO:0000305|PubMed:17215869}.
METAL 237 237 Calcium. {ECO:0000244|PDB:2J5Z,
ECO:0000244|PDB:2J60,
ECO:0000269|PubMed:17215869}.
METAL 239 239 Calcium. {ECO:0000244|PDB:2J5Z,
ECO:0000244|PDB:2J60,
ECO:0000269|PubMed:17215869}.
METAL 241 241 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:2J5Z,
ECO:0000244|PDB:2J60,
ECO:0000269|PubMed:17215869}.
METAL 243 243 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:2J5Z,
ECO:0000244|PDB:2J60,
ECO:0000269|PubMed:17215869}.
MOD_RES 50 50 Hydroxyproline.
{ECO:0000269|PubMed:9694814}.
MOD_RES 53 53 Hydroxyproline.
{ECO:0000269|PubMed:9694814}.
MOD_RES 59 59 Hydroxyproline.
{ECO:0000269|PubMed:9694814}.
MOD_RES 65 65 Hydroxyproline.
{ECO:0000269|PubMed:9694814}.
MOD_RES 68 68 Hydroxyproline.
{ECO:0000269|PubMed:9694814}.
MOD_RES 77 77 Hydroxyproline.
{ECO:0000269|PubMed:9694814}.
CARBOHYD 189 189 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
DISULFID 86 110 {ECO:0000244|PDB:2J5Z,
ECO:0000244|PDB:2J60,
ECO:0000269|PubMed:17215869}.
DISULFID 93 121 {ECO:0000244|PDB:2J5Z,
ECO:0000244|PDB:2J60,
ECO:0000269|PubMed:17215869}.
DISULFID 245 258 {ECO:0000244|PDB:2J5Z,
ECO:0000244|PDB:2J60,
ECO:0000269|PubMed:17215869}.
VAR_SEQ 79 89 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_001541.
CONFLICT 271 271 E -> D (in Ref. 1; BAA32277 and 6;
AAH20731). {ECO:0000305}.
HELIX 93 98 {ECO:0000244|PDB:2J5Z}.
STRAND 103 110 {ECO:0000244|PDB:2J5Z}.
STRAND 116 122 {ECO:0000244|PDB:2J5Z}.
HELIX 125 127 {ECO:0000244|PDB:2J5Z}.
STRAND 130 139 {ECO:0000244|PDB:2J5Z}.
HELIX 147 152 {ECO:0000244|PDB:2J5Z}.
STRAND 154 156 {ECO:0000244|PDB:2J5Z}.
HELIX 165 172 {ECO:0000244|PDB:2J5Z}.
STRAND 173 175 {ECO:0000244|PDB:2J5Z}.
STRAND 178 184 {ECO:0000244|PDB:2J5Z}.
STRAND 190 196 {ECO:0000244|PDB:2J5Z}.
STRAND 198 200 {ECO:0000244|PDB:2J5Z}.
HELIX 203 205 {ECO:0000244|PDB:2J5Z}.
STRAND 209 211 {ECO:0000244|PDB:2J5Z}.
STRAND 214 216 {ECO:0000244|PDB:2J60}.
HELIX 224 226 {ECO:0000244|PDB:2J5Z}.
STRAND 239 243 {ECO:0000244|PDB:2J5Z}.
HELIX 245 249 {ECO:0000244|PDB:2J5Z}.
STRAND 256 258 {ECO:0000244|PDB:2J5Z}.
STRAND 269 271 {ECO:0000244|PDB:2J5Z}.
TURN 282 285 {ECO:0000244|PDB:2J5Z}.
STRAND 292 299 {ECO:0000244|PDB:2J5Z}.
SEQUENCE 299 AA; 32903 MW; 5CB8A7D3668FA364 CRC64;
MDLLWILPSL WLLLLGGPAC LKTQEHPSCP GPRELEASKV VLLPSCPGAP GSPGEKGAPG
PQGPPGPPGK MGPKGEPGDP VNLLRCQEGP RNCRELLSQG ATLSGWYHLC LPEGRALPVF
CDMDTEGGGW LVFQRRQDGS VDFFRSWSSY RAGFGNQESE FWLGNENLHQ LTLQGNWELR
VELEDFNGNR TFAHYATFRL LGEVDHYQLA LGKFSEGTAG DSLSLHSGRP FTTYDADHDS
SNSNCAVIVH GAWWYASCYR SNLNGRYAVS EAAAHKYGID WASGRGVGHP YRRVRMMLR


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U1903h CLIA Collagen_fibrinogen domain-containing lectin 3 p35,Collagen_fibrinogen domain-containing protein 3,FCN3,FCNH,Ficolin-3,HAKA1,Hakata antigen,Homo sapiens,Human 96T
FCRL1 FCN3 Gene ficolin (collagen_fibrinogen domain containing) 3 (Hakata antigen)
U1907h CLIA 37 kDa elastin-binding protein,Collagen_fibrinogen domain-containing protein 2,EBP-37,FCN2,FCNL,Ficolin-2,Ficolin-B,Ficolin-beta,Homo sapiens,Hucolin,Human,L-ficolin,Serum lectin p35 96T
E1907h ELISA 37 kDa elastin-binding protein,Collagen_fibrinogen domain-containing protein 2,EBP-37,FCN2,FCNL,Ficolin-2,Ficolin-B,Ficolin-beta,Homo sapiens,Hucolin,Human,L-ficolin,Serum lectin p35 96T
U1907h CLIA kit 37 kDa elastin-binding protein,Collagen_fibrinogen domain-containing protein 2,EBP-37,FCN2,FCNL,Ficolin-2,Ficolin-B,Ficolin-beta,Homo sapiens,Hucolin,Human,L-ficolin,Serum lectin p35 96T
E1907h ELISA kit 37 kDa elastin-binding protein,Collagen_fibrinogen domain-containing protein 2,EBP-37,FCN2,FCNL,Ficolin-2,Ficolin-B,Ficolin-beta,Homo sapiens,Hucolin,Human,L-ficolin,Serum lectin p35 96T
CSB-PA008552GA01HU Rabbit anti-human ficolin (collagen_fibrinogen domain containing) 3 (Hakata antigen) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA008552GA01HU Rabbit anti-human ficolin (collagen_fibrinogen domain containing) 3 (Hakata antigen) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
U1907r CLIA kit Collagen_fibrinogen domain-containing protein 2,Fcn2,Fcnb,Ficolin-2,Ficolin-B,Ficolin-beta,L-ficolin,Rat,Rattus norvegicus 96T
U1907m CLIA kit Collagen_fibrinogen domain-containing protein 2,Fcn2,Fcnb,Ficolin-2,Ficolin-B,Ficolin-beta,L-ficolin,Mouse,Mus musculus 96T
EIAAB14673 Collagen_fibrinogen domain-containing protein 1,FCN1,FCNM,Ficolin-1,Ficolin-A,Ficolin-alpha,Homo sapiens,Human,M-ficolin
U1907r CLIA Collagen_fibrinogen domain-containing protein 2,Fcn2,Fcnb,Ficolin-2,Ficolin-B,Ficolin-beta,L-ficolin,Rat,Rattus norvegicus 96T
E1907r ELISA Collagen_fibrinogen domain-containing protein 2,Fcn2,Fcnb,Ficolin-2,Ficolin-B,Ficolin-beta,L-ficolin,Rat,Rattus norvegicus 96T
E1907m ELISA kit Collagen_fibrinogen domain-containing protein 2,Fcn2,Fcnb,Ficolin-2,Ficolin-B,Ficolin-beta,L-ficolin,Mouse,Mus musculus 96T
E1907m ELISA Collagen_fibrinogen domain-containing protein 2,Fcn2,Fcnb,Ficolin-2,Ficolin-B,Ficolin-beta,L-ficolin,Mouse,Mus musculus 96T
U1907m CLIA Collagen_fibrinogen domain-containing protein 2,Fcn2,Fcnb,Ficolin-2,Ficolin-B,Ficolin-beta,L-ficolin,Mouse,Mus musculus 96T
E1907r ELISA kit Collagen_fibrinogen domain-containing protein 2,Fcn2,Fcnb,Ficolin-2,Ficolin-B,Ficolin-beta,L-ficolin,Rat,Rattus norvegicus 96T
EIAAB14675 Collagen_fibrinogen domain-containing protein 1,Fcn1,Fcna,Ficolin-1,Ficolin-A,Ficolin-alpha,M-ficolin,Mouse,Mus musculus
EIAAB14676 Collagen_fibrinogen domain-containing protein 1,Fcn1,Fcna,Ficolin-1,Ficolin-A,Ficolin-alpha,M-ficolin,Rat,Rattus norvegicus
U1907b CLIA Bos taurus,Bovine,Collagen_fibrinogen domain-containing protein 2,FCN2,Ficolin-2,Ficolin-B,Ficolin-beta,L-ficolin 96T
E1907b ELISA kit Bos taurus,Bovine,Collagen_fibrinogen domain-containing protein 2,FCN2,Ficolin-2,Ficolin-B,Ficolin-beta,L-ficolin 96T
E1907b ELISA Bos taurus,Bovine,Collagen_fibrinogen domain-containing protein 2,FCN2,Ficolin-2,Ficolin-B,Ficolin-beta,L-ficolin 96T


 

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