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UniProtKB/Swiss-Prot entry O75636


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FCN3_HUMAN
Primary accession number O75636
Secondary accession numbers Q6IBJ5 Q8WW86
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on March 7, 2006 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 93)
Name and origin of the protein
Protein name Ficolin-3 [Precursor]
Synonyms Collagen/fibrinogen domain-containing protein 3
Collagen/fibrinogen domain-containing lectin 3 p35
Hakata antigen
Gene name
Name: FCN3
Synonyms: FCNH, HAKA1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Lung;
DOI=10.1074/jbc.273.33.20721; PubMed=9694814 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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 program for genomic applications;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04728; PubMed=16641997 [NCBI, ExPASy, EBI, Israel, Japan]
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-189, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
3D-STRUCTURE MODELING.
Mallena S.C., Yadugiri K.;
"In silico designed structure of ficolin precursor.";
Submitted (NOV-2002) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D88587; BAA32277.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK075140; BAC11429.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456808; CAG33089.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY756173; AAU85296.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL663123; CAI14774.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020731; AAH20731.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_003656.2; -.
NP_775628.1; -.
UniGene Hs.333383
3D structure databases
PDB
1LA5; Model; -; A=1-299.[ExPASy / RCSB / EBI]
2J5Z; X-ray; 1.73 A; A/B/C=79-299.[ExPASy / RCSB / EBI]
2J60; X-ray; 1.80 A; A/B/C=79-299.[ExPASy / RCSB / EBI]
2J64; X-ray; 2.20 A; A/B/C=79-299.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1LA5; -.
2J5Z; -.
2J60; -.
2J64; -.
ModBase O75636.
Organism-specific databases
H-InvDB HIX0000313; -.
HGNC HGNC:3625; FCN3.
GenAtlas FCN3.
MIM 604973; gene. [NCBI / EBI]
PharmGKB PA28071; -.
GeneCards O75636.
Gene expression databases
ArrayExpress O75636; -.
CleanEx HS_FCN3; -.
GermOnline ENSG00000142748; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (traceable author statement from ProtInc).
GO:0005102; Molecular function: receptor binding (inferred from electronic annotation from InterPro).
GO:0005529; Molecular function: sugar binding (traceable author statement from ProtInc).
GO:0007165; Biological process: signal transduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR002181; Fibrinogen_a/b/g_C.
IPR014716; Fibrinogen_a/b/g_C_1.
Graphical view of domain structure.
Gene3D G3DSA:3.90.215.10; Fibrinogen_a/b/g_C_1; 1.
Pfam PF00147; Fibrinogen_C; 1.
Pfam graphical view of domain structure.
SMART SM00186; FBG; 1.
SMART graphical view of domain structure.
PROSITE PS00514; FIBRINOGEN_C_1; 1.
PS51406; FIBRINOGEN_C_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS O75636.
ProtoNet O75636.
Proteomic databases
PeptideAtlas O75636; -.
Genome annotation databases
Ensembl ENSG00000142748; Homo sapiens. [Contig view]
GeneID 8547; -.
KEGG hsa:8547; -.
Phylogenomic databases
HOGENOM O75636; -.
HOVERGEN O75636; -.
Other
NextBio 32022; -.
SOURCE FCN3; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Collagen; Direct protein sequencing; Glycoprotein; Hydroxylation; Lectin; Repeat; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    23  23      
CHAIN   24   299  276     Ficolin-3. PRO_0000009142
DOMAIN   48    80  33     Collagen-like. 
DOMAIN   84   299  216     Fibrinogen C-terminal. 
MOD_RES   50    50        Hydroxyproline. 
MOD_RES   53    53        Hydroxyproline. 
MOD_RES   59    59        Hydroxyproline. 
MOD_RES   65    65        Hydroxyproline. 
MOD_RES   68    68        Hydroxyproline. 
MOD_RES   77    77        Hydroxyproline. 
CARBOHYD   189   189        N-linked (GlcNAc...). 
VAR_SEQ   79    89        Missing (in isoform 2). VSP_001541
CONFLICT   271   271        E -> D (in Ref. 1; BAA32277 and 6; AAH20731). 
HELIX   93    98  6      
STRAND   103   110  8      
STRAND   116   122  7      
HELIX   125   127  3      
STRAND   130   139  10      
HELIX   147   152  6      
STRAND   154   156  3      
HELIX   165   172  8      
STRAND   173   175  3      
STRAND   178   184  7      
STRAND   190   196  7      
STRAND   198   200  3      
HELIX   203   205  3      
STRAND   209   211  3      
HELIX   224   226  3      
STRAND   239   243  5      
HELIX   245   249  5      
STRAND   256   258  3      
STRAND   269   271  3      
TURN   282   285  4      
Sequence information
Length: 299 AA [This is the length of the unprocessed precursor] Molecular weight: 32903 Da [This is the MW of the unprocessed precursor] CRC64: 5CB8A7D3668FA364 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDLLWILPSL WLLLLGGPAC LKTQEHPSCP GPRELEASKV VLLPSCPGAP GSPGEKGAPG 

        70         80         90        100        110        120 
PQGPPGPPGK MGPKGEPGDP VNLLRCQEGP RNCRELLSQG ATLSGWYHLC LPEGRALPVF 

       130        140        150        160        170        180 
CDMDTEGGGW LVFQRRQDGS VDFFRSWSSY RAGFGNQESE FWLGNENLHQ LTLQGNWELR 

       190        200        210        220        230        240 
VELEDFNGNR TFAHYATFRL LGEVDHYQLA LGKFSEGTAG DSLSLHSGRP FTTYDADHDS 

       250        260        270        280        290 
SNSNCAVIVH GAWWYASCYR SNLNGRYAVS EAAAHKYGID WASGRGVGHP YRRVRMMLR 

O75636 in FASTA format

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