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Ficolin-1 (Collagen/fibrinogen domain-containing protein 1) (Ficolin-A) (Ficolin-alpha) (M-ficolin)

 FCN1_HUMAN              Reviewed;         326 AA.
O00602; Q5VYV5; Q92596;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
02-MAY-2002, sequence version 2.
12-SEP-2018, entry version 166.
RecName: Full=Ficolin-1;
AltName: Full=Collagen/fibrinogen domain-containing protein 1;
AltName: Full=Ficolin-A;
AltName: Full=Ficolin-alpha;
AltName: Full=M-ficolin;
Flags: Precursor;
Name=FCN1; Synonyms=FCNM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Uterus;
PubMed=8573080; DOI=10.1042/bj3130473;
Lu J., Tay P.N., Kon O.L., Reid K.B.;
"Human ficolin: cDNA cloning, demonstration of peripheral blood
leucocytes as the major site of synthesis and assignment of the gene
to chromosome 9.";
Biochem. J. 313:473-478(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
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.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-326.
TISSUE=Uterus;
PubMed=8947836; DOI=10.1093/oxfordjournals.jbchem.a021474;
Harumiya S., Takeda K., Sugiura T., Fukumoto Y., Tachikawa H.,
Miyazono K., Fujimoto D., Ichijo H.;
"Characterization of ficolins as novel elastin-binding proteins and
molecular cloning of human ficolin-1.";
J. Biochem. 120:745-751(1996).
[7]
PROTEIN SEQUENCE OF 30-44.
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]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CRP AND FFAR2.
PubMed=21037097; DOI=10.4049/jimmunol.1001225;
Zhang J., Yang L., Ang Z., Yoong S.L., Tran T.T., Anand G.S.,
Tan N.S., Ho B., Ding J.L.;
"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.";
J. Immunol. 185:6899-6910(2010).
[9]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=20400674; DOI=10.1189/jlb.1209802;
Honore C., Rorvig S., Hummelshoj T., Skjoedt M.O., Borregaard N.,
Garred P.;
"Tethering of Ficolin-1 to cell surfaces through recognition of sialic
acid by the fibrinogen-like domain.";
J. Leukoc. Biol. 88:145-158(2010).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 115-326 IN COMPLEX WITH
CALCIUM, SUBUNIT, DISULFIDE BONDS, CALCIUM-BINDING SITES,
PH-DEPENDENCY, AND DOMAIN.
PubMed=17148457; DOI=10.1074/jbc.M608627200;
Tanio M., Kondo S., Sugio S., Kohno T.;
"Trivalent recognition unit of innate immunity system: crystal
structure of trimeric human M-ficolin fibrinogen-like domain.";
J. Biol. Chem. 282:3889-3895(2007).
[11]
X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 109-326 IN COMPLEX WITH
CALCIUM AND CARBOHYDRATE, SUBUNIT, DISULFIDE BONDS, CALCIUM-BINDING
SITES, PH-DEPENDENCY, AND DOMAIN.
PubMed=17897951; DOI=10.1074/jbc.M705741200;
Garlatti V., Martin L., Gout E., Reiser J.B., Fujita T., Arlaud G.J.,
Thielens N.M., Gaboriaud C.;
"Structural basis for innate immune sensing by M-ficolin and its
control by a pH-dependent conformational switch.";
J. Biol. Chem. 282:35814-35820(2007).
[12]
X-RAY CRYSTALLOGRAPHY (1.21 ANGSTROMS) OF 110-326 IN COMPLEX WITH
CALCIUM, DISULFIDE BONDS, FUNCTION, SUBUNIT, SUBSTRATE SPECIFICITY,
CALCIUM-BINDING SITES, AND MUTAGENESIS OF GLY-250; ALA-285 AND
TYR-300.
PubMed=20032467; DOI=10.1074/jbc.M109.065854;
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.;
"Carbohydrate recognition properties of human ficolins: glycan array
screening reveals the sialic acid binding specificity of M-ficolin.";
J. Biol. Chem. 285:6612-6622(2010).
[13]
VARIANT [LARGE SCALE ANALYSIS] CYS-175.
PubMed=16959974; DOI=10.1126/science.1133427;
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., 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.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:20032467, ECO:0000269|PubMed:21037097}.
-!- SUBUNIT: Homotrimer (PubMed:17897951). Interacts with elastin/ELN.
Interacts (via Fibrinogen C-terminal domain) with FFAR2. Interacts
with CRP; may regulate monocyte activation by FCN1.
{ECO:0000269|PubMed:17148457, ECO:0000269|PubMed:17897951,
ECO:0000269|PubMed:20032467, ECO:0000269|PubMed:21037097}.
-!- INTERACTION:
Q2TS39:CRP-1 (xeno); NbExp=3; IntAct=EBI-5282479, EBI-7468648;
P26022:PTX3; NbExp=3; IntAct=EBI-5282479, EBI-11574553;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20400674,
ECO:0000269|PubMed:21037097}. Cell membrane
{ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097};
Peripheral membrane protein {ECO:0000269|PubMed:20400674,
ECO:0000269|PubMed:21037097}; Extracellular side
{ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}.
Note=Found on the monocyte and granulocyte surface
(PubMed:20400674).
-!- 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.
{ECO:0000269|PubMed:20400674}.
-!- 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. {ECO:0000269|PubMed:17148457,
ECO:0000269|PubMed:17897951}.
-!- SIMILARITY: Belongs to the ficolin lectin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA12120.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; S80990; AAB50706.1; -; mRNA.
EMBL; AK314867; BAG37382.1; -; mRNA.
EMBL; AL353611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW88137.1; -; Genomic_DNA.
EMBL; BC020635; AAH20635.1; -; mRNA.
EMBL; D83920; BAA12120.1; ALT_INIT; mRNA.
CCDS; CCDS6985.1; -.
PIR; S61517; S61517.
RefSeq; NP_001994.2; NM_002003.4.
UniGene; Hs.440898; -.
UniGene; Hs.638586; -.
PDB; 2D39; X-ray; 1.90 A; A/B/C=115-326.
PDB; 2JHH; X-ray; 1.70 A; C/F=109-326.
PDB; 2JHI; X-ray; 1.80 A; F=109-326.
PDB; 2JHK; X-ray; 1.75 A; F=109-326.
PDB; 2JHL; X-ray; 1.75 A; F=109-326.
PDB; 2JHM; X-ray; 1.52 A; F=109-326.
PDB; 2WNP; X-ray; 1.21 A; F=110-326.
PDBsum; 2D39; -.
PDBsum; 2JHH; -.
PDBsum; 2JHI; -.
PDBsum; 2JHK; -.
PDBsum; 2JHL; -.
PDBsum; 2JHM; -.
PDBsum; 2WNP; -.
ProteinModelPortal; O00602; -.
SMR; O00602; -.
BioGrid; 108513; 16.
IntAct; O00602; 3.
MINT; O00602; -.
STRING; 9606.ENSP00000360871; -.
UniLectin; O00602; -.
PhosphoSitePlus; O00602; -.
BioMuta; FCN1; -.
EPD; O00602; -.
PaxDb; O00602; -.
PeptideAtlas; O00602; -.
PRIDE; O00602; -.
ProteomicsDB; 47994; -.
DNASU; 2219; -.
Ensembl; ENST00000371806; ENSP00000360871; ENSG00000085265.
GeneID; 2219; -.
KEGG; hsa:2219; -.
UCSC; uc004cfi.4; human.
CTD; 2219; -.
DisGeNET; 2219; -.
EuPathDB; HostDB:ENSG00000085265.10; -.
GeneCards; FCN1; -.
HGNC; HGNC:3623; FCN1.
HPA; CAB016760; -.
HPA; HPA000685; -.
HPA; HPA001295; -.
MIM; 601252; gene.
neXtProt; NX_O00602; -.
OpenTargets; ENSG00000085265; -.
PharmGKB; PA28069; -.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
GeneTree; ENSGT00920000148944; -.
HOGENOM; HOG000037127; -.
HOVERGEN; HBG001644; -.
InParanoid; O00602; -.
KO; K10104; -.
OMA; WYADCHA; -.
PhylomeDB; O00602; -.
TreeFam; TF329953; -.
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.
Reactome; R-HSA-6798695; Neutrophil degranulation.
EvolutionaryTrace; O00602; -.
GeneWiki; FCN1; -.
GenomeRNAi; 2219; -.
PRO; PR:O00602; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000085265; Expressed in 122 organ(s), highest expression level in bone marrow.
CleanEx; HS_FCN1; -.
ExpressionAtlas; O00602; baseline and differential.
Genevisible; O00602; HS.
GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0001664; F:G-protein coupled receptor binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0033691; F:sialic acid binding; IDA:UniProtKB.
GO; GO:0008329; F:signaling pattern recognition receptor activity; IMP:UniProtKB.
GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; IMP:UniProtKB.
GO; GO:0006956; P:complement activation; TAS:Reactome.
GO; GO:0001867; P:complement activation, lectin pathway; TAS:Reactome.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:2000484; P:positive regulation of interleukin-8 secretion; IMP:UniProtKB.
GO; GO:0034394; P:protein localization to cell surface; IDA: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; IPR008160; Collagen.
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; PF01391; Collagen; 1.
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; Calcium; Cell membrane; Collagen; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
Innate immunity; Lectin; Membrane; Metal-binding; Polymorphism;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 29 {ECO:0000269|PubMed:15340161}.
CHAIN 30 326 Ficolin-1.
/FTId=PRO_0000009136.
DOMAIN 55 93 Collagen-like.
DOMAIN 109 326 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
REGION 115 154 A domain; contributes to trimerization.
REGION 155 243 B domain; contributes to trimerization.
REGION 282 284 Carbohydrate-binding.
{ECO:0000269|PubMed:17897951}.
REGION 317 326 P domain. {ECO:0000303|PubMed:17148457}.
METAL 262 262 Calcium. {ECO:0000244|PDB:2D39,
ECO:0000244|PDB:2WNP,
ECO:0000269|PubMed:17148457,
ECO:0000269|PubMed:17897951,
ECO:0000269|PubMed:20032467}.
METAL 264 264 Calcium. {ECO:0000244|PDB:2D39,
ECO:0000244|PDB:2WNP,
ECO:0000269|PubMed:17148457,
ECO:0000269|PubMed:17897951,
ECO:0000269|PubMed:20032467}.
METAL 266 266 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:2D39,
ECO:0000244|PDB:2WNP,
ECO:0000269|PubMed:17148457,
ECO:0000269|PubMed:17897951,
ECO:0000269|PubMed:20032467}.
METAL 268 268 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:2D39,
ECO:0000244|PDB:2WNP,
ECO:0000269|PubMed:17148457,
ECO:0000269|PubMed:17897951,
ECO:0000269|PubMed:20032467}.
SITE 300 300 Mediates specificity for sialic acids.
{ECO:0000305|PubMed:17897951,
ECO:0000305|PubMed:20032467}.
SITE 312 312 Mediates specificity for sialic acids.
{ECO:0000305|PubMed:17897951}.
CARBOHYD 305 305 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 111 139 {ECO:0000244|PDB:2WNP,
ECO:0000269|PubMed:17897951,
ECO:0000269|PubMed:20032467}.
DISULFID 118 146 {ECO:0000244|PDB:2WNP,
ECO:0000269|PubMed:17148457,
ECO:0000269|PubMed:17897951,
ECO:0000269|PubMed:20032467}.
DISULFID 270 283 {ECO:0000244|PDB:2WNP,
ECO:0000269|PubMed:17148457,
ECO:0000269|PubMed:17897951,
ECO:0000269|PubMed:20032467}.
VARIANT 93 93 R -> Q (in dbSNP:rs56345770).
/FTId=VAR_061172.
VARIANT 126 126 Y -> H (in dbSNP:rs771359747).
/FTId=VAR_024450.
VARIANT 175 175 Y -> C (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036341.
MUTAGEN 250 250 G->F: Inhibits binding to the 9-O-
acetylated sialic acid derivatives.
{ECO:0000269|PubMed:20032467}.
MUTAGEN 285 285 A->V: Inhibits binding to the 9-O-
acetylated sialic acid derivatives.
{ECO:0000269|PubMed:20032467}.
MUTAGEN 300 300 Y->F: Abolishes interaction with all
sialic acid-containing glycans.
{ECO:0000269|PubMed:20032467}.
CONFLICT 133 133 T -> N (in Ref. 1; AAB50706).
{ECO:0000305}.
CONFLICT 287 287 N -> S (in Ref. 1; AAB50706).
{ECO:0000305}.
TURN 111 113 {ECO:0000244|PDB:2WNP}.
HELIX 118 123 {ECO:0000244|PDB:2WNP}.
STRAND 130 135 {ECO:0000244|PDB:2WNP}.
STRAND 141 147 {ECO:0000244|PDB:2WNP}.
HELIX 150 152 {ECO:0000244|PDB:2WNP}.
STRAND 155 164 {ECO:0000244|PDB:2WNP}.
HELIX 172 177 {ECO:0000244|PDB:2WNP}.
STRAND 179 181 {ECO:0000244|PDB:2D39}.
HELIX 190 198 {ECO:0000244|PDB:2WNP}.
STRAND 202 209 {ECO:0000244|PDB:2WNP}.
STRAND 215 221 {ECO:0000244|PDB:2WNP}.
STRAND 223 225 {ECO:0000244|PDB:2WNP}.
HELIX 228 230 {ECO:0000244|PDB:2WNP}.
STRAND 234 236 {ECO:0000244|PDB:2WNP}.
STRAND 239 241 {ECO:0000244|PDB:2WNP}.
HELIX 249 251 {ECO:0000244|PDB:2WNP}.
STRAND 264 268 {ECO:0000244|PDB:2WNP}.
HELIX 270 273 {ECO:0000244|PDB:2WNP}.
STRAND 281 283 {ECO:0000244|PDB:2WNP}.
STRAND 285 287 {ECO:0000244|PDB:2WNP}.
STRAND 298 301 {ECO:0000244|PDB:2WNP}.
STRAND 303 306 {ECO:0000244|PDB:2WNP}.
TURN 307 309 {ECO:0000244|PDB:2WNP}.
STRAND 312 315 {ECO:0000244|PDB:2JHK}.
STRAND 317 325 {ECO:0000244|PDB:2WNP}.
SEQUENCE 326 AA; 35078 MW; 184D24B371B251AB CRC64;
MELSGATMAR GLAVLLVLFL HIKNLPAQAA DTCPEVKVVG LEGSDKLTIL RGCPGLPGAP
GPKGEAGVIG ERGERGLPGA PGKAGPVGPK GDRGEKGMRG EKGDAGQSQS CATGPRNCKD
LLDRGYFLSG WHTIYLPDCR PLTVLCDMDT DGGGWTVFQR RMDGSVDFYR DWAAYKQGFG
SQLGEFWLGN DNIHALTAQG SSELRVDLVD FEGNHQFAKY KSFKVADEAE KYKLVLGAFV
GGSAGNSLTG HNNNFFSTKD QDNDVSSSNC AEKFQGAWWY ADCHASNLNG LYLMGPHESY
ANGINWSAAK GYKYSYKVSE MKVRPA


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