FCN3_HUMAN
ID FCN3_HUMAN Reviewed; 299 AA.
AC O75636; Q6IBJ5; Q8WW86;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Ficolin-3;
DE AltName: Full=Collagen/fibrinogen domain-containing lectin 3 p35;
DE AltName: Full=Collagen/fibrinogen domain-containing protein 3;
DE AltName: Full=Hakata antigen;
DE Flags: Precursor;
GN Name=FCN3; Synonyms=FCNH, HAKA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP HYDROXYLATION AT PRO-50; PRO-53; PRO-59; PRO-65; PRO-68 AND PRO-77.
RC TISSUE=Lung;
RX PubMed=9694814; DOI=10.1074/jbc.273.33.20721;
RA Sugimoto R., Yae Y., Akaiwa M., Kitajima S., Shibata Y., Sato H.,
RA Hirata J., Okochi K., Izuhara K., Hamasaki N.;
RT "Cloning and characterization of the Hakata antigen, a member of the
RT ficolin/opsonin p35 lectin family.";
RL J. Biol. Chem. 273:20721-20727(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 24-38.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=10330454; DOI=10.1177/002215549904700607;
RA Akaiwa M., Yae Y., Sugimoto R., Suzuki S.O., Iwaki T., Izuhara K.,
RA Hamasaki N.;
RT "Hakata antigen, a new member of the ficolin/opsonin p35 family, is a novel
RT human lectin secreted into bronchus/alveolus and bile.";
RL J. Histochem. Cytochem. 47:777-786(1999).
RN [9]
RP FUNCTION, AND INTERACTION WITH MASP1 AND MASP2.
RX PubMed=11907111; DOI=10.4049/jimmunol.168.7.3502;
RA Matsushita M., Kuraya M., Hamasaki N., Tsujimura M., Shiraki H., Fujita T.;
RT "Activation of the lectin complement pathway by H-ficolin (Hakata
RT antigen).";
RL J. Immunol. 168:3502-3506(2002).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-189.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-189.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
RP GLYCOSYLATION AT ASN-189.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [13]
RP INVOLVEMENT IN FCN3D.
RX PubMed=19535802; DOI=10.1056/nejmoa0900381;
RA Munthe-Fog L., Hummelshoj T., Honore C., Madsen H.O., Permin H., Garred P.;
RT "Immunodeficiency associated with FCN3 mutation and ficolin-3 deficiency.";
RL N. Engl. J. Med. 360:2637-2644(2009).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 79-299 IN COMPLEX WITH CALCIUM
RP AND GALACTOSE, DISULFIDE BONDS, SUBUNIT, AND FUNCTION.
RX PubMed=17215869; DOI=10.1038/sj.emboj.7601500;
RA Garlatti V., Belloy N., Martin L., Lacroix M., Matsushita M., Endo Y.,
RA Fujita T., Fontecilla-Camps J.C., Arlaud G.J., Thielens N.M., Gaboriaud C.;
RT "Structural insights into the innate immune recognition specificities of
RT L- and H-ficolins.";
RL EMBO J. 26:623-633(2007).
CC -!- FUNCTION: May function in innate immunity through activation of the
CC lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin.
CC Has affinity with GalNAc, GlcNAc, D-fucose, as mono/oligosaccharide and
CC lipopolysaccharides from S.typhimurium and S.minnesota.
CC {ECO:0000269|PubMed:11907111, ECO:0000269|PubMed:17215869}.
CC -!- SUBUNIT: Homotrimer (PubMed:17215869). May form an octadecamer
CC consisting of an elementary trimer unit. Does not interact with
CC fibronectin, elastin or zymosan. Interacts with MASP1 and MASP2.
CC {ECO:0000269|PubMed:11907111, ECO:0000269|PubMed:17215869}.
CC -!- INTERACTION:
CC O75636; P17927: CR1; NbExp=2; IntAct=EBI-11786958, EBI-2807625;
CC O75636; Q15485: FCN2; NbExp=12; IntAct=EBI-11786958, EBI-7468784;
CC O75636; P02751: FN1; NbExp=3; IntAct=EBI-11786958, EBI-1220319;
CC O75636; P48740-2: MASP1; NbExp=5; IntAct=EBI-11786958, EBI-26435098;
CC O75636; P48740-3: MASP1; NbExp=3; IntAct=EBI-11786958, EBI-26435118;
CC O75636; PRO_0000000214 [P9WQP3]: fbpA; Xeno; NbExp=2; IntAct=EBI-11786958, EBI-26878164;
CC O75636; P9WQP1: fbpB; Xeno; NbExp=4; IntAct=EBI-11786958, EBI-26878221;
CC PRO_0000009142; PRO_0000009142 [O75636]: FCN3; NbExp=2; IntAct=EBI-27105453, EBI-27105453;
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Found in blood plasma, bronchus,
CC alveolus and bile duct.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75636-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75636-2; Sequence=VSP_001541;
CC -!- TISSUE SPECIFICITY: Liver and lung. In liver it is produced by bile
CC duct epithelial cells and hepatocytes. In lung it is produced by both
CC ciliated bronchial epithelial cells and type II alveolar epithelial
CC cells. {ECO:0000269|PubMed:10330454}.
CC -!- PTM: The N-terminus is blocked.
CC -!- DISEASE: Ficolin 3 deficiency (FCN3D) [MIM:613860]: A disorder
CC characterized by immunodeficiency, recurrent infections, brain
CC abscesses and recurrent warts on the fingers. Affected individuals have
CC normal levels of lymphocytes, normal T-cell responses, and normal
CC antibodies, but a selective deficient antibody response to pneumococcal
CC polysaccharide vaccine. {ECO:0000269|PubMed:19535802}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ficolin lectin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/fcn3/";
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DR EMBL; D88587; BAA32277.1; -; mRNA.
DR EMBL; AK075140; BAC11429.1; -; mRNA.
DR EMBL; CR456808; CAG33089.1; -; mRNA.
DR EMBL; AY756173; AAU85296.1; -; Genomic_DNA.
DR EMBL; FO393419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020731; AAH20731.1; -; mRNA.
DR CCDS; CCDS300.1; -. [O75636-1]
DR CCDS; CCDS301.1; -. [O75636-2]
DR RefSeq; NP_003656.2; NM_003665.3. [O75636-1]
DR RefSeq; NP_775628.1; NM_173452.2. [O75636-2]
DR PDB; 2J5Z; X-ray; 1.73 A; A/B/C=79-299.
DR PDB; 2J60; X-ray; 1.80 A; A/B/C=79-299.
DR PDB; 2J64; X-ray; 2.20 A; A/B/C=79-299.
DR PDBsum; 2J5Z; -.
DR PDBsum; 2J60; -.
DR PDBsum; 2J64; -.
DR AlphaFoldDB; O75636; -.
DR SMR; O75636; -.
DR BioGRID; 114117; 56.
DR ComplexPortal; CPX-6179; FCN3-MASP1 lectin-protease complex.
DR ComplexPortal; CPX-6239; FCN3-MASP2 lectin-protease complex.
DR IntAct; O75636; 13.
DR STRING; 9606.ENSP00000270879; -.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR UniLectin; O75636; -.
DR GlyConnect; 1247; 2 N-Linked glycans (1 site).
DR GlyGen; O75636; 1 site, 4 N-linked glycans (1 site).
DR iPTMnet; O75636; -.
DR PhosphoSitePlus; O75636; -.
DR BioMuta; FCN3; -.
DR CPTAC; non-CPTAC-1124; -.
DR jPOST; O75636; -.
DR MassIVE; O75636; -.
DR PaxDb; O75636; -.
DR PeptideAtlas; O75636; -.
DR PRIDE; O75636; -.
DR ProteomicsDB; 50132; -. [O75636-1]
DR ProteomicsDB; 50133; -. [O75636-2]
DR Antibodypedia; 30776; 255 antibodies from 27 providers.
DR DNASU; 8547; -.
DR Ensembl; ENST00000270879.9; ENSP00000270879.4; ENSG00000142748.13. [O75636-1]
DR Ensembl; ENST00000354982.2; ENSP00000347077.2; ENSG00000142748.13. [O75636-2]
DR GeneID; 8547; -.
DR KEGG; hsa:8547; -.
DR MANE-Select; ENST00000270879.9; ENSP00000270879.4; NM_003665.4; NP_003656.2.
DR UCSC; uc001boa.4; human. [O75636-1]
DR CTD; 8547; -.
DR DisGeNET; 8547; -.
DR GeneCards; FCN3; -.
DR HGNC; HGNC:3625; FCN3.
DR HPA; ENSG00000142748; Group enriched (liver, lung).
DR MalaCards; FCN3; -.
DR MIM; 604973; gene.
DR MIM; 613860; phenotype.
DR neXtProt; NX_O75636; -.
DR OpenTargets; ENSG00000142748; -.
DR Orphanet; 331190; Immunodeficiency due to ficolin3 deficiency.
DR PharmGKB; PA28071; -.
DR VEuPathDB; HostDB:ENSG00000142748; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000163188; -.
DR HOGENOM; CLU_038628_6_0_1; -.
DR InParanoid; O75636; -.
DR OMA; GNCAVIV; -.
DR PhylomeDB; O75636; -.
DR TreeFam; TF351983; -.
DR PathwayCommons; O75636; -.
DR Reactome; R-HSA-166662; Lectin pathway of complement activation.
DR Reactome; R-HSA-166663; Initial triggering of complement.
DR Reactome; R-HSA-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface.
DR SignaLink; O75636; -.
DR SIGNOR; O75636; -.
DR BioGRID-ORCS; 8547; 6 hits in 1060 CRISPR screens.
DR ChiTaRS; FCN3; human.
DR EvolutionaryTrace; O75636; -.
DR GeneWiki; FCN3; -.
DR GenomeRNAi; 8547; -.
DR Pharos; O75636; Tbio.
DR PRO; PR:O75636; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75636; protein.
DR Bgee; ENSG00000142748; Expressed in right lung and 103 other tissues.
DR ExpressionAtlas; O75636; baseline and differential.
DR Genevisible; O75636; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IDA:ComplexPortal.
DR GO; GO:0003823; F:antigen binding; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0006956; P:complement activation; IDA:UniProtKB.
DR GO; GO:0001867; P:complement activation, lectin pathway; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:1902679; P:negative regulation of RNA biosynthetic process; IDA:UniProtKB.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IMP:UniProtKB.
DR GO; GO:1903028; P:positive regulation of opsonization; IDA:ComplexPortal.
DR GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
DR GO; GO:0043654; P:recognition of apoptotic cell; IDA:UniProtKB.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR020837; Fibrinogen_CS.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Collagen;
KW Complement activation lectin pathway; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydroxylation; Immunity; Innate immunity;
KW Lectin; Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 24..299
FT /note="Ficolin-3"
FT /id="PRO_0000009142"
FT DOMAIN 48..80
FT /note="Collagen-like"
FT DOMAIN 84..299
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 44..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..74
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17215869,
FT ECO:0007744|PDB:2J5Z, ECO:0007744|PDB:2J60"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17215869,
FT ECO:0007744|PDB:2J5Z, ECO:0007744|PDB:2J60"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17215869,
FT ECO:0007744|PDB:2J5Z, ECO:0007744|PDB:2J60"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17215869,
FT ECO:0007744|PDB:2J5Z, ECO:0007744|PDB:2J60"
FT BINDING 258..259
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000305|PubMed:17215869"
FT MOD_RES 50
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:9694814"
FT MOD_RES 53
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:9694814"
FT MOD_RES 59
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:9694814"
FT MOD_RES 65
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:9694814"
FT MOD_RES 68
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:9694814"
FT MOD_RES 77
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:9694814"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218"
FT DISULFID 86..110
FT /evidence="ECO:0000269|PubMed:17215869,
FT ECO:0007744|PDB:2J5Z, ECO:0007744|PDB:2J60"
FT DISULFID 93..121
FT /evidence="ECO:0000269|PubMed:17215869,
FT ECO:0007744|PDB:2J5Z, ECO:0007744|PDB:2J60"
FT DISULFID 245..258
FT /evidence="ECO:0000269|PubMed:17215869,
FT ECO:0007744|PDB:2J5Z, ECO:0007744|PDB:2J60"
FT VAR_SEQ 79..89
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_001541"
FT CONFLICT 271
FT /note="E -> D (in Ref. 1; BAA32277 and 6; AAH20731)"
FT /evidence="ECO:0000305"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:2J5Z"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:2J5Z"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:2J5Z"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:2J5Z"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:2J5Z"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:2J5Z"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2J5Z"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:2J5Z"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:2J5Z"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:2J5Z"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:2J5Z"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:2J5Z"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:2J5Z"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:2J5Z"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2J60"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:2J5Z"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:2J5Z"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:2J5Z"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:2J5Z"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2J5Z"
FT TURN 282..285
FT /evidence="ECO:0007829|PDB:2J5Z"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:2J5Z"
SQ 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
