ITLN1_HUMAN
ID ITLN1_HUMAN Reviewed; 313 AA.
AC Q8WWA0; Q5IWS4; Q5VYI4; Q6YDJ3; Q9NP67;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Intelectin-1;
DE Short=ITLN-1;
DE AltName: Full=Endothelial lectin HL-1;
DE AltName: Full=Galactofuranose-binding lectin;
DE AltName: Full=Intestinal lactoferrin receptor {ECO:0000303|PubMed:11747454};
DE AltName: Full=Omentin {ECO:0000303|PubMed:16531507};
DE Flags: Precursor;
GN Name=ITLN1; Synonyms=INTL, ITLN, LFR; ORFNames=UNQ640/PRO1270;
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], FUNCTION, INTERACTION WITH LTF, PUTATIVE
RP GPI-ANCHOR, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Small intestine;
RX PubMed=11747454; DOI=10.1021/bi0155899;
RA Suzuki Y.A., Shin K., Loennerdal B.;
RT "Molecular cloning and functional expression of a human intestinal
RT lactoferrin receptor.";
RL Biochemistry 40:15771-15779(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Small intestine;
RX PubMed=11181563; DOI=10.1093/glycob/11.1.65;
RA Lee J.K., Schnee J., Pang M., Wolfert M., Baum L.G., Moremen K.W.,
RA Pierce M.;
RT "Human homologs of the Xenopus oocyte cortical granule lectin XL35.";
RL Glycobiology 11:65-73(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-28, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT, GLYCOSYLATION, AND
RP VARIANT ASP-109.
RC TISSUE=Placenta;
RX PubMed=11313366; DOI=10.1074/jbc.m103162200;
RA Tsuji S., Uehori J., Matsumoto M., Suzuki Y., Matsuhisa A., Toyoshima K.,
RA Seya T.;
RT "Human intelectin is a novel soluble lectin that recognizes galactofuranose
RT in carbohydrate chains of bacterial cell wall.";
RL J. Biol. Chem. 276:23456-23463(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-313.
RX PubMed=14720597; DOI=10.1016/s1095-6433(03)00269-1;
RA Chang B.Y., Peavy T.R., Wardrip N.J., Hedrick J.L.;
RT "The Xenopus laevis cortical granule lectin: cDNA cloning, developmental
RT expression, and identification of the eglectin family of lectins.";
RL Comp. Biochem. Physiol. 137A:115-129(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Adipose tissue;
RX PubMed=16531507; DOI=10.1152/ajpendo.00572.2004;
RA Yang R.-Z., Lee M.-J., Hu H., Pray J., Wu H.-B., Hansen B.C.,
RA Shuldiner A.R., Fried S.K., McLenithan J.C., Gong D.-W.;
RT "Identification of omentin as a novel depot-specific adipokine in human
RT adipose tissue: possible role in modulating insulin action.";
RL Am. J. Physiol. 290:E1253-E1261(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-313.
RC TISSUE=Ovary;
RA Peavy T.R., Hedrick J.L.;
RT "Human homolog of the Xenopus laevis egg cortical granule lectin.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adipose tissue;
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 [9]
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 [10]
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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [13]
RP SUBUNIT, MASS SPECTROMETRY, GLYCOSYLATION, DISULFIDE BOND, AND MUTAGENESIS
RP OF CYS-31 AND CYS-48.
RX PubMed=17621593; DOI=10.1093/glycob/cwm075;
RA Tsuji S., Yamashita M., Nishiyama A., Shinohara T., Li Z., Myrvik Q.N.,
RA Hoffman D.R., Henriksen R.A., Shibata Y.;
RT "Differential structure and activity between human and mouse intelectin-1:
RT human intelectin-1 is a disulfide-linked trimer, whereas mouse homologue is
RT a monomer.";
RL Glycobiology 17:1045-1051(2007).
RN [14]
RP FUNCTION, AND INTERACTION WITH LTF.
RX PubMed=23921499; DOI=10.1093/jb/mvt073;
RA Akiyama Y., Oshima K., Kuhara T., Shin K., Abe F., Iwatsuki K., Nadano D.,
RA Matsuda T.;
RT "A lactoferrin-receptor, intelectin 1, affects uptake, sub-cellular
RT localization and release of immunochemically detectable lactoferrin by
RT intestinal epithelial Caco-2 cells.";
RL J. Biochem. 154:437-448(2013).
RN [15] {ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 29-313 IN COMPLEX WITH CALCIUM
RP IONS AND CARBOHYDRATE, FUNCTION, DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=26148048; DOI=10.1038/nsmb.3053;
RA Wesener D.A., Wangkanont K., McBride R., Song X., Kraft M.B., Hodges H.L.,
RA Zarling L.C., Splain R.A., Smith D.F., Cummings R.D., Paulson J.C.,
RA Forest K.T., Kiessling L.L.;
RT "Recognition of microbial glycans by human intelectin-1.";
RL Nat. Struct. Mol. Biol. 22:603-610(2015).
CC -!- FUNCTION: Lectin that specifically recognizes microbial carbohydrate
CC chains in a calcium-dependent manner (PubMed:11313366,
CC PubMed:26148048). Binds to microbial glycans that contain a terminal
CC acyclic 1,2-diol moiety, including beta-linked D-galactofuranose (beta-
CC Galf), D-phosphoglycerol-modified glycans, D-glycero-D-talo-oct-2-
CC ulosonic acid (KO) and 3-deoxy-D-manno-oct-2-ulosonic acid (KDO)
CC (PubMed:26148048). Binds to glycans from Gram-positive and Gram-
CC negative bacteria, including K.pneumoniae, S.pneumoniae, Y.pestis,
CC P.mirabilis and P.vulgaris (PubMed:26148048). Does not bind human
CC glycans (PubMed:26148048). Probably plays a role in the defense system
CC against microorganisms (Probable). May function as adipokine that has
CC no effect on basal glucose uptake but enhances insulin-stimulated
CC glucose uptake in adipocytes (PubMed:16531507). Increases AKT
CC phosphorylation in the absence and presence of insulin
CC (PubMed:16531507). May interact with lactoferrin/LTF and increase its
CC uptake, and may thereby play a role in iron absorption
CC (PubMed:11747454, PubMed:23921499). {ECO:0000269|PubMed:11313366,
CC ECO:0000269|PubMed:16531507, ECO:0000269|PubMed:23921499,
CC ECO:0000269|PubMed:26148048, ECO:0000305, ECO:0000305|PubMed:11747454}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked (PubMed:11313366,
CC PubMed:17621593, PubMed:26148048). May interact with LTF
CC (PubMed:11747454, PubMed:23921499). {ECO:0000269|PubMed:11313366,
CC ECO:0000269|PubMed:11747454, ECO:0000269|PubMed:17621593,
CC ECO:0000269|PubMed:23921499, ECO:0000269|PubMed:26148048}.
CC -!- INTERACTION:
CC Q8WWA0; Q8WWA0: ITLN1; NbExp=2; IntAct=EBI-16163679, EBI-16163679;
CC Q8WWA0; Q6UWW9: TMEM207; NbExp=2; IntAct=EBI-16163679, EBI-13301303;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11747454};
CC Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:11747454}. Secreted
CC {ECO:0000269|PubMed:11313366, ECO:0000269|PubMed:16531507,
CC ECO:0000305|PubMed:11747454}. Note=Enriched in lipid rafts.
CC {ECO:0000250|UniProtKB:O88310}.
CC -!- TISSUE SPECIFICITY: Highly expressed in omental adipose tissue where it
CC is found in stromal vascular cells but not in fat cells but is barely
CC detectable in subcutaneous adipose tissue (at protein level)
CC (PubMed:16531507). Highly expressed in the small intestine. Also found
CC in the heart, testis, colon, salivary gland, skeletal muscle, pancreas
CC and thyroid and, to a lesser degree, in the uterus, spleen, prostate,
CC lymph node and thymus. {ECO:0000269|PubMed:11181563,
CC ECO:0000269|PubMed:11313366, ECO:0000269|PubMed:11747454,
CC ECO:0000269|PubMed:16531507}.
CC -!- DEVELOPMENTAL STAGE: Found in fetal small intestine and thymus.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11313366,
CC ECO:0000269|PubMed:17621593}.
CC -!- MASS SPECTROMETRY: Mass=35500; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17621593};
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DR EMBL; AF271386; AAM20741.1; -; mRNA.
DR EMBL; AY065972; AAL58073.1; -; mRNA.
DR EMBL; AB036706; BAA96094.1; -; mRNA.
DR EMBL; AY157361; AAO17800.1; -; mRNA.
DR EMBL; AY157362; AAO17801.1; -; mRNA.
DR EMBL; AY549722; AAS49907.1; -; mRNA.
DR EMBL; AY619692; AAU88048.1; -; mRNA.
DR EMBL; AY358359; AAQ88725.1; -; mRNA.
DR EMBL; AK000029; BAA90893.1; -; mRNA.
DR EMBL; CR457224; CAG33505.1; -; mRNA.
DR EMBL; AL354714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52690.1; -; Genomic_DNA.
DR EMBL; BC020664; AAH20664.1; -; mRNA.
DR CCDS; CCDS1211.1; -.
DR RefSeq; NP_060095.2; NM_017625.2.
DR PDB; 4WMQ; X-ray; 1.80 A; A/B=29-313.
DR PDB; 4WMY; X-ray; 1.60 A; A/B=29-313.
DR PDB; 6USC; X-ray; 1.59 A; A/B=35-313.
DR PDBsum; 4WMQ; -.
DR PDBsum; 4WMY; -.
DR PDBsum; 6USC; -.
DR AlphaFoldDB; Q8WWA0; -.
DR SMR; Q8WWA0; -.
DR BioGRID; 120741; 71.
DR DIP; DIP-61704N; -.
DR IntAct; Q8WWA0; 8.
DR STRING; 9606.ENSP00000323587; -.
DR UniLectin; Q8WWA0; -.
DR GlyGen; Q8WWA0; 1 site.
DR iPTMnet; Q8WWA0; -.
DR PhosphoSitePlus; Q8WWA0; -.
DR BioMuta; ITLN1; -.
DR DMDM; 55976553; -.
DR jPOST; Q8WWA0; -.
DR MassIVE; Q8WWA0; -.
DR PaxDb; Q8WWA0; -.
DR PeptideAtlas; Q8WWA0; -.
DR PRIDE; Q8WWA0; -.
DR ProteomicsDB; 74869; -.
DR Antibodypedia; 47062; 333 antibodies from 35 providers.
DR DNASU; 55600; -.
DR Ensembl; ENST00000326245.4; ENSP00000323587.3; ENSG00000179914.5.
DR GeneID; 55600; -.
DR KEGG; hsa:55600; -.
DR MANE-Select; ENST00000326245.4; ENSP00000323587.3; NM_017625.3; NP_060095.2.
DR UCSC; uc001fxc.4; human.
DR CTD; 55600; -.
DR DisGeNET; 55600; -.
DR GeneCards; ITLN1; -.
DR HGNC; HGNC:18259; ITLN1.
DR HPA; ENSG00000179914; Group enriched (adipose tissue, intestine).
DR MIM; 609873; gene.
DR neXtProt; NX_Q8WWA0; -.
DR OpenTargets; ENSG00000179914; -.
DR PharmGKB; PA134870726; -.
DR VEuPathDB; HostDB:ENSG00000179914; -.
DR eggNOG; ENOG502QU6C; Eukaryota.
DR GeneTree; ENSGT00940000154757; -.
DR HOGENOM; CLU_066147_0_0_1; -.
DR InParanoid; Q8WWA0; -.
DR OMA; HTNTGFL; -.
DR OrthoDB; 754383at2759; -.
DR PhylomeDB; Q8WWA0; -.
DR TreeFam; TF328530; -.
DR PathwayCommons; Q8WWA0; -.
DR Reactome; R-HSA-6803157; Antimicrobial peptides.
DR SignaLink; Q8WWA0; -.
DR BioGRID-ORCS; 55600; 5 hits in 1070 CRISPR screens.
DR ChiTaRS; ITLN1; human.
DR GeneWiki; ITLN1; -.
DR GenomeRNAi; 55600; -.
DR Pharos; Q8WWA0; Tbio.
DR PRO; PR:Q8WWA0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8WWA0; protein.
DR Bgee; ENSG00000179914; Expressed in parietal pleura and 107 other tissues.
DR Genevisible; Q8WWA0; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0070492; F:oligosaccharide binding; IDA:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; IDA:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
DR GO; GO:0009624; P:response to nematode; ISS:UniProtKB.
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 SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; GPI-anchor; Lectin; Lipoprotein; Membrane;
KW Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:11313366,
FT ECO:0000269|PubMed:17621593"
FT CHAIN 19..298
FT /note="Intelectin-1"
FT /id="PRO_0000009143"
FT PROPEP 299..313
FT /evidence="ECO:0000255"
FT /id="PRO_0000009144"
FT DOMAIN 32..255
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT BINDING 262..263
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMY"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT BINDING 274
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMY"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT LIPID 298
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 31
FT /note="Interchain (with C-48)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739,
FT ECO:0000269|PubMed:17621593, ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT DISULFID 41..70
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT DISULFID 48
FT /note="Interchain (with C-31)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739,
FT ECO:0000269|PubMed:17621593, ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT DISULFID 94..280
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT DISULFID 199..259
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT DISULFID 251..265
FT /evidence="ECO:0000269|PubMed:26148048,
FT ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY"
FT VARIANT 109
FT /note="V -> D (in dbSNP:rs2274907)"
FT /evidence="ECO:0000269|PubMed:11313366"
FT /id="VAR_019924"
FT VARIANT 313
FT /note="R -> P (in dbSNP:rs8144)"
FT /evidence="ECO:0000269|PubMed:14720597, ECO:0000269|Ref.6"
FT /id="VAR_019925"
FT MUTAGEN 31
FT /note="C->S: Forms mainly monomers; when associated with S-
FT 48."
FT /evidence="ECO:0000269|PubMed:17621593"
FT MUTAGEN 48
FT /note="C->S: Forms mainly dimers. Forms mainly monomers;
FT when associated with S-31."
FT /evidence="ECO:0000269|PubMed:17621593"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:6USC"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:6USC"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:6USC"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:6USC"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:6USC"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:6USC"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:6USC"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6USC"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:6USC"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:6USC"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:6USC"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6USC"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:6USC"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:6USC"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:6USC"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:6USC"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:6USC"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:6USC"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:6USC"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:6USC"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:6USC"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:6USC"
FT STRAND 231..241
FT /evidence="ECO:0007829|PDB:6USC"
FT STRAND 247..256
FT /evidence="ECO:0007829|PDB:6USC"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:6USC"
FT TURN 274..279
FT /evidence="ECO:0007829|PDB:6USC"
FT TURN 282..289
FT /evidence="ECO:0007829|PDB:6USC"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:6USC"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:6USC"
SQ SEQUENCE 313 AA; 34962 MW; 56219FE937FC802E CRC64;
MNQLSFLLFL IATTRGWSTD EANTYFKEWT CSSSPSLPRS CKEIKDECPS AFDGLYFLRT
ENGVIYQTFC DMTSGGGGWT LVASVHENDM RGKCTVGDRW SSQQGSKAVY PEGDGNWANY
NTFGSAEAAT SDDYKNPGYY DIQAKDLGIW HVPNKSPMQH WRNSSLLRYR TDTGFLQTLG
HNLFGIYQKY PVKYGEGKCW TDNGPVIPVV YDFGDAQKTA SYYSPYGQRE FTAGFVQFRV
FNNERAANAL CAGMRVTGCN TEHHCIGGGG YFPEASPQQC GDFSGFDWSG YGTHVGYSSS
REITEAAVLL FYR
