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 24-JAN-2024, entry version 158. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; Q8WWA0; 1 site, No reported glycans. 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; 9606-ENSP00000323587; -. DR PeptideAtlas; Q8WWA0; -. DR ProteomicsDB; 74869; -. DR Antibodypedia; 47062; 369 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 AGR; HGNC:18259; -. 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; EIKDECP; -. DR OrthoDB; 5395990at2759; -. DR PhylomeDB; Q8WWA0; -. DR TreeFam; TF328530; -. DR PathwayCommons; Q8WWA0; -. DR Reactome; R-HSA-6803157; Antimicrobial peptides. DR SignaLink; Q8WWA0; -. DR SIGNOR; Q8WWA0; -. DR BioGRID-ORCS; 55600; 5 hits in 1148 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 108 other cell types or tissues. 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:0098552; C:side of membrane; IEA:UniProtKB-KW. 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; Gamma Fibrinogen, chain A, domain 1; 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 NCBIfam; NF040941; GGGWT_bact; 1. DR PANTHER; PTHR16146; INTELECTIN; 1. DR PANTHER; PTHR16146:SF38; INTELECTIN-1; 1. DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1. DR PROSITE; PS51406; FIBRINOGEN_C_2; 1. DR Genevisible; Q8WWA0; HS. 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 FT S-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 //