ITL1A_MOUSE
ID ITL1A_MOUSE Reviewed; 313 AA.
AC O88310; Q5IWS3;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Intelectin-1a;
DE AltName: Full=Galactofuranose-binding lectin;
DE AltName: Full=Intestinal lactoferrin receptor {ECO:0000303|PubMed:16866365, ECO:0000305|PubMed:15222482};
DE Flags: Precursor;
GN Name=Itln1; Synonyms=Intl, Itln, Itln1a, Itlna;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Intestine;
RX PubMed=9790983; DOI=10.1006/bbrc.1998.9513;
RA Komiya T., Tanigawa Y., Hirohashi S.;
RT "Cloning of the novel gene intelectin, which is expressed in intestinal
RT Paneth cells in mice.";
RL Biochem. Biophys. Res. Commun. 251:759-762(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Intestine, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NIH Swiss; TISSUE=Ovary;
RA Peavy T.R., Hedrick J.L.;
RT "Mouse homolog of the Xenopus laevis egg cortical granule lectin.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15222482; DOI=10.1023/b:biom.0000027709.42733.e4;
RA Suzuki Y.A., Lonnerdal B.;
RT "Baculovirus expression of mouse lactoferrin receptor and tissue
RT distribution in the mouse.";
RL BioMetals 17:301-309(2004).
RN [6]
RP TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Intestine;
RX PubMed=15265922; DOI=10.4049/jimmunol.173.3.1894;
RA Pemberton A.D., Knight P.A., Gamble J., Colledge W.H., Lee J.K., Pierce M.,
RA Miller H.R.;
RT "Innate BALB/c enteric epithelial responses to Trichinella spiralis:
RT inducible expression of a novel goblet cell lectin, intelectin-2, and its
RT natural deletion in C57BL/10 mice.";
RL J. Immunol. 173:1894-1901(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=16936804; DOI=10.1139/o06-059;
RA Lopez V., Suzuki Y.A., Loennerdal B.;
RT "Ontogenic changes in lactoferrin receptor and DMT1 in mouse small
RT intestine: implications for iron absorption during early life.";
RL Biochem. Cell Biol. 84:337-344(2006).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16866365; DOI=10.1021/bi060570x;
RA Wrackmeyer U., Hansen G.H., Seya T., Danielsen E.M.;
RT "Intelectin: a novel lipid raft-associated protein in the enterocyte brush
RT border.";
RL Biochemistry 45:9188-9197(2006).
RN [9]
RP INDUCTION.
RX PubMed=17420014; DOI=10.1016/j.exppara.2007.02.015;
RA Voehringer D., Stanley S.A., Cox J.S., Completo G.C., Lowary T.L.,
RA Locksley R.M.;
RT "Nippostrongylus brasiliensis: identification of intelectin-1 and -2 as
RT Stat6-dependent genes expressed in lung and intestine during infection.";
RL Exp. Parasitol. 116:458-466(2007).
RN [10]
RP SUBUNIT, AND MASS SPECTROMETRY.
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 [11]
RP FUNCTION.
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:26148048). Binds to
CC microbial glycans that contain a terminal acyclic 1,2-diol moiety,
CC including beta-linked D-galactofuranose (beta-Galf), D-phosphoglycerol-
CC modified glycans, D-glycero-D-talo-oct-2-ulosonic acid (KO) and 3-
CC deoxy-D-manno-oct-2-ulosonic acid (KDO). Binds to glycans from Gram-
CC positive and Gram-negative bacteria, including K.pneumoniae,
CC S.pneumoniae, Y.pestis, P.mirabilis and P.vulgaris. Does not bind
CC mammalian glycans. Probably plays a role in the defense system against
CC microorganisms. May function as adipokine that has no effect on basal
CC glucose uptake but enhances insulin-stimulated glucose uptake in
CC adipocytes. Increases AKT phosphorylation in the absence and presence
CC of insulin. May interact with lactoferrin/LTF and increase its uptake,
CC and may thereby play a role in iron absorption (By similarity).
CC {ECO:0000250|UniProtKB:Q8WWA0, ECO:0000269|PubMed:26148048}.
CC -!- SUBUNIT: Monomer (PubMed:17621593). May interact with LTF (By
CC similarity). {ECO:0000250|UniProtKB:Q8WWA0,
CC ECO:0000269|PubMed:17621593}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8WWA0};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8WWA0}. Secreted
CC {ECO:0000250|UniProtKB:Q8WWA0}. Note=Enriched in lipid rafts.
CC {ECO:0000269|PubMed:16866365}.
CC -!- TISSUE SPECIFICITY: Expressed in small intestinal Paneth cells in
CC uninfected mice. Expression also detected in various other tissues
CC including stomach, kidney, ovary and brain.
CC {ECO:0000269|PubMed:15222482, ECO:0000269|PubMed:15265922,
CC ECO:0000269|PubMed:16866365, ECO:0000269|PubMed:16936804,
CC ECO:0000269|PubMed:9790983}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, levels are highest at day 7,
CC decrease by mid-embryogenesis at day 11 and increase again in late
CC embryogenesis at day 17. {ECO:0000269|PubMed:15222482}.
CC -!- INDUCTION: By infection with the helminth parasite N.brasiliensis.
CC {ECO:0000269|PubMed:17420014}.
CC -!- MASS SPECTROMETRY: Mass=34000; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17621593};
CC -!- MISCELLANEOUS: Constitutive expression does not lead to enhanced
CC immunity to N.brasiliensis or M.tuberculosis.
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DR EMBL; AB016496; BAA31992.1; -; mRNA.
DR EMBL; AY157363; AAO17802.1; -; mRNA.
DR EMBL; AY157364; AAO17803.1; -; mRNA.
DR EMBL; AY619693; AAU88049.1; -; mRNA.
DR EMBL; AK007447; BAB25043.1; -; mRNA.
DR CCDS; CCDS35777.1; -.
DR PIR; JE0328; JE0328.
DR RefSeq; NP_034714.1; NM_010584.3.
DR AlphaFoldDB; O88310; -.
DR SMR; O88310; -.
DR BioGRID; 200841; 1.
DR STRING; 10090.ENSMUSP00000043837; -.
DR iPTMnet; O88310; -.
DR PhosphoSitePlus; O88310; -.
DR MaxQB; O88310; -.
DR PaxDb; O88310; -.
DR PRIDE; O88310; -.
DR ProteomicsDB; 269415; -.
DR Antibodypedia; 47062; 333 antibodies from 35 providers.
DR DNASU; 16429; -.
DR Ensembl; ENSMUST00000043094; ENSMUSP00000043837; ENSMUSG00000038209.
DR GeneID; 16429; -.
DR KEGG; mmu:16429; -.
DR UCSC; uc007doq.2; mouse.
DR CTD; 55600; -.
DR MGI; MGI:1333831; Itln1.
DR VEuPathDB; HostDB:ENSMUSG00000038209; -.
DR eggNOG; ENOG502QU6C; Eukaryota.
DR GeneTree; ENSGT00940000154757; -.
DR HOGENOM; CLU_066147_0_0_1; -.
DR InParanoid; O88310; -.
DR OMA; HTNTGFL; -.
DR OrthoDB; 754383at2759; -.
DR PhylomeDB; O88310; -.
DR TreeFam; TF328530; -.
DR Reactome; R-MMU-6803157; Antimicrobial peptides.
DR BioGRID-ORCS; 16429; 7 hits in 71 CRISPR screens.
DR PRO; PR:O88310; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O88310; protein.
DR Bgee; ENSMUSG00000038209; Expressed in crypt of Lieberkuhn of small intestine and 47 other tissues.
DR ExpressionAtlas; O88310; baseline and differential.
DR Genevisible; O88310; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; ISS:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0070492; F:oligosaccharide binding; IDA:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; ISO:MGI.
DR GO; GO:0009624; P:response to nematode; IDA: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 Pfam; PF00147; Fibrinogen_C; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lectin;
KW Lipoprotein; Membrane; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT CHAIN 19..298
FT /note="Intelectin-1a"
FT /id="PRO_0000009145"
FT PROPEP 299..313
FT /evidence="ECO:0000255"
FT /id="PRO_0000009146"
FT DOMAIN 32..251
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:0000250|UniProtKB:Q8WWA0"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q5PPM0"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 262..263
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 274
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT LIPID 298
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT DISULFID 41..70
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT DISULFID 94..280
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT DISULFID 199..259
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT DISULFID 251..265
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
SQ SEQUENCE 313 AA; 34953 MW; D2FA447D3D8547A4 CRC64;
MTQLGFLLFI MVATRGCSAA EENLDTNRWG NSFFSSLPRS CKEIKQEHTK AQDGLYFLRT
KNGVIYQTFC DMTTAGGGWT LVASVHENNM RGKCTVGDRW SSQQGNRADY PEGDGNWANY
NTFGSAEAAT SDDYKNPGYF DIQAENLGIW HVPNKSPLHN WRKSSLLRYR TFTGFLQHLG
HNLFGLYKKY PVKYGEGKCW TDNGPALPVV YDFGDARKTA SYYSPSGQRE FTAGYVQFRV
FNNERAASAL CAGVRVTGCN TEHHCIGGGG FFPEGNPVQC GDFASFDWDG YGTHNGYSSS
RKITEAAVLL FYR
