ITL1B_MOUSE
ID ITL1B_MOUSE Reviewed; 313 AA.
AC Q80ZA0;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Intelectin-1b;
DE AltName: Full=Intelectin-2;
DE Flags: Precursor;
GN Name=Itln1b; Synonyms=Itln2, Itlnb;
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 INDUCTION.
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 [2]
RP INDUCTION.
RX PubMed=15048991; DOI=10.1002/pmic.200300658;
RA Pemberton A.D., Knight P.A., Wright S.H., Miller H.R.;
RT "Proteomic analysis of mouse jejunal epithelium and its response to
RT infection with the intestinal nematode, Trichinella spiralis.";
RL Proteomics 4:1101-1108(2004).
RN [3]
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).
CC -!- FUNCTION: May play a protective role in the innate immune response to
CC parasite infection. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8WWA0};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8WWA0}. Secreted
CC {ECO:0000250|UniProtKB:Q8WWA0}.
CC -!- TISSUE SPECIFICITY: Expressed in the globlet and Paneth cells of the
CC small intestine of infected mice. Expressed in the ileum of uninfected
CC mice.
CC -!- INDUCTION: Up-regulated by infection with T.spiralis (at protein
CC level). Also induced by infection with the helminth parasite
CC N.brasiliensis. {ECO:0000269|PubMed:15048991,
CC ECO:0000269|PubMed:15265922, ECO:0000269|PubMed:17420014}.
CC -!- MISCELLANEOUS: Constitutive expression does not lead to enhanced
CC immunity to N.brasiliensis or M.tuberculosis.
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DR EMBL; AY217760; AAO60215.1; -; mRNA.
DR RefSeq; NP_001007553.1; NM_001007552.1.
DR AlphaFoldDB; Q80ZA0; -.
DR SMR; Q80ZA0; -.
DR GlyGen; Q80ZA0; 1 site.
DR PRIDE; Q80ZA0; -.
DR GeneID; 493583; -.
DR KEGG; mmu:493583; -.
DR CTD; 493583; -.
DR MGI; MGI:3057189; Itlnb.
DR InParanoid; Q80ZA0; -.
DR PRO; PR:Q80ZA0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80ZA0; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0070492; F:oligosaccharide binding; ISO:MGI.
DR GO; GO:0002215; P:defense response to nematode; IMP:MGI.
DR GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..298
FT /note="Intelectin-1b"
FT /id="PRO_0000009147"
FT PROPEP 299..313
FT /evidence="ECO:0000255"
FT /id="PRO_0000009148"
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 CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
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; 35070 MW; BEF4E2757C71FC00 CRC64;
MTQLGFLLFI MIATRVCSAA EENLDTNRWG NSFFSSLPRS CKEIKQEDTK AQDGLYFLRT
ENGVIYQTFC DMTTAGGGWT LVASVHENNL RGRCTVGDRW SSQQGNRADY PEGDGNWANY
NTFGSAEGAT SDDYKNPGYF DIQAENLGIW HVPNNSPLHT WRNSSLLRYR TFTGFLQRLG
HNLFGLYQKY PVKYGEGKCW TDNGPAFPVV YDFGDAQKTA SYYSPSGRNE FTAGYVQFRV
FNNERAASAL CAGVRVTGCN TEHHCIGGGG FFPEFDPEEC GDFAAFDANG YGTHIRYSNS
REITEAAVLL FYR
