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UniProtKB/Swiss-Prot entry Q8WWA0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ITLN1_HUMAN
Primary accession number Q8WWA0
Secondary accession numbers Q6YDJ3 Q9NP67
Integrated into Swiss-Prot on November 23, 2004
Sequence was last modified on March 1, 2002 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 52)
Name and origin of the protein
Protein name Intelectin-1 [Precursor]
Synonyms ITLN-1
Intestinal lactoferrin receptor
Galactofuranose-binding lectin
Endothelial lectin HL-1
Omentin
Gene name
Name: ITLN1
Synonyms: INTL, ITLN, LFR
ORFNames: UNQ640/PRO1270
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], GPI-ANCHOR, AND TISSUE SPECIFICITY.
TISSUE=Small intestine;
DOI=10.1021/bi0155899; PubMed=11747454 [NCBI, ExPASy, EBI, Israel, Japan]
Suzuki Y.A., Shin K., Loennerdal B.;
"Molecular cloning and functional expression of a human intestinal lactoferrin receptor.";
Biochemistry 40:15771-15779(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Small intestine;
DOI=10.1093/glycob/11.1.65; PubMed=11181563 [NCBI, ExPASy, EBI, Israel, Japan]
Lee J.K., Schnee J., Pang M., Wolfert M., Baum L.G., Moremen K.W., Pierce M.;
"Human homologs of the Xenopus oocyte cortical granule lectin XL35.";
Glycobiology 11:65-73(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-28, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT, GLYCOSYLATION, AND VARIANT ASP-109.
TISSUE=Placenta;
DOI=10.1074/jbc.M103162200; PubMed=11313366 [NCBI, ExPASy, EBI, Israel, Japan]
Tsuji S., Uehori J., Matsumoto M., Suzuki Y., Matsuhisa A., Toyoshima K., Seya T.;
"Human intelectin is a novel soluble lectin that recognizes galactofuranose in carbohydrate chains of bacterial cell wall.";
J. Biol. Chem. 276:23456-23463(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-313.
DOI=10.1016/S1095-6433(03)00269-1; PubMed=14720597 [NCBI, ExPASy, EBI, Israel, Japan]
Chang B.Y., Peavy T.R., Wardrip N.J., Hedrick J.L.;
"The Xenopus laevis cortical granule lectin: cDNA cloning, developmental expression, and identification of the eglectin family of lectins.";
Comp. Biochem. Physiol. 137A:115-129(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Adipose tissue;
DOI=10.1152/ajpendo.00572.2004; PubMed=16531507 [NCBI, ExPASy, EBI, Israel, Japan]
Yang R.-Z., Lee M.-J., Hu H., Pray J., Wu H.-B., Hansen B.C., Shuldiner A.R., Fried S.K., McLenithan J.C., Gong D.-W.;
"Identification of omentin as a novel depot-specific adipokine in human adipose tissue: possible role in modulating insulin action.";
Am. J. Physiol. 290:E1253-E1261(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.1293003; PubMed=12975309 [NCBI, ExPASy, EBI, Israel, Japan]
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Adipose tissue;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
SUBUNIT, MASS SPECTROMETRY, GLYCOSYLATION, DISULFIDE BOND, AND MUTAGENESIS OF CYS-31 AND CYS-48.
DOI=10.1093/glycob/cwm075; PubMed=17621593 [NCBI, ExPASy, EBI, Israel, Japan]
Tsuji S., Yamashita M., Nishiyama A., Shinohara T., Li Z., Myrvik Q.N., Hoffman D.R., Henriksen R.A., Shibata Y.;
"Differential structure and activity between human and mouse intelectin-1: human intelectin-1 is a disulfide-linked trimer, whereas mouse homologue is a monomer.";
Glycobiology 17:1045-1051(2007).
Comments
  • FUNCTION: Has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes. Increases AKT phosphorylation in the absence and presence of insulin. May play a role in the defense system against microorganisms. May specifically recognize carbohydrate chains of pathogens and bacterial components containing galactofuranosyl residues, in a calcium-dependent manner. May be involved in iron metabolism.
  • SUBUNIT: Homotrimer; disulfide-linked.
  • SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Secreted. Note=Enriched in lipid rafts (By similarity).
  • TISSUE SPECIFICITY: Highly expressed in omental adipose tissue where it is found in stromal vascular cells but not in fat cells but is barely detectable in subcutaneous adipose tissue (at protein level). Highly expressed in the small intestine. Also found in the heart, testis, colon, salivary gland, skeletal muscle, pancreas and thyroid and, to a lesser degree, in the uterus, spleen, prostate, lymph node and thymus.
  • DEVELOPMENTAL STAGE: Found in fetal small intestine and thymus.
  • PTM: N-glycosylated.
  • MASS SPECTROMETRY: Mass=35500; Method=MALDI; Range=19-298; Source=PubMed:17621593;.
  • SIMILARITY: Contains 1 fibrinogen C-terminal domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF271386; AAM20741.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY065972; AAL58073.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB036706; BAA96094.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY157361; AAO17800.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY157362; AAO17801.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY549722; AAS49907.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR457224; CAG33505.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY358359; AAQ88725.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK000029; BAA90893.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020664; AAH20664.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_060095.2; -.
UniGene Hs.50813
3D structure databases
ModBase Q8WWA0.
Organism-specific databases
GeneCards GC01M159112; -.
H-InvDB HIX0019706; -.
HGNC HGNC:18259; ITLN1.
GenAtlas ITLN1.
HPA CAB012652; -.
MIM 609873; gene. [NCBI / EBI]
PharmGKB PA134870726; -.
GeneCards Q8WWA0.
Gene expression databases
ArrayExpress Q8WWA0; -.
CleanEx HS_ITLN1; -.
GermOnline ENSG00000179914; Homo sapiens.
Ontologies
GO
GO:0031225; Cellular component: anchored to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0031526; Cellular component: brush border membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0045121; Cellular component: membrane raft (inferred from sequence or structural similarity from UniProtKB).
GO:0005102; Molecular function: receptor binding (inferred from electronic annotation from InterPro).
GO:0005529; Molecular function: sugar binding (inferred from electronic annotation from UniProtKB-KW).
GO:0046326; Biological process: positive regulation of glucose import (inferred from direct assay from UniProtKB).
GO:0001934; Biological process: positive regulation of protein amino acid phosphorylation (inferred from direct assay from UniProtKB).
GO:0009624; Biological process: response to nematode (inferred from sequence or structural similarity from UniProtKB).
GO:0007165; Biological process: signal transduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR002181; Fibrinogen_a/b/g_C.
Graphical view of domain structure.
Pfam PF00147; Fibrinogen_C; 1.
Pfam graphical view of domain structure.
SMART SM00186; FBG; 1.
SMART graphical view of domain structure.
PROSITE PS00514; FIBRINOGEN_C_1; FALSE_NEG.
PS51406; FIBRINOGEN_C_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE Q8WWA0; -.
Genome annotation databases
Ensembl ENSG00000179914; Homo sapiens. [Contig view]
GeneID 55600; -.
KEGG hsa:55600; -.
Phylogenomic databases
HOGENOM Q8WWA0; -.
HOVERGEN Q8WWA0; -.
Other
NextBio 60138; -.
SOURCE ITLN1; Homo sapiens.
ProtoNet Q8WWA0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor; Lectin; Lipoprotein; Membrane; Polymorphism; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18      
CHAIN   19   298  280     Intelectin-1. PRO_0000009143
PROPEP   299   313  15     Potential. PRO_0000009144
DOMAIN   32   255  224     Fibrinogen C-terminal. 
LIPID   298   298        GPI-anchor amidated serine (Potential). 
CARBOHYD   163   163        N-linked (GlcNAc...) (Probable). 
DISULFID   31    48         
VARIANT   109   109  1     V -> D (in dbSNP:rs2274907 [NCBI]). VAR_019924 
VARIANT   313   313  1     R -> P (in dbSNP:rs8144 [NCBI]). VAR_019925 
MUTAGEN   31    31        C->S: Forms mainly monomers; when associated with S-48. 
MUTAGEN   48    48        C->S: Forms mainly dimers. Forms mainly monomers; when associated with S-31. 
Sequence information
Length: 313 AA [This is the length of the unprocessed precursor] Molecular weight: 34962 Da [This is the MW of the unprocessed precursor] CRC64: 56219FE937FC802E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNQLSFLLFL IATTRGWSTD EANTYFKEWT CSSSPSLPRS CKEIKDECPS AFDGLYFLRT 

        70         80         90        100        110        120 
ENGVIYQTFC DMTSGGGGWT LVASVHENDM RGKCTVGDRW SSQQGSKAVY PEGDGNWANY 

       130        140        150        160        170        180 
NTFGSAEAAT SDDYKNPGYY DIQAKDLGIW HVPNKSPMQH WRNSSLLRYR TDTGFLQTLG 

       190        200        210        220        230        240 
HNLFGIYQKY PVKYGEGKCW TDNGPVIPVV YDFGDAQKTA SYYSPYGQRE FTAGFVQFRV 

       250        260        270        280        290        300 
FNNERAANAL CAGMRVTGCN TEHHCIGGGG YFPEASPQQC GDFSGFDWSG YGTHVGYSSS 

       310 
REITEAAVLL FYR 

Q8WWA0 in FASTA format

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