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   19-JAN-2010, entry version 64.
DE   RecName: Full=Intelectin-1;
DE            Short=ITLN-1;
DE   AltName: Full=Intestinal lactoferrin receptor;
DE   AltName: Full=Galactofuranose-binding lectin;
DE   AltName: Full=Endothelial lectin HL-1;
DE   AltName: Full=Omentin;
DE   Flags: Precursor;
GN   Name=ITLN1; Synonyms=INTL, ITLN, LFR; ORFNames=UNQ640/PRO1270;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], GPI-ANCHOR, AND TISSUE SPECIFICITY.
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   MEDLINE=21096026; 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.,
RA   Toyoshima K., Seya T.;
RT   "Human intelectin is a novel soluble lectin that recognizes
RT   galactofuranose 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,
RT   developmental expression, and identification of the eglectin family of
RT   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
RT   human 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   MEDLINE=22887296; 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.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   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.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   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.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [13]
RP   SUBUNIT, MASS SPECTROMETRY, GLYCOSYLATION, DISULFIDE BOND, AND
RP   MUTAGENESIS 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.,
RA   Myrvik Q.N., Hoffman D.R., Henriksen R.A., Shibata Y.;
RT   "Differential structure and activity between human and mouse
RT   intelectin-1: human intelectin-1 is a disulfide-linked trimer, whereas
RT   mouse homologue is a monomer.";
RL   Glycobiology 17:1045-1051(2007).
CC   -!- FUNCTION: Has no effect on basal glucose uptake but enhances
CC       insulin-stimulated glucose uptake in adipocytes. Increases AKT
CC       phosphorylation in the absence and presence of insulin. May play a
CC       role in the defense system against microorganisms. May
CC       specifically recognize carbohydrate chains of pathogens and
CC       bacterial components containing galactofuranosyl residues, in a
CC       calcium-dependent manner. May be involved in iron metabolism.
CC   -!- SUBUNIT: Homotrimer; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC       Secreted. Note=Enriched in lipid rafts (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in omental adipose tissue
CC       where it is found in stromal vascular cells but not in fat cells
CC       but is barely detectable in subcutaneous adipose tissue (at
CC       protein level). Highly expressed in the small intestine. Also
CC       found in the heart, testis, colon, salivary gland, skeletal
CC       muscle, pancreas and thyroid and, to a lesser degree, in the
CC       uterus, spleen, prostate, lymph node and thymus.
CC   -!- DEVELOPMENTAL STAGE: Found in fetal small intestine and thymus.
CC   -!- PTM: N-glycosylated.
CC   -!- MASS SPECTROMETRY: Mass=35500; Method=MALDI; Range=19-298;
CC       Source=PubMed:17621593;
CC   -!- SIMILARITY: Contains 1 fibrinogen C-terminal domain.
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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; CAH72357.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW52690.1; -; Genomic_DNA.
DR   EMBL; BC020664; AAH20664.1; -; mRNA.
DR   IPI; IPI00291737; -.
DR   RefSeq; NP_060095.2; -.
DR   UniGene; Hs.50813; -.
DR   SMR; Q8WWA0; 36-84, 38-127.
DR   STRING; Q8WWA0; -.
DR   PRIDE; Q8WWA0; -.
DR   Ensembl; ENST00000326245; ENSP00000323587; ENSG00000179914; Homo sapiens.
DR   GeneID; 55600; -.
DR   KEGG; hsa:55600; -.
DR   UCSC; uc001fxc.1; human.
DR   CTD; 55600; -.
DR   GeneCards; GC01M159112; -.
DR   H-InvDB; HIX0019706; -.
DR   HGNC; HGNC:18259; ITLN1.
DR   HPA; CAB012652; -.
DR   MIM; 609873; gene.
DR   PharmGKB; PA134870726; -.
DR   eggNOG; prNOG15313; -.
DR   HOGENOM; HBG444124; -.
DR   HOVERGEN; Q8WWA0; -.
DR   InParanoid; Q8WWA0; -.
DR   OMA; TDEANTY; -.
DR   OrthoDB; EOG9PZMRX; -.
DR   PhylomeDB; Q8WWA0; -.
DR   NextBio; 60138; -.
DR   ArrayExpress; Q8WWA0; -.
DR   Bgee; Q8WWA0; -.
DR   CleanEx; HS_ITLN1; -.
DR   Genevestigator; Q8WWA0; -.
DR   GermOnline; ENSG00000179914; Homo sapiens.
DR   GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR   GO; GO:0005102; F:receptor binding; IEA:InterPro.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   GO; GO:0046326; P:positive regulation of glucose import; IDA:UniProtKB.
DR   GO; GO:0001934; P:positive regulation of protein amino acid p...; IDA:UniProtKB.
DR   GO; GO:0009624; P:response to nematode; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C.
DR   SMART; SM00186; FBG; 1.
DR   PROSITE; PS00514; FIBRINOGEN_C_1; FALSE_NEG.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; GPI-anchor; Lectin; Lipoprotein;
KW   Membrane; Polymorphism; Secreted; Signal.
FT   SIGNAL        1     18
FT   CHAIN        19    298       Intelectin-1.
FT                                /FTId=PRO_0000009143.
FT   PROPEP      299    313       Potential.
FT                                /FTId=PRO_0000009144.
FT   DOMAIN       32    255       Fibrinogen C-terminal.
FT   LIPID       298    298       GPI-anchor amidated serine (Potential).
FT   CARBOHYD    163    163       N-linked (GlcNAc...) (Probable).
FT   DISULFID     31     48
FT   VARIANT     109    109       V -> D (in dbSNP:rs2274907).
FT                                /FTId=VAR_019924.
FT   VARIANT     313    313       R -> P (in dbSNP:rs8144).
FT                                /FTId=VAR_019925.
FT   MUTAGEN      31     31       C->S: Forms mainly monomers; when
FT                                associated with S-48.
FT   MUTAGEN      48     48       C->S: Forms mainly dimers. Forms mainly
FT                                monomers; when associated with S-31.
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
//