Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Lactotransferrin (Lactoferrin) (EC 3.4.21.-) (Growth-inhibiting protein 12) (Talalactoferrin) [Cleaved into: Lactoferricin-H (Lfcin-H); Kaliocin-1; Lactoferroxin-A; Lactoferroxin-B; Lactoferroxin-C]

 TRFL_HUMAN              Reviewed;         710 AA.
P02788; A8K9U8; B2MV13; B7Z4X2; E7EQH5; O00756; Q16780; Q16785;
Q16786; Q16789; Q5DSM0; Q8IU92; Q8IZH6; Q8TCD2; Q96KZ4; Q96KZ5;
Q9H1Z3; Q9UCY5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
24-JAN-2006, sequence version 6.
25-OCT-2017, entry version 218.
RecName: Full=Lactotransferrin;
Short=Lactoferrin;
EC=3.4.21.-;
AltName: Full=Growth-inhibiting protein 12;
AltName: Full=Talalactoferrin;
Contains:
RecName: Full=Lactoferricin-H;
Short=Lfcin-H;
Contains:
RecName: Full=Kaliocin-1;
Contains:
RecName: Full=Lactoferroxin-A;
Contains:
RecName: Full=Lactoferroxin-B;
Contains:
RecName: Full=Lactoferroxin-C;
Flags: Precursor;
Name=LTF; Synonyms=GIG12, LF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-22 INS;
THR-148 AND CYS-422.
TISSUE=Mammary gland;
PubMed=2402455; DOI=10.1093/nar/18.17.5288;
Rey M.W., Woloshuk S.L., de Boer H.A., Pieper F.R.;
"Complete nucleotide sequence of human mammary gland lactoferrin.";
Nucleic Acids Res. 18:5288-5288(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-22 INS.
TISSUE=Mammary gland;
Cho Y.Y.;
"Cloning of human lactoferrin gene and its polymorphism in normal and
cancer cells.";
Thesis (1994), Genetic Engineering Research Institute, South Korea.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND DELTALF), ALTERNATIVE
SPLICING, AND TISSUE SPECIFICITY.
TISSUE=Lung;
PubMed=9122171; DOI=10.1073/pnas.94.6.2198;
Siebert P.D., Huang B.C.;
"Identification of an alternative form of human lactoferrin mRNA that
is expressed differentially in normal tissues and tumor-derived cell
lines.";
Proc. Natl. Acad. Sci. U.S.A. 94:2198-2203(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-22 INS;
THR-29; ARG-47 AND ASP-579.
TISSUE=Mammary gland;
PubMed=11702692;
Cheng H., Chen X.Z., Huan L.D.;
"cDNA cloning and sequence analysis of human lactoferrin.";
Sheng Wu Gong Cheng Xue Bao 17:385-387(2001).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (3.40
ANGSTROMS) OF 22-710 IN COMPLEX WITH IRON AND CARBONATE, AND VARIANTS
ARG-22 INS; THR-29; ARG-47 AND ASP-579.
TISSUE=Seminal vesicle;
PubMed=22900286;
Kumar J., Weber W., Munchau S., Yadav S., Singh S.B., Saravanan K.,
Paramasivam M., Sharma S., Kaur P., Bhushan A., Srinivasan A.,
Betzel C., Singh T.P.;
"Crystal structure of human seminal diferric lactoferrin at 3.4
Angstrom resolution.";
Indian J. Biochem. Biophys. 40:14-21(2003).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 20-30,
FUNCTION, AND VARIANTS ARG-22 INS; THR-29 AND ARG-47.
TISSUE=Blood;
PubMed=14573629; DOI=10.1128/IAI.71.11.6141-6147.2003;
Velliyagounder K., Kaplan J.B., Furgang D., Legarda D., Diamond G.,
Parkin R.E., Fine D.H.;
"One of two human lactoferrin variants exhibits increased
antibacterial and transcriptional activation activities and is
associated with localized juvenile periodontitis.";
Infect. Immun. 71:6141-6147(2003).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Bone marrow;
Wei X., Han J., Rado T.A.;
"Human neutrophil lactoferrin coding and 5' flanking region DNA
sequences.";
Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-22 INS;
THR-29 AND ARG-47.
TISSUE=Prostate;
Conneely O.M.;
Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-22 INS;
THR-29; ARG-47 AND ASP-579.
TISSUE=Mammary gland;
Shi Y.-Q., Zhang Y., Zheng Y.-M.;
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-22 INS AND
CYS-422.
Kim J.W.;
"Identification of a growth inhibition gene.";
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-22 INS; THR-29 AND
ARG-47.
Allayous C., Marianne-Pepin T.;
"Mutations in ELA2 and LTF genes.";
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND DELTALF), AND
VARIANT ARG-22 INS.
TISSUE=Lung, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
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).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-22
INS.
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
PubMed=1480183; DOI=10.1210/mend.6.11.1480183;
Teng C.T., Liu Y., Yang N., Walmer D., Panella T.;
"Differential molecular mechanism of the estrogen action that
regulates lactoferrin gene in human and mouse.";
Mol. Endocrinol. 6:1969-1981(1992).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-710 (ISOFORM 1), AND VARIANT ARG-22
INS.
TISSUE=Mammary gland;
PubMed=2374734; DOI=10.1093/nar/18.13.4013;
Powell M.J., Ogden J.E.;
"Nucleotide sequence of human lactoferrin cDNA.";
Nucleic Acids Res. 18:4013-4013(1990).
[17]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-710 (ISOFORM 1), AND VARIANT ARG-22
INS.
TISSUE=Mammary gland;
Liang Q., Jimenez-Flores R., Richardson T.;
"Molecular cloning and sequence analysis of human lactoferrin.";
Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases.
[18]
PROTEIN SEQUENCE OF 20-710 (ISOFORM 1), AND DISULFIDE BONDS.
PubMed=6510420; DOI=10.1111/j.1432-1033.1984.tb08607.x;
Metz-Boutigue M.-H., Jolles J., Mazurier J., Schoentgen F.,
Legrand D., Spik G., Montreuil J., Jolles P.;
"Human lactotransferrin: amino acid sequence and structural
comparisons with other transferrins.";
Eur. J. Biochem. 145:659-676(1984).
[19]
PRELIMINARY PROTEIN SEQUENCE OF 20-72; 133-170; 256-277; 359-528 AND
608-663 (ISOFORM 1).
PubMed=6794640; DOI=10.1016/0005-2795(81)90016-7;
Metz-Boutigue M.-H., Mazurier J., Jolles J., Spik G., Montreuil J.,
Jolles P.;
"The present state of the human lactotransferrin sequence. Study and
alignment of the cyanogen bromide fragments and characterization of
N- and C-terminal domains.";
Biochim. Biophys. Acta 670:243-254(1981).
[20]
PROTEIN SEQUENCE OF 20-65 (ISOFORM 1), IDENTIFICATION OF LACTOFERRICIN
PEPTIDE, FUNCTION, AND SYNTHESIS OF 36-58.
TISSUE=Milk;
PubMed=1599934; DOI=10.1016/0167-4838(92)90346-F;
Bellamy W., Takase M., Yamauchi K., Wakabayashi H., Kawase K.,
Tomita M.;
"Identification of the bactericidal domain of lactoferrin.";
Biochim. Biophys. Acta 1121:130-136(1992).
[21]
PROTEIN SEQUENCE OF 20-40 (ISOFORM 1), FUNCTION, GLYCOSAMINOGLYCAN
BINDING, AND SYNTHESIS OF 20-51; 20-45 AND 25-51.
TISSUE=Milk;
PubMed=8089135;
Mann D.M., Romm E., Migliorini M.;
"Delineation of the glycosaminoglycan-binding site in the human
inflammatory response protein lactoferrin.";
J. Biol. Chem. 269:23661-23667(1994).
[22]
PROTEIN SEQUENCE OF 20-56 (ISOFORM 1).
TISSUE=Seminal plasma;
PubMed=8551695;
Sato I.;
"Characterization of the 84-kDa protein with ABH activity in human
seminal plasma.";
Nihon Hoigaku Zasshi 49:281-293(1995).
[23]
PROTEIN SEQUENCE OF 24-32; 38-43; 50-57 AND 59-67 (ISOFORM 1),
STRUCTURE BY NMR OF 20-67 (LACTOFERRICIN), MASS SPECTROMETRY, AND
DISULFIDE BONDS.
TISSUE=Milk;
PubMed=16048952; DOI=10.1128/AAC.49.8.3387-3395.2005;
Hunter H.N., Demcoe A.R., Jenssen H., Gutteberg T.J., Vogel H.J.;
"Human lactoferricin is partially folded in aqueous solution and is
better stabilized in a membrane mimetic solvent.";
Antimicrob. Agents Chemother. 49:3387-3395(2005).
[24]
PROTEIN SEQUENCE OF 38-57; 235-261; 509-525 AND 651-710, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Tear;
PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179;
Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I.,
Suarez T., Elortza F.;
"Human basal tear peptidome characterization by CID, HCD, and ETD
followed by in silico and in vitro analyses for antimicrobial peptide
identification.";
J. Proteome Res. 14:2649-2658(2015).
[25]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-710, AND VARIANT ASP-579.
McCombie W.R., Wilson R., Chen E., Gibbs R., Zuo L., Johnson D.,
Nhan M., Parnell L., Dedhia N., Ansari A., Mardis E., Schutz K.,
Gnoj L., la Bastide M., Kaplan N., Greco T., Touchman J., Muzny D.,
Chen C.N., Evans C., Fitzgerald M., See L.H., Tang M., Porcel B.M.,
Dragan Y., Giacalone J., Pae A., Powell E., Solinsky K.A., Desilva U.,
Diaz-Perez S., Zhou X., Yu Y., Watanabe M., Doggett N., Garcia D.,
Sagripanti J.L.;
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[26]
NUCLEOTIDE SEQUENCE [MRNA] OF 435-710.
TISSUE=Myeloid;
PubMed=3477300;
Rado T.A., Wei X., Benz E.J. Jr.;
"Isolation of lactoferrin cDNA from a human myeloid library and
expression of mRNA during normal and leukemic myelopoiesis.";
Blood 70:989-993(1987).
[27]
PROTEIN SEQUENCE OF 608-710.
PubMed=7049727; DOI=10.1016/0014-5793(82)80229-9;
Metz-Boutigue M.-H., Jolles J., Mazurier J., Spik G., Montreuil J.,
Jolles P.;
"An 88 amino acid long C-terminal sequence of human
lactotransferrin.";
FEBS Lett. 142:107-110(1982).
[28]
FUNCTION.
PubMed=6802759;
Arnold R.R., Russell J.E., Champion W.J., Brewer M., Gauthier J.J.;
"Bactericidal activity of human lactoferrin: differentiation from the
stasis of iron deprivation.";
Infect. Immun. 35:792-799(1982).
[29]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=2981589;
Cramer E., Pryzwansky K.B., Villeval J.L., Testa U., Breton-Gorius J.;
"Ultrastructural localization of lactoferrin and myeloperoxidase in
human neutrophils by immunogold.";
Blood 65:423-432(1985).
[30]
FUNCTION.
PubMed=3169987;
Ellison R.T. III, Giehl T.J., LaForce F.M.;
"Damage of the outer membrane of enteric gram-negative bacteria by
lactoferrin and transferrin.";
Infect. Immun. 56:2774-2781(1988).
[31]
CHARACTERIZATION OF LACTOFERROXINS.
PubMed=1369293; DOI=10.1271/bbb1961.54.1803;
Tani F., Iio K., Chiba H., Yoshikawa M.;
"Isolation and characterization of opioid antagonist peptides derived
from human lactoferrin.";
Agric. Biol. Chem. 54:1803-1810(1990).
[32]
FUNCTION, AND MUTAGENESIS OF 20-G--R-23.
PubMed=9359845;
van Berkel P.H., Geerts M.E., van Veen H.A., Mericskay M.,
de Boer H.A., Nuijens J.H.;
"N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is
essential for binding to heparin, bacterial lipopolysaccharide, human
lysozyme and DNA.";
Biochem. J. 328:145-151(1997).
[33]
FUNCTION.
PubMed=11083624; DOI=10.1128/AAC.44.12.3257-3263.2000;
Lupetti A., Paulusma-Annema A., Welling M.M., Senesi S.,
van Dissel J.T., Nibbering P.H.;
"Candidacidal activities of human lactoferrin peptides derived from
the N terminus.";
Antimicrob. Agents Chemother. 44:3257-3263(2000).
[34]
TISSUE SPECIFICITY.
PubMed=10792619; DOI=10.1046/j.1523-1755.2000.00050.x;
Abrink M., Larsson E., Gobl A., Hellman L.;
"Expression of lactoferrin in the kidney: implications for innate
immunity and iron metabolism.";
Kidney Int. 57:2004-2010(2000).
[35]
FUNCTION, SYNTHESIS OF 20-29 AND 39-49, AND MUTAGENESIS OF
20-GLY--ARG-22.
PubMed=11179314; DOI=10.1128/IAI.69.3.1469-1476.2001;
Nibbering P.H., Ravensbergen E., Welling M.M., van Berkel L.A.,
van Berkel P.H., Pauwels E.K., Nuijens J.H.;
"Human lactoferrin and peptides derived from its N terminus are highly
effective against infections with antibiotic-resistant bacteria.";
Infect. Immun. 69:1469-1476(2001).
[36]
FUNCTION.
PubMed=12037568; DOI=10.1038/417552a;
Singh P.K., Parsek M.R., Greenberg E.P., Welsh M.J.;
"A component of innate immunity prevents bacterial biofilm
development.";
Nature 417:552-555(2002).
[37]
SUBCELLULAR LOCATION, AND ALTERNATIVE PROMOTER USAGE.
PubMed=12565886; DOI=10.1016/S0006-291X(02)03077-2;
Liu D., Wang X., Zhang Z., Teng C.T.;
"An intronic alternative promoter of the human lactoferrin gene is
activated by Ets.";
Biochem. Biophys. Res. Commun. 301:472-479(2003).
[38]
FUNCTION, AND SYNTHESIS OF 36-58 AND 171-201 (KALIOCIN-1).
PubMed=12693969; DOI=10.1023/A:1022657630698;
Viejo-Diaz M., Andres M.T., Perez-Gil J., Sanchez M., Fierro J.F.;
"Potassium efflux induced by a new lactoferrin-derived peptide
mimicking the effect of native human lactoferrin on the bacterial
cytoplasmic membrane.";
Biochemistry (Mosc.) 68:217-227(2003).
[39]
FUNCTION AS A PROTEASE, AND MUTAGENESIS OF LYS-92; PRO-270 AND
SER-278.
PubMed=12535064; DOI=10.1046/j.1365-2958.2003.03327.x;
Hendrixson D.R., Qiu J., Shewry S.C., Fink D.L., Petty S., Baker E.N.,
Plaut A.G., St Geme J.W. III;
"Human milk lactoferrin is a serine protease that cleaves Haemophilus
surface proteins at arginine-rich sites.";
Mol. Microbiol. 47:607-617(2003).
[40]
FUNCTION, AND SUBCELLULAR LOCATION (DELTALF).
PubMed=15222485; DOI=10.1023/B:BIOM.0000027712.81056.13;
Breton M., Mariller C., Benaissa M., Caillaux K., Browaeys E.,
Masson M., Vilain J.P., Mazurier J., Pierce A.;
"Expression of delta-lactoferrin induces cell cycle arrest.";
BioMetals 17:325-329(2004).
[41]
FUNCTION.
PubMed=15166119; DOI=10.1210/en.2003-1307;
Cornish J., Callon K.E., Naot D., Palmano K.P., Banovic T., Bava U.,
Watson M., Lin J.M., Tong P.C., Chen Q., Chan V.A., Reid H.E.,
Fazzalari N., Baker H.M., Baker E.N., Haggarty N.W., Grey A.B.,
Reid I.R.;
"Lactoferrin is a potent regulator of bone cell activity and increases
bone formation in vivo.";
Endocrinology 145:4366-4374(2004).
[42]
FUNCTION.
PubMed=16842782; DOI=10.1016/j.febslet.2006.06.091;
Kim C.W., Son K.N., Choi S.Y., Kim J.;
"Human lactoferrin upregulates expression of KDR/Flk-1 and stimulates
VEGF-A-mediated endothelial cell proliferation and migration.";
FEBS Lett. 580:4332-4336(2006).
[43]
FUNCTION.
PubMed=17481742; DOI=10.1016/j.antiviral.2007.03.012;
Mistry N., Drobni P., Naslund J., Sunkari V.G., Jenssen H.,
Evander M.;
"The anti-papillomavirus activity of human and bovine lactoferricin.";
Antiviral Res. 75:258-265(2007).
[44]
IDENTIFICATION IN A COMPLEX WITH CLU; SEMG1 AND EPPIN.
PubMed=17567961; DOI=10.1095/biolreprod.107.060194;
Wang Z., Widgren E.E., Richardson R.T., O'Rand M.G.;
"Characterization of an eppin protein complex from human semen and
spermatozoa.";
Biol. Reprod. 77:476-484(2007).
[45]
FUNCTION.
PubMed=17079302; DOI=10.1128/JVI.01995-06;
Johansson C., Jonsson M., Marttila M., Persson D., Fan X.L., Skog J.,
Frangsmyr L., Wadell G., Arnberg N.;
"Adenoviruses use lactoferrin as a bridge for CAR-independent binding
to and infection of epithelial cells.";
J. Virol. 81:954-963(2007).
[46]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156; ASN-497 AND ASN-642.
TISSUE=Milk;
PubMed=18780401; DOI=10.1002/pmic.200701057;
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
"Identification of N-linked glycoproteins in human milk by hydrophilic
interaction liquid chromatography and mass spectrometry.";
Proteomics 8:3833-3847(2008).
[47]
FUNCTION.
PubMed=19033648; DOI=10.1172/JCI36226;
Bournazou I., Pound J.D., Duffin R., Bournazos S., Melville L.A.,
Brown S.B., Rossi A.G., Gregory C.D.;
"Apoptotic human cells inhibit migration of granulocytes via release
of lactoferrin.";
J. Clin. Invest. 119:20-32(2009).
[48]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-497.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[49]
FUNCTION, AND PTM.
PubMed=20345905; DOI=10.1111/j.1742-4658.2010.07620.x;
Ando K., Hasegawa K., Shindo K., Furusawa T., Fujino T., Kikugawa K.,
Nakano H., Takeuchi O., Akira S., Akiyama T., Gohda J., Inoue J.,
Hayakawa M.;
"Human lactoferrin activates NF-kappaB through the Toll-like receptor
4 pathway while it interferes with the lipopolysaccharide-stimulated
TLR4 signaling.";
FEBS J. 277:2051-2066(2010).
[50]
GLYCOSYLATION AT SER-10 (ISOFORM DELTALF), PHOSPHORYLATION AT SER-10
(ISOFORM DELTALF), AND UBIQUITINATION AT LYS-379 AND LYS-391 (ISOFORM
DELTALF).
PubMed=20404350; DOI=10.1074/jbc.M109.080572;
Hardiville S., Hoedt E., Mariller C., Benaissa M., Pierce A.;
"O-GlcNAcylation/phosphorylation cycling at Ser10 controls both
transcriptional activity and stability of delta-lactoferrin.";
J. Biol. Chem. 285:19205-19218(2010).
[51]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[52]
FUNCTION AS A TRANSCRIPTION FACTOR (ISOFORM DELTALF), AND DNA-BINDING
(ISOFORM DELTALF).
PubMed=22320386; DOI=10.1139/o11-070;
Mariller C., Hardiville S., Hoedt E., Huvent I., Pina-Canseco S.,
Pierce A.;
"Delta-lactoferrin, an intracellular lactoferrin isoform that acts as
a transcription factor.";
Biochem. Cell Biol. 90:307-319(2012).
[53]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[54]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SEQUENCE REVISION.
PubMed=2585506; DOI=10.1016/0022-2836(89)90602-5;
Anderson B.F., Baker H.M., Norris G.E., Rice D.W., Baker E.N.;
"Structure of human lactoferrin: crystallographic structure analysis
and refinement at 2.8-A resolution.";
J. Mol. Biol. 209:711-734(1989).
[55]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 20-710.
PubMed=1772635; DOI=10.1107/S0108768191008418;
Norris G.E., Anderson B.F., Baker E.N.;
"Molecular replacement solution of the structure of apolactoferrin, a
protein displaying large-scale conformational change.";
Acta Crystallogr. B 47:998-1004(1991).
[56]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 20-710 IN COMPLEX WITH
COPPER AND CARBONATE, AND GLYCOSYLATION AT ASN-156 AND ASN-497.
PubMed=1581307; DOI=10.1021/bi00133a020;
Smith C.A., Anderson B.F., Baker H.M., Baker E.N.;
"Metal substitution in transferrins: the crystal structure of human
copper-lactoferrin at 2.1-A resolution.";
Biochemistry 31:4527-4533(1992).
[57]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 21-352 IN COMPLEX WITH IRON
AND CARBONATE, AND DISULFIDE BONDS.
PubMed=8371268; DOI=10.1006/jmbi.1993.1462;
Day C.L., Anderson B.F., Tweedie J.W., Baker E.N.;
"Structure of the recombinant N-terminal lobe of human lactoferrin at
2.0 A resolution.";
J. Mol. Biol. 232:1084-1100(1993).
[58]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 20-710 IN COMPLEX WITH
COPPER AND OXALATE, AND GLYCOSYLATION AT ASN-156.
PubMed=15299444; DOI=10.1107/S0907444994000491;
Smith C.A., Anderson B.F., Baker H.M., Baker E.N.;
"Structure of copper- and oxalate-substituted human lactoferrin at 2.0
A resolution.";
Acta Crystallogr. D 50:302-316(1994).
[59]
X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 110-268, AND GLYCOSYLATION
AT ASN-156.
PubMed=8069634; DOI=10.1016/S0969-2126(00)00022-8;
Bourne Y., Mazurier J., Legrand D., Rouge P., Montreuil J., Spik G.,
Cambillau C.;
"Structures of a legume lectin complexed with the human
lactotransferrin N2 fragment, and with an isolated biantennary
glycopeptide: role of the fucose moiety.";
Structure 2:209-219(1994).
[60]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 20-710 IN COMPLEX WITH IRON
AND CARBONATE, AND GLYCOSYLATION AT ASN-156 AND ASN-497.
PubMed=15299793; DOI=10.1107/S0907444994013521;
Haridas M., Anderson B.F., Baker E.N.;
"Structure of human diferric lactoferrin refined at 2.2-A
resolution.";
Acta Crystallogr. D 51:629-646(1995).
[61]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 20-710 IN COMPLEX WITH IRON
AND OXALATE.
PubMed=8703903; DOI=10.1021/bi960288y;
Baker H.M., Anderson B.F., Brodie A.M., Shongwe M.S., Smith C.A.,
Baker E.N.;
"Anion binding by transferrins: importance of second-shell effects
revealed by the crystal structure of oxalate-substituted diferric
lactoferrin.";
Biochemistry 35:9007-9013(1996).
[62]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 22-352 OF MUTANTS GLU-140
AND SER-140 IN COMPLEX WITH IRON AND CARBONATE, AND MUTAGENESIS OF
ARG-140.
PubMed=8931543; DOI=10.1021/bi961729g;
Faber H.R., Baker C.J., Day C.L., Tweedie J.W., Baker E.N.;
"Mutation of arginine 121 in lactoferrin destabilizes iron binding by
disruption of anion binding: crystal structures of R121S and R121E
mutants.";
Biochemistry 35:14473-14479(1996).
[63]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 21-352 OF MUTANT SER-79 IN
COMPLEX WITH IRON AND CARBONATE, AND MUTAGENESIS OF ASP-79.
PubMed=8594202; DOI=10.1006/jmbi.1996.0091;
Faber H.R., Bland T., Day C.L., Norris G.E., Tweedie J.W., Baker E.N.;
"Altered domain closure and iron binding in transferrins: the crystal
structure of the Asp60Ser mutant of the amino-terminal half-molecule
of human lactoferrin.";
J. Mol. Biol. 256:352-363(1996).
[64]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-353 OF MUTANT MET-272 IN
COMPLEX WITH IRON AND CARBONATE, AND MUTAGENESIS OF HIS-272.
PubMed=9003186; DOI=10.1021/bi961908y;
Nicholson H., Anderson B.F., Bland T., Shewry S.C., Tweedie J.W.,
Baker E.N.;
"Mutagenesis of the histidine ligand in human lactoferrin: iron
binding properties and crystal structure of the histidine-
253-->methionine mutant.";
Biochemistry 36:341-346(1997).
[65]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 20-710.
PubMed=10089508; DOI=10.1107/S0907444998004417;
Jameson G.B., Anderson B.F., Norris G.E., Thomas D.H., Baker E.N.;
"Structure of human apolactoferrin at 2.0 A resolution. Refinement and
analysis of ligand-induced conformational change.";
Acta Crystallogr. D 54:1319-1335(1998).
[66]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) 20-710 IN COMPLEX WITH IRON AND
CARBONATE.
PubMed=10089347; DOI=10.1107/S0907444998011226;
Sun X.L., Baker H.M., Shewry S.C., Jameson G.B., Baker E.N.;
"Structure of recombinant human lactoferrin expressed in Aspergillus
awamori.";
Acta Crystallogr. D 55:403-407(1999).
[67]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 21-348 OF MUTANT LYS-229 IN
COMPLEX WITH IRON AND CARBONATE, AND MUTAGENESIS OF ARG-229.
PubMed=10828980; DOI=10.1021/bi0001224;
Peterson N.A., Anderson B.F., Jameson G.B., Tweedie J.W., Baker E.N.;
"Crystal structure and iron-binding properties of the R210K mutant of
the N-lobe of human lactoferrin: implications for iron release from
transferrins.";
Biochemistry 39:6625-6633(2000).
[68]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 21-710 IN COMPLEX WITH
CERIUM AND CARBONATE.
PubMed=11128996; DOI=10.1007/s007750000157;
Baker H.M., Baker C.J., Smith C.A., Baker E.N.;
"Metal substitution in transferrins: specific binding of cerium(IV)
revealed by the crystal structure of cerium-substituted human
lactoferrin.";
J. Biol. Inorg. Chem. 5:692-698(2000).
[69]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 21-351 OF MUTANT ASP-140,
AND MUTAGENESIS OF ARG-140.
PubMed=12037297; DOI=10.1107/S0907444902005127;
Jameson G.B., Anderson B.F., Breyer W.A., Day C.L., Tweedie J.W.,
Baker E.N.;
"Structure of a domain-opened mutant (R121D) of the human lactoferrin
N-lobe refined from a merohedrally twinned crystal form.";
Acta Crystallogr. D 58:955-962(2002).
[70]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 21-352 OF MUTANTS GLY-229;
GLU-229 AND LEU-229 IN COMPLEX WITH IRON AND CARBONATE, AND
MUTAGENESIS OF ARG-229.
PubMed=12450380; DOI=10.1021/bi020443a;
Peterson N.A., Arcus V.L., Anderson B.F., Tweedie J.W., Jameson G.B.,
Baker E.N.;
"'Dilysine trigger' in transferrins probed by mutagenesis of
lactoferrin: crystal structures of the R210G, R210E, and R210L mutants
of human lactoferrin.";
Biochemistry 41:14167-14175(2002).
[71]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 20-710 IN COMPLEX WITH IRON
AND CARBONATE, AND GLYCOSYLATION AT ASN-156 AND ASN-497.
Vikram P., Prem Kumar R., Singh N., Kumar J., Ethayathulla A.S.,
Sharma S., Kaur P., Singh T.P.;
"Structure of human diferric lactoferrin at 2.5A resolution using
crystals grown at pH 6.5.";
Submitted (MAR-2004) to the PDB data bank.
[72]
STRUCTURE BY NMR OF 39-49 IN COMPLEX WITH LIPOPOLYSACCHARIDE, AND
SYNTHESIS OF 39-49.
PubMed=15687491; DOI=10.1074/jbc.M500266200;
Japelj B., Pristovsek P., Majerle A., Jerala R.;
"Structural origin of endotoxin neutralization and antimicrobial
activity of a lactoferrin-based peptide.";
J. Biol. Chem. 280:16955-16961(2005).
[73]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 20-710 IN COMPLEX WITH IRON
AND CARBONATE, GLYCOSYLATION AT ASN-156 AND ASN-497, AND VARIANT
ASP-579.
PubMed=16201406; DOI=10.1007/s11248-005-3233-0;
Thomassen E.A., van Veen H.A., van Berkel P.H., Nuijens J.H.,
Abrahams J.P.;
"The protein structure of recombinant human lactoferrin produced in
the milk of transgenic cows closely matches the structure of human
milk-derived lactoferrin.";
Transgenic Res. 14:397-405(2005).
[74]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 528-535 IN COMPLEX WITH
PROTEINASE K.
Singh A.K., Singh N., Sharma S., Bhushan A., Singh T.P.;
"Crystal structure of the complex formed between proteinase K and a
human lactoferrin fragment at 2.9 A resolution.";
Submitted (MAY-2006) to the PDB data bank.
[75]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 528-535 IN COMPLEX WITH
PROTEINASE K.
Prem Kumar R., Singh A.K., Singh N., Kaur P., Sharma S., Singh T.P.;
"Crystal structure of proteinase K inhibited by a lactoferrin
octapeptide Gly-Asp-Glu-Gln-Gly-Glu-Asn-Lys at 2.15 A resolution.";
Submitted (JUN-2006) to the PDB data bank.
[76]
STRUCTURE BY NMR OF 39-49.
PubMed=17263370; DOI=10.1021/ja067419v;
Japelj B., Zorko M., Majerle A., Pristovsek P., Sanchez-Gomez S.,
Martinez de Tejada G., Moriyon I., Blondelle S.E., Brandenburg K.,
Andra J., Lohner K., Jerala R.;
"The acyl group as the central element of the structural organization
of antimicrobial lipopeptide.";
J. Am. Chem. Soc. 129:1022-1023(2007).
[77]
X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 21-362 IN COMPLEX WITH
PNEUMOCOCCAL SURFACE PROTEIN A FRAGMENT; IRON AND CARBONATE.
PubMed=17543335; DOI=10.1016/j.jmb.2007.04.075;
Senkovich O., Cook W.J., Mirza S., Hollingshead S.K.,
Protasevich I.I., Briles D.E., Chattopadhyay D.;
"Structure of a complex of human lactoferrin N-lobe with pneumococcal
surface protein a provides insight into microbial defense mechanism.";
J. Mol. Biol. 370:701-713(2007).
[78]
VARIANTS THR-29 AND ARG-47.
PubMed=9873069;
Klintworth G.K., Sommer J.R., Obrian G., Han L., Ahmed M.N.,
Qumsiyeh M.B., Lin P.-Y., Basti S., Reddy M.K., Kanai A., Hotta Y.,
Sugar J., Kumaramanickavel G., Munier F., Schorderet D.F.,
El Matri L., Iwata F., Kaiser-Kupfer M., Nagata M., Nakayasu K.,
Hejtmancik J.F., Teng C.T.;
"Familial subepithelial corneal amyloidosis (gelatinous drop-like
corneal dystrophy): exclusion of linkage to lactoferrin gene.";
Mol. Vis. 4:31-32(1998).
[79]
VARIANTS ARG-22 INS AND ARG-47.
PubMed=22406253; DOI=10.1016/j.humimm.2012.02.014;
Videm V., Dahl H., Walberg L.E., Wiseth R.;
"Functional polymorphisms in the LTF gene and risk of coronary artery
stenosis.";
Hum. Immunol. 73:554-559(2012).
-!- FUNCTION: Transferrins are iron binding transport proteins which
can bind two Fe(3+) ions in association with the binding of an
anion, usually bicarbonate.
-!- FUNCTION: Lactotransferrin is a major iron-binding and
multifunctional protein found in exocrine fluids such as breast
milk and mucosal secretions. Has antimicrobial activity, which
depends on the extracellular cation concentration. Antimicrobial
properties include bacteriostasis, which is related to its ability
to sequester free iron and thus inhibit microbial growth, as well
as direct bactericidal properties leading to the release of
lipopolysaccharides from the bacterial outer membrane. Can also
prevent bacterial biofilm development in P.aeruginosa infection.
Has weak antifungal activity against C.albicans. Has anabolic,
differentiating and anti-apoptotic effects on osteoblasts and can
also inhibit osteoclastogenesis, possibly playing a role in the
regulation of bone growth. Promotes binding of species C
adenoviruses to epithelial cells, promoting adenovirus infection.
Can inhibit papillomavirus infections. Stimulates the TLR4
signaling pathway leading to NF-kappa-B activation and subsequent
pro-inflammatory cytokine production while also interfering with
the lipopolysaccharide (LPS)-stimulated TLR4 signaling. Inhibits
neutrophil granulocyte migration to sites of apoptosis, when
secreted by apoptotic cells. Stimulates VEGFA-mediated endothelial
cell migration and proliferation. Binds heparin, chondroitin
sulfate and possibly other glycosaminoglycans (GAGs). Also binds
specifically to pneumococcal surface protein A (pspA), the lipid A
portion of bacterial lipopolysaccharide (LPS), lysozyme and DNA.
-!- FUNCTION: Lactoferricin binds to the bacterial surface and is
crucial for the bactericidal functions. Has some antiviral
activity against papillomavirus infection. N-terminal region shows
strong antifungal activity against C.albicans. Contains two BBXB
heparin-binding consensus sequences that appear to form the
predominate functional GAG-binding site.
-!- FUNCTION: Kaliocin-1 has antimicrobial activity and is able to
permeabilize different ions through liposomal membranes.
-!- FUNCTION: Lactoferroxins A, B and C have opioid antagonist
activity. Lactoferroxin A shows preference for mu-receptors, while
lactoferroxin B and C have somewhat higher degrees of preference
for kappa-receptors than for mu-receptors.
-!- FUNCTION: The lactotransferrin transferrin-like domain 1 functions
as a serine protease of the peptidase S60 family that cuts
arginine rich regions. This function contributes to the
antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-
Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-
aminomethylcoumarin sites.
-!- FUNCTION: Isoform DeltaLf: transcription factor with
antiproliferative properties and ability to induce cell cycle
arrest. Binds to the DeltaLf response element found in the SKP1,
BAX, DCPS, and SELENOH promoters.
-!- SUBUNIT: Monomer. Found in a complex with LTF, CLU, EPPIN and
SEMG1. {ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:11128996, ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299444, ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:15687491, ECO:0000269|PubMed:1581307,
ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:17567961, ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8703903, ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186, ECO:0000269|Ref.71,
ECO:0000269|Ref.74, ECO:0000269|Ref.75}.
-!- INTERACTION:
P27958:- (xeno); NbExp=3; IntAct=EBI-1058602, EBI-6904259;
P62157:CALM (xeno); NbExp=2; IntAct=EBI-1058602, EBI-397403;
P75358:gapA (xeno); NbExp=3; IntAct=EBI-1058602, EBI-2259469;
P75390:pdhA (xeno); NbExp=3; IntAct=EBI-1058602, EBI-2259629;
P75391:pdhB (xeno); NbExp=3; IntAct=EBI-1058602, EBI-2259621;
P75392:pdhC (xeno); NbExp=3; IntAct=EBI-1058602, EBI-2259593;
P78031:pyk (xeno); NbExp=3; IntAct=EBI-1058602, EBI-2259473;
-!- SUBCELLULAR LOCATION: Isoform 1: Secreted. Cytoplasmic granule.
Note=Secreted into most exocrine fluids by various endothelial
cells. Stored in the secondary granules of neutrophils.
-!- SUBCELLULAR LOCATION: Isoform DeltaLf: Cytoplasm. Nucleus.
Note=Mainly localized in the cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=1;
IsoId=P02788-1; Sequence=Displayed;
Name=DeltaLf; Synonyms=Delta-lactoferrin;
IsoId=P02788-2; Sequence=VSP_044308;
Note=Contains a phosphoserine at position 10 (alternate).
Contains a O-linked (GlcNAc) serine at position 10 (alternate).
O-GlcNAcylation at Ser-10 inhibits DNA binding and negatively
regulates DeltaLf transcriptional activity, whereas
phosphorylation activates it. Phosphorylation at Ser-10 also
promotes proteasomal degradation. Contains a glycyl lysine
isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) at
position 379. Contains a glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin) at position 391.
{ECO:0000269|PubMed:20404350};
-!- TISSUE SPECIFICITY: High levels are found in saliva and tears,
intermediate levels in serum and plasma, and low levels in urine.
In kidney, detected in the distal collecting tubules in the
medulla but not in the cortical region or in blood vessels.
Detected in peripheral blood neutrophils (at protein level).
Isoform 1 and isoform DeltaLf are expressed in breast, prostate,
spleen, pancreas, kidney, small intestine, lung, skeletal muscle,
uterus, thymus and fetal liver. Isoform 1 is expressed in brain,
testis and peripheral blood leukocytes; isoform DeltaLf is barely
detectable in these tissues. Isoform DeltaLf is expressed in
placenta, liver and ovary; isoform 1 is barely detectable in these
tissues. In kidney, isoform 1 is expressed at high levels in the
collecting tubules of the medulla but at very low levels in the
cortex. {ECO:0000269|PubMed:10792619, ECO:0000269|PubMed:2981589,
ECO:0000269|PubMed:9122171}.
-!- PTM: Isoform DeltaLf: Ubiquitinated at Lys-379 and Lys-391.
-!- PTM: Poly-N-acetyllactosaminic carbohydrate moiety seems to be
needed for TLR4 activation.
-!- MASS SPECTROMETRY: Mass=5737.8; Method=Electrospray; Range=20-67;
Evidence={ECO:0000269|PubMed:16048952};
-!- POLYMORPHISM: The sequence shown corresponds to the reference
genome sequence and is likely to represent the minor allele,
whereas most publications refer to the longer sequence containing
variant Arg-22 ins. Insertion of the additional arginine in
variant Arg-22 ins creates an N-terminal basic cluster of four
arginines, all of which appear to be important for the full
functionality of the protein, including bactericidal and
antifungal activities as well as binding to glycosaminoglycans,
pspA, LPS, lysozyme and DNA.
-!- SIMILARITY: Belongs to the transferrin family.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Lactotransferrin entry;
URL="https://en.wikipedia.org/wiki/Lactotransferrin";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X53961; CAA37914.1; -; mRNA.
EMBL; U07643; AAB60324.1; -; mRNA.
EMBL; AF332168; AAG48753.1; -; mRNA.
EMBL; AY178998; AAN75578.2; -; mRNA.
EMBL; AY137470; AAN11304.1; -; mRNA.
EMBL; M73700; AAA59479.1; -; Genomic_DNA.
EMBL; M93150; AAA36159.1; -; mRNA.
EMBL; AY165046; AAN63998.1; -; mRNA.
EMBL; AY493417; AAS72878.1; -; mRNA.
EMBL; EU622050; ACC95966.1; -; Genomic_DNA.
EMBL; AK292813; BAF85502.1; -; mRNA.
EMBL; AK298035; BAH12708.1; -; mRNA.
EMBL; AC098613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015822; AAH15822.1; -; mRNA.
EMBL; BC015823; AAH15823.1; -; mRNA.
EMBL; BC022347; AAH22347.1; -; mRNA.
EMBL; S52659; AAB24877.1; -; Genomic_DNA.
EMBL; X52941; CAA37116.1; -; mRNA.
EMBL; M83202; AAA59511.1; -; mRNA.
EMBL; M83205; AAA58656.1; -; mRNA.
EMBL; U95626; AAB57795.1; -; Genomic_DNA.
EMBL; M18642; AAA86665.1; -; mRNA.
CCDS; CCDS33747.1; -. [P02788-1]
CCDS; CCDS56251.1; -. [P02788-2]
PIR; G01394; TFHUL.
RefSeq; NP_001186078.1; NM_001199149.1. [P02788-2]
RefSeq; NP_001308050.1; NM_001321121.1.
RefSeq; NP_001308051.1; NM_001321122.1.
RefSeq; NP_002334.2; NM_002343.5. [P02788-1]
UniGene; Hs.529517; -.
PDB; 1B0L; X-ray; 2.20 A; A=20-710.
PDB; 1BKA; X-ray; 2.40 A; A=20-710.
PDB; 1CB6; X-ray; 2.00 A; A=20-710.
PDB; 1DSN; X-ray; 2.05 A; A=21-352.
PDB; 1EH3; X-ray; 2.00 A; A=21-352.
PDB; 1FCK; X-ray; 2.20 A; A=21-710.
PDB; 1H43; X-ray; 2.20 A; A=21-352.
PDB; 1H44; X-ray; 2.00 A; A=21-352.
PDB; 1H45; X-ray; 1.95 A; A=21-352.
PDB; 1HSE; X-ray; 2.20 A; A=21-353.
PDB; 1L5T; X-ray; 3.00 A; A/B=21-351.
PDB; 1LCF; X-ray; 2.00 A; A=20-710.
PDB; 1LCT; X-ray; 2.00 A; A=21-352.
PDB; 1LFG; X-ray; 2.20 A; A=20-710.
PDB; 1LFH; X-ray; 2.80 A; A=20-710.
PDB; 1LFI; X-ray; 2.10 A; A=20-710.
PDB; 1LGB; X-ray; 3.30 A; C=110-268.
PDB; 1N76; X-ray; 3.40 A; A=21-710.
PDB; 1SQY; X-ray; 2.50 A; A=20-710.
PDB; 1U62; NMR; -; A=39-44.
PDB; 1VFD; X-ray; 2.50 A; A=20-349.
PDB; 1VFE; X-ray; 2.30 A; A=20-352.
PDB; 1XV4; NMR; -; A=39-44.
PDB; 1XV7; NMR; -; A=39-44.
PDB; 1Z6V; NMR; -; A=21-67.
PDB; 1Z6W; NMR; -; A=21-67.
PDB; 2BJJ; X-ray; 2.40 A; X=21-710.
PDB; 2DP4; X-ray; 2.90 A; I=528-535.
PDB; 2GMC; NMR; -; A=39-44.
PDB; 2GMD; NMR; -; A=39-44.
PDB; 2HD4; X-ray; 2.15 A; B=528-535.
PDB; 2PMS; X-ray; 2.91 A; A/B=21-362.
PDBsum; 1B0L; -.
PDBsum; 1BKA; -.
PDBsum; 1CB6; -.
PDBsum; 1DSN; -.
PDBsum; 1EH3; -.
PDBsum; 1FCK; -.
PDBsum; 1H43; -.
PDBsum; 1H44; -.
PDBsum; 1H45; -.
PDBsum; 1HSE; -.
PDBsum; 1L5T; -.
PDBsum; 1LCF; -.
PDBsum; 1LCT; -.
PDBsum; 1LFG; -.
PDBsum; 1LFH; -.
PDBsum; 1LFI; -.
PDBsum; 1LGB; -.
PDBsum; 1N76; -.
PDBsum; 1SQY; -.
PDBsum; 1U62; -.
PDBsum; 1VFD; -.
PDBsum; 1VFE; -.
PDBsum; 1XV4; -.
PDBsum; 1XV7; -.
PDBsum; 1Z6V; -.
PDBsum; 1Z6W; -.
PDBsum; 2BJJ; -.
PDBsum; 2DP4; -.
PDBsum; 2GMC; -.
PDBsum; 2GMD; -.
PDBsum; 2HD4; -.
PDBsum; 2PMS; -.
DisProt; DP00616; -.
ProteinModelPortal; P02788; -.
SMR; P02788; -.
BioGrid; 110235; 37.
CORUM; P02788; -.
DIP; DIP-41354N; -.
IntAct; P02788; 17.
MINT; MINT-1511753; -.
STRING; 9606.ENSP00000231751; -.
DrugBank; DB06987; 2-(4-(2-HYDROXY-3-(ISOPROPYLAMINO)PROPOXY)PHENYL)ETHANAMIDE.
DrugBank; DB03485; Alpha-D-Fucose.
DrugBank; DB03017; Lauric Acid.
DrugBank; DB04743; Nimesulide.
DrugBank; DB03040; Nitrilotriacetic Acid.
DrugBank; DB08439; Parecoxib.
Allergome; 1384; Hom s LF.
MEROPS; S60.001; -.
iPTMnet; P02788; -.
PhosphoSitePlus; P02788; -.
UniCarbKB; P02788; -.
BioMuta; LTF; -.
DMDM; 85700158; -.
EPD; P02788; -.
PaxDb; P02788; -.
PeptideAtlas; P02788; -.
PRIDE; P02788; -.
DNASU; 4057; -.
Ensembl; ENST00000231751; ENSP00000231751; ENSG00000012223. [P02788-1]
Ensembl; ENST00000426532; ENSP00000405719; ENSG00000012223. [P02788-2]
GeneID; 4057; -.
KEGG; hsa:4057; -.
UCSC; uc003fzr.4; human. [P02788-1]
CTD; 4057; -.
DisGeNET; 4057; -.
EuPathDB; HostDB:ENSG00000012223.12; -.
GeneCards; LTF; -.
HGNC; HGNC:6720; LTF.
HPA; CAB008646; -.
HPA; CAB016201; -.
HPA; HPA057177; -.
HPA; HPA059976; -.
MIM; 150210; gene.
neXtProt; NX_P02788; -.
OpenTargets; ENSG00000012223; -.
PharmGKB; PA30482; -.
eggNOG; ENOG410IEAI; Eukaryota.
eggNOG; ENOG410XQ36; LUCA.
GeneTree; ENSGT00390000001619; -.
HOVERGEN; HBG000055; -.
InParanoid; P02788; -.
KO; K17283; -.
OMA; LRPFLNW; -.
OrthoDB; EOG091G0242; -.
PhylomeDB; P02788; -.
TreeFam; TF324013; -.
Reactome; R-HSA-1222449; Mtb iron assimilation by chelation.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6799990; Metal sequestration by antimicrobial proteins.
Reactome; R-HSA-6803157; Antimicrobial peptides.
Reactome; R-HSA-977225; Amyloid fiber formation.
SIGNOR; P02788; -.
ChiTaRS; LTF; human.
EvolutionaryTrace; P02788; -.
GeneWiki; Lactoferrin; -.
GenomeRNAi; 4057; -.
PRO; PR:P02788; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000012223; -.
ExpressionAtlas; P02788; baseline and differential.
Genevisible; P02788; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IMP:AgBase.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0044218; C:other organism cell membrane; IMP:UniProtKB.
GO; GO:0097013; C:phagocytic vesicle lumen; TAS:Reactome.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0030141; C:secretory granule; IDA:MGI.
GO; GO:0042581; C:specific granule; IDA:UniProtKB.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:CAFA.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0008201; F:heparin binding; IDA:MGI.
GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
GO; GO:0019732; P:antifungal humoral response; IDA:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IMP:UniProtKB.
GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
GO; GO:0060349; P:bone morphogenesis; IDA:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
GO; GO:0002227; P:innate immune response in mucosa; IDA:UniProtKB.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
GO; GO:0033214; P:iron assimilation by chelation and transport; TAS:Reactome.
GO; GO:0031640; P:killing of cells of other organism; IDA:UniProtKB.
GO; GO:0051673; P:membrane disruption in other organism; IMP:UniProtKB.
GO; GO:0044793; P:negative regulation by host of viral process; IMP:AgBase.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0032780; P:negative regulation of ATPase activity; IMP:AgBase.
GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IDA:CAFA.
GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0045837; P:negative regulation of membrane potential; IMP:UniProtKB.
GO; GO:2001205; P:negative regulation of osteoclast development; ISS:UniProtKB.
GO; GO:1900229; P:negative regulation of single-species biofilm formation in or on host organism; IDA:UniProtKB.
GO; GO:2000308; P:negative regulation of tumor necrosis factor (ligand) superfamily member 11 production; ISS:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IMP:AgBase.
GO; GO:0048525; P:negative regulation of viral process; IMP:AgBase.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
GO; GO:1900159; P:positive regulation of bone mineralization involved in bone maturation; ISS:UniProtKB.
GO; GO:1902732; P:positive regulation of chondrocyte proliferation; IDA:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:UniProtKB.
GO; GO:0033690; P:positive regulation of osteoblast proliferation; IDA:UniProtKB.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; IMP:UniProtKB.
GO; GO:0001817; P:regulation of cytokine production; IDA:UniProtKB.
GO; GO:0032680; P:regulation of tumor necrosis factor production; IDA:UniProtKB.
GO; GO:0001895; P:retina homeostasis; IEP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR030684; Lactotransferrin.
InterPro; IPR016357; Transferrin.
InterPro; IPR001156; Transferrin-like_dom.
InterPro; IPR018195; Transferrin_Fe_BS.
PANTHER; PTHR11485:SF33; PTHR11485:SF33; 1.
Pfam; PF00405; Transferrin; 2.
PIRSF; PIRSF500683; Lactotransferrin; 1.
PIRSF; PIRSF002549; Transferrin; 1.
PRINTS; PR00422; TRANSFERRIN.
SMART; SM00094; TR_FER; 2.
PROSITE; PS00205; TRANSFERRIN_LIKE_1; 2.
PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
1: Evidence at protein level;
3D-structure; Alternative promoter usage; Antibiotic; Antimicrobial;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disulfide bond; DNA-binding; Glycoprotein; Heparin-binding; Hydrolase;
Immunity; Ion transport; Iron; Iron transport; Isopeptide bond;
Metal-binding; Nucleus; Osteogenesis; Polymorphism; Protease;
Reference proteome; Repeat; Secreted; Serine protease; Signal;
Transcription; Transcription regulation; Transport; Ubl conjugation.
SIGNAL 1 19 {ECO:0000269|PubMed:14573629}.
CHAIN 20 710 Lactotransferrin.
/FTId=PRO_0000035732.
PEPTIDE 20 67 Lactoferricin-H.
/FTId=PRO_0000422770.
PEPTIDE 171 201 Kaliocin-1.
/FTId=PRO_0000035733.
PEPTIDE 338 343 Lactoferroxin-A.
/FTId=PRO_0000035734.
PEPTIDE 543 547 Lactoferroxin-B.
/FTId=PRO_0000035735.
PEPTIDE 680 686 Lactoferroxin-C.
/FTId=PRO_0000035736.
DOMAIN 25 352 Transferrin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
DOMAIN 364 695 Transferrin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
REGION 20 29 Bactericidal and antifungal activity.
REGION 20 24 Critical for glycosaminoglycan, lipid A,
lysozyme and DNA binding.
REGION 21 22 Important for full bactericidal and
antifungal activities.
REGION 39 49 Bactericidal and antifungal activity.
REGION 39 49 Interaction with lipopolysaccharide.
REGION 39 46 Interaction with pspA.
REGION 46 51 Involved in glycosaminoglycan binding.
REGION 57 58 Interaction with pspA.
ACT_SITE 92 92 {ECO:0000305}.
ACT_SITE 278 278 Nucleophile. {ECO:0000305}.
METAL 79 79 Iron or copper 1. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8703903,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
METAL 111 111 Iron or copper 1. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8703903,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
METAL 211 211 Iron or copper 1. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8703903,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
METAL 272 272 Iron or copper 1; via tele nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8703903,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
METAL 414 414 Iron or copper 2. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8703903,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
METAL 454 454 Iron or copper 2. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8703903,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
METAL 547 547 Iron or copper 2. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8703903,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
METAL 616 616 Iron or copper 2; via tele nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8703903,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
BINDING 23 23 PspA.
BINDING 32 32 PspA.
BINDING 136 136 Carbonate or oxalate 1.
{ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:11128996,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:1581307,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
BINDING 140 140 Carbonate or oxalate 1.
{ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:11128996,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:1581307,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
BINDING 142 142 Carbonate or oxalate 1; via amide
nitrogen. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:11128996,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:1581307,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
BINDING 143 143 Carbonate or oxalate 1; via amide
nitrogen. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:11128996,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:1581307,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
BINDING 480 480 Carbonate or oxalate 2.
{ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:11128996,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:1581307,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
BINDING 484 484 Carbonate or oxalate 2.
{ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:11128996,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:1581307,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
BINDING 486 486 Carbonate or oxalate 2; via amide
nitrogen. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:11128996,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:1581307,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
BINDING 487 487 Carbonate or oxalate 2; via amide
nitrogen. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:10089347,
ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:11128996,
ECO:0000269|PubMed:12450380,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:1581307,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:17543335,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:8371268,
ECO:0000269|PubMed:8594202,
ECO:0000269|PubMed:8931543,
ECO:0000269|PubMed:9003186,
ECO:0000269|Ref.71}.
SITE 229 229 Important for iron binding.
CARBOHYD 156 156 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15299444,
ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:1581307,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:18780401,
ECO:0000269|PubMed:8069634,
ECO:0000269|Ref.71}.
CARBOHYD 497 497 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15299793,
ECO:0000269|PubMed:1581307,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:18780401,
ECO:0000269|PubMed:19159218,
ECO:0000269|Ref.71}.
CARBOHYD 642 642 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401}.
DISULFID 28 64
DISULFID 38 55
DISULFID 134 217
DISULFID 176 192
DISULFID 189 200
DISULFID 250 264
DISULFID 367 399
DISULFID 377 390
DISULFID 424 705
DISULFID 446 668
DISULFID 478 553
DISULFID 502 696
DISULFID 512 526
DISULFID 523 536
DISULFID 594 608
DISULFID 646 651
VAR_SEQ 1 44 Missing (in isoform DeltaLf).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:9122171}.
/FTId=VSP_044308.
VARIANT 22 22 R -> RR (associated with lower plasma
lactoferrin concentrations;
dbSNP:rs10662431).
{ECO:0000269|PubMed:11702692,
ECO:0000269|PubMed:14573629,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:22406253,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:2374734,
ECO:0000269|PubMed:2402455,
ECO:0000269|Ref.10, ECO:0000269|Ref.11,
ECO:0000269|Ref.17, ECO:0000269|Ref.2,
ECO:0000269|Ref.8, ECO:0000269|Ref.9}.
/FTId=VAR_069298.
VARIANT 29 29 A -> T (in dbSNP:rs1126477).
{ECO:0000269|PubMed:11702692,
ECO:0000269|PubMed:14573629,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:9873069,
ECO:0000269|Ref.11, ECO:0000269|Ref.8,
ECO:0000269|Ref.9}.
/FTId=VAR_013504.
VARIANT 47 47 K -> R (decreased antibacterial activity
against Gram-positive bacteria; seems to
reduce susceptibility to localized
juvenile periodontitis; associated with
increased plasma lactoferrin
concentrations and possibly with
susceptibility to coronary artery
stenosis; dbSNP:rs1126478).
{ECO:0000269|PubMed:11702692,
ECO:0000269|PubMed:14573629,
ECO:0000269|PubMed:22406253,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:9873069,
ECO:0000269|Ref.11, ECO:0000269|Ref.8,
ECO:0000269|Ref.9}.
/FTId=VAR_013505.
VARIANT 148 148 I -> T (in dbSNP:rs1126479).
{ECO:0000269|PubMed:2402455}.
/FTId=VAR_013506.
VARIANT 422 422 G -> C (in dbSNP:rs1042055).
{ECO:0000269|PubMed:2402455,
ECO:0000269|Ref.10}.
/FTId=VAR_013507.
VARIANT 579 579 E -> D (in dbSNP:rs2073495).
{ECO:0000269|PubMed:11702692,
ECO:0000269|PubMed:16201406,
ECO:0000269|PubMed:22900286,
ECO:0000269|PubMed:25946035,
ECO:0000269|Ref.25, ECO:0000269|Ref.9}.
/FTId=VAR_013508.
MUTAGEN 20 23 Missing: Abolishes binding to heparin,
lipid A, lysozyme and DNA.
{ECO:0000269|PubMed:9359845}.
MUTAGEN 20 22 Missing: Greatly impairs binding to
heparin, lipid A, lysozyme and DNA.
Impairs antibacterial activity.
{ECO:0000269|PubMed:11179314}.
MUTAGEN 20 21 Missing: Impairs binding to heparin,
lipid A, lysozyme and DNA.
MUTAGEN 79 79 D->S: Impairs iron binding and changes
domain closure.
{ECO:0000269|PubMed:8594202}.
MUTAGEN 92 92 K->A: Almost no protease activity.
{ECO:0000269|PubMed:12535064}.
MUTAGEN 140 140 R->D,E,S: Disrupts anion binding site and
destabilizes iron binding.
{ECO:0000269|PubMed:12037297,
ECO:0000269|PubMed:8931543}.
MUTAGEN 229 229 R->G,E: Destabilizes iron binding
slightly. {ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:12450380}.
MUTAGEN 229 229 R->K,L: Destabilizes iron binding
significantly.
{ECO:0000269|PubMed:10828980,
ECO:0000269|PubMed:12450380}.
MUTAGEN 270 270 P->V: No effect.
{ECO:0000269|PubMed:12535064}.
MUTAGEN 272 272 H->A,C,G,E,F,L,M,P,Q,T,Y: Destabilizes
iron binding.
{ECO:0000269|PubMed:9003186}.
MUTAGEN 278 278 S->A: No protease activity.
{ECO:0000269|PubMed:12535064}.
CONFLICT 14 14 L -> P (in Ref. 17; AAA58656).
{ECO:0000305}.
CONFLICT 21 21 R -> S (in Ref. 14; AAH15822/AAH15823).
{ECO:0000305}.
CONFLICT 36 36 T -> D (in Ref. 22; AA sequence).
{ECO:0000305}.
CONFLICT 49 49 R -> C (in Ref. 14; AAH22347).
{ECO:0000305}.
CONFLICT 130 130 G -> C (in Ref. 14; AAH15823).
{ECO:0000305}.
CONFLICT 138 138 L -> R (in Ref. 14; AAH22347).
{ECO:0000305}.
CONFLICT 140 140 Missing (in Ref. 18; AA sequence).
{ECO:0000305}.
CONFLICT 169 169 Missing (in Ref. 18; AA sequence).
{ECO:0000305}.
CONFLICT 409 410 DA -> NASVLMDSEGGFLAR (in Ref. 18; AA
sequence). {ECO:0000305}.
CONFLICT 415 415 G -> E (in Ref. 17; AAA59511).
{ECO:0000305}.
CONFLICT 431 431 A -> G (in Ref. 17; AAA58656).
{ECO:0000305}.
CONFLICT 456 456 A -> T (in Ref. 14; AAH15822/AAH15823).
{ECO:0000305}.
CONFLICT 487 487 G -> A (in Ref. 26; AAA86665).
{ECO:0000305}.
CONFLICT 531 531 Q -> E (in Ref. 18; AA sequence).
{ECO:0000305}.
CONFLICT 537 537 V -> E (in Ref. 14; AAH15822).
{ECO:0000305}.
CONFLICT 694 694 K -> R (in Ref. 18; AA sequence and 27;
AA sequence). {ECO:0000305}.
STRAND 24 31 {ECO:0000244|PDB:1H45}.
HELIX 32 47 {ECO:0000244|PDB:1H45}.
STRAND 50 52 {ECO:0000244|PDB:1Z6W}.
STRAND 53 57 {ECO:0000244|PDB:1H45}.
HELIX 61 69 {ECO:0000244|PDB:1H45}.
STRAND 75 78 {ECO:0000244|PDB:1H45}.
HELIX 80 87 {ECO:0000244|PDB:1H45}.
TURN 89 91 {ECO:0000244|PDB:1H45}.
STRAND 93 102 {ECO:0000244|PDB:1H45}.
STRAND 104 118 {ECO:0000244|PDB:1H45}.
STRAND 119 121 {ECO:0000244|PDB:1LGB}.
HELIX 125 127 {ECO:0000244|PDB:1H45}.
STRAND 132 136 {ECO:0000244|PDB:1H45}.
TURN 141 144 {ECO:0000244|PDB:1H45}.
HELIX 145 151 {ECO:0000244|PDB:1H45}.
HELIX 152 154 {ECO:0000244|PDB:1H45}.
TURN 159 161 {ECO:0000244|PDB:1LCT}.
HELIX 164 171 {ECO:0000244|PDB:1H45}.
STRAND 172 176 {ECO:0000244|PDB:1H45}.
TURN 182 184 {ECO:0000244|PDB:1H45}.
HELIX 186 188 {ECO:0000244|PDB:1H45}.
TURN 189 191 {ECO:0000244|PDB:1H45}.
HELIX 196 198 {ECO:0000244|PDB:1H45}.
STRAND 206 208 {ECO:0000244|PDB:1N76}.
HELIX 210 219 {ECO:0000244|PDB:1H45}.
STRAND 224 229 {ECO:0000244|PDB:1H45}.
HELIX 232 236 {ECO:0000244|PDB:1H45}.
HELIX 240 243 {ECO:0000244|PDB:1H45}.
STRAND 246 250 {ECO:0000244|PDB:1H45}.
TURN 251 253 {ECO:0000244|PDB:1H45}.
STRAND 254 257 {ECO:0000244|PDB:1H45}.
HELIX 258 263 {ECO:0000244|PDB:1H45}.
STRAND 266 270 {ECO:0000244|PDB:1H45}.
STRAND 273 280 {ECO:0000244|PDB:1H45}.
HELIX 283 297 {ECO:0000244|PDB:1H45}.
TURN 299 301 {ECO:0000244|PDB:1H45}.
STRAND 317 319 {ECO:0000244|PDB:1H45}.
STRAND 325 328 {ECO:0000244|PDB:1H45}.
HELIX 335 339 {ECO:0000244|PDB:1H45}.
HELIX 341 348 {ECO:0000244|PDB:1LFI}.
HELIX 349 351 {ECO:0000244|PDB:1LFI}.
HELIX 354 362 {ECO:0000244|PDB:1CB6}.
STRAND 363 370 {ECO:0000244|PDB:1CB6}.
HELIX 371 383 {ECO:0000244|PDB:1CB6}.
TURN 384 386 {ECO:0000244|PDB:1CB6}.
STRAND 387 395 {ECO:0000244|PDB:1CB6}.
HELIX 396 404 {ECO:0000244|PDB:1CB6}.
STRAND 410 413 {ECO:0000244|PDB:1CB6}.
HELIX 415 423 {ECO:0000244|PDB:1CB6}.
STRAND 427 434 {ECO:0000244|PDB:1CB6}.
STRAND 436 439 {ECO:0000244|PDB:1CB6}.
STRAND 440 442 {ECO:0000244|PDB:1B0L}.
HELIX 446 448 {ECO:0000244|PDB:1CB6}.
STRAND 454 463 {ECO:0000244|PDB:1CB6}.
HELIX 469 471 {ECO:0000244|PDB:1CB6}.
STRAND 475 480 {ECO:0000244|PDB:1CB6}.
TURN 485 488 {ECO:0000244|PDB:1CB6}.
HELIX 489 499 {ECO:0000244|PDB:1CB6}.
HELIX 504 506 {ECO:0000244|PDB:1CB6}.
STRAND 508 512 {ECO:0000244|PDB:1CB6}.
STRAND 514 516 {ECO:0000244|PDB:1LFI}.
HELIX 521 523 {ECO:0000244|PDB:1CB6}.
TURN 533 536 {ECO:0000244|PDB:1LFH}.
HELIX 546 555 {ECO:0000244|PDB:1CB6}.
STRAND 560 565 {ECO:0000244|PDB:1CB6}.
HELIX 566 570 {ECO:0000244|PDB:1CB6}.
STRAND 573 576 {ECO:0000244|PDB:1LFI}.
HELIX 580 583 {ECO:0000244|PDB:1CB6}.
HELIX 587 589 {ECO:0000244|PDB:1CB6}.
STRAND 590 593 {ECO:0000244|PDB:1CB6}.
STRAND 599 601 {ECO:0000244|PDB:1CB6}.
HELIX 602 607 {ECO:0000244|PDB:1CB6}.
STRAND 610 613 {ECO:0000244|PDB:1CB6}.
STRAND 617 620 {ECO:0000244|PDB:1CB6}.
HELIX 622 624 {ECO:0000244|PDB:1CB6}.
HELIX 625 639 {ECO:0000244|PDB:1CB6}.
STRAND 640 642 {ECO:0000244|PDB:1N76}.
TURN 646 649 {ECO:0000244|PDB:1CB6}.
STRAND 655 657 {ECO:0000244|PDB:1CB6}.
STRAND 666 670 {ECO:0000244|PDB:1CB6}.
HELIX 678 682 {ECO:0000244|PDB:1CB6}.
HELIX 684 696 {ECO:0000244|PDB:1CB6}.
HELIX 700 709 {ECO:0000244|PDB:1CB6}.
SEQUENCE 710 AA; 78182 MW; 0489CABA6D13C098 CRC64;
MKLVFLVLLF LGALGLCLAG RRRSVQWCAV SQPEATKCFQ WQRNMRKVRG PPVSCIKRDS
PIQCIQAIAE NRADAVTLDG GFIYEAGLAP YKLRPVAAEV YGTERQPRTH YYAVAVVKKG
GSFQLNELQG LKSCHTGLRR TAGWNVPIGT LRPFLNWTGP PEPIEAAVAR FFSASCVPGA
DKGQFPNLCR LCAGTGENKC AFSSQEPYFS YSGAFKCLRD GAGDVAFIRE STVFEDLSDE
AERDEYELLC PDNTRKPVDK FKDCHLARVP SHAVVARSVN GKEDAIWNLL RQAQEKFGKD
KSPKFQLFGS PSGQKDLLFK DSAIGFSRVP PRIDSGLYLG SGYFTAIQNL RKSEEEVAAR
RARVVWCAVG EQELRKCNQW SGLSEGSVTC SSASTTEDCI ALVLKGEADA MSLDGGYVYT
AGKCGLVPVL AENYKSQQSS DPDPNCVDRP VEGYLAVAVV RRSDTSLTWN SVKGKKSCHT
AVDRTAGWNI PMGLLFNQTG SCKFDEYFSQ SCAPGSDPRS NLCALCIGDE QGENKCVPNS
NERYYGYTGA FRCLAENAGD VAFVKDVTVL QNTDGNNNEA WAKDLKLADF ALLCLDGKRK
PVTEARSCHL AMAPNHAVVS RMDKVERLKQ VLLHQQAKFG RNGSDCPDKF CLFQSETKNL
LFNDNTECLA RLHGKTTYEK YLGPQYVAGI TNLKKCSTSP LLEACEFLRK


Related products :

Catalog number Product name Quantity
E0780h ELISA kit Homo sapiens,Human,Lactoferrin,Lactotransferrin,LF,LTF,Talalactoferrin 96T
U0780h CLIA Homo sapiens,Human,Lactoferrin,Lactotransferrin,LF,LTF,Talalactoferrin 96T
E0780h ELISA Homo sapiens,Human,Lactoferrin,Lactotransferrin,LF,LTF,Talalactoferrin 96T
20-321-175257 LACTOFERRICIN B - MONOCLONAL ANTIBODY TO BOVINE LACTOFERRICIN B; EC 3.4.21.-; Lactoferrin Monoclonal 0.1 mg
18-321-177030 LACTOFERRIN (LF) - POLYCLONAL ANTIBODY HUMAN LACTOFERRIN (LF); EC 3.4.21.-; Lactoferrin; Talalactoferrin alfa Polyclonal 0.1 mg
20-321-175214 LACTOFERRIN (LF) - MONOCLONAL ANTIBODY TO HUMAN LACTOFERRIN (LF); EC 3.4.21.-; Lactoferrin; Talalactoferrin alfa Monoclonal 0.1 mg
KP0970 Human Lactotransferrin (37 - 61), Lactoferricin H 1 mg
'AM32105PU-N Lactotransferrin (Lactoferricin-B) IgG1 antibody Ab host: Mouse 0.1 mg
AM32105PU-N Lactotransferrin (Lactoferricin-B) Mouse IgG1 antibody Ab Liquid 0.1 mg
KP1059 Lactoferricin B, Lactoferrin (17 - 41) 1 mg
orb81202 Human Lactoferrin Apo protein Recombinant Human Apo Lactoferrin produced in Plant is glycosylated polypeptide chain having an approximate molecular mass of 77-80 kDa.The Lactotransferrin is purified b 10 mg
11096-H08H LTF _ Lactoferrin _ Lactotransferrin Protein (His Tag) 50
orb81203 Human Lactoferrin Holo protein Recombinant Human Holo Lactoferrin produced in Plant is glycosylated polypeptide chain having an approximate molecular mass of 77-80 kDa.The Human Holo Lactotransferrin 10 mg
E0780p ELISA Lactoferrin,Lactotransferrin,LTF,Pig,Sus scrofa 96T
U0780p CLIA Lactoferrin,Lactotransferrin,LTF,Pig,Sus scrofa 96T
E0780p ELISA kit Lactoferrin,Lactotransferrin,LTF,Pig,Sus scrofa 96T
E0780m ELISA Lactoferrin,Lactotransferrin,Ltf,Mouse,Mus musculus 96T
E0780b ELISA kit Bos taurus,Bovine,Lactoferrin,Lactotransferrin,LTF 96T
E0780b ELISA Bos taurus,Bovine,Lactoferrin,Lactotransferrin,LTF 96T
E0780m ELISA kit Lactoferrin,Lactotransferrin,Ltf,Mouse,Mus musculus 96T
U0780b CLIA Bos taurus,Bovine,Lactoferrin,Lactotransferrin,LTF 96T
U0780m CLIA Lactoferrin,Lactotransferrin,Ltf,Mouse,Mus musculus 96T
Y050656 Anti-RAB13(Ras-related protein Rab-13, growth-inhibiting gene 4 protein) Antibody 100ug
Y050656 Anti-RAB13Ras-related protein Rab-13 growth-inhibiting gene 4 protein antibody 250ug
EIAAB33427 Cell growth-inhibiting gene 4 protein,GIG4,Homo sapiens,Human,RAB13,Ras-related protein Rab-13


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur