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P02788 (TRFL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lactotransferrin

Short name=Lactoferrin
EC=3.4.21.-
Alternative name(s):
Talalactoferrin
Gene names
Name:LTF
Synonyms:LF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length710 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate. Ref.23 Ref.29

Lactotransferrin has antimicrobial activity which depends on the extracellular cation concentration. Ref.23 Ref.29

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. Ref.23 Ref.29

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. Ref.23 Ref.29

Isoform DeltaLf: transcription factor with antiproliferative properties and inducing cell cycle arrest. Binds to DeltaLf response element found in the SKP1, BAX, DCPS, and SELH promoters. Ref.23 Ref.29

Catalytic activity

Preferential at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin.

Subunit structure

Monomer. Found in a complex with LTF, CLU, EPPIN and SEMG1. Ref.24

Subcellular location

Isoform 1: Secreted.

Isoform DeltaLf: Cytoplasm. Nucleus.

Post-translational modification

Isoform DeltaLf: Ubiquitinated at Lys-379 and Lys-391. Ref.27

Sequence similarities

Belongs to the transferrin family.

Contains 2 transferrin-like domains.

Ontologies

Keywords
   Biological processIon transport
Iron transport
Transcription
Transcription regulation
Transport
   Cellular componentCytoplasm
Nucleus
Secreted
   Coding sequence diversityAlternative promoter usage
Polymorphism
   DomainRepeat
Signal
   LigandDNA-binding
Iron
Metal-binding
   Molecular functionAntibiotic
Antimicrobial
Hydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

humoral immune response

Traceable author statement PubMed 9770539. Source: ProtInc

iron assimilation by chelation and transport

Traceable author statement. Source: Reactome

iron ion transport

Inferred from electronic annotation. Source: InterPro

phagosome maturation

Traceable author statement. Source: Reactome

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

response to host immune response

Traceable author statement. Source: Reactome

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

phagocytic vesicle lumen

Traceable author statement. Source: Reactome

secretory granule

Inferred from direct assay PubMed 11907569. Source: MGI

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

ferric iron binding

Inferred from electronic annotation. Source: InterPro

heparin binding

Inferred from direct assay PubMed 11907569. Source: MGI

serine-type endopeptidase activity

Traceable author statement PubMed 9770539. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CALMP621572EBI-1058602,EBI-397403From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform 1 (identifier: P02788-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform DeltaLf (identifier: P02788-2)

Also known as: Delta-lactoferrin;

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.
Note: Phosphorylated at Ser-10. Glycosylated at Ser-10. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.15 Ref.16 Ref.17
Chain20 – 710691Lactotransferrin
PRO_0000035732
Peptide171 – 20131Kaliocin-1
PRO_0000035733
Peptide338 – 3436Lactoferroxin-A
PRO_0000035734
Peptide543 – 5475Lactoferroxin-B
PRO_0000035735
Peptide680 – 6867Lactoferroxin-C
PRO_0000035736

Regions

Domain25 – 352328Transferrin-like 1
Domain364 – 695332Transferrin-like 2

Sites

Active site921 Probable
Active site2781Nucleophile Probable
Metal binding791Iron 1
Metal binding1111Iron 1
Metal binding2111Iron 1
Metal binding2721Iron 1
Metal binding4141Iron 2
Metal binding4541Iron 2
Metal binding5471Iron 2
Metal binding6161Iron 2
Binding site1361Carbonate 1
Binding site1401Carbonate 1
Binding site1421Carbonate 1; via amide nitrogen
Binding site1431Carbonate 1; via amide nitrogen
Binding site4801Carbonate 2
Binding site4841Carbonate 2
Binding site4861Carbonate 2; via amide nitrogen
Binding site4871Carbonate 2; via amide nitrogen

Amino acid modifications

Glycosylation1561N-linked (GlcNAc...) Ref.25
Glycosylation4971N-linked (GlcNAc...) Ref.25 Ref.26
Glycosylation6421N-linked (GlcNAc...) Ref.25
Disulfide bond28 ↔ 64
Disulfide bond38 ↔ 55
Disulfide bond134 ↔ 217
Disulfide bond176 ↔ 192
Disulfide bond189 ↔ 200
Disulfide bond250 ↔ 264
Disulfide bond367 ↔ 399
Disulfide bond377 ↔ 390
Disulfide bond424 ↔ 705
Disulfide bond446 ↔ 668
Disulfide bond478 ↔ 553
Disulfide bond502 ↔ 696
Disulfide bond512 ↔ 526
Disulfide bond523 ↔ 536
Disulfide bond594 ↔ 608
Disulfide bond646 ↔ 651

Natural variations

Alternative sequence1 – 4444Missing in isoform DeltaLf.
VSP_044308
Natural variant291A → T. Ref.3 Ref.6 Ref.7 Ref.8 Ref.9 Ref.35
Corresponds to variant rs1126477 [ dbSNP | Ensembl ].
VAR_013504
Natural variant471K → R. Ref.3 Ref.6 Ref.7 Ref.8 Ref.9 Ref.35
Corresponds to variant rs1126478 [ dbSNP | Ensembl ].
VAR_013505
Natural variant1481I → T. Ref.1
Corresponds to variant rs1126479 [ dbSNP | Ensembl ].
VAR_013506
Natural variant4221G → C. Ref.1
Corresponds to variant rs1042055 [ dbSNP | Ensembl ].
VAR_013507
Natural variant5791E → D. Ref.6 Ref.8 Ref.9 Ref.20
Corresponds to variant rs2073495 [ dbSNP | Ensembl ].
VAR_013508

Experimental info

Mutagenesis921K → A: Almost no protease activity. Ref.23
Mutagenesis2701P → V: No effect. Ref.23
Mutagenesis2781S → A: No protease activity. Ref.23
Sequence conflict141L → P in AAA58656. Ref.4
Sequence conflict201G → GS in AAH15822. Ref.12
Sequence conflict201G → GS in AAH15823. Ref.12
Sequence conflict231R → RR in CAA37914. Ref.1
Sequence conflict231R → RR in AAB60324. Ref.2
Sequence conflict231R → RR in AAA36159. Ref.3
Sequence conflict231R → RR in AAA59511. Ref.4
Sequence conflict231R → RR in AAA58656. Ref.4
Sequence conflict231R → RR in AAG48753. Ref.6
Sequence conflict231R → RR in AAN11304. Ref.7
Sequence conflict231R → RR in AAN63998. Ref.8
Sequence conflict231R → RR in AAN75578. Ref.9
Sequence conflict231R → RR in AAH22347. Ref.12
Sequence conflict231R → RR in CAA37116. Ref.14
Sequence conflict361T → D AA sequence Ref.17
Sequence conflict491R → C in AAH22347. Ref.12
Sequence conflict1301G → C in AAH15823. Ref.12
Sequence conflict1381L → R in AAH22347. Ref.12
Sequence conflict1401Missing AA sequence Ref.15
Sequence conflict1691Missing AA sequence Ref.15
Sequence conflict409 – 4102DA → NASVLMDSEGGFLAR AA sequence Ref.15
Sequence conflict4151G → E in AAA59511. Ref.4
Sequence conflict4311A → G in AAA58656. Ref.4
Sequence conflict4561A → T in AAH15822. Ref.12
Sequence conflict4561A → T in AAH15823. Ref.12
Sequence conflict4871G → A in AAA86665. Ref.19
Sequence conflict5311Q → E AA sequence Ref.15
Sequence conflict5371V → E in AAH15822. Ref.12
Sequence conflict6941K → R AA sequence Ref.15
Sequence conflict6941K → R AA sequence Ref.18

Secondary structure

................................................................................................................................................ 710
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 24, 2006. Version 6.
Checksum: 0489CABA6D13C098

FASTA71078,182
        10         20         30         40         50         60 
MKLVFLVLLF LGALGLCLAG RRRSVQWCAV SQPEATKCFQ WQRNMRKVRG PPVSCIKRDS 

        70         80         90        100        110        120 
PIQCIQAIAE NRADAVTLDG GFIYEAGLAP YKLRPVAAEV YGTERQPRTH YYAVAVVKKG 

       130        140        150        160        170        180 
GSFQLNELQG LKSCHTGLRR TAGWNVPIGT LRPFLNWTGP PEPIEAAVAR FFSASCVPGA 

       190        200        210        220        230        240 
DKGQFPNLCR LCAGTGENKC AFSSQEPYFS YSGAFKCLRD GAGDVAFIRE STVFEDLSDE 

       250        260        270        280        290        300 
AERDEYELLC PDNTRKPVDK FKDCHLARVP SHAVVARSVN GKEDAIWNLL RQAQEKFGKD 

       310        320        330        340        350        360 
KSPKFQLFGS PSGQKDLLFK DSAIGFSRVP PRIDSGLYLG SGYFTAIQNL RKSEEEVAAR 

       370        380        390        400        410        420 
RARVVWCAVG EQELRKCNQW SGLSEGSVTC SSASTTEDCI ALVLKGEADA MSLDGGYVYT 

       430        440        450        460        470        480 
AGKCGLVPVL AENYKSQQSS DPDPNCVDRP VEGYLAVAVV RRSDTSLTWN SVKGKKSCHT 

       490        500        510        520        530        540 
AVDRTAGWNI PMGLLFNQTG SCKFDEYFSQ SCAPGSDPRS NLCALCIGDE QGENKCVPNS 

       550        560        570        580        590        600 
NERYYGYTGA FRCLAENAGD VAFVKDVTVL QNTDGNNNEA WAKDLKLADF ALLCLDGKRK 

       610        620        630        640        650        660 
PVTEARSCHL AMAPNHAVVS RMDKVERLKQ VLLHQQAKFG RNGSDCPDKF CLFQSETKNL 

       670        680        690        700        710 
LFNDNTECLA RLHGKTTYEK YLGPQYVAGI TNLKKCSTSP LLEACEFLRK 

« Hide

Isoform DeltaLf (Delta-lactoferrin) [UniParc].

Checksum: C498CC5861CA1A12
Show »

FASTA66673,161

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of human mammary gland lactoferrin."
Rey M.W., Woloshuk S.L., de Boer H.A., Pieper F.R.
Nucleic Acids Res. 18:5288-5288(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS THR-148 AND CYS-422.
Tissue: Mammary gland.
[2]Cho Y.Y.
Thesis (1994), Genetic Engineering Research Institute, South Korea
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Mammary gland.
[3]Conneely O.M.
Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS THR-29 AND ARG-47.
[4]"Molecular cloning and sequence analysis of human lactoferrin."
Liang Q., Jimenez-Flores R., Richardson T.
Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Mammary gland.
[5]"Human neutrophil lactoferrin coding and 5' flanking region DNA sequences."
Wei X., Han J., Rado T.A.
Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Tissue: Bone marrow.
[6]"cDNA cloning and sequence analysis of human lactoferrin."
Cheng H., Chen X.Z., Huan L.D.
Sheng Wu Gong Cheng Xue Bao 17:385-387(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS THR-29; ARG-47 AND ASP-579.
Tissue: Mammary gland.
[7]"Characterization of an amino acid polymorphism in the antibacterial domain of human lactoferrin."
Kaplan J.B., Fine D.H.
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS THR-29 AND ARG-47.
[8]Shi Y.-Q., Zhang Y., Zheng Y.-M.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS THR-29; ARG-47 AND ASP-579.
Tissue: Mammary gland.
[9]Baskar Singh S., Saravanan K., Paramasivam M., Srinivasan A., Singh T.P.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS THR-29; ARG-47 AND ASP-579.
Tissue: Seminal vesicle.
[10]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTALF).
Tissue: Lung.
[11]"The DNA sequence, annotation and analysis of human chromosome 3."
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. expand/collapse author list , 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.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Prostate.
[13]"Differential molecular mechanism of the estrogen action that regulates lactoferrin gene in human and mouse."
Teng C.T., Liu Y., Yang N., Walmer D., Panella T.
Mol. Endocrinol. 6:1969-1981(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
[14]"Nucleotide sequence of human lactoferrin cDNA."
Powell M.J., Ogden J.E.
Nucleic Acids Res. 18:4013-4013(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-710 (ISOFORM DELTALF).
Tissue: Mammary gland.
[15]"Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins."
Metz-Boutigue M.-H., Jolles J., Mazurier J., Schoentgen F., Legrand D., Spik G., Montreuil J., Jolles P.
Eur. J. Biochem. 145:659-676(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-710.
[16]"The present state of the human lactotransferrin sequence. Study and alignment of the cyanogen bromide fragments and characterization of N- and C-terminal domains."
Metz-Boutigue M.-H., Mazurier J., Jolles J., Spik G., Montreuil J., Jolles P.
Biochim. Biophys. Acta 670:243-254(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 20-72; 133-170; 256-277 AND 346-529.
[17]"Characterization of the 84-kDa protein with ABH activity in human seminal plasma."
Sato I.
Nihon Hoigaku Zasshi 49:281-293(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-56.
Tissue: Seminal plasma.
[18]"An 88 amino acid long C-terminal sequence of human lactotransferrin."
Metz-Boutigue M.-H., Jolles J., Mazurier J., Spik G., Montreuil J., Jolles P.
FEBS Lett. 142:107-110(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 608-710.
[19]"Isolation of lactoferrin cDNA from a human myeloid library and expression of mRNA during normal and leukemic myelopoiesis."
Rado T.A., Wei X., Benz E.J. Jr.
Blood 70:989-993(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 435-710.
[20]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-710, VARIANT ASP-579.
[21]"Isolation and characterization of opioid antagonist peptides derived from human lactoferrin."
Tani F., Iio K., Chiba H., Yoshikawa M.
Agric. Biol. Chem. 54:1803-1810(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF LACTOFERROXINS.
[22]"Potassium efflux induced by a new lactoferrin-derived peptide mimicking the effect of native human lactoferrin on the bacterial cytoplasmic membrane."
Viejo-Diaz M., Andres M.T., Perez-Gil J., Sanchez M., Fierro J.F.
Biokhimiia 68:217-227(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 171-201 (KALIOCIN-1).
[23]"Human milk lactoferrin is a serine protease that cleaves Haemophilus surface proteins at arginine-rich sites."
Hendrixson D.R., Qiu J., Shewry S.C., Fink D.L., Petty S., Baker E.N., Plaut A.G., St Geme J.W. III
Mol. Microbiol. 47:607-617(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A PROTEASE, MUTAGENESIS OF LYS-92; PRO-270 AND SER-278.
[24]"Characterization of an eppin protein complex from human semen and spermatozoa."
Wang Z., Widgren E.E., Richardson R.T., O'Rand M.G.
Biol. Reprod. 77:476-484(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CLU; SEMG1 AND EPPIN.
[25]"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156; ASN-497 AND ASN-642, MASS SPECTROMETRY.
Tissue: Milk.
[26]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-497, MASS SPECTROMETRY.
Tissue: Liver.
[27]"O-GlcNAcylation/phosphorylation cycling at Ser10 controls both transcriptional activity and stability of delta-lactoferrin."
Hardiville S., Hoedt E., Mariller C., Benaissa M., Pierce A.
J. Biol. Chem. 285:19205-19218(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, PHOSPHORYLATION, UBIQUITINATION (ISOFORM DELTALF).
[28]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor."
Mariller C., Hardiville S., Hoedt E., Huvent I., Pina-Canseco S., Pierce A.
Biochem. Cell Biol. 90:307-319(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A TRANSCRIPTION FACTOR (ISOFORM DELTALF), DNA-BINDING (ISOFORM DELTALF).
[30]"Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8-A resolution."
Anderson B.F., Baker H.M., Norris G.E., Rice D.W., Baker E.N.
J. Mol. Biol. 209:711-734(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SEQUENCE REVISION.
[31]"Structure of human diferric lactoferrin refined at 2.2-A resolution."
Haridas M., Anderson B.F., Baker E.N.
Acta Crystallogr. D 51:629-646(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[32]"Mutagenesis of the histidine ligand in human lactoferrin: iron binding properties and crystal structure of the histidine-253-->methionine mutant."
Nicholson H., Anderson B.F., Bland T., Shewry S.C., Tweedie J.W., Baker E.N.
Biochemistry 36:341-346(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-352.
[33]"Structure of recombinant human lactoferrin expressed in Aspergillus awamori."
Sun X.L., Baker H.M., Shewry S.C., Jameson G.B., Baker E.N.
Acta Crystallogr. D 55:403-407(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[34]"Structure of human apolactoferrin at 2.0-A resolution. Refinement and analysis of ligand-induced conformational change."
Jameson G.B., Anderson B.F., Norris G.E., Thomas D.H., Baker E.N.
Acta Crystallogr. D 54:1319-1335(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[35]"Familial subepithelial corneal amyloidosis (gelatinous drop-like corneal dystrophy): exclusion of linkage to lactoferrin gene."
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. expand/collapse author list , Nagata M., Nakayasu K., Hejtmancik J.F., Teng C.T.
Mol. Vis. 4:31-32(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THR-29 AND ARG-47.
+Additional computationally mapped references.

Web resources

Wikipedia

Lactotransferrin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53961 mRNA. Translation: CAA37914.1.
U07643 mRNA. Translation: AAB60324.1.
M93150 mRNA. Translation: AAA36159.1.
M83202 mRNA. Translation: AAA59511.1.
M83205 mRNA. Translation: AAA58656.1.
M73700 Genomic DNA. Translation: AAA59479.1.
AF332168 mRNA. Translation: AAG48753.1.
AY137470 mRNA. Translation: AAN11304.1.
AY165046 mRNA. Translation: AAN63998.1.
AY178998 mRNA. Translation: AAN75578.2.
AK298035 mRNA. Translation: BAH12708.1.
AC098613 Genomic DNA. No translation available.
BC015822 mRNA. Translation: AAH15822.1.
BC015823 mRNA. Translation: AAH15823.1.
BC022347 mRNA. Translation: AAH22347.1.
S52659 Genomic DNA. Translation: AAB24877.1.
X52941 mRNA. Translation: CAA37116.1.
M18642 mRNA. Translation: AAA86665.1.
U95626 Genomic DNA. Translation: AAB57795.1.
IPIIPI00298860.
PIRTFHUL. G01394.
RefSeqNP_001186078.1. NM_001199149.1.
NP_002334.2. NM_002343.3.
UniGeneHs.529517.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0LX-ray2.20A20-710[»]
1BKAX-ray2.40A20-710[»]
1CB6X-ray2.00A20-710[»]
1DSNX-ray2.05A21-352[»]
1EH3X-ray2.00A21-348[»]
1FCKX-ray2.20A21-710[»]
1H43X-ray2.20A21-352[»]
1H44X-ray2.00A21-352[»]
1H45X-ray1.95A21-352[»]
1HSEX-ray2.20A21-353[»]
1L5TX-ray3.00A/B21-351[»]
1LCFX-ray2.00A20-710[»]
1LCTX-ray2.00A21-352[»]
1LFGX-ray2.20A20-710[»]
1LFHX-ray2.80A20-710[»]
1LFIX-ray2.10A20-710[»]
1LGBX-ray3.30C110-268[»]
1N76X-ray3.40A21-710[»]
1SQYX-ray2.50A20-710[»]
1U62NMR-A39-49[»]
1VFDX-ray2.50A22-349[»]
1VFEX-ray2.30A22-352[»]
1XV4NMR-A39-49[»]
1XV7NMR-A39-49[»]
1Z6VNMR-A21-67[»]
1Z6WNMR-A21-67[»]
2BJJX-ray2.40X21-710[»]
2DP4X-ray2.90I528-535[»]
2GMCNMR-A39-49[»]
2GMDNMR-A39-49[»]
2HD4X-ray2.15B528-535[»]
2PMSX-ray2.91A/B21-362[»]
ProteinModelPortalP02788.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-41354N.
IntActP02788. 5 interactions.
MINTMINT-1511753.

Protein family/group databases

Allergome1384. Hom s Lactoferrin.
MEROPSS60.001.

PTM databases

GlycoSuiteDBP02788.
PhosphoSiteP02788.

Polymorphism databases

DMDM85700158.

Proteomic databases

PaxDbP02788.
PRIDEP02788.

Protocols and materials databases

DNASU4057.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000231751; ENSP00000231751; ENSG00000012223.
ENST00000426532; ENSP00000405719; ENSG00000012223.
GeneID4057.
KEGGhsa:4057.
UCSCuc003cpq.3. human.

Organism-specific databases

CTD4057.
GeneCardsGC03M046452.
HGNCHGNC:6720. LTF.
HPACAB008645.
MIM150210. gene.
245480. phenotype.
neXtProtNX_P02788.
PharmGKBPA30482.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG87503.
HOVERGENHBG000055.
InParanoidP02788.
OMARPVEGYL.
OrthoDBEOG4CRKZG.
PhylomeDBP02788.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Gene expression databases

ArrayExpressP02788.
BgeeP02788.
GenevestigatorP02788.
GermOnlineENSG00000012223. Homo sapiens.

Family and domain databases

InterProIPR016357. Transferrin.
IPR001156. Transferrin_fam.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PANTHERPTHR11485. PTHR11485. 1 hit.
PfamPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFPIRSF002549. Transferrin. 1 hit.
PRINTSPR00422. TRANSFERRIN.
SMARTSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEPS00205. TRANSFERRIN_LIKE_1. 2 hits.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLTF. human.
DrugBankDB00487. Pefloxacin.
EvolutionaryTraceP02788.
GenomeRNAi4057.
NextBio15896.
SOURCESearch...

Entry information

Entry nameTRFL_HUMAN
AccessionPrimary (citable) accession number: P02788
Secondary accession number(s): B7Z4X2 expand/collapse secondary AC list , E7EQH5, O00756, Q16780, Q16785, Q16786, Q16789, Q8IU92, Q8IZH6, Q8TCD2, Q96KZ4, Q96KZ5, Q9H1Z3, Q9UCY5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 24, 2006
Last modified: May 29, 2013
This is version 170 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families