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Entry version 104 (11 Dec 2019)
Sequence version 1 (01 Nov 1998)
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Protein

Lactotransferrin

Gene

LTF

Organism
Bubalus bubalis (Domestic water buffalo)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate.
Lactotransferrin is a major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity. Antimicrobial properties may 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. The most effective inhibitory activity is seen against E.coli and P.aeruginosa. Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. Interferes with the lipopolysaccharide (LPS)-stimulated TLR4 signaling, but cannot directly stimulate the TLR4 signaling pathway and subsequent NF-kappa-B activation (By similarity).By similarity
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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi79Iron 1PROSITE-ProRule annotation2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei92PROSITE-ProRule annotation1
Metal bindingi111Iron 1PROSITE-ProRule annotation2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei136Carbonate 1PROSITE-ProRule annotation2 Publications1
Binding sitei140Carbonate 1PROSITE-ProRule annotation2 Publications1
Binding sitei142Carbonate 1; via amide nitrogenPROSITE-ProRule annotation2 Publications1
Binding sitei143Carbonate 1; via amide nitrogenPROSITE-ProRule annotation2 Publications1
Metal bindingi211Iron 1PROSITE-ProRule annotation2 Publications1
Metal bindingi272Iron 1; via tele nitrogenPROSITE-ProRule annotation2 Publications1
Active sitei278NucleophilePROSITE-ProRule annotation1
Metal bindingi414Iron 2PROSITE-ProRule annotation2 Publications1
Metal bindingi452Iron 2PROSITE-ProRule annotation2 Publications1
Binding sitei478Carbonate 2PROSITE-ProRule annotation2 Publications1
Binding sitei482Carbonate 2PROSITE-ProRule annotation2 Publications1
Binding sitei484Carbonate 2; via amide nitrogenPROSITE-ProRule annotation2 Publications1
Binding sitei485Carbonate 2; via amide nitrogenPROSITE-ProRule annotation2 Publications1
Metal bindingi545Iron 2PROSITE-ProRule annotation2 Publications1
Metal bindingi614Iron 2; via tele nitrogenPROSITE-ProRule annotation2 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processImmunity, Ion transport, Iron transport, Osteogenesis, Transport
LigandIron, Metal-binding

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S60.001

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Lactotransferrin (EC:3.4.21.-)
Short name:
Lactoferrin
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:LTF
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBubalus bubalis (Domestic water buffalo)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri89462 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBubalus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 19Add BLAST19
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003572820 – 708LactotransferrinAdd BLAST689

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi28 ↔ 64
Disulfide bondi38 ↔ 55
Disulfide bondi134 ↔ 217
Disulfide bondi176 ↔ 192
Disulfide bondi179 ↔ 202
Disulfide bondi189 ↔ 200
Disulfide bondi250 ↔ 264
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi252N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi300N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi367 ↔ 399
Disulfide bondi377 ↔ 390
Disulfide bondi424 ↔ 703
Disulfide bondi444 ↔ 666
Disulfide bondi476 ↔ 551
Glycosylationi495N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi500 ↔ 694
Disulfide bondi510 ↔ 524
Disulfide bondi521 ↔ 534
Glycosylationi564N-linked (GlcNAc...) asparagine1
Disulfide bondi592 ↔ 606
Disulfide bondi644 ↔ 649

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
O77698

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

Found in a complex with LTF, CLU, EPPIN and SEMG1 (By similarity).

By similarity

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1708
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
O77698

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O77698

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini25 – 352Transferrin-like 1PROSITE-ProRule annotationAdd BLAST328
Domaini364 – 693Transferrin-like 2PROSITE-ProRule annotationAdd BLAST330

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the transferrin family.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR030684 Lactotransferrin
IPR016357 Transferrin
IPR001156 Transferrin-like_dom
IPR018195 Transferrin_Fe_BS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00405 Transferrin, 2 hits

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF500683 Lactotransferrin, 1 hit
PIRSF002549 Transferrin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00422 TRANSFERRIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00094 TR_FER, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00205 TRANSFERRIN_LIKE_1, 2 hits
PS00206 TRANSFERRIN_LIKE_2, 2 hits
PS00207 TRANSFERRIN_LIKE_3, 2 hits
PS51408 TRANSFERRIN_LIKE_4, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

O77698-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKLFVPALLS LGALGLCLAA PRKNVRWCTI SQPEWLKCHR WQWRMKKLGA
60 70 80 90 100
PSITCVRRAF VLECIRAITE KKADAVTLDG GMVFEAGLDP YKLRPVAAEI
110 120 130 140 150
YGTKESPQTH YYAVAVVKKG SNFQLDQLQG RNSCHTGLGR SAGWNIPMGI
160 170 180 190 200
LRPYLSWTES LEPFQGAVAK FFSASCVPCV DRQAYPNLCQ LCKGEGENQC
210 220 230 240 250
ACSPREPYFG YSGAFKCLQD GAGDVAFVKE TTVFENLPEK ADRDQYELLC
260 270 280 290 300
LNNTRAPVDA FKECHLAQVP SHAVVARSVD GKEDLIWKLL SKAQEKFGKN
310 320 330 340 350
KSGSFQLFGS PPGQRDLLFK DCALGFLRIP SKVDSALYLG SRYLTALKNL
360 370 380 390 400
RETAEEVQAR RARVVWCAVG PEEQKKCQQW SQQSGQIVTC ATASTTDDCI
410 420 430 440 450
ALVLKGEADA LSLDGGYIYT AGKCGLVPVL AENRKSSKHS SLDCVLRPTE
460 470 480 490 500
GYLAVAVVKK ANEGLTWNSL KGKKSCHTAV DRTAGWNIPM GLIANQTGSC
510 520 530 540 550
AFDEFFSQSC APGADPKSRL CALCAGDDQG LDKCVPNSKE KYYGYTGAFR
560 570 580 590 600
CLAEDVGDVA FVKNDTVWEN TNGESTADWA KNLNREDFRL LCLDGTRKPV
610 620 630 640 650
TEAQSCHLAV APNHAVVSLS ERAAHVEQVL LHQQALFGEN GKNCPDKFCL
660 670 680 690 700
FKSETKNLLF NDNTECLAKL GGRPTYEEYL GTEYVTAIAN LKKCSTSPLL

EACAFLTR
Length:708
Mass (Da):77,730
Last modified:November 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i08D2600AAB2F9ACD
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ005203 mRNA Translation: CAA06441.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005203 mRNA Translation: CAA06441.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BIYX-ray3.37A20-708[»]
1CE2X-ray2.50A20-708[»]
SMRiO77698
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

MEROPSiS60.001

Proteomic databases

PRIDEiO77698

Miscellaneous databases

EvolutionaryTraceiO77698

Family and domain databases

InterProiView protein in InterPro
IPR030684 Lactotransferrin
IPR016357 Transferrin
IPR001156 Transferrin-like_dom
IPR018195 Transferrin_Fe_BS
PfamiView protein in Pfam
PF00405 Transferrin, 2 hits
PIRSFiPIRSF500683 Lactotransferrin, 1 hit
PIRSF002549 Transferrin, 1 hit
PRINTSiPR00422 TRANSFERRIN
SMARTiView protein in SMART
SM00094 TR_FER, 2 hits
PROSITEiView protein in PROSITE
PS00205 TRANSFERRIN_LIKE_1, 2 hits
PS00206 TRANSFERRIN_LIKE_2, 2 hits
PS00207 TRANSFERRIN_LIKE_3, 2 hits
PS51408 TRANSFERRIN_LIKE_4, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTRFL_BUBBU
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O77698
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: December 11, 2019
This is version 104 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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