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Protein

Lactotransferrin

Gene

LTF

Organism
Equus caballus (Horse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. May have anabolic, differentiating and anti-apoptotic effects on osteoblasts and may also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. May interfere with the lipopolysaccharide (LPS)-stimulated TLR4 signaling (By similarity). Can bind glucose.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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi66 – 661Iron 1PROSITE-ProRule annotation4 Publications
Active sitei79 – 791PROSITE-ProRule annotation
Metal bindingi98 – 981Iron 1PROSITE-ProRule annotation4 Publications
Binding sitei123 – 1231Carbonate 1PROSITE-ProRule annotation2 Publications
Binding sitei127 – 1271Carbonate 1PROSITE-ProRule annotation2 Publications
Binding sitei129 – 1291Carbonate 1; via amide nitrogenPROSITE-ProRule annotation2 Publications
Binding sitei130 – 1301Carbonate 1; via amide nitrogenPROSITE-ProRule annotation2 Publications
Metal bindingi198 – 1981Iron 1PROSITE-ProRule annotation4 Publications
Metal bindingi259 – 2591Iron 1; via tele nitrogenPROSITE-ProRule annotation4 Publications
Active sitei265 – 2651NucleophilePROSITE-ProRule annotation
Metal bindingi401 – 4011Iron 2PROSITE-ProRule annotation4 Publications
Binding sitei436 – 4361Glucose; via carbonyl oxygen1 Publication
Metal bindingi439 – 4391Iron 2PROSITE-ProRule annotation4 Publications
Binding sitei465 – 4651Carbonate 2PROSITE-ProRule annotation2 Publications
Binding sitei469 – 4691Carbonate 2PROSITE-ProRule annotation2 Publications
Binding sitei471 – 4711Carbonate 2; via amide nitrogenPROSITE-ProRule annotation2 Publications
Binding sitei472 – 4721Carbonate 2; via amide nitrogenPROSITE-ProRule annotation2 Publications
Metal bindingi532 – 5321Iron 2PROSITE-ProRule annotation4 Publications
Binding sitei600 – 6001Glucose1 Publication
Metal bindingi601 – 6011Iron 2; via tele nitrogenPROSITE-ProRule annotation4 Publications
Binding sitei666 – 6661Glucose1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Immunity, Ion transport, Iron transport, Osteogenesis, Transport

Keywords - Ligandi

Iron, Metal-binding

Protein family/group databases

MEROPSiS60.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Lactotransferrin (EC:3.4.21.-)
Short name:
Lactoferrin
Gene namesi
Name:LTF
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
Proteomesi
  • UP000002281 Componenti: Unplaced

Subcellular locationi

  • Secreted
  • Cytoplasmic granule By similarity

  • Note: Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 6›6
Chaini7 – 695689LactotransferrinPRO_0000035731Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi15 ↔ 51
Disulfide bondi25 ↔ 42
Disulfide bondi121 ↔ 204
Glycosylationi143 – 1431N-linked (GlcNAc...)Sequence analysis
Disulfide bondi163 ↔ 179
Disulfide bondi166 ↔ 189
Disulfide bondi176 ↔ 187
Disulfide bondi237 ↔ 251
Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence analysis
Disulfide bondi354 ↔ 386
Disulfide bondi364 ↔ 377
Disulfide bondi411 ↔ 690
Disulfide bondi431 ↔ 653
Disulfide bondi463 ↔ 538
Glycosylationi482 – 4821N-linked (GlcNAc...)Sequence analysis
Disulfide bondi487 ↔ 681
Disulfide bondi497 ↔ 511
Disulfide bondi508 ↔ 521
Disulfide bondi579 ↔ 593
Disulfide bondi631 ↔ 636

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO77811.
PRIDEiO77811.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiO77811. 1 interaction.
STRINGi9796.ENSECAP00000019516.

Structurei

Secondary structure

1
695
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 187Combined sources
Helixi19 – 3416Combined sources
Beta strandi40 – 445Combined sources
Helixi48 – 569Combined sources
Beta strandi62 – 654Combined sources
Helixi67 – 748Combined sources
Turni76 – 783Combined sources
Beta strandi80 – 889Combined sources
Beta strandi91 – 933Combined sources
Beta strandi95 – 10511Combined sources
Helixi112 – 1143Combined sources
Beta strandi119 – 1235Combined sources
Turni128 – 1314Combined sources
Helixi132 – 1376Combined sources
Helixi139 – 1424Combined sources
Helixi151 – 1588Combined sources
Beta strandi159 – 1635Combined sources
Turni169 – 1713Combined sources
Helixi173 – 1753Combined sources
Turni176 – 1783Combined sources
Turni183 – 1875Combined sources
Beta strandi189 – 1935Combined sources
Helixi197 – 20610Combined sources
Beta strandi211 – 2188Combined sources
Helixi219 – 2235Combined sources
Helixi227 – 2304Combined sources
Beta strandi233 – 2375Combined sources
Turni238 – 2403Combined sources
Beta strandi241 – 2444Combined sources
Helixi245 – 2473Combined sources
Turni248 – 2503Combined sources
Beta strandi253 – 2575Combined sources
Beta strandi260 – 2678Combined sources
Helixi270 – 28415Combined sources
Turni286 – 2883Combined sources
Beta strandi299 – 3013Combined sources
Beta strandi304 – 3063Combined sources
Beta strandi312 – 3154Combined sources
Helixi322 – 3265Combined sources
Helixi328 – 3369Combined sources
Helixi341 – 3499Combined sources
Beta strandi350 – 3578Combined sources
Helixi358 – 37013Combined sources
Beta strandi373 – 38210Combined sources
Helixi383 – 39210Combined sources
Beta strandi397 – 4004Combined sources
Helixi402 – 4109Combined sources
Beta strandi414 – 4229Combined sources
Beta strandi424 – 4263Combined sources
Helixi429 – 4335Combined sources
Beta strandi439 – 44810Combined sources
Helixi454 – 4563Combined sources
Beta strandi462 – 4654Combined sources
Turni470 – 4734Combined sources
Helixi474 – 48411Combined sources
Helixi489 – 4913Combined sources
Beta strandi493 – 4975Combined sources
Beta strandi499 – 5013Combined sources
Beta strandi508 – 5103Combined sources
Beta strandi523 – 5275Combined sources
Helixi531 – 54010Combined sources
Beta strandi545 – 5506Combined sources
Helixi551 – 5555Combined sources
Turni556 – 5605Combined sources
Helixi565 – 5684Combined sources
Beta strandi574 – 5785Combined sources
Beta strandi580 – 5823Combined sources
Beta strandi584 – 5863Combined sources
Helixi587 – 5926Combined sources
Beta strandi595 – 5984Combined sources
Beta strandi602 – 6054Combined sources
Turni607 – 6093Combined sources
Helixi610 – 62415Combined sources
Helixi631 – 6344Combined sources
Turni641 – 6433Combined sources
Beta strandi651 – 6555Combined sources
Helixi663 – 6675Combined sources
Helixi669 – 67911Combined sources
Helixi685 – 6939Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B1XX-ray2.62A7-695[»]
1B7UX-ray3.80A7-695[»]
1B7ZX-ray2.70A7-695[»]
1F9BX-ray2.70A1-695[»]
1I6BX-ray3.20A7-695[»]
1QJMX-ray3.40A7-695[»]
3CR9X-ray3.49A7-695[»]
ProteinModelPortaliO77811.
SMRiO77811. Positions 7-695.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO77811.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 339328Transferrin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini351 – 680330Transferrin-like 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the transferrin family.PROSITE-ProRule annotation
Contains 2 transferrin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IEAI. Eukaryota.
ENOG410XQ36. LUCA.
HOGENOMiHOG000043759.
HOVERGENiHBG000055.
InParanoidiO77811.

Family and domain databases

InterProiIPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. 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]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

O77811-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
LGLCLAAPRK SVRWCTISPA EAAKCAKFQR NMKKVRGPSV SCIRKTSSFE
60 70 80 90 100
CIQAIAANKA DAVTLDGGLV YEAGLHPYKL RPVAAEVYQT RGKPQTRYYA
110 120 130 140 150
VAVVKKGSGF QLNQLQGVKS CHTGLGRSAG WNIPIGTLRP YLNWTGPPEP
160 170 180 190 200
LQKAVANFFS ASCVPCADGK QYPNLCRLCA GTEADKCACS SQEPYFGYSG
210 220 230 240 250
AFKCLENGAG DVAFVKDSTV FENLPDEADR DKYELLCPDN TRKPVDAFKE
260 270 280 290 300
CHLARVPSHA VVARSVDGRE DLIWRLLHRA QEEFGRNKSS AFQLFKSTPE
310 320 330 340 350
NKDLLFKDSA LGFVRIPSQI DSGLYLGANY LTATQNLRET AAEVAARRER
360 370 380 390 400
VVWCAVGPEE ERKCKQWSDV SNRKVACASA STTEECIALV LKGEADALNL
410 420 430 440 450
DGGFIYVAGK CGLVPVLAEN QKSQNSNAPD CVHRPPEGYL AVAVVRKSDA
460 470 480 490 500
DLTWNSLSGK KSCHTGVGRT AAWNIPMGLL FNQTGSCKFD KFFSQSCAPG
510 520 530 540 550
ADPQSSLCAL CVGNNENENK CMPNSEERYY GYTGAFRCLA EKAGDVAFVK
560 570 580 590 600
DVTVLQNTDG KNSEPWAKDL KQEDFELLCL DGTRKPVAEA ESCHLARAPN
610 620 630 640 650
HAVVSQSDRA QHLKKVLFLQ QDQFGGNGPD CPGKFCLFKS ETKNLLFNDN
660 670 680 690
TECLAELQGK TTYEQYLGSE YVTSITNLRR CSSSPLLEAC AFLRA
Length:695
Mass (Da):75,991
Last modified:November 1, 1998 - v1
Checksum:i07BB84D50E1B165D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010930 mRNA. Translation: CAA09407.1.
UniGeneiEca.13037.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010930 mRNA. Translation: CAA09407.1.
UniGeneiEca.13037.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B1XX-ray2.62A7-695[»]
1B7UX-ray3.80A7-695[»]
1B7ZX-ray2.70A7-695[»]
1F9BX-ray2.70A1-695[»]
1I6BX-ray3.20A7-695[»]
1QJMX-ray3.40A7-695[»]
3CR9X-ray3.49A7-695[»]
ProteinModelPortaliO77811.
SMRiO77811. Positions 7-695.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO77811. 1 interaction.
STRINGi9796.ENSECAP00000019516.

Protein family/group databases

MEROPSiS60.001.

Proteomic databases

PaxDbiO77811.
PRIDEiO77811.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IEAI. Eukaryota.
ENOG410XQ36. LUCA.
HOGENOMiHOG000043759.
HOVERGENiHBG000055.
InParanoidiO77811.

Miscellaneous databases

EvolutionaryTraceiO77811.

Family and domain databases

InterProiIPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiTRFL_HORSE
AccessioniPrimary (citable) accession number: O77811
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: November 11, 2015
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.