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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)DescriptionActionsGraphical viewLength
Metal bindingi66Iron 1PROSITE-ProRule annotation4 Publications1
Active sitei79PROSITE-ProRule annotation1
Metal bindingi98Iron 1PROSITE-ProRule annotation4 Publications1
Binding sitei123Carbonate 1PROSITE-ProRule annotation2 Publications1
Binding sitei127Carbonate 1PROSITE-ProRule annotation2 Publications1
Binding sitei129Carbonate 1; via amide nitrogenPROSITE-ProRule annotation2 Publications1
Binding sitei130Carbonate 1; via amide nitrogenPROSITE-ProRule annotation2 Publications1
Metal bindingi198Iron 1PROSITE-ProRule annotation4 Publications1
Metal bindingi259Iron 1; via tele nitrogenPROSITE-ProRule annotation4 Publications1
Active sitei265NucleophilePROSITE-ProRule annotation1
Metal bindingi401Iron 2PROSITE-ProRule annotation4 Publications1
Binding sitei436Glucose; via carbonyl oxygen1 Publication1
Metal bindingi439Iron 2PROSITE-ProRule annotation4 Publications1
Binding sitei465Carbonate 2PROSITE-ProRule annotation2 Publications1
Binding sitei469Carbonate 2PROSITE-ProRule annotation2 Publications1
Binding sitei471Carbonate 2; via amide nitrogenPROSITE-ProRule annotation2 Publications1
Binding sitei472Carbonate 2; via amide nitrogenPROSITE-ProRule annotation2 Publications1
Metal bindingi532Iron 2PROSITE-ProRule annotation4 Publications1
Binding sitei600Glucose1 Publication1
Metal bindingi601Iron 2; via tele nitrogenPROSITE-ProRule annotation4 Publications1
Binding sitei666Glucose1 Publication1

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)DescriptionActionsGraphical viewLength
Signal peptidei‹1 – 6›6
ChainiPRO_00000357317 – 695LactotransferrinAdd BLAST689

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi15 ↔ 51
Disulfide bondi25 ↔ 42
Disulfide bondi121 ↔ 204
Glycosylationi143N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi163 ↔ 179
Disulfide bondi166 ↔ 189
Disulfide bondi176 ↔ 187
Disulfide bondi237 ↔ 251
Glycosylationi287N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi354 ↔ 386
Disulfide bondi364 ↔ 377
Disulfide bondi411 ↔ 690
Disulfide bondi431 ↔ 653
Disulfide bondi463 ↔ 538
Glycosylationi482N-linked (GlcNAc...)Sequence analysis1
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 interactor.
STRINGi9796.ENSECAP00000019516.

Structurei

Secondary structure

1695
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 18Combined sources7
Helixi19 – 34Combined sources16
Beta strandi40 – 44Combined sources5
Helixi48 – 56Combined sources9
Beta strandi62 – 65Combined sources4
Helixi67 – 74Combined sources8
Turni76 – 78Combined sources3
Beta strandi80 – 88Combined sources9
Beta strandi91 – 93Combined sources3
Beta strandi95 – 105Combined sources11
Helixi112 – 114Combined sources3
Beta strandi119 – 123Combined sources5
Turni128 – 131Combined sources4
Helixi132 – 137Combined sources6
Helixi139 – 142Combined sources4
Helixi151 – 158Combined sources8
Beta strandi159 – 163Combined sources5
Turni169 – 171Combined sources3
Helixi173 – 175Combined sources3
Turni176 – 178Combined sources3
Turni183 – 187Combined sources5
Beta strandi189 – 193Combined sources5
Helixi197 – 206Combined sources10
Beta strandi211 – 218Combined sources8
Helixi219 – 223Combined sources5
Helixi227 – 230Combined sources4
Beta strandi233 – 237Combined sources5
Turni238 – 240Combined sources3
Beta strandi241 – 244Combined sources4
Helixi245 – 247Combined sources3
Turni248 – 250Combined sources3
Beta strandi253 – 257Combined sources5
Beta strandi260 – 267Combined sources8
Helixi270 – 284Combined sources15
Turni286 – 288Combined sources3
Beta strandi299 – 301Combined sources3
Beta strandi304 – 306Combined sources3
Beta strandi312 – 315Combined sources4
Helixi322 – 326Combined sources5
Helixi328 – 336Combined sources9
Helixi341 – 349Combined sources9
Beta strandi350 – 357Combined sources8
Helixi358 – 370Combined sources13
Beta strandi373 – 382Combined sources10
Helixi383 – 392Combined sources10
Beta strandi397 – 400Combined sources4
Helixi402 – 410Combined sources9
Beta strandi414 – 422Combined sources9
Beta strandi424 – 426Combined sources3
Helixi429 – 433Combined sources5
Beta strandi439 – 448Combined sources10
Helixi454 – 456Combined sources3
Beta strandi462 – 465Combined sources4
Turni470 – 473Combined sources4
Helixi474 – 484Combined sources11
Helixi489 – 491Combined sources3
Beta strandi493 – 497Combined sources5
Beta strandi499 – 501Combined sources3
Beta strandi508 – 510Combined sources3
Beta strandi523 – 527Combined sources5
Helixi531 – 540Combined sources10
Beta strandi545 – 550Combined sources6
Helixi551 – 555Combined sources5
Turni556 – 560Combined sources5
Helixi565 – 568Combined sources4
Beta strandi574 – 578Combined sources5
Beta strandi580 – 582Combined sources3
Beta strandi584 – 586Combined sources3
Helixi587 – 592Combined sources6
Beta strandi595 – 598Combined sources4
Beta strandi602 – 605Combined sources4
Turni607 – 609Combined sources3
Helixi610 – 624Combined sources15
Helixi631 – 634Combined sources4
Turni641 – 643Combined sources3
Beta strandi651 – 655Combined sources5
Helixi663 – 667Combined sources5
Helixi669 – 679Combined sources11
Helixi685 – 693Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO77811.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 339Transferrin-like 1PROSITE-ProRule annotationAdd BLAST328
Domaini351 – 680Transferrin-like 2PROSITE-ProRule annotationAdd BLAST330

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)DescriptionActionsGraphical viewLength
Non-terminal residuei11

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO77811. 1 interactor.
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 2, 2016
This is version 103 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.