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Protein

Lactotransferrin

Gene

LTF

Organism
Camelus dromedarius (Dromedary) (Arabian camel)
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.By similarity
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).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 bindingi79Iron 1PROSITE-ProRule annotation1
Active sitei92PROSITE-ProRule annotation1
Metal bindingi111Iron 1PROSITE-ProRule annotation1 Publication1
Binding sitei136Carbonate 1PROSITE-ProRule annotation1
Binding sitei140Carbonate 1PROSITE-ProRule annotation1 Publication1
Binding sitei142Carbonate 1; via amide nitrogenPROSITE-ProRule annotation1
Binding sitei143Carbonate 1; via amide nitrogenPROSITE-ProRule annotation1
Metal bindingi211Iron 1PROSITE-ProRule annotation1 Publication1
Metal bindingi272Iron 1PROSITE-ProRule annotation1
Active sitei278NucleophilePROSITE-ProRule annotation1
Metal bindingi414Iron 2PROSITE-ProRule annotation1
Metal bindingi452Iron 2PROSITE-ProRule annotation1 Publication1
Binding sitei478Carbonate 2PROSITE-ProRule annotation1
Binding sitei482Carbonate 2PROSITE-ProRule annotation1 Publication1
Binding sitei484Carbonate 2; via amide nitrogenPROSITE-ProRule annotation1
Binding sitei485Carbonate 2; via amide nitrogenPROSITE-ProRule annotation1
Metal bindingi545Iron 2PROSITE-ProRule annotation1 Publication1
Metal bindingi614Iron 2PROSITE-ProRule annotation1

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
OrganismiCamelus dromedarius (Dromedary) (Arabian camel)
Taxonomic identifieri9838 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaTylopodaCamelidaeCamelus

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 peptidei1 – 19By similarityAdd BLAST19
ChainiPRO_000003572920 – 708LactotransferrinAdd BLAST689

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 64
Disulfide bondi38 ↔ 55
Disulfide bondi134 ↔ 217
Disulfide bondi176 ↔ 192
Disulfide bondi179 ↔ 202
Disulfide bondi189 ↔ 200
Disulfide bondi250 ↔ 264
Glycosylationi252N-linked (GlcNAc...)1 Publication1
Disulfide bondi367 ↔ 399
Disulfide bondi377 ↔ 390
Glycosylationi385N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi424 ↔ 703
Disulfide bondi444 ↔ 666
Disulfide bondi476 ↔ 551
Disulfide bondi500 ↔ 694
Disulfide bondi510 ↔ 524
Disulfide bondi521 ↔ 534
Glycosylationi537N-linked (GlcNAc...)1 Publication1
Disulfide bondi592 ↔ 606
Glycosylationi594N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi644 ↔ 649

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ9TUM0.

Interactioni

Subunit structurei

Monomer (By similarity). Found in a complex with LTF, CLU, EPPIN and SEMG1 (By similarity). Interacts with E.coli outer membrane protein C (OmpC).By similarity2 Publications

Structurei

Secondary structure

1708
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 31Combined sources9
Helixi32 – 46Combined sources15
Turni47 – 49Combined sources3
Beta strandi53 – 57Combined sources5
Helixi61 – 69Combined sources9
Beta strandi75 – 78Combined sources4
Helixi80 – 87Combined sources8
Turni89 – 91Combined sources3
Beta strandi93 – 99Combined sources7
Beta strandi104 – 106Combined sources3
Beta strandi108 – 120Combined sources13
Helixi125 – 127Combined sources3
Beta strandi132 – 136Combined sources5
Turni141 – 144Combined sources4
Helixi145 – 150Combined sources6
Helixi152 – 154Combined sources3
Helixi164 – 171Combined sources8
Beta strandi172 – 176Combined sources5
Beta strandi178 – 180Combined sources3
Turni182 – 184Combined sources3
Helixi186 – 189Combined sources4
Helixi196 – 198Combined sources3
Helixi210 – 219Combined sources10
Beta strandi220 – 222Combined sources3
Beta strandi224 – 229Combined sources6
Helixi232 – 236Combined sources5
Helixi240 – 243Combined sources4
Beta strandi246 – 250Combined sources5
Turni251 – 253Combined sources3
Beta strandi254 – 256Combined sources3
Helixi258 – 260Combined sources3
Turni261 – 263Combined sources3
Beta strandi266 – 270Combined sources5
Beta strandi273 – 278Combined sources6
Helixi283 – 297Combined sources15
Beta strandi317 – 319Combined sources3
Beta strandi326 – 328Combined sources3
Helixi335 – 339Combined sources5
Helixi341 – 348Combined sources8
Turni349 – 351Combined sources3
Helixi354 – 362Combined sources9
Beta strandi363 – 370Combined sources8
Helixi371 – 384Combined sources14
Beta strandi387 – 395Combined sources9
Helixi396 – 404Combined sources9
Beta strandi410 – 413Combined sources4
Helixi415 – 422Combined sources8
Turni423 – 425Combined sources3
Beta strandi427 – 434Combined sources8
Turni444 – 446Combined sources3
Beta strandi453 – 461Combined sources9
Turni467 – 472Combined sources6
Beta strandi473 – 478Combined sources6
Turni483 – 493Combined sources11
Beta strandi494 – 497Combined sources4
Beta strandi504 – 510Combined sources7
Beta strandi521 – 523Combined sources3
Turni528 – 530Combined sources3
Helixi544 – 553Combined sources10
Beta strandi558 – 563Combined sources6
Helixi564 – 567Combined sources4
Turni569 – 574Combined sources6
Beta strandi575 – 578Combined sources4
Beta strandi580 – 582Combined sources3
Beta strandi588 – 591Combined sources4
Helixi600 – 605Combined sources6
Beta strandi615 – 618Combined sources4
Turni620 – 622Combined sources3
Helixi623 – 637Combined sources15
Turni642 – 646Combined sources5
Beta strandi654 – 656Combined sources3
Beta strandi664 – 669Combined sources6
Helixi676 – 680Combined sources5
Helixi682 – 692Combined sources11
Helixi698 – 705Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DTZX-ray2.65A20-708[»]
1I6QX-ray2.70A20-708[»]
2J4UX-ray2.99S/X20-64[»]
ProteinModelPortaliQ9TUM0.
SMRiQ9TUM0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9TUM0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 352Transferrin-like 1PROSITE-ProRule annotationAdd BLAST328
Domaini364 – 693Transferrin-like 2PROSITE-ProRule annotationAdd BLAST330

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni44 – 51Interaction with E.coli ompC8

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOVERGENiHBG000055.
OrthoDBiEOG091G0242.

Family and domain databases

InterProiIPR030684. Lactotransferrin.
IPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF500683. Lactotransferrin. 1 hit.
PIRSF002549. 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: Complete.

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

Q9TUM0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLFFPALLS LGALGLCLAA SKKSVRWCTT SPAESSKCAQ WQRRMKKVRG
60 70 80 90 100
PSVTCVKKTS RFECIQAIST EKADAVTLDG GLVYDAGLDP YKLRPIAAEV
110 120 130 140 150
YGTENNPQTH YYAVAIAKKG TNFQLNQLQG LKSCHTGLGR SAGWNIPMGL
160 170 180 190 200
LRPFLDWTGP PEPLQKAVAK FFSASCVPCV DGKEYPNLCQ LCAGTGENKC
210 220 230 240 250
ACSSQEPYFG YSGAFKCLQD GAGDVAFVKD STVFESLPAK ADRDQYELLC
260 270 280 290 300
PNNTRKPVDA FQECHLARVP SHAVVARSVN GKEDLIWKLL VKAQEKFGRG
310 320 330 340 350
KPSGFQLFGS PAGQKDLLFK DSALGLLRIS SKIDSGLYLG SNYITAIRGL
360 370 380 390 400
RETAAEVELR RAQVVWCAVG SDEQLKCQEW SRQSNQSVVC ATASTTEDCI
410 420 430 440 450
ALVLKGEADA LSLDGGYIYI AGKCGLVPVL AESQQSPESS GLDCVHRPVK
460 470 480 490 500
GYLAVAVVRK ANDKITWNSL RGKKSCHTAV DRTAGWNIPM GLLSKNTDSC
510 520 530 540 550
RFDEFLSQSC APGSDPRSKL CALCAGNEEG QNKCVPNSSE RYYGYTGAFR
560 570 580 590 600
CLAENVGDVA FVKDVTVLDN TDGKNTEQWA KDLKLGDFEL LCLNGTRKPV
610 620 630 640 650
TEAESCHLAV APNHAVVSRI DKVAHLEQVL LRQQAHFGRN GRDCPGKFCL
660 670 680 690 700
FQSKTKNLLF NDNTECLAKL QGKTTYEEYL GPQYVTAIAK LRRCSTSPLL

EACAFLMR
Length:708
Mass (Da):77,211
Last modified:May 1, 2000 - v1
Checksum:i0B0C175A0B69D430
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti261F → S in AAF82241 (PubMed:11397094).Curated1
Sequence conflicti304G → A in AAF82241 (PubMed:11397094).Curated1
Sequence conflicti330S → P in AAF82241 (PubMed:11397094).Curated1
Sequence conflicti492 – 494LLS → PLF in AAF82241 (PubMed:11397094).Curated3
Sequence conflicti506L → F in AAF82241 (PubMed:11397094).Curated1
Sequence conflicti609A → P in AAF82241 (PubMed:11397094).Curated1
Sequence conflicti642R → Q in AAF82241 (PubMed:11397094).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131674 mRNA. Translation: CAB53387.1.
AF165879 mRNA. Translation: AAF82241.1.
RefSeqiNP_001290496.1. NM_001303567.1.

Genome annotation databases

GeneIDi105103507.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131674 mRNA. Translation: CAB53387.1.
AF165879 mRNA. Translation: AAF82241.1.
RefSeqiNP_001290496.1. NM_001303567.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DTZX-ray2.65A20-708[»]
1I6QX-ray2.70A20-708[»]
2J4UX-ray2.99S/X20-64[»]
ProteinModelPortaliQ9TUM0.
SMRiQ9TUM0.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS60.001.

Proteomic databases

PRIDEiQ9TUM0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi105103507.

Organism-specific databases

CTDi4057.

Phylogenomic databases

HOVERGENiHBG000055.
OrthoDBiEOG091G0242.

Miscellaneous databases

EvolutionaryTraceiQ9TUM0.

Family and domain databases

InterProiIPR030684. Lactotransferrin.
IPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF500683. Lactotransferrin. 1 hit.
PIRSF002549. 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_CAMDR
AccessioniPrimary (citable) accession number: Q9TUM0
Secondary accession number(s): Q9MZS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 97 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

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.