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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi79 – 791Iron 1PROSITE-ProRule annotation
Active sitei92 – 921PROSITE-ProRule annotation
Metal bindingi111 – 1111Iron 1PROSITE-ProRule annotation1 Publication
Binding sitei136 – 1361Carbonate 1PROSITE-ProRule annotation
Binding sitei140 – 1401Carbonate 1PROSITE-ProRule annotation1 Publication
Binding sitei142 – 1421Carbonate 1; via amide nitrogenPROSITE-ProRule annotation
Binding sitei143 – 1431Carbonate 1; via amide nitrogenPROSITE-ProRule annotation
Metal bindingi211 – 2111Iron 1PROSITE-ProRule annotation1 Publication
Metal bindingi272 – 2721Iron 1PROSITE-ProRule annotation
Active sitei278 – 2781NucleophilePROSITE-ProRule annotation
Metal bindingi414 – 4141Iron 2PROSITE-ProRule annotation
Metal bindingi452 – 4521Iron 2PROSITE-ProRule annotation1 Publication
Binding sitei478 – 4781Carbonate 2PROSITE-ProRule annotation
Binding sitei482 – 4821Carbonate 2PROSITE-ProRule annotation1 Publication
Binding sitei484 – 4841Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
Binding sitei485 – 4851Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
Metal bindingi545 – 5451Iron 2PROSITE-ProRule annotation1 Publication
Metal bindingi614 – 6141Iron 2PROSITE-ProRule annotation

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 708689LactotransferrinPRO_0000035729Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 64
Disulfide bondi38 ↔ 55
Disulfide bondi134 ↔ 217
Disulfide bondi176 ↔ 192
Disulfide bondi179 ↔ 202
Disulfide bondi189 ↔ 200
Disulfide bondi250 ↔ 264
Glycosylationi252 – 2521N-linked (GlcNAc...)1 Publication
Disulfide bondi367 ↔ 399
Disulfide bondi377 ↔ 390
Glycosylationi385 – 3851N-linked (GlcNAc...)Sequence analysis
Disulfide bondi424 ↔ 703
Disulfide bondi444 ↔ 666
Disulfide bondi476 ↔ 551
Disulfide bondi500 ↔ 694
Disulfide bondi510 ↔ 524
Disulfide bondi521 ↔ 534
Glycosylationi537 – 5371N-linked (GlcNAc...)1 Publication
Disulfide bondi592 ↔ 606
Glycosylationi594 – 5941N-linked (GlcNAc...)Sequence analysis
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

1
708
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 319Combined sources
Helixi32 – 4615Combined sources
Turni47 – 493Combined sources
Beta strandi53 – 575Combined sources
Helixi61 – 699Combined sources
Beta strandi75 – 784Combined sources
Helixi80 – 878Combined sources
Turni89 – 913Combined sources
Beta strandi93 – 997Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi108 – 12013Combined sources
Helixi125 – 1273Combined sources
Beta strandi132 – 1365Combined sources
Turni141 – 1444Combined sources
Helixi145 – 1506Combined sources
Helixi152 – 1543Combined sources
Helixi164 – 1718Combined sources
Beta strandi172 – 1765Combined sources
Beta strandi178 – 1803Combined sources
Turni182 – 1843Combined sources
Helixi186 – 1894Combined sources
Helixi196 – 1983Combined sources
Helixi210 – 21910Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi224 – 2296Combined sources
Helixi232 – 2365Combined sources
Helixi240 – 2434Combined sources
Beta strandi246 – 2505Combined sources
Turni251 – 2533Combined sources
Beta strandi254 – 2563Combined sources
Helixi258 – 2603Combined sources
Turni261 – 2633Combined sources
Beta strandi266 – 2705Combined sources
Beta strandi273 – 2786Combined sources
Helixi283 – 29715Combined sources
Beta strandi317 – 3193Combined sources
Beta strandi326 – 3283Combined sources
Helixi335 – 3395Combined sources
Helixi341 – 3488Combined sources
Turni349 – 3513Combined sources
Helixi354 – 3629Combined sources
Beta strandi363 – 3708Combined sources
Helixi371 – 38414Combined sources
Beta strandi387 – 3959Combined sources
Helixi396 – 4049Combined sources
Beta strandi410 – 4134Combined sources
Helixi415 – 4228Combined sources
Turni423 – 4253Combined sources
Beta strandi427 – 4348Combined sources
Turni444 – 4463Combined sources
Beta strandi453 – 4619Combined sources
Turni467 – 4726Combined sources
Beta strandi473 – 4786Combined sources
Turni483 – 49311Combined sources
Beta strandi494 – 4974Combined sources
Beta strandi504 – 5107Combined sources
Beta strandi521 – 5233Combined sources
Turni528 – 5303Combined sources
Helixi544 – 55310Combined sources
Beta strandi558 – 5636Combined sources
Helixi564 – 5674Combined sources
Turni569 – 5746Combined sources
Beta strandi575 – 5784Combined sources
Beta strandi580 – 5823Combined sources
Beta strandi588 – 5914Combined sources
Helixi600 – 6056Combined sources
Beta strandi615 – 6184Combined sources
Turni620 – 6223Combined sources
Helixi623 – 63715Combined sources
Turni642 – 6465Combined sources
Beta strandi654 – 6563Combined sources
Beta strandi664 – 6696Combined sources
Helixi676 – 6805Combined sources
Helixi682 – 69211Combined sources
Helixi698 – 7058Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DTZX-ray2.65A20-708[»]
1I6QX-ray2.70A20-708[»]
2J4UX-ray2.99S/X20-64[»]
ProteinModelPortaliQ9TUM0.
SMRiQ9TUM0. Positions 20-708.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9TUM0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 352328Transferrin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini364 – 693330Transferrin-like 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 518Interaction with E.coli ompC

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti261 – 2611F → S in AAF82241 (PubMed:11397094).Curated
Sequence conflicti304 – 3041G → A in AAF82241 (PubMed:11397094).Curated
Sequence conflicti330 – 3301S → P in AAF82241 (PubMed:11397094).Curated
Sequence conflicti492 – 4943LLS → PLF in AAF82241 (PubMed:11397094).Curated
Sequence conflicti506 – 5061L → F in AAF82241 (PubMed:11397094).Curated
Sequence conflicti609 – 6091A → P in AAF82241 (PubMed:11397094).Curated
Sequence conflicti642 – 6421R → Q in AAF82241 (PubMed:11397094).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1DTZX-ray2.65A20-708[»]
1I6QX-ray2.70A20-708[»]
2J4UX-ray2.99S/X20-64[»]
ProteinModelPortaliQ9TUM0.
SMRiQ9TUM0. Positions 20-708.
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: September 7, 2016
This is version 95 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.