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Protein

Lactotransferrin

Gene

LTF

Organism
Capra hircus (Goat)
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. 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 (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 Publication1
Active sitei92PROSITE-ProRule annotation1
Metal bindingi111Iron 1PROSITE-ProRule annotation1 Publication1
Binding sitei140Carbonate 1PROSITE-ProRule annotation1
Binding sitei142Carbonate 1; via amide nitrogenPROSITE-ProRule annotation1
Binding sitei143Carbonate 1; via amide nitrogenPROSITE-ProRule annotation1
Metal bindingi211Iron 1PROSITE-ProRule annotation1 Publication1
Metal bindingi272Iron 1; via tele nitrogenPROSITE-ProRule annotation1 Publication1
Active sitei278NucleophilePROSITE-ProRule annotation1
Metal bindingi414Iron 2PROSITE-ProRule annotation1 Publication1
Metal bindingi452Iron 2PROSITE-ProRule annotation1 Publication1
Binding sitei478Carbonate 2PROSITE-ProRule annotation1
Binding sitei482Carbonate 2PROSITE-ProRule annotation1
Binding sitei484Carbonate 2; via amide nitrogenPROSITE-ProRule annotation1
Binding sitei485Carbonate 2; via amide nitrogenPROSITE-ProRule annotation1
Metal bindingi545Iron 2PROSITE-ProRule annotation1 Publication1
Metal bindingi614Iron 2; via tele nitrogenPROSITE-ProRule annotation1 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
OrganismiCapra hircus (Goat)
Taxonomic identifieri9925 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

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_000003573020 – 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...)Sequence analysis1
Glycosylationi300N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi367 ↔ 399
Disulfide bondi377 ↔ 390
Glycosylationi387N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi424 ↔ 703
Disulfide bondi444 ↔ 666
Disulfide bondi476 ↔ 551
Glycosylationi495N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi500 ↔ 694
Disulfide bondi510 ↔ 524
Disulfide bondi521 ↔ 534
Glycosylationi564N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi592 ↔ 606
Disulfide bondi644 ↔ 649

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ29477.

Expressioni

Developmental stagei

Expressed in mammary glands at various stages of development, with weak expression detected in virgin goats and during pregnancy and lactation and high expression detected at the stage of involution.1 Publication

Interactioni

Subunit structurei

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

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JW1X-ray4.00A20-708[»]
ProteinModelPortaliQ29477.
SMRiQ29477.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ29477.

Family & Domainsi

Domains and Repeats

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

HOVERGENiHBG000055.
KOiK17283.
OrthoDBiEOG091G0242.

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: Complete.

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

Q29477-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLFVPALLS LGALGLCLAA PRKNVRWCAI SLPEWSKCYQ WQRRMRKLGA
60 70 80 90 100
PSITCIRRTS ALECIRAIAG KNADAVTLDS GMVFEAGLDP YKLRPVAAEI
110 120 130 140 150
YGTEKSPQTH YYAVAVVKKG SNFQLDQLQG QKSCHMGLGR SAGWNIPVGI
160 170 180 190 200
LRPFLSWTES AEPLQGAVAR FFSASCVPCV DGKAYPNLCQ LCKGVGENKC
210 220 230 240 250
ACSSQEPYFG YSGAFKCLQD GAGDVAFVKE TTVFENLPEK ADRDQYELLC
260 270 280 290 300
LNNTRAPVDA FKECHLAQVP SHAVVARSVD GKENLIWELL RKAQEKFGKN
310 320 330 340 350
KSQSFQLFGS PEGRRDLLFK DSALGFVRIP SKVDSALYLG SRYLTALKNL
360 370 380 390 400
RETAEELKAR CTRVVWCAVG PEEQSKCQQW SEQSGQNVTC ATASTTDDCI
410 420 430 440 450
ALVLKGEADA LSLDGGYIYT AGKCGLVPVM AENRKSSKYS SLDCVLRPTE
460 470 480 490 500
GYLAVAVVKK ANEGLTWNSL KGKKSCHTAV DRTAGWNIPM GLIANQTGSC
510 520 530 540 550
AFDEFFSQSC APGADPKSSL CALCAGDDQG LDKCVPNSKE KYYGYTGAFR
560 570 580 590 600
CLAEDVGDVA FVKNDTVWEN TNGESSADWA KNLNREDFRL LCLDGTTKPV
610 620 630 640 650
TEAQSCYLAV APNHAVVSRS DRAAHVEQVL LHQQALFGKN GKNCPDQFCL
660 670 680 690 700
FKSETKNLLF NDNTECLAKL GGRPTYEKYL GTEYVTAIAN LKKCSTSPLL

EACAFLTR
Length:708
Mass (Da):77,358
Last modified:November 1, 1996 - v1
Checksum:iF2EDA3C83539960D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti56I → V in CAA55517 (PubMed:8093048).Curated1
Sequence conflicti88L → R in CAA55517 (PubMed:8093048).Curated1
Sequence conflicti124Q → K in CAA55517 (PubMed:8093048).Curated1
Sequence conflicti154F → P in CAA55517 (PubMed:8093048).Curated1
Sequence conflicti304S → R in CAA55517 (PubMed:8093048).Curated1
Sequence conflicti414D → G in CAA55517 (PubMed:8093048).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78902 mRNA. Translation: CAA55517.1.
U53857 mRNA. Translation: AAA97958.1.
PIRiJC2323.
RefSeqiNP_001272477.1. NM_001285548.1.
UniGeneiChi.6573.

Genome annotation databases

GeneIDi100861194.
KEGGichx:100861194.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78902 mRNA. Translation: CAA55517.1.
U53857 mRNA. Translation: AAA97958.1.
PIRiJC2323.
RefSeqiNP_001272477.1. NM_001285548.1.
UniGeneiChi.6573.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JW1X-ray4.00A20-708[»]
ProteinModelPortaliQ29477.
SMRiQ29477.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS60.001.

Proteomic databases

PRIDEiQ29477.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100861194.
KEGGichx:100861194.

Organism-specific databases

CTDi4057.

Phylogenomic databases

HOVERGENiHBG000055.
KOiK17283.
OrthoDBiEOG091G0242.

Miscellaneous databases

EvolutionaryTraceiQ29477.

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_CAPHI
AccessioniPrimary (citable) accession number: Q29477
Secondary accession number(s): Q29479
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 94 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.