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Protein

Lactotransferrin

Gene

LTF

Organism
Sus scrofa (Pig)
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).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 bindingi77 – 771Iron 1PROSITE-ProRule annotation
Active sitei88 – 881PROSITE-ProRule annotation
Metal bindingi107 – 1071Iron 1PROSITE-ProRule annotation
Binding sitei132 – 1321Carbonate 1PROSITE-ProRule annotation
Binding sitei136 – 1361Carbonate 1PROSITE-ProRule annotation
Binding sitei138 – 1381Carbonate 1; via amide nitrogenPROSITE-ProRule annotation
Binding sitei139 – 1391Carbonate 1; via amide nitrogenPROSITE-ProRule annotation
Metal bindingi207 – 2071Iron 1PROSITE-ProRule annotation
Metal bindingi268 – 2681Iron 1PROSITE-ProRule annotation
Active sitei274 – 2741NucleophilePROSITE-ProRule annotation
Metal bindingi410 – 4101Iron 2PROSITE-ProRule annotation
Metal bindingi448 – 4481Iron 2PROSITE-ProRule annotation
Binding sitei474 – 4741Carbonate 2PROSITE-ProRule annotation
Binding sitei478 – 4781Carbonate 2PROSITE-ProRule annotation
Binding sitei480 – 4801Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
Binding sitei481 – 4811Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
Metal bindingi541 – 5411Iron 2PROSITE-ProRule annotation
Metal bindingi610 – 6101Iron 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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 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 peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 704685LactotransferrinPRO_0000035738Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 62PROSITE-ProRule annotation
Disulfide bondi38 ↔ 53PROSITE-ProRule annotation
Disulfide bondi130 ↔ 213PROSITE-ProRule annotation
Disulfide bondi172 ↔ 188PROSITE-ProRule annotation
Disulfide bondi185 ↔ 196PROSITE-ProRule annotation
Disulfide bondi246 ↔ 260PROSITE-ProRule annotation
Disulfide bondi363 ↔ 395PROSITE-ProRule annotation
Disulfide bondi373 ↔ 386PROSITE-ProRule annotation
Glycosylationi385 – 3851N-linked (GlcNAc...)Sequence analysis
Disulfide bondi420 ↔ 699PROSITE-ProRule annotation
Disulfide bondi472 ↔ 547PROSITE-ProRule annotation
Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence analysis
Disulfide bondi496 ↔ 690PROSITE-ProRule annotation
Disulfide bondi506 ↔ 520PROSITE-ProRule annotation
Disulfide bondi517 ↔ 530PROSITE-ProRule annotation
Disulfide bondi588 ↔ 602PROSITE-ProRule annotation
Disulfide bondi640 ↔ 645PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP14632.
PRIDEiP14632.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000026769.

Structurei

3D structure databases

ProteinModelPortaliP14632.
SMRiP14632. Positions 20-704.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 348324Transferrin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini360 – 689330Transferrin-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.
HOVERGENiHBG000055.
InParanoidiP14632.
KOiK17283.

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.

P14632-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLFIPALLF LGTLGLCLAA PKKGVRWCVI STAEYSKCRQ WQSKIRRTNP
60 70 80 90 100
MFCIRRASPT DCIRAIAAKR ADAVTLDGGL VFEADQYKLR PVAAEIYGTE
110 120 130 140 150
ENPQTYYYAV AVVKKGFNFQ LNQLQGRKSC HTGLGRSAGW NIPIGLLRRF
160 170 180 190 200
LDWAGPPEPL QKAVAKFFSQ SCVPCADGNA YPNLCQLCIG KGKDKCACSS
210 220 230 240 250
QEPYFGYSGA FNCLHKGIGD VAFVKESTVF ENLPQKADRD KYELLCPDNT
260 270 280 290 300
RKPVEAFREC HLARVPSHAV VARSVNGKEN SIWELLYQSQ KKFGKSNPQE
310 320 330 340 350
FQLFGSPGQQ KDLLFRDATI GFLKIPSKID SKLYLGLPYL TAIQGLRETA
360 370 380 390 400
AEVEARQAKV VWCAVGPEEL RKCRQWSSQS SQNLNCSLAS TTEDCIVQVL
410 420 430 440 450
KGEADAMSLD GGFIYTAGKC GLVPVLAENQ KSRQSSSSDC VHRPTQGYFA
460 470 480 490 500
VAVVRKANGG ITWNSVRGTK SCHTAVDRTA GWNIPMGLLV NQTGSCKFDE
510 520 530 540 550
FFSQSCAPGS QPGSNLCALC VGNDQGVDKC VPNSNERYYG YTGAFRCLAE
560 570 580 590 600
NAGDVAFVKD VTVLDNTNGQ NTEEWARELR SDDFELLCLD GTRKPVTEAQ
610 620 630 640 650
NCHLAVAPSH AVVSRKEKAA QVEQVLLTEQ AQFGRYGKDC PDKFCLFRSE
660 670 680 690 700
TKNLLFNDNT EVLAQLQGKT TYEKYLGSEY VTAIANLKQC SVSPLLEACA

FMMR
Length:704
Mass (Da):77,626
Last modified:December 15, 1998 - v3
Checksum:i93261EFD608AD358
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121G → W in AAA31102 (PubMed:1511016).Curated
Sequence conflicti46 – 483RRT → TTR AA sequence (PubMed:2605266).Curated
Sequence conflicti51 – 511M → I in AAA31102 (PubMed:1511016).Curated
Sequence conflicti85 – 851D → G in AAA31102 (PubMed:1511016).Curated
Sequence conflicti121 – 1211Missing in AAA31059 (PubMed:1503259).Curated
Sequence conflicti132 – 1321T → I in AAA31102 (PubMed:1511016).Curated
Sequence conflicti284 – 2841E → S in AAA31102 (PubMed:1511016).Curated
Sequence conflicti573 – 5731E → Q in AAA31102 (PubMed:1511016).Curated
Sequence conflicti590 – 5901D → N in AAA31102 (PubMed:1511016).Curated
Sequence conflicti625 – 6251V → M in AAA31102 (PubMed:1511016).Curated
Sequence conflicti662 – 6621V → C in AAA31102 (PubMed:1511016).Curated
Sequence conflicti686 – 70419NLKQC…AFMMR → T in AAA31102 (PubMed:1511016).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81327 mRNA. Translation: AAA31059.1.
M92089 mRNA. Translation: AAA31102.1.
PIRiA45543.
RefSeqiNP_999527.1. NM_214362.1.
UniGeneiSsc.11136.
Ssc.13769.

Genome annotation databases

GeneIDi397649.
KEGGissc:397649.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81327 mRNA. Translation: AAA31059.1.
M92089 mRNA. Translation: AAA31102.1.
PIRiA45543.
RefSeqiNP_999527.1. NM_214362.1.
UniGeneiSsc.11136.
Ssc.13769.

3D structure databases

ProteinModelPortaliP14632.
SMRiP14632. Positions 20-704.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000026769.

Protein family/group databases

MEROPSiS60.001.

Proteomic databases

PaxDbiP14632.
PRIDEiP14632.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397649.
KEGGissc:397649.

Organism-specific databases

CTDi4057.

Phylogenomic databases

eggNOGiENOG410IEAI. Eukaryota.
ENOG410XQ36. LUCA.
HOVERGENiHBG000055.
InParanoidiP14632.
KOiK17283.

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...

Publicationsi

  1. "Cloning and sequencing of the porcine lactoferrin cDNA."
    Alexander L.J., Levine W.B., Teng C.T., Beattie C.W.
    Anim. Genet. 23:251-256(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary gland.
  2. "Nucleotide and primary amino acid sequence of porcine lactoferrin."
    Lyndon J.P., O'Malley B.R., Saucedo O., Lee T., Headon D.R., Conneely O.M.
    Biochim. Biophys. Acta 1132:97-99(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary gland.
  3. "Rapid purification of porcine colostral whey lactoferrin by affinity chromatography on single-stranded DNA-agarose. Characterization, amino acid composition and N-terminal amino acid sequence."
    Hutchens T.W., Magnuson J.S., Yip T.-T.
    Biochim. Biophys. Acta 999:323-329(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-49.

Entry informationi

Entry nameiTRFL_PIG
AccessioniPrimary (citable) accession number: P14632
Secondary accession number(s): Q29557
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: December 15, 1998
Last modified: November 11, 2015
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.