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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi79 – 791Iron 1PROSITE-ProRule annotation1 Publication
Active sitei92 – 921PROSITE-ProRule annotation
Metal bindingi111 – 1111Iron 1PROSITE-ProRule annotation1 Publication
Binding sitei140 – 1401Carbonate 1PROSITE-ProRule annotation
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 1; via tele nitrogenPROSITE-ProRule annotation1 Publication
Active sitei278 – 2781NucleophilePROSITE-ProRule annotation
Metal bindingi414 – 4141Iron 2PROSITE-ProRule annotation1 Publication
Metal bindingi452 – 4521Iron 2PROSITE-ProRule annotation1 Publication
Binding sitei478 – 4781Carbonate 2PROSITE-ProRule annotation
Binding sitei482 – 4821Carbonate 2PROSITE-ProRule annotation
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 2; via tele nitrogenPROSITE-ProRule annotation1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 708689LactotransferrinPRO_0000035730Add
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...)Sequence analysis
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence analysis
Disulfide bondi367 ↔ 399
Disulfide bondi377 ↔ 390
Glycosylationi387 – 3871N-linked (GlcNAc...)Sequence analysis
Disulfide bondi424 ↔ 703
Disulfide bondi444 ↔ 666
Disulfide bondi476 ↔ 551
Glycosylationi495 – 4951N-linked (GlcNAc...)Sequence analysis
Disulfide bondi500 ↔ 694
Disulfide bondi510 ↔ 524
Disulfide bondi521 ↔ 534
Glycosylationi564 – 5641N-linked (GlcNAc...)Sequence analysis
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

Secondary structure

1
708
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 327
Turni33 – 353
Helixi38 – 4811
Beta strandi49 – 513
Beta strandi54 – 574
Turni61 – 655
Helixi66 – 694
Turni81 – 877
Beta strandi88 – 914
Beta strandi93 – 953
Beta strandi99 – 1035
Beta strandi106 – 1116
Helixi125 – 1273
Beta strandi129 – 1324
Helixi141 – 1455
Beta strandi149 – 1513
Helixi153 – 1553
Turni159 – 1613
Turni164 – 1663
Beta strandi167 – 1748
Beta strandi178 – 1803
Turni182 – 1843
Beta strandi189 – 1913
Beta strandi206 – 2105
Turni211 – 2133
Helixi216 – 2194
Beta strandi220 – 2234
Beta strandi230 – 2323
Helixi233 – 2364
Beta strandi243 – 2453
Turni261 – 2644
Beta strandi273 – 2819
Helixi283 – 2864
Helixi288 – 2914
Turni292 – 2976
Helixi335 – 3384
Beta strandi341 – 3433
Turni344 – 3485
Helixi349 – 3513
Beta strandi354 – 3585
Turni359 – 3613
Beta strandi364 – 3663
Beta strandi370 – 3723
Turni373 – 3764
Helixi377 – 3793
Turni380 – 3834
Beta strandi384 – 3907
Beta strandi394 – 3985
Helixi399 – 4024
Turni403 – 4064
Helixi416 – 4194
Beta strandi420 – 4256
Turni438 – 4414
Beta strandi452 – 4554
Helixi467 – 4693
Beta strandi477 – 4815
Turni483 – 4864
Helixi487 – 4904
Turni491 – 4977
Helixi502 – 5054
Beta strandi506 – 5083
Beta strandi518 – 5214
Beta strandi527 – 5304
Turni545 – 5506
Turni552 – 5554
Beta strandi561 – 5633
Helixi564 – 5685
Beta strandi569 – 5735
Beta strandi580 – 5823
Helixi585 – 5873
Beta strandi599 – 6013
Turni603 – 6053
Beta strandi608 – 6114
Turni623 – 6264
Helixi627 – 6337
Turni634 – 6363
Turni642 – 6476
Turni654 – 6563
Beta strandi658 – 6603
Beta strandi662 – 6643
Helixi677 – 6804
Helixi682 – 69110
Turni698 – 7014
Beta strandi702 – 7065

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JW1X-ray4.00A20-708[»]
ProteinModelPortaliQ29477.
SMRiQ29477. Positions 20-708.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ29477.

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

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561I → V in CAA55517 (PubMed:8093048).Curated
Sequence conflicti88 – 881L → R in CAA55517 (PubMed:8093048).Curated
Sequence conflicti124 – 1241Q → K in CAA55517 (PubMed:8093048).Curated
Sequence conflicti154 – 1541F → P in CAA55517 (PubMed:8093048).Curated
Sequence conflicti304 – 3041S → R in CAA55517 (PubMed:8093048).Curated
Sequence conflicti414 – 4141D → G in CAA55517 (PubMed:8093048).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1JW1X-ray4.00A20-708[»]
ProteinModelPortaliQ29477.
SMRiQ29477. Positions 20-708.
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: September 7, 2016
This is version 92 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.