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lactotransferrin; lactoferrin; talalactoferrin; contains: kaliocin-1; lactoferroxin-A; lactoferroxin-B; lactoferroxin-C (LTF, LF)
Function:
- transferrins are iron binding transport proteins which can bind two Fe+3 ions in association with the binding of an anion, usually bicarbonate
- lactotransferrin has antimicrobial activity which depends on the extracellular cation concentration
- lactoferroxins A, B & C have opioid antagonist activity
- lactoferroxin A shows preference for opioid mu-receptors
- lactoferroxin B & C have somewhat higher degrees of preference for opioid kappa-receptors than for opioid mu-receptors
- 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
- preferential at -Arg-Ser-Arg-Arg-|- & -Arg-Arg-Ser-Arg-|-, & of Z-Phe-Arg-|-aminomethylcoumarin
Structure:
- monomer
- belongs to the transferrin family
- contains 2 transferrin-like domains
Compartment: secreted
Pathology:
- found associated with amyloid deposits in Alzheimer's disease
General
glycoprotein
metalloprotein
milk protein
phosphoprotein
Properties
SIZE: entity length = 710 aa
MW = 78 kD
COMPARTMENT: lysosome
MOTIF: signal sequence {1-19}
Transferrin-like 1 {25-352}
MOTIF: cysteine residue {C28}
MODIFICATION: cysteine residue {C64}
cysteine residue {C38}
MODIFICATION: cysteine residue {C55}
cysteine residue {C55}
MODIFICATION: cysteine residue {C38}
cysteine residue {C64}
MODIFICATION: cysteine residue {C28}
Iron [Fe]-binding site
SITE: 79-79
lysine residue {K92}
Iron [Fe]-binding site
SITE: 111-111
cysteine residue {C134}
MODIFICATION: cysteine residue {C217}
binding site
SITE: 136-136
FOR-BINDING-OF: Carbonate 1
binding site
SITE: 140-140
FOR-BINDING-OF: Carbonate 1
binding site
SITE: 142-142
FOR-BINDING-OF: Carbonate 1; via amide nitrogen
binding site
SITE: 143-143
FOR-BINDING-OF: Carbonate 1; via amide nitrogen
N-glycosylation site {N156}
cysteine residue {C176}
MODIFICATION: cysteine residue {C192}
cysteine residue {C189}
MODIFICATION: cysteine residue {C200}
cysteine residue {C192}
MODIFICATION: cysteine residue {C176}
cysteine residue {C200}
MODIFICATION: cysteine residue {C189}
Iron [Fe]-binding site
SITE: 211-211
cysteine residue {C217}
MODIFICATION: cysteine residue {C134}
cysteine residue {C250}
MODIFICATION: cysteine residue {C264}
cysteine residue {C264}
MODIFICATION: cysteine residue {C250}
Iron [Fe]-binding site
SITE: 272-272
serine residue {S278}
Transferrin-like 2 {364-695}
MOTIF: cysteine residue {C367}
MODIFICATION: cysteine residue {C399}
cysteine residue {C377}
MODIFICATION: cysteine residue {C390}
cysteine residue {C390}
MODIFICATION: cysteine residue {C377}
cysteine residue {C399}
MODIFICATION: cysteine residue {C367}
Iron [Fe]-binding site
SITE: 414-414
cysteine residue {C424}
MODIFICATION: cysteine residue {C705}
cysteine residue {C446}
MODIFICATION: cysteine residue {C668}
Iron [Fe]-binding site
SITE: 454-454
cysteine residue {C478}
MODIFICATION: cysteine residue {C553}
binding site
SITE: 480-480
FOR-BINDING-OF: Carbonate 2
binding site
SITE: 484-484
FOR-BINDING-OF: Carbonate 2
binding site
SITE: 486-486
FOR-BINDING-OF: Carbonate 2; via amide nitrogen
binding site
SITE: 487-487
FOR-BINDING-OF: Carbonate 2; via amide nitrogen
N-glycosylation site {N497}
cysteine residue {C502}
MODIFICATION: cysteine residue {C696}
cysteine residue {C512}
MODIFICATION: cysteine residue {C526}
cysteine residue {C523}
MODIFICATION: cysteine residue {C536}
cysteine residue {C526}
MODIFICATION: cysteine residue {C512}
cysteine residue {C536}
MODIFICATION: cysteine residue {C523}
Iron [Fe]-binding site
SITE: 547-547
Tyr phosphorylation site {Y547}
cysteine residue {C553}
MODIFICATION: cysteine residue {C478}
cysteine residue {C594}
MODIFICATION: cysteine residue {C608}
cysteine residue {C608}
MODIFICATION: cysteine residue {C594}
Iron [Fe]-binding site
SITE: 616-616
N-glycosylation site {N642}
cysteine residue {C646}
MODIFICATION: cysteine residue {C651}
cysteine residue {C651}
MODIFICATION: cysteine residue {C646}
cysteine residue {C668}
MODIFICATION: cysteine residue {C446}
cysteine residue {C696}
MODIFICATION: cysteine residue {C502}
cysteine residue {C705}
MODIFICATION: cysteine residue {C424}
Database Correlations
OMIM correlations
UniProt P02788
Pfam PF00405
Entrez Gene 4057
Kegg hsa:4057
References
- UniProt :accession P02788
- Kawamata et al Neurosci Abs 1991 #573.15
- Wikipedia; Note: lactotransferrin entry
http://en.wikipedia.org/wiki/lactotransferrin