| General information | | DisProt: | DP00616 | | Name: | Lactotransferrin | | Synonym(s): | TRFL_HUMAN
Lactoferrin
Talalactoferrin
Kaliocin-1 [cleavage product 1]
Lactoferroxin-A [cleavage product 2]
Lactoferroxin-B [cleavage product 3]
Lactoferroxin-C [cleavage product 4]
| | First appeared in release: | Release 5.1 (05/28/2010) | | UniProt: | P02788 | | UniGene: | Hs.529517 | | SwissProt: | TRFL_HUMAN | | TrEMBL: | | | NCBI (GI): | 85700158 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 710 | | Percent disordered: | 3% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MKLVFLVLLF LGALGLCLAG RRRSVQWCAV SQPEATKCFQ WQRNMRKVRG PPVSCIKRDS - 60
PIQCIQAIAE NRADAVTLDG GFIYEAGLAP YKLRPVAAEV YGTERQPRTH YYAVAVVKKG - 120
GSFQLNELQG LKSCHTGLRR TAGWNVPIGT LRPFLNWTGP PEPIEAAVAR FFSASCVPGA - 180
DKGQFPNLCR LCAGTGENKC AFSSQEPYFS YSGAFKCLRD GAGDVAFIRE STVFEDLSDE - 240
AERDEYELLC PDNTRKPVDK FKDCHLARVP SHAVVARSVN GKEDAIWNLL RQAQEKFGKD - 300
KSPKFQLFGS PSGQKDLLFK DSAIGFSRVP PRIDSGLYLG SGYFTAIQNL RKSEEEVAAR - 360
RARVVWCAVG EQELRKCNQW SGLSEGSVTC SSASTTEDCI ALVLKGEADA MSLDGGYVYT - 420
AGKCGLVPVL AENYKSQQSS DPDPNCVDRP VEGYLAVAVV RRSDTSLTWN SVKGKKSCHT - 480
AVDRTAGWNI PMGLLFNQTG SCKFDEYFSQ SCAPGSDPRS NLCALCIGDE QGENKCVPNS - 540
NERYYGYTGA FRCLAENAGD VAFVKDVTVL QNTDGNNNEA WAKDLKLADF ALLCLDGKRK - 600
PVTEARSCHL AMAPNHAVVS RMDKVERLKQ VLLHQQAKFG RNGSDCPDKF CLFQSETKNL - 660
LFNDNTECLA RLHGKTTYEK YLGPQYVAGI TNLKKCSTSP LLEACEFLRK
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| Functional narrative |
Transferrins are iron binding transport proteins which can bind two Fe3+ 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 and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for 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.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | Cell-penetrating peptide (CPP) | | Location: | 38 - 59 | | Length: | 22 | | Region sequence: |
CFQWQRNMRKVRGPPVSCIKRD | | Modification type: | Fragment
| | PDB: | 1B0L:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Self-transport through channel
| Detection methods:
- Immunochemistry
- Circular dichroism (CD) spectroscopy, far-UV (293 K; CPP 17.5 uM; SDS or DPC (1:570 for micellar solns)) 10 mM)
- Circular dichroism (CD) spectroscopy, far-UV (303 K; hLF peptide 17.5 uM; lipid (1:80 vesicle dispersions) 1.45 mM)
- Nuclear magnetic resonance (NMR) (283 K; H2O/D2O buffer (95:5 v:v) 300 uL; hLF peptide 0.83 mg; NMR performed at 283K and/or 293K )
| References:
- Duchardt F, Ruttekolk IR, Verdurmen WP, Lortat-Jacob H, Burck J, Hufnagel H, Fischer R, van den Heuvel M, Lowik DW, Vuister GW, Ulrich A, de Waard M, Brock R. "A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency." J Biol Chem. 2009; 284(52): 36099-108. PubMed: 19858187
| Comments:CPP mediates protein cargo delivery through cell membrane.
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| References |
- Duchardt F, Ruttekolk IR, Verdurmen WP, Lortat-Jacob H, Burck J, Hufnagel H, Fischer R, van den Heuvel M, Lowik DW, Vuister GW, Ulrich A, de Waard M, Brock R. "A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency." J Biol Chem. 2009; 284(52): 36099-108. PubMed: 19858187
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