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Lactotransferrin (Lactoferrin) (EC 3.4.21.-)

 TRFL_CAPHI              Reviewed;         708 AA.
Q29477; Q29479;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 100.
RecName: Full=Lactotransferrin;
Short=Lactoferrin;
EC=3.4.21.-;
Flags: Precursor;
Name=LTF;
Capra hircus (Goat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Capra.
NCBI_TaxID=9925;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary gland;
PubMed=8093048; DOI=10.1006/bbrc.1994.2327;
le Provost F., Nocart M., Guerin G., Martin P.;
"Characterization of the goat lactoferrin cDNA. Assignment of the
relevant locus to bovine U12 synteny group.";
Biochem. Biophys. Res. Commun. 203:1324-1332(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], ANTIBACTERIAL ACTIVITY, AND DEVELOPMENTAL
STAGE.
STRAIN=Korean Native; TISSUE=Mammary gland;
PubMed=9363601; DOI=10.1111/j.1365-2052.1997.00154.x;
Lee T.H., Shimazaki K., Yu S.L., Nam M.S., Kim S.J., Lee K.K.,
Yu D.Y.;
"Polymorphic sequence of Korean Native goat lactoferrin exhibiting
greater antibacterial activity.";
Anim. Genet. 28:367-369(1997).
[3]
X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 20-708 IN COMPLEX WITH IRON.
PubMed=22896884;
Kumar P., Yadav S., Singh T.P.;
"Crystallization and structure determination of goat lactoferrin at
4.0A resolution: A new form of packing in lactoferrins with a high
solvent content in crystals.";
Indian J. Biochem. Biophys. 39:16-21(2002).
-!- FUNCTION: Transferrins are iron binding transport proteins which
can bind two Fe(3+) ions in association with the binding of an
anion, usually bicarbonate.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: 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. Shows a preferential cleavage at -Arg-Ser-
Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-
aminomethylcoumarin sites. {ECO:0000250}.
-!- SUBUNIT: Monomer. Found in a complex with LTF, CLU, EPPIN and
SEMG1. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule {ECO:0000250}.
Note=Secreted into most exocrine fluids by various endothelial
cells. Stored in the secondary granules of neutrophils (By
similarity). {ECO:0000250}.
-!- DEVELOPMENTAL STAGE: 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. {ECO:0000269|PubMed:9363601}.
-!- SIMILARITY: Belongs to the transferrin family.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
-----------------------------------------------------------------------
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EMBL; X78902; CAA55517.1; -; mRNA.
EMBL; U53857; AAA97958.1; -; mRNA.
PIR; JC2323; JC2323.
RefSeq; NP_001272477.1; NM_001285548.1.
UniGene; Chi.6573; -.
PDB; 1JW1; X-ray; 4.00 A; A=20-708.
PDBsum; 1JW1; -.
ProteinModelPortal; Q29477; -.
SMR; Q29477; -.
MEROPS; S60.001; -.
PRIDE; Q29477; -.
GeneID; 100861194; -.
KEGG; chx:100861194; -.
CTD; 4057; -.
HOVERGEN; HBG000055; -.
KO; K17283; -.
OrthoDB; EOG091G0242; -.
EvolutionaryTrace; Q29477; -.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0042581; C:specific granule; ISS:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0019731; P:antibacterial humoral response; ISS:UniProtKB.
GO; GO:0019732; P:antifungal humoral response; ISS:UniProtKB.
GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
GO; GO:0002227; P:innate immune response in mucosa; ISS:UniProtKB.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:2001205; P:negative regulation of osteoclast development; ISS:UniProtKB.
GO; GO:1900229; P:negative regulation of single-species biofilm formation in or on host organism; ISS:UniProtKB.
GO; GO:2000308; P:negative regulation of tumor necrosis factor (ligand) superfamily member 11 production; ISS:UniProtKB.
GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
GO; GO:1900159; P:positive regulation of bone mineralization involved in bone maturation; ISS:UniProtKB.
GO; GO:1902732; P:positive regulation of chondrocyte proliferation; ISS:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
GO; GO:0033690; P:positive regulation of osteoblast proliferation; ISS:UniProtKB.
GO; GO:0001817; P:regulation of cytokine production; ISS:UniProtKB.
GO; GO:0032680; P:regulation of tumor necrosis factor production; ISS:UniProtKB.
InterPro; IPR030684; Lactotransferrin.
InterPro; IPR016357; Transferrin.
InterPro; IPR001156; Transferrin-like_dom.
InterPro; IPR018195; Transferrin_Fe_BS.
PANTHER; PTHR11485:SF33; PTHR11485:SF33; 1.
Pfam; PF00405; Transferrin; 2.
PIRSF; PIRSF002549; Transferrin; 1.
PRINTS; PR00422; TRANSFERRIN.
SMART; SM00094; TR_FER; 2.
PROSITE; PS00205; TRANSFERRIN_LIKE_1; 2.
PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
1: Evidence at protein level;
3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Immunity;
Ion transport; Iron; Iron transport; Metal-binding; Osteogenesis;
Protease; Repeat; Secreted; Serine protease; Signal; Transport.
SIGNAL 1 19 {ECO:0000250}.
CHAIN 20 708 Lactotransferrin.
/FTId=PRO_0000035730.
DOMAIN 25 352 Transferrin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
DOMAIN 364 693 Transferrin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
ACT_SITE 92 92 {ECO:0000255|PROSITE-ProRule:PRU00741}.
ACT_SITE 278 278 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 79 79 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
METAL 111 111 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
METAL 211 211 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
METAL 272 272 Iron 1; via tele nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
METAL 414 414 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
METAL 452 452 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
METAL 545 545 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
METAL 614 614 Iron 2; via tele nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
BINDING 140 140 Carbonate 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 142 142 Carbonate 1; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 143 143 Carbonate 1; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 478 478 Carbonate 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 482 482 Carbonate 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 484 484 Carbonate 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 485 485 Carbonate 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
CARBOHYD 252 252 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 387 387 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 495 495 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 564 564 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 64
DISULFID 38 55
DISULFID 134 217
DISULFID 176 192
DISULFID 179 202
DISULFID 189 200
DISULFID 250 264
DISULFID 367 399
DISULFID 377 390
DISULFID 424 703
DISULFID 444 666
DISULFID 476 551
DISULFID 500 694
DISULFID 510 524
DISULFID 521 534
DISULFID 592 606
DISULFID 644 649
CONFLICT 56 56 I -> V (in Ref. 1; CAA55517).
{ECO:0000305}.
CONFLICT 88 88 L -> R (in Ref. 1; CAA55517).
{ECO:0000305}.
CONFLICT 124 124 Q -> K (in Ref. 1; CAA55517).
{ECO:0000305}.
CONFLICT 154 154 F -> P (in Ref. 1; CAA55517).
{ECO:0000305}.
CONFLICT 304 304 S -> R (in Ref. 1; CAA55517).
{ECO:0000305}.
CONFLICT 414 414 D -> G (in Ref. 1; CAA55517).
{ECO:0000305}.
SEQUENCE 708 AA; 77358 MW; F2EDA3C83539960D CRC64;
MKLFVPALLS LGALGLCLAA PRKNVRWCAI SLPEWSKCYQ WQRRMRKLGA PSITCIRRTS
ALECIRAIAG KNADAVTLDS GMVFEAGLDP YKLRPVAAEI YGTEKSPQTH YYAVAVVKKG
SNFQLDQLQG QKSCHMGLGR SAGWNIPVGI LRPFLSWTES AEPLQGAVAR FFSASCVPCV
DGKAYPNLCQ LCKGVGENKC ACSSQEPYFG YSGAFKCLQD GAGDVAFVKE TTVFENLPEK
ADRDQYELLC LNNTRAPVDA FKECHLAQVP SHAVVARSVD GKENLIWELL RKAQEKFGKN
KSQSFQLFGS PEGRRDLLFK DSALGFVRIP SKVDSALYLG SRYLTALKNL RETAEELKAR
CTRVVWCAVG PEEQSKCQQW SEQSGQNVTC ATASTTDDCI ALVLKGEADA LSLDGGYIYT
AGKCGLVPVM AENRKSSKYS SLDCVLRPTE GYLAVAVVKK ANEGLTWNSL KGKKSCHTAV
DRTAGWNIPM GLIANQTGSC AFDEFFSQSC APGADPKSSL CALCAGDDQG LDKCVPNSKE
KYYGYTGAFR CLAEDVGDVA FVKNDTVWEN TNGESSADWA KNLNREDFRL LCLDGTTKPV
TEAQSCYLAV APNHAVVSRS DRAAHVEQVL LHQQALFGKN GKNCPDQFCL FKSETKNLLF
NDNTECLAKL GGRPTYEKYL GTEYVTAIAN LKKCSTSPLL EACAFLTR


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