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Lactotransferrin (Lactoferrin) (EC 3.4.21.-)

 TRFL_PIG                Reviewed;         704 AA.
P14632; Q29557;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 3.
25-OCT-2017, entry version 114.
RecName: Full=Lactotransferrin;
Short=Lactoferrin;
EC=3.4.21.-;
Flags: Precursor;
Name=LTF;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary gland;
PubMed=1503259;
Alexander L.J., Levine W.B., Teng C.T., Beattie C.W.;
"Cloning and sequencing of the porcine lactoferrin cDNA.";
Anim. Genet. 23:251-256(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary gland;
PubMed=1511016; DOI=10.1016/0167-4781(92)90061-4;
Lyndon J.P., O'Malley B.R., Saucedo O., Lee T., Headon D.R.,
Conneely O.M.;
"Nucleotide and primary amino acid sequence of porcine lactoferrin.";
Biochim. Biophys. Acta 1132:97-99(1992).
[3]
PROTEIN SEQUENCE OF 20-49.
PubMed=2605266;
Hutchens T.W., Magnuson J.S., Yip T.-T.;
"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.";
Biochim. Biophys. Acta 999:323-329(1989).
-!- 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. 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). {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 (By similarity). {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}.
-!- SIMILARITY: Belongs to the transferrin family.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
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EMBL; M81327; AAA31059.1; -; mRNA.
EMBL; M92089; AAA31102.1; -; mRNA.
PIR; A45543; A45543.
RefSeq; NP_999527.1; NM_214362.1.
UniGene; Ssc.11136; -.
UniGene; Ssc.13769; -.
ProteinModelPortal; P14632; -.
SMR; P14632; -.
STRING; 9823.ENSSSCP00000026769; -.
MEROPS; S60.001; -.
PaxDb; P14632; -.
PeptideAtlas; P14632; -.
PRIDE; P14632; -.
GeneID; 397649; -.
KEGG; ssc:397649; -.
CTD; 4057; -.
eggNOG; ENOG410IEAI; Eukaryota.
eggNOG; ENOG410XQ36; LUCA.
HOVERGEN; HBG000055; -.
InParanoid; P14632; -.
KO; K17283; -.
Proteomes; UP000008227; Unplaced.
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; PIRSF500683; Lactotransferrin; 1.
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;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hydrolase; Immunity; Ion transport; Iron;
Iron transport; Metal-binding; Osteogenesis; Protease;
Reference proteome; Repeat; Secreted; Serine protease; Signal;
Transport.
SIGNAL 1 19 {ECO:0000269|PubMed:2605266}.
CHAIN 20 704 Lactotransferrin.
/FTId=PRO_0000035738.
DOMAIN 25 348 Transferrin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
DOMAIN 360 689 Transferrin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
ACT_SITE 88 88 {ECO:0000255|PROSITE-ProRule:PRU00741}.
ACT_SITE 274 274 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 77 77 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 107 107 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 207 207 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 268 268 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 410 410 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 448 448 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 541 541 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 610 610 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 132 132 Carbonate 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 136 136 Carbonate 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 138 138 Carbonate 1; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 139 139 Carbonate 1; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 474 474 Carbonate 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 478 478 Carbonate 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 480 480 Carbonate 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 481 481 Carbonate 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
CARBOHYD 385 385 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 491 491 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 62 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 38 53 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 130 213 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 172 188 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 185 196 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 246 260 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 363 395 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 373 386 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 420 699 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 472 547 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 496 690 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 506 520 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 517 530 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 588 602 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 640 645 {ECO:0000255|PROSITE-ProRule:PRU00741}.
CONFLICT 12 12 G -> W (in Ref. 2; AAA31102).
{ECO:0000305}.
CONFLICT 46 48 RRT -> TTR (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 51 51 M -> I (in Ref. 2; AAA31102).
{ECO:0000305}.
CONFLICT 85 85 D -> G (in Ref. 2; AAA31102).
{ECO:0000305}.
CONFLICT 121 121 Missing (in Ref. 1; AAA31059).
{ECO:0000305}.
CONFLICT 132 132 T -> I (in Ref. 2; AAA31102).
{ECO:0000305}.
CONFLICT 284 284 E -> S (in Ref. 2; AAA31102).
{ECO:0000305}.
CONFLICT 573 573 E -> Q (in Ref. 2; AAA31102).
{ECO:0000305}.
CONFLICT 590 590 D -> N (in Ref. 2; AAA31102).
{ECO:0000305}.
CONFLICT 625 625 V -> M (in Ref. 2; AAA31102).
{ECO:0000305}.
CONFLICT 662 662 V -> C (in Ref. 2; AAA31102).
{ECO:0000305}.
CONFLICT 686 704 NLKQCSVSPLLEACAFMMR -> T (in Ref. 2;
AAA31102). {ECO:0000305}.
SEQUENCE 704 AA; 77626 MW; 93261EFD608AD358 CRC64;
MKLFIPALLF LGTLGLCLAA PKKGVRWCVI STAEYSKCRQ WQSKIRRTNP MFCIRRASPT
DCIRAIAAKR ADAVTLDGGL VFEADQYKLR PVAAEIYGTE ENPQTYYYAV AVVKKGFNFQ
LNQLQGRKSC HTGLGRSAGW NIPIGLLRRF LDWAGPPEPL QKAVAKFFSQ SCVPCADGNA
YPNLCQLCIG KGKDKCACSS QEPYFGYSGA FNCLHKGIGD VAFVKESTVF ENLPQKADRD
KYELLCPDNT RKPVEAFREC HLARVPSHAV VARSVNGKEN SIWELLYQSQ KKFGKSNPQE
FQLFGSPGQQ KDLLFRDATI GFLKIPSKID SKLYLGLPYL TAIQGLRETA AEVEARQAKV
VWCAVGPEEL RKCRQWSSQS SQNLNCSLAS TTEDCIVQVL KGEADAMSLD GGFIYTAGKC
GLVPVLAENQ KSRQSSSSDC VHRPTQGYFA VAVVRKANGG ITWNSVRGTK SCHTAVDRTA
GWNIPMGLLV NQTGSCKFDE FFSQSCAPGS QPGSNLCALC VGNDQGVDKC VPNSNERYYG
YTGAFRCLAE NAGDVAFVKD VTVLDNTNGQ NTEEWARELR SDDFELLCLD GTRKPVTEAQ
NCHLAVAPSH AVVSRKEKAA QVEQVLLTEQ AQFGRYGKDC PDKFCLFRSE TKNLLFNDNT
EVLAQLQGKT TYEKYLGSEY VTAIANLKQC SVSPLLEACA FMMR


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