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Protein

Lactotransferrin

Gene

LTF

Organism
Bos taurus (Bovine)
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.
Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria.
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.

Catalytic activityi

Preferential at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin.

Enzyme regulationi

Inhibited by PMSF and Pefabloc.

Kineticsi

  1. KM=50 µM for Z-Phe-Arg-|-aminomethylcoumarin1 Publication

    pH dependencei

    Optimum pH is 7.5.1 Publication

    Temperature dependencei

    Optimum temperature is 25 degrees Celsius.1 Publication

    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 sitei136 – 1361Carbonate 1
    Binding sitei140 – 1401Carbonate 1PROSITE-ProRule annotation1 Publication
    Binding sitei142 – 1421Carbonate 1; via amide nitrogen
    Binding sitei143 – 1431Carbonate 1; via amide nitrogen
    Metal bindingi211 – 2111Iron 1PROSITE-ProRule annotation1 Publication
    Metal bindingi272 – 2721Iron 1PROSITE-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 2
    Binding sitei482 – 4821Carbonate 2PROSITE-ProRule annotation1 Publication
    Binding sitei484 – 4841Carbonate 2; via amide nitrogen
    Binding sitei485 – 4851Carbonate 2; via amide nitrogen
    Metal bindingi545 – 5451Iron 2PROSITE-ProRule annotation1 Publication
    Metal bindingi614 – 6141Iron 2PROSITE-ProRule annotation1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Immunity, Ion transport, Iron transport, Osteogenesis, Transport

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiR-BTA-1222556. ROS, RNS production in response to bacteria.
    SABIO-RKP24627.

    Protein family/group databases

    MEROPSiS60.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lactotransferrin (EC:3.4.21.-)
    Short name:
    Lactoferrin
    Cleaved into the following chain:
    Lactoferricin-B
    Short name:
    Lfcin-B
    Gene namesi
    Name:LTF
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    Proteomesi
    • UP000009136 Componenti: Chromosome 22

    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

    Pathology & Biotechi

    Protein family/group databases

    Allergomei1065. Bos d LF.

    Chemistry

    ChEMBLiCHEMBL2796.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 708689LactotransferrinPRO_0000035726Add
    BLAST
    Peptidei36 – 6025Lactoferricin-BPRO_0000035727Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 64PROSITE-ProRule annotation
    Disulfide bondi38 ↔ 55
    Disulfide bondi134 ↔ 217PROSITE-ProRule annotation
    Disulfide bondi176 ↔ 192PROSITE-ProRule annotation
    Disulfide bondi189 ↔ 200PROSITE-ProRule annotation
    Disulfide bondi250 ↔ 264PROSITE-ProRule annotation
    Glycosylationi252 – 2521N-linked (GlcNAc...)CAR_000186
    Disulfide bondi367 ↔ 399PROSITE-ProRule annotation
    Disulfide bondi377 ↔ 390PROSITE-ProRule annotation
    Glycosylationi387 – 3871N-linked (GlcNAc...)
    Disulfide bondi424 ↔ 703PROSITE-ProRule annotation
    Disulfide bondi444 ↔ 666PROSITE-ProRule annotation
    Disulfide bondi476 ↔ 551PROSITE-ProRule annotation
    Glycosylationi495 – 4951N-linked (GlcNAc...)CAR_000197
    Disulfide bondi500 ↔ 694PROSITE-ProRule annotation
    Disulfide bondi510 ↔ 524PROSITE-ProRule annotation
    Disulfide bondi521 ↔ 534PROSITE-ProRule annotation
    Glycosylationi564 – 5641N-linked (GlcNAc...)CAR_000198
    Disulfide bondi592 ↔ 606PROSITE-ProRule annotation
    Disulfide bondi644 ↔ 649PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP24627.
    PRIDEiP24627.

    PTM databases

    UniCarbKBiP24627.

    Miscellaneous databases

    PMAP-CutDBP24627.

    Expressioni

    Gene expression databases

    ExpressionAtlasiP24627. baseline and differential.

    Interactioni

    Subunit structurei

    Monomer. Found in a complex with LTF, CLU, EPPIN and SEMG1 (By similarity).By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P279583EBI-8076910,EBI-6904269From a different organism.

    GO - Molecular functioni

    • receptor binding Source: AgBase

    Protein-protein interaction databases

    BioGridi158240. 1 interaction.
    IntActiP24627. 4 interactions.
    STRINGi9913.ENSBTAP00000001704.

    Structurei

    Secondary structure

    1
    708
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 317Combined sources
    Helixi32 – 4514Combined sources
    Helixi46 – 483Combined sources
    Beta strandi53 – 575Combined sources
    Helixi61 – 699Combined sources
    Beta strandi75 – 784Combined sources
    Helixi80 – 878Combined sources
    Turni89 – 913Combined sources
    Beta strandi93 – 10210Combined sources
    Beta strandi104 – 12017Combined sources
    Beta strandi133 – 1364Combined sources
    Turni141 – 1444Combined sources
    Helixi145 – 15511Combined sources
    Turni159 – 1613Combined sources
    Helixi164 – 1696Combined sources
    Beta strandi172 – 1765Combined sources
    Turni182 – 1843Combined sources
    Helixi186 – 1883Combined sources
    Helixi210 – 21910Combined sources
    Beta strandi224 – 2296Combined sources
    Helixi232 – 2365Combined sources
    Helixi240 – 2434Combined sources
    Beta strandi246 – 2483Combined sources
    Turni261 – 2633Combined sources
    Beta strandi266 – 2705Combined sources
    Beta strandi273 – 2808Combined sources
    Helixi283 – 29614Combined sources
    Turni298 – 3003Combined sources
    Beta strandi325 – 3284Combined sources
    Helixi335 – 35117Combined sources
    Helixi354 – 3629Combined sources
    Beta strandi364 – 3696Combined sources
    Helixi370 – 38314Combined sources
    Turni384 – 3863Combined sources
    Beta strandi387 – 3959Combined sources
    Helixi396 – 4049Combined sources
    Beta strandi410 – 4134Combined sources
    Helixi415 – 4239Combined sources
    Beta strandi427 – 4348Combined sources
    Beta strandi437 – 4393Combined sources
    Beta strandi440 – 4423Combined sources
    Helixi444 – 4463Combined sources
    Beta strandi452 – 4598Combined sources
    Helixi467 – 4693Combined sources
    Beta strandi474 – 4785Combined sources
    Turni483 – 4864Combined sources
    Helixi487 – 49711Combined sources
    Helixi502 – 5043Combined sources
    Beta strandi505 – 5106Combined sources
    Helixi519 – 5213Combined sources
    Beta strandi527 – 5304Combined sources
    Turni531 – 5344Combined sources
    Helixi544 – 55310Combined sources
    Beta strandi558 – 5636Combined sources
    Helixi564 – 5696Combined sources
    Beta strandi571 – 5755Combined sources
    Turni578 – 5825Combined sources
    Helixi585 – 5873Combined sources
    Beta strandi588 – 5914Combined sources
    Beta strandi597 – 5993Combined sources
    Helixi600 – 6056Combined sources
    Beta strandi608 – 6114Combined sources
    Beta strandi615 – 6184Combined sources
    Helixi620 – 63718Combined sources
    Beta strandi638 – 6403Combined sources
    Turni642 – 6476Combined sources
    Beta strandi653 – 6564Combined sources
    Beta strandi658 – 6603Combined sources
    Beta strandi664 – 6685Combined sources
    Beta strandi671 – 6733Combined sources
    Helixi676 – 6805Combined sources
    Helixi682 – 69211Combined sources
    Helixi698 – 7036Combined sources
    Helixi704 – 7074Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BLFX-ray2.80A20-708[»]
    1LFCNMR-A36-60[»]
    1NKXX-ray1.90A361-708[»]
    1SDXX-ray2.06A361-695[»]
    E700-704[»]
    1Y58NMR-A38-49[»]
    2ALUX-ray2.09A361-708[»]
    2AYSX-ray1.86A361-708[»]
    2B65X-ray1.50A361-705[»]
    2DOJX-ray2.40A361-705[»]
    2DP8X-ray2.50A361-705[»]
    2DQVX-ray2.70A361-705[»]
    2DS9X-ray2.80A361-705[»]
    2DSFX-ray2.80A361-705[»]
    2DVCX-ray3.00A361-705[»]
    2DWAX-ray2.07A361-705[»]
    2DWHX-ray2.80A361-705[»]
    2DWIX-ray2.20A361-705[»]
    2DWJX-ray2.30A361-705[»]
    2DXRX-ray2.85A361-705[»]
    2DXYX-ray2.03A361-705[»]
    2DYXX-ray2.00A361-705[»]
    2E0SX-ray2.15A361-705[»]
    2E1SX-ray2.70A361-705[»]
    2FA7X-ray2.38A361-705[»]
    2G93X-ray1.90A361-705[»]
    2H4IX-ray2.55A361-705[»]
    2HCAX-ray2.80A361-705[»]
    2MD1NMR-A287-303[»]
    2MD2NMR-A287-296[»]
    2MD3NMR-A296-303[»]
    2MD4NMR-A287-298[»]
    2NUVX-ray2.25A361-705[»]
    2NWJX-ray2.25A361-705[»]
    2O1LX-ray1.97A361-705[»]
    2O51X-ray3.00A361-705[»]
    2OCUX-ray2.38A361-705[»]
    2P1SX-ray1.93A361-704[»]
    2PX1X-ray2.50A361-705[»]
    2Q8JX-ray2.71A361-708[»]
    2QJEX-ray2.30A361-708[»]
    2R71X-ray2.07A361-705[»]
    2R9JX-ray2.55A361-705[»]
    2ZMBX-ray2.90A361-705[»]
    3CFLX-ray2.25A361-705[»]
    3CI8X-ray2.40A361-705[»]
    3CRBX-ray2.60A361-705[»]
    3E9XX-ray2.70A361-705[»]
    3IAZX-ray2.00A361-705[»]
    3IB0X-ray1.40A361-705[»]
    3IB1X-ray2.20A361-705[»]
    3IB2X-ray2.29A361-705[»]
    3K0VX-ray1.91A361-705[»]
    3KJ7X-ray1.91A361-705[»]
    3MJNX-ray2.38A361-705[»]
    3O97X-ray2.68A361-705[»]
    3RGYX-ray2.00A361-705[»]
    3SDFX-ray2.10A361-705[»]
    3TAJX-ray1.70A361-705[»]
    3TODX-ray1.38A361-695[»]
    B700-705[»]
    3TTRX-ray2.27A361-705[»]
    3TUSX-ray2.50A361-705[»]
    3U72X-ray2.20A361-695[»]
    B700-705[»]
    3U8QX-ray1.97A361-695[»]
    B700-705[»]
    3UGWX-ray1.87A361-695[»]
    B700-705[»]
    3UK4X-ray1.98A361-695[»]
    B700-705[»]
    3USDX-ray2.40A361-695[»]
    B700-705[»]
    3V5AX-ray1.44A361-695[»]
    B700-705[»]
    3VDFX-ray1.46A361-695[»]
    B700-705[»]
    4DIGX-ray1.80A361-695[»]
    B700-705[»]
    4DXUX-ray1.46A361-695[»]
    B700-705[»]
    4FIMX-ray1.80A361-695[»]
    B700-705[»]
    4FJPX-ray1.68A361-695[»]
    B700-705[»]
    4FORX-ray1.58A361-695[»]
    B700-705[»]
    4G2ZX-ray1.90A361-695[»]
    B700-705[»]
    4G77X-ray1.98A361-705[»]
    4G8HX-ray1.88A361-705[»]
    4GRKX-ray1.68A361-695[»]
    B700-705[»]
    4N6PX-ray1.40A361-695[»]
    B700-705[»]
    4NEDX-ray2.10A361-705[»]
    4OQOX-ray2.42A/B361-708[»]
    5CRYX-ray2.79A/B361-708[»]
    5HBCX-ray2.79A/B361-708[»]
    ProteinModelPortaliP24627.
    SMRiP24627. Positions 24-708.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24627.

    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

    eggNOGiENOG410IEAI. Eukaryota.
    ENOG410XQ36. LUCA.
    GeneTreeiENSGT00390000001619.
    HOGENOMiHOG000043759.
    HOVERGENiHBG000055.
    InParanoidiP24627.
    KOiK17283.
    OMAiRPVEGYL.
    OrthoDBiEOG7D59N7.
    TreeFamiTF324013.

    Family and domain databases

    InterProiIPR030684. Lactotransferrin.
    IPR016357. Transferrin.
    IPR001156. Transferrin-like_dom.
    IPR018195. Transferrin_Fe_BS.
    [Graphical view]
    PfamiPF00405. Transferrin. 2 hits.
    [Graphical view]
    PIRSFiPIRSF500683. Lactotransferrin. 1 hit.
    PIRSF002549. 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.

    P24627-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKLFVPALLS LGALGLCLAA PRKNVRWCTI SQPEWFKCRR WQWRMKKLGA
    60 70 80 90 100
    PSITCVRRAF ALECIRAIAE KKADAVTLDG GMVFEAGRDP YKLRPVAAEI
    110 120 130 140 150
    YGTKESPQTH YYAVAVVKKG SNFQLDQLQG RKSCHTGLGR SAGWIIPMGI
    160 170 180 190 200
    LRPYLSWTES LEPLQGAVAK FFSASCVPCI DRQAYPNLCQ LCKGEGENQC
    210 220 230 240 250
    ACSSREPYFG YSGAFKCLQD GAGDVAFVKE TTVFENLPEK ADRDQYELLC
    260 270 280 290 300
    LNNSRAPVDA FKECHLAQVP SHAVVARSVD GKEDLIWKLL SKAQEKFGKN
    310 320 330 340 350
    KSRSFQLFGS PPGQRDLLFK DSALGFLRIP SKVDSALYLG SRYLTTLKNL
    360 370 380 390 400
    RETAEEVKAR YTRVVWCAVG PEEQKKCQQW SQQSGQNVTC ATASTTDDCI
    410 420 430 440 450
    VLVLKGEADA LNLDGGYIYT AGKCGLVPVL AENRKSSKHS SLDCVLRPTE
    460 470 480 490 500
    GYLAVAVVKK ANEGLTWNSL KDKKSCHTAV DRTAGWNIPM GLIVNQTGSC
    510 520 530 540 550
    AFDEFFSQSC APGADPKSRL CALCAGDDQG LDKCVPNSKE KYYGYTGAFR
    560 570 580 590 600
    CLAEDVGDVA FVKNDTVWEN TNGESTADWA KNLNREDFRL LCLDGTRKPV
    610 620 630 640 650
    TEAQSCHLAV APNHAVVSRS DRAAHVKQVL LHQQALFGKN GKNCPDKFCL
    660 670 680 690 700
    FKSETKNLLF NDNTECLAKL GGRPTYEEYL GTEYVTAIAN LKKCSTSPLL

    EACAFLTR
    Length:708
    Mass (Da):78,056
    Last modified:October 1, 1993 - v2
    Checksum:iC6FD7FC15D68E93F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti63 – 631E → A in AAA21722 (PubMed:8206385).Curated
    Sequence conflicti66 – 672RA → PG in AAA30617 (PubMed:1718281).Curated
    Sequence conflicti145 – 1451I → V in CAA40366 (PubMed:2001696).Curated
    Sequence conflicti145 – 1451I → V in AAA21722 (PubMed:8206385).Curated
    Sequence conflicti145 – 1451I → V in AAA30610 (PubMed:8206385).Curated
    Sequence conflicti164 – 1652LQ → PP in CAA40366 (PubMed:2001696).Curated
    Sequence conflicti264 – 2641C → Y in AAA21722 (PubMed:8206385).Curated
    Sequence conflicti273 – 2731A → P in AAA21722 (PubMed:8206385).Curated
    Sequence conflicti281 – 2811G → A in AAA21722 (PubMed:8206385).Curated
    Sequence conflicti291 – 2911S → R in AAA21722 (PubMed:8206385).Curated
    Sequence conflicti297 – 2971F → S in AAA30617 (PubMed:1718281).Curated
    Sequence conflicti340 – 3401G → A in CAA40366 (PubMed:2001696).Curated
    Sequence conflicti418 – 4181I → V in AAA21722 (PubMed:8206385).Curated
    Sequence conflicti436 – 4361S → T in AAA30610 (PubMed:8206385).Curated
    Sequence conflicti439 – 4391H → Y in CAA40366 (PubMed:2001696).Curated
    Sequence conflicti439 – 4391H → Y in AAA30610 (PubMed:8206385).Curated
    Sequence conflicti459 – 4591K → R in AAA21722 (PubMed:8206385).Curated
    Sequence conflicti514 – 5141A → R in CAA40366 (PubMed:2001696).Curated
    Sequence conflicti514 – 5141A → R in AAA30610 (PubMed:8206385).Curated
    Sequence conflicti632 – 6321H → R in BAB03470 (Ref. 5) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X57084 mRNA. Translation: CAA40366.1.
    M63502 mRNA. Translation: AAA30617.1.
    L08604 mRNA. Translation: AAA30609.1.
    L19993
    , L19982, L19983, L19984, L19985, L19986, L19988, L19989, L19990, L19991, L19992 Genomic DNA. Translation: AAA21722.1.
    L19981 mRNA. Translation: AAA30610.1.
    AB046664 mRNA. Translation: BAB03470.1.
    BC116051 mRNA. Translation: AAI16052.1.
    PIRiI45919. TFBOL.
    RefSeqiNP_851341.1. NM_180998.2.
    XP_015315141.1. XM_015459655.1.
    UniGeneiBt.44264.

    Genome annotation databases

    EnsembliENSBTAT00000001704; ENSBTAP00000001704; ENSBTAG00000001292.
    GeneIDi280846.
    KEGGibta:280846.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X57084 mRNA. Translation: CAA40366.1.
    M63502 mRNA. Translation: AAA30617.1.
    L08604 mRNA. Translation: AAA30609.1.
    L19993
    , L19982, L19983, L19984, L19985, L19986, L19988, L19989, L19990, L19991, L19992 Genomic DNA. Translation: AAA21722.1.
    L19981 mRNA. Translation: AAA30610.1.
    AB046664 mRNA. Translation: BAB03470.1.
    BC116051 mRNA. Translation: AAI16052.1.
    PIRiI45919. TFBOL.
    RefSeqiNP_851341.1. NM_180998.2.
    XP_015315141.1. XM_015459655.1.
    UniGeneiBt.44264.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BLFX-ray2.80A20-708[»]
    1LFCNMR-A36-60[»]
    1NKXX-ray1.90A361-708[»]
    1SDXX-ray2.06A361-695[»]
    E700-704[»]
    1Y58NMR-A38-49[»]
    2ALUX-ray2.09A361-708[»]
    2AYSX-ray1.86A361-708[»]
    2B65X-ray1.50A361-705[»]
    2DOJX-ray2.40A361-705[»]
    2DP8X-ray2.50A361-705[»]
    2DQVX-ray2.70A361-705[»]
    2DS9X-ray2.80A361-705[»]
    2DSFX-ray2.80A361-705[»]
    2DVCX-ray3.00A361-705[»]
    2DWAX-ray2.07A361-705[»]
    2DWHX-ray2.80A361-705[»]
    2DWIX-ray2.20A361-705[»]
    2DWJX-ray2.30A361-705[»]
    2DXRX-ray2.85A361-705[»]
    2DXYX-ray2.03A361-705[»]
    2DYXX-ray2.00A361-705[»]
    2E0SX-ray2.15A361-705[»]
    2E1SX-ray2.70A361-705[»]
    2FA7X-ray2.38A361-705[»]
    2G93X-ray1.90A361-705[»]
    2H4IX-ray2.55A361-705[»]
    2HCAX-ray2.80A361-705[»]
    2MD1NMR-A287-303[»]
    2MD2NMR-A287-296[»]
    2MD3NMR-A296-303[»]
    2MD4NMR-A287-298[»]
    2NUVX-ray2.25A361-705[»]
    2NWJX-ray2.25A361-705[»]
    2O1LX-ray1.97A361-705[»]
    2O51X-ray3.00A361-705[»]
    2OCUX-ray2.38A361-705[»]
    2P1SX-ray1.93A361-704[»]
    2PX1X-ray2.50A361-705[»]
    2Q8JX-ray2.71A361-708[»]
    2QJEX-ray2.30A361-708[»]
    2R71X-ray2.07A361-705[»]
    2R9JX-ray2.55A361-705[»]
    2ZMBX-ray2.90A361-705[»]
    3CFLX-ray2.25A361-705[»]
    3CI8X-ray2.40A361-705[»]
    3CRBX-ray2.60A361-705[»]
    3E9XX-ray2.70A361-705[»]
    3IAZX-ray2.00A361-705[»]
    3IB0X-ray1.40A361-705[»]
    3IB1X-ray2.20A361-705[»]
    3IB2X-ray2.29A361-705[»]
    3K0VX-ray1.91A361-705[»]
    3KJ7X-ray1.91A361-705[»]
    3MJNX-ray2.38A361-705[»]
    3O97X-ray2.68A361-705[»]
    3RGYX-ray2.00A361-705[»]
    3SDFX-ray2.10A361-705[»]
    3TAJX-ray1.70A361-705[»]
    3TODX-ray1.38A361-695[»]
    B700-705[»]
    3TTRX-ray2.27A361-705[»]
    3TUSX-ray2.50A361-705[»]
    3U72X-ray2.20A361-695[»]
    B700-705[»]
    3U8QX-ray1.97A361-695[»]
    B700-705[»]
    3UGWX-ray1.87A361-695[»]
    B700-705[»]
    3UK4X-ray1.98A361-695[»]
    B700-705[»]
    3USDX-ray2.40A361-695[»]
    B700-705[»]
    3V5AX-ray1.44A361-695[»]
    B700-705[»]
    3VDFX-ray1.46A361-695[»]
    B700-705[»]
    4DIGX-ray1.80A361-695[»]
    B700-705[»]
    4DXUX-ray1.46A361-695[»]
    B700-705[»]
    4FIMX-ray1.80A361-695[»]
    B700-705[»]
    4FJPX-ray1.68A361-695[»]
    B700-705[»]
    4FORX-ray1.58A361-695[»]
    B700-705[»]
    4G2ZX-ray1.90A361-695[»]
    B700-705[»]
    4G77X-ray1.98A361-705[»]
    4G8HX-ray1.88A361-705[»]
    4GRKX-ray1.68A361-695[»]
    B700-705[»]
    4N6PX-ray1.40A361-695[»]
    B700-705[»]
    4NEDX-ray2.10A361-705[»]
    4OQOX-ray2.42A/B361-708[»]
    5CRYX-ray2.79A/B361-708[»]
    5HBCX-ray2.79A/B361-708[»]
    ProteinModelPortaliP24627.
    SMRiP24627. Positions 24-708.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi158240. 1 interaction.
    IntActiP24627. 4 interactions.
    STRINGi9913.ENSBTAP00000001704.

    Chemistry

    ChEMBLiCHEMBL2796.

    Protein family/group databases

    Allergomei1065. Bos d LF.
    MEROPSiS60.001.

    PTM databases

    UniCarbKBiP24627.

    Proteomic databases

    PaxDbiP24627.
    PRIDEiP24627.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSBTAT00000001704; ENSBTAP00000001704; ENSBTAG00000001292.
    GeneIDi280846.
    KEGGibta:280846.

    Organism-specific databases

    CTDi4057.

    Phylogenomic databases

    eggNOGiENOG410IEAI. Eukaryota.
    ENOG410XQ36. LUCA.
    GeneTreeiENSGT00390000001619.
    HOGENOMiHOG000043759.
    HOVERGENiHBG000055.
    InParanoidiP24627.
    KOiK17283.
    OMAiRPVEGYL.
    OrthoDBiEOG7D59N7.
    TreeFamiTF324013.

    Enzyme and pathway databases

    ReactomeiR-BTA-1222556. ROS, RNS production in response to bacteria.
    SABIO-RKP24627.

    Miscellaneous databases

    EvolutionaryTraceiP24627.
    PMAP-CutDBP24627.

    Gene expression databases

    ExpressionAtlasiP24627. baseline and differential.

    Family and domain databases

    InterProiIPR030684. Lactotransferrin.
    IPR016357. Transferrin.
    IPR001156. Transferrin-like_dom.
    IPR018195. Transferrin_Fe_BS.
    [Graphical view]
    PfamiPF00405. Transferrin. 2 hits.
    [Graphical view]
    PIRSFiPIRSF500683. Lactotransferrin. 1 hit.
    PIRSF002549. 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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Molecular cloning and sequence analysis of bovine lactotransferrin."
      Pierce A., Colavizza D., Benaissa M., Maes P., Tartar A., Montreuil J., Spik G.
      Eur. J. Biochem. 196:177-184(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Submandibular gland.
    2. "Bovine lactoferrin mRNA: sequence, analysis, and expression in the mammary gland."
      Goodman R.E., Schanbacher F.L.
      Biochem. Biophys. Res. Commun. 180:75-84(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning of a 80-kD advanced glycosylation end product (AGE) binding protein from bovine lung."
      Tsang T.C., Burns D.K., Wang F., Pan Y.C.E., Schmidt A.M., Stern D.
      FASEB J. 6:233-233(1991)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    4. "Structure of the bovine lactoferrin-encoding gene and its promoter."
      Seyfert H.-M., Tuckoricz A., Interthal H., Koczan D., Hobom G.
      Gene 143:265-269(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Blood and Mammary gland.
    5. "Bovine lactoferrin."
      Nakamura I., Shimazaki K., Yagi Y., Watanabe A.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. NIH - Mammalian Gene Collection (MGC) project
      Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Ascending colon.
    7. "Purification and characterization of bovine lactoferrin from secretions of the involuting mammary gland: identification of multiple molecular weight forms."
      Rejman J.J., Hegarty H.M., Hurley W.L.
      Comp. Biochem. Physiol. 93B:929-934(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-59.
    8. Cited for: PROTEIN SEQUENCE OF 36-60, IDENTIFICATION OF LACTOFERRICIN PEPTIDE, FUNCTION, SYNTHESIS OF 36-60.
      Tissue: Milk.
    9. "Antibacterial activity in bovine lactoferrin-derived peptides."
      Hoek K.S., Milne J.M., Grieve P.A., Dionysius D.A., Smith R.
      Antimicrob. Agents Chemother. 41:54-59(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF LACTOFERRICIN.
    10. "Antibacterial effect of bovine lactoferrin against udder pathogens."
      Kutila T., Pyorala S., Saloniemi H., Kaartinen L.
      Acta Vet. Scand. 44:35-42(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ANTIMICROBIAL ACTIVITY.
    11. Cited for: PROTEASE FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    12. Cited for: FUNCTION.
    13. "Human lactoferrin activates NF-kappaB through the Toll-like receptor 4 pathway while it interferes with the lipopolysaccharide-stimulated TLR4 signaling."
      Ando K., Hasegawa K., Shindo K., Furusawa T., Fujino T., Kikugawa K., Nakano H., Takeuchi O., Akira S., Akiyama T., Gohda J., Inoue J., Hayakawa M.
      FEBS J. 277:2051-2066(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Three-dimensional structure of diferric bovine lactoferrin at 2.8-A resolution."
      Moore S.A., Anderson B.F., Groom C.R., Haridas M., Baker E.N.
      J. Mol. Biol. 274:222-236(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    15. "Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin."
      Hwang P.M., Zhou N., Shan X., Arrowsmith C.H., Vogel H.J.
      Biochemistry 37:4288-4298(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 36-60.

    Entry informationi

    Entry nameiTRFL_BOVIN
    AccessioniPrimary (citable) accession number: P24627
    Secondary accession number(s): Q1JQC9
    , Q29629, Q6LEC7, Q9MZY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: October 1, 1993
    Last modified: June 8, 2016
    This is version 165 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    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.