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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)DescriptionActionsGraphical viewLength
    Metal bindingi79Iron 1PROSITE-ProRule annotation1 Publication1
    Active sitei92PROSITE-ProRule annotation1
    Metal bindingi111Iron 1PROSITE-ProRule annotation1 Publication1
    Binding sitei136Carbonate 11
    Binding sitei140Carbonate 1PROSITE-ProRule annotation1 Publication1
    Binding sitei142Carbonate 1; via amide nitrogen1
    Binding sitei143Carbonate 1; via amide nitrogen1
    Metal bindingi211Iron 1PROSITE-ProRule annotation1 Publication1
    Metal bindingi272Iron 1PROSITE-ProRule annotation1 Publication1
    Active sitei278NucleophilePROSITE-ProRule annotation1
    Metal bindingi414Iron 2PROSITE-ProRule annotation1 Publication1
    Metal bindingi452Iron 2PROSITE-ProRule annotation1 Publication1
    Binding sitei478Carbonate 21
    Binding sitei482Carbonate 2PROSITE-ProRule annotation1 Publication1
    Binding sitei484Carbonate 2; via amide nitrogen1
    Binding sitei485Carbonate 2; via amide nitrogen1
    Metal bindingi545Iron 2PROSITE-ProRule annotation1 Publication1
    Metal bindingi614Iron 2PROSITE-ProRule annotation1 Publication1

    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.
    R-BTA-6798695. Neutrophil degranulation.
    R-BTA-6799990. Metal sequestration by antimicrobial proteins.
    R-BTA-6803157. Antimicrobial peptides.
    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 databases

    ChEMBLiCHEMBL2796.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 191 PublicationAdd BLAST19
    ChainiPRO_000003572620 – 708LactotransferrinAdd BLAST689
    PeptideiPRO_000003572736 – 60Lactoferricin-BAdd BLAST25

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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
    GlycosylationiCAR_000186252N-linked (GlcNAc...)1
    Disulfide bondi367 ↔ 399PROSITE-ProRule annotation
    Disulfide bondi377 ↔ 390PROSITE-ProRule annotation
    Glycosylationi387N-linked (GlcNAc...)1
    Disulfide bondi424 ↔ 703PROSITE-ProRule annotation
    Disulfide bondi444 ↔ 666PROSITE-ProRule annotation
    Disulfide bondi476 ↔ 551PROSITE-ProRule annotation
    GlycosylationiCAR_000197495N-linked (GlcNAc...)1
    Disulfide bondi500 ↔ 694PROSITE-ProRule annotation
    Disulfide bondi510 ↔ 524PROSITE-ProRule annotation
    Disulfide bondi521 ↔ 534PROSITE-ProRule annotation
    GlycosylationiCAR_000198564N-linked (GlcNAc...)1
    Disulfide bondi592 ↔ 606PROSITE-ProRule annotation
    Disulfide bondi644 ↔ 649PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP24627.
    PeptideAtlasiP24627.
    PRIDEiP24627.

    PTM databases

    UniCarbKBiP24627.

    Miscellaneous databases

    PMAP-CutDBP24627.

    Expressioni

    Gene expression databases

    BgeeiENSBTAG00000001292.
    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 interactor.
    IntActiP24627. 4 interactors.
    STRINGi9913.ENSBTAP00000001704.

    Structurei

    Secondary structure

    1708
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi25 – 31Combined sources7
    Helixi32 – 45Combined sources14
    Helixi46 – 48Combined sources3
    Beta strandi53 – 57Combined sources5
    Helixi61 – 69Combined sources9
    Beta strandi75 – 78Combined sources4
    Helixi80 – 87Combined sources8
    Turni89 – 91Combined sources3
    Beta strandi93 – 102Combined sources10
    Beta strandi104 – 120Combined sources17
    Beta strandi133 – 136Combined sources4
    Turni141 – 144Combined sources4
    Helixi145 – 155Combined sources11
    Turni159 – 161Combined sources3
    Helixi164 – 169Combined sources6
    Beta strandi172 – 176Combined sources5
    Turni182 – 184Combined sources3
    Helixi186 – 188Combined sources3
    Helixi210 – 219Combined sources10
    Beta strandi224 – 229Combined sources6
    Helixi232 – 236Combined sources5
    Helixi240 – 243Combined sources4
    Beta strandi246 – 248Combined sources3
    Turni261 – 263Combined sources3
    Beta strandi266 – 270Combined sources5
    Beta strandi273 – 280Combined sources8
    Helixi283 – 296Combined sources14
    Turni298 – 300Combined sources3
    Beta strandi325 – 328Combined sources4
    Helixi335 – 351Combined sources17
    Helixi354 – 362Combined sources9
    Beta strandi364 – 369Combined sources6
    Helixi370 – 383Combined sources14
    Turni384 – 386Combined sources3
    Beta strandi387 – 395Combined sources9
    Helixi396 – 404Combined sources9
    Beta strandi410 – 413Combined sources4
    Helixi415 – 423Combined sources9
    Beta strandi427 – 434Combined sources8
    Beta strandi437 – 439Combined sources3
    Beta strandi440 – 442Combined sources3
    Helixi444 – 446Combined sources3
    Beta strandi452 – 459Combined sources8
    Helixi467 – 469Combined sources3
    Beta strandi474 – 478Combined sources5
    Turni483 – 486Combined sources4
    Helixi487 – 497Combined sources11
    Helixi502 – 504Combined sources3
    Beta strandi505 – 510Combined sources6
    Helixi519 – 521Combined sources3
    Beta strandi527 – 530Combined sources4
    Turni531 – 534Combined sources4
    Helixi544 – 553Combined sources10
    Beta strandi558 – 563Combined sources6
    Helixi564 – 569Combined sources6
    Beta strandi571 – 575Combined sources5
    Turni578 – 582Combined sources5
    Helixi585 – 587Combined sources3
    Beta strandi588 – 591Combined sources4
    Beta strandi597 – 599Combined sources3
    Helixi600 – 605Combined sources6
    Beta strandi608 – 611Combined sources4
    Beta strandi615 – 618Combined sources4
    Helixi620 – 637Combined sources18
    Beta strandi638 – 640Combined sources3
    Turni642 – 647Combined sources6
    Beta strandi653 – 656Combined sources4
    Beta strandi658 – 660Combined sources3
    Beta strandi664 – 668Combined sources5
    Beta strandi671 – 673Combined sources3
    Helixi676 – 680Combined sources5
    Helixi682 – 692Combined sources11
    Helixi698 – 703Combined sources6
    Helixi704 – 707Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24627.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini25 – 352Transferrin-like 1PROSITE-ProRule annotationAdd BLAST328
    Domaini364 – 693Transferrin-like 2PROSITE-ProRule annotationAdd BLAST330

    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.
    OrthoDBiEOG091G0242.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti63E → A in AAA21722 (PubMed:8206385).Curated1
    Sequence conflicti66 – 67RA → PG in AAA30617 (PubMed:1718281).Curated2
    Sequence conflicti145I → V in CAA40366 (PubMed:2001696).Curated1
    Sequence conflicti145I → V in AAA21722 (PubMed:8206385).Curated1
    Sequence conflicti145I → V in AAA30610 (PubMed:8206385).Curated1
    Sequence conflicti164 – 165LQ → PP in CAA40366 (PubMed:2001696).Curated2
    Sequence conflicti264C → Y in AAA21722 (PubMed:8206385).Curated1
    Sequence conflicti273A → P in AAA21722 (PubMed:8206385).Curated1
    Sequence conflicti281G → A in AAA21722 (PubMed:8206385).Curated1
    Sequence conflicti291S → R in AAA21722 (PubMed:8206385).Curated1
    Sequence conflicti297F → S in AAA30617 (PubMed:1718281).Curated1
    Sequence conflicti340G → A in CAA40366 (PubMed:2001696).Curated1
    Sequence conflicti418I → V in AAA21722 (PubMed:8206385).Curated1
    Sequence conflicti436S → T in AAA30610 (PubMed:8206385).Curated1
    Sequence conflicti439H → Y in CAA40366 (PubMed:2001696).Curated1
    Sequence conflicti439H → Y in AAA30610 (PubMed:8206385).Curated1
    Sequence conflicti459K → R in AAA21722 (PubMed:8206385).Curated1
    Sequence conflicti514A → R in CAA40366 (PubMed:2001696).Curated1
    Sequence conflicti514A → R in AAA30610 (PubMed:8206385).Curated1
    Sequence conflicti632H → R in BAB03470 (Ref. 5) Curated1

    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi158240. 1 interactor.
    IntActiP24627. 4 interactors.
    STRINGi9913.ENSBTAP00000001704.

    Chemistry databases

    ChEMBLiCHEMBL2796.

    Protein family/group databases

    Allergomei1065. Bos d LF.
    MEROPSiS60.001.

    PTM databases

    UniCarbKBiP24627.

    Proteomic databases

    PaxDbiP24627.
    PeptideAtlasiP24627.
    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.
    OrthoDBiEOG091G0242.
    TreeFamiTF324013.

    Enzyme and pathway databases

    ReactomeiR-BTA-1222556. ROS, RNS production in response to bacteria.
    R-BTA-6798695. Neutrophil degranulation.
    R-BTA-6799990. Metal sequestration by antimicrobial proteins.
    R-BTA-6803157. Antimicrobial peptides.
    SABIO-RKP24627.

    Miscellaneous databases

    EvolutionaryTraceiP24627.
    PMAP-CutDBP24627.

    Gene expression databases

    BgeeiENSBTAG00000001292.
    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...

    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: November 30, 2016
    This is version 170 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.