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P08071

- TRFL_MOUSE

UniProt

P08071 - TRFL_MOUSE

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Protein

Lactotransferrin

Gene

Ltf

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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. 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).By similarity
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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi78 – 781Iron 1PROSITE-ProRule annotation
Active sitei91 – 911PROSITE-ProRule annotation
Metal bindingi110 – 1101Iron 1PROSITE-ProRule annotation
Binding sitei135 – 1351Carbonate 1PROSITE-ProRule annotation
Binding sitei139 – 1391Carbonate 1PROSITE-ProRule annotation
Binding sitei141 – 1411Carbonate 1; via amide nitrogenPROSITE-ProRule annotation
Binding sitei142 – 1421Carbonate 1; via amide nitrogenPROSITE-ProRule annotation
Metal bindingi210 – 2101Iron 1PROSITE-ProRule annotation
Metal bindingi271 – 2711Iron 1PROSITE-ProRule annotation
Active sitei277 – 2771NucleophilePROSITE-ProRule annotation
Metal bindingi413 – 4131Iron 2PROSITE-ProRule annotation
Metal bindingi451 – 4511Iron 2PROSITE-ProRule annotation
Binding sitei477 – 4771Carbonate 2PROSITE-ProRule annotation
Binding sitei481 – 4811Carbonate 2PROSITE-ProRule annotation
Binding sitei483 – 4831Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
Binding sitei484 – 4841Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
Metal bindingi544 – 5441Iron 2PROSITE-ProRule annotation
Metal bindingi613 – 6131Iron 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. ferric iron binding Source: InterPro
  2. heparin binding Source: Ensembl
  3. peptidase activity Source: MGI
  4. protein serine/threonine kinase activator activity Source: Ensembl
  5. serine-type peptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. antibacterial humoral response Source: UniProtKB
  2. antifungal humoral response Source: UniProtKB
  3. bone morphogenesis Source: UniProtKB
  4. cellular iron ion homeostasis Source: InterPro
  5. innate immune response in mucosa Source: UniProtKB
  6. iron ion transport Source: InterPro
  7. negative regulation of apoptotic process Source: UniProtKB
  8. negative regulation of lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  9. negative regulation of osteoclast development Source: UniProtKB
  10. negative regulation of single-species biofilm formation in or on host organism Source: UniProtKB
  11. negative regulation of tumor necrosis factor (ligand) superfamily member 11 production Source: UniProtKB
  12. ossification Source: UniProtKB-KW
  13. positive regulation of bone mineralization involved in bone maturation Source: UniProtKB
  14. positive regulation of chondrocyte proliferation Source: UniProtKB
  15. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  16. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
  17. positive regulation of osteoblast differentiation Source: UniProtKB
  18. positive regulation of osteoblast proliferation Source: UniProtKB
  19. positive regulation of toll-like receptor 4 signaling pathway Source: Ensembl
  20. regulation of cytokine production Source: UniProtKB
  21. regulation of tumor necrosis factor production Source: UniProtKB
  22. retina homeostasis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Immunity, Ion transport, Iron transport, Osteogenesis, Transport

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_198345. Phagosomal maturation (early endosomal stage).
REACT_198563. Amyloids.

Protein family/group databases

MEROPSiS60.970.

Names & Taxonomyi

Protein namesi
Recommended name:
Lactotransferrin (EC:3.4.21.-)
Short name:
Lactoferrin
Gene namesi
Name:Ltf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:96837. Ltf.

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

  1. cytoplasm Source: MGI
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. nucleus Source: Ensembl
  5. specific granule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 707688LactotransferrinPRO_0000035737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 63PROSITE-ProRule annotation
Disulfide bondi37 ↔ 54PROSITE-ProRule annotation
Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi133 ↔ 216PROSITE-ProRule annotation
Disulfide bondi175 ↔ 191PROSITE-ProRule annotation
Disulfide bondi188 ↔ 199PROSITE-ProRule annotation
Disulfide bondi249 ↔ 263PROSITE-ProRule annotation
Disulfide bondi366 ↔ 398PROSITE-ProRule annotation
Disulfide bondi376 ↔ 389PROSITE-ProRule annotation
Disulfide bondi423 ↔ 702PROSITE-ProRule annotation
Disulfide bondi443 ↔ 665PROSITE-ProRule annotation
Disulfide bondi475 ↔ 550PROSITE-ProRule annotation
Glycosylationi494 – 4941N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi499 ↔ 693PROSITE-ProRule annotation
Disulfide bondi509 ↔ 523PROSITE-ProRule annotation
Disulfide bondi520 ↔ 533PROSITE-ProRule annotation
Disulfide bondi591 ↔ 605PROSITE-ProRule annotation
Disulfide bondi643 ↔ 648PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP08071.
PaxDbiP08071.
PRIDEiP08071.

PTM databases

PhosphoSiteiP08071.

Expressioni

Gene expression databases

BgeeiP08071.
CleanExiMM_LTF.
GenevestigatoriP08071.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP08071. 1 interaction.
MINTiMINT-4138470.

Structurei

3D structure databases

ProteinModelPortaliP08071.
SMRiP08071. Positions 23-707.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 351328Transferrin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini363 – 692330Transferrin-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

eggNOGiNOG87503.
GeneTreeiENSGT00390000001619.
HOGENOMiHOG000043759.
HOVERGENiHBG000055.
InParanoidiP08071.
KOiK17283.
OMAiRPVEGYL.
OrthoDBiEOG7D59N7.
TreeFamiTF324013.

Family and domain databases

InterProiIPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. TRANSFERRIN_LIKE_1. 1 hit.
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.

P08071-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLLIPSLIF LEALGLCLAK ATTVQWCAVS NSEEEKCLRW QNEMRKVGGP
60 70 80 90 100
PLSCVKKSST RQCIQAIVTN RADAMTLDGG TMFDAGKPPY KLRPVAAEVY
110 120 130 140 150
GTKEQPRTHY YAVAVVKNSS NFHLNQLQGL RSCHTGIGRS AGWKIPIGTL
160 170 180 190 200
RPYLNWNGPP ASLEEAVSKF FSKSCVPGAQ KDRFPNLCSS CAGTGANKCA
210 220 230 240 250
SSPEEPYSGY AGALRCLRDN AGDVAFTRGS TVFEELPNKA ERDQYKLLCP
260 270 280 290 300
DNTWKPVTEY KECHLAQVPS HAVVSRSTND KEEAIWELLR QSQEKFGKKQ
310 320 330 340 350
ASGFQLFASP SGQKDLLFKE SAIGFVRVPQ KVDVGLYLTF SYTTSIQNLN
360 370 380 390 400
KKQQDVIASK ARVTWCAVGS EEKRKCDQWN RASRGRVTCI SFPTTEDCIV
410 420 430 440 450
AIMKGDADAM SLDGGYIYTA GKCGLVPVLA ENQKSSKSNG LDCVNRPVEG
460 470 480 490 500
YLAVAAVRRE DAGFTWSSLR GKKSCHTAVD RTAGWNIPMG LLANQTRSCK
510 520 530 540 550
FNEFFSQSCA PGADPKSNLC ALCIGDEKGE NKCAPNSKER YQGYTGALRC
560 570 580 590 600
LAEKAGNVAF LKDSTVLQNT DGKNTEEWAR NLKLKDFELL CLDDTRKPVT
610 620 630 640 650
EAKNCHLAIA PNHAVVSRTD KVEVLQQVLL DQQVQFGRNG QRCPGEFCLF
660 670 680 690 700
QSKTKNLLFN DNTECLAKIP GKTTSEKYLG KEYVIATERL KQCSSSPLLE

ACAFLTQ
Length:707
Mass (Da):77,838
Last modified:July 27, 2011 - v4
Checksum:iE1B32F5FD8748A0F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 22MR → IQG in AAA40525. (PubMed:3611056)Curated
Sequence conflicti25 – 251Q → R in AAA40525. (PubMed:3611056)Curated
Sequence conflicti25 – 251Q → R in AAH06904. (PubMed:15489334)Curated
Sequence conflicti82 – 821M → L in BAA13633. 1 PublicationCurated
Sequence conflicti359 – 3591S → T in BAA13633. 1 PublicationCurated
Sequence conflicti382 – 3821A → D in AAA40525. (PubMed:3611056)Curated
Sequence conflicti449 – 4491E → G in BAA13633. 1 PublicationCurated
Sequence conflicti629 – 6291L → V in AAA40525. (PubMed:3611056)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03298 mRNA. Translation: AAA40525.1.
D88510 mRNA. Translation: BAA13633.1.
AK036491 mRNA. Translation: BAC29450.1.
AK144556 mRNA. Translation: BAE25936.1.
AK151822 mRNA. Translation: BAE30719.1.
BC006904 mRNA. Translation: AAH06904.1.
M74778 Genomic DNA. Translation: AAA39427.1.
CCDSiCCDS23581.1.
PIRiA28438.
RefSeqiNP_032548.2. NM_008522.3.
UniGeneiMm.282359.

Genome annotation databases

EnsembliENSMUST00000035077; ENSMUSP00000035077; ENSMUSG00000032496.
GeneIDi17002.
KEGGimmu:17002.
UCSCiuc009rvj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03298 mRNA. Translation: AAA40525.1 .
D88510 mRNA. Translation: BAA13633.1 .
AK036491 mRNA. Translation: BAC29450.1 .
AK144556 mRNA. Translation: BAE25936.1 .
AK151822 mRNA. Translation: BAE30719.1 .
BC006904 mRNA. Translation: AAH06904.1 .
M74778 Genomic DNA. Translation: AAA39427.1 .
CCDSi CCDS23581.1.
PIRi A28438.
RefSeqi NP_032548.2. NM_008522.3.
UniGenei Mm.282359.

3D structure databases

ProteinModelPortali P08071.
SMRi P08071. Positions 23-707.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P08071. 1 interaction.
MINTi MINT-4138470.

Protein family/group databases

MEROPSi S60.970.

PTM databases

PhosphoSitei P08071.

Proteomic databases

MaxQBi P08071.
PaxDbi P08071.
PRIDEi P08071.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035077 ; ENSMUSP00000035077 ; ENSMUSG00000032496 .
GeneIDi 17002.
KEGGi mmu:17002.
UCSCi uc009rvj.1. mouse.

Organism-specific databases

CTDi 4057.
MGIi MGI:96837. Ltf.

Phylogenomic databases

eggNOGi NOG87503.
GeneTreei ENSGT00390000001619.
HOGENOMi HOG000043759.
HOVERGENi HBG000055.
InParanoidi P08071.
KOi K17283.
OMAi RPVEGYL.
OrthoDBi EOG7D59N7.
TreeFami TF324013.

Enzyme and pathway databases

Reactomei REACT_198345. Phagosomal maturation (early endosomal stage).
REACT_198563. Amyloids.

Miscellaneous databases

ChiTaRSi LTF. mouse.
NextBioi 291116.
PROi P08071.
SOURCEi Search...

Gene expression databases

Bgeei P08071.
CleanExi MM_LTF.
Genevestigatori P08071.

Family and domain databases

InterProi IPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view ]
Pfami PF00405. Transferrin. 2 hits.
[Graphical view ]
PIRSFi PIRSF002549. Transferrin. 1 hit.
PRINTSi PR00422. TRANSFERRIN.
SMARTi SM00094. TR_FER. 2 hits.
[Graphical view ]
PROSITEi PS00205. TRANSFERRIN_LIKE_1. 1 hit.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Lactotransferrin is the major estrogen inducible protein of mouse uterine secretions."
    Pentecost B.T., Teng C.T.
    J. Biol. Chem. 262:10134-10139(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Uterus.
  2. Moriishi K.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Uterus.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone, Bone marrow and Gall bladder.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Characterization of estrogen-responsive mouse lactoferrin promoter."
    Liu Y., Teng C.T.
    J. Biol. Chem. 266:21880-21885(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.

Entry informationi

Entry nameiTRFL_MOUSE
AccessioniPrimary (citable) accession number: P08071
Secondary accession number(s): P70690
, Q61799, Q8CBA0, Q922P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 131 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3