Reviewed, UniProtKB/Swiss-Prot P02788 (TRFL_HUMAN)

Names and origin

Protein names

Recommended name:
    Lactotransferrin
      Short name=Lactoferrin
    EC=3.4.21.-
Alternative name(s):
    Talalactoferrin
Cleaved into the following 4 chains:
    1- Recommended name:
            Kaliocin-1
    2- Recommended name:
            Lactoferroxin-A
    3- Recommended name:
            Lactoferroxin-B
    4- Recommended name:
            Lactoferroxin-C

Gene names

Name:	LTF
Synonyms:	LF

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	710 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate. Ref.20 Lactotransferrin has antimicrobial activity which depends on the extracellular cation concentration. Ref.20 Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors. Ref.20 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. Ref.20
Catalytic activity	Preferential at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin.
Subunit structure	Monomer.
Subcellular location	Secreted.
Sequence similarities	Belongs to the transferrin family. Contains 2 transferrin-like domains.

Ontologies

Keywords
Biological process	Ion transport Iron transport Transport
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Ligand	Iron Metal-binding
Molecular function	Antibiotic Antimicrobial Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular iron ion homeostasis Inferred from electronic annotation. Source: InterPro defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW humoral immune response Traceable author statement. Source: ProtInc iron ion transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell secretory granule Inferred from direct assay. Source: MGI
Molecular function	ferric iron binding Inferred from electronic annotation. Source: InterPro heparin binding Inferred from direct assay. Source: MGI protein binding Inferred from physical interaction. Source: IntAct serine-type endopeptidase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SGK1	O00141	1	EBI-1058602,EBI-1042854

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.13 Ref.14

Chain

20 – 710

691

Lactotransferrin

PRO_0000035732

Peptide

171 – 201

31

Kaliocin-1

PRO_0000035733

Peptide

338 – 343

6

Lactoferroxin-A

PRO_0000035734

Peptide

543 – 547

5

Lactoferroxin-B

PRO_0000035735

Peptide

680 – 686

7

Lactoferroxin-C

PRO_0000035736

Regions

Domain

25 – 352

328

Transferrin-like 1

Domain

364 – 695

332

Transferrin-like 2

Sites

Active site

92

1

Probable

Active site

278

1

Nucleophile Probable

Metal binding

79

1

Iron 1

Metal binding

111

1

Iron 1

Metal binding

211

1

Iron 1

Metal binding

272

1

Iron 1

Metal binding

414

1

Iron 2

Metal binding

454

1

Iron 2

Metal binding

547

1

Iron 2

Metal binding

616

1

Iron 2

Binding site

136

1

Carbonate 1

Binding site

140

1

Carbonate 1

Binding site

142

1

Carbonate 1; via amide nitrogen

Binding site

143

1

Carbonate 1; via amide nitrogen

Binding site

480

1

Carbonate 2

Binding site

484

1

Carbonate 2

Binding site

486

1

Carbonate 2; via amide nitrogen

Binding site

487

1

Carbonate 2; via amide nitrogen

Amino acid modifications

Modified residue

547

1

Phosphotyrosine Ref.21

Glycosylation

156

1

N-linked (GlcNAc...) Ref.22

Glycosylation

497

1

N-linked (GlcNAc...) Ref.22 Ref.24

Glycosylation

642

1

N-linked (GlcNAc...) Ref.22

Disulfide bond

28 ↔ 64

Disulfide bond

38 ↔ 55

Disulfide bond

134 ↔ 217

Disulfide bond

176 ↔ 192

Disulfide bond

189 ↔ 200

Disulfide bond

250 ↔ 264

Disulfide bond

367 ↔ 399

Disulfide bond

377 ↔ 390

Disulfide bond

424 ↔ 705

Disulfide bond

446 ↔ 668

Disulfide bond

478 ↔ 553

Disulfide bond

502 ↔ 696

Disulfide bond

512 ↔ 526

Disulfide bond

523 ↔ 536

Disulfide bond

594 ↔ 608

Disulfide bond

646 ↔ 651

Natural variations

Natural variant

29

1

A → T: dbSNP rs1126477. Ref.3 Ref.6 Ref.7 Ref.8 Ref.9 Ref.30

VAR_013504

Natural variant

47

1

K → R: dbSNP rs1126478. Ref.3 Ref.6 Ref.7 Ref.8 Ref.9 Ref.30

VAR_013505

Natural variant

148

1

I → T: dbSNP rs1126479. Ref.1

VAR_013506

Natural variant

422

1

G → C: dbSNP rs1042055. Ref.1

VAR_013507

Natural variant

579

1

E → D: dbSNP rs2073495. Ref.6 Ref.8 Ref.9 Ref.17

VAR_013508

Experimental info

Mutagenesis

92

1

K → A: Almost no protease activity. Ref.20

Mutagenesis

270

1

P → V: No effect. Ref.20

Mutagenesis

278

1

S → A: No protease activity. Ref.20

Sequence conflict

14

1

L → P in AAA58656. Ref.4

Sequence conflict

20

1

G → GS in AAH15822. Ref.10

Sequence conflict

20

1

G → GS in AAH15823. Ref.10

Sequence conflict

23

1

R → RR in CAA37914. Ref.1

Sequence conflict

23

1

R → RR in AAB60324. Ref.2

Sequence conflict

23

1

R → RR in AAA36159. Ref.3

Sequence conflict

23

1

R → RR in AAA59511. Ref.4

Sequence conflict

23

1

R → RR in AAA58656. Ref.4

Sequence conflict

23

1

R → RR in AAG48753. Ref.6

Sequence conflict

23

1

R → RR in AAN11304. Ref.7

Sequence conflict

23

1

R → RR in AAN63998. Ref.8

Sequence conflict

23

1

R → RR in AAN75578. Ref.9

Sequence conflict

23

1

R → RR in AAH22347. Ref.10

Sequence conflict

23

1

R → RR in CAA37116. Ref.12

Sequence conflict

49

1

R → C in AAH22347. Ref.10

Sequence conflict

130

1

G → C in AAH15823. Ref.10

Sequence conflict

138

1

L → R in AAH22347. Ref.10

Sequence conflict

140

1

Missing AA sequence Ref.13

Sequence conflict

169

1

Missing AA sequence Ref.13

Sequence conflict

409 – 410

2

DA → NASVLMDSEGGFLAR AA sequence Ref.13

Sequence conflict

415

1

G → E in AAA59511. Ref.4

Sequence conflict

431

1

A → G in AAA58656. Ref.4

Sequence conflict

456

1

A → T in AAH15822. Ref.10

Sequence conflict

456

1

A → T in AAH15823. Ref.10

Sequence conflict

487

1

G → A in AAA86665. Ref.16

Sequence conflict

531

1

Q → E AA sequence Ref.13

Sequence conflict

537

1

V → E in AAH15822. Ref.10

Sequence conflict

694

1

K → R AA sequence Ref.13

Sequence conflict

694

1

K → R AA sequence Ref.15

Secondary structure

1

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710

Helix Strand Turn

Details...

Beta strand

25 – 31

7

Helix

32 – 46

15

Turn

47 – 49

3

Beta strand

53 – 57

5

Helix

61 – 69

9

Beta strand

75 – 78

4

Helix

80 – 87

8

Turn

89 – 91

3

Beta strand

93 – 102

10

Beta strand

104 – 118

15

Helix

125 – 127

3

Beta strand

132 – 136

5

Turn

141 – 144

4

Helix

145 – 151

7

Helix

152 – 154

3

Helix

164 – 171

8

Beta strand

172 – 176

5

Turn

182 – 184

3

Helix

186 – 189

4

Helix

196 – 198

3

Helix

210 – 219

10

Beta strand

224 – 229

6

Helix

232 – 236

5

Helix

240 – 243

4

Beta strand

246 – 249

4

Beta strand

255 – 257

3

Helix

261 – 263

3

Beta strand

266 – 270

5

Beta strand

273 – 280

8

Helix

283 – 297

15

Beta strand

317 – 319

3

Beta strand

325 – 328

4

Helix

335 – 339

5

Helix

341 – 349

9

Helix

354 – 362

9

Beta strand

363 – 370

8

Helix

371 – 382

12

Beta strand

387 – 395

9

Helix

396 – 404

9

Beta strand

410 – 413

4

Helix

415 – 423

9

Beta strand

427 – 435

9

Beta strand

440 – 442

3

Helix

446 – 448

3

Beta strand

454 – 463

10

Helix

469 – 471

3

Beta strand

477 – 480

4

Turn

485 – 488

4

Helix

489 – 499

11

Helix

504 – 506

3

Beta strand

507 – 512

6

Helix

521 – 523

3

Helix

546 – 555

10

Beta strand

560 – 565

6

Helix

566 – 571

6

Helix

580 – 582

3

Helix

587 – 589

3

Beta strand

590 – 593

4

Beta strand

599 – 601

3

Helix

602 – 607

6

Beta strand

610 – 613

4

Beta strand

617 – 620

4

Helix

622 – 624

3

Helix

625 – 639

15

Turn

644 – 649

6

Beta strand

655 – 658

4

Beta strand

666 – 671

6

Helix

678 – 682

5

Helix

684 – 693

10

Helix

700 – 709

10

Sequences

	Sequence		Length	Mass (Da)
	P02788-1 [UniParc]. Last modified January 24, 2006. Version 6. Checksum: 0489CABA6D13C098	FASTA	710	78,182
	10 20 30 40 50 60 MKLVFLVLLF LGALGLCLAG RRRSVQWCAV SQPEATKCFQ WQRNMRKVRG PPVSCIKRDS 70 80 90 100 110 120 PIQCIQAIAE NRADAVTLDG GFIYEAGLAP YKLRPVAAEV YGTERQPRTH YYAVAVVKKG 130 140 150 160 170 180 GSFQLNELQG LKSCHTGLRR TAGWNVPIGT LRPFLNWTGP PEPIEAAVAR FFSASCVPGA 190 200 210 220 230 240 DKGQFPNLCR LCAGTGENKC AFSSQEPYFS YSGAFKCLRD GAGDVAFIRE STVFEDLSDE 250 260 270 280 290 300 AERDEYELLC PDNTRKPVDK FKDCHLARVP SHAVVARSVN GKEDAIWNLL RQAQEKFGKD 310 320 330 340 350 360 KSPKFQLFGS PSGQKDLLFK DSAIGFSRVP PRIDSGLYLG SGYFTAIQNL RKSEEEVAAR 370 380 390 400 410 420 RARVVWCAVG EQELRKCNQW SGLSEGSVTC SSASTTEDCI ALVLKGEADA MSLDGGYVYT 430 440 450 460 470 480 AGKCGLVPVL AENYKSQQSS DPDPNCVDRP VEGYLAVAVV RRSDTSLTWN SVKGKKSCHT 490 500 510 520 530 540 AVDRTAGWNI PMGLLFNQTG SCKFDEYFSQ SCAPGSDPRS NLCALCIGDE QGENKCVPNS 550 560 570 580 590 600 NERYYGYTGA FRCLAENAGD VAFVKDVTVL QNTDGNNNEA WAKDLKLADF ALLCLDGKRK 610 620 630 640 650 660 PVTEARSCHL AMAPNHAVVS RMDKVERLKQ VLLHQQAKFG RNGSDCPDKF CLFQSETKNL 670 680 690 700 710 LFNDNTECLA RLHGKTTYEK YLGPQYVAGI TNLKKCSTSP LLEACEFLRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete nucleotide sequence of human mammary gland lactoferrin." Rey M.W., Woloshuk S.L., de Boer H.A., Pieper F.R. Nucleic Acids Res. 18:5288-5288(1990) [PubMed: 2402455] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS THR-148 AND CYS-422. Tissue: Mammary gland.
[2]	Cho Y.Y. Thesis (1994), Genetic Engineering Research Institute, South Korea Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary gland.
[3]	Conneely O.M. Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS THR-29 AND ARG-47.
[4]	"Molecular cloning and sequence analysis of human lactoferrin." Liang Q., Jimenez-Flores R., Richardson T. Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary gland.
[5]	"Human neutrophil lactoferrin coding and 5' flanking region DNA sequences." Wei X., Han J., Rado T.A. Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Bone marrow.
[6]	"cDNA cloning and sequence analysis of human lactoferrin." Cheng H., Chen X.Z., Huan L.D. Sheng Wu Gong Cheng Xue Bao 17:385-387(2001) [PubMed: 11702692] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS THR-29; ARG-47 AND ASP-579. Tissue: Mammary gland.
[7]	"Characterization of an amino acid polymorphism in the antibacterial domain of human lactoferrin." Kaplan J.B., Fine D.H. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS THR-29 AND ARG-47.
[8]	Shi Y.-Q., Zhang Y., Zheng Y.-M. Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS THR-29; ARG-47 AND ASP-579. Tissue: Mammary gland.
[9]	Baskar Singh S., Saravanan K., Paramasivam M., Srinivasan A., Singh T.P. Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS THR-29; ARG-47 AND ASP-579. Tissue: Seminal vesicle.
[10]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
[11]	"Differential molecular mechanism of the estrogen action that regulates lactoferrin gene in human and mouse." Teng C.T., Liu Y., Yang N., Walmer D., Panella T. Mol. Endocrinol. 6:1969-1981(1992) [PubMed: 1480183] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
[12]	"Nucleotide sequence of human lactoferrin cDNA." Powell M.J., Ogden J.E. Nucleic Acids Res. 18:4013-4013(1990) [PubMed: 2374734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-710. Tissue: Mammary gland.
[13]	"Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins." Metz-Boutigue M.-H., Jolles J., Mazurier J., Schoentgen F., Legrand D., Spik G., Montreuil J., Jolles P. Eur. J. Biochem. 145:659-676(1984) [PubMed: 6510420] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-710.
[14]	"The present state of the human lactotransferrin sequence. Study and alignment of the cyanogen bromide fragments and characterization of N- and C-terminal domains." Metz-Boutigue M.-H., Mazurier J., Jolles J., Spik G., Montreuil J., Jolles P. Biochim. Biophys. Acta 670:243-254(1981) [PubMed: 6794640] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 20-72; 133-170; 256-277 AND 346-529.
[15]	"An 88 amino acid long C-terminal sequence of human lactotransferrin." Metz-Boutigue M.-H., Jolles J., Mazurier J., Spik G., Montreuil J., Jolles P. FEBS Lett. 142:107-110(1982) [PubMed: 7049727] [Abstract] Cited for: PROTEIN SEQUENCE OF 608-710.
[16]	"Isolation of lactoferrin cDNA from a human myeloid library and expression of mRNA during normal and leukemic myelopoiesis." Rado T.A., Wei X., Benz E.J. Jr. Blood 70:989-993(1987) [PubMed: 3477300] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 435-710.
[17]	McCombie W.R., Wilson R., Chen E., Gibbs R., Zuo L., Johnson D., Nhan M., Parnell L., Dedhia N., Ansari A., Mardis E., Schutz K., Gnoj L., la Bastide M., Kaplan N., Greco T., Touchman J., Muzny D. , Chen C.N., Evans C., Fitzgerald M., See L.H., Tang M., Porcel B.M., Dragan Y., Giacalone J., Pae A., Powell E., Solinsky K.A., Desilva U., Diaz-Perez S., Zhou X., Yu Y., Watanabe M., Doggett N., Garcia D., Sagripanti J.L. Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-710, VARIANT ASP-579.
[18]	"Isolation and characterization of opioid antagonist peptides derived from human lactoferrin." Tani F., Iio K., Chiba H., Yoshikawa M. Agric. Biol. Chem. 54:1803-1810(1990) [PubMed: 1369293] [Abstract] Cited for: CHARACTERIZATION OF LACTOFERROXINS.
[19]	"Potassium efflux induced by a new lactoferrin-derived peptide mimicking the effect of native human lactoferrin on the bacterial cytoplasmic membrane." Viejo-Diaz M., Andres M.T., Perez-Gil J., Sanchez M., Fierro J.F. Biokhimiia 68:217-227(2003) [PubMed: 12693969] [Abstract] Cited for: SYNTHESIS OF 171-201 (KALIOCIN-1).
[20]	"Human milk lactoferrin is a serine protease that cleaves Haemophilus surface proteins at arginine-rich sites." Hendrixson D.R., Qiu J., Shewry S.C., Fink D.L., Petty S., Baker E.N., Plaut A.G., St Geme J.W. III Mol. Microbiol. 47:607-617(2003) [PubMed: 12535064] [Abstract] Cited for: FUNCTION AS A PROTEASE, MUTAGENESIS OF LYS-92; PRO-270 AND SER-278.
[21]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-547, MASS SPECTROMETRY.
[22]	"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry." Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F. Proteomics 8:3833-3847(2008) [PubMed: 18780401] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156; ASN-497 AND ASN-642, MASS SPECTROMETRY. Tissue: Milk.
[23]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[24]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-497, MASS SPECTROMETRY. Tissue: Liver.
[25]	"Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8-A resolution." Anderson B.F., Baker H.M., Norris G.E., Rice D.W., Baker E.N. J. Mol. Biol. 209:711-734(1989) [PubMed: 2585506] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SEQUENCE REVISION.
[26]	"Structure of human diferric lactoferrin refined at 2.2-A resolution." Haridas M., Anderson B.F., Baker E.N. Acta Crystallogr. D 51:629-646(1995) [PubMed: 15299793] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[27]	"Mutagenesis of the histidine ligand in human lactoferrin: iron binding properties and crystal structure of the histidine-253-->methionine mutant." Nicholson H., Anderson B.F., Bland T., Shewry S.C., Tweedie J.W., Baker E.N. Biochemistry 36:341-346(1997) [PubMed: 9003186] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-352.
[28]	"Structure of recombinant human lactoferrin expressed in Aspergillus awamori." Sun X.L., Baker H.M., Shewry S.C., Jameson G.B., Baker E.N. Acta Crystallogr. D 55:403-407(1999) [PubMed: 10089347] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[29]	"Structure of human apolactoferrin at 2.0-A resolution. Refinement and analysis of ligand-induced conformational change." Jameson G.B., Anderson B.F., Norris G.E., Thomas D.H., Baker E.N. Acta Crystallogr. D 54:1319-1335(1998) [PubMed: 10089508] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[30]	"Familial subepithelial corneal amyloidosis (gelatinous drop-like corneal dystrophy): exclusion of linkage to lactoferrin gene." Klintworth G.K., Sommer J.R., Obrian G., Han L., Ahmed M.N., Qumsiyeh M.B., Lin P.-Y., Basti S., Reddy M.K., Kanai A., Hotta Y., Sugar J., Kumaramanickavel G., Munier F., Schorderet D.F., El Matri L., Iwata F., Kaiser-Kupfer M. , Nagata M., Nakayasu K., Hejtmancik J.F., Teng C.T. Mol. Vis. 4:31-32(1998) [PubMed: 9873069] [Abstract] Cited for: VARIANTS THR-29 AND ARG-47.
+	Additional computationally mapped references.

Web resources

Wikipedia

Lactotransferrin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X53961 mRNA. Translation: CAA37914.1.
U07643 mRNA. Translation: AAB60324.1.
M93150 mRNA. Translation: AAA36159.1.
M83202 mRNA. Translation: AAA59511.1.
M83205 mRNA. Translation: AAA58656.1.
M73700 Genomic DNA. Translation: AAA59479.1.
AF332168 mRNA. Translation: AAG48753.1.
AY137470 mRNA. Translation: AAN11304.1.
AY165046 mRNA. Translation: AAN63998.1.
AY178998 mRNA. Translation: AAN75578.2.
BC015822 mRNA. Translation: AAH15822.1.
BC015823 mRNA. Translation: AAH15823.1.
BC022347 mRNA. Translation: AAH22347.1.
S52659 Genomic DNA. Translation: AAB24877.1.
X52941 mRNA. Translation: CAA37116.1.
M18642 mRNA. Translation: AAA86665.1.
U95626 Genomic DNA. Translation: AAB57795.1.

IPI

IPI00298860.

PIR

TFHUL. G01394.

RefSeq

NP_002334.2.

UniGene

Hs.529517

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B0L	X-ray	2.20	A	20-710	[»]
1BKA	X-ray	2.40	A	20-710	[»]
1CB6	X-ray	2.00	A	20-710	[»]
1DSN	X-ray	2.05	A	21-352	[»]
1EH3	X-ray	2.00	A	21-348	[»]
1FCK	X-ray	2.20	A	21-710	[»]
1H43	X-ray	2.20	A	21-352	[»]
1H44	X-ray	2.00	A	21-352	[»]
1H45	X-ray	1.95	A	21-352	[»]
1HSE	X-ray	2.20	A	21-353	[»]
1L5T	X-ray	3.00	A/B	21-351	[»]
1LCF	X-ray	2.00	A	20-710	[»]
1LCT	X-ray	2.00	A	21-352	[»]
1LFG	X-ray	2.20	A	20-710	[»]
1LFH	X-ray	2.80	A	20-710	[»]
1LFI	X-ray	2.10	A	20-710	[»]
1LGB	X-ray	3.30	C	110-268	[»]
1N76	X-ray	3.40	A	21-710	[»]
1SQY	X-ray	2.50	A	20-710	[»]
1VFD	X-ray	2.50	A	22-349	[»]
1VFE	X-ray	2.30	A	22-352	[»]
1Z6V	NMR	-	A	21-67	[»]
1Z6W	NMR	-	A	21-67	[»]
2BJJ	X-ray	2.40	X	21-710	[»]
2DP4	X-ray	2.90	I	528-535	[»]
2HD4	X-ray	2.15	B	528-535	[»]
2PMS	X-ray	2.91	A/B	21-362	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P02788. 2 interactions.

STRING

P02788.

Protein family/group databases

MEROPS

S60.001.
S60.970.

PTM databases

GlycoSuiteDB

P02788.

PhosphoSite

P02788.

Proteomic databases

PRIDE

P02788.

Genome annotation databases

Ensembl

ENST00000231751; ENSP00000231751; ENSG00000012223; Homo sapiens. [Genome view]

GeneID

4057.

KEGG

hsa:4057.

UCSC

uc003cpq.1. human.

Organism-specific databases

CTD

4057.

GeneCards

GC03M046452.
GC03M046453.

H-InvDB

HIX0003248.

HGNC

HGNC:6720. LTF.

HPA

CAB008645.

MIM

150210. gene.
245480. phenotype.

PharmGKB

PA30482.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17139.

HOVERGEN

P02788.

InParanoid

P02788.

OMA

ETKNLLF.

OrthoDB

EOG9J6V99.

PhylomeDB

P02788.

Gene expression databases

ArrayExpress

P02788.

Bgee

P02788.

Genevestigator

P02788.

GermOnline

ENSG00000012223. Homo sapiens.

Family and domain databases

InterPro

IPR001156. Peptidase_S60.
IPR016357. Transferrin.
IPR018195. Transferrin_Fe_BS.
[Graphical view]

PANTHER

PTHR11485. Peptidase_S60. 1 hit.

Pfam

PF00405. Transferrin. 2 hits.
[Graphical view]

PIRSF

PIRSF002549. Transferrin. 1 hit.

PRINTS

PR00422. TRANSFERRIN.

SMART

SM00094. TR_FER. 2 hits.
[Graphical view]

PROSITE

PS00205. 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]

ProtoNet

Search...

Other Resources

DrugBank

DB00487. Pefloxacin.

NextBio

15896.

SOURCE

Search...

Entry information

Entry name

TRFL_HUMAN

Accession

Primary (citable) accession number: P02788
Secondary accession number(s): O00756 , Q16780, Q16785, Q16786, Q16789, Q8IU92, Q8IZH6, Q8TCD2, Q96KZ4, Q96KZ5, Q9H1Z3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 24, 2006
Last modified:	February 9, 2010
This is version 137 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.