TRFL_BOVIN
ID TRFL_BOVIN Reviewed; 708 AA.
AC P24627; Q1JQC9; Q29629; Q6LEC7; Q9MZY3;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Lactotransferrin;
DE Short=Lactoferrin;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Lactoferricin-B;
DE Short=Lfcin-B;
DE Flags: Precursor;
GN Name=LTF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Submandibular gland;
RX PubMed=2001696; DOI=10.1111/j.1432-1033.1991.tb15801.x;
RA Pierce A., Colavizza D., Benaissa M., Maes P., Tartar A., Montreuil J.,
RA Spik G.;
RT "Molecular cloning and sequence analysis of bovine lactotransferrin.";
RL Eur. J. Biochem. 196:177-184(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1718281; DOI=10.1016/s0006-291x(05)81257-4;
RA Goodman R.E., Schanbacher F.L.;
RT "Bovine lactoferrin mRNA: sequence, analysis, and expression in the mammary
RT gland.";
RL Biochem. Biophys. Res. Commun. 180:75-84(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RA Tsang T.C., Burns D.K., Wang F., Pan Y.C.E., Schmidt A.M., Stern D.;
RT "Cloning of a 80-kD advanced glycosylation end product (AGE) binding
RT protein from bovine lung.";
RL FASEB J. 6:233-233(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Blood, and Mammary gland;
RX PubMed=8206385; DOI=10.1016/0378-1119(94)90108-2;
RA Seyfert H.-M., Tuckoricz A., Interthal H., Koczan D., Hobom G.;
RT "Structure of the bovine lactoferrin-encoding gene and its promoter.";
RL Gene 143:265-269(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nakamura I., Shimazaki K., Yagi Y., Watanabe A.;
RT "Bovine lactoferrin.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 20-59.
RX PubMed=2805645; DOI=10.1016/0305-0491(89)90068-0;
RA Rejman J.J., Hegarty H.M., Hurley W.L.;
RT "Purification and characterization of bovine lactoferrin from secretions of
RT the involuting mammary gland: identification of multiple molecular weight
RT forms.";
RL Comp. Biochem. Physiol. 93B:929-934(1989).
RN [8]
RP PROTEIN SEQUENCE OF 36-60, IDENTIFICATION OF LACTOFERRICIN PEPTIDE,
RP FUNCTION, AND SYNTHESIS OF 36-60.
RC TISSUE=Milk;
RX PubMed=1599934; DOI=10.1016/0167-4838(92)90346-f;
RA Bellamy W., Takase M., Yamauchi K., Wakabayashi H., Kawase K., Tomita M.;
RT "Identification of the bactericidal domain of lactoferrin.";
RL Biochim. Biophys. Acta 1121:130-136(1992).
RN [9]
RP FUNCTION OF LACTOFERRICIN.
RX PubMed=8980754; DOI=10.1128/aac.41.1.54;
RA Hoek K.S., Milne J.M., Grieve P.A., Dionysius D.A., Smith R.;
RT "Antibacterial activity in bovine lactoferrin-derived peptides.";
RL Antimicrob. Agents Chemother. 41:54-59(1997).
RN [10]
RP ANTIMICROBIAL ACTIVITY.
RX PubMed=14650542; DOI=10.1186/1751-0147-44-35;
RA Kutila T., Pyorala S., Saloniemi H., Kaartinen L.;
RT "Antibacterial effect of bovine lactoferrin against udder pathogens.";
RL Acta Vet. Scand. 44:35-42(2003).
RN [11]
RP PROTEASE FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15222473; DOI=10.1023/b:biom.0000027700.90780.45;
RA Massucci M.T., Giansanti F., Di Nino G., Turacchio M., Giardi M.F.,
RA Botti D., Ippoliti R., De Giulio B., Siciliano R.A., Donnarumma G.,
RA Valenti P., Bocedi A., Polticelli F., Ascenzi P., Antonini G.;
RT "Proteolytic activity of bovine lactoferrin.";
RL BioMetals 17:249-255(2004).
RN [12]
RP FUNCTION.
RX PubMed=15166119; DOI=10.1210/en.2003-1307;
RA Cornish J., Callon K.E., Naot D., Palmano K.P., Banovic T., Bava U.,
RA Watson M., Lin J.M., Tong P.C., Chen Q., Chan V.A., Reid H.E.,
RA Fazzalari N., Baker H.M., Baker E.N., Haggarty N.W., Grey A.B., Reid I.R.;
RT "Lactoferrin is a potent regulator of bone cell activity and increases bone
RT formation in vivo.";
RL Endocrinology 145:4366-4374(2004).
RN [13]
RP FUNCTION.
RX PubMed=20345905; DOI=10.1111/j.1742-4658.2010.07620.x;
RA Ando K., Hasegawa K., Shindo K., Furusawa T., Fujino T., Kikugawa K.,
RA Nakano H., Takeuchi O., Akira S., Akiyama T., Gohda J., Inoue J.,
RA Hayakawa M.;
RT "Human lactoferrin activates NF-kappaB through the Toll-like receptor 4
RT pathway while it interferes with the lipopolysaccharide-stimulated TLR4
RT signaling.";
RL FEBS J. 277:2051-2066(2010).
RN [14]
RP ERRATUM OF PUBMED:20345905.
RA Massucci M.T., Giansanti F., Di Nino G., Turacchio M., Giardi M.F.,
RA Botti D., Ippoliti R., De Giulio B., Siciliano R.A., Donnarumma G.,
RA Valenti P., Bocedi A., Polticelli F., Ascenzi P., Antonini G.;
RL BioMetals 17:745-745(2004).
RN [15]
RP GLYCOSYLATION AT ASN-252; ASN-300; ASN-387; ASN-495 AND ASN-564,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DISULFIDE BONDS.
RX DOI=10.1016/j.idairyj.2021.104999;
RA Gnanesh Kumar B.S., Mattad S.;
RT "Comprehensive analysis of lactoferrin N-glycans with site-specificity from
RT bovine colostrum using specific proteases and RP-UHPLC-MS/MSComprehensive
RT analysis of lactoferrin N-glycans with site-specificity from bovine
RT colostrum using specific proteases and RP-UHPLC-MS/MS.";
RL Int. Dairy J. 119:104999-104999(2021).
RN [16] {ECO:0007744|PDB:1BLF}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 20-708 IN COMPLEX WITH IRON AND
RP MANNOSE, AND GLYCOSYLATION AT ASN-387; ASN-495 AND ASN-564.
RX PubMed=9398529; DOI=10.1006/jmbi.1997.1386;
RA Moore S.A., Anderson B.F., Groom C.R., Haridas M., Baker E.N.;
RT "Three-dimensional structure of diferric bovine lactoferrin at 2.8-A
RT resolution.";
RL J. Mol. Biol. 274:222-236(1997).
RN [17] {ECO:0007744|PDB:1LFC}
RP STRUCTURE BY NMR OF 36-60.
RX PubMed=9521752; DOI=10.1021/bi972323m;
RA Hwang P.M., Zhou N., Shan X., Arrowsmith C.H., Vogel H.J.;
RT "Three-dimensional solution structure of lactoferricin B, an antimicrobial
RT peptide derived from bovine lactoferrin.";
RL Biochemistry 37:4288-4298(1998).
CC -!- FUNCTION: Transferrins are iron binding transport proteins which can
CC bind two Fe(3+) ions in association with the binding of an anion,
CC usually bicarbonate.
CC -!- FUNCTION: Lactotransferrin is a major iron-binding and multifunctional
CC protein found in exocrine fluids such as breast milk and mucosal
CC secretions. Has antimicrobial activity. Antimicrobial properties may
CC include bacteriostasis, which is related to its ability to sequester
CC free iron and thus inhibit microbial growth, as well as direct
CC bactericidal properties leading to the release of lipopolysaccharides
CC from the bacterial outer membrane. The most effective inhibitory
CC activity is seen against E.coli and P.aeruginosa. Has anabolic,
CC differentiating and anti-apoptotic effects on osteoblasts and can also
CC inhibit osteoclastogenesis, possibly playing a role in the regulation
CC of bone growth. Interferes with the lipopolysaccharide (LPS)-stimulated
CC TLR4 signaling, but cannot directly stimulate the TLR4 signaling
CC pathway and subsequent NF-kappa-B activation.
CC -!- FUNCTION: Lactoferricin B is an antimicrobial peptide. Inhibits the
CC growth of Gram-negative and Gram-positive bacteria.
CC -!- FUNCTION: The lactotransferrin transferrin-like domain 1 functions as a
CC serine protease of the peptidase S60 family that cuts arginine rich
CC regions. This function contributes to the antimicrobial activity. Shows
CC a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-,
CC and of Z-Phe-Arg-|-aminomethylcoumarin sites.
CC -!- ACTIVITY REGULATION: Inhibited by PMSF and Pefabloc.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for Z-Phe-Arg-|-aminomethylcoumarin
CC {ECO:0000269|PubMed:15222473};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:15222473};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius.
CC {ECO:0000269|PubMed:15222473};
CC -!- SUBUNIT: Monomer. Found in a complex with LTF, CLU, EPPIN and SEMG1 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P24627; PRO_0000037570 [P27958]; Xeno; NbExp=3; IntAct=EBI-8076910, EBI-6904269;
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule {ECO:0000250}.
CC Note=Secreted into most exocrine fluids by various endothelial cells.
CC Stored in the secondary granules of neutrophils (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; X57084; CAA40366.1; -; mRNA.
DR EMBL; M63502; AAA30617.1; -; mRNA.
DR EMBL; L08604; AAA30609.1; -; mRNA.
DR EMBL; L19993; AAA21722.1; -; Genomic_DNA.
DR EMBL; L19982; AAA21722.1; JOINED; Genomic_DNA.
DR EMBL; L19983; AAA21722.1; JOINED; Genomic_DNA.
DR EMBL; L19984; AAA21722.1; JOINED; Genomic_DNA.
DR EMBL; L19985; AAA21722.1; JOINED; Genomic_DNA.
DR EMBL; L19986; AAA21722.1; JOINED; Genomic_DNA.
DR EMBL; L19988; AAA21722.1; JOINED; Genomic_DNA.
DR EMBL; L19989; AAA21722.1; JOINED; Genomic_DNA.
DR EMBL; L19990; AAA21722.1; JOINED; Genomic_DNA.
DR EMBL; L19991; AAA21722.1; JOINED; Genomic_DNA.
DR EMBL; L19992; AAA21722.1; JOINED; Genomic_DNA.
DR EMBL; L19981; AAA30610.1; -; mRNA.
DR EMBL; AB046664; BAB03470.1; -; mRNA.
DR EMBL; BC116051; AAI16052.1; -; mRNA.
DR PIR; I45919; TFBOL.
DR RefSeq; NP_851341.1; NM_180998.2.
DR RefSeq; XP_015315141.1; XM_015459655.1.
DR PDB; 1BLF; X-ray; 2.80 A; A=20-708.
DR PDB; 1LFC; NMR; -; A=36-60.
DR PDB; 1NKX; X-ray; 1.90 A; A=361-708.
DR PDB; 1SDX; X-ray; 2.06 A; A=361-695, E=700-704.
DR PDB; 1Y58; NMR; -; A=38-49.
DR PDB; 2ALU; X-ray; 2.09 A; A=361-708.
DR PDB; 2AYS; X-ray; 1.86 A; A=361-708.
DR PDB; 2B65; X-ray; 1.50 A; A=361-705.
DR PDB; 2DOJ; X-ray; 2.40 A; A=361-705.
DR PDB; 2DP8; X-ray; 2.50 A; A=361-705.
DR PDB; 2DQV; X-ray; 2.70 A; A=361-705.
DR PDB; 2DS9; X-ray; 2.80 A; A=361-705.
DR PDB; 2DSF; X-ray; 2.80 A; A=361-705.
DR PDB; 2DVC; X-ray; 3.00 A; A=361-705.
DR PDB; 2DWA; X-ray; 2.07 A; A=361-705.
DR PDB; 2DWH; X-ray; 2.80 A; A=361-705.
DR PDB; 2DWI; X-ray; 2.20 A; A=361-705.
DR PDB; 2DWJ; X-ray; 2.30 A; A=361-705.
DR PDB; 2DXR; X-ray; 2.85 A; A=361-705.
DR PDB; 2DXY; X-ray; 2.03 A; A=361-705.
DR PDB; 2DYX; X-ray; 2.00 A; A=361-705.
DR PDB; 2E0S; X-ray; 2.15 A; A=361-705.
DR PDB; 2E1S; X-ray; 2.70 A; A=361-705.
DR PDB; 2FA7; X-ray; 2.38 A; A=361-705.
DR PDB; 2G93; X-ray; 1.90 A; A=361-705.
DR PDB; 2H4I; X-ray; 2.55 A; A=361-705.
DR PDB; 2HCA; X-ray; 2.80 A; A=361-705.
DR PDB; 2MD1; NMR; -; A=287-303.
DR PDB; 2MD2; NMR; -; A=287-296.
DR PDB; 2MD3; NMR; -; A=296-303.
DR PDB; 2MD4; NMR; -; A=287-298.
DR PDB; 2NUV; X-ray; 2.25 A; A=361-705.
DR PDB; 2NWJ; X-ray; 2.25 A; A=361-705.
DR PDB; 2O1L; X-ray; 1.97 A; A=361-705.
DR PDB; 2O51; X-ray; 3.00 A; A=361-705.
DR PDB; 2OCU; X-ray; 2.38 A; A=361-705.
DR PDB; 2P1S; X-ray; 1.93 A; A=361-704.
DR PDB; 2PX1; X-ray; 2.50 A; A=361-705.
DR PDB; 2Q8J; X-ray; 2.71 A; A=361-708.
DR PDB; 2QJE; X-ray; 2.30 A; A=361-708.
DR PDB; 2R71; X-ray; 2.07 A; A=361-705.
DR PDB; 2R9J; X-ray; 2.55 A; A=361-705.
DR PDB; 2ZMB; X-ray; 2.90 A; A=361-705.
DR PDB; 3CFL; X-ray; 2.25 A; A=361-705.
DR PDB; 3CI8; X-ray; 2.40 A; A=361-705.
DR PDB; 3CRB; X-ray; 2.60 A; A=361-705.
DR PDB; 3E9X; X-ray; 2.70 A; A=361-705.
DR PDB; 3IAZ; X-ray; 2.00 A; A=361-705.
DR PDB; 3IB0; X-ray; 1.40 A; A=361-705.
DR PDB; 3IB1; X-ray; 2.20 A; A=361-705.
DR PDB; 3IB2; X-ray; 2.29 A; A=361-705.
DR PDB; 3K0V; X-ray; 1.91 A; A=361-705.
DR PDB; 3KJ7; X-ray; 1.91 A; A=361-705.
DR PDB; 3MJN; X-ray; 2.38 A; A=361-705.
DR PDB; 3O97; X-ray; 2.68 A; A=361-705.
DR PDB; 3RGY; X-ray; 2.00 A; A=361-705.
DR PDB; 3SDF; X-ray; 2.10 A; A=361-705.
DR PDB; 3TAJ; X-ray; 1.70 A; A=361-705.
DR PDB; 3TOD; X-ray; 1.38 A; A=361-695, B=700-705.
DR PDB; 3TTR; X-ray; 2.27 A; A=361-705.
DR PDB; 3TUS; X-ray; 2.50 A; A=361-705.
DR PDB; 3U72; X-ray; 2.20 A; A=361-695, B=700-705.
DR PDB; 3U8Q; X-ray; 1.97 A; A=361-695, B=700-705.
DR PDB; 3UGW; X-ray; 1.87 A; A=361-695, B=700-705.
DR PDB; 3UK4; X-ray; 1.98 A; A=361-695, B=700-705.
DR PDB; 3USD; X-ray; 2.40 A; A=361-695, B=700-705.
DR PDB; 3V5A; X-ray; 1.44 A; A=361-695, B=700-705.
DR PDB; 3VDF; X-ray; 1.46 A; A=361-695, B=700-705.
DR PDB; 4DIG; X-ray; 1.80 A; A=361-695, B=700-705.
DR PDB; 4DXU; X-ray; 1.46 A; A=361-695, B=700-705.
DR PDB; 4FIM; X-ray; 1.80 A; A=361-695, B=700-705.
DR PDB; 4FJP; X-ray; 1.68 A; A=361-695, B=700-705.
DR PDB; 4FOR; X-ray; 1.58 A; A=361-695, B=700-705.
DR PDB; 4G2Z; X-ray; 1.90 A; A=361-695, B=700-705.
DR PDB; 4G77; X-ray; 1.98 A; A=361-705.
DR PDB; 4G8H; X-ray; 1.88 A; A=361-705.
DR PDB; 4GRK; X-ray; 1.68 A; A=361-695, B=700-705.
DR PDB; 4N6P; X-ray; 1.40 A; A=361-695, B=700-705.
DR PDB; 4NED; X-ray; 2.10 A; A=361-705.
DR PDB; 4OQO; X-ray; 2.42 A; A/B=361-708.
DR PDB; 5CRY; X-ray; 2.79 A; A/B=361-708.
DR PDB; 5HBC; X-ray; 2.79 A; A/B=361-708.
DR PDB; 7ENU; X-ray; 2.32 A; A/B=361-708.
DR PDB; 7EQU; X-ray; 2.74 A; A/B=361-708.
DR PDB; 7EV0; X-ray; 2.70 A; A/P=361-708.
DR PDB; 7EVQ; X-ray; 2.60 A; A/B=361-708.
DR PDB; 7FDW; X-ray; 2.28 A; A/B=361-708.
DR PDBsum; 1BLF; -.
DR PDBsum; 1LFC; -.
DR PDBsum; 1NKX; -.
DR PDBsum; 1SDX; -.
DR PDBsum; 1Y58; -.
DR PDBsum; 2ALU; -.
DR PDBsum; 2AYS; -.
DR PDBsum; 2B65; -.
DR PDBsum; 2DOJ; -.
DR PDBsum; 2DP8; -.
DR PDBsum; 2DQV; -.
DR PDBsum; 2DS9; -.
DR PDBsum; 2DSF; -.
DR PDBsum; 2DVC; -.
DR PDBsum; 2DWA; -.
DR PDBsum; 2DWH; -.
DR PDBsum; 2DWI; -.
DR PDBsum; 2DWJ; -.
DR PDBsum; 2DXR; -.
DR PDBsum; 2DXY; -.
DR PDBsum; 2DYX; -.
DR PDBsum; 2E0S; -.
DR PDBsum; 2E1S; -.
DR PDBsum; 2FA7; -.
DR PDBsum; 2G93; -.
DR PDBsum; 2H4I; -.
DR PDBsum; 2HCA; -.
DR PDBsum; 2MD1; -.
DR PDBsum; 2MD2; -.
DR PDBsum; 2MD3; -.
DR PDBsum; 2MD4; -.
DR PDBsum; 2NUV; -.
DR PDBsum; 2NWJ; -.
DR PDBsum; 2O1L; -.
DR PDBsum; 2O51; -.
DR PDBsum; 2OCU; -.
DR PDBsum; 2P1S; -.
DR PDBsum; 2PX1; -.
DR PDBsum; 2Q8J; -.
DR PDBsum; 2QJE; -.
DR PDBsum; 2R71; -.
DR PDBsum; 2R9J; -.
DR PDBsum; 2ZMB; -.
DR PDBsum; 3CFL; -.
DR PDBsum; 3CI8; -.
DR PDBsum; 3CRB; -.
DR PDBsum; 3E9X; -.
DR PDBsum; 3IAZ; -.
DR PDBsum; 3IB0; -.
DR PDBsum; 3IB1; -.
DR PDBsum; 3IB2; -.
DR PDBsum; 3K0V; -.
DR PDBsum; 3KJ7; -.
DR PDBsum; 3MJN; -.
DR PDBsum; 3O97; -.
DR PDBsum; 3RGY; -.
DR PDBsum; 3SDF; -.
DR PDBsum; 3TAJ; -.
DR PDBsum; 3TOD; -.
DR PDBsum; 3TTR; -.
DR PDBsum; 3TUS; -.
DR PDBsum; 3U72; -.
DR PDBsum; 3U8Q; -.
DR PDBsum; 3UGW; -.
DR PDBsum; 3UK4; -.
DR PDBsum; 3USD; -.
DR PDBsum; 3V5A; -.
DR PDBsum; 3VDF; -.
DR PDBsum; 4DIG; -.
DR PDBsum; 4DXU; -.
DR PDBsum; 4FIM; -.
DR PDBsum; 4FJP; -.
DR PDBsum; 4FOR; -.
DR PDBsum; 4G2Z; -.
DR PDBsum; 4G77; -.
DR PDBsum; 4G8H; -.
DR PDBsum; 4GRK; -.
DR PDBsum; 4N6P; -.
DR PDBsum; 4NED; -.
DR PDBsum; 4OQO; -.
DR PDBsum; 5CRY; -.
DR PDBsum; 5HBC; -.
DR PDBsum; 7ENU; -.
DR PDBsum; 7EQU; -.
DR PDBsum; 7EV0; -.
DR PDBsum; 7EVQ; -.
DR PDBsum; 7FDW; -.
DR AlphaFoldDB; P24627; -.
DR BMRB; P24627; -.
DR PCDDB; P24627; -.
DR SMR; P24627; -.
DR BioGRID; 158240; 1.
DR IntAct; P24627; 4.
DR MINT; P24627; -.
DR STRING; 9913.ENSBTAP00000001704; -.
DR ChEMBL; CHEMBL2796; -.
DR Allergome; 1065; Bos d LF.
DR MEROPS; S60.001; -.
DR MEROPS; S60.970; -.
DR CarbonylDB; P24627; -.
DR GlyConnect; 319; 22 N-Linked glycans (4 sites).
DR PaxDb; P24627; -.
DR PeptideAtlas; P24627; -.
DR PRIDE; P24627; -.
DR Ensembl; ENSBTAT00000001704; ENSBTAP00000001704; ENSBTAG00000001292.
DR GeneID; 280846; -.
DR KEGG; bta:280846; -.
DR CTD; 4057; -.
DR VEuPathDB; HostDB:ENSBTAG00000001292; -.
DR VGNC; VGNC:31077; LTF.
DR eggNOG; ENOG502QSZB; Eukaryota.
DR GeneTree; ENSGT00940000156055; -.
DR HOGENOM; CLU_011309_1_0_1; -.
DR InParanoid; P24627; -.
DR OMA; KSVRWCT; -.
DR OrthoDB; 232859at2759; -.
DR TreeFam; TF324013; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-6799990; Metal sequestration by antimicrobial proteins.
DR Reactome; R-BTA-6803157; Antimicrobial peptides.
DR SABIO-RK; P24627; -.
DR EvolutionaryTrace; P24627; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000001292; Expressed in parenchyma of mammary gland and 102 other tissues.
DR ExpressionAtlas; P24627; baseline and differential.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0042581; C:specific granule; ISS:UniProtKB.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:CAFA.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0005506; F:iron ion binding; IEA:Ensembl.
DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IMP:AgBase.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0019732; P:antifungal humoral response; ISS:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IEA:Ensembl.
DR GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl.
DR GO; GO:0002227; P:innate immune response in mucosa; ISS:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:Ensembl.
DR GO; GO:0051673; P:membrane disruption in another organism; IEA:Ensembl.
DR GO; GO:0044793; P:negative regulation by host of viral process; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; IEA:Ensembl.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IDA:CAFA.
DR GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:2001205; P:negative regulation of osteoclast development; IDA:UniProtKB.
DR GO; GO:1900229; P:negative regulation of single-species biofilm formation in or on host organism; ISS:UniProtKB.
DR GO; GO:2000308; P:negative regulation of tumor necrosis factor (ligand) superfamily member 11 production; IDA:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:1900159; P:positive regulation of bone mineralization involved in bone maturation; IDA:UniProtKB.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IDA:UniProtKB.
DR GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0001817; P:regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; ISS:UniProtKB.
DR InterPro; IPR030684; Lactotransferrin.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR Pfam; PF00405; Transferrin; 2.
DR PIRSF; PIRSF500683; Lactotransferrin; 1.
DR PIRSF; PIRSF002549; Transferrin; 1.
DR PRINTS; PR00422; TRANSFERRIN.
DR SMART; SM00094; TR_FER; 2.
DR PROSITE; PS00205; TRANSFERRIN_LIKE_1; 2.
DR PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
DR PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunity; Ion transport; Iron;
KW Iron transport; Metal-binding; Osteogenesis; Protease; Reference proteome;
KW Repeat; Secreted; Serine protease; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:2805645"
FT CHAIN 20..708
FT /note="Lactotransferrin"
FT /id="PRO_0000035726"
FT PEPTIDE 36..60
FT /note="Lactoferricin-B"
FT /id="PRO_0000035727"
FT DOMAIN 25..352
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 364..693
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT ACT_SITE 92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT ACT_SITE 278
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 79
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF"
FT BINDING 111
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF"
FT BINDING 136
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 140
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 142
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 143
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 211
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF"
FT BINDING 272
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF"
FT BINDING 414
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF"
FT BINDING 452
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF"
FT BINDING 478
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 482
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 484
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 485
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 545
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF"
FT BINDING 614
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|Ref.15"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|Ref.15"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:9398529, ECO:0000269|Ref.15,
FT ECO:0007744|PDB:1BLF"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:9398529, ECO:0000269|Ref.15,
FT ECO:0007744|PDB:1BLF"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:9398529, ECO:0000269|Ref.15,
FT ECO:0007744|PDB:1BLF"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:9398529, ECO:0000269|Ref.15,
FT ECO:0007744|PDB:1BLF"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:9398529, ECO:0000269|Ref.15,
FT ECO:0007744|PDB:1BLF"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:9398529, ECO:0000269|Ref.15,
FT ECO:0007744|PDB:1BLF"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:9398529, ECO:0000269|Ref.15,
FT ECO:0007744|PDB:1BLF"
FT DISULFID 28..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 38..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 134..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 176..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 189..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 250..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|Ref.15"
FT DISULFID 367..399
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|Ref.15"
FT DISULFID 377..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|Ref.15"
FT DISULFID 424..703
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 444..666
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 476..551
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 500..694
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|Ref.15"
FT DISULFID 510..524
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|Ref.15"
FT DISULFID 521..534
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 592..606
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 644..649
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT CONFLICT 63
FT /note="E -> A (in Ref. 4; AAA21722)"
FT /evidence="ECO:0000305"
FT CONFLICT 66..67
FT /note="RA -> PG (in Ref. 2; AAA30617)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="I -> V (in Ref. 1; CAA40366 and 4; AAA21722/
FT AAA30610)"
FT /evidence="ECO:0000305"
FT CONFLICT 164..165
FT /note="LQ -> PP (in Ref. 1; CAA40366)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="C -> Y (in Ref. 4; AAA21722)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="A -> P (in Ref. 4; AAA21722)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="G -> A (in Ref. 4; AAA21722)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="S -> R (in Ref. 4; AAA21722)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="F -> S (in Ref. 2; AAA30617)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="G -> A (in Ref. 1; CAA40366)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="I -> V (in Ref. 4; AAA21722)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="S -> T (in Ref. 4; AAA30610)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="H -> Y (in Ref. 1; CAA40366 and 4; AAA30610)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="K -> R (in Ref. 4; AAA21722)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="A -> R (in Ref. 1; CAA40366 and 4; AAA30610)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="H -> R (in Ref. 5; BAB03470)"
FT /evidence="ECO:0000305"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:1BLF"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:1BLF"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1BLF"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1BLF"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:1BLF"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1BLF"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:1BLF"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1BLF"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:1BLF"
FT STRAND 104..120
FT /evidence="ECO:0007829|PDB:1BLF"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:1BLF"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:1BLF"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:1BLF"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1BLF"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:1BLF"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1BLF"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:1BLF"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1BLF"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:1BLF"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:1BLF"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:1BLF"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:1BLF"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:1BLF"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:1BLF"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:1BLF"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:1BLF"
FT HELIX 283..296
FT /evidence="ECO:0007829|PDB:1BLF"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:2MD1"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:1BLF"
FT HELIX 335..351
FT /evidence="ECO:0007829|PDB:1BLF"
FT HELIX 354..362
FT /evidence="ECO:0007829|PDB:1BLF"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:3TOD"
FT HELIX 370..383
FT /evidence="ECO:0007829|PDB:3TOD"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 387..395
FT /evidence="ECO:0007829|PDB:3TOD"
FT HELIX 396..404
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:3TOD"
FT HELIX 415..423
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 427..434
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:2B65"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:7FDW"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 452..459
FT /evidence="ECO:0007829|PDB:3TOD"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 474..478
FT /evidence="ECO:0007829|PDB:3TOD"
FT TURN 483..486
FT /evidence="ECO:0007829|PDB:3TOD"
FT HELIX 487..497
FT /evidence="ECO:0007829|PDB:3TOD"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 505..510
FT /evidence="ECO:0007829|PDB:3TOD"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 527..530
FT /evidence="ECO:0007829|PDB:7EVQ"
FT TURN 531..534
FT /evidence="ECO:0007829|PDB:3TOD"
FT HELIX 544..553
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 558..563
FT /evidence="ECO:0007829|PDB:3TOD"
FT HELIX 564..569
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 571..575
FT /evidence="ECO:0007829|PDB:2ZMB"
FT TURN 578..582
FT /evidence="ECO:0007829|PDB:3TOD"
FT HELIX 585..587
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 588..591
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:7EV0"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:3TOD"
FT HELIX 600..605
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 608..611
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 615..618
FT /evidence="ECO:0007829|PDB:3TOD"
FT HELIX 620..637
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:1SDX"
FT TURN 642..647
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:3IB0"
FT STRAND 658..660
FT /evidence="ECO:0007829|PDB:4OQO"
FT STRAND 664..668
FT /evidence="ECO:0007829|PDB:3TOD"
FT STRAND 671..673
FT /evidence="ECO:0007829|PDB:2O1L"
FT HELIX 676..680
FT /evidence="ECO:0007829|PDB:3TOD"
FT HELIX 682..692
FT /evidence="ECO:0007829|PDB:3TOD"
FT HELIX 698..703
FT /evidence="ECO:0007829|PDB:7FDW"
FT HELIX 704..707
FT /evidence="ECO:0007829|PDB:7FDW"
SQ SEQUENCE 708 AA; 78056 MW; C6FD7FC15D68E93F CRC64;
MKLFVPALLS LGALGLCLAA PRKNVRWCTI SQPEWFKCRR WQWRMKKLGA PSITCVRRAF
ALECIRAIAE KKADAVTLDG GMVFEAGRDP YKLRPVAAEI YGTKESPQTH YYAVAVVKKG
SNFQLDQLQG RKSCHTGLGR SAGWIIPMGI LRPYLSWTES LEPLQGAVAK FFSASCVPCI
DRQAYPNLCQ LCKGEGENQC ACSSREPYFG YSGAFKCLQD GAGDVAFVKE TTVFENLPEK
ADRDQYELLC LNNSRAPVDA FKECHLAQVP SHAVVARSVD GKEDLIWKLL SKAQEKFGKN
KSRSFQLFGS PPGQRDLLFK DSALGFLRIP SKVDSALYLG SRYLTTLKNL RETAEEVKAR
YTRVVWCAVG PEEQKKCQQW SQQSGQNVTC ATASTTDDCI VLVLKGEADA LNLDGGYIYT
AGKCGLVPVL AENRKSSKHS SLDCVLRPTE GYLAVAVVKK ANEGLTWNSL KDKKSCHTAV
DRTAGWNIPM GLIVNQTGSC AFDEFFSQSC APGADPKSRL CALCAGDDQG LDKCVPNSKE
KYYGYTGAFR CLAEDVGDVA FVKNDTVWEN TNGESTADWA KNLNREDFRL LCLDGTRKPV
TEAQSCHLAV APNHAVVSRS DRAAHVKQVL LHQQALFGKN GKNCPDKFCL FKSETKNLLF
NDNTECLAKL GGRPTYEEYL GTEYVTAIAN LKKCSTSPLL EACAFLTR
