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Ovotransferrin (Allergen Gal d III) (Conalbumin) (Serum transferrin) (allergen Gal d 3)

 TRFE_CHICK              Reviewed;         705 AA.
P02789;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
10-MAY-2017, entry version 144.
RecName: Full=Ovotransferrin;
AltName: Full=Allergen Gal d III;
AltName: Full=Conalbumin;
AltName: Full=Serum transferrin;
AltName: Allergen=Gal d 3;
Flags: Precursor;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7060577; DOI=10.1111/j.1432-1033.1982.tb05879.x;
Jeltsch J.-M., Chambon P.;
"The complete nucleotide sequence of the chicken ovotransferrin
mRNA.";
Eur. J. Biochem. 122:291-295(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3658709; DOI=10.1093/nar/15.18.7643;
Jeltsch J.-M., Hen R., Maroteaux L., Garnier J.-M., Chambon P.;
"Sequence of the chicken ovotransferrin gene.";
Nucleic Acids Res. 15:7643-7645(1987).
[3]
PROTEIN SEQUENCE OF 1-19.
TISSUE=Egg white, and Serum;
PubMed=649604;
Thibodeau S.N., Lee D.C., Palmiter R.D.;
"Identical precursors for serum transferrin and egg white
conalbumin.";
J. Biol. Chem. 253:3771-3774(1978).
[4]
PARTIAL PROTEIN SEQUENCE.
PubMed=6895872; DOI=10.1111/j.1432-1033.1982.tb05880.x;
Williams J., Elleman T.C., Kingston I.B., Wilkins A.G., Kuhn K.A.;
"The primary structure of hen ovotransferrin.";
Eur. J. Biochem. 122:297-303(1982).
[5]
PROTEIN SEQUENCE OF 480-582.
PubMed=1172663; DOI=10.1042/bj1470463;
Kingston I.B., Williams J.;
"The amino acid sequence of a carbohydrate-containing fragment of hen
ovotransferrin.";
Biochem. J. 147:463-472(1975).
[6]
DISULFIDE BONDS.
PubMed=4907959; DOI=10.1042/bj1160515;
Elleman T.C., Williams J.;
"The amino acid sequences of cysteic acid-containing peptides from
performic acid-oxidized ovotransferrin.";
Biochem. J. 116:515-532(1970).
[7]
STRUCTURE OF CARBOHYDRATES.
PubMed=574451; DOI=10.1111/j.1432-1033.1979.tb04203.x;
Dorland L., Haverkamp J., Vliegenthart J.F.G., Spik G., Fournet B.,
Montreuil J.;
"Investigation by 360-MHz 1H-nuclear-magnetic-resonance spectroscopy
and methylation analysis of the single glycan chain of chicken
ovotransferrin.";
Eur. J. Biochem. 100:569-574(1979).
[8]
STRUCTURE OF CARBOHYDRATES.
PubMed=7881176; DOI=10.1093/glycob/4.5.617;
Jacquinot P.-M., Leger D., Wieruszeski J.-M., Coddeville B.,
Montreuil J., Spik G.;
"Change in glycosylation of chicken transferrin glycans biosynthesized
during embryogenesis and primary culture of embryo hepatocytes.";
Glycobiology 4:617-624(1994).
[9]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-351.
PubMed=8218271; DOI=10.1021/bi00096a004;
Dewan J.C., Mikami B., Hirose M., Sacchettini J.C.;
"Structural evidence for a pH-sensitive dilysine trigger in the hen
ovotransferrin N-lobe: implications for transferrin iron release.";
Biochemistry 32:11963-11968(1993).
[10]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND METAL- AND
CARBONATE-BINDING SITES.
PubMed=7490743; DOI=10.1006/jmbi.1995.0611;
Kurokawa H., Mikami B., Hirose M.;
"Crystal structure of diferric hen ovotransferrin at 2.4-A
resolution.";
J. Mol. Biol. 254:196-207(1995).
[11]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=10497206; DOI=10.1074/jbc.274.40.28445;
Kurokawa H., Dewan J.C., Mikami B., Sacchettini J.C., Hirose M.;
"Crystal structure of hen apo-ovotransferrin. Both lobes adopt an open
conformation upon loss of iron.";
J. Biol. Chem. 274:28445-28452(1999).
-!- FUNCTION: Transferrins are iron binding transport proteins which
can bind two Fe(3+) ions in association with the binding of an
anion, usually bicarbonate. Responsible for the transport of iron
from sites of absorption and heme degradation to those of storage
and utilization. There are two forms of hen transferrin,
ovotransferrin, found in the ovoducts and, serum transferrin,
secreted by the liver. Serum transferrin may also have a role in
stimulating cell proliferation and is regulated by iron levels.
Ovotransferrin has a bacteriostatic function and, is not
controlled by iron levels.
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: Different forms of hen transferrin are distinguished by their
carbohydrate composition. Ovotransferrin and embryo serum
transferrin but not adult serum transferrin, have bisecting N-
acetylglucosamine. Transferrin secreted by embryo hepatocytes in
primary culture is marked by the presence of (alpha1-6)
fucosylation of the core N-acetylglucosamine. Serum transferrins
also differ in the number of attached neuraminic acid residues. In
both embryo forms, sialylation occurs on the Man (alpha 1-3)-
linked antennae.
-!- ALLERGEN: Causes an allergic reaction in human.
-!- SIMILARITY: Belongs to the transferrin family.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
-----------------------------------------------------------------------
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EMBL; X02009; CAA26040.1; -; mRNA.
EMBL; Y00407; CAA68468.1; -; Genomic_DNA.
PIR; A26845; TFCHE.
RefSeq; NP_990635.1; NM_205304.1.
UniGene; Gga.2551; -.
PDB; 1AIV; X-ray; 3.00 A; A=20-705.
PDB; 1D9K; X-ray; 3.20 A; P/Q=153-165.
PDB; 1IEJ; X-ray; 1.65 A; A=20-351.
PDB; 1IQ7; X-ray; 2.30 A; A=361-705.
PDB; 1JL4; X-ray; 4.30 A; C=153-165.
PDB; 1N04; X-ray; 2.80 A; A=20-705.
PDB; 1NFT; X-ray; 2.10 A; A=23-351.
PDB; 1NNT; X-ray; 2.30 A; A=24-351.
PDB; 1OVT; X-ray; 2.40 A; A=20-705.
PDB; 1RYX; X-ray; 3.50 A; A=20-705.
PDB; 1TFA; X-ray; 1.90 A; A=23-351.
PDB; 2D3I; X-ray; 2.15 A; A=20-705.
PDBsum; 1AIV; -.
PDBsum; 1D9K; -.
PDBsum; 1IEJ; -.
PDBsum; 1IQ7; -.
PDBsum; 1JL4; -.
PDBsum; 1N04; -.
PDBsum; 1NFT; -.
PDBsum; 1NNT; -.
PDBsum; 1OVT; -.
PDBsum; 1RYX; -.
PDBsum; 1TFA; -.
PDBsum; 2D3I; -.
ProteinModelPortal; P02789; -.
SMR; P02789; -.
BioGrid; 676501; 1.
IntAct; P02789; 2.
Allergome; 3293; Gal d 3.0101.
Allergome; 361; Gal d 3.
MEROPS; S60.970; -.
UniCarbKB; P02789; -.
PRIDE; P02789; -.
GeneID; 396241; -.
KEGG; gga:396241; -.
CTD; 7018; -.
HOVERGEN; HBG000055; -.
KO; K14736; -.
PhylomeDB; P02789; -.
EvolutionaryTrace; P02789; -.
PRO; PR:P02789; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005623; C:cell; IDA:AgBase.
GO; GO:0031012; C:extracellular matrix; IDA:AgBase.
GO; GO:0005615; C:extracellular space; IDA:AgBase.
GO; GO:0008199; F:ferric iron binding; IDA:AgBase.
GO; GO:0005506; F:iron ion binding; IDA:AgBase.
GO; GO:0006953; P:acute-phase response; IEP:AgBase.
GO; GO:0019730; P:antimicrobial humoral response; TAS:AgBase.
GO; GO:0006881; P:extracellular sequestering of iron ion; NAS:AgBase.
GO; GO:0006880; P:intracellular sequestering of iron ion; TAS:AgBase.
GO; GO:0006826; P:iron ion transport; NAS:AgBase.
GO; GO:0042493; P:response to drug; IMP:AgBase.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:AgBase.
InterPro; IPR016357; Transferrin.
InterPro; IPR001156; Transferrin-like_dom.
InterPro; IPR018195; Transferrin_Fe_BS.
Pfam; PF00405; Transferrin; 2.
PIRSF; PIRSF002549; Transferrin; 1.
PRINTS; PR00422; TRANSFERRIN.
SMART; SM00094; TR_FER; 2.
PROSITE; PS00205; TRANSFERRIN_LIKE_1; 2.
PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
1: Evidence at protein level;
3D-structure; Allergen; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Ion transport; Iron; Iron transport;
Metal-binding; Polymorphism; Reference proteome; Repeat; Secreted;
Signal; Transport.
SIGNAL 1 19 {ECO:0000269|PubMed:649604}.
CHAIN 20 705 Ovotransferrin.
/FTId=PRO_0000035719.
DOMAIN 26 352 Transferrin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
DOMAIN 364 689 Transferrin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
REGION 352 360 Connecting region.
METAL 79 79 Iron 1.
METAL 111 111 Iron 1.
METAL 210 210 Iron 1.
METAL 269 269 Iron 1.
METAL 414 414 Iron 2.
METAL 450 450 Iron 2.
METAL 543 543 Iron 2.
METAL 611 611 Iron 2.
BINDING 136 136 Carbonate 1.
BINDING 140 140 Carbonate 1.
BINDING 142 142 Carbonate 1; via amide nitrogen.
BINDING 143 143 Carbonate 1; via amide nitrogen.
BINDING 475 475 Carbonate 2.
BINDING 479 479 Carbonate 2.
BINDING 481 481 Carbonate 2; via amide nitrogen.
BINDING 482 482 Carbonate 2; via amide nitrogen.
CARBOHYD 492 492 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:6895872}.
DISULFID 29 64 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:4907959,
ECO:0000269|PubMed:6895872}.
DISULFID 39 55 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:4907959}.
DISULFID 134 216 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:4907959,
ECO:0000269|PubMed:6895872}.
DISULFID 179 193 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:4907959,
ECO:0000269|PubMed:6895872}.
DISULFID 190 201 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:4907959,
ECO:0000269|PubMed:6895872}.
DISULFID 247 261 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:4907959,
ECO:0000269|PubMed:6895872}.
DISULFID 367 399 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:4907959,
ECO:0000269|PubMed:6895872}.
DISULFID 377 390 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:4907959}.
DISULFID 424 699 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:4907959}.
DISULFID 440 662 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:4907959,
ECO:0000269|PubMed:6895872}.
DISULFID 473 549 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:4907959,
ECO:0000269|PubMed:6895872}.
DISULFID 497 690 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:4907959,
ECO:0000269|PubMed:6895872}.
DISULFID 507 521 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:4907959}.
DISULFID 518 532 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:4907959}.
DISULFID 589 603 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:4907959}.
VARIANT 83 83 A -> V.
VARIANT 100 100 V -> I.
VARIANT 154 154 R -> W.
VARIANT 239 240 QK -> LN.
VARIANT 686 686 S -> N.
CONFLICT 132 132 T -> N (in Ref. 1; CAA26040).
{ECO:0000305}.
CONFLICT 317 317 L -> F (in Ref. 1; CAA26040).
{ECO:0000305}.
STRAND 24 32 {ECO:0000244|PDB:1IEJ}.
HELIX 33 45 {ECO:0000244|PDB:1IEJ}.
TURN 46 48 {ECO:0000244|PDB:1IEJ}.
STRAND 49 57 {ECO:0000244|PDB:1IEJ}.
HELIX 61 69 {ECO:0000244|PDB:1IEJ}.
TURN 70 72 {ECO:0000244|PDB:1AIV}.
STRAND 75 78 {ECO:0000244|PDB:1IEJ}.
HELIX 80 87 {ECO:0000244|PDB:1IEJ}.
TURN 89 91 {ECO:0000244|PDB:1IEJ}.
STRAND 94 102 {ECO:0000244|PDB:1IEJ}.
STRAND 104 118 {ECO:0000244|PDB:1IEJ}.
HELIX 125 127 {ECO:0000244|PDB:1IEJ}.
STRAND 129 131 {ECO:0000244|PDB:1AIV}.
STRAND 132 136 {ECO:0000244|PDB:1IEJ}.
TURN 141 144 {ECO:0000244|PDB:1IEJ}.
HELIX 145 153 {ECO:0000244|PDB:1IEJ}.
STRAND 155 157 {ECO:0000244|PDB:1RYX}.
HELIX 162 164 {ECO:0000244|PDB:1IEJ}.
HELIX 167 174 {ECO:0000244|PDB:1IEJ}.
STRAND 175 179 {ECO:0000244|PDB:1IEJ}.
HELIX 187 190 {ECO:0000244|PDB:1IEJ}.
TURN 197 201 {ECO:0000244|PDB:1IEJ}.
STRAND 205 207 {ECO:0000244|PDB:1RYX}.
HELIX 209 218 {ECO:0000244|PDB:1IEJ}.
STRAND 223 228 {ECO:0000244|PDB:1IEJ}.
HELIX 231 235 {ECO:0000244|PDB:1IEJ}.
STRAND 237 239 {ECO:0000244|PDB:1AIV}.
HELIX 240 242 {ECO:0000244|PDB:1IEJ}.
STRAND 243 246 {ECO:0000244|PDB:1IEJ}.
STRAND 248 250 {ECO:0000244|PDB:1AIV}.
STRAND 252 254 {ECO:0000244|PDB:1IEJ}.
HELIX 255 257 {ECO:0000244|PDB:1IEJ}.
TURN 258 260 {ECO:0000244|PDB:1IEJ}.
STRAND 263 267 {ECO:0000244|PDB:1IEJ}.
STRAND 270 273 {ECO:0000244|PDB:1IEJ}.
STRAND 275 277 {ECO:0000244|PDB:1N04}.
HELIX 279 293 {ECO:0000244|PDB:1IEJ}.
STRAND 294 296 {ECO:0000244|PDB:1OVT}.
STRAND 298 300 {ECO:0000244|PDB:1IEJ}.
STRAND 308 310 {ECO:0000244|PDB:1IEJ}.
HELIX 312 314 {ECO:0000244|PDB:1IEJ}.
STRAND 315 319 {ECO:0000244|PDB:1NFT}.
STRAND 323 328 {ECO:0000244|PDB:1IEJ}.
HELIX 335 339 {ECO:0000244|PDB:1IEJ}.
HELIX 341 350 {ECO:0000244|PDB:1IEJ}.
STRAND 354 357 {ECO:0000244|PDB:1OVT}.
TURN 359 362 {ECO:0000244|PDB:1N04}.
STRAND 363 369 {ECO:0000244|PDB:2D3I}.
HELIX 370 383 {ECO:0000244|PDB:2D3I}.
TURN 384 386 {ECO:0000244|PDB:2D3I}.
STRAND 387 395 {ECO:0000244|PDB:2D3I}.
HELIX 396 405 {ECO:0000244|PDB:2D3I}.
STRAND 410 413 {ECO:0000244|PDB:2D3I}.
HELIX 415 423 {ECO:0000244|PDB:2D3I}.
STRAND 427 433 {ECO:0000244|PDB:2D3I}.
HELIX 437 439 {ECO:0000244|PDB:2D3I}.
STRAND 441 445 {ECO:0000244|PDB:1AIV}.
STRAND 450 460 {ECO:0000244|PDB:2D3I}.
HELIX 465 467 {ECO:0000244|PDB:1OVT}.
STRAND 470 475 {ECO:0000244|PDB:2D3I}.
TURN 480 483 {ECO:0000244|PDB:2D3I}.
HELIX 484 494 {ECO:0000244|PDB:2D3I}.
HELIX 499 501 {ECO:0000244|PDB:2D3I}.
STRAND 503 507 {ECO:0000244|PDB:2D3I}.
STRAND 513 515 {ECO:0000244|PDB:1IQ7}.
HELIX 516 518 {ECO:0000244|PDB:2D3I}.
STRAND 525 528 {ECO:0000244|PDB:2D3I}.
STRAND 534 540 {ECO:0000244|PDB:1RYX}.
HELIX 542 552 {ECO:0000244|PDB:2D3I}.
STRAND 555 560 {ECO:0000244|PDB:2D3I}.
HELIX 563 566 {ECO:0000244|PDB:2D3I}.
STRAND 568 571 {ECO:0000244|PDB:1N04}.
TURN 575 579 {ECO:0000244|PDB:2D3I}.
HELIX 582 584 {ECO:0000244|PDB:2D3I}.
STRAND 585 588 {ECO:0000244|PDB:2D3I}.
STRAND 590 592 {ECO:0000244|PDB:1OVT}.
STRAND 594 596 {ECO:0000244|PDB:2D3I}.
HELIX 597 602 {ECO:0000244|PDB:2D3I}.
STRAND 605 608 {ECO:0000244|PDB:2D3I}.
STRAND 612 615 {ECO:0000244|PDB:2D3I}.
HELIX 617 619 {ECO:0000244|PDB:2D3I}.
HELIX 620 634 {ECO:0000244|PDB:2D3I}.
TURN 639 643 {ECO:0000244|PDB:2D3I}.
STRAND 650 652 {ECO:0000244|PDB:2D3I}.
STRAND 654 656 {ECO:0000244|PDB:1IQ7}.
STRAND 662 665 {ECO:0000244|PDB:2D3I}.
HELIX 672 676 {ECO:0000244|PDB:2D3I}.
HELIX 678 687 {ECO:0000244|PDB:2D3I}.
TURN 688 690 {ECO:0000244|PDB:2D3I}.
HELIX 694 703 {ECO:0000244|PDB:2D3I}.
SEQUENCE 705 AA; 77777 MW; 864201A93146FA84 CRC64;
MKLILCTVLS LGIAAVCFAA PPKSVIRWCT ISSPEEKKCN NLRDLTQQER ISLTCVQKAT
YLDCIKAIAN NEADAISLDG GQAFEAGLAP YKLKPIAAEV YEHTEGSTTS YYAVAVVKKG
TEFTVNDLQG KTSCHTGLGR SAGWNIPIGT LLHRGAIEWE GIESGSVEQA VAKFFSASCV
PGATIEQKLC RQCKGDPKTK CARNAPYSGY SGAFHCLKDG KGDVAFVKHT TVNENAPDQK
DEYELLCLDG SRQPVDNYKT CNWARVAAHA VVARDDNKVE DIWSFLSKAQ SDFGVDTKSD
FHLFGPPGKK DPVLKDLLFK DSAIMLKRVP SLMDSQLYLG FEYYSAIQSM RKDQLTPSPR
ENRIQWCAVG KDEKSKCDRW SVVSNGDVEC TVVDETKDCI IKIMKGEADA VALDGGLVYT
AGVCGLVPVM AERYDDESQC SKTDERPASY FAVAVARKDS NVNWNNLKGK KSCHTAVGRT
AGWVIPMGLI HNRTGTCNFD EYFSEGCAPG SPPNSRLCQL CQGSGGIPPE KCVASSHEKY
FGYTGALRCL VEKGDVAFIQ HSTVEENTGG KNKADWAKNL QMDDFELLCT DGRRANVMDY
RECNLAEVPT HAVVVRPEKA NKIRDLLERQ EKRFGVNGSE KSKFMMFESQ NKDLLFKDLT
KCLFKVREGT TYKEFLGDKF YTVISSLKTC NPSDILQMCS FLEGK


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