CHICK:TRFE

Species (Taxon ID)	Gallus gallus (Chicken). (9031)
Gene Name(s)	No Information Provided.
Protein Name(s)	Ovotransferrin Allergen Gal d III Conalbumin Serum transferrin
External Links
UniProt	P02789
EMBL	X02009 Y00407
PIR	A26845
RefSeq	NP_990635.1
UniGene	Gga.2551
PDB	1AIV 1D9K 1IEJ 1IQ7 1JL4 1N04 1NFT 1NNT 1OVT 1RYX 1TFA 2D3I
PDBsum	1AIV 1D9K 1IEJ 1IQ7 1JL4 1N04 1NFT 1NNT 1OVT 1RYX 1TFA 2D3I
ProteinModelPortal	P02789
SMR	P02789
BioGrid	676501
IntAct	P02789
Allergome	3293 361
MEROPS	S60.970
UniCarbKB	P02789
PaxDb	P02789
PRIDE	P02789
GeneID	396241
KEGG	gga:396241
CTD	7018
eggNOG	COG2229
HOVERGEN	HBG000055
KO	K14736
PhylomeDB	P02789
EvolutionaryTrace	P02789
NextBio	20816293
Proteomes	UP000000539
GO	GO:0031012 GO:0005615 GO:0008199 GO:0006953 GO:0006879 GO:0006826 GO:0032496
InterPro	IPR016357 IPR001156 IPR018195
Pfam	PF00405
PIRSF	PIRSF002549
PRINTS	PR00422
SMART	SM00094
PROSITE	PS00205 PS00206 PS00207 PS51408

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0005615	extracellular space	PMID:721826^[1]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005506	iron ion binding	PMID:6895872^[2]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006881	extracellular sequestering of iron ion	PMID:7490743^[3]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006826	iron ion transport	PMID:7490743^[3]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005506	iron ion binding	PMID:7490743^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:16721662^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008199	ferric iron binding	PMID:15323571^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:15323571^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:6805466^[6]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008199	ferric iron binding	PMID:6319414^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	PMID:10777107^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005506	iron ion binding	PMID:173291^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008199	ferric iron binding	PMID:7881176^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005623	cell	PMID:25086240^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000019)	Seeded From UniProt	complete
involved_in	GO:0032496	response to lipopolysaccharide	PMID:10777107^[8]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:1990377	organomineral extracellular matrix	PMID:10780658^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006953	acute-phase response	PMID:10777107^[8]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:10875774^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:10777107^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR018195	C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016357	C		Seeded From UniProt	complete
involved_in	GO:0019730	antimicrobial humoral response	PMID:3032619^[14]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:272676^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006880	intracellular sequestering of iron ion	PMID:18459044^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
involved_in	GO:0006811	ion transport	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0406	P		Seeded From UniProt	complete
involved_in	GO:0055072	iron ion homeostasis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0410	P		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Thibodeau, SN et al. (1978) Precursor of egg white ovomucoid. Amino acid sequence of an NH2-terminal extension. J. Biol. Chem. 253 9018-23 PubMed GONUTS page
↑ Williams, J et al. (1982) The primary structure of hen ovotransferrin. Eur. J. Biochem. 122 297-303 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Kurokawa, H et al. (1995) Crystal structure of diferric hen ovotransferrin at 2.4 A resolution. J. Mol. Biol. 254 196-207 PubMed GONUTS page
↑ Ahlborn, GJ et al. (2006) Identification of eggshell membrane proteins and purification of ovotransferrin and beta-NAGase from hen egg white. Protein J. 25 71-81 PubMed GONUTS page
↑ ^5.0 ^5.1 Okamoto, I et al. (2004) Iron-binding process in the amino- and carboxyl-terminal lobes of ovotransferrin: quantitative studies utilizing single Fe3+-binding mutants. Biochemistry 43 11118-25 PubMed GONUTS page
↑ Williams, J et al. (1982) Evolutionary significance of the renal excretion of transferrin half-molecule fragments. Biochem. J. 201 417-9 PubMed GONUTS page
↑ Brown-Mason, A & Woodworth, RC (1984) Physiological levels of binding and iron donation by complementary half-molecules of ovotransferrin to transferrin receptors of chick reticulocytes. J. Biol. Chem. 259 1866-73 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Cermelli, S et al. (2000) Extracellular fatty acid binding protein (Ex-FABP) modulation by inflammatory agents: "physiological" acute phase response in endochondral bone formation. Eur. J. Cell Biol. 79 155-64 PubMed GONUTS page
↑ Butterworth, RM et al. (1975) Electron-paramagnetic-resonance spectroscopy of iron-binding fragments of hen ovotransferrins. Biochem. J. 149 559-63 PubMed GONUTS page
↑ Jacquinot, PM et al. (1994) Change in glycosylation of chicken transferrin glycans biosynthesized during embryogenesis and primary culture of embryo hepatocytes. Glycobiology 4 617-24 PubMed GONUTS page
↑ Labas, V et al. (2015) Qualitative and quantitative peptidomic and proteomic approaches to phenotyping chicken semen. J Proteomics 112 313-35 PubMed GONUTS page
↑ Panheleux, M et al. (2000) Extraction and quantification by ELISA of eggshell organic matrix proteins (ovocleidin-17, ovalbumin, ovotransferrin) in shell from young and old hens. Poult. Sci. 79 580-8 PubMed GONUTS page
↑ Dominguez-Vera, JM et al. (2000) The effect of avian uterine fluid on the growth behavior of calcite crystals. Poult. Sci. 79 901-7 PubMed GONUTS page
↑ Crichton, RR & Charloteaux-Wauters, M (1987) Iron transport and storage. Eur. J. Biochem. 164 485-506 PubMed GONUTS page
↑ Palmiter, RD et al. (1978) Ovalbumin: a secreted protein without a transient hydrophobic leader sequence. Proc. Natl. Acad. Sci. U.S.A. 75 94-8 PubMed GONUTS page
↑ Kim, DW et al. (2008) Expression of transferrin binding protein in the capillaries of the brain in the developing chick embryo. Neurochem. Res. 33 2288-93 PubMed GONUTS page

[PMID:721826-1] Thibodeau, SN et al. (1978) Precursor of egg white ovomucoid. Amino acid sequence of an NH2-terminal extension. J. Biol. Chem. 253 9018-23 PubMed GONUTS page

[PMID:6895872-2] Williams, J et al. (1982) The primary structure of hen ovotransferrin. Eur. J. Biochem. 122 297-303 PubMed GONUTS page

[PMID:7490743-3] 3.0 ^3.1 ^3.2 Kurokawa, H et al. (1995) Crystal structure of diferric hen ovotransferrin at 2.4 A resolution. J. Mol. Biol. 254 196-207 PubMed GONUTS page

[PMID:16721662-4] Ahlborn, GJ et al. (2006) Identification of eggshell membrane proteins and purification of ovotransferrin and beta-NAGase from hen egg white. Protein J. 25 71-81 PubMed GONUTS page

[PMID:15323571-5] 5.0 ^5.1 Okamoto, I et al. (2004) Iron-binding process in the amino- and carboxyl-terminal lobes of ovotransferrin: quantitative studies utilizing single Fe3+-binding mutants. Biochemistry 43 11118-25 PubMed GONUTS page

[PMID:6805466-6] Williams, J et al. (1982) Evolutionary significance of the renal excretion of transferrin half-molecule fragments. Biochem. J. 201 417-9 PubMed GONUTS page

[PMID:6319414-7] Brown-Mason, A & Woodworth, RC (1984) Physiological levels of binding and iron donation by complementary half-molecules of ovotransferrin to transferrin receptors of chick reticulocytes. J. Biol. Chem. 259 1866-73 PubMed GONUTS page

[PMID:10777107-8] 8.0 ^8.1 ^8.2 ^8.3 Cermelli, S et al. (2000) Extracellular fatty acid binding protein (Ex-FABP) modulation by inflammatory agents: "physiological" acute phase response in endochondral bone formation. Eur. J. Cell Biol. 79 155-64 PubMed GONUTS page

[PMID:173291-9] Butterworth, RM et al. (1975) Electron-paramagnetic-resonance spectroscopy of iron-binding fragments of hen ovotransferrins. Biochem. J. 149 559-63 PubMed GONUTS page

[PMID:7881176-10] Jacquinot, PM et al. (1994) Change in glycosylation of chicken transferrin glycans biosynthesized during embryogenesis and primary culture of embryo hepatocytes. Glycobiology 4 617-24 PubMed GONUTS page

[PMID:25086240-11] Labas, V et al. (2015) Qualitative and quantitative peptidomic and proteomic approaches to phenotyping chicken semen. J Proteomics 112 313-35 PubMed GONUTS page

[PMID:10780658-12] Panheleux, M et al. (2000) Extraction and quantification by ELISA of eggshell organic matrix proteins (ovocleidin-17, ovalbumin, ovotransferrin) in shell from young and old hens. Poult. Sci. 79 580-8 PubMed GONUTS page

[PMID:10875774-13] Dominguez-Vera, JM et al. (2000) The effect of avian uterine fluid on the growth behavior of calcite crystals. Poult. Sci. 79 901-7 PubMed GONUTS page

[PMID:3032619-14] Crichton, RR & Charloteaux-Wauters, M (1987) Iron transport and storage. Eur. J. Biochem. 164 485-506 PubMed GONUTS page

[PMID:272676-15] Palmiter, RD et al. (1978) Ovalbumin: a secreted protein without a transient hydrophobic leader sequence. Proc. Natl. Acad. Sci. U.S.A. 75 94-8 PubMed GONUTS page

[PMID:18459044-16] Kim, DW et al. (2008) Expression of transferrin binding protein in the capillaries of the brain in the developing chick embryo. Neurochem. Res. 33 2288-93 PubMed GONUTS page

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CHICK:TRFE

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