AVID_CHICK
ID AVID_CHICK Reviewed; 152 AA.
AC P02701; Q91958; Q98SH4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Avidin;
DE Flags: Precursor;
GN Name=AVD;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3575102; DOI=10.1093/nar/15.8.3595;
RA Gope M.L., Keinaenen R.A., Kristo P.A., Conneely O.M., Beatie W.G.,
RA Zarucki-Schulz T., O'Malley B.W., Kulomaa M.S.;
RT "Molecular cloning of the chicken avidin cDNA.";
RL Nucleic Acids Res. 15:3595-3606(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2143802; DOI=10.1016/0076-6879(90)84261-e;
RA Chandra G., Gray J.G.;
RT "Cloning and expression of avidin in Escherichia coli.";
RL Methods Enzymol. 184:70-79(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=White leghorn; TISSUE=Oviduct;
RX PubMed=7665080; DOI=10.1016/0378-1119(95)00187-b;
RA Wallen M.J., Laukkanen M.O., Kulomaa M.S.;
RT "Cloning and sequencing of the chicken egg-white avidin-encoding gene and
RT its relationship with the avidin-related genes Avr1-Avr5.";
RL Gene 161:205-209(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-58.
RX PubMed=11167523; DOI=10.1046/j.1365-2052.2000.00681.x;
RA Ahlroth M.K., Kola E.H., Ewald D., Masabanda J., Sazanov A., Fries R.,
RA Kulomaa M.S.;
RT "Characterization and chromosomal localization of the chicken avidin gene
RT family.";
RL Anim. Genet. 31:367-375(2000).
RN [5]
RP PROTEIN SEQUENCE OF 25-152, AND GLYCOSYLATION AT ASN-41.
RX PubMed=5100763; DOI=10.1016/s0021-9258(18)62469-x;
RA Delange R.J., Huang T.-S.;
RT "Egg white avidin. 3. Sequence of the 78-residue middle cyanogen bromide
RT peptide. Complete amino acid sequence of the protein subunit.";
RL J. Biol. Chem. 246:698-709(1971).
RN [6]
RP PROTEIN SEQUENCE OF 25-152, AND VARIANT THR-58.
RX PubMed=5100762; DOI=10.1016/s0021-9258(18)62468-8;
RA Huang T.-S., DeLange R.J.;
RT "Egg white avidin. II. Isolation, composition, and amino acid sequences of
RT the tryptic peptides.";
RL J. Biol. Chem. 246:686-697(1971).
RN [7]
RP IMPORTANCE OF TYR IN BIOTIN-BINDING.
RX PubMed=2386489; DOI=10.1042/bj2690527;
RA Gitlin G., Bayer E.A., Wilchek M.;
RT "Studies on the biotin-binding sites of avidin and streptavidin. Tyrosine
RT residues are involved in the binding site.";
RL Biochem. J. 269:527-530(1990).
RN [8]
RP BIOTIN-BINDING STUDIES.
RX PubMed=1898347; DOI=10.1042/bj2780573;
RA Hiller Y., Bayer E.A., Wilchek M.;
RT "Studies on the biotin-binding site of avidin. Minimized fragments that
RT bind biotin.";
RL Biochem. J. 278:573-585(1991).
RN [9]
RP STRUCTURE OF CARBOHYDRATE.
RX PubMed=6816268; DOI=10.1021/bi00264a033;
RA Bruch R.C., White H.B. III;
RT "Compositional and structural heterogeneity of avidin glycopeptides.";
RL Biochemistry 21:5334-5341(1982).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=8506353; DOI=10.1073/pnas.90.11.5076;
RA Livnah O., Bayer E.A., Wilchek M., Sussman J.L.;
RT "Three-dimensional structures of avidin and the avidin-biotin complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5076-5080(1993).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=8515446; DOI=10.1006/jmbi.1993.1321;
RA Pugliese L., Coda A., Malcovati M., Bolognesi M.;
RT "Three-dimensional structure of the tetragonal crystal form of egg-white
RT avidin in its functional complex with biotin at 2.7-A resolution.";
RL J. Mol. Biol. 231:698-710(1993).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=9760187; DOI=10.1046/j.1432-1327.1998.2560453.x;
RA Nardone E., Rosano C., Santambrogio P., Curnis F., Corti A., Magni F.,
RA Siccardi A.G., Paganelli G., Losso R., Apreda B., Bolognesi M., Sidoli A.,
RA Arosio P.;
RT "Biochemical characterization and crystal structure of a recombinant hen
RT avidin and its acidic mutant expressed in Escherichia coli.";
RL Eur. J. Biochem. 256:453-460(1998).
CC -!- FUNCTION: The biological function of avidin is not known. Forms a
CC strong non-covalent specific complex with biotin (one molecule of
CC biotin per subunit of avidin).
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Synthesized in hen oviduct and concentrated in egg
CC white (where it represent 0.05% of the total protein).
CC -!- PTM: N-linked glycan at Asn-41 consists of GlcNAc(beta1-2)Man(alpha1-
CC 3)[GlcNAc(beta1-4)][Man(alpha1-?)Man(alpha1-6)] Man(beta1-
CC 4)GlcNAc(beta1-4)GlcNAc. {ECO:0000269|PubMed:5100763}.
CC -!- SIMILARITY: Belongs to the avidin/streptavidin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/AV/";
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DR EMBL; X05343; CAA28954.1; -; mRNA.
DR EMBL; L27818; AAB59733.1; -; Genomic_DNA.
DR EMBL; AJ311647; CAC34569.1; -; Genomic_DNA.
DR PIR; A54975; VICH.
DR RefSeq; NP_990651.1; NM_205320.1.
DR PDB; 1AVD; X-ray; 2.70 A; A/B=25-152.
DR PDB; 1AVE; X-ray; 2.80 A; A/B=25-152.
DR PDB; 1IJ8; X-ray; 2.00 A; A/B=25-152.
DR PDB; 1LDO; X-ray; 2.20 A; A/B=25-152.
DR PDB; 1LDQ; X-ray; 2.70 A; A/B=25-152.
DR PDB; 1LEL; X-ray; 2.90 A; A/B=25-152.
DR PDB; 1NQN; X-ray; 1.80 A; A/B=26-147.
DR PDB; 1RAV; X-ray; 2.20 A; A/B=26-152.
DR PDB; 1VYO; X-ray; 1.48 A; A/B=25-152.
DR PDB; 2A5B; X-ray; 2.49 A; A/B=25-148.
DR PDB; 2A5C; X-ray; 2.50 A; A/B=25-147.
DR PDB; 2A8G; X-ray; 1.99 A; A/B=27-152.
DR PDB; 2AVI; X-ray; 3.00 A; A/B=25-152.
DR PDB; 2C4I; X-ray; 1.95 A; A=22-80.
DR PDB; 2CAM; X-ray; 2.20 A; A/B=26-152.
DR PDB; 2JGS; X-ray; 1.90 A; A/B/C/D=69-152.
DR PDB; 2MF6; NMR; -; A/B/C/D=25-61, A/B/C/D=85-152.
DR PDB; 3FDC; X-ray; 3.10 A; A/B=25-152.
DR PDB; 3MM0; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/K/M/N=25-61, A/B/C/D/E/F/G/H/I/K/M/N=85-152.
DR PDB; 3VGW; X-ray; 1.60 A; A/B/C/D/E/F/G/H=25-147.
DR PDB; 3VHH; X-ray; 2.26 A; A/B/C/D=25-147.
DR PDB; 3VHI; X-ray; 1.76 A; A/B/C/D=26-147.
DR PDB; 3VHM; X-ray; 2.00 A; A/B/C/D=25-147.
DR PDB; 4I60; X-ray; 2.50 A; A=25-152.
DR PDB; 4JHQ; X-ray; 1.99 A; A/B=25-152.
DR PDB; 4U46; X-ray; 1.95 A; A/B=25-152.
DR PDB; 5CHK; X-ray; 2.20 A; A=25-152.
DR PDB; 5HLM; X-ray; 2.50 A; A/B/C/D=25-152.
DR PDB; 5IRU; X-ray; 2.00 A; A/B/C/D=25-152.
DR PDB; 5IRW; X-ray; 2.10 A; A/B/C/D=25-152.
DR PDB; 5LUR; X-ray; 2.70 A; A/B=21-152.
DR PDB; 5MYQ; X-ray; 1.89 A; A/B/C/D=25-152.
DR PDB; 6XND; X-ray; 1.58 A; A/B/C/D=25-152.
DR PDB; 7P4Z; X-ray; 2.20 A; A/B=27-147.
DR PDBsum; 1AVD; -.
DR PDBsum; 1AVE; -.
DR PDBsum; 1IJ8; -.
DR PDBsum; 1LDO; -.
DR PDBsum; 1LDQ; -.
DR PDBsum; 1LEL; -.
DR PDBsum; 1NQN; -.
DR PDBsum; 1RAV; -.
DR PDBsum; 1VYO; -.
DR PDBsum; 2A5B; -.
DR PDBsum; 2A5C; -.
DR PDBsum; 2A8G; -.
DR PDBsum; 2AVI; -.
DR PDBsum; 2C4I; -.
DR PDBsum; 2CAM; -.
DR PDBsum; 2JGS; -.
DR PDBsum; 2MF6; -.
DR PDBsum; 3FDC; -.
DR PDBsum; 3MM0; -.
DR PDBsum; 3VGW; -.
DR PDBsum; 3VHH; -.
DR PDBsum; 3VHI; -.
DR PDBsum; 3VHM; -.
DR PDBsum; 4I60; -.
DR PDBsum; 4JHQ; -.
DR PDBsum; 4U46; -.
DR PDBsum; 5CHK; -.
DR PDBsum; 5HLM; -.
DR PDBsum; 5IRU; -.
DR PDBsum; 5IRW; -.
DR PDBsum; 5LUR; -.
DR PDBsum; 5MYQ; -.
DR PDBsum; 6XND; -.
DR PDBsum; 7P4Z; -.
DR AlphaFoldDB; P02701; -.
DR PCDDB; P02701; -.
DR SMR; P02701; -.
DR DIP; DIP-60471N; -.
DR STRING; 9031.ENSGALP00000003846; -.
DR BindingDB; P02701; -.
DR ChEMBL; CHEMBL2189156; -.
DR GlyConnect; 65; 1 N-Linked glycan.
DR PaxDb; P02701; -.
DR PRIDE; P02701; -.
DR Ensembl; ENSGALT00000003855; ENSGALP00000003846; ENSGALG00000025945.
DR GeneID; 396260; -.
DR KEGG; gga:396260; -.
DR CTD; 567678; -.
DR VEuPathDB; HostDB:geneid_396260; -.
DR eggNOG; ENOG502S55G; Eukaryota.
DR GeneTree; ENSGT00390000001847; -.
DR HOGENOM; CLU_122441_0_0_1; -.
DR InParanoid; P02701; -.
DR OMA; WKFSEST; -.
DR OrthoDB; 1512982at2759; -.
DR PhylomeDB; P02701; -.
DR TreeFam; TF336756; -.
DR BioCyc; MetaCyc:MON-5341; -.
DR EvolutionaryTrace; P02701; -.
DR PRO; PR:P02701; -.
DR Proteomes; UP000000539; Chromosome Z.
DR Bgee; ENSGALG00000025945; Expressed in granulocyte and 11 other tissues.
DR ExpressionAtlas; P02701; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009374; F:biotin binding; IBA:GO_Central.
DR GO; GO:0019731; P:antibacterial humoral response; NAS:AgBase.
DR Gene3D; 2.40.128.30; -; 1.
DR InterPro; IPR005469; Avidin.
DR InterPro; IPR017889; Avidin-like_CS.
DR InterPro; IPR036896; Avidin-like_sf.
DR InterPro; IPR005468; Avidin/str.
DR Pfam; PF01382; Avidin; 1.
DR PRINTS; PR00709; AVIDIN.
DR SUPFAM; SSF50876; SSF50876; 1.
DR PROSITE; PS00577; AVIDIN_1; 1.
DR PROSITE; PS51326; AVIDIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biotin; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:5100762,
FT ECO:0000269|PubMed:5100763"
FT CHAIN 25..152
FT /note="Avidin"
FT /id="PRO_0000002722"
FT DOMAIN 26..149
FT /note="Avidin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00656"
FT BINDING 57
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:5100763"
FT /id="CAR_000230"
FT DISULFID 28..107
FT VARIANT 58
FT /note="I -> T (in about 50% of the molecules)"
FT /evidence="ECO:0000269|PubMed:11167523,
FT ECO:0000269|PubMed:5100762"
FT CONFLICT 22
FT /note="G -> S (in Ref. 3; AAB59733)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="T -> D (in Ref. 4; CAC34569)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="R -> K (in Ref. 4; CAC34569)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="Q -> E (in Ref. 5; AA sequence and 6; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1VYO"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1VYO"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:1VYO"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1VYO"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1VYO"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1VYO"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:1VYO"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1VYO"
FT STRAND 100..109
FT /evidence="ECO:0007829|PDB:1VYO"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2A8G"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:1VYO"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:1VYO"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:1VYO"
SQ SEQUENCE 152 AA; 16768 MW; 7795A458481AEC09 CRC64;
MVHATSPLLL LLLLSLALVA PGLSARKCSL TGKWTNDLGS NMTIGAVNSR GEFTGTYITA
VTATSNEIKE SPLHGTQNTI NKRTQPTFGF TVNWKFSEST TVFTGQCFID RNGKEVLKTM
WLLRSSVNDI GDDWKATRVG INIFTRLRTQ KE
