AVR2_CHICK
ID AVR2_CHICK Reviewed; 150 AA.
AC P56732; Q546L5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Avidin-related protein 2;
DE Flags: Precursor;
GN Name=AVR2;
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 [GENOMIC DNA].
RC STRAIN=White leghorn; TISSUE=Oviduct;
RX PubMed=8125122; DOI=10.1111/j.1432-1033.1994.tb18663.x;
RA Keinaenen R.A., Wallen M.J., Kristo P.A., Laukkanen M.O., Toimela T.A.,
RA Helenius M.A., Kulomaa M.S.;
RT "Molecular cloning and nucleotide sequence of chicken avidin-related genes
RT 1-5.";
RL Eur. J. Biochem. 220:615-621(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [3]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 25-150 IN COMPLEX WITH BIOTIN,
RP DISULFIDE BOND, SUBUNIT, AND MASS SPECTROMETRY.
RX PubMed=16212654; DOI=10.1186/1472-6750-5-28;
RA Hytoenen V.P., Maeaettae J.A., Kidron H., Halling K.K., Hoerhae J.,
RA Kulomaa T., Nyholm T.K., Johnson M.S., Salminen T.A., Kulomaa M.S.,
RA Airenne T.T.;
RT "Avidin related protein 2 shows unique structural and functional features
RT among the avidin protein family.";
RL BMC Biotechnol. 5:28-28(2005).
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|PROSITE-ProRule:PRU00656,
CC ECO:0000269|PubMed:16212654}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00656}.
CC -!- MASS SPECTROMETRY: Mass=14310; Mass_error=0.3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16212654};
CC -!- SIMILARITY: Belongs to the avidin/streptavidin family. {ECO:0000305}.
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DR EMBL; Z21554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z21535; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AJ311648; CAC34570.1; -; Genomic_DNA.
DR PIR; S42202; S42202.
DR RefSeq; NP_001025519.1; NM_001030348.1.
DR PDB; 1WBI; X-ray; 1.40 A; A/B/C/D/E/F/G/H=25-150.
DR PDBsum; 1WBI; -.
DR AlphaFoldDB; P56732; -.
DR SMR; P56732; -.
DR STRING; 9031.ENSGALP00000038525; -.
DR PaxDb; P56732; -.
DR Ensembl; ENSGALT00000039315; ENSGALP00000038525; ENSGALG00000028039.
DR GeneID; 395367; -.
DR KEGG; gga:395367; -.
DR CTD; 395367; -.
DR VEuPathDB; HostDB:geneid_395367; -.
DR eggNOG; ENOG502S55G; Eukaryota.
DR GeneTree; ENSGT00950000184837; -.
DR HOGENOM; CLU_122441_0_0_1; -.
DR InParanoid; P56732; -.
DR OrthoDB; 1512982at2759; -.
DR EvolutionaryTrace; P56732; -.
DR PRO; PR:P56732; -.
DR Proteomes; UP000000539; Chromosome Z.
DR ExpressionAtlas; P56732; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009374; F:biotin binding; IDA:UniProtKB.
DR GO; GO:0015878; P:biotin transport; TAS:UniProtKB.
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; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..150
FT /note="Avidin-related protein 2"
FT /id="PRO_0000002724"
FT DOMAIN 26..147
FT /note="Avidin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00656"
FT BINDING 57
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000250"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..105
FT /evidence="ECO:0000269|PubMed:16212654"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1WBI"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1WBI"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:1WBI"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1WBI"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1WBI"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1WBI"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:1WBI"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:1WBI"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:1WBI"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:1WBI"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:1WBI"
SQ SEQUENCE 150 AA; 16435 MW; 763D1E2B1A93A66D CRC64;
MVHATSPLLL LLLLSLALVA PSLSARKCSL TGEWDNDLGS IMTIGAVNDN GEFDGTYITA
VADNPGNITL SPLLGIQHKR ASQPTFGFTV HWNFSESTSV FVGQCFVDRS GKEVLKTKWL
QRLAVDDISD DWIATRVGNN DFTRQHTVEE
