ID   AVR4_CHICK              Reviewed;         150 AA.
AC   P56734;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Avidin-related protein 4/5;
DE   Flags: Precursor;
GN   Name=AVR4;
GN   and
GN   Name=AVR5;
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   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 25-150, DISULFIDE BOND, AND
RP   GLYCOSYLATION AT ASN-67 AND ASN-141.
RX   PubMed=15858262; DOI=10.1107/s0907444905003914;
RA   Eisenberg-Domovich Y., Hytoenen V.P., Wilchek M., Bayer E.A., Kulomaa M.S.,
RA   Livnah O.;
RT   "High-resolution crystal structure of an avidin-related protein: insight
RT   into high-affinity biotin binding and protein stability.";
RL   Acta Crystallogr. D 61:528-538(2005).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00656}.
CC   -!- MISCELLANEOUS: The sequences of the coding regions of genes AVR4 and
CC       AVR5 are identical.
CC   -!- SIMILARITY: Belongs to the avidin/streptavidin family. {ECO:0000305}.
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DR   EMBL; Z22883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S42204; S42204.
DR   PDB; 1Y52; X-ray; 1.70 A; X/Y=25-150.
DR   PDB; 1Y53; X-ray; 1.20 A; X/Y=25-150.
DR   PDB; 1Y55; X-ray; 1.00 A; X/Y=25-150.
DR   PDB; 2FHL; X-ray; 1.05 A; A/B=25-145.
DR   PDB; 2FHN; X-ray; 1.30 A; X/Y=25-145.
DR   PDB; 2MF6; NMR; -; A/B/C/D=62-82.
DR   PDB; 2OF8; X-ray; 1.05 A; A/B=25-150.
DR   PDB; 2OF9; X-ray; 1.35 A; A/B=25-150.
DR   PDB; 2OFA; X-ray; 1.50 A; A/B=25-150.
DR   PDB; 2OFB; X-ray; 1.16 A; A/B=25-150.
DR   PDB; 3MM0; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/K/M/N=62-82.
DR   PDB; 4BCS; X-ray; 1.80 A; A/B=25-147.
DR   PDBsum; 1Y52; -.
DR   PDBsum; 1Y53; -.
DR   PDBsum; 1Y55; -.
DR   PDBsum; 2FHL; -.
DR   PDBsum; 2FHN; -.
DR   PDBsum; 2MF6; -.
DR   PDBsum; 2OF8; -.
DR   PDBsum; 2OF9; -.
DR   PDBsum; 2OFA; -.
DR   PDBsum; 2OFB; -.
DR   PDBsum; 3MM0; -.
DR   PDBsum; 4BCS; -.
DR   AlphaFoldDB; P56734; -.
DR   SMR; P56734; -.
DR   STRING; 9031.ENSGALP00000033787; -.
DR   iPTMnet; P56734; -.
DR   VEuPathDB; HostDB:LOC121108603; -.
DR   eggNOG; ENOG502S55G; Eukaryota.
DR   InParanoid; P56734; -.
DR   PhylomeDB; P56734; -.
DR   EvolutionaryTrace; P56734; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009374; F:biotin binding; IBA:GO_Central.
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 4/5"
FT                   /id="PRO_0000002726"
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:0000269|PubMed:15858262"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15858262"
FT   DISULFID        28..105
FT                   /evidence="ECO:0000269|PubMed:15858262"
FT   STRAND          32..36
FT                   /evidence="ECO:0007829|PDB:1Y55"
FT   STRAND          41..44
FT                   /evidence="ECO:0007829|PDB:1Y55"
FT   STRAND          51..58
FT                   /evidence="ECO:0007829|PDB:1Y55"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:1Y55"
FT   STRAND          71..77
FT                   /evidence="ECO:0007829|PDB:1Y55"
FT   STRAND          80..83
FT                   /evidence="ECO:0007829|PDB:2MF6"
FT   STRAND          85..91
FT                   /evidence="ECO:0007829|PDB:1Y55"
FT   STRAND          93..96
FT                   /evidence="ECO:0007829|PDB:4BCS"
FT   STRAND          98..107
FT                   /evidence="ECO:0007829|PDB:1Y55"
FT   STRAND          113..122
FT                   /evidence="ECO:0007829|PDB:1Y55"
FT   HELIX           128..133
FT                   /evidence="ECO:0007829|PDB:1Y55"
FT   STRAND          135..144
FT                   /evidence="ECO:0007829|PDB:1Y55"
SQ   SEQUENCE   150 AA;  16644 MW;  9A6C6C6310EFE13A CRC64;
     MVHTTSPLLL LLLLSLALVA PSLSARKCSL TGKWTNNLGS IMTIRAVNSR GEFTGTYLTA
     VADNPGNITL SPLLGIQHKR ASQPTFGFTV HWNFSESTTV FTGQCFIDRN GKEVLKTMWL
     LRSSVNDISY DWKATRVGYN NFTRLCTVEE