ASOL_BRANA
ID ASOL_BRANA Reviewed; 555 AA.
AC Q00624;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=L-ascorbate oxidase homolog;
DE EC=1.10.3.-;
DE Flags: Precursor;
GN Name=Bp10;
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Westar;
RX PubMed=1303799; DOI=10.1111/j.1365-313x.1992.00331.x;
RA Albani D., Sardana R., Robert L.S., Altosaar I., Arnison P.G.,
RA Fabijanski S.F.;
RT "A Brassica napus gene family which shows sequence similarity to ascorbate
RT oxidase is expressed in developing pollen. Molecular characterization and
RT analysis of promoter activity in transgenic tobacco plants.";
RL Plant J. 2:331-342(1992).
CC -!- FUNCTION: Probable oxidase that may be involved in pollen tube growth.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Maximal expression in early binucleate microspores;
CC declines considerably in mature trinucleate pollen.
CC {ECO:0000269|PubMed:1303799}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X64257; CAA45554.1; -; Genomic_DNA.
DR PIR; S23763; S23763.
DR RefSeq; XP_013749860.1; XM_013894406.1.
DR AlphaFoldDB; Q00624; -.
DR SMR; Q00624; -.
DR EnsemblPlants; CDY43995; CDY43995; GSBRNA2T00079392001.
DR GeneID; 106452325; -.
DR Gramene; CDY43995; CDY43995; GSBRNA2T00079392001.
DR KEGG; bna:106452325; -.
DR OMA; MTHRNFI; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd13872; CuRO_2_AAO_like_1; 1.
DR CDD; cd13894; CuRO_3_AAO_like_1; 1.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034271; CuRO_2_AO-like.
DR InterPro; IPR034275; CuRO_3_AO-like.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
PE 2: Evidence at transcript level;
KW Disulfide bond; Germination; Glycoprotein; Metal-binding; Oxidoreductase;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..555
FT /note="L-ascorbate oxidase homolog"
FT /id="PRO_0000002905"
FT DOMAIN 25..145
FT /note="Plastocyanin-like 1"
FT DOMAIN 158..301
FT /note="Plastocyanin-like 2"
FT DOMAIN 345..524
FT /note="Plastocyanin-like 3"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..539
FT /evidence="ECO:0000255"
SQ SEQUENCE 555 AA; 62131 MW; 5BF23C9D73EA6C6A CRC64;
MRGVKLLAAC LYLAAAATVV VHAEDPYFHH VWNVTYGTAS PLGVPQQVIL INGQFPGPNI
NSTSNNNVII NVFNNLDEPF LLTWNGIQHR KNCWQDGTPG TMCPIMPGTN YTYHFQPKDQ
IGSYFYYPTT GMHRAAGGYG GLRVNSRLLI PVPYADPEDD YTVLIGDWYT KSHTQLKKFL
DGGRTIGRPD GIVINGKSGK GDGSDAPLFT LKPGKTYRVR ICNVGVKTSI NFRIQNHKMK
LVEMEGSHVL QNDYDSLDVH VGQCFGTIVT ANQEPKDYYM VASSRFLKTV ITTTGLLRYE
GGKGPASSQL PAGPVGWAWS LNQFRSFRWN LTASAARPNP QGSYHYGKIN ITRTIKLVNT
QGKVDGKLRF ALNGVSHTEP ETPLKLAEYF GISDKVFKYD TITDDPTPEQ IKNIKIEPNV
LNITHRTFVE VVFENHEKSV QSWHLDGYSF FSVAVEPGTW TPEKRKNYNL LDAVSRHTVQ
VYPKCWAAIL LTFDNCGMWN VRSENTERRY LGQQLYASVL SPEKSLRDEY NMPETSLQCG
LVKNTPKPVN PYAGA