ID   ASOL_TOBAC              Reviewed;         554 AA.
AC   P29162;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=L-ascorbate oxidase homolog;
DE            EC=1.10.3.-;
DE   AltName: Full=Pollen-specific protein NTP303;
DE   Flags: Precursor;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND INDUCTION.
RC   STRAIN=cv. Petit Havana SR1; TISSUE=Pollen;
RX   PubMed=1600146; DOI=10.1007/bf00047713;
RA   Weterings K., Reijnen W., van Aarssen R., Kortstee A., Spijkers J.,
RA   van Herpen M., Schrauwen J., Wullems G.;
RT   "Characterization of a pollen-specific cDNA clone from Nicotiana tabacum
RT   expressed during microgametogenesis and germination.";
RL   Plant Mol. Biol. 18:1101-1111(1992).
CC   -!- FUNCTION: Probable oxidoreductase that may be involved in pollen tube
CC       growth. {ECO:0000269|PubMed:1600146}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Pollen. {ECO:0000269|PubMed:1600146}.
CC   -!- DEVELOPMENTAL STAGE: Appears after the first haploid mitosis and are
CC       expressed during microgametogenesis, germination and tube growth.
CC       {ECO:0000269|PubMed:1600146}.
CC   -!- INDUCTION: Expression regulated by the haploid gametophyte itself.
CC       {ECO:0000269|PubMed:1600146}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR   EMBL; X61146; CAA43454.1; -; mRNA.
DR   PIR; S22495; S22495.
DR   RefSeq; NP_001311861.1; NM_001324932.1.
DR   AlphaFoldDB; P29162; -.
DR   SMR; P29162; -.
DR   STRING; 4097.P29162; -.
DR   ProMEX; P29162; -.
DR   GeneID; 107766889; -.
DR   KEGG; nta:107766889; -.
DR   OMA; ENHENTM; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   CDD; cd13846; CuRO_1_AAO_like_1; 1.
DR   CDD; cd13872; CuRO_2_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; IPR034273; CuRO_1_AAO-like.
DR   InterPro; IPR034271; CuRO_2_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   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..554
FT                   /note="L-ascorbate oxidase homolog"
FT                   /id="PRO_0000002909"
FT   DOMAIN          22..143
FT                   /note="Plastocyanin-like 1"
FT   DOMAIN          196..296
FT                   /note="Plastocyanin-like 2"
FT   DOMAIN          411..521
FT                   /note="Plastocyanin-like 3"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        101..540
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   554 AA;  62034 MW;  9D38DAB1F52E2F85 CRC64;
     MGSGKVTFVA LLLCLSVGVI AEDPYLYFNW NVTYGTIAPL GVPQQGILIN GQFPGPRINC
     TSNNNIVVNV FNNLDEPFLF TWNGVQHRKN SWQDGTPGTM CPIMPGQNFT YRFQVKDQIG
     SYSYFPTTAL HRAAGGYGAL NVHSRALIPV PFDNPADEYN VFVGDWYNKG HKTLKKILDG
     GRTIGRPDGI IINGKSAKVG EAKEPLFTME AGKTYRYRFC NLGMRSSVNI RFQGHPMKLV
     ELEGSHTVQN IYDSLDLHVG QCLSVLVTAD QEPKDYYLVV SSRFLKQALS SVAIIRYANG
     KGPASPELPT PPPENTEGIA WSMNQFRSFR WNLTASAARP NPQGSYHYGQ INITRTIKIF
     NSMSQVGGKL RYGLNGISHT NGETPLKLVE YFGATNKAFK YDLMADEAPA DPSKLTIATN
     VKNATYRNFV EIIFENHEKT IRTYHLDGYS FFAVAVEPGR WSPEKRKNYN LVDGLSRNNI
     QVYPNSWAAI MLTFDNAGMW NLRSEMWEKT YLGEQLYFSV LSPSRSLRDE YNIPDNHPLC
     GIVKGLSMPA PYKA