ASP39_ARATH
ID ASP39_ARATH Reviewed; 475 AA.
AC Q9S9K4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Aspartic proteinase 39 {ECO:0000303|PubMed:27872247};
DE EC=3.4.23.- {ECO:0000269|PubMed:27872247};
DE Flags: Precursor;
GN Name=A39 {ECO:0000303|PubMed:27872247};
GN OrderedLocusNames=At1g65240 {ECO:0000312|Araport:AT1G65240};
GN ORFNames=T23K8.15 {ECO:0000312|EMBL:AAD26876.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION, MUTAGENESIS OF ASP-92, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=27872247; DOI=10.1104/pp.16.01719;
RA Gao H., Zhang Y., Wang W., Zhao K., Liu C., Bai L., Li R., Guo Y.;
RT "Two membrane-anchored aspartic proteases contribute to pollen and ovule
RT development.";
RL Plant Physiol. 173:219-239(2017).
RN [4]
RP REVIEW.
RX PubMed=28402691; DOI=10.1080/15592324.2017.1304343;
RA Gao H., Li R., Guo Y.;
RT "Arabidopsis aspartic proteases A36 and A39 play roles in plant
RT reproduction.";
RL Plant Signal. Behav. 12:e1304343-e1304343(2017).
CC -!- FUNCTION: Displays aspartic proteolytic activity (PubMed:27872247).
CC Together with A36, contributes to pollen and ovule development,
CC including the apical cell wall constitution of the growing pollen tubes
CC (PubMed:27872247). {ECO:0000269|PubMed:27872247}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27872247};
CC Lipid-anchor, GPI-anchor {ECO:0000255}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:27872247}. Note=Displays punctate cytosolic
CC localization and colocalizes with the GPI-anchored protein COBL10 at
CC the plasma membrane and in the cytosol (PubMed:27872247). In pollen
CC grains, mainly present at the plasma membrane and in reticular
CC structures in the cytosol (PubMed:27872247). In pollen tubes, exhibits
CC a punctate localization in the cytosol and occurs weakly at the plasma
CC membrane (PubMed:27872247). {ECO:0000269|PubMed:27872247}.
CC -!- TISSUE SPECIFICITY: Highly expressed in pollen and pollen tubes
CC (PubMed:27872247). Mostly expressed in inflorescence, flowers and
CC siliques, and barely in leaves and seedlings (PubMed:27872247).
CC {ECO:0000269|PubMed:27872247}.
CC -!- DEVELOPMENTAL STAGE: In flowers, expressed in the pollen and growing
CC pollen tubes (PubMed:27872247). During microspore development, observed
CC expressed from tetrad to tricellular pollen (PubMed:27872247). Also
CC present in young siliques and developing ovules (PubMed:27872247).
CC {ECO:0000269|PubMed:27872247}.
CC -!- DISRUPTION PHENOTYPE: The double mutant a36 a39 produces inviable
CC pollen which undergoes apoptosis-like programmed cell death, exhibits a
CC compromised pollen tubes micropylar guidance and has degenerated female
CC gametes (PubMed:27872247). The double mutant a36 a39 accumulates
CC abnormally highly methylesterified homogalacturonans and xyloglucans in
CC the apical pollen tube wall (PubMed:27872247).
CC {ECO:0000269|PubMed:27872247}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01103, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD26876.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007230; AAD26876.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34347.1; -; Genomic_DNA.
DR PIR; E96676; E96676.
DR RefSeq; NP_176703.1; NM_105197.3.
DR AlphaFoldDB; Q9S9K4; -.
DR SMR; Q9S9K4; -.
DR STRING; 3702.AT1G65240.1; -.
DR MEROPS; A01.A37; -.
DR PaxDb; Q9S9K4; -.
DR PRIDE; Q9S9K4; -.
DR ProteomicsDB; 246699; -.
DR EnsemblPlants; AT1G65240.1; AT1G65240.1; AT1G65240.
DR GeneID; 842831; -.
DR Gramene; AT1G65240.1; AT1G65240.1; AT1G65240.
DR KEGG; ath:AT1G65240; -.
DR Araport; AT1G65240; -.
DR TAIR; locus:2200365; AT1G65240.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_7_0_1; -.
DR InParanoid; Q9S9K4; -.
DR OMA; MVPNQMH; -.
DR OrthoDB; 753343at2759; -.
DR PhylomeDB; Q9S9K4; -.
DR PRO; PR:Q9S9K4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S9K4; baseline and differential.
DR Genevisible; Q9S9K4; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0090406; C:pollen tube; IDA:UniProtKB.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0009860; P:pollen tube growth; IMP:UniProtKB.
DR GO; GO:0010183; P:pollen tube guidance; IMP:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd05476; pepsin_A_like_plant; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034161; Pepsin-like_plant.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR PANTHER; PTHR13683; PTHR13683; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Cell membrane; Cytoplasm; Glycoprotein; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Protease; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..449
FT /note="Aspartic proteinase 39"
FT /id="PRO_0000259444"
FT PROPEP 450..475
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000259445"
FT DOMAIN 74..422
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT LIPID 449
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 92
FT /note="D->N: Impaired proteolytic activity."
FT /evidence="ECO:0000269|PubMed:27872247"
SQ SEQUENCE 475 AA; 51828 MW; 1DD9C1A5EF147BA0 CRC64;
MELRRKLCIV VAVFVIVIEF ASANFVFKAQ HKFAGKKKNL EHFKSHDTRR HSRMLASIDL
PLGGDSRVDS VGLYFTKIKL GSPPKEYHVQ VDTGSDILWI NCKPCPKCPT KTNLNFRLSL
FDMNASSTSK KVGCDDDFCS FISQSDSCQP ALGCSYHIVY ADESTSDGKF IRDMLTLEQV
TGDLKTGPLG QEVVFGCGSD QSGQLGNGDS AVDGVMGFGQ SNTSVLSQLA ATGDAKRVFS
HCLDNVKGGG IFAVGVVDSP KVKTTPMVPN QMHYNVMLMG MDVDGTSLDL PRSIVRNGGT
IVDSGTTLAY FPKVLYDSLI ETILARQPVK LHIVEETFQC FSFSTNVDEA FPPVSFEFED
SVKLTVYPHD YLFTLEEELY CFGWQAGGLT TDERSEVILL GDLVLSNKLV VYDLDNEVIG
WADHNCSSSI KIKDGSGGVY SVGADNLSSA PRLLMITKLL TILSPLIVMA FTSLA
