ASP36_ARATH
ID ASP36_ARATH Reviewed; 482 AA.
AC Q4V3D2; Q9FG60;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Aspartic proteinase 36 {ECO:0000303|PubMed:27872247};
DE EC=3.4.23.- {ECO:0000269|PubMed:27872247};
DE Flags: Precursor;
GN Name=A36 {ECO:0000303|PubMed:27872247};
GN OrderedLocusNames=At5g36260 {ECO:0000312|Araport:AT5G36260};
GN ORFNames=T30G6.12 {ECO:0000312|EMBL:AED94063.1};
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, MUTAGENESIS OF ASP-96 AND ASP-310, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, 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 [5]
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 A39, 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 roots, flowers and
CC inflorescence, and at lower levels in stems, seedlings and siliques
CC (PubMed:27872247). {ECO:0000269|PubMed:27872247}.
CC -!- DEVELOPMENTAL STAGE: In flowers, expressed exclusively in the pollen
CC and growing pollen tubes (PubMed:27872247). During microspore
CC development, confined to tricellular pollen (PubMed:27872247).
CC {ECO:0000269|PubMed:27872247}.
CC -!- DISRUPTION PHENOTYPE: Reduced pollen activity and germination rate
CC leading to a decreased male transmission efficiency (PubMed:27872247).
CC The double mutant a36 a39 produces inviable pollen which undergoes
CC apoptosis-like programmed cell death, exhibits a compromised pollen
CC tubes micropylar guidance and has degenerated female gametes
CC (PubMed:27872247). The double mutant a36 a39 accumulates abnormally
CC highly methylesterified homogalacturonans and xyloglucans in the apical
CC pollen tube wall (PubMed:27872247). {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=BAB09366.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB026661; BAB09366.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED94063.1; -; Genomic_DNA.
DR EMBL; BT023424; AAY56415.1; -; mRNA.
DR RefSeq; NP_198475.2; NM_123017.4.
DR AlphaFoldDB; Q4V3D2; -.
DR SMR; Q4V3D2; -.
DR STRING; 3702.AT5G36260.1; -.
DR MEROPS; A01.A58; -.
DR PaxDb; Q4V3D2; -.
DR PRIDE; Q4V3D2; -.
DR ProteomicsDB; 185300; -.
DR EnsemblPlants; AT5G36260.1; AT5G36260.1; AT5G36260.
DR GeneID; 833623; -.
DR Gramene; AT5G36260.1; AT5G36260.1; AT5G36260.
DR KEGG; ath:AT5G36260; -.
DR Araport; AT5G36260; -.
DR TAIR; locus:2183617; AT5G36260.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_7_0_1; -.
DR InParanoid; Q4V3D2; -.
DR OMA; IGWTEYD; -.
DR OrthoDB; 753343at2759; -.
DR PhylomeDB; Q4V3D2; -.
DR PRO; PR:Q4V3D2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q4V3D2; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; TAS: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:0009555; P:pollen development; IMP:UniProtKB.
DR GO; GO:0009846; P:pollen germination; IMP: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; Disulfide bond; Glycoprotein;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Protease; Reference proteome;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..456
FT /note="Aspartic proteinase 36"
FT /id="PRO_0000450671"
FT PROPEP 457..482
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000450672"
FT DOMAIN 78..429
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT LIPID 456
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 347..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT MUTAGEN 96
FT /note="D->N: Impaired proteolytic activity; when associated
FT with N-310."
FT /evidence="ECO:0000269|PubMed:27872247"
FT MUTAGEN 310
FT /note="D->N: Impaired proteolytic activity; when associated
FT with N-96."
FT /evidence="ECO:0000269|PubMed:27872247"
SQ SEQUENCE 482 AA; 51981 MW; 8EDF5AE1E3663203 CRC64;
MVTTMDPSRI SRIVAVVFVL VIQVVSGNFV FNVTHKFAGK EKQLSELKSH DSFRHARMLA
NIDLPLGGDS RADSIGLYFT KIKLGSPPKE YYVQVDTGSD ILWVNCAPCP KCPVKTDLGI
PLSLYDSKTS STSKNVGCED DFCSFIMQSE TCGAKKPCSY HVVYGDGSTS DGDFIKDNIT
LEQVTGNLRT APLAQEVVFG CGKNQSGQLG QTDSAVDGIM GFGQSNTSII SQLAAGGSTK
RIFSHCLDNM NGGGIFAVGE VESPVVKTTP IVPNQVHYNV ILKGMDVDGD PIDLPPSLAS
TNGDGGTIID SGTTLAYLPQ NLYNSLIEKI TAKQQVKLHM VQETFACFSF TSNTDKAFPV
VNLHFEDSLK LSVYPHDYLF SLREDMYCFG WQSGGMTTQD GADVILLGDL VLSNKLVVYD
LENEVIGWAD HNCSSSIKVK DGSGAAYQLG AENLISAASS VMNGTLVTLL SILIWVFHSF
TS
