ASPR1_ARATH
ID ASPR1_ARATH Reviewed; 447 AA.
AC Q3EBM5;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Probable aspartic protease At2g35615;
DE EC=3.4.-.-;
DE Flags: Precursor;
GN OrderedLocusNames=At2g35615; ORFNames=T20F21;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 PREDICTION.
RX PubMed=15333753; DOI=10.1104/pp.104.043695;
RA Reumann S., Ma C., Lemke S., Babujee L.;
RT "AraPerox. A database of putative Arabidopsis proteins from plant
RT peroxisomes.";
RL Plant Physiol. 136:2587-2608(2004).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=19748917; DOI=10.1104/pp.109.142505;
RA Lingard M.J., Bartel B.;
RT "Arabidopsis LON2 is necessary for peroxisomal function and sustained
RT matrix protein import.";
RL Plant Physiol. 151:1354-1365(2009).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Note=Prediction of a
CC peroxisomal location. {ECO:0000269|PubMed:15333753}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:19748917}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AC006068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC09130.1; -; Genomic_DNA.
DR RefSeq; NP_850251.1; NM_179920.2.
DR AlphaFoldDB; Q3EBM5; -.
DR SMR; Q3EBM5; -.
DR STRING; 3702.AT2G35615.1; -.
DR MEROPS; A01.A22; -.
DR PaxDb; Q3EBM5; -.
DR PRIDE; Q3EBM5; -.
DR ProteomicsDB; 246805; -.
DR EnsemblPlants; AT2G35615.1; AT2G35615.1; AT2G35615.
DR GeneID; 818129; -.
DR Gramene; AT2G35615.1; AT2G35615.1; AT2G35615.
DR KEGG; ath:AT2G35615; -.
DR Araport; AT2G35615; -.
DR TAIR; locus:504955954; AT2G35615.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_1_3_1; -.
DR InParanoid; Q3EBM5; -.
DR OMA; GCDEAKN; -.
DR OrthoDB; 753343at2759; -.
DR PhylomeDB; Q3EBM5; -.
DR PRO; PR:Q3EBM5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q3EBM5; baseline.
DR GO; GO:0005576; C:extracellular region; IDA:TAIR.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004175; F:endopeptidase activity; IDA:TAIR.
DR GO; GO:0010183; P:pollen tube guidance; IGI:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05476; pepsin_A_like_plant; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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 Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..447
FT /note="Probable aspartic protease At2g35615"
FT /id="PRO_0000405232"
FT DOMAIN 85..439
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 447 AA; 48089 MW; 1D3D5C921B5D6432 CRC64;
MATQILLCFF LFFSVTLSSS GHPKNFSVEL IHRDSPLSPI YNPQITVTDR LNAAFLRSVS
RSRRFNHQLS QTDLQSGLIG ADGEFFMSIT IGTPPIKVFA IADTGSDLTW VQCKPCQQCY
KENGPIFDKK KSSTYKSEPC DSRNCQALSS TERGCDESNN ICKYRYSYGD QSFSKGDVAT
ETVSIDSASG SPVSFPGTVF GCGYNNGGTF DETGSGIIGL GGGHLSLISQ LGSSISKKFS
YCLSHKSATT NGTSVINLGT NSIPSSLSKD SGVVSTPLVD KEPLTYYYLT LEAISVGKKK
IPYTGSSYNP NDDGILSETS GNIIIDSGTT LTLLEAGFFD KFSSAVEESV TGAKRVSDPQ
GLLSHCFKSG SAEIGLPEIT VHFTGADVRL SPINAFVKLS EDMVCLSMVP TTEVAIYGNF
AQMDFLVGYD LETRTVSFQH MDCSANL
