APA1_ARATH
ID APA1_ARATH Reviewed; 506 AA.
AC O65390; Q38934;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Aspartic proteinase A1;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=APA1; Synonyms=PRA1; OrderedLocusNames=At1g11910; ORFNames=F12F1.24;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-506.
RC STRAIN=cv. Columbia;
RX PubMed=9037171; DOI=10.1023/a:1005794917200;
RA D'Hondt K., Stack S., Gutteridge S., Vandekerckhove J., Krebbers E.,
RA Gal S.;
RT "Aspartic proteinase genes in the Brassicaceae Arabidopsis thaliana and
RT Brassica napus.";
RL Plant Mol. Biol. 33:187-192(1997).
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION BY LIGHT.
RX PubMed=12230581; DOI=10.1046/j.1432-1033.2002.03168.x;
RA Chen X., Pfeil J.E., Gal S.;
RT "The three typical aspartic proteinase genes of Arabidopsis thaliana are
RT differentially expressed.";
RL Eur. J. Biochem. 269:4675-4684(2002).
RN [7]
RP INDUCTION BY SENESCENCE.
RX PubMed=12947053; DOI=10.1093/jxb/erg267;
RA Navabpour S., Morris K., Allen R., Harrison E., A-H-Mackerness S.,
RA Buchanan-Wollaston V.;
RT "Expression of senescence-enhanced genes in response to oxidative stress.";
RL J. Exp. Bot. 54:2285-2292(2003).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=17012602; DOI=10.1105/tpc.106.040931;
RA Otegui M.S., Herder R., Schulze J., Jung R., Staehelin L.A.;
RT "The proteolytic processing of seed storage proteins in Arabidopsis embryo
RT cells starts in the multivesicular bodies.";
RL Plant Cell 18:2567-2581(2006).
RN [9]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20079503; DOI=10.1016/j.phytochem.2009.12.005;
RA Mazorra-Manzano M.A., Tanaka T., Dee D.R., Yada R.Y.;
RT "Structure-function characterization of the recombinant aspartic proteinase
RT A1 from Arabidopsis thaliana.";
RL Phytochemistry 71:515-523(2010).
CC -!- FUNCTION: Involved in the breakdown of propeptides of storage proteins
CC in protein-storage vacuoles (By similarity). Possesses aspartic
CC protease activity in vitro. {ECO:0000250, ECO:0000269|PubMed:20079503}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.0-6.0 with insulin B chain as substrate and at 37
CC degrees Celsius. {ECO:0000269|PubMed:20079503};
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:17012602}.
CC Note=Located in protein storage vacuoles (PSV) of the embryo.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, petals, carpels,
CC seed pods and dry seeds. {ECO:0000269|PubMed:12230581}.
CC -!- INDUCTION: By light and during senescence.
CC {ECO:0000269|PubMed:12230581, ECO:0000269|PubMed:12947053}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AC002131; AAC17620.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28813.1; -; Genomic_DNA.
DR EMBL; AY056387; AAL08243.1; -; mRNA.
DR EMBL; AY056403; AAL08259.1; -; mRNA.
DR EMBL; AY063974; AAL36330.1; -; mRNA.
DR EMBL; BT001980; AAN71979.1; -; mRNA.
DR EMBL; AY088657; AAM66979.1; -; mRNA.
DR EMBL; U51036; AAC49730.1; -; mRNA.
DR PIR; F86253; F86253.
DR RefSeq; NP_172655.1; NM_101062.4.
DR AlphaFoldDB; O65390; -.
DR SMR; O65390; -.
DR BioGRID; 22980; 12.
DR IntAct; O65390; 11.
DR STRING; 3702.AT1G11910.1; -.
DR MEROPS; A01.A02; -.
DR PaxDb; O65390; -.
DR PRIDE; O65390; -.
DR ProteomicsDB; 246949; -.
DR EnsemblPlants; AT1G11910.1; AT1G11910.1; AT1G11910.
DR GeneID; 837740; -.
DR Gramene; AT1G11910.1; AT1G11910.1; AT1G11910.
DR KEGG; ath:AT1G11910; -.
DR Araport; AT1G11910; -.
DR TAIR; locus:2008940; AT1G11910.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_1_1; -.
DR InParanoid; O65390; -.
DR PhylomeDB; O65390; -.
DR PRO; PR:O65390; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O65390; baseline and differential.
DR Genevisible; O65390; AT.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IDA:TAIR.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IDA:TAIR.
DR CDD; cd06098; phytepsin; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033869; Phytepsin.
DR InterPro; IPR007856; SapB_1.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR008139; SaposinB_dom.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR Pfam; PF05184; SapB_1; 1.
DR Pfam; PF03489; SapB_2; 1.
DR PRINTS; PR00792; PEPSIN.
DR SMART; SM00741; SapB; 1.
DR SUPFAM; SSF47862; SSF47862; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
DR PROSITE; PS50015; SAP_B; 2.
PE 1: Evidence at protein level;
KW Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Repeat; Signal; Vacuole; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..64
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420625"
FT CHAIN 65..506
FT /note="Aspartic proteinase A1"
FT /id="PRO_0000420626"
FT DOMAIN 82..503
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT DOMAIN 312..417
FT /note="Saposin B-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT ACT_SITE 100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 113..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 278..282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 317..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 342..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 348..380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 425..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
SQ SEQUENCE 506 AA; 54614 MW; 171E16AA7A0D6FA9 CRC64;
MKIYSRTVAV SLIVSFLLCF SAFAERNDGT FRVGLKKLKL DSKNRLAARV ESKQEKPLRA
YRLGDSGDAD VVVLKNYLDA QYYGEIAIGT PPQKFTVVFD TGSSNLWVPS SKCYFSLACL
LHPKYKSSRS STYEKNGKAA AIHYGTGAIA GFFSNDAVTV GDLVVKDQEF IEATKEPGIT
FVVAKFDGIL GLGFQEISVG KAAPVWYNML KQGLIKEPVF SFWLNRNADE EEGGELVFGG
VDPNHFKGKH TYVPVTQKGY WQFDMGDVLI GGAPTGFCES GCSAIADSGT SLLAGPTTII
TMINHAIGAA GVVSQQCKTV VDQYGQTILD LLLSETQPKK ICSQIGLCTF DGTRGVSMGI
ESVVDKENAK LSNGVGDAAC SACEMAVVWI QSQLRQNMTQ ERILNYVNEL CERLPSPMGE
SAVDCAQLST MPTVSLTIGG KVFDLAPEEY VLKVGEGPVA QCISGFIALD VAPPRGPLWI
LGDVFMGKYH TVFDFGNEQV GFAEAA
