APA2_ARATH
ID APA2_ARATH Reviewed; 513 AA.
AC Q8VYL3; O04593;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Aspartic proteinase A2;
DE EC=3.4.23.-;
DE AltName: Full=Aspartic protease 57;
DE Short=AtASP57;
DE Flags: Precursor;
GN Name=APA2; OrderedLocusNames=At1g62290; ORFNames=F19K23.21;
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].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Involved in the breakdown of propeptides of storage proteins
CC in protein-storage vacuoles. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in seed pods and dry seeds.
CC {ECO:0000269|PubMed:12230581}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB60773.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC000375; AAB60773.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33946.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33947.1; -; Genomic_DNA.
DR EMBL; AY070453; AAL49856.1; -; mRNA.
DR EMBL; AY142687; AAN13225.1; -; mRNA.
DR EMBL; AK317285; BAH19961.1; -; mRNA.
DR PIR; E96649; E96649.
DR RefSeq; NP_001031219.1; NM_001036142.3.
DR RefSeq; NP_176419.2; NM_104909.5.
DR AlphaFoldDB; Q8VYL3; -.
DR SMR; Q8VYL3; -.
DR STRING; 3702.AT1G62290.1; -.
DR MEROPS; A01.A02; -.
DR iPTMnet; Q8VYL3; -.
DR PaxDb; Q8VYL3; -.
DR PRIDE; Q8VYL3; -.
DR ProteomicsDB; 240325; -.
DR EnsemblPlants; AT1G62290.1; AT1G62290.1; AT1G62290.
DR EnsemblPlants; AT1G62290.2; AT1G62290.2; AT1G62290.
DR GeneID; 842526; -.
DR Gramene; AT1G62290.1; AT1G62290.1; AT1G62290.
DR Gramene; AT1G62290.2; AT1G62290.2; AT1G62290.
DR KEGG; ath:AT1G62290; -.
DR Araport; AT1G62290; -.
DR TAIR; locus:2018037; AT1G62290.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_1_1; -.
DR InParanoid; Q8VYL3; -.
DR OMA; GVHDAAC; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; Q8VYL3; -.
DR PRO; PR:Q8VYL3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VYL3; baseline and differential.
DR Genevisible; Q8VYL3; AT.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; 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:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; 2.
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 2: Evidence at transcript 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..71
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420627"
FT CHAIN 72..513
FT /note="Aspartic proteinase A2"
FT /id="PRO_0000420628"
FT DOMAIN 89..510
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT DOMAIN 319..424
FT /note="Saposin B-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT ACT_SITE 107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 120..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 285..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 324..418
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 349..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 355..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 432..469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
SQ SEQUENCE 513 AA; 55748 MW; D449D42CEB6A7441 CRC64;
MGVYSRAVAF SVFVSFLLFF TAYSKRNDGT FRVGLKKLKL DPNNRLATRF GSKQEEALRS
SLRSYNNNLG GDSGDADIVP LKNYLDAQYY GEIAIGTPPQ KFTVIFDTGS SNLWVPSGKC
FFSLSCYFHA KYKSSRSSTY KKSGKRAAIH YGSGSISGFF SYDAVTVGDL VVKDQEFIET
TSEPGLTFLV AKFDGLLGLG FQEIAVGNAT PVWYNMLKQG LIKRPVFSFW LNRDPKSEEG
GEIVFGGVDP KHFRGEHTFV PVTQRGYWQF DMGEVLIAGE STGYCGSGCS AIADSGTSLL
AGPTAVVAMI NKAIGASGVV SQQCKTVVDQ YGQTILDLLL AETQPKKICS QIGLCAYDGT
HGVSMGIESV VDKENTRSSS GLRDAGCPAC EMAVVWIQSQ LRQNMTQERI VNYINEICER
MPSPNGESAV DCSQLSKMPT VSFTIGGKVF DLAPEEYVLK IGEGPVAQCI SGFTALDIPP
PRGPLWILGD VFMGKYHTVF DFGNEQVGFA EAV
