APF2_ARATH
ID APF2_ARATH Reviewed; 485 AA.
AC Q9LNJ3; Q8L9B9;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Aspartyl protease family protein 2 {ECO:0000305};
DE EC=3.4.23.- {ECO:0000305};
DE Flags: Precursor;
GN Name=APF2 {ECO:0000305};
GN OrderedLocusNames=At1g01300 {ECO:0000312|Araport:AT1G01300};
GN ORFNames=F6F3.10 {ECO:0000312|EMBL:AAF97328.1};
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 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 GENE FAMILY.
RX PubMed=16381599; DOI=10.2174/138920305774933268;
RA Faro C., Gal S.;
RT "Aspartic proteinase content of the Arabidopsis genome.";
RL Curr. Protein Pept. Sci. 6:493-500(2005).
RN [6]
RP FUNCTION.
RX PubMed=26739014; DOI=10.1105/tpc.15.00626;
RA Li Y., Kabbage M., Liu W., Dickman M.B.;
RT "Aspartyl protease-mediated cleavage of BAG6 is necessary for autophagy and
RT fungal resistance in plants.";
RL Plant Cell 28:233-247(2016).
CC -!- FUNCTION: Aspartyl protease. Not able to cleave BAG6.
CC {ECO:0000269|PubMed:26739014}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AC023628; AAF97328.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27268.1; -; Genomic_DNA.
DR EMBL; AY128344; AAM91547.1; -; mRNA.
DR EMBL; BT006619; AAP31963.1; -; mRNA.
DR EMBL; AY088528; AAM66061.1; -; mRNA.
DR PIR; C86143; C86143.
DR RefSeq; NP_171637.1; NM_100012.3.
DR AlphaFoldDB; Q9LNJ3; -.
DR SMR; Q9LNJ3; -.
DR IntAct; Q9LNJ3; 1.
DR STRING; 3702.AT1G01300.1; -.
DR MEROPS; A01.A05; -.
DR iPTMnet; Q9LNJ3; -.
DR MetOSite; Q9LNJ3; -.
DR SwissPalm; Q9LNJ3; -.
DR PaxDb; Q9LNJ3; -.
DR PRIDE; Q9LNJ3; -.
DR ProteomicsDB; 246776; -.
DR EnsemblPlants; AT1G01300.1; AT1G01300.1; AT1G01300.
DR GeneID; 839375; -.
DR Gramene; AT1G01300.1; AT1G01300.1; AT1G01300.
DR KEGG; ath:AT1G01300; -.
DR Araport; AT1G01300; -.
DR TAIR; locus:2035297; AT1G01300.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_5_0_1; -.
DR InParanoid; Q9LNJ3; -.
DR OMA; PPRYVYM; -.
DR OrthoDB; 753343at2759; -.
DR PhylomeDB; Q9LNJ3; -.
DR PRO; PR:Q9LNJ3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNJ3; baseline and differential.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05472; cnd41_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033873; CND41-like.
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; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..485
FT /note="Aspartyl protease family protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5005943290"
FT DOMAIN 142..480
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT REGION 43..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CONFLICT 89
FT /note="D -> Q (in Ref. 4; AAM66061)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="K -> R (in Ref. 4; AAM66061)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="D -> N (in Ref. 4; AAM66061)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="G -> R (in Ref. 4; AAM66061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 52175 MW; 1A71782027531709 CRC64;
MVGRRKALLF SLCFFFLSLP SFSSLPSFQT LFPNSHSLPC ASPVSFQPDS DSESLLESEF
ESGSDSESSS SITLNLDHID ALSSNKTPDE LFSSRLQRDS RRVKSIATLA AQIPGRNVTH
APRPGGFSSS VVSGLSQGSG EYFTRLGVGT PARYVYMVLD TGSDIVWLQC APCRRCYSQS
DPIFDPRKSK TYATIPCSSP HCRRLDSAGC NTRRKTCLYQ VSYGDGSFTV GDFSTETLTF
RRNRVKGVAL GCGHDNEGLF VGAAGLLGLG KGKLSFPGQT GHRFNQKFSY CLVDRSASSK
PSSVVFGNAA VSRIARFTPL LSNPKLDTFY YVGLLGISVG GTRVPGVTAS LFKLDQIGNG
GVIIDSGTSV TRLIRPAYIA MRDAFRVGAK TLKRAPDFSL FDTCFDLSNM NEVKVPTVVL
HFRGADVSLP ATNYLIPVDT NGKFCFAFAG TMGGLSIIGN IQQQGFRVVY DLASSRVGFA
PGGCA