APF1_ARATH
ID APF1_ARATH Reviewed; 513 AA.
AC Q8VYV9;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Aspartyl protease family protein 1 {ECO:0000305};
DE EC=3.4.23.- {ECO:0000305};
DE Flags: Precursor;
GN Name=APF1 {ECO:0000305};
GN OrderedLocusNames=At2g17760 {ECO:0000312|Araport:AT2G17760};
GN ORFNames=T17A5.8 {ECO:0000305};
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 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 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 [5]
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; CP002685; AEC06679.1; -; Genomic_DNA.
DR EMBL; AY069886; AAL47439.1; -; mRNA.
DR EMBL; AY142012; AAM98276.1; -; mRNA.
DR PIR; T08860; T08860.
DR RefSeq; NP_849967.1; NM_179636.3.
DR AlphaFoldDB; Q8VYV9; -.
DR SMR; Q8VYV9; -.
DR IntAct; Q8VYV9; 1.
DR STRING; 3702.AT2G17760.1; -.
DR MEROPS; A01.A38; -.
DR iPTMnet; Q8VYV9; -.
DR PaxDb; Q8VYV9; -.
DR PRIDE; Q8VYV9; -.
DR ProteomicsDB; 244437; -.
DR EnsemblPlants; AT2G17760.1; AT2G17760.1; AT2G17760.
DR GeneID; 816285; -.
DR Gramene; AT2G17760.1; AT2G17760.1; AT2G17760.
DR KEGG; ath:AT2G17760; -.
DR Araport; AT2G17760; -.
DR TAIR; locus:2827921; AT2G17760.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_029667_2_0_1; -.
DR InParanoid; Q8VYV9; -.
DR OMA; LETNNAQ; -.
DR OrthoDB; 753343at2759; -.
DR PhylomeDB; Q8VYV9; -.
DR PRO; PR:Q8VYV9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8VYV9; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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 Aspartyl protease; Cell membrane; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Protease; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..484
FT /note="Aspartyl protease family protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5005941369"
FT PROPEP 485..513
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436002"
FT DOMAIN 104..445
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT REGION 452..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT LIPID 484
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 513 AA; 56028 MW; 2B5C2BD201488974 CRC64;
MVWYSSCRIL FLGLLILLAS SWVLDRCEGF GEFGFEFHHR FSDQVVGVLP GDGLPNRDSS
KYYRVMAHRD RLIRGRRLAN EDQSLVTFSD GNETVRVDAL GFLHYANVTV GTPSDWFMVA
LDTGSDLFWL PCDCTNCVRE LKAPGGSSLD LNIYSPNASS TSTKVPCNST LCTRGDRCAS
PESDCPYQIR YLSNGTSSTG VLVEDVLHLV SNDKSSKAIP ARVTFGCGQV QTGVFHDGAA
PNGLFGLGLE DISVPSVLAK EGIAANSFSM CFGNDGAGRI SFGDKGSVDQ RETPLNIRQP
HPTYNITVTK ISVGGNTGDL EFDAVFDSGT SFTYLTDAAY TLISESFNSL ALDKRYQTTD
SELPFEYCYA LSPNKDSFQY PAVNLTMKGG SSYPVYHPLV VIPMKDTDVY CLAIMKIEDI
SIIGQNFMTG YRVVFDREKL ILGWKESDCY TGETSARTLP SNRSSSSARP PASSFDPEAT
NIPSQRPNTS TTSAAYSLSI SLSLFFFSIL AIL
