ID   F4JKD9_ARATH            Unreviewed;       354 AA.
AC   F4JKD9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   25-APR-2018, entry version 60.
DE   SubName: Full=Eukaryotic aspartyl protease family protein {ECO:0000313|EMBL:AEE84544.1};
GN   OrderedLocusNames=At4g22050 {ECO:0000313|Araport:AT4G22050,
GN   ECO:0000313|EMBL:AEE84544.1};
GN   ORFNames=F1N20.150 {ECO:0000313|EMBL:AEE84544.1}, F1N20_150
GN   {ECO:0000313|EMBL:AEE84544.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000313|EMBL:AEE84544.1, ECO:0000313|Proteomes:UP000006548};
RN   [1] {ECO:0000313|EMBL:AEE84544.1, ECO:0000313|Proteomes:UP000006548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=10617198; DOI=10.1038/47134;
RG   EU;
RG   CSHL and WU Arabidopsis Sequencing Project;
RA   Mayer K., Schuller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Dusterhoft A., Stiekema W., Entian K.D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Muller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B.,
RA   Portatelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P.,
RA   Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.A.,
RA   McCullagh B., Bilham L., Robben J., Van der Schueren J.,
RA   Grymonprez B., Chuang Y.J., Vandenbussche F., Braeken M., Weltjens I.,
RA   Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G.,
RA   Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S.,
RA   van Staveren M., Dirske W., Mooijman P., Klein Lankhorst R., Rose M.,
RA   Hauf J., Kotter P., Berneiser S., Hempel S., Feldpausch M.,
RA   Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J.,
RA   Villarroel R., De Clercq R., Van Montagu M., Rogers J., Cronin A.,
RA   Quail M., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M.,
RA   Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M.,
RA   Benes V., Rechmann S., Borkova D., Blocker H., Scharfe M., Grimm M.,
RA   Lohnert T.H., Dose S., de Haan M., Maarse A., Schafer M.,
RA   Muller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K.,
RA   Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R.,
RA   Piravandi E., Massenet O., Quigley F., Clabauld G., Mundlein A.,
RA   Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Montfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.W., Stocker S., Zaccaria P.,
RA   Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L.,
RA   Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sehkon M.,
RA   Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T.,
RA   Kalicki J., Graves T., Harmon G., Edwards J., Latreille P.,
RA   Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P.,
RA   Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J.,
RA   Fulton L., Mardis E., Dante M., Pepin K., Hillier L., Nelson J.,
RA   Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J.,
RA   Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffmann J., Till S., Granat S.,
RA   Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E.,
RA   Marra M., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [2] {ECO:0000313|Proteomes:UP000006548}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01103,
CC       ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00692226}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01103}.
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DR   EMBL; CP002687; AEE84544.1; -; Genomic_DNA.
DR   RefSeq; NP_193936.2; NM_118326.3.
DR   UniGene; At.2110; -.
DR   ProteinModelPortal; F4JKD9; -.
DR   SMR; F4JKD9; -.
DR   STRING; 3702.AT4G22050.1; -.
DR   MEROPS; A01.A33; -.
DR   PaxDb; F4JKD9; -.
DR   EnsemblPlants; AT4G22050.1; AT4G22050.1; AT4G22050.
DR   GeneID; 828294; -.
DR   Gramene; AT4G22050.1; AT4G22050.1; AT4G22050.
DR   KEGG; ath:AT4G22050; -.
DR   Araport; AT4G22050; -.
DR   TAIR; locus:2120688; AT4G22050.
DR   eggNOG; KOG1339; Eukaryota.
DR   eggNOG; ENOG410XNV7; LUCA.
DR   InParanoid; F4JKD9; -.
DR   KO; K01379; -.
DR   OMA; QNRNGQV; -.
DR   OrthoDB; EOG0936179B; -.
DR   Reactome; R-ATH-2132295; MHC class II antigen presentation.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JKD9; baseline and differential.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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   PANTHER; PTHR13683; PTHR13683; 2.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
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 {ECO:0000256|PROSITE-ProRule:PRU01103,
KW   ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00629219};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006548};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01103,
KW   ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00629231};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01103,
KW   ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00629201,
KW   ECO:0000313|EMBL:AEE84544.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18    354       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003315478.
FT   DOMAIN       46    350       Peptidase A1. {ECO:0000259|PROSITE:
FT                                PS51767}.
FT   ACT_SITE     64     64       {ECO:0000256|PROSITE-ProRule:PRU01103}.
FT   ACT_SITE    251    251       {ECO:0000256|PROSITE-ProRule:PRU01103}.
SQ   SEQUENCE   354 AA;  39230 MW;  8F12917A9F28A05C CRC64;
     MYTSIFFIFS FLSVSEALVR IPLQIDHALS TNNDGVQLKN VKDFLYYGKI QIGNPGQTFT
     VLFDTGSSSL WVPSENWLAK TENPRNRYIS SASRTFKENG TKAELKYGKG SLTGFLSVDT
     VTVGGISITS QTFIEGVKTP YKEFFKKMPF DGILGLRFTD PLNFGTSVWH SMVFQGKIAK
     NVFSIWLRRF SNSGEINGGE VVFGGIIPAH FSGDHTYVDV EGPGNFFAMS NIWVGGKNTN
     ICSSGCKAIV DSGSSNINVP MDSADEIHRY IGVEPNCNNF ETLPDVTFTI GGKAFVLTPL
     DYIRRSRSQC TSKFVGKTNR SHWTLGIPFM RVFHTVFDYQ NTLAVKVGFA KSTD
//