APA3_ARATH
ID APA3_ARATH Reviewed; 508 AA.
AC Q9XEC4;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Aspartic proteinase A3;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=APA3; OrderedLocusNames=At4g04460; ORFNames=T26N6.7;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., 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., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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 processing and degradation of storage
CC proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9XEC4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in petals, carpels and seed pods.
CC {ECO:0000269|PubMed:12230581}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AF076243; AAD29758.1; -; Genomic_DNA.
DR EMBL; AL161500; CAB77914.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82390.1; -; Genomic_DNA.
DR EMBL; AF372974; AAK50111.1; -; mRNA.
DR PIR; D85056; D85056.
DR RefSeq; NP_192355.1; NM_116684.4. [Q9XEC4-1]
DR AlphaFoldDB; Q9XEC4; -.
DR SMR; Q9XEC4; -.
DR IntAct; Q9XEC4; 1.
DR STRING; 3702.AT4G04460.1; -.
DR MEROPS; A01.A03; -.
DR PaxDb; Q9XEC4; -.
DR PRIDE; Q9XEC4; -.
DR ProteomicsDB; 244411; -. [Q9XEC4-1]
DR EnsemblPlants; AT4G04460.1; AT4G04460.1; AT4G04460. [Q9XEC4-1]
DR GeneID; 825776; -.
DR Gramene; AT4G04460.1; AT4G04460.1; AT4G04460. [Q9XEC4-1]
DR KEGG; ath:AT4G04460; -.
DR Araport; AT4G04460; -.
DR TAIR; locus:2137189; AT4G04460.
DR eggNOG; KOG1339; Eukaryota.
DR InParanoid; Q9XEC4; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; Q9XEC4; -.
DR PRO; PR:Q9XEC4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9XEC4; baseline and differential.
DR Genevisible; Q9XEC4; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 GO; GO:0046686; P:response to cadmium ion; IEP: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 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 Alternative splicing; Aspartyl protease; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Repeat; Secreted; Signal; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..69
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420629"
FT CHAIN 70..508
FT /note="Aspartic proteinase A3"
FT /id="PRO_0000420630"
FT DOMAIN 87..505
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT DOMAIN 317..419
FT /note="Saposin B-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT ACT_SITE 105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 118..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 283..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 322..413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 347..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 353..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 427..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
SQ SEQUENCE 508 AA; 55571 MW; 2A4F1BC4F598F8F5 CRC64;
MGTRFQSFLL VFLLSCLILI STASCERNGD GTIRIGLKKR KLDRSNRLAS QLFLKNRGSH
WSPKHYFRLN DENADMVPLK NYLDAQYYGD ITIGTPPQKF TVIFDTGSSN LWIPSTKCYL
SVACYFHSKY KASQSSSYRK NGKPASIRYG TGAISGYFSN DDVKVGDIVV KEQEFIEATS
EPGITFLLAK FDGILGLGFK EISVGNSTPV WYNMVEKGLV KEPIFSFWLN RNPKDPEGGE
IVFGGVDPKH FKGEHTFVPV THKGYWQFDM GDLQIAGKPT GYCAKGCSAI ADSGTSLLTG
PSTVITMINH AIGAQGIVSR ECKAVVDQYG KTMLNSLLAQ EDPKKVCSQI GVCAYDGTQS
VSMGIQSVVD DGTSGLLNQA MCSACEMAAV WMESELTQNQ TQERILAYAA ELCDHIPTQN
QQSAVDCGRV SSMPIVTFSI GGRSFDLTPQ DYIFKIGEGV ESQCTSGFTA MDIAPPRGPL
WILGDIFMGP YHTVFDYGKG RVGFAKAA
