UND_ARATH
ID UND_ARATH Reviewed; 389 AA.
AC Q9SV77;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Aspartyl protease UND {ECO:0000305};
DE EC=3.4.23.- {ECO:0000305};
DE AltName: Full=Protein UNDEAD {ECO:0000303|PubMed:21673079};
DE Flags: Precursor;
GN Name=UND {ECO:0000303|PubMed:21673079};
GN OrderedLocusNames=At4g12920 {ECO:0000312|Araport:AT4G12920};
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 FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=21673079; DOI=10.1105/tpc.110.082651;
RA Phan H.A., Iacuone S., Li S.F., Parish R.W.;
RT "The MYB80 transcription factor is required for pollen development and the
RT regulation of tapetal programmed cell death in Arabidopsis thaliana.";
RL Plant Cell 23:2209-2224(2011).
CC -!- FUNCTION: Probable aspartic protease activated by the transcription
CC factor MYB80. May participate in the regulation of the timing of
CC tapetal programmed cell death (PCD) which is critical for pollen
CC development. {ECO:0000269|PubMed:21673079}.
CC -!- DEVELOPMENTAL STAGE: During anther development, expressed from stage 6
CC to stage 9 in tapetal cells and developing microspores.
CC {ECO:0000269|PubMed:21673079}.
CC -!- DISRUPTION PHENOTYPE: Premature apoptosis-like programmed cell death
CC (PCD) in tapetum and pollen from developing anthers, leading to
CC collapsed pollen grains. {ECO:0000269|PubMed:21673079}.
CC -!- MISCELLANEOUS: Plants silencing UND exhibit partial male sterility with
CC reduced silique elongation and seed set. Premature apoptosis-like
CC programmed cell death (PCD) in tapetum from developing anthers, leading
CC to collapsed pollen grains. {ECO:0000269|PubMed:21673079}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AL079349; CAB45491.1; -; Genomic_DNA.
DR EMBL; AL161535; CAB78334.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83203.1; -; Genomic_DNA.
DR PIR; T10194; T10194.
DR RefSeq; NP_193028.1; NM_117361.1.
DR AlphaFoldDB; Q9SV77; -.
DR SMR; Q9SV77; -.
DR STRING; 3702.AT4G12920.1; -.
DR MEROPS; A01.A49; -.
DR PaxDb; Q9SV77; -.
DR PRIDE; Q9SV77; -.
DR EnsemblPlants; AT4G12920.1; AT4G12920.1; AT4G12920.
DR GeneID; 826904; -.
DR Gramene; AT4G12920.1; AT4G12920.1; AT4G12920.
DR KEGG; ath:AT4G12920; -.
DR Araport; AT4G12920; -.
DR TAIR; locus:2123196; AT4G12920.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_8_0_1; -.
DR InParanoid; Q9SV77; -.
DR OMA; YICLGIS; -.
DR OrthoDB; 753343at2759; -.
DR PhylomeDB; Q9SV77; -.
DR PRO; PR:Q9SV77; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SV77; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0043067; P:regulation of programmed cell death; IMP:TAIR.
DR CDD; cd05476; pepsin_A_like_plant; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR034161; Pepsin-like_plant.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease; Developmental protein; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..389
FT /note="Aspartyl protease UND"
FT /id="PRO_5006752426"
FT DOMAIN 58..383
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 86..92
FT /evidence="ECO:0000250|UniProtKB:P42210"
FT DISULFID 304..346
FT /evidence="ECO:0000250|UniProtKB:P42210"
SQ SEQUENCE 389 AA; 43308 MW; B1253A35E4A0E034 CRC64;
MKTTMNFVFL FFLPLLINAK PKRVTLHIPL VHNGANFYDS KVVSLPLSSP HSQRGLAFMA
EIHFGSPQKK QFLHMDTGSS LTWTQCFPCS DCYAQKIYPK YRPAASITYR DAMCEDSHPK
SNPHFAFDPL TRICTYQQHY LDETNIKGTL AQEMITVDTH DGGFKRVHGV YFGCNTLSDG
SYFTGTGILG LGVGKYSIIG EFGSKFSFCL GEISEPKASH NLILGDGANV QGHPTVINIT
EGHTIFQLES IIVGEEITLD DPVQVFVDTG STLSHLSTNL YYKFVDAFDD LIGSRPLSYE
PTLCYKADTI ERLEKMDVGF KFDVGAELSV NIHNIFIQQG PPEIRCLAIQ NNKESFSHVI
IGVIAMQGYN VGYDLSAKTA YINKQDCDM
