ASPA_ARATH
ID ASPA_ARATH Reviewed; 474 AA.
AC Q8S9J6; Q9LEW2;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Aspartyl protease family protein At5g10770;
DE EC=3.4.23.- {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=At5g10770 {ECO:0000312|Araport:AT5G10770};
GN ORFNames=T30N20_40 {ECO:0000312|EMBL:CAB96832.1};
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 {ECO:0000312|EMBL:AAL77663.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 FUNCTION, AND INDUCTION.
RX PubMed=24755512; DOI=10.1104/pp.114.239665;
RA Breitenbach H.H., Wenig M., Wittek F., Jorda L., Maldonado-Alconada A.M.,
RA Sarioglu H., Colby T., Knappe C., Bichlmeier M., Pabst E., Mackey D.,
RA Parker J.E., Vlot A.C.;
RT "Contrasting roles of the apoplastic aspartyl protease APOPLASTIC, ENHANCED
RT DISEASE SUSCEPTIBILITY1-DEPENDENT1 and LEGUME LECTIN-LIKE PROTEIN1 in
RT Arabidopsis systemic acquired resistance.";
RL Plant Physiol. 165:791-809(2014).
CC -!- FUNCTION: Probably not redundant with AED1 and not involved in
CC restriction of salicylic acid (SA) or systemic acquired resistance
CC (SAR) signaling. {ECO:0000269|PubMed:24755512}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}.
CC -!- INDUCTION: Up-regulated in AED1 mutants. {ECO:0000269|PubMed:24755512}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB96832.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL365234; CAB96832.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91594.1; -; Genomic_DNA.
DR EMBL; AY075656; AAL77663.1; -; mRNA.
DR EMBL; BT001004; AAN46758.1; -; mRNA.
DR PIR; T50786; T50786.
DR RefSeq; NP_196638.2; NM_121115.4.
DR AlphaFoldDB; Q8S9J6; -.
DR SMR; Q8S9J6; -.
DR STRING; 3702.AT5G10770.1; -.
DR MEROPS; A01.A15; -.
DR PaxDb; Q8S9J6; -.
DR PRIDE; Q8S9J6; -.
DR ProMEX; Q8S9J6; -.
DR ProteomicsDB; 246694; -.
DR EnsemblPlants; AT5G10770.1; AT5G10770.1; AT5G10770.
DR GeneID; 830944; -.
DR Gramene; AT5G10770.1; AT5G10770.1; AT5G10770.
DR KEGG; ath:AT5G10770; -.
DR Araport; AT5G10770; -.
DR TAIR; locus:2183730; AT5G10770.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_5_2_1; -.
DR InParanoid; Q8S9J6; -.
DR OMA; CVKSCYK; -.
DR OrthoDB; 753343at2759; -.
DR PhylomeDB; Q8S9J6; -.
DR PRO; PR:Q8S9J6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8S9J6; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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 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; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Protease; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..443
FT /note="Aspartyl protease family protein At5g10770"
FT /evidence="ECO:0000255"
FT /id="PRO_5005941279"
FT PROPEP 444..474
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436023"
FT DOMAIN 132..469
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT LIPID 443
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 391..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ SEQUENCE 474 AA; 49864 MW; 9AC6366FBD3225E9 CRC64;
MSINRNLLNI IIILCICLNL GCNDGAQERE TDSHTIQVSS LLPSSSSSCV LSPRASTTKS
SLHVTHRHGT CSRLNNGKAT SPDHVEILRL DQARVNSIHS KLSKKLATDH VSESKSTDLP
AKDGSTLGSG NYIVTVGLGT PKNDLSLIFD TGSDLTWTQC QPCVRTCYDQ KEPIFNPSKS
TSYYNVSCSS AACGSLSSAT GNAGSCSASN CIYGIQYGDQ SFSVGFLAKE KFTLTNSDVF
DGVYFGCGEN NQGLFTGVAG LLGLGRDKLS FPSQTATAYN KIFSYCLPSS ASYTGHLTFG
SAGISRSVKF TPISTITDGT SFYGLNIVAI TVGGQKLPIP STVFSTPGAL IDSGTVITRL
PPKAYAALRS SFKAKMSKYP TTSGVSILDT CFDLSGFKTV TIPKVAFSFS GGAVVELGSK
GIFYVFKISQ VCLAFAGNSD DSNAAIFGNV QQQTLEVVYD GAGGRVGFAP NGCS
