ID Q9LV70_ARATH Unreviewed; 406 AA.
AC Q9LV70;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 154.
DE SubName: Full=At5g48430 {ECO:0000313|EMBL:AAY56442.1};
DE SubName: Full=Dermal glycoprotein {ECO:0000313|EMBL:BAA96963.1, ECO:0000313|EMBL:BAD94668.1};
DE SubName: Full=Eukaryotic aspartyl protease family protein {ECO:0000313|EMBL:AED95669.1};
GN Name=MJE7.6 {ECO:0000313|EMBL:AED95669.1};
GN Synonyms=MJE7_6 {ECO:0000313|EMBL:AED95669.1};
GN OrderedLocusNames=At5g48430 {ECO:0000313|Araport:AT5G48430,
GN ECO:0000313|EMBL:AED95669.1};
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:0000313|EMBL:BAA96963.1};
RN [1] {ECO:0000313|EMBL:BAA96963.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2] {ECO:0000313|EMBL:AED95669.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130714; DOI=10.1038/35048507;
RG Kazusa DNA Research Institute;
RG Cold Spring Harbor and Washington University in St Louis Sequencing Consortium;
RG European Union Arabidopsis Genome Sequencing Consortium;
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., See L.H., Vil D., Baker J.,
RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Dusterhoft A., Stiekema W., Pohl T., Entian K.D.,
RA Terryn N., Hartley N., Bent E., Johnson S., Langham S.A., McCullagh B.,
RA Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H.,
RA Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Lankhorst R.K., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S.,
RA Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J.,
RA Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K., Rudd S., Schoof H.,
RA Schueller C., Zaccaria P., Mewes H.W., Bevan M., Fransz P.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3] {ECO:0000313|EMBL:BAD94668.1}
RP NUCLEOTIDE SEQUENCE.
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AAY56442.1}
RP NUCLEOTIDE SEQUENCE.
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:ABO38746.1}
RP NUCLEOTIDE SEQUENCE.
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:AED95669.1}
RP NUCLEOTIDE SEQUENCE.
RG TAIR;
RA Swarbreck D., Lamesch P., Wilks C., Huala E.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:AED95669.1}
RP NUCLEOTIDE SEQUENCE.
RA Krishnakumar V., Cheng C.-Y., Chan A.P., Schobel S., Kim M., Ferlanti E.S.,
RA Belyaeva I., Rosen B.D., Micklem G., Miller J.R., Vaughn M., Town C.D.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [8] {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 reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; BT023451; AAY56442.1; -; mRNA.
DR EMBL; BT030333; ABO38746.1; -; mRNA.
DR EMBL; CP002688; AED95669.1; -; Genomic_DNA.
DR EMBL; AB020745; BAA96963.1; -; Genomic_DNA.
DR EMBL; AK221487; BAD94668.1; -; mRNA.
DR RefSeq; NP_199654.1; NM_124218.3.
DR AlphaFoldDB; Q9LV70; -.
DR SMR; Q9LV70; -.
DR STRING; 3702.Q9LV70; -.
DR PaxDb; 3702-AT5G48430-1; -.
DR ProteomicsDB; 183021; -.
DR EnsemblPlants; AT5G48430.1; AT5G48430.1; AT5G48430.
DR GeneID; 834898; -.
DR Gramene; AT5G48430.1; AT5G48430.1; AT5G48430.
DR KEGG; ath:AT5G48430; -.
DR Araport; AT5G48430; -.
DR TAIR; AT5G48430; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_032185_1_0_1; -.
DR OMA; VNDNTVC; -.
DR OrthoDB; 373682at2759; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LV70; baseline and differential.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05489; xylanase_inhibitor_I_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR InterPro; IPR033868; Xylanase_inhibitor_I-like.
DR PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR PANTHER; PTHR47965:SF63; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Hydrolase {ECO:0000313|EMBL:AED95669.1};
KW Protease {ECO:0000313|EMBL:AED95669.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q9LV70,
KW ECO:0007829|ProteomicsDB:Q9LV70};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..406
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014313030"
FT DOMAIN 29..389
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 406 AA; 44445 MW; 546FBF03DC82B548 CRC64;
MEKSLLVLCL ILFFTYSYVS ANYYPPKALV STVSKNTILP IFTFTLNTNQ EFFIHIGGPY
LVRKCNDGLP RPIVPCGSPV CALTRRFTPH QCSLPSNKII NGVCACQATA FEPFQRICNS
DQFTYGDLSI SSLKPISPSV TINNVYYLCI PQPFLVDFPP GVFGLAGLAP TALATWNQLT
RPRLGLEKKF ALCLPSDENP LKKGAIYFGG GPYKLRNIDA RSMLSYTRLI TNPRKLNNYF
LGLKGISVNG NRILFAPNAF AFDRNGDGGV TLSTIFPFTM LRSDIYRVFI EAFSQATSGI
PRVSSTTPFE FCLSTTTNFQ VPRIDLELAN GVIWKLSPAN AMKKVSDDVA CLAFVNGGDA
AAQAVMIGIH QMENTLVEFD VGRSAFGFSS SLGLVSASCG DFQTRP
//
