ASPL1_ARATH
ID ASPL1_ARATH Reviewed; 528 AA.
AC Q9LX20; Q0WVG6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Aspartic proteinase-like protein 1;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN OrderedLocusNames=At5g10080; ORFNames=T31P16.70;
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=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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE98882.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL356332; CAB92049.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91491.1; -; Genomic_DNA.
DR EMBL; AK226784; BAE98882.1; ALT_FRAME; mRNA.
DR PIR; T50012; T50012.
DR RefSeq; NP_196570.1; NM_121046.2.
DR AlphaFoldDB; Q9LX20; -.
DR SMR; Q9LX20; -.
DR STRING; 3702.AT5G10080.1; -.
DR MEROPS; A01.A55; -.
DR PaxDb; Q9LX20; -.
DR PRIDE; Q9LX20; -.
DR ProteomicsDB; 246698; -.
DR EnsemblPlants; AT5G10080.1; AT5G10080.1; AT5G10080.
DR GeneID; 830872; -.
DR Gramene; AT5G10080.1; AT5G10080.1; AT5G10080.
DR KEGG; ath:AT5G10080; -.
DR Araport; AT5G10080; -.
DR TAIR; locus:2184138; AT5G10080.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_029667_2_0_1; -.
DR InParanoid; Q9LX20; -.
DR OMA; LGWLYYT; -.
DR OrthoDB; 753343at2759; -.
DR PhylomeDB; Q9LX20; -.
DR PRO; PR:Q9LX20; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LX20; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; HDA:TAIR.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Protease; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..503
FT /note="Aspartic proteinase-like protein 1"
FT /id="PRO_0000259442"
FT PROPEP 504..528
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000259443"
FT DOMAIN 100..449
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT REGION 451..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT LIPID 503
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 528 AA; 57961 MW; C1D156857EA7B119 CRC64;
MVSRSAFLLF CVLFLATEET LASLFSSRLI HRFSDEGRAS IKTPSSSDSL PNKQSLEYYR
LLAESDFRRQ RMNLGAKVQS LVPSEGSKTI SSGNDFGWLH YTWIDIGTPS VSFLVALDTG
SNLLWIPCNC VQCAPLTSTY YSSLATKDLN EYNPSSSSTS KVFLCSHKLC DSASDCESPK
EQCPYTVNYL SGNTSSSGLL VEDILHLTYN TNNRLMNGSS SVKARVVIGC GKKQSGDYLD
GVAPDGLMGL GPAEISVPSF LSKAGLMRNS FSLCFDEEDS GRIYFGDMGP SIQQSTPFLQ
LDNNKYSGYI VGVEACCIGN SCLKQTSFTT FIDSGQSFTY LPEEIYRKVA LEIDRHINAT
SKNFEGVSWE YCYESSAEPK VPAIKLKFSH NNTFVIHKPL FVFQQSQGLV QFCLPISPSG
QEGIGSIGQN YMRGYRMVFD RENMKLGWSP SKCQEDKIEP PQASPGSTSS PNPLPTDEQQ
SRGGHAVSPA IAGKTPSKTP SSSSSYSFSS IMRLFNSLLL LHWLASLM
