PCS1L_ARATH
ID PCS1L_ARATH Reviewed; 453 AA.
AC Q9LZL3;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Aspartic proteinase PCS1;
DE EC=3.4.23.-;
DE AltName: Full=Aspartic protease 38;
DE Short=AtASP38;
DE AltName: Full=Protein EMBRYO DEFECTIVE 24;
DE AltName: Full=Protein PROMOTION OF CELL SURVIVAL 1;
DE Flags: Precursor;
GN Name=PCS1; Synonyms=EMB24; OrderedLocusNames=At5g02190; ORFNames=T7H20.240;
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 Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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.
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15723040; DOI=10.1038/sj.embor.7400357;
RA Ge X., Dietrich C., Matsuno M., Li G., Berg H., Xia Y.;
RT "An Arabidopsis aspartic protease functions as an anti-cell-death component
RT in reproduction and embryogenesis.";
RL EMBO Rep. 6:282-288(2005).
CC -!- FUNCTION: Embryo-specific aspartic protease that limits programmed cell
CC death during reproductive development. Possesses peptidase activity
CC toward casein in vitro. {ECO:0000269|PubMed:15723040}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum.
CC -!- TISSUE SPECIFICITY: Expressed specifically in developing gametophytes
CC and developing seeds. {ECO:0000269|PubMed:15723040}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000269|PubMed:15723040}.
CC -!- MISCELLANEOUS: Ectopic expression of PCS1 induces survival of cells of
CC the anther wall including stomium and septum cells. This leads to a
CC failure in anther dehiscence and subsequent male sterility
CC (PubMed:15723040). {ECO:0000305|PubMed:15723040}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AL162508; CAB82992.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90442.1; -; Genomic_DNA.
DR EMBL; BT015130; AAT85726.1; -; mRNA.
DR EMBL; BT015855; AAU94418.1; -; mRNA.
DR EMBL; AK226937; BAE99007.1; -; mRNA.
DR PIR; T48240; T48240.
DR RefSeq; NP_195839.1; NM_120297.4.
DR AlphaFoldDB; Q9LZL3; -.
DR SMR; Q9LZL3; -.
DR STRING; 3702.AT5G02190.1; -.
DR MEROPS; A01.074; -.
DR PaxDb; Q9LZL3; -.
DR PRIDE; Q9LZL3; -.
DR ProteomicsDB; 236373; -.
DR EnsemblPlants; AT5G02190.1; AT5G02190.1; AT5G02190.
DR GeneID; 831845; -.
DR Gramene; AT5G02190.1; AT5G02190.1; AT5G02190.
DR KEGG; ath:AT5G02190; -.
DR Araport; AT5G02190; -.
DR TAIR; locus:2185173; AT5G02190.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_8_4_1; -.
DR OMA; WMEFDLQ; -.
DR OrthoDB; 753343at2759; -.
DR PhylomeDB; Q9LZL3; -.
DR PRO; PR:Q9LZL3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZL3; baseline and differential.
DR Genevisible; Q9LZL3; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; ISS:TAIR.
DR GO; GO:0008233; F:peptidase activity; IDA:TAIR.
DR GO; GO:0012501; P:programmed cell death; IMP:TAIR.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd05476; pepsin_A_like_plant; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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 PANTHER; PTHR47965; PTHR47965; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
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; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..57
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420631"
FT CHAIN 58..453
FT /note="Aspartic proteinase PCS1"
FT /id="PRO_0000420632"
FT DOMAIN 73..438
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 453 AA; 49678 MW; CC13D71E40C3BD1F CRC64;
MFSRFHALFL LLVLSVRTYK CVSSSSSSSS SFSFSSFSSS SSSQTLVLPL KTRITPTDHR
PTDKLHFHHN VTLTVTLTVG TPPQNISMVI DTGSELSWLR CNRSSNPNPV NNFDPTRSSS
YSPIPCSSPT CRTRTRDFLI PASCDSDKLC HATLSYADAS SSEGNLAAEI FHFGNSTNDS
NLIFGCMGSV SGSDPEEDTK TTGLLGMNRG SLSFISQMGF PKFSYCISGT DDFPGFLLLG
DSNFTWLTPL NYTPLIRIST PLPYFDRVAY TVQLTGIKVN GKLLPIPKSV LVPDHTGAGQ
TMVDSGTQFT FLLGPVYTAL RSHFLNRTNG ILTVYEDPDF VFQGTMDLCY RISPVRIRSG
ILHRLPTVSL VFEGAEIAVS GQPLLYRVPH LTVGNDSVYC FTFGNSDLMG MEAYVIGHHH
QQNMWIEFDL QRSRIGLAPV ECDVSGQRLG IGS
