CRSP_ARATH
ID CRSP_ARATH Reviewed; 769 AA.
AC Q9LNU1; F4HSQ4; Q8LAE1;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=CO(2)-response secreted protease {ECO:0000303|PubMed:25043023};
DE AltName: Full=Subtilisin-like serine protease {ECO:0000303|PubMed:25043023};
DE Short=AtSBT5.2 {ECO:0000303|PubMed:25043023};
DE AltName: Full=Tripeptidyl-peptidase II {ECO:0000255|PROSITE-ProRule:PRU10081};
DE EC=3.4.14.10 {ECO:0000255|PROSITE-ProRule:PRU10081};
DE Flags: Precursor;
GN Name=CRSP {ECO:0000303|PubMed:25043023};
GN Synonyms=SBT5.2 {ECO:0000303|PubMed:25043023};
GN OrderedLocusNames=At1g20160 {ECO:0000312|Araport:AT1G20160};
GN ORFNames=T20H2.6 {ECO:0000312|EMBL:AAF79897.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INDUCTION BY CO(2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=25043023; DOI=10.1038/nature13452;
RA Engineer C.B., Ghassemian M., Anderson J.C., Peck S.C., Hu H.,
RA Schroeder J.I.;
RT "Carbonic anhydrases, EPF2 and a novel protease mediate CO2 control of
RT stomatal development.";
RL Nature 513:246-250(2014).
CC -!- FUNCTION: Mediates CO(2)-controlled stomatal development by cleaving
CC peptide EPF2 (AC Q8LC53). Not active on peptides EPF1 (AC Q8S8I4) or
CC stomagen (AC Q9SV72). {ECO:0000269|PubMed:25043023}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC EC=3.4.14.10; Evidence={ECO:0000255|PROSITE-ProRule:PRU10081};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:25043023}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LNU1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LNU1-2; Sequence=VSP_056784;
CC -!- TISSUE SPECIFICITY: Expressed in roots, guard cells and meristemoid and
CC pavement cells. {ECO:0000269|PubMed:25043023}.
CC -!- INDUCTION: Induced by high CO(2). {ECO:0000269|PubMed:25043023}.
CC -!- DISRUPTION PHENOTYPE: Increased stomata number at elevated CO(2)
CC concentration and increased number of epidermal cells.
CC {ECO:0000269|PubMed:25043023}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; AC022472; AAF79897.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29945.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29946.1; -; Genomic_DNA.
DR EMBL; AK228874; BAF00765.1; -; mRNA.
DR EMBL; AY087872; AAM65424.1; -; mRNA.
DR PIR; D86335; D86335.
DR RefSeq; NP_001031070.1; NM_001035993.1. [Q9LNU1-2]
DR RefSeq; NP_564107.1; NM_101870.3. [Q9LNU1-1]
DR AlphaFoldDB; Q9LNU1; -.
DR SMR; Q9LNU1; -.
DR STRING; 3702.AT1G20160.1; -.
DR MEROPS; S08.A22; -.
DR iPTMnet; Q9LNU1; -.
DR PaxDb; Q9LNU1; -.
DR PRIDE; Q9LNU1; -.
DR ProteomicsDB; 220450; -. [Q9LNU1-1]
DR EnsemblPlants; AT1G20160.1; AT1G20160.1; AT1G20160. [Q9LNU1-1]
DR EnsemblPlants; AT1G20160.2; AT1G20160.2; AT1G20160. [Q9LNU1-2]
DR GeneID; 838606; -.
DR Gramene; AT1G20160.1; AT1G20160.1; AT1G20160. [Q9LNU1-1]
DR Gramene; AT1G20160.2; AT1G20160.2; AT1G20160. [Q9LNU1-2]
DR KEGG; ath:AT1G20160; -.
DR Araport; AT1G20160; -.
DR TAIR; locus:2198656; AT1G20160.
DR eggNOG; ENOG502QUSK; Eukaryota.
DR InParanoid; Q9LNU1; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9LNU1; -.
DR PRO; PR:Q9LNU1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNU1; baseline and differential.
DR Genevisible; Q9LNU1; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; NAS:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:TAIR.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:1900425; P:negative regulation of defense response to bacterium; IMP:TAIR.
DR GO; GO:2000122; P:negative regulation of stomatal complex development; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:TAIR.
DR GO; GO:2000038; P:regulation of stomatal complex development; IMP:TAIR.
DR GO; GO:0010037; P:response to carbon dioxide; IMP:TAIR.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR045051; SBT.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795; PTHR10795; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell wall; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..769
FT /note="CO(2)-response secreted protease"
FT /id="PRO_0000430504"
FT DOMAIN 35..108
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 112..613
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 381..465
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 210
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 546
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT VAR_SEQ 1..39
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056784"
FT CONFLICT 34
FT /note="G -> V (in Ref. 4; AAM65424)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="E -> K (in Ref. 4; AAM65424)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 769 AA; 81480 MW; 2236DA60DE0D3E01 CRC64;
MKGITFFTPF LSFLYLLCIL FMTETEAGSR NGDGVYIVYM GSASSAANAN RAQILINTMF
KRRANDLLHT YKHGFSGFAA RLTAEEAKVI AKKPGVVSVF PDPHFQLHTT HSWDFLKYQT
SVKVDSGPPS SASDGSYDSI VGILDTGIWP ESESFNDKDM GPIPSRWKGT CMEAKDFKSS
NCNRKIIGAR YYKNPDDDSE YYTTRDVIGH GSHVSSTIAG SAVENASYYG VASGTAKGGS
QNARIAMYKV CNPGGCTGSS ILAAFDDAIA DGVDVLSLSL GAPAYARIDL NTDPIAIGAF
HAVEQGILVI CSAGNDGPDG GTVTNTAPWI MTVAANTIDR DFESDVVLGG NKVIKGEGIH
FSNVSKSPVY PLIHGKSAKS ADASEGSARA CDSDSLDQEK VKGKIVLCEN VGGSYYASSA
RDEVKSKGGT GCVFVDDRTR AVASAYGSFP TTVIDSKEAA EIFSYLNSTK DPVATILPTA
TVEKFTPAPA VAYFSSRGPS SLTRSILKPD ITAPGVSILA AWTGNDSSIS LEGKPASQYN
VISGTSMAAP HVSAVASLIK SQHPTWGPSA IRSAIMTTAT QTNNDKGLIT TETGATATPY
DSGAGELSST ASMQPGLVYE TTETDYLNFL CYYGYNVTTI KAMSKAFPEN FTCPADSNLD
LISTINYPSI GISGFKGNGS KTVTRTVTNV GEDGEAVYTV SVETPPGFNI QVTPEKLQFT
KDGEKLTYQV IVSATASLKQ DVFGALTWSN AKYKVRSPIV ISSESSRTN
