AIR3_ARATH
ID AIR3_ARATH Reviewed; 772 AA.
AC Q9ZSP5; Q8S896; Q8S8B0; Q93W36;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Subtilisin-like protease SBT5.3;
DE EC=3.4.21.-;
DE AltName: Full=Auxin-induced in root cultures protein 3;
DE AltName: Full=Subtilase subfamily 5 member 3;
DE Short=AtSBT5.3;
DE AltName: Full=Subtilisin-like protease AIR3;
DE Flags: Precursor;
GN Name=AIR3; Synonyms=SBT5.3; OrderedLocusNames=At2g04160;
GN ORFNames=F3L12, T16B23;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10231025; DOI=10.1093/dnares/6.1.13;
RA Neuteboom L.W., Veth-Tello L.M., Clijdesdale O.R., Hooykaas P.J.,
RA van der Zaal B.J.;
RT "A novel subtilisin-like protease gene from Arabidopsis thaliana is
RT expressed at sites of lateral root emergence.";
RL DNA Res. 6:13-19(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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 [5]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10080694; DOI=10.1023/a:1006104205959;
RA Neuteboom L.W., Ng J.M.Y., Kuyper M., Clijdesdale O.R., Hooykaas P.J.J.,
RA van der Zaal B.J.;
RT "Isolation and characterization of cDNA clones corresponding with mRNAs
RT that accumulate during auxin-induced lateral root formation.";
RL Plant Mol. Biol. 39:273-287(1999).
CC -!- FUNCTION: Serine protease. Has a substrate preference for the
CC hydrophobic residues Phe and Ala and the basic residue Asp in the P1
CC position, and for Asp, Leu or Ala in the P1' position. May play a role
CC in the degradation of structural proteins in the extracellular matrix
CC of cells located above sites of lateral root formation and thus
CC facilitate lateral root emergence (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Secreted, cell wall
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed specifically at sites of lateral root
CC emergence. {ECO:0000269|PubMed:10231025}.
CC -!- DEVELOPMENTAL STAGE: Expressed during auxin-induced lateral root
CC formation. {ECO:0000269|PubMed:10080694}.
CC -!- INDUCTION: Induced between 4 and 8 hours after treatment with auxin and
CC remains high for at least 24 hours. {ECO:0000269|PubMed:10080694}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01240}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK74005.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM15440.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF098632; AAD12260.1; -; Genomic_DNA.
DR EMBL; AC007178; AAM15440.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007293; AAM15483.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05801.1; -; Genomic_DNA.
DR EMBL; AY045647; AAK74005.1; ALT_FRAME; mRNA.
DR EMBL; AY058235; AAL15409.1; -; mRNA.
DR RefSeq; NP_565309.2; NM_126453.5.
DR AlphaFoldDB; Q9ZSP5; -.
DR SMR; Q9ZSP5; -.
DR STRING; 3702.AT2G04160.1; -.
DR MEROPS; S08.119; -.
DR iPTMnet; Q9ZSP5; -.
DR PaxDb; Q9ZSP5; -.
DR PRIDE; Q9ZSP5; -.
DR ProteomicsDB; 245014; -.
DR EnsemblPlants; AT2G04160.1; AT2G04160.1; AT2G04160.
DR GeneID; 814953; -.
DR Gramene; AT2G04160.1; AT2G04160.1; AT2G04160.
DR KEGG; ath:AT2G04160; -.
DR Araport; AT2G04160; -.
DR TAIR; locus:2050215; AT2G04160.
DR eggNOG; ENOG502QT1T; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; Q9ZSP5; -.
DR OMA; ERMALHT; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9ZSP5; -.
DR PRO; PR:Q9ZSP5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZSP5; baseline and differential.
DR Genevisible; Q9ZSP5; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:TAIR.
DR GO; GO:0010102; P:lateral root morphogenesis; IEP:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009733; P:response to auxin; IEP: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; 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; PS00138; SUBTILASE_SER; 1.
PE 2: Evidence at transcript level;
KW Cell wall; Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..772
FT /note="Subtilisin-like protease SBT5.3"
FT /id="PRO_0000429356"
FT DOMAIN 31..116
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 120..628
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 398..480
FT /note="PA"
FT ACT_SITE 153
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 561
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 772 AA; 82874 MW; 75DCCA0DED63F47E CRC64;
MKLTHNFSFL LLLLLVHMSS KHILASKDSS SYVVYFGAHS HVGEITEDAM DRVKETHYDF
LGSFTGSRER ATDAIFYSYT KHINGFAAHL DHDLAYEISK HPEVVSVFPN KALKLHTTRS
WDFLGLEHNS YVPSSSIWRK ARFGEDTIIA NLDTGVWPES KSFRDEGLGP IPSRWKGICQ
NQKDATFHCN RKLIGARYFN KGYAAAVGHL NSSFDSPRDL DGHGSHTLST AAGDFVPGVS
IFGQGNGTAK GGSPRARVAA YKVCWPPVKG NECYDADVLA AFDAAIHDGA DVISVSLGGE
PTSFFNDSVA IGSFHAAKKR IVVVCSAGNS GPADSTVSNV APWQITVGAS TMDREFASNL
VLGNGKHYKG QSLSSTALPH AKFYPIMASV NAKAKNASAL DAQLCKLGSL DPIKTKGKIL
VCLRGQNGRV EKGRAVALGG GIGMVLENTY VTGNDLLADP HVLPATQLTS KDSFAVSRYI
SQTKKPIAHI TPSRTDLGLK PAPVMASFSS KGPSIVAPQI LKPDITAPGV SVIAAYTGAV
SPTNEQFDPR RLLFNAISGT SMSCPHISGI AGLLKTRYPS WSPAAIRSAI MTTATIMDDI
PGPIQNATNM KATPFSFGAG HVQPNLAVNP GLVYDLGIKD YLNFLCSLGY NASQISVFSG
NNFTCSSPKI SLVNLNYPSI TVPNLTSSKV TVSRTVKNVG RPSMYTVKVN NPQGVYVAVK
PTSLNFTKVG EQKTFKVILV KSKGNVAKGY VFGELVWSDK KHRVRSPIVV KL
