ID B3H581_ARATH Unreviewed; 606 AA.
AC B3H581;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 100.
DE SubName: Full=DEGP protease 2 {ECO:0000313|EMBL:AEC10915.1};
GN Name=DEG2 {ECO:0000313|EMBL:AEC10915.1, ECO:0000313|TAIR:AT2G47940};
GN Synonyms=DEGP protease 2 {ECO:0000313|EMBL:AEC10915.1}, DEGP2
GN {ECO:0000313|EMBL:AEC10915.1}, EMB3117 {ECO:0000313|EMBL:AEC10915.1},
GN EMBRYO DEFECTIVE 3117 {ECO:0000313|EMBL:AEC10915.1};
GN OrderedLocusNames=At2g47940 {ECO:0000313|Araport:AT2G47940,
GN ECO:0000313|EMBL:AEC10915.1};
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:AEC10915.1, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:AEC10915.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S., Shea T.P., Benito M.I., Town C.D.,
RA Fujii C.Y., Mason T., Bowman C.L., Barnstead M., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee 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 [2] {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 S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP002685; AEC10915.1; -; Genomic_DNA.
DR RefSeq; NP_001118544.1; NM_001125072.1.
DR AlphaFoldDB; B3H581; -.
DR SMR; B3H581; -.
DR MEROPS; S01.279; -.
DR EnsemblPlants; AT2G47940.2; AT2G47940.2; AT2G47940.
DR GeneID; 819406; -.
DR Gramene; AT2G47940.2; AT2G47940.2; AT2G47940.
DR Araport; AT2G47940; -.
DR TAIR; AT2G47940; DEG2.
DR HOGENOM; CLU_020120_10_0_1; -.
DR OMA; CVEHNTQ; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; B3H581; baseline and differential.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.20.190.20; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR041517; DEGP_PDZ.
DR InterPro; IPR046449; DEGP_PDZ_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR45980; -; 1.
DR PANTHER; PTHR45980:SF6; PROTEASE DO-LIKE 2, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF17815; PDZ_3; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 1: Evidence at protein level;
KW Hydrolase {ECO:0000313|EMBL:AEC10915.1};
KW Protease {ECO:0000313|EMBL:AEC10915.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B3H581,
KW ECO:0007829|ProteomicsDB:B3H581};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548}.
FT DOMAIN 321..419
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF13180"
FT DOMAIN 428..569
FT /note="Protease Do-like PDZ"
FT /evidence="ECO:0000259|Pfam:PF17815"
FT REGION 41..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 66674 MW; 64EB33BD12C44F89 CRC64;
MAASVANCCF SVLNASVKIQ SSSISSPWCF VSASSLTPRA SSNIKRKSSR SDSPSPILNP
ENYPGRVRDE SSNPPQKMAF KAFGSPKKEK KESLSDFSRD QQTDPAKIHD ASFLNAVVKV
YCTHTAPDYS LPWQKQRQFT STGSAFMIGD GKLLTNAHCV EHDTQVKVKR RGDDRKYVAK
VLVRGVDCDI ALLSVESEDF WKGAEPLRLG HLPRLQDSVT VVGYPLGGDT ISVTKGVVSR
IEVTSYAHGS SDLLGIQIDA AINPGNSGGP AFNDQGECIG VAFQVYRSEE TENIGYVIPT
TVVSHFLTDY ERNGKYTGYP CLGVLLQKLE NPALRECLKV PTNEGVLVRR VEPTSDASKV
LKEGDVIVSF DDLHVGCEGT VPFRSSERIA FRYLISQKFA GDIAEIGIIR AGEHKKVQVV
LRPRVHLVPY HIDGGQPSYI IVAGLVFTPL SEPLIEEECE DTIGLKLLTK ARYSVARFRG
EQIVILSQVL ANEVNIGYED MNNQQVLKFN GIPIRNIHHL AHLIDMCKDK YLVFEFEDNY
VAVLEREASN SASLCILKDY GIPSERSADL LEPYVDPIDD TQALDQGIGD SPVSNLEIGF
DGLVWA
//