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EDA2_ARATH
ID   EDA2_ARATH              Reviewed;         489 AA.
AC   Q1PF50; Q9SL39;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Probable serine protease EDA2;
DE            EC=3.4.-.-;
DE   AltName: Full=Protein EMBRYO SAC DEVELOPMENT ARREST 2;
DE   Flags: Precursor;
GN   Name=EDA2; OrderedLocusNames=At2g18080; ORFNames=T27K22.5;
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=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   [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] OF 73-489.
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [4]
RP   PREDICTION.
RX   PubMed=15333753; DOI=10.1104/pp.104.043695;
RA   Reumann S., Ma C., Lemke S., Babujee L.;
RT   "AraPerox. A database of putative Arabidopsis proteins from plant
RT   peroxisomes.";
RL   Plant Physiol. 136:2587-2608(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=15634699; DOI=10.1242/dev.01595;
RA   Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA   Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT   "Genetic and molecular identification of genes required for female
RT   gametophyte development and function in Arabidopsis.";
RL   Development 132:603-614(2005).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19748917; DOI=10.1104/pp.109.142505;
RA   Lingard M.J., Bartel B.;
RT   "Arabidopsis LON2 is necessary for peroxisomal function and sustained
RT   matrix protein import.";
RL   Plant Physiol. 151:1354-1365(2009).
CC   -!- FUNCTION: May be involved in a proteolytic pathway controlling the
CC       nuclear division phase of megagametogenesis.
CC       {ECO:0000269|PubMed:15634699}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Note=Prediction of a
CC       peroxisomal location. {ECO:0000269|PubMed:15333753}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:19748917}.
CC   -!- SIMILARITY: Belongs to the peptidase S28 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD20118.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC006201; AAD20118.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC06724.1; -; Genomic_DNA.
DR   EMBL; DQ446516; ABE65823.1; -; mRNA.
DR   PIR; A84560; A84560.
DR   RefSeq; NP_179399.5; NM_127364.6.
DR   AlphaFoldDB; Q1PF50; -.
DR   SMR; Q1PF50; -.
DR   STRING; 3702.AT2G18080.1; -.
DR   MEROPS; S28.A05; -.
DR   iPTMnet; Q1PF50; -.
DR   PaxDb; Q1PF50; -.
DR   PRIDE; Q1PF50; -.
DR   ProteomicsDB; 222058; -.
DR   EnsemblPlants; AT2G18080.1; AT2G18080.1; AT2G18080.
DR   GeneID; 816320; -.
DR   Gramene; AT2G18080.1; AT2G18080.1; AT2G18080.
DR   KEGG; ath:AT2G18080; -.
DR   Araport; AT2G18080; -.
DR   TAIR; locus:2060959; AT2G18080.
DR   eggNOG; KOG2182; Eukaryota.
DR   HOGENOM; CLU_020959_4_1_1; -.
DR   InParanoid; Q1PF50; -.
DR   OMA; ACYNRIE; -.
DR   OrthoDB; 555765at2759; -.
DR   PhylomeDB; Q1PF50; -.
DR   PRO; PR:Q1PF50; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q1PF50; baseline and differential.
DR   Genevisible; Q1PF50; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IBA:GO_Central.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009561; P:megagametogenesis; IMP:TAIR.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.980; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR008758; Peptidase_S28.
DR   InterPro; IPR042269; Ser_carbopepase_S28_SKS.
DR   Pfam; PF05577; Peptidase_S28; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..489
FT                   /note="Probable serine protease EDA2"
FT                   /id="PRO_0000405231"
FT   ACT_SITE        178
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        410
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        436
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        365
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        406
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        419
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        456
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   489 AA;  55807 MW;  E284E3BA7C226F59 CRC64;
     MSLEFGFILI NIFTAIVSFS TLSHALLHPS SVSHNVSRSR YYMTTNELWF NQTLDHESPN
     DHRKFRQRYY EFMDYFRSPD GPMFMIICGE GPCSGIANDY INVLAKKFQA GVVSLEHRYY
     GKSSPFNSLA TENLKYLSSK QALYDLASFR QYYQESLNKK LNISSGGSDN PWFFFGISYS
     GALSAWFRLK FPHLTCGSLA SSAVVRAIYE FSEFDQQIGE SAGQECKLAL QETNKLLELG
     LKVKNKAVKS LFNATELDVD ADFLYLTADA AVMAFQYGNP DKLCVPLVEA KKNGSDLVVT
     YSTYVREYCM RIWGLRVRTY NRKHLRNTVV TADSAYRLWW FQACTELGYF QVAPKYDSVR
     SHQINTTFHL DLCKSLFGKD VYPKVDATNL YYGGDRLAAT KIIFTNGSED PWRHASKQNS
     THEMPSYIIK CRNCGHGSDI RGCPQSPMVI EGKSNNCSLP DYVNKVRQQM VEHIDLWLSE
     CRQSIRSSI
 
 
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